HEADER SIGNALING PROTEIN 29-APR-15 4ZJ8 TITLE STRUCTURES OF THE HUMAN OX1 OREXIN RECEPTOR BOUND TO SELECTIVE AND TITLE 2 DUAL ANTAGONISTS COMPND MOL_ID: 1; COMPND 2 MOLECULE: HUMAN OX1R FUSION PROTEIN TO P.ABYSII GLYCOGEN SYNTHASE; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: UNP O43613 RESIDUES 1-245,UNP Q9V2J8 RESIDUES 218-413,UNP COMPND 5 O43613 RESIDUES 288-380; COMPND 6 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, PYROCOCCUS ABYSSI (STRAIN GE5 / SOURCE 3 ORSAY); SOURCE 4 ORGANISM_COMMON: HUMAN; SOURCE 5 ORGANISM_TAXID: 9606, 272844; SOURCE 6 STRAIN: GE5 / ORSAY; SOURCE 7 GENE: HCRTR1, PAB2292, PYRAB00770; SOURCE 8 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 9 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 11 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS; SOURCE 12 EXPRESSION_SYSTEM_PLASMID: PFASTBAC1 KEYWDS OREXIN, SUVOREXANT, SB674042, SIGNALING PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR J.YIN,C.A.BRAUTIGAM,Z.SHAO,L.CLARK,C.M.HARRELL,A.L.GOTTER,P.COLEMAN, AUTHOR 2 J.J.RENGER,D.M.ROSENBAUM REVDAT 3 13-APR-16 4ZJ8 1 JRNL REVDAT 2 23-MAR-16 4ZJ8 1 JRNL REVDAT 1 09-MAR-16 4ZJ8 0 JRNL AUTH J.YIN,K.BABAOGLU,C.A.BRAUTIGAM,L.CLARK,Z.SHAO, JRNL AUTH 2 T.H.SCHEUERMANN,C.M.HARRELL,A.L.GOTTER,A.J.ROECKER, JRNL AUTH 3 C.J.WINROW,J.J.RENGER,P.J.COLEMAN,D.M.ROSENBAUM JRNL TITL STRUCTURE AND LIGAND-BINDING MECHANISM OF THE HUMAN OX1 AND JRNL TITL 2 OX2 OREXIN RECEPTORS. JRNL REF NAT.STRUCT.MOL.BIOL. V. 23 293 2016 JRNL REFN ESSN 1545-9985 JRNL PMID 26950369 JRNL DOI 10.1038/NSMB.3183 REMARK 2 REMARK 2 RESOLUTION. 2.75 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.9_1692 REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.75 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.71 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360 REMARK 3 COMPLETENESS FOR RANGE (%) : 77.4 REMARK 3 NUMBER OF REFLECTIONS : 15601 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.225 REMARK 3 R VALUE (WORKING SET) : 0.223 REMARK 3 FREE R VALUE : 0.273 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.310 REMARK 3 FREE R VALUE TEST SET COUNT : 828 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 43.7199 - 4.9960 1.00 3332 194 0.2110 0.2544 REMARK 3 2 4.9960 - 3.9663 1.00 3189 182 0.1977 0.2471 REMARK 3 3 3.9663 - 3.4652 1.00 3158 175 0.2229 0.2689 REMARK 3 4 3.4652 - 3.1485 0.88 2741 157 0.2627 0.3271 REMARK 3 5 3.1485 - 2.9229 0.48 1521 87 0.2778 0.3463 REMARK 3 6 2.9229 - 2.7506 0.26 832 33 0.2665 0.3273 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) : 0.380 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.220 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.003 4212 REMARK 3 ANGLE : 0.732 5684 REMARK 3 CHIRALITY : 0.024 628 REMARK 3 PLANARITY : 0.003 731 REMARK 3 DIHEDRAL : 10.833 1557 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 26:39) REMARK 3 ORIGIN FOR THE GROUP (A): -2.3805 1.2180 -82.1274 REMARK 3 T TENSOR REMARK 3 T11: 0.5932 T22: 0.3637 REMARK 3 T33: 0.4368 T12: 0.1570 REMARK 3 T13: -0.0182 T23: -0.1458 REMARK 3 L TENSOR REMARK 3 L11: 6.1557 L22: 7.3640 REMARK 3 L33: 7.4378 L12: 0.9500 REMARK 3 L13: 2.4819 L23: -2.0781 REMARK 3 S TENSOR REMARK 3 S11: 0.2609 S12: -0.6163 S13: 1.0537 REMARK 3 S21: 0.5571 S22: -0.0735 S23: 0.3984 REMARK 3 S31: -0.8118 S32: -0.5519 S33: -0.1853 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: (CHAIN A AND RESID 40:48) REMARK 3 ORIGIN FOR THE GROUP (A): 12.5585 3.5801 -63.3248 REMARK 3 T TENSOR REMARK 3 T11: 1.4435 T22: 1.3972 REMARK 3 T33: 0.7543 T12: -0.5146 REMARK 3 T13: 0.2574 T23: -0.1759 REMARK 3 L TENSOR REMARK 3 L11: 8.5913 L22: 2.9007 REMARK 3 L33: 5.9696 L12: 0.0238 REMARK 3 L13: 5.4052 L23: 2.2672 REMARK 3 S TENSOR REMARK 3 S11: 0.5769 S12: 0.5785 S13: 0.4950 REMARK 3 S21: -0.9102 S22: 0.3292 S23: -0.1350 REMARK 3 S31: 1.2651 S32: -0.7885 S33: -0.9465 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: (CHAIN A AND RESID 49:153) REMARK 3 ORIGIN FOR THE GROUP (A): -4.5206 -3.2858 -40.1631 REMARK 3 T TENSOR REMARK 3 T11: 0.5315 T22: 0.4097 REMARK 3 T33: -0.0069 T12: 0.0550 REMARK 3 T13: 0.0109 T23: -0.3103 REMARK 3 L TENSOR REMARK 3 L11: 0.4298 L22: 0.8126 REMARK 3 L33: 0.5227 L12: -0.3043 REMARK 3 L13: -0.2333 L23: 0.5973 REMARK 3 S TENSOR REMARK 3 S11: 0.0346 S12: -0.1393 S13: -0.1569 REMARK 3 S21: 0.2562 S22: 0.0613 S23: -0.1265 REMARK 3 S31: 0.4761 S32: 0.0491 S33: 0.1257 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: (CHAIN A AND RESID 154:169) REMARK 3 ORIGIN FOR THE GROUP (A): -16.3476 -5.1431 -27.8882 REMARK 3 T TENSOR REMARK 3 T11: 1.1057 T22: 0.7900 REMARK 3 T33: 0.5207 T12: -0.2840 REMARK 3 T13: 0.2479 T23: -0.0788 REMARK 3 L TENSOR REMARK 3 L11: 8.4744 L22: 2.5677 REMARK 3 L33: 6.6408 L12: -1.9704 REMARK 3 L13: -1.5041 L23: -3.3175 REMARK 3 S TENSOR REMARK 3 S11: -0.5526 S12: -1.0383 S13: -0.8950 REMARK 3 S21: 1.3843 S22: 0.0988 S23: 0.7855 REMARK 3 S31: 1.8147 S32: -1.2828 S33: 0.4352 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: (CHAIN A AND RESID 170:179) REMARK 3 ORIGIN FOR THE GROUP (A): -18.3198 -4.7293 -47.9562 REMARK 3 T TENSOR REMARK 3 T11: 0.3840 T22: 0.7022 REMARK 3 T33: 0.5438 T12: -0.0571 REMARK 3 T13: 0.0068 T23: -0.4030 REMARK 3 L TENSOR REMARK 3 L11: 1.8048 L22: 3.7982 REMARK 3 L33: 7.7673 L12: 0.8947 REMARK 3 L13: 3.6063 L23: 0.7128 REMARK 3 S TENSOR REMARK 3 S11: 0.0285 S12: 0.3846 S13: -0.1783 REMARK 3 S21: -0.6415 S22: 0.1267 S23: 0.0871 REMARK 3 S31: 0.1608 S32: 0.3858 S33: -0.1461 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: (CHAIN A AND RESID 180:203) REMARK 3 ORIGIN FOR THE GROUP (A): -9.3750 -6.4859 -70.9978 REMARK 3 T TENSOR REMARK 3 T11: 0.5839 T22: 0.7111 REMARK 3 T33: 0.2026 T12: 0.0039 REMARK 3 T13: -0.0714 T23: -0.2111 REMARK 3 L TENSOR REMARK 3 L11: 0.1830 L22: 0.7891 REMARK 3 L33: 5.7294 L12: 0.3555 REMARK 3 L13: 0.0341 L23: 0.4926 REMARK 3 S TENSOR REMARK 3 S11: -0.0652 S12: -0.0055 S13: 0.1077 REMARK 3 S21: -0.1834 S22: -0.1578 S23: 0.3178 REMARK 3 S31: -0.2092 S32: -0.9630 S33: 0.1535 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: (CHAIN A AND RESID 204:208) REMARK 3 ORIGIN FOR THE GROUP (A): -19.1145 -0.2100 -63.8641 REMARK 3 T TENSOR REMARK 3 T11: 1.0949 T22: 1.2968 REMARK 3 T33: 0.8996 T12: 0.4309 REMARK 3 T13: -0.4264 T23: -0.5278 REMARK 3 L TENSOR REMARK 3 L11: 3.7874 L22: 1.6074 REMARK 3 L33: 2.7016 L12: -0.4397 REMARK 3 L13: 1.8688 L23: -1.8812 REMARK 3 S TENSOR REMARK 3 S11: -0.5433 S12: -0.6237 S13: 0.8258 REMARK 3 S21: -1.3276 S22: -0.2362 S23: 1.2522 REMARK 3 S31: -1.9698 S32: -1.5346 S33: 0.8179 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: (CHAIN A AND RESID 209:228) REMARK 3 ORIGIN FOR THE GROUP (A): -17.7451 7.3312 -51.7952 REMARK 3 T TENSOR REMARK 3 T11: 0.6983 T22: 0.7354 REMARK 3 T33: 0.3598 T12: 0.4234 REMARK 3 T13: -0.2416 T23: -0.2528 REMARK 3 L TENSOR REMARK 3 L11: 1.8798 L22: 2.1440 REMARK 3 L33: 2.7762 L12: 0.8588 REMARK 3 L13: -0.4832 L23: -1.4818 REMARK 3 S TENSOR REMARK 3 S11: -0.0152 S12: 0.4040 S13: -0.1141 REMARK 3 S21: -0.6564 S22: -0.0741 S23: 0.4921 REMARK 3 S31: -0.0217 S32: -0.6528 S33: 0.1379 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: (CHAIN A AND RESID 229:246) REMARK 3 ORIGIN FOR THE GROUP (A): -10.0836 17.0820 -26.3932 REMARK 3 T TENSOR REMARK 3 T11: 0.2679 T22: 0.2237 REMARK 3 T33: 0.1180 T12: 0.1196 REMARK 3 T13: 0.0526 T23: 0.0603 REMARK 3 L TENSOR REMARK 3 L11: 6.9276 L22: 8.1096 REMARK 3 L33: 7.1434 L12: 4.1415 REMARK 3 L13: 4.6784 L23: 5.1813 REMARK 3 S TENSOR REMARK 3 S11: -0.3284 S12: 0.1197 S13: 0.3336 REMARK 3 S21: -0.3393 S22: -0.3310 S23: 0.4904 REMARK 3 S31: -0.4787 S32: -0.2455 S33: 0.5215 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: (CHAIN A AND RESID 1001:1029) REMARK 3 ORIGIN FOR THE GROUP (A): 5.2369 21.7711 6.8028 REMARK 3 T TENSOR REMARK 3 T11: 0.2262 T22: 0.6165 REMARK 3 T33: 0.1234 T12: -0.0210 REMARK 3 T13: -0.0916 T23: -0.0619 REMARK 3 L TENSOR REMARK 3 L11: 1.2071 L22: 1.4313 REMARK 3 L33: 5.1788 L12: 0.1933 REMARK 3 L13: 0.9587 L23: 0.9759 REMARK 3 S TENSOR REMARK 3 S11: -0.0979 S12: -0.4407 S13: 0.2452 REMARK 3 S21: 0.1942 S22: -0.0945 S23: 0.0823 REMARK 3 S31: -0.1154 S32: -0.1617 S33: 0.1330 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: (CHAIN A AND RESID 1030:1122) REMARK 3 ORIGIN FOR THE GROUP (A): -7.5890 32.6514 5.3165 REMARK 3 T TENSOR REMARK 3 T11: 0.5867 T22: 0.5735 REMARK 3 T33: 0.2670 T12: 0.1190 REMARK 3 T13: -0.0577 T23: -0.2181 REMARK 3 L TENSOR REMARK 3 L11: 1.8132 L22: 1.3338 REMARK 3 L33: 4.1528 L12: 0.3444 REMARK 3 L13: -1.3124 L23: 0.5551 REMARK 3 S TENSOR REMARK 3 S11: 0.0311 S12: -0.5359 S13: 0.8013 REMARK 3 S21: 0.0379 S22: 0.0026 S23: 0.2374 REMARK 3 S31: -1.3996 S32: -0.3375 S33: -0.0133 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: (CHAIN A AND RESID 1123:1162) REMARK 3 ORIGIN FOR THE GROUP (A): -10.9519 19.3836 -3.0250 REMARK 3 T TENSOR REMARK 3 T11: 0.1911 T22: 0.3444 REMARK 3 T33: 0.0782 T12: 0.0480 REMARK 3 T13: -0.0272 T23: 0.0007 REMARK 3 L TENSOR REMARK 3 L11: 6.5651 L22: 3.9484 REMARK 3 L33: 4.2509 L12: -0.1532 REMARK 3 L13: -0.7225 L23: 0.0498 REMARK 3 S TENSOR REMARK 3 S11: -0.1901 S12: -0.1184 S13: -0.1645 REMARK 3 S21: -0.1103 S22: 0.1097 S23: 0.5412 REMARK 3 S31: 0.1276 S32: -0.6322 S33: 0.0480 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: (CHAIN A AND RESID 1163:1180) REMARK 3 ORIGIN FOR THE GROUP (A): -15.6624 20.8728 11.1461 REMARK 3 T TENSOR REMARK 3 T11: 0.3755 T22: 0.8607 REMARK 3 T33: 0.2917 T12: 0.0111 REMARK 3 T13: 0.1339 T23: -0.1577 REMARK 3 L TENSOR REMARK 3 L11: 3.7030 L22: 5.2947 REMARK 3 L33: 5.8635 L12: -2.6382 REMARK 3 L13: -1.7272 L23: -0.9109 REMARK 3 S TENSOR REMARK 3 S11: -0.1939 S12: 0.1040 S13: -0.2373 REMARK 3 S21: 0.6426 S22: 0.0737 S23: 0.4416 REMARK 3 S31: -0.0185 S32: -0.1012 S33: 0.1606 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: (CHAIN A AND (RESID 1181:1196) OR (RESID 288:288)) REMARK 3 ORIGIN FOR THE GROUP (A): -4.1338 10.8185 -0.1207 REMARK 3 T TENSOR REMARK 3 T11: 0.4294 T22: 0.3861 REMARK 3 T33: 0.0696 T12: -0.0061 REMARK 3 T13: -0.0616 T23: 0.1417 REMARK 3 L TENSOR REMARK 3 L11: 0.9094 L22: 0.8153 REMARK 3 L33: 1.3733 L12: -0.1546 REMARK 3 L13: 0.1293 L23: -0.1146 REMARK 3 S TENSOR REMARK 3 S11: -0.0227 S12: -0.1566 S13: -0.1068 REMARK 3 S21: 0.1551 S22: -0.0378 S23: -0.0146 REMARK 3 S31: 0.1425 S32: 0.0242 S33: 0.0011 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: (CHAIN A AND RESID 289:301) REMARK 3 ORIGIN FOR THE GROUP (A): -2.5628 10.8970 -22.3788 REMARK 3 T TENSOR REMARK 3 T11: 0.4302 T22: 0.3118 REMARK 3 T33: 0.0693 T12: 0.0055 REMARK 3 T13: -0.0572 T23: -0.1016 REMARK 3 L TENSOR REMARK 3 L11: 3.9643 L22: 2.6625 REMARK 3 L33: 5.3121 L12: 0.2927 REMARK 3 L13: -0.7162 L23: 1.3281 REMARK 3 S TENSOR REMARK 3 S11: -0.0956 S12: -0.2630 S13: 0.0958 REMARK 3 S21: 0.1620 S22: -0.0854 S23: 0.0405 REMARK 3 S31: -0.1923 S32: 0.0634 S33: -0.0143 REMARK 3 TLS GROUP : 16 REMARK 3 SELECTION: (CHAIN A AND RESID 302:325) REMARK 3 ORIGIN FOR THE GROUP (A): -7.2892 10.0798 -49.7860 REMARK 3 T TENSOR REMARK 3 T11: 0.8539 T22: 0.2692 REMARK 3 T33: 0.1556 T12: 0.1182 REMARK 3 T13: -0.0044 T23: -0.1079 REMARK 3 L TENSOR REMARK 3 L11: 0.4224 L22: 1.1763 REMARK 3 L33: 0.9905 L12: -0.0600 REMARK 3 L13: -0.0777 L23: 0.4710 REMARK 3 S TENSOR REMARK 3 S11: 0.0640 S12: 0.2299 S13: 0.0127 REMARK 3 S21: -0.7134 S22: -0.2650 S23: 0.3245 REMARK 3 S31: -0.3904 S32: -0.3611 S33: 0.1843 REMARK 3 TLS GROUP : 17 REMARK 3 SELECTION: (CHAIN A AND RESID 326:334) REMARK 3 ORIGIN FOR THE GROUP (A): -4.6596 11.2277 -68.4733 REMARK 3 T TENSOR REMARK 3 T11: 1.9883 T22: 1.0823 REMARK 3 T33: 1.0425 T12: 0.1395 REMARK 3 T13: 0.0329 T23: -0.0672 REMARK 3 L TENSOR REMARK 3 L11: 2.9590 L22: 3.9680 REMARK 3 L33: 3.6299 L12: -1.1959 REMARK 3 L13: -3.1253 L23: 2.3335 REMARK 3 S TENSOR REMARK 3 S11: 0.1652 S12: 2.2759 S13: -0.6953 REMARK 3 S21: -1.2240 S22: -0.0633 S23: -0.3632 REMARK 3 S31: -0.5238 S32: -0.3160 S33: -0.1146 REMARK 3 TLS GROUP : 18 REMARK 3 SELECTION: (CHAIN A AND RESID 335:341) REMARK 3 ORIGIN FOR THE GROUP (A): 0.3393 7.8087 -60.7562 REMARK 3 T TENSOR REMARK 3 T11: 1.4032 T22: 0.5313 REMARK 3 T33: 0.3796 T12: -0.0777 REMARK 3 T13: -0.0071 T23: -0.1082 REMARK 3 L TENSOR REMARK 3 L11: 9.0537 L22: 1.7576 REMARK 3 L33: 6.1013 L12: -3.7932 REMARK 3 L13: -6.0724 L23: 3.1286 REMARK 3 S TENSOR REMARK 3 S11: 0.0936 S12: 1.1393 S13: -0.4249 REMARK 3 S21: -0.4378 S22: -0.1543 S23: 0.1287 REMARK 3 S31: -0.3502 S32: -0.2515 S33: 0.0416 REMARK 3 TLS GROUP : 19 REMARK 3 SELECTION: (CHAIN A AND RESID 342:363) REMARK 3 ORIGIN FOR THE GROUP (A): 2.9182 3.6207 -40.4858 REMARK 3 T TENSOR REMARK 3 T11: 0.3417 T22: 0.3338 REMARK 3 T33: 0.1560 T12: 0.0291 REMARK 3 T13: 0.0432 T23: -0.1961 REMARK 3 L TENSOR REMARK 3 L11: 0.6609 L22: 0.1892 REMARK 3 L33: 2.5908 L12: -0.3220 REMARK 3 L13: -0.6131 L23: 0.0497 REMARK 3 S TENSOR REMARK 3 S11: 0.0426 S12: -0.1462 S13: 0.0890 REMARK 3 S21: 0.0053 S22: 0.0616 S23: -0.1345 REMARK 3 S31: 0.0083 S32: 0.2612 S33: -0.0122 REMARK 3 TLS GROUP : 20 REMARK 3 SELECTION: (CHAIN A AND RESID 364:373) REMARK 3 ORIGIN FOR THE GROUP (A): 8.3982 -3.5306 -25.6051 REMARK 3 T TENSOR REMARK 3 T11: 1.0134 T22: 0.8905 REMARK 3 T33: 0.5316 T12: 0.1150 REMARK 3 T13: -0.3143 T23: -0.2498 REMARK 3 L TENSOR REMARK 3 L11: 9.7389 L22: 0.9304 REMARK 3 L33: 8.3385 L12: -0.5239 REMARK 3 L13: 1.3943 L23: -2.7853 REMARK 3 S TENSOR REMARK 3 S11: 0.5301 S12: -1.1424 S13: -0.0593 REMARK 3 S21: 0.6938 S22: 0.1860 S23: -0.7039 REMARK 3 S31: 0.3804 S32: 1.7891 S33: -0.6919 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 4ZJ8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-APR-15. REMARK 100 THE DEPOSITION ID IS D_1000209376. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 07-DEC-14 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 5.4 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 23-ID-D REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.033 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000 REMARK 200 DATA SCALING SOFTWARE : HKL-3000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20480 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.750 REMARK 200 RESOLUTION RANGE LOW (A) : 43.750 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 200 DATA REDUNDANCY : 12.80 REMARK 200 R MERGE (I) : 0.13000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 17.2000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.75 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.80 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8 REMARK 200 DATA REDUNDANCY IN SHELL : 11.20 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.190 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: 4S0V,2BFW REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 58.65 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.97 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM SODIUM CITRATE PH 5.4, 31% PEG REMARK 280 400, 200 MM SODIUM FORMATE, LIPIDIC CUBIC PHASE, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 REMARK 290 4555 X+1/2,-Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 31.62100 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 90.73900 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 32.49600 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 90.73900 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 31.62100 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 32.49600 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 -7 REMARK 465 TYR A -6 REMARK 465 LYS A -5 REMARK 465 ASP A -4 REMARK 465 ASP A -3 REMARK 465 ASP A -2 REMARK 465 ASP A -1 REMARK 465 ALA A 0 REMARK 465 MET A 1 REMARK 465 GLU A 2 REMARK 465 PRO A 3 REMARK 465 SER A 4 REMARK 465 ALA A 5 REMARK 465 THR A 6 REMARK 465 PRO A 7 REMARK 465 GLY A 8 REMARK 465 ALA A 9 REMARK 465 GLN A 10 REMARK 465 MET A 11 REMARK 465 GLY A 12 REMARK 465 VAL A 13 REMARK 465 PRO A 14 REMARK 465 PRO A 15 REMARK 465 GLY A 16 REMARK 465 SER A 17 REMARK 465 ARG A 18 REMARK 465 GLU A 19 REMARK 465 PRO A 20 REMARK 465 SER A 21 REMARK 465 PRO A 22 REMARK 465 VAL A 23 REMARK 465 PRO A 24 REMARK 465 PRO A 25 REMARK 465 SER A 374 REMARK 465 CYS A 375 REMARK 465 CYS A 376 REMARK 465 LEU A 377 REMARK 465 PRO A 378 REMARK 465 GLY A 379 REMARK 465 LEU A 380 REMARK 465 HIS A 381 REMARK 465 HIS A 382 REMARK 465 HIS A 383 REMARK 465 HIS A 384 REMARK 465 HIS A 385 REMARK 465 HIS A 386 REMARK 465 HIS A 387 REMARK 465 HIS A 388 REMARK 465 HIS A 389 REMARK 465 HIS A 390 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 27 45.40 -103.53 REMARK 500 ARG A 78 67.13 -68.40 REMARK 500 SER A 156 77.13 -159.43 REMARK 500 ARG A 162 76.83 -67.57 REMARK 500 SER A 187 -85.98 -130.93 REMARK 500 ALA A 207 -85.52 -95.11 REMARK 500 TYR A 224 -61.82 -147.48 REMARK 500 ARG A 245 73.04 -117.94 REMARK 500 GLN A1045 -75.84 -141.23 REMARK 500 SER A1060 -146.78 -88.44 REMARK 500 LYS A1061 155.59 63.41 REMARK 500 SER A1111 -52.55 -123.74 REMARK 500 PRO A1118 37.62 -83.63 REMARK 500 PHE A1121 13.76 -155.10 REMARK 500 GLU A1122 106.51 -29.22 REMARK 500 THR A1151 -162.93 -106.82 REMARK 500 THR A1154 23.92 -161.05 REMARK 500 LEU A1181 -8.74 63.65 REMARK 500 VAL A 323 -66.80 -120.55 REMARK 500 PHE A 327 76.96 -110.33 REMARK 500 ALA A 330 -145.15 51.38 REMARK 500 SER A 331 44.72 -81.67 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 610 OLA A 2003 REMARK 610 OLA A 2004 REMARK 610 OLA A 2005 REMARK 610 OLA A 2006 REMARK 610 OLA A 2007 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 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2002 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2003 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2004 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2005 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2006 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 4ZJC RELATED DB: PDB DBREF 4ZJ8 A 1 246 UNP O43613 OX1R_HUMAN 1 246 DBREF 4ZJ8 A 1001 1196 UNP Q9V2J8 Q9V2J8_PYRAB 218 413 DBREF 4ZJ8 A 288 380 UNP O43613 OX1R_HUMAN 288 380 SEQADV 4ZJ8 ASP A -7 UNP O43613 EXPRESSION TAG SEQADV 4ZJ8 TYR A -6 UNP O43613 EXPRESSION TAG SEQADV 4ZJ8 LYS A -5 UNP O43613 EXPRESSION TAG SEQADV 4ZJ8 ASP A -4 UNP O43613 EXPRESSION TAG SEQADV 4ZJ8 ASP A -3 UNP O43613 EXPRESSION TAG SEQADV 4ZJ8 ASP A -2 UNP O43613 EXPRESSION TAG SEQADV 4ZJ8 ASP A -1 UNP O43613 EXPRESSION TAG SEQADV 4ZJ8 ALA A 0 UNP O43613 EXPRESSION TAG SEQADV 4ZJ8 ILE A 319 UNP O43613 VAL 319 ENGINEERED MUTATION SEQADV 4ZJ8 HIS A 381 UNP O43613 EXPRESSION TAG SEQADV 4ZJ8 HIS A 382 UNP O43613 EXPRESSION TAG SEQADV 4ZJ8 HIS A 383 UNP O43613 EXPRESSION TAG SEQADV 4ZJ8 HIS A 384 UNP O43613 EXPRESSION TAG SEQADV 4ZJ8 HIS A 385 UNP O43613 EXPRESSION TAG SEQADV 4ZJ8 HIS A 386 UNP O43613 EXPRESSION TAG SEQADV 4ZJ8 HIS A 387 UNP O43613 EXPRESSION TAG SEQADV 4ZJ8 HIS A 388 UNP O43613 EXPRESSION TAG SEQADV 4ZJ8 HIS A 389 UNP O43613 EXPRESSION TAG SEQADV 4ZJ8 HIS A 390 UNP O43613 EXPRESSION TAG SEQRES 1 A 553 ASP TYR LYS ASP ASP ASP ASP ALA MET GLU PRO SER ALA SEQRES 2 A 553 THR PRO GLY ALA GLN MET GLY VAL PRO PRO GLY SER ARG SEQRES 3 A 553 GLU PRO SER PRO VAL PRO PRO ASP TYR GLU ASP GLU PHE SEQRES 4 A 553 LEU ARG TYR LEU TRP ARG ASP TYR LEU TYR PRO LYS GLN SEQRES 5 A 553 TYR GLU TRP VAL LEU ILE ALA ALA TYR VAL ALA VAL PHE SEQRES 6 A 553 VAL VAL ALA LEU VAL GLY ASN THR LEU VAL CYS LEU ALA SEQRES 7 A 553 VAL TRP ARG ASN HIS HIS MET ARG THR VAL THR ASN TYR SEQRES 8 A 553 PHE ILE VAL ASN LEU SER LEU ALA ASP VAL LEU VAL THR SEQRES 9 A 553 ALA ILE CYS LEU PRO ALA SER LEU LEU VAL ASP ILE THR SEQRES 10 A 553 GLU SER TRP LEU PHE GLY HIS ALA LEU CYS LYS VAL ILE SEQRES 11 A 553 PRO TYR LEU GLN ALA VAL SER VAL SER VAL ALA VAL LEU SEQRES 12 A 553 THR LEU SER PHE ILE ALA LEU ASP ARG TRP TYR ALA ILE SEQRES 13 A 553 CYS HIS PRO LEU LEU PHE LYS SER THR ALA ARG ARG ALA SEQRES 14 A 553 ARG GLY SER ILE LEU GLY ILE TRP ALA VAL SER LEU ALA SEQRES 15 A 553 ILE MET VAL PRO GLN ALA ALA VAL MET GLU CYS SER SER SEQRES 16 A 553 VAL LEU PRO GLU LEU ALA ASN ARG THR ARG LEU PHE SER SEQRES 17 A 553 VAL CYS ASP GLU ARG TRP ALA ASP ASP LEU TYR PRO LYS SEQRES 18 A 553 ILE TYR HIS SER CYS PHE PHE ILE VAL THR TYR LEU ALA SEQRES 19 A 553 PRO LEU GLY LEU MET ALA MET ALA TYR PHE GLN ILE PHE SEQRES 20 A 553 ARG LYS LEU TRP GLY ARG GLN GLY ILE ASP CYS SER PHE SEQRES 21 A 553 TRP ASN GLU SER TYR LEU THR GLY SER ARG ASP GLU ARG SEQRES 22 A 553 LYS LYS SER LEU LEU SER LYS PHE GLY MET ASP GLU GLY SEQRES 23 A 553 VAL THR PHE MET PHE ILE GLY ARG PHE ASP ARG GLY GLN SEQRES 24 A 553 LYS GLY VAL ASP VAL LEU LEU LYS ALA ILE GLU ILE LEU SEQRES 25 A 553 SER SER LYS LYS GLU PHE GLN GLU MET ARG PHE ILE ILE SEQRES 26 A 553 ILE GLY LYS GLY ASP PRO GLU LEU GLU GLY TRP ALA ARG SEQRES 27 A 553 SER LEU GLU GLU LYS HIS GLY ASN VAL LYS VAL ILE THR SEQRES 28 A 553 GLU MET LEU SER ARG GLU PHE VAL ARG GLU LEU TYR GLY SEQRES 29 A 553 SER VAL ASP PHE VAL ILE ILE PRO SER TYR PHE GLU PRO SEQRES 30 A 553 PHE GLY LEU VAL ALA LEU GLU ALA MET CYS LEU GLY ALA SEQRES 31 A 553 ILE PRO ILE ALA SER ALA VAL GLY GLY LEU ARG ASP ILE SEQRES 32 A 553 ILE THR ASN GLU THR GLY ILE LEU VAL LYS ALA GLY ASP SEQRES 33 A 553 PRO GLY GLU LEU ALA ASN ALA ILE LEU LYS ALA LEU GLU SEQRES 34 A 553 LEU SER ARG SER ASP LEU SER LYS PHE ARG GLU ASN CYS SEQRES 35 A 553 LYS LYS ARG ALA MET SER PHE SER LYS GLN MET ARG ALA SEQRES 36 A 553 ARG ARG LYS THR ALA LYS MET LEU MET VAL VAL LEU LEU SEQRES 37 A 553 VAL PHE ALA LEU CYS TYR LEU PRO ILE SER VAL LEU ASN SEQRES 38 A 553 ILE LEU LYS ARG VAL PHE GLY MET PHE ARG GLN ALA SER SEQRES 39 A 553 ASP ARG GLU ALA VAL TYR ALA CYS PHE THR PHE SER HIS SEQRES 40 A 553 TRP LEU VAL TYR ALA ASN SER ALA ALA ASN PRO ILE ILE SEQRES 41 A 553 TYR ASN PHE LEU SER GLY LYS PHE ARG GLU GLN PHE LYS SEQRES 42 A 553 ALA ALA PHE SER CYS CYS LEU PRO GLY LEU HIS HIS HIS SEQRES 43 A 553 HIS HIS HIS HIS HIS HIS HIS HET SUV A2001 32 HET OLA A2002 7 HET OLA A2003 9 HET OLA A2004 8 HET OLA A2005 16 HET OLA A2006 11 HET OLA A2007 7 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 6(C18 H34 O2) FORMUL 9 HOH *18(H2 O) HELIX 1 AA1 TYR A 27 ARG A 37 1 11 HELIX 2 AA2 GLU A 46 ASN A 74 1 29 HELIX 3 AA3 THR A 79 GLU A 110 1 32 HELIX 4 AA4 GLY A 115 HIS A 150 1 36 HELIX 5 AA5 PRO A 151 PHE A 154 5 4 HELIX 6 AA6 THR A 157 ILE A 175 1 19 HELIX 7 AA7 MET A 176 VAL A 182 1 7 HELIX 8 AA8 ASP A 209 TYR A 224 1 16 HELIX 9 AA9 TYR A 224 TRP A 243 1 20 HELIX 10 AB1 ASN A 1008 LEU A 1012 5 5 HELIX 11 AB2 SER A 1015 PHE A 1027 1 13 HELIX 12 AB3 GLY A 1047 LEU A 1058 1 12 HELIX 13 AB4 LYS A 1062 GLN A 1065 5 4 HELIX 14 AB5 ASP A 1076 HIS A 1090 1 15 HELIX 15 AB6 SER A 1101 GLY A 1110 1 10 HELIX 16 AB7 GLY A 1125 CYS A 1133 1 9 HELIX 17 AB8 GLY A 1144 ILE A 1150 1 7 HELIX 18 AB9 ASP A 1162 SER A 1177 1 16 HELIX 19 AC1 LEU A 1181 VAL A 323 1 52 HELIX 20 AC2 ARG A 333 SER A 362 1 30 HELIX 21 AC3 SER A 362 ALA A 372 1 11 SHEET 1 AA1 2 MET A 183 SER A 186 0 SHEET 2 AA1 2 VAL A 201 GLU A 204 -1 O ASP A 203 N GLU A 184 SHEET 1 AA2 6 VAL A1093 ILE A1096 0 SHEET 2 AA2 6 MET A1067 ILE A1072 1 N PHE A1069 O LYS A1094 SHEET 3 AA2 6 VAL A1033 ILE A1038 1 N PHE A1037 O ILE A1072 SHEET 4 AA2 6 PHE A1114 ILE A1117 1 O PHE A1114 N THR A1034 SHEET 5 AA2 6 ILE A1137 SER A1141 1 O ILE A1139 N VAL A1115 SHEET 6 AA2 6 ILE A1156 VAL A1158 1 O ILE A1156 N PRO A1138 SSBOND 1 CYS A 119 CYS A 202 1555 1555 2.03 SITE 1 AC1 15 ALA A 102 SER A 103 VAL A 106 TRP A 112 SITE 2 AC1 15 PRO A 123 GLN A 126 VAL A 130 GLN A 179 SITE 3 AC1 15 MET A 183 GLU A 204 PHE A 219 ILE A 314 SITE 4 AC1 15 ASN A 318 HIS A 344 TYR A 348 SITE 1 AC2 4 ILE A 50 PHE A 236 OLA A2003 OLA A2004 SITE 1 AC3 3 PHE A 236 ARG A 240 OLA A2002 SITE 1 AC4 3 MET A 233 PHE A 236 OLA A2002 SITE 1 AC5 4 THR A 109 PHE A 236 ARG A 240 TRP A 243 SITE 1 AC6 1 TYR A 146 CRYST1 63.242 64.992 181.478 90.00 90.00 90.00 P 21 21 21 4 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.015812 0.000000 0.000000 0.00000 SCALE2 0.000000 0.015387 0.000000 0.00000 SCALE3 0.000000 0.000000 0.005510 0.00000 ATOM 1 N ASP A 26 -11.568 6.995 -87.268 1.00 66.94 N ANISOU 1 N ASP A 26 7942 6514 10980 4000 -157 -46 N ATOM 2 CA ASP A 26 -12.300 5.737 -87.250 1.00 64.77 C ANISOU 2 CA ASP A 26 7293 6742 10573 3992 -262 86 C ATOM 3 C ASP A 26 -11.579 4.679 -86.427 1.00 60.65 C ANISOU 3 C ASP A 26 6938 6514 9592 3762 -135 -168 C ATOM 4 O ASP A 26 -11.976 4.376 -85.302 1.00 60.85 O ANISOU 4 O ASP A 26 6760 6842 9517 3808 181 -393 O ATOM 5 CB ASP A 26 -12.523 5.225 -88.676 1.00 63.47 C ANISOU 5 CB ASP A 26 7092 6643 10380 3830 -716 568 C ATOM 6 CG ASP A 26 -13.628 5.968 -89.398 1.00 68.61 C ANISOU 6 CG ASP A 26 7498 7285 11287 4116 -836 900 C ATOM 7 OD1 ASP A 26 -13.809 7.176 -89.136 1.00 70.46 O ANISOU 7 OD1 ASP A 26 7806 7256 11711 4410 -638 782 O ATOM 8 OD2 ASP A 26 -14.318 5.338 -90.225 1.00 69.33 O ANISOU 8 OD2 ASP A 26 7399 7633 11309 4031 -1228 1182 O ATOM 9 N TYR A 27 -10.517 4.120 -86.996 1.00 54.73 N ANISOU 9 N TYR A 27 6549 5700 8545 3395 -346 -93 N ATOM 10 CA TYR A 27 -9.756 3.072 -86.327 1.00 49.23 C ANISOU 10 CA TYR A 27 6015 5249 7440 3042 -269 -261 C ATOM 11 C TYR A 27 -8.448 3.616 -85.758 1.00 51.40 C ANISOU 11 C TYR A 27 6696 5248 7587 2959 -128 -577 C ATOM 12 O TYR A 27 -7.395 2.998 -85.912 1.00 48.26 O ANISOU 12 O TYR A 27 6539 4871 6926 2662 -231 -580 O ATOM 13 CB TYR A 27 -9.466 1.920 -87.296 1.00 54.67 C ANISOU 13 CB TYR A 27 6801 6085 7886 2719 -602 12 C ATOM 14 CG TYR A 27 -10.673 1.429 -88.067 1.00 56.25 C ANISOU 14 CG TYR A 27 6672 6490 8211 2728 -870 365 C ATOM 15 CD1 TYR A 27 -11.610 0.595 -87.472 1.00 49.21 C ANISOU 15 CD1 TYR A 27 5407 5985 7307 2629 -841 439 C ATOM 16 CD2 TYR A 27 -10.866 1.788 -89.395 1.00 57.31 C ANISOU 16 CD2 TYR A 27 6870 6447 8457 2786 -1185 662 C ATOM 17 CE1 TYR A 27 -12.711 0.139 -88.173 1.00 62.76 C ANISOU 17 CE1 TYR A 27 6786 7892 9166 2578 -1144 794 C ATOM 18 CE2 TYR A 27 -11.964 1.338 -90.106 1.00 60.66 C ANISOU 18 CE2 TYR A 27 7004 7059 8986 2755 -1506 999 C ATOM 19 CZ TYR A 27 -12.884 0.513 -89.490 1.00 63.05 C ANISOU 19 CZ TYR A 27 6903 7733 9320 2645 -1498 1062 C ATOM 20 OH TYR A 27 -13.979 0.061 -90.192 1.00 65.24 O ANISOU 20 OH TYR A 27 6854 8201 9732 2559 -1872 1429 O ATOM 21 N GLU A 28 -8.515 4.768 -85.097 1.00 50.97 N ANISOU 21 N GLU A 28 6710 4922 7733 3227 89 -847 N ATOM 22 CA GLU A 28 -7.307 5.415 -84.592 1.00 52.70 C ANISOU 22 CA GLU A 28 7309 4844 7871 3050 159 -1108 C ATOM 23 C GLU A 28 -6.785 4.761 -83.317 1.00 51.91 C ANISOU 23 C GLU A 28 7332 4981 7410 2889 315 -1433 C ATOM 24 O GLU A 28 -5.621 4.372 -83.252 1.00 49.54 O ANISOU 24 O GLU A 28 7256 4666 6900 2576 199 -1459 O ATOM 25 CB GLU A 28 -7.550 6.904 -84.339 1.00 55.35 C ANISOU 25 CB GLU A 28 7705 4792 8533 3211 305 -1242 C ATOM 26 CG GLU A 28 -6.290 7.654 -83.930 1.00 72.96 C ANISOU 26 CG GLU A 28 10321 6685 10717 2968 298 -1449 C ATOM 27 CD GLU A 28 -6.541 9.119 -83.638 1.00 77.77 C ANISOU 27 CD GLU A 28 11050 6856 11642 3139 417 -1602 C ATOM 28 OE1 GLU A 28 -7.628 9.621 -83.992 1.00 79.80 O ANISOU 28 OE1 GLU A 28 11089 7025 12205 3462 485 -1479 O ATOM 29 OE2 GLU A 28 -5.649 9.768 -83.049 1.00 79.09 O ANISOU 29 OE2 GLU A 28 11533 6752 11765 2954 422 -1837 O ATOM 30 N ASP A 29 -7.641 4.655 -82.305 1.00 51.76 N ANISOU 30 N ASP A 29 7132 5225 7311 3056 589 -1637 N ATOM 31 CA ASP A 29 -7.263 4.039 -81.035 1.00 64.44 C ANISOU 31 CA ASP A 29 8853 7119 8512 2835 745 -1891 C ATOM 32 C ASP A 29 -6.789 2.607 -81.271 1.00 58.35 C ANISOU 32 C ASP A 29 8041 6655 7473 2448 527 -1633 C ATOM 33 O ASP A 29 -5.787 2.160 -80.708 1.00 54.05 O ANISOU 33 O ASP A 29 7731 6146 6658 2168 448 -1742 O ATOM 34 CB ASP A 29 -8.442 4.061 -80.059 1.00 71.87 C ANISOU 34 CB ASP A 29 9537 8396 9376 3084 1120 -2067 C ATOM 35 CG ASP A 29 -8.002 4.077 -78.608 1.00 76.27 C ANISOU 35 CG ASP A 29 10378 9085 9518 2966 1346 -2468 C ATOM 36 OD1 ASP A 29 -6.851 3.682 -78.329 1.00 75.23 O ANISOU 36 OD1 ASP A 29 10554 8901 9128 2605 1142 -2514 O ATOM 37 OD2 ASP A 29 -8.811 4.487 -77.747 1.00 81.76 O ANISOU 37 OD2 ASP A 29 10957 9948 10160 3147 1712 -2673 O ATOM 38 N GLU A 30 -7.527 1.913 -82.130 1.00 58.01 N ANISOU 38 N GLU A 30 7710 6798 7534 2447 391 -1289 N ATOM 39 CA GLU A 30 -7.220 0.557 -82.566 1.00 55.69 C ANISOU 39 CA GLU A 30 7408 6707 7043 2133 136 -1036 C ATOM 40 C GLU A 30 -5.798 0.430 -83.123 1.00 38.65 C ANISOU 40 C GLU A 30 5561 4313 4811 1957 -76 -1032 C ATOM 41 O GLU A 30 -4.973 -0.335 -82.605 1.00 36.76 O ANISOU 41 O GLU A 30 5468 4171 4330 1721 -154 -1089 O ATOM 42 CB GLU A 30 -8.253 0.140 -83.619 1.00 57.86 C ANISOU 42 CB GLU A 30 7389 7094 7503 2192 -40 -689 C ATOM 43 CG GLU A 30 -8.126 -1.259 -84.181 1.00 57.50 C ANISOU 43 CG GLU A 30 7375 7197 7275 1894 -346 -444 C ATOM 44 CD GLU A 30 -9.300 -1.607 -85.082 1.00 60.83 C ANISOU 44 CD GLU A 30 7506 7740 7868 1916 -554 -119 C ATOM 45 OE1 GLU A 30 -10.323 -0.890 -85.023 1.00 66.49 O ANISOU 45 OE1 GLU A 30 7885 8531 8847 2158 -414 -62 O ATOM 46 OE2 GLU A 30 -9.204 -2.590 -85.847 1.00 59.44 O ANISOU 46 OE2 GLU A 30 7438 7572 7573 1705 -878 71 O ATOM 47 N PHE A 31 -5.517 1.203 -84.167 1.00 40.13 N ANISOU 47 N PHE A 31 5823 4205 5218 2078 -164 -938 N ATOM 48 CA PHE A 31 -4.244 1.125 -84.876 1.00 38.09 C ANISOU 48 CA PHE A 31 5781 3785 4907 1929 -315 -872 C ATOM 49 C PHE A 31 -3.069 1.603 -84.025 1.00 38.50 C ANISOU 49 C PHE A 31 6027 3700 4901 1797 -248 -1118 C ATOM 50 O PHE A 31 -1.994 1.001 -84.044 1.00 37.06 O ANISOU 50 O PHE A 31 5927 3575 4580 1605 -352 -1099 O ATOM 51 CB PHE A 31 -4.319 1.935 -86.172 1.00 38.82 C ANISOU 51 CB PHE A 31 5905 3628 5218 2062 -398 -662 C ATOM 52 CG PHE A 31 -3.173 1.689 -87.110 1.00 35.37 C ANISOU 52 CG PHE A 31 5629 3137 4672 1912 -509 -520 C ATOM 53 CD1 PHE A 31 -2.926 0.418 -87.602 1.00 33.26 C ANISOU 53 CD1 PHE A 31 5383 3088 4166 1807 -634 -422 C ATOM 54 CD2 PHE A 31 -2.355 2.731 -87.514 1.00 38.59 C ANISOU 54 CD2 PHE A 31 6169 3275 5220 1881 -479 -478 C ATOM 55 CE1 PHE A 31 -1.875 0.187 -88.470 1.00 32.87 C ANISOU 55 CE1 PHE A 31 5463 3031 3995 1734 -667 -325 C ATOM 56 CE2 PHE A 31 -1.303 2.507 -88.383 1.00 38.12 C ANISOU 56 CE2 PHE A 31 6195 3246 5042 1743 -514 -318 C ATOM 57 CZ PHE A 31 -1.063 1.233 -88.861 1.00 35.45 C ANISOU 57 CZ PHE A 31 5855 3171 4442 1701 -579 -260 C ATOM 58 N LEU A 32 -3.277 2.688 -83.284 1.00 39.13 N ANISOU 58 N LEU A 32 6181 3588 5099 1912 -96 -1355 N ATOM 59 CA LEU A 32 -2.246 3.217 -82.397 1.00 40.12 C ANISOU 59 CA LEU A 32 6531 3555 5158 1749 -90 -1614 C ATOM 60 C LEU A 32 -1.892 2.197 -81.322 1.00 41.50 C ANISOU 60 C LEU A 32 6728 4043 4997 1539 -114 -1729 C ATOM 61 O LEU A 32 -0.711 1.970 -81.037 1.00 41.53 O ANISOU 61 O LEU A 32 6836 4037 4908 1305 -260 -1755 O ATOM 62 CB LEU A 32 -2.701 4.530 -81.757 1.00 47.59 C ANISOU 62 CB LEU A 32 7612 4209 6260 1932 67 -1895 C ATOM 63 CG LEU A 32 -2.666 5.763 -82.661 1.00 46.37 C ANISOU 63 CG LEU A 32 7502 3640 6476 2019 25 -1756 C ATOM 64 CD1 LEU A 32 -3.185 6.986 -81.924 1.00 51.72 C ANISOU 64 CD1 LEU A 32 8271 4062 7319 2151 197 -2011 C ATOM 65 CD2 LEU A 32 -1.256 6.006 -83.177 1.00 45.34 C ANISOU 65 CD2 LEU A 32 7545 3282 6398 1758 -178 -1647 C ATOM 66 N ARG A 33 -2.914 1.582 -80.733 1.00 39.58 N ANISOU 66 N ARG A 33 6359 4094 4586 1606 14 -1754 N ATOM 67 CA ARG A 33 -2.687 0.500 -79.783 1.00 38.88 C ANISOU 67 CA ARG A 33 6298 4316 4157 1378 -39 -1774 C ATOM 68 C ARG A 33 -1.909 -0.629 -80.449 1.00 40.66 C ANISOU 68 C ARG A 33 6490 4607 4351 1210 -303 -1522 C ATOM 69 O ARG A 33 -1.035 -1.229 -79.830 1.00 40.80 O ANISOU 69 O ARG A 33 6607 4704 4191 1006 -455 -1543 O ATOM 70 CB ARG A 33 -4.007 -0.029 -79.215 1.00 40.54 C ANISOU 70 CB ARG A 33 6324 4867 4212 1442 152 -1740 C ATOM 71 CG ARG A 33 -4.576 0.796 -78.069 1.00 44.91 C ANISOU 71 CG ARG A 33 6953 5485 4624 1578 468 -2071 C ATOM 72 CD ARG A 33 -5.790 0.118 -77.448 1.00 56.90 C ANISOU 72 CD ARG A 33 8223 7455 5939 1587 699 -1980 C ATOM 73 NE ARG A 33 -6.435 0.956 -76.440 1.00 62.04 N ANISOU 73 NE ARG A 33 8916 8214 6444 1804 1093 -2321 N ATOM 74 CZ ARG A 33 -6.168 0.905 -75.138 1.00 66.27 C ANISOU 74 CZ ARG A 33 9705 8944 6529 1651 1227 -2570 C ATOM 75 NH1 ARG A 33 -5.264 0.052 -74.678 1.00 63.82 N ANISOU 75 NH1 ARG A 33 9599 8732 5916 1265 950 -2466 N ATOM 76 NH2 ARG A 33 -6.808 1.706 -74.296 1.00 72.80 N ANISOU 76 NH2 ARG A 33 10598 9868 7195 1907 1632 -2927 N ATOM 77 N TYR A 34 -2.213 -0.905 -81.715 1.00 39.72 N ANISOU 77 N TYR A 34 6252 4443 4398 1318 -372 -1294 N ATOM 78 CA TYR A 34 -1.509 -1.964 -82.439 1.00 35.49 C ANISOU 78 CA TYR A 34 5730 3941 3815 1230 -587 -1111 C ATOM 79 C TYR A 34 -0.028 -1.643 -82.652 1.00 34.89 C ANISOU 79 C TYR A 34 5731 3721 3806 1162 -658 -1148 C ATOM 80 O TYR A 34 0.816 -2.538 -82.617 1.00 34.28 O ANISOU 80 O TYR A 34 5662 3717 3647 1079 -811 -1092 O ATOM 81 CB TYR A 34 -2.176 -2.233 -83.790 1.00 30.61 C ANISOU 81 CB TYR A 34 5035 3297 3298 1359 -649 -898 C ATOM 82 CG TYR A 34 -1.576 -3.402 -84.544 1.00 28.99 C ANISOU 82 CG TYR A 34 4908 3115 2993 1316 -852 -771 C ATOM 83 CD1 TYR A 34 -1.792 -4.708 -84.124 1.00 34.93 C ANISOU 83 CD1 TYR A 34 5694 3989 3588 1196 -1025 -714 C ATOM 84 CD2 TYR A 34 -0.797 -3.200 -85.677 1.00 28.54 C ANISOU 84 CD2 TYR A 34 4913 2946 2985 1403 -860 -708 C ATOM 85 CE1 TYR A 34 -1.248 -5.780 -84.808 1.00 34.18 C ANISOU 85 CE1 TYR A 34 5726 3842 3420 1212 -1224 -647 C ATOM 86 CE2 TYR A 34 -0.249 -4.267 -86.369 1.00 27.93 C ANISOU 86 CE2 TYR A 34 4932 2891 2788 1433 -997 -652 C ATOM 87 CZ TYR A 34 -0.478 -5.554 -85.930 1.00 27.65 C ANISOU 87 CZ TYR A 34 4963 2915 2628 1360 -1190 -646 C ATOM 88 OH TYR A 34 0.064 -6.621 -86.612 1.00 27.85 O ANISOU 88 OH TYR A 34 5138 2891 2554 1441 -1341 -636 O ATOM 89 N LEU A 35 0.287 -0.370 -82.871 1.00 32.19 N ANISOU 89 N LEU A 35 5422 3164 3644 1198 -562 -1218 N ATOM 90 CA LEU A 35 1.668 0.030 -83.127 1.00 35.44 C ANISOU 90 CA LEU A 35 5841 3464 4161 1081 -624 -1193 C ATOM 91 C LEU A 35 2.492 0.145 -81.847 1.00 33.85 C ANISOU 91 C LEU A 35 5706 3277 3880 867 -727 -1370 C ATOM 92 O LEU A 35 3.679 -0.185 -81.836 1.00 36.46 O ANISOU 92 O LEU A 35 5953 3660 4240 737 -863 -1300 O ATOM 93 CB LEU A 35 1.711 1.361 -83.884 1.00 34.47 C ANISOU 93 CB LEU A 35 5751 3070 4278 1128 -534 -1137 C ATOM 94 CG LEU A 35 1.185 1.348 -85.321 1.00 39.27 C ANISOU 94 CG LEU A 35 6315 3658 4947 1292 -489 -896 C ATOM 95 CD1 LEU A 35 1.459 2.677 -86.006 1.00 35.58 C ANISOU 95 CD1 LEU A 35 5905 2904 4709 1274 -445 -779 C ATOM 96 CD2 LEU A 35 1.797 0.199 -86.106 1.00 38.08 C ANISOU 96 CD2 LEU A 35 6100 3721 4649 1298 -541 -745 C ATOM 97 N TRP A 36 1.862 0.605 -80.770 1.00 35.55 N ANISOU 97 N TRP A 36 6061 3467 3978 841 -666 -1599 N ATOM 98 CA TRP A 36 2.591 0.901 -79.539 1.00 42.42 C ANISOU 98 CA TRP A 36 7080 4319 4717 612 -792 -1801 C ATOM 99 C TRP A 36 2.396 -0.140 -78.437 1.00 42.02 C ANISOU 99 C TRP A 36 7086 4554 4326 505 -879 -1845 C ATOM 100 O TRP A 36 2.765 0.096 -77.287 1.00 44.36 O ANISOU 100 O TRP A 36 7565 4874 4415 314 -981 -2032 O ATOM 101 CB TRP A 36 2.182 2.279 -79.015 1.00 40.98 C ANISOU 101 CB TRP A 36 7122 3866 4584 641 -674 -2087 C ATOM 102 CG TRP A 36 2.589 3.395 -79.922 1.00 44.06 C ANISOU 102 CG TRP A 36 7518 3902 5321 654 -678 -2016 C ATOM 103 CD1 TRP A 36 1.928 3.833 -81.033 1.00 43.91 C ANISOU 103 CD1 TRP A 36 7422 3732 5529 880 -541 -1863 C ATOM 104 CD2 TRP A 36 3.754 4.218 -79.798 1.00 44.39 C ANISOU 104 CD2 TRP A 36 7649 3694 5525 383 -867 -2043 C ATOM 105 NE1 TRP A 36 2.611 4.876 -81.609 1.00 46.50 N ANISOU 105 NE1 TRP A 36 7811 3725 6132 768 -614 -1778 N ATOM 106 CE2 TRP A 36 3.738 5.131 -80.870 1.00 48.78 C ANISOU 106 CE2 TRP A 36 8186 3947 6401 448 -809 -1883 C ATOM 107 CE3 TRP A 36 4.815 4.266 -78.888 1.00 50.82 C ANISOU 107 CE3 TRP A 36 8547 4515 6248 54 -1121 -2148 C ATOM 108 CZ2 TRP A 36 4.736 6.084 -81.056 1.00 52.00 C ANISOU 108 CZ2 TRP A 36 8652 4055 7052 171 -973 -1813 C ATOM 109 CZ3 TRP A 36 5.806 5.213 -79.073 1.00 54.05 C ANISOU 109 CZ3 TRP A 36 8987 4635 6916 -218 -1306 -2097 C ATOM 110 CH2 TRP A 36 5.759 6.109 -80.148 1.00 54.65 C ANISOU 110 CH2 TRP A 36 9036 4407 7321 -170 -1219 -1924 C ATOM 111 N ARG A 37 1.835 -1.292 -78.790 1.00 35.62 N ANISOU 111 N ARG A 37 6156 3941 3437 591 -877 -1655 N ATOM 112 CA ARG A 37 1.500 -2.319 -77.804 1.00 36.10 C ANISOU 112 CA ARG A 37 6279 4257 3179 462 -964 -1623 C ATOM 113 C ARG A 37 2.719 -2.922 -77.109 1.00 43.04 C ANISOU 113 C ARG A 37 7210 5194 3949 242 -1283 -1568 C ATOM 114 O ARG A 37 2.599 -3.495 -76.027 1.00 43.42 O ANISOU 114 O ARG A 37 7390 5423 3684 68 -1395 -1565 O ATOM 115 CB ARG A 37 0.695 -3.437 -78.464 1.00 34.11 C ANISOU 115 CB ARG A 37 5901 4128 2929 557 -966 -1388 C ATOM 116 CG ARG A 37 1.368 -4.033 -79.681 1.00 31.87 C ANISOU 116 CG ARG A 37 5516 3733 2861 663 -1114 -1210 C ATOM 117 CD ARG A 37 0.594 -5.226 -80.204 1.00 30.74 C ANISOU 117 CD ARG A 37 5347 3661 2672 709 -1199 -1017 C ATOM 118 NE ARG A 37 1.195 -5.765 -81.419 1.00 47.81 N ANISOU 118 NE ARG A 37 7482 5699 4986 860 -1309 -916 N ATOM 119 CZ ARG A 37 0.674 -6.756 -82.134 1.00 47.08 C ANISOU 119 CZ ARG A 37 7434 5581 4875 922 -1429 -786 C ATOM 120 NH1 ARG A 37 -0.465 -7.321 -81.756 1.00 46.95 N ANISOU 120 NH1 ARG A 37 7437 5660 4743 796 -1483 -684 N ATOM 121 NH2 ARG A 37 1.290 -7.179 -83.229 1.00 46.76 N ANISOU 121 NH2 ARG A 37 7424 5426 4916 1096 -1493 -758 N ATOM 122 N ASP A 38 3.887 -2.802 -77.731 1.00 43.91 N ANISOU 122 N ASP A 38 7191 5179 4316 245 -1432 -1489 N ATOM 123 CA ASP A 38 5.104 -3.375 -77.169 1.00 48.08 C ANISOU 123 CA ASP A 38 7673 5769 4827 78 -1765 -1395 C ATOM 124 C ASP A 38 6.070 -2.294 -76.699 1.00 48.88 C ANISOU 124 C ASP A 38 7798 5760 5013 -130 -1891 -1528 C ATOM 125 O ASP A 38 7.229 -2.575 -76.390 1.00 49.74 O ANISOU 125 O ASP A 38 7779 5913 5206 -275 -2192 -1419 O ATOM 126 CB ASP A 38 5.793 -4.278 -78.192 1.00 51.23 C ANISOU 126 CB ASP A 38 7833 6162 5470 258 -1861 -1171 C ATOM 127 CG ASP A 38 6.212 -3.527 -79.440 1.00 56.24 C ANISOU 127 CG ASP A 38 8283 6681 6405 399 -1669 -1147 C ATOM 128 OD1 ASP A 38 5.396 -2.736 -79.960 1.00 54.55 O ANISOU 128 OD1 ASP A 38 8142 6366 6218 472 -1423 -1226 O ATOM 129 OD2 ASP A 38 7.360 -3.722 -79.893 1.00 63.04 O ANISOU 129 OD2 ASP A 38 8907 7570 7476 438 -1760 -1024 O ATOM 130 N TYR A 39 5.589 -1.058 -76.652 1.00 41.20 N ANISOU 130 N TYR A 39 6984 4621 4049 -145 -1694 -1753 N ATOM 131 CA TYR A 39 6.404 0.055 -76.190 1.00 44.40 C ANISOU 131 CA TYR A 39 7491 4843 4534 -387 -1850 -1908 C ATOM 132 C TYR A 39 6.443 0.094 -74.668 1.00 47.75 C ANISOU 132 C TYR A 39 8144 5394 4605 -628 -1975 -2057 C ATOM 133 O TYR A 39 5.608 0.738 -74.034 1.00 51.67 O ANISOU 133 O TYR A 39 8850 5876 4908 -604 -1726 -2292 O ATOM 134 CB TYR A 39 5.873 1.382 -76.743 1.00 46.44 C ANISOU 134 CB TYR A 39 7867 4799 4980 -287 -1600 -2076 C ATOM 135 CG TYR A 39 6.659 2.602 -76.309 1.00 48.99 C ANISOU 135 CG TYR A 39 8360 4838 5416 -571 -1798 -2243 C ATOM 136 CD1 TYR A 39 7.903 2.882 -76.858 1.00 49.97 C ANISOU 136 CD1 TYR A 39 8225 4887 5875 -779 -2005 -2019 C ATOM 137 CD2 TYR A 39 6.149 3.480 -75.360 1.00 57.19 C ANISOU 137 CD2 TYR A 39 9708 5753 6269 -626 -1691 -2548 C ATOM 138 CE1 TYR A 39 8.622 3.997 -76.468 1.00 57.26 C ANISOU 138 CE1 TYR A 39 9301 5525 6932 -1113 -2244 -2133 C ATOM 139 CE2 TYR A 39 6.861 4.597 -74.964 1.00 61.17 C ANISOU 139 CE2 TYR A 39 10361 5985 6895 -892 -1869 -2677 C ATOM 140 CZ TYR A 39 8.096 4.851 -75.521 1.00 61.10 C ANISOU 140 CZ TYR A 39 10196 5813 7205 -1171 -2205 -2482 C ATOM 141 OH TYR A 39 8.807 5.963 -75.129 1.00 65.88 O ANISOU 141 OH TYR A 39 10934 6144 7954 -1488 -2413 -2565 O ATOM 142 N LEU A 40 7.402 -0.614 -74.083 1.00123.55 N ANISOU 142 N LEU A 40 20425 19249 7267 -5673 295 -1146 N ATOM 143 CA LEU A 40 7.623 -0.514 -72.649 1.00119.55 C ANISOU 143 CA LEU A 40 19752 18416 7254 -5824 410 -1134 C ATOM 144 C LEU A 40 8.507 0.696 -72.383 1.00117.04 C ANISOU 144 C LEU A 40 19103 18154 7215 -5581 1018 -996 C ATOM 145 O LEU A 40 9.545 0.871 -73.021 1.00118.28 O ANISOU 145 O LEU A 40 19314 18423 7204 -5286 1301 -1159 O ATOM 146 CB LEU A 40 8.247 -1.799 -72.086 1.00119.77 C ANISOU 146 CB LEU A 40 20148 18031 7328 -5850 56 -1593 C ATOM 147 CG LEU A 40 9.583 -2.340 -72.610 1.00121.56 C ANISOU 147 CG LEU A 40 20640 18173 7373 -5448 92 -2121 C ATOM 148 CD1 LEU A 40 10.763 -1.805 -71.808 1.00118.92 C ANISOU 148 CD1 LEU A 40 20111 17689 7383 -5241 553 -2241 C ATOM 149 CD2 LEU A 40 9.575 -3.862 -72.593 1.00124.45 C ANISOU 149 CD2 LEU A 40 21480 18165 7641 -5512 -606 -2566 C ATOM 150 N TYR A 41 8.073 1.551 -71.465 1.00114.13 N ANISOU 150 N TYR A 41 18350 17748 7265 -5710 1201 -713 N ATOM 151 CA TYR A 41 8.860 2.718 -71.101 1.00114.47 C ANISOU 151 CA TYR A 41 18058 17761 7676 -5499 1703 -592 C ATOM 152 C TYR A 41 9.595 2.455 -69.794 1.00111.13 C ANISOU 152 C TYR A 41 17583 17021 7622 -5487 1798 -870 C ATOM 153 O TYR A 41 8.974 2.369 -68.735 1.00109.16 O ANISOU 153 O TYR A 41 17172 16700 7604 -5710 1653 -829 O ATOM 154 CB TYR A 41 7.977 3.961 -70.981 1.00111.55 C ANISOU 154 CB TYR A 41 17261 17540 7582 -5553 1800 -166 C ATOM 155 CG TYR A 41 8.762 5.241 -70.808 1.00110.45 C ANISOU 155 CG TYR A 41 16796 17320 7851 -5330 2236 -3 C ATOM 156 CD1 TYR A 41 9.273 5.919 -71.907 1.00117.64 C ANISOU 156 CD1 TYR A 41 17725 18373 8600 -5180 2466 253 C ATOM 157 CD2 TYR A 41 8.998 5.769 -69.545 1.00107.32 C ANISOU 157 CD2 TYR A 41 16062 16722 7992 -5295 2392 -91 C ATOM 158 CE1 TYR A 41 9.995 7.088 -71.754 1.00117.13 C ANISOU 158 CE1 TYR A 41 17365 18188 8950 -5045 2815 458 C ATOM 159 CE2 TYR A 41 9.718 6.937 -69.382 1.00110.92 C ANISOU 159 CE2 TYR A 41 16215 17045 8884 -5095 2729 36 C ATOM 160 CZ TYR A 41 10.214 7.592 -70.489 1.00113.76 C ANISOU 160 CZ TYR A 41 16613 17484 9126 -4992 2928 331 C ATOM 161 OH TYR A 41 10.932 8.755 -70.331 1.00113.51 O ANISOU 161 OH TYR A 41 16282 17277 9570 -4859 3217 512 O ATOM 162 N PRO A 42 10.926 2.316 -69.870 1.00111.32 N ANISOU 162 N PRO A 42 17719 16914 7665 -5228 2036 -1170 N ATOM 163 CA PRO A 42 11.755 2.023 -68.696 1.00108.08 C ANISOU 163 CA PRO A 42 17295 16185 7587 -5163 2101 -1482 C ATOM 164 C PRO A 42 11.738 3.154 -67.671 1.00104.97 C ANISOU 164 C PRO A 42 16426 15741 7718 -5151 2404 -1297 C ATOM 165 O PRO A 42 12.305 4.219 -67.916 1.00102.60 O ANISOU 165 O PRO A 42 15846 15484 7653 -4955 2789 -1170 O ATOM 166 CB PRO A 42 13.156 1.842 -69.290 1.00109.35 C ANISOU 166 CB PRO A 42 17593 16336 7621 -4833 2335 -1839 C ATOM 167 CG PRO A 42 13.123 2.584 -70.583 1.00110.00 C ANISOU 167 CG PRO A 42 17565 16802 7426 -4748 2593 -1555 C ATOM 168 CD PRO A 42 11.728 2.425 -71.101 1.00113.70 C ANISOU 168 CD PRO A 42 18135 17438 7629 -4982 2254 -1249 C ATOM 169 N LYS A 43 11.088 2.918 -66.535 1.00101.03 N ANISOU 169 N LYS A 43 15818 15179 7390 -5374 2202 -1286 N ATOM 170 CA LYS A 43 11.022 3.910 -65.469 1.00105.96 C ANISOU 170 CA LYS A 43 15958 15817 8485 -5328 2431 -1215 C ATOM 171 C LYS A 43 12.382 4.058 -64.796 1.00103.69 C ANISOU 171 C LYS A 43 15618 15260 8517 -5064 2697 -1529 C ATOM 172 O LYS A 43 13.019 3.067 -64.438 1.00103.09 O ANISOU 172 O LYS A 43 15869 14969 8331 -5057 2539 -1835 O ATOM 173 CB LYS A 43 9.955 3.526 -64.441 1.00106.14 C ANISOU 173 CB LYS A 43 15844 15994 8491 -5662 2148 -1153 C ATOM 174 CG LYS A 43 9.766 4.543 -63.324 1.00104.91 C ANISOU 174 CG LYS A 43 15120 15976 8765 -5582 2346 -1158 C ATOM 175 CD LYS A 43 8.647 4.125 -62.380 1.00107.15 C ANISOU 175 CD LYS A 43 15213 16593 8908 -5954 2084 -1097 C ATOM 176 CE LYS A 43 8.424 5.159 -61.287 1.00106.74 C ANISOU 176 CE LYS A 43 14526 16794 9236 -5817 2266 -1195 C ATOM 177 NZ LYS A 43 7.287 4.793 -60.397 1.00 97.07 N ANISOU 177 NZ LYS A 43 13023 16070 7789 -6203 2050 -1144 N ATOM 178 N GLN A 44 12.820 5.302 -64.631 1.00103.23 N ANISOU 178 N GLN A 44 15150 15181 8891 -4843 3049 -1463 N ATOM 179 CA GLN A 44 14.130 5.592 -64.059 1.00101.61 C ANISOU 179 CA GLN A 44 14830 14736 9043 -4581 3327 -1758 C ATOM 180 C GLN A 44 14.221 5.159 -62.599 1.00 97.42 C ANISOU 180 C GLN A 44 14242 14092 8683 -4614 3196 -2027 C ATOM 181 O GLN A 44 15.214 4.565 -62.178 1.00 95.79 O ANISOU 181 O GLN A 44 14233 13655 8509 -4482 3199 -2366 O ATOM 182 CB GLN A 44 14.441 7.086 -64.180 1.00103.84 C ANISOU 182 CB GLN A 44 14654 14987 9813 -4392 3658 -1575 C ATOM 183 CG GLN A 44 15.818 7.483 -63.672 1.00104.41 C ANISOU 183 CG GLN A 44 14557 14817 10300 -4136 3957 -1867 C ATOM 184 CD GLN A 44 16.059 8.979 -63.754 1.00106.52 C ANISOU 184 CD GLN A 44 14365 14986 11123 -4004 4201 -1645 C ATOM 185 OE1 GLN A 44 15.224 9.727 -64.264 1.00109.62 O ANISOU 185 OE1 GLN A 44 14599 15468 11585 -4082 4123 -1261 O ATOM 186 NE2 GLN A 44 17.205 9.423 -63.249 1.00105.75 N ANISOU 186 NE2 GLN A 44 14053 14667 11459 -3804 4445 -1891 N ATOM 187 N TYR A 45 13.177 5.454 -61.832 1.00 95.76 N ANISOU 187 N TYR A 45 13739 14096 8551 -4785 3064 -1889 N ATOM 188 CA TYR A 45 13.171 5.151 -60.407 1.00 95.18 C ANISOU 188 CA TYR A 45 13537 14051 8577 -4851 2960 -2091 C ATOM 189 C TYR A 45 12.285 3.952 -60.085 1.00 95.84 C ANISOU 189 C TYR A 45 13919 14298 8198 -5281 2555 -1976 C ATOM 190 O TYR A 45 11.111 4.108 -59.750 1.00 97.82 O ANISOU 190 O TYR A 45 13901 14934 8334 -5540 2432 -1779 O ATOM 191 CB TYR A 45 12.714 6.376 -59.611 1.00 93.17 C ANISOU 191 CB TYR A 45 12641 14021 8737 -4722 3105 -2096 C ATOM 192 CG TYR A 45 13.655 7.554 -59.721 1.00 92.39 C ANISOU 192 CG TYR A 45 12235 13670 9200 -4330 3428 -2217 C ATOM 193 CD1 TYR A 45 15.009 7.364 -59.974 1.00 87.84 C ANISOU 193 CD1 TYR A 45 11884 12754 8739 -4133 3620 -2415 C ATOM 194 CD2 TYR A 45 13.192 8.856 -59.577 1.00 93.04 C ANISOU 194 CD2 TYR A 45 11781 13847 9724 -4162 3497 -2152 C ATOM 195 CE1 TYR A 45 15.874 8.436 -60.078 1.00 92.16 C ANISOU 195 CE1 TYR A 45 12123 13084 9809 -3846 3910 -2487 C ATOM 196 CE2 TYR A 45 14.050 9.935 -59.680 1.00 93.09 C ANISOU 196 CE2 TYR A 45 11518 13550 10301 -3855 3724 -2219 C ATOM 197 CZ TYR A 45 15.390 9.718 -59.931 1.00 92.90 C ANISOU 197 CZ TYR A 45 11719 13212 10365 -3731 3949 -2357 C ATOM 198 OH TYR A 45 16.249 10.788 -60.034 1.00 93.12 O ANISOU 198 OH TYR A 45 11453 12956 10972 -3492 4171 -2387 O ATOM 199 N GLU A 46 12.855 2.756 -60.189 1.00 96.38 N ANISOU 199 N GLU A 46 14526 14074 8021 -5362 2313 -2114 N ATOM 200 CA GLU A 46 12.127 1.533 -59.873 1.00 93.59 C ANISOU 200 CA GLU A 46 14522 13758 7280 -5816 1844 -1973 C ATOM 201 C GLU A 46 12.688 0.843 -58.637 1.00 98.15 C ANISOU 201 C GLU A 46 15266 14149 7876 -5899 1643 -2139 C ATOM 202 O GLU A 46 11.932 0.387 -57.780 1.00100.16 O ANISOU 202 O GLU A 46 15482 14647 7928 -6318 1393 -1932 O ATOM 203 CB GLU A 46 12.152 0.567 -61.058 1.00 95.77 C ANISOU 203 CB GLU A 46 15351 13794 7242 -5890 1542 -1974 C ATOM 204 CG GLU A 46 11.197 0.930 -62.179 1.00 98.10 C ANISOU 204 CG GLU A 46 15555 14367 7352 -5988 1567 -1706 C ATOM 205 CD GLU A 46 10.984 -0.215 -63.150 1.00101.00 C ANISOU 205 CD GLU A 46 16465 14563 7349 -6146 1144 -1719 C ATOM 206 OE1 GLU A 46 11.623 -1.274 -62.969 1.00102.11 O ANISOU 206 OE1 GLU A 46 17054 14323 7419 -6150 807 -1964 O ATOM 207 OE2 GLU A 46 10.175 -0.059 -64.089 1.00101.41 O ANISOU 207 OE2 GLU A 46 16493 14841 7197 -6240 1097 -1516 O ATOM 208 N TRP A 47 14.013 0.769 -58.549 1.00 92.26 N ANISOU 208 N TRP A 47 14690 13014 7352 -5519 1744 -2499 N ATOM 209 CA TRP A 47 14.667 0.082 -57.439 1.00 93.30 C ANISOU 209 CA TRP A 47 15039 12898 7514 -5538 1501 -2688 C ATOM 210 C TRP A 47 14.359 0.758 -56.107 1.00 91.24 C ANISOU 210 C TRP A 47 14275 13014 7378 -5607 1677 -2628 C ATOM 211 O TRP A 47 14.308 0.102 -55.065 1.00 92.44 O ANISOU 211 O TRP A 47 14567 13188 7369 -5864 1386 -2570 O ATOM 212 CB TRP A 47 16.180 0.014 -57.663 1.00 91.56 C ANISOU 212 CB TRP A 47 15005 12235 7548 -5041 1611 -3162 C ATOM 213 CG TRP A 47 16.854 1.350 -57.712 1.00 91.53 C ANISOU 213 CG TRP A 47 14485 12329 7961 -4615 2185 -3351 C ATOM 214 CD1 TRP A 47 17.011 2.150 -58.806 1.00 88.80 C ANISOU 214 CD1 TRP A 47 13938 12067 7735 -4409 2549 -3325 C ATOM 215 CD2 TRP A 47 17.475 2.038 -56.619 1.00 87.25 C ANISOU 215 CD2 TRP A 47 13570 11796 7785 -4371 2414 -3573 C ATOM 216 NE1 TRP A 47 17.687 3.296 -58.461 1.00 87.04 N ANISOU 216 NE1 TRP A 47 13245 11855 7970 -4089 2968 -3482 N ATOM 217 CE2 TRP A 47 17.983 3.251 -57.125 1.00 88.22 C ANISOU 217 CE2 TRP A 47 13272 11952 8296 -4034 2893 -3674 C ATOM 218 CE3 TRP A 47 17.648 1.746 -55.263 1.00 87.36 C ANISOU 218 CE3 TRP A 47 13564 11805 7824 -4419 2234 -3681 C ATOM 219 CZ2 TRP A 47 18.653 4.172 -56.321 1.00 86.63 C ANISOU 219 CZ2 TRP A 47 12626 11728 8563 -3728 3172 -3921 C ATOM 220 CZ3 TRP A 47 18.312 2.661 -54.467 1.00 85.26 C ANISOU 220 CZ3 TRP A 47 12848 11577 7971 -4077 2540 -3957 C ATOM 221 CH2 TRP A 47 18.806 3.859 -54.998 1.00 86.11 C ANISOU 221 CH2 TRP A 47 12533 11667 8517 -3728 2994 -4095 C ATOM 222 N VAL A 48 14.145 2.069 -56.145 1.00 89.52 N ANISOU 222 N VAL A 48 13468 13106 7439 -5375 2110 -2646 N ATOM 223 CA VAL A 48 13.758 2.807 -54.949 1.00 92.88 C ANISOU 223 CA VAL A 48 13329 13975 7987 -5376 2261 -2675 C ATOM 224 C VAL A 48 12.330 2.462 -54.545 1.00 97.63 C ANISOU 224 C VAL A 48 13778 15146 8171 -5916 2039 -2321 C ATOM 225 O VAL A 48 12.006 2.426 -53.358 1.00 92.36 O ANISOU 225 O VAL A 48 12840 14898 7355 -6104 1983 -2309 O ATOM 226 CB VAL A 48 13.880 4.331 -55.150 1.00 90.03 C ANISOU 226 CB VAL A 48 12369 13729 8111 -4952 2688 -2830 C ATOM 227 CG1 VAL A 48 15.337 4.756 -55.113 1.00 86.53 C ANISOU 227 CG1 VAL A 48 11927 12836 8114 -4474 2925 -3200 C ATOM 228 CG2 VAL A 48 13.226 4.754 -56.455 1.00 89.35 C ANISOU 228 CG2 VAL A 48 12256 13684 8007 -4988 2765 -2579 C ATOM 229 N LEU A 49 11.478 2.204 -55.533 1.00 38.16 N ANISOU 229 N LEU A 49 5113 5351 4036 679 254 -1956 N ATOM 230 CA LEU A 49 10.098 1.829 -55.258 1.00 39.68 C ANISOU 230 CA LEU A 49 5375 5530 4172 652 246 -1895 C ATOM 231 C LEU A 49 10.043 0.427 -54.668 1.00 44.02 C ANISOU 231 C LEU A 49 5979 6058 4688 677 191 -1900 C ATOM 232 O LEU A 49 9.287 0.168 -53.730 1.00 48.36 O ANISOU 232 O LEU A 49 6562 6611 5203 665 164 -1872 O ATOM 233 CB LEU A 49 9.245 1.905 -56.524 1.00 29.18 C ANISOU 233 CB LEU A 49 4099 4170 2818 621 297 -1853 C ATOM 234 CG LEU A 49 7.758 1.638 -56.283 1.00 28.67 C ANISOU 234 CG LEU A 49 4096 4096 2702 587 291 -1796 C ATOM 235 CD1 LEU A 49 7.250 2.511 -55.149 1.00 30.74 C ANISOU 235 CD1 LEU A 49 4321 4393 2964 567 278 -1777 C ATOM 236 CD2 LEU A 49 6.946 1.871 -57.549 1.00 28.45 C ANISOU 236 CD2 LEU A 49 4109 4046 2655 562 338 -1762 C ATOM 237 N ILE A 50 10.850 -0.473 -55.223 1.00 42.17 N ANISOU 237 N ILE A 50 5757 5800 4465 711 179 -1936 N ATOM 238 CA ILE A 50 10.954 -1.831 -54.703 1.00 41.18 C ANISOU 238 CA ILE A 50 5684 5651 4312 741 126 -1948 C ATOM 239 C ILE A 50 11.479 -1.816 -53.277 1.00 38.52 C ANISOU 239 C ILE A 50 5312 5343 3981 777 68 -1976 C ATOM 240 O ILE A 50 10.927 -2.475 -52.397 1.00 37.69 O ANISOU 240 O ILE A 50 5261 5226 3832 780 32 -1956 O ATOM 241 CB ILE A 50 11.882 -2.707 -55.562 1.00 40.41 C ANISOU 241 CB ILE A 50 5593 5527 4234 778 120 -1990 C ATOM 242 CG1 ILE A 50 11.453 -2.664 -57.026 1.00 40.06 C ANISOU 242 CG1 ILE A 50 5580 5455 4184 747 179 -1967 C ATOM 243 CG2 ILE A 50 11.889 -4.138 -55.043 1.00 31.43 C ANISOU 243 CG2 ILE A 50 4518 4361 3065 808 64 -1998 C ATOM 244 CD1 ILE A 50 12.274 -3.549 -57.935 1.00 39.33 C ANISOU 244 CD1 ILE A 50 5501 5334 4108 779 179 -2005 C ATOM 245 N ALA A 51 12.550 -1.059 -53.057 1.00 38.37 N ANISOU 245 N ALA A 51 5204 5361 4016 805 60 -2026 N ATOM 246 CA ALA A 51 13.149 -0.947 -51.732 1.00 38.10 C ANISOU 246 CA ALA A 51 5124 5360 3992 846 1 -2062 C ATOM 247 C ALA A 51 12.147 -0.386 -50.731 1.00 37.90 C ANISOU 247 C ALA A 51 5113 5354 3932 815 -1 -2017 C ATOM 248 O ALA A 51 12.039 -0.878 -49.609 1.00 31.07 O ANISOU 248 O ALA A 51 4278 4492 3036 841 -52 -2016 O ATOM 249 CB ALA A 51 14.394 -0.077 -51.782 1.00 31.81 C ANISOU 249 CB ALA A 51 4217 4604 3267 869 3 -2128 C ATOM 250 N ALA A 52 11.415 0.642 -51.148 1.00 37.71 N ANISOU 250 N ALA A 52 5072 5342 3914 761 54 -1979 N ATOM 251 CA ALA A 52 10.400 1.252 -50.297 1.00 37.65 C ANISOU 251 CA ALA A 52 5074 5353 3878 726 58 -1935 C ATOM 252 C ALA A 52 9.312 0.242 -49.945 1.00 39.04 C ANISOU 252 C ALA A 52 5355 5491 3987 707 45 -1888 C ATOM 253 O ALA A 52 8.869 0.160 -48.795 1.00 38.71 O ANISOU 253 O ALA A 52 5338 5457 3912 706 17 -1873 O ATOM 254 CB ALA A 52 9.798 2.469 -50.981 1.00 36.24 C ANISOU 254 CB ALA A 52 4863 5188 3717 674 119 -1903 C ATOM 255 N TYR A 53 8.899 -0.537 -50.940 1.00 36.87 N ANISOU 255 N TYR A 53 5143 5175 3692 690 68 -1868 N ATOM 256 CA TYR A 53 7.834 -1.515 -50.756 1.00 34.88 C ANISOU 256 CA TYR A 53 4988 4884 3380 661 64 -1829 C ATOM 257 C TYR A 53 8.245 -2.671 -49.849 1.00 34.87 C ANISOU 257 C TYR A 53 5036 4863 3349 702 8 -1851 C ATOM 258 O TYR A 53 7.453 -3.107 -49.021 1.00 33.72 O ANISOU 258 O TYR A 53 4954 4703 3154 679 -4 -1824 O ATOM 259 CB TYR A 53 7.363 -2.059 -52.106 1.00 34.05 C ANISOU 259 CB TYR A 53 4929 4742 3266 635 100 -1811 C ATOM 260 CG TYR A 53 6.066 -1.447 -52.596 1.00 34.15 C ANISOU 260 CG TYR A 53 4960 4753 3261 577 146 -1760 C ATOM 261 CD1 TYR A 53 4.838 -1.951 -52.185 1.00 31.07 C ANISOU 261 CD1 TYR A 53 4641 4343 2823 533 148 -1724 C ATOM 262 CD2 TYR A 53 6.070 -0.369 -53.471 1.00 31.57 C ANISOU 262 CD2 TYR A 53 4583 4445 2967 565 187 -1753 C ATOM 263 CE1 TYR A 53 3.651 -1.398 -52.631 1.00 28.09 C ANISOU 263 CE1 TYR A 53 4276 3967 2432 486 184 -1683 C ATOM 264 CE2 TYR A 53 4.888 0.190 -53.924 1.00 28.01 C ANISOU 264 CE2 TYR A 53 4148 3994 2499 521 221 -1709 C ATOM 265 CZ TYR A 53 3.683 -0.328 -53.501 1.00 27.81 C ANISOU 265 CZ TYR A 53 4186 3952 2429 484 216 -1676 C ATOM 266 OH TYR A 53 2.506 0.227 -53.949 1.00 27.39 O ANISOU 266 OH TYR A 53 4144 3902 2363 446 244 -1638 O ATOM 267 N VAL A 54 9.468 -3.174 -50.001 1.00 30.59 N ANISOU 267 N VAL A 54 4469 4320 2835 762 -28 -1902 N ATOM 268 CA VAL A 54 9.921 -4.277 -49.155 1.00 40.31 C ANISOU 268 CA VAL A 54 5747 5531 4037 813 -90 -1925 C ATOM 269 C VAL A 54 10.215 -3.778 -47.744 1.00 40.22 C ANISOU 269 C VAL A 54 5706 5555 4020 845 -132 -1939 C ATOM 270 O VAL A 54 10.007 -4.503 -46.767 1.00 39.59 O ANISOU 270 O VAL A 54 5692 5458 3893 864 -173 -1934 O ATOM 271 CB VAL A 54 11.175 -4.993 -49.728 1.00 34.44 C ANISOU 271 CB VAL A 54 4984 4775 3328 876 -123 -1980 C ATOM 272 CG1 VAL A 54 10.878 -5.569 -51.103 1.00 35.21 C ANISOU 272 CG1 VAL A 54 5117 4835 3427 847 -82 -1967 C ATOM 273 CG2 VAL A 54 12.379 -4.063 -49.779 1.00 34.80 C ANISOU 273 CG2 VAL A 54 4918 4867 3439 917 -133 -2033 C ATOM 274 N ALA A 55 10.684 -2.536 -47.642 1.00 40.41 N ANISOU 274 N ALA A 55 5633 5629 4093 850 -123 -1959 N ATOM 275 CA ALA A 55 10.907 -1.909 -46.347 1.00 40.85 C ANISOU 275 CA ALA A 55 5648 5725 4147 876 -159 -1974 C ATOM 276 C ALA A 55 9.588 -1.851 -45.595 1.00 40.67 C ANISOU 276 C ALA A 55 5695 5693 4066 823 -141 -1916 C ATOM 277 O ALA A 55 9.456 -2.413 -44.507 1.00 40.20 O ANISOU 277 O ALA A 55 5692 5624 3959 846 -183 -1914 O ATOM 278 CB ALA A 55 11.495 -0.515 -46.511 1.00 31.17 C ANISOU 278 CB ALA A 55 4302 4554 2987 874 -140 -2004 C ATOM 279 N VAL A 56 8.611 -1.183 -46.201 1.00 39.20 N ANISOU 279 N VAL A 56 5507 5507 3881 753 -80 -1872 N ATOM 280 CA VAL A 56 7.268 -1.098 -45.641 1.00 39.36 C ANISOU 280 CA VAL A 56 5589 5515 3850 693 -56 -1818 C ATOM 281 C VAL A 56 6.709 -2.484 -45.322 1.00 39.03 C ANISOU 281 C VAL A 56 5663 5423 3743 681 -70 -1801 C ATOM 282 O VAL A 56 6.084 -2.683 -44.285 1.00 40.00 O ANISOU 282 O VAL A 56 5841 5540 3816 661 -80 -1781 O ATOM 283 CB VAL A 56 6.312 -0.364 -46.603 1.00 38.09 C ANISOU 283 CB VAL A 56 5416 5354 3702 626 8 -1777 C ATOM 284 CG1 VAL A 56 4.863 -0.600 -46.213 1.00 39.19 C ANISOU 284 CG1 VAL A 56 5636 5470 3786 562 32 -1726 C ATOM 285 CG2 VAL A 56 6.628 1.120 -46.620 1.00 38.86 C ANISOU 285 CG2 VAL A 56 5408 5504 3853 626 24 -1786 C ATOM 286 N PHE A 57 6.965 -3.438 -46.210 1.00 30.37 N ANISOU 286 N PHE A 57 4601 4290 2648 691 -70 -1812 N ATOM 287 CA PHE A 57 6.487 -4.808 -46.055 1.00 33.60 C ANISOU 287 CA PHE A 57 5114 4650 3003 678 -81 -1802 C ATOM 288 C PHE A 57 6.988 -5.437 -44.757 1.00 33.73 C ANISOU 288 C PHE A 57 5172 4663 2982 733 -143 -1823 C ATOM 289 O PHE A 57 6.192 -5.814 -43.886 1.00 33.53 O ANISOU 289 O PHE A 57 5218 4624 2899 700 -142 -1798 O ATOM 290 CB PHE A 57 6.923 -5.650 -47.258 1.00 30.92 C ANISOU 290 CB PHE A 57 4786 4278 2682 695 -79 -1821 C ATOM 291 CG PHE A 57 6.406 -7.060 -47.240 1.00 35.88 C ANISOU 291 CG PHE A 57 5514 4857 3261 677 -85 -1814 C ATOM 292 CD1 PHE A 57 5.070 -7.326 -47.487 1.00 35.73 C ANISOU 292 CD1 PHE A 57 5551 4818 3208 593 -38 -1779 C ATOM 293 CD2 PHE A 57 7.262 -8.121 -47.000 1.00 31.97 C ANISOU 293 CD2 PHE A 57 5053 4337 2758 745 -140 -1847 C ATOM 294 CE1 PHE A 57 4.595 -8.625 -47.478 1.00 35.91 C ANISOU 294 CE1 PHE A 57 5656 4800 3190 572 -41 -1780 C ATOM 295 CE2 PHE A 57 6.793 -9.421 -46.991 1.00 32.34 C ANISOU 295 CE2 PHE A 57 5190 4337 2760 730 -147 -1842 C ATOM 296 CZ PHE A 57 5.458 -9.674 -47.230 1.00 32.01 C ANISOU 296 CZ PHE A 57 5196 4278 2686 641 -95 -1810 C ATOM 297 N VAL A 58 8.309 -5.534 -44.622 1.00 36.16 N ANISOU 297 N VAL A 58 5433 4984 3321 820 -198 -1870 N ATOM 298 CA VAL A 58 8.891 -6.180 -43.451 1.00 38.05 C ANISOU 298 CA VAL A 58 5714 5219 3526 891 -268 -1894 C ATOM 299 C VAL A 58 8.576 -5.406 -42.172 1.00 41.07 C ANISOU 299 C VAL A 58 6087 5635 3883 887 -279 -1881 C ATOM 300 O VAL A 58 8.222 -6.009 -41.156 1.00 43.07 O ANISOU 300 O VAL A 58 6422 5870 4072 896 -306 -1868 O ATOM 301 CB VAL A 58 10.429 -6.363 -43.591 1.00 37.93 C ANISOU 301 CB VAL A 58 5638 5216 3556 992 -331 -1955 C ATOM 302 CG1 VAL A 58 10.744 -7.322 -44.726 1.00 37.43 C ANISOU 302 CG1 VAL A 58 5602 5112 3509 1002 -327 -1968 C ATOM 303 CG2 VAL A 58 11.141 -5.034 -43.806 1.00 37.02 C ANISOU 303 CG2 VAL A 58 5394 5160 3512 1007 -324 -1987 C ATOM 304 N VAL A 59 8.672 -4.079 -42.229 1.00 32.11 N ANISOU 304 N VAL A 59 4857 4550 2794 872 -256 -1885 N ATOM 305 CA VAL A 59 8.437 -3.253 -41.050 1.00 37.07 C ANISOU 305 CA VAL A 59 5463 5215 3406 871 -266 -1878 C ATOM 306 C VAL A 59 7.002 -3.412 -40.557 1.00 36.88 C ANISOU 306 C VAL A 59 5528 5169 3317 788 -224 -1822 C ATOM 307 O VAL A 59 6.764 -3.560 -39.359 1.00 37.86 O ANISOU 307 O VAL A 59 5701 5295 3388 798 -250 -1815 O ATOM 308 CB VAL A 59 8.728 -1.763 -41.328 1.00 36.65 C ANISOU 308 CB VAL A 59 5285 5219 3421 862 -242 -1892 C ATOM 309 CG1 VAL A 59 8.291 -0.904 -40.152 1.00 36.06 C ANISOU 309 CG1 VAL A 59 5193 5181 3326 848 -245 -1878 C ATOM 310 CG2 VAL A 59 10.210 -1.556 -41.606 1.00 37.28 C ANISOU 310 CG2 VAL A 59 5269 5330 3564 941 -286 -1958 C ATOM 311 N ALA A 60 6.051 -3.396 -41.486 1.00 31.16 N ANISOU 311 N ALA A 60 4822 4423 2595 707 -161 -1786 N ATOM 312 CA ALA A 60 4.647 -3.580 -41.137 1.00 30.90 C ANISOU 312 CA ALA A 60 4866 4369 2505 619 -117 -1741 C ATOM 313 C ALA A 60 4.416 -4.970 -40.558 1.00 31.55 C ANISOU 313 C ALA A 60 5056 4410 2519 621 -140 -1741 C ATOM 314 O ALA A 60 3.698 -5.125 -39.568 1.00 35.44 O ANISOU 314 O ALA A 60 5609 4902 2955 585 -135 -1722 O ATOM 315 CB ALA A 60 3.756 -3.355 -42.349 1.00 30.24 C ANISOU 315 CB ALA A 60 4777 4270 2442 544 -52 -1711 C ATOM 316 N LEU A 61 5.034 -5.977 -41.172 1.00 31.94 N ANISOU 316 N LEU A 61 5132 4429 2576 665 -167 -1763 N ATOM 317 CA LEU A 61 4.873 -7.354 -40.711 1.00 44.08 C ANISOU 317 CA LEU A 61 6772 5924 4054 678 -193 -1765 C ATOM 318 C LEU A 61 5.371 -7.563 -39.282 1.00 42.98 C ANISOU 318 C LEU A 61 6673 5790 3867 749 -257 -1775 C ATOM 319 O LEU A 61 4.592 -7.917 -38.385 1.00 41.03 O ANISOU 319 O LEU A 61 6501 5534 3555 713 -249 -1753 O ATOM 320 CB LEU A 61 5.594 -8.319 -41.652 1.00 45.62 C ANISOU 320 CB LEU A 61 6978 6083 4271 727 -217 -1790 C ATOM 321 CG LEU A 61 4.798 -8.733 -42.889 1.00 44.48 C ANISOU 321 CG LEU A 61 6847 5913 4139 650 -158 -1776 C ATOM 322 CD1 LEU A 61 5.519 -9.837 -43.638 1.00 46.45 C ANISOU 322 CD1 LEU A 61 7122 6124 4403 704 -189 -1802 C ATOM 323 CD2 LEU A 61 3.398 -9.175 -42.489 1.00 45.19 C ANISOU 323 CD2 LEU A 61 7006 5990 4173 559 -115 -1748 C ATOM 324 N VAL A 62 6.666 -7.339 -39.070 1.00 41.94 N ANISOU 324 N VAL A 62 6491 5677 3768 851 -320 -1812 N ATOM 325 CA VAL A 62 7.256 -7.583 -37.759 1.00 41.85 C ANISOU 325 CA VAL A 62 6520 5670 3713 937 -392 -1828 C ATOM 326 C VAL A 62 6.689 -6.618 -36.720 1.00 41.65 C ANISOU 326 C VAL A 62 6480 5684 3662 902 -376 -1808 C ATOM 327 O VAL A 62 6.473 -6.999 -35.573 1.00 40.29 O ANISOU 327 O VAL A 62 6384 5502 3421 923 -405 -1797 O ATOM 328 CB VAL A 62 8.803 -7.479 -37.788 1.00 35.00 C ANISOU 328 CB VAL A 62 5584 4821 2894 1057 -468 -1883 C ATOM 329 CG1 VAL A 62 9.384 -8.540 -38.709 1.00 35.32 C ANISOU 329 CG1 VAL A 62 5650 4819 2953 1097 -490 -1903 C ATOM 330 CG2 VAL A 62 9.262 -6.090 -38.206 1.00 34.42 C ANISOU 330 CG2 VAL A 62 5372 4808 2900 1052 -449 -1907 C ATOM 331 N GLY A 63 6.420 -5.383 -37.133 1.00 39.76 N ANISOU 331 N GLY A 63 6148 5486 3475 848 -328 -1802 N ATOM 332 CA GLY A 63 5.872 -4.386 -36.235 1.00 40.39 C ANISOU 332 CA GLY A 63 6205 5604 3538 812 -310 -1784 C ATOM 333 C GLY A 63 4.504 -4.782 -35.717 1.00 42.21 C ANISOU 333 C GLY A 63 6530 5813 3697 720 -262 -1741 C ATOM 334 O GLY A 63 4.277 -4.841 -34.504 1.00 43.26 O ANISOU 334 O GLY A 63 6714 5953 3770 730 -283 -1733 O ATOM 335 N ASN A 64 3.592 -5.071 -36.638 1.00 41.24 N ANISOU 335 N ASN A 64 6426 5666 3578 629 -199 -1717 N ATOM 336 CA ASN A 64 2.227 -5.407 -36.254 1.00 32.63 C ANISOU 336 CA ASN A 64 5405 4564 2428 530 -147 -1685 C ATOM 337 C ASN A 64 2.135 -6.748 -35.527 1.00 42.57 C ANISOU 337 C ASN A 64 6771 5790 3612 557 -179 -1687 C ATOM 338 O ASN A 64 1.321 -6.907 -34.606 1.00 43.75 O ANISOU 338 O ASN A 64 6976 5947 3699 514 -162 -1669 O ATOM 339 CB ASN A 64 1.318 -5.401 -37.481 1.00 31.95 C ANISOU 339 CB ASN A 64 5304 4464 2371 435 -77 -1669 C ATOM 340 CG ASN A 64 1.090 -4.004 -38.022 1.00 31.11 C ANISOU 340 CG ASN A 64 5115 4383 2321 401 -39 -1652 C ATOM 341 OD1 ASN A 64 0.252 -3.259 -37.513 1.00 30.78 O ANISOU 341 OD1 ASN A 64 5072 4359 2264 340 -5 -1628 O ATOM 342 ND2 ASN A 64 1.839 -3.639 -39.057 1.00 30.80 N ANISOU 342 ND2 ASN A 64 5007 4346 2348 445 -48 -1665 N ATOM 343 N THR A 65 2.971 -7.707 -35.918 1.00 42.29 N ANISOU 343 N THR A 65 6768 5718 3580 635 -227 -1706 N ATOM 344 CA THR A 65 3.008 -8.966 -35.182 1.00 42.83 C ANISOU 344 CA THR A 65 6952 5745 3576 684 -269 -1702 C ATOM 345 C THR A 65 3.525 -8.730 -33.765 1.00 42.31 C ANISOU 345 C THR A 65 6921 5694 3463 762 -328 -1703 C ATOM 346 O THR A 65 3.041 -9.346 -32.817 1.00 43.35 O ANISOU 346 O THR A 65 7151 5805 3516 764 -337 -1683 O ATOM 347 CB THR A 65 3.876 -10.030 -35.878 1.00 43.68 C ANISOU 347 CB THR A 65 7093 5804 3700 761 -315 -1723 C ATOM 348 OG1 THR A 65 5.128 -9.455 -36.269 1.00 42.09 O ANISOU 348 OG1 THR A 65 6807 5622 3562 842 -360 -1755 O ATOM 349 CG2 THR A 65 3.163 -10.577 -37.106 1.00 43.34 C ANISOU 349 CG2 THR A 65 7048 5737 3681 682 -257 -1719 C ATOM 350 N LEU A 66 4.493 -7.828 -33.618 1.00 40.29 N ANISOU 350 N LEU A 66 6582 5473 3252 829 -369 -1728 N ATOM 351 CA LEU A 66 5.002 -7.477 -32.294 1.00 39.37 C ANISOU 351 CA LEU A 66 6482 5379 3097 907 -428 -1736 C ATOM 352 C LEU A 66 3.910 -6.837 -31.446 1.00 40.49 C ANISOU 352 C LEU A 66 6639 5552 3195 821 -378 -1706 C ATOM 353 O LEU A 66 3.813 -7.102 -30.246 1.00 42.24 O ANISOU 353 O LEU A 66 6938 5769 3343 857 -409 -1694 O ATOM 354 CB LEU A 66 6.206 -6.538 -32.393 1.00 38.68 C ANISOU 354 CB LEU A 66 6279 5336 3081 989 -476 -1779 C ATOM 355 CG LEU A 66 7.554 -7.212 -32.656 1.00 39.70 C ANISOU 355 CG LEU A 66 6405 5445 3235 1114 -558 -1822 C ATOM 356 CD1 LEU A 66 8.691 -6.209 -32.548 1.00 36.70 C ANISOU 356 CD1 LEU A 66 5898 5122 2922 1194 -606 -1874 C ATOM 357 CD2 LEU A 66 7.765 -8.380 -31.707 1.00 41.60 C ANISOU 357 CD2 LEU A 66 6781 5639 3388 1197 -623 -1815 C ATOM 358 N VAL A 67 3.092 -5.997 -32.074 1.00 34.94 N ANISOU 358 N VAL A 67 5865 4877 2535 712 -302 -1692 N ATOM 359 CA VAL A 67 1.935 -5.422 -31.397 1.00 34.68 C ANISOU 359 CA VAL A 67 5842 4871 2464 617 -247 -1665 C ATOM 360 C VAL A 67 1.014 -6.523 -30.873 1.00 35.23 C ANISOU 360 C VAL A 67 6024 4914 2450 576 -227 -1642 C ATOM 361 O VAL A 67 0.719 -6.589 -29.668 1.00 35.81 O ANISOU 361 O VAL A 67 6158 4996 2453 587 -241 -1628 O ATOM 362 CB VAL A 67 1.134 -4.491 -32.330 1.00 33.59 C ANISOU 362 CB VAL A 67 5623 4755 2386 507 -169 -1653 C ATOM 363 CG1 VAL A 67 -0.184 -4.093 -31.682 1.00 33.39 C ANISOU 363 CG1 VAL A 67 5617 4753 2316 400 -109 -1627 C ATOM 364 CG2 VAL A 67 1.955 -3.261 -32.691 1.00 33.22 C ANISOU 364 CG2 VAL A 67 5466 4738 2418 553 -186 -1669 C ATOM 365 N CYS A 68 0.577 -7.392 -31.783 1.00 35.11 N ANISOU 365 N CYS A 68 6034 4865 2442 535 -197 -1640 N ATOM 366 CA CYS A 68 -0.344 -8.472 -31.432 1.00 41.02 C ANISOU 366 CA CYS A 68 6878 5587 3122 499 -175 -1622 C ATOM 367 C CYS A 68 0.195 -9.363 -30.314 1.00 42.01 C ANISOU 367 C CYS A 68 7130 5667 3165 603 -242 -1609 C ATOM 368 O CYS A 68 -0.515 -9.653 -29.348 1.00 43.08 O ANISOU 368 O CYS A 68 7344 5799 3227 586 -230 -1584 O ATOM 369 CB CYS A 68 -0.666 -9.318 -32.664 1.00 35.39 C ANISOU 369 CB CYS A 68 6168 4840 2439 465 -147 -1629 C ATOM 370 SG CYS A 68 -1.813 -8.532 -33.818 1.00 49.42 S ANISOU 370 SG CYS A 68 7827 6666 4283 325 -56 -1638 S ATOM 371 N LEU A 69 1.448 -9.789 -30.449 1.00 44.26 N ANISOU 371 N LEU A 69 7439 5918 3462 716 -315 -1625 N ATOM 372 CA LEU A 69 2.104 -10.598 -29.425 1.00 46.78 C ANISOU 372 CA LEU A 69 7880 6190 3705 831 -389 -1615 C ATOM 373 C LEU A 69 2.096 -9.884 -28.079 1.00 49.05 C ANISOU 373 C LEU A 69 8180 6514 3942 857 -410 -1606 C ATOM 374 O LEU A 69 1.643 -10.438 -27.069 1.00 50.94 O ANISOU 374 O LEU A 69 8537 6726 4092 871 -416 -1575 O ATOM 375 CB LEU A 69 3.544 -10.924 -29.831 1.00 46.37 C ANISOU 375 CB LEU A 69 7816 6113 3690 954 -470 -1647 C ATOM 376 CG LEU A 69 3.742 -11.904 -30.987 1.00 38.69 C ANISOU 376 CG LEU A 69 6863 5088 2749 959 -468 -1656 C ATOM 377 CD1 LEU A 69 5.222 -12.171 -31.215 1.00 39.15 C ANISOU 377 CD1 LEU A 69 6906 5129 2840 1090 -555 -1692 C ATOM 378 CD2 LEU A 69 2.994 -13.198 -30.719 1.00 45.47 C ANISOU 378 CD2 LEU A 69 7869 5877 3531 942 -451 -1621 C ATOM 379 N ALA A 70 2.591 -8.648 -28.088 1.00 47.13 N ANISOU 379 N ALA A 70 7819 6331 3758 863 -420 -1631 N ATOM 380 CA ALA A 70 2.696 -7.832 -26.883 1.00 44.94 C ANISOU 380 CA ALA A 70 7534 6096 3447 892 -444 -1631 C ATOM 381 C ALA A 70 1.373 -7.739 -26.136 1.00 44.44 C ANISOU 381 C ALA A 70 7521 6048 3318 796 -381 -1595 C ATOM 382 O ALA A 70 1.332 -7.903 -24.916 1.00 45.17 O ANISOU 382 O ALA A 70 7700 6135 3330 842 -410 -1577 O ATOM 383 CB ALA A 70 3.191 -6.442 -27.231 1.00 37.77 C ANISOU 383 CB ALA A 70 6476 5248 2625 886 -443 -1662 C ATOM 384 N VAL A 71 0.291 -7.480 -26.862 1.00 44.61 N ANISOU 384 N VAL A 71 7488 6091 3373 666 -296 -1586 N ATOM 385 CA VAL A 71 -1.006 -7.345 -26.207 1.00 37.74 C ANISOU 385 CA VAL A 71 6645 5245 2449 573 -235 -1561 C ATOM 386 C VAL A 71 -1.562 -8.688 -25.735 1.00 46.13 C ANISOU 386 C VAL A 71 7856 6248 3424 589 -232 -1528 C ATOM 387 O VAL A 71 -1.960 -8.826 -24.579 1.00 46.97 O ANISOU 387 O VAL A 71 8048 6350 3449 602 -234 -1501 O ATOM 388 CB VAL A 71 -2.038 -6.681 -27.129 1.00 56.19 C ANISOU 388 CB VAL A 71 8872 7629 4849 438 -150 -1568 C ATOM 389 CG1 VAL A 71 -3.387 -6.586 -26.429 1.00 36.70 C ANISOU 389 CG1 VAL A 71 6420 5197 2329 355 -94 -1550 C ATOM 390 CG2 VAL A 71 -1.558 -5.305 -27.553 1.00 54.00 C ANISOU 390 CG2 VAL A 71 8473 7392 4652 419 -145 -1588 C ATOM 391 N TRP A 72 -1.586 -9.672 -26.630 1.00 45.80 N ANISOU 391 N TRP A 72 7851 6152 3397 591 -226 -1528 N ATOM 392 CA TRP A 72 -2.205 -10.964 -26.344 1.00 47.35 C ANISOU 392 CA TRP A 72 8193 6278 3521 595 -212 -1494 C ATOM 393 C TRP A 72 -1.546 -11.673 -25.171 1.00 50.57 C ANISOU 393 C TRP A 72 8757 6624 3833 711 -277 -1466 C ATOM 394 O TRP A 72 -2.244 -12.265 -24.327 1.00 50.71 O ANISOU 394 O TRP A 72 8902 6600 3764 704 -254 -1425 O ATOM 395 CB TRP A 72 -2.144 -11.867 -27.572 1.00 44.56 C ANISOU 395 CB TRP A 72 7848 5873 3209 589 -204 -1504 C ATOM 396 CG TRP A 72 -3.166 -11.533 -28.592 1.00 42.06 C ANISOU 396 CG TRP A 72 7425 5599 2958 474 -131 -1521 C ATOM 397 CD1 TRP A 72 -4.336 -10.862 -28.385 1.00 41.37 C ANISOU 397 CD1 TRP A 72 7275 5572 2874 383 -70 -1518 C ATOM 398 CD2 TRP A 72 -3.118 -11.840 -29.988 1.00 40.46 C ANISOU 398 CD2 TRP A 72 7159 5386 2826 446 -115 -1545 C ATOM 399 NE1 TRP A 72 -5.024 -10.738 -29.566 1.00 40.21 N ANISOU 399 NE1 TRP A 72 7029 5454 2796 308 -23 -1542 N ATOM 400 CE2 TRP A 72 -4.297 -11.329 -30.566 1.00 39.21 C ANISOU 400 CE2 TRP A 72 6903 5284 2710 342 -47 -1558 C ATOM 401 CE3 TRP A 72 -2.196 -12.498 -30.807 1.00 37.75 C ANISOU 401 CE3 TRP A 72 6834 4994 2516 506 -154 -1560 C ATOM 402 CZ2 TRP A 72 -4.578 -11.457 -31.924 1.00 38.01 C ANISOU 402 CZ2 TRP A 72 6673 5139 2628 296 -19 -1585 C ATOM 403 CZ3 TRP A 72 -2.476 -12.624 -32.154 1.00 37.15 C ANISOU 403 CZ3 TRP A 72 6682 4924 2509 452 -120 -1584 C ATOM 404 CH2 TRP A 72 -3.657 -12.106 -32.700 1.00 36.34 C ANISOU 404 CH2 TRP A 72 6486 4877 2445 348 -53 -1596 C ATOM 405 N ARG A 73 -0.211 -11.627 -25.121 1.00 55.14 N ANISOU 405 N ARG A 73 9330 7193 4426 822 -359 -1487 N ATOM 406 CA ARG A 73 0.519 -12.427 -24.136 1.00 60.57 C ANISOU 406 CA ARG A 73 10170 7817 5026 951 -434 -1466 C ATOM 407 C ARG A 73 0.374 -11.881 -22.699 1.00 62.46 C ANISOU 407 C ARG A 73 10455 8085 5191 978 -448 -1446 C ATOM 408 O ARG A 73 0.025 -12.635 -21.780 1.00 58.30 O ANISOU 408 O ARG A 73 10087 7499 4563 1010 -449 -1403 O ATOM 409 CB ARG A 73 1.992 -12.535 -24.521 1.00 64.02 C ANISOU 409 CB ARG A 73 10576 8242 5507 1074 -524 -1504 C ATOM 410 CG ARG A 73 2.308 -13.458 -25.707 1.00 66.34 C ANISOU 410 CG ARG A 73 10882 8481 5844 1084 -529 -1515 C ATOM 411 CD ARG A 73 3.799 -13.486 -25.983 1.00 67.42 C ANISOU 411 CD ARG A 73 10979 8614 6023 1213 -623 -1557 C ATOM 412 NE ARG A 73 4.585 -13.560 -24.745 1.00 72.54 N ANISOU 412 NE ARG A 73 11708 9251 6603 1347 -710 -1556 N ATOM 413 CZ ARG A 73 5.201 -14.652 -24.297 1.00 76.38 C ANISOU 413 CZ ARG A 73 12337 9660 7022 1467 -780 -1544 C ATOM 414 NH1 ARG A 73 5.121 -15.791 -24.971 1.00 77.70 N ANISOU 414 NH1 ARG A 73 12597 9748 7178 1476 -776 -1530 N ATOM 415 NH2 ARG A 73 5.896 -14.605 -23.169 1.00 78.20 N ANISOU 415 NH2 ARG A 73 12633 9888 7191 1594 -862 -1548 N ATOM 416 N ASN A 74 0.625 -10.587 -22.505 1.00 67.44 N ANISOU 416 N ASN A 74 10956 8800 5870 964 -455 -1476 N ATOM 417 CA ASN A 74 0.597 -10.006 -21.167 1.00 71.79 C ANISOU 417 CA ASN A 74 11538 9382 6356 997 -476 -1465 C ATOM 418 C ASN A 74 -0.805 -9.627 -20.709 1.00 69.22 C ANISOU 418 C ASN A 74 11215 9091 5996 874 -387 -1435 C ATOM 419 O ASN A 74 -1.678 -9.316 -21.526 1.00 63.75 O ANISOU 419 O ASN A 74 10433 8430 5360 754 -313 -1441 O ATOM 420 CB ASN A 74 1.507 -8.780 -21.103 1.00 77.59 C ANISOU 420 CB ASN A 74 12134 10189 7157 1043 -525 -1513 C ATOM 421 CG ASN A 74 2.955 -9.117 -21.386 1.00 82.64 C ANISOU 421 CG ASN A 74 12767 10803 7828 1184 -622 -1549 C ATOM 422 OD1 ASN A 74 3.355 -9.236 -22.542 1.00 83.69 O ANISOU 422 OD1 ASN A 74 12829 10930 8041 1176 -621 -1574 O ATOM 423 ND2 ASN A 74 3.749 -9.278 -20.332 1.00 85.75 N ANISOU 423 ND2 ASN A 74 13236 11185 8161 1318 -708 -1555 N ATOM 424 N HIS A 75 -1.017 -9.650 -19.396 1.00 69.61 N ANISOU 424 N HIS A 75 11365 9133 5950 910 -399 -1405 N ATOM 425 CA HIS A 75 -2.337 -9.367 -18.830 1.00 68.69 C ANISOU 425 CA HIS A 75 11265 9043 5791 805 -318 -1375 C ATOM 426 C HIS A 75 -2.580 -7.865 -18.659 1.00 61.98 C ANISOU 426 C HIS A 75 10259 8299 4994 736 -294 -1406 C ATOM 427 O HIS A 75 -3.682 -7.385 -18.857 1.00 61.00 O ANISOU 427 O HIS A 75 10065 8221 4893 619 -217 -1404 O ATOM 428 CB HIS A 75 -2.515 -10.087 -17.486 1.00 72.11 C ANISOU 428 CB HIS A 75 11889 9416 6093 870 -332 -1324 C ATOM 429 CG HIS A 75 -3.823 -9.807 -16.808 1.00 73.97 C ANISOU 429 CG HIS A 75 12150 9676 6281 773 -251 -1292 C ATOM 430 ND1 HIS A 75 -5.043 -10.101 -17.381 1.00 74.82 N ANISOU 430 ND1 HIS A 75 12249 9772 6407 659 -162 -1276 N ATOM 431 CD2 HIS A 75 -4.100 -9.258 -15.602 1.00 75.64 C ANISOU 431 CD2 HIS A 75 12393 9921 6426 779 -247 -1277 C ATOM 432 CE1 HIS A 75 -6.012 -9.744 -16.559 1.00 75.88 C ANISOU 432 CE1 HIS A 75 12407 9931 6493 600 -106 -1252 C ATOM 433 NE2 HIS A 75 -5.467 -9.229 -15.470 1.00 76.37 N ANISOU 433 NE2 HIS A 75 12494 10022 6500 668 -154 -1250 N ATOM 434 N HIS A 76 -1.550 -7.108 -18.302 1.00 57.49 N ANISOU 434 N HIS A 76 9630 7765 4448 814 -361 -1438 N ATOM 435 CA HIS A 76 -1.703 -5.682 -18.052 1.00 55.24 C ANISOU 435 CA HIS A 76 9213 7568 4209 757 -341 -1464 C ATOM 436 C HIS A 76 -1.973 -4.961 -19.370 1.00 51.14 C ANISOU 436 C HIS A 76 8535 7090 3806 653 -289 -1494 C ATOM 437 O HIS A 76 -2.277 -3.769 -19.384 1.00 50.29 O ANISOU 437 O HIS A 76 8315 7046 3747 582 -255 -1511 O ATOM 438 CB HIS A 76 -0.456 -5.122 -17.349 1.00 54.12 C ANISOU 438 CB HIS A 76 9052 7444 4065 883 -433 -1494 C ATOM 439 CG HIS A 76 0.790 -5.245 -18.152 1.00 53.34 C ANISOU 439 CG HIS A 76 8900 7327 4040 976 -501 -1532 C ATOM 440 ND1 HIS A 76 1.569 -6.386 -18.159 1.00 52.96 N ANISOU 440 ND1 HIS A 76 8959 7210 3953 1094 -570 -1527 N ATOM 441 CD2 HIS A 76 1.411 -4.362 -18.972 1.00 51.05 C ANISOU 441 CD2 HIS A 76 8462 7076 3860 973 -512 -1575 C ATOM 442 CE1 HIS A 76 2.594 -6.209 -18.973 1.00 52.27 C ANISOU 442 CE1 HIS A 76 8781 7129 3952 1156 -619 -1571 C ATOM 443 NE2 HIS A 76 2.522 -4.989 -19.479 1.00 51.10 N ANISOU 443 NE2 HIS A 76 8478 7045 3895 1085 -583 -1600 N ATOM 444 N MET A 77 -1.665 -5.643 -20.467 1.00 51.28 N ANISOU 444 N MET A 77 8548 7065 3870 663 -294 -1500 N ATOM 445 CA MET A 77 -1.861 -5.091 -21.808 1.00 39.08 C ANISOU 445 CA MET A 77 6871 5548 2431 577 -247 -1525 C ATOM 446 C MET A 77 -3.281 -5.304 -22.343 1.00 40.10 C ANISOU 446 C MET A 77 6978 5692 2565 448 -157 -1511 C ATOM 447 O MET A 77 -3.738 -4.572 -23.224 1.00 37.81 O ANISOU 447 O MET A 77 6569 5444 2352 356 -106 -1530 O ATOM 448 CB MET A 77 -0.849 -5.699 -22.778 1.00 47.43 C ANISOU 448 CB MET A 77 7924 6558 3539 652 -295 -1543 C ATOM 449 CG MET A 77 0.587 -5.386 -22.412 1.00 48.31 C ANISOU 449 CG MET A 77 8019 6669 3667 787 -387 -1571 C ATOM 450 SD MET A 77 0.946 -3.629 -22.583 1.00 50.17 S ANISOU 450 SD MET A 77 8087 6978 3998 762 -380 -1606 S ATOM 451 CE MET A 77 0.437 -3.349 -24.277 1.00 37.15 C ANISOU 451 CE MET A 77 6338 5329 2449 646 -303 -1609 C ATOM 452 N ARG A 78 -3.981 -6.302 -21.810 1.00 44.84 N ANISOU 452 N ARG A 78 7698 6254 3083 451 -140 -1478 N ATOM 453 CA ARG A 78 -5.317 -6.641 -22.302 1.00 45.24 C ANISOU 453 CA ARG A 78 7734 6313 3140 356 -66 -1468 C ATOM 454 C ARG A 78 -6.334 -5.552 -21.976 1.00 46.07 C ANISOU 454 C ARG A 78 7737 6508 3262 265 -11 -1478 C ATOM 455 O ARG A 78 -7.252 -5.754 -21.180 1.00 46.79 O ANISOU 455 O ARG A 78 7888 6601 3289 246 20 -1451 O ATOM 456 CB ARG A 78 -5.777 -7.985 -21.729 1.00 49.46 C ANISOU 456 CB ARG A 78 8447 6764 3582 391 -61 -1422 C ATOM 457 CG ARG A 78 -4.878 -9.144 -22.124 1.00 51.76 C ANISOU 457 CG ARG A 78 8844 6964 3857 478 -111 -1412 C ATOM 458 CD ARG A 78 -5.483 -10.491 -21.773 1.00 54.34 C ANISOU 458 CD ARG A 78 9350 7194 4103 489 -87 -1364 C ATOM 459 NE ARG A 78 -4.518 -11.569 -21.968 1.00 57.00 N ANISOU 459 NE ARG A 78 9801 7443 4414 585 -145 -1355 N ATOM 460 CZ ARG A 78 -3.919 -12.224 -20.979 1.00 59.89 C ANISOU 460 CZ ARG A 78 10323 7743 4687 687 -196 -1322 C ATOM 461 NH1 ARG A 78 -4.201 -11.926 -19.719 1.00 62.17 N ANISOU 461 NH1 ARG A 78 10680 8044 4899 700 -192 -1295 N ATOM 462 NH2 ARG A 78 -3.048 -13.187 -21.251 1.00 60.05 N ANISOU 462 NH2 ARG A 78 10436 7687 4691 779 -252 -1318 N ATOM 463 N THR A 79 -6.155 -4.396 -22.604 1.00 45.23 N ANISOU 463 N THR A 79 7483 6463 3239 210 3 -1512 N ATOM 464 CA THR A 79 -7.064 -3.271 -22.450 1.00 44.82 C ANISOU 464 CA THR A 79 7316 6499 3215 122 54 -1529 C ATOM 465 C THR A 79 -7.930 -3.160 -23.699 1.00 42.94 C ANISOU 465 C THR A 79 6963 6301 3052 56 101 -1553 C ATOM 466 O THR A 79 -7.514 -3.571 -24.782 1.00 42.30 O ANISOU 466 O THR A 79 6868 6182 3020 58 96 -1563 O ATOM 467 CB THR A 79 -6.298 -1.950 -22.220 1.00 45.08 C ANISOU 467 CB THR A 79 7288 6554 3289 103 42 -1542 C ATOM 468 OG1 THR A 79 -5.222 -2.170 -21.300 1.00 46.47 O ANISOU 468 OG1 THR A 79 7558 6687 3410 213 -29 -1529 O ATOM 469 CG2 THR A 79 -7.222 -0.871 -21.667 1.00 44.93 C ANISOU 469 CG2 THR A 79 7188 6606 3275 20 90 -1545 C ATOM 470 N VAL A 80 -9.135 -2.618 -23.540 1.00 42.49 N ANISOU 470 N VAL A 80 6820 6303 3020 30 131 -1545 N ATOM 471 CA VAL A 80 -10.048 -2.404 -24.659 1.00 34.56 C ANISOU 471 CA VAL A 80 5698 5319 2113 30 145 -1543 C ATOM 472 C VAL A 80 -9.370 -1.614 -25.777 1.00 37.79 C ANISOU 472 C VAL A 80 5983 5731 2644 -30 155 -1550 C ATOM 473 O VAL A 80 -9.469 -1.970 -26.959 1.00 37.19 O ANISOU 473 O VAL A 80 5866 5641 2626 -21 155 -1557 O ATOM 474 CB VAL A 80 -11.319 -1.664 -24.201 1.00 35.76 C ANISOU 474 CB VAL A 80 5800 5512 2275 72 148 -1522 C ATOM 475 CG1 VAL A 80 -12.173 -1.273 -25.396 1.00 34.86 C ANISOU 475 CG1 VAL A 80 5626 5371 2248 136 133 -1502 C ATOM 476 CG2 VAL A 80 -12.110 -2.528 -23.230 1.00 35.28 C ANISOU 476 CG2 VAL A 80 5907 5410 2087 74 174 -1506 C ATOM 477 N THR A 81 -8.669 -0.552 -25.391 1.00 38.20 N ANISOU 477 N THR A 81 6042 5755 2719 -112 178 -1532 N ATOM 478 CA THR A 81 -7.905 0.252 -26.335 1.00 36.61 C ANISOU 478 CA THR A 81 5899 5424 2588 -179 205 -1489 C ATOM 479 C THR A 81 -6.905 -0.619 -27.089 1.00 36.99 C ANISOU 479 C THR A 81 5991 5439 2625 -108 167 -1516 C ATOM 480 O THR A 81 -6.777 -0.518 -28.308 1.00 38.04 O ANISOU 480 O THR A 81 6118 5514 2823 -125 183 -1499 O ATOM 481 CB THR A 81 -7.156 1.400 -25.627 1.00 36.33 C ANISOU 481 CB THR A 81 5954 5317 2533 -141 181 -1459 C ATOM 482 OG1 THR A 81 -8.097 2.244 -24.951 1.00 36.15 O ANISOU 482 OG1 THR A 81 5956 5266 2512 -201 217 -1412 O ATOM 483 CG2 THR A 81 -6.371 2.230 -26.632 1.00 31.69 C ANISOU 483 CG2 THR A 81 5380 4654 2005 -67 154 -1443 C ATOM 484 N ASN A 82 -6.217 -1.492 -26.360 1.00 33.63 N ANISOU 484 N ASN A 82 5637 5031 2109 -23 116 -1552 N ATOM 485 CA ASN A 82 -5.221 -2.368 -26.965 1.00 33.90 C ANISOU 485 CA ASN A 82 5728 5023 2129 50 74 -1576 C ATOM 486 C ASN A 82 -5.835 -3.528 -27.745 1.00 34.95 C ANISOU 486 C ASN A 82 5859 5158 2261 40 90 -1589 C ATOM 487 O ASN A 82 -5.213 -4.052 -28.666 1.00 33.87 O ANISOU 487 O ASN A 82 5735 4973 2160 73 72 -1593 O ATOM 488 CB ASN A 82 -4.273 -2.911 -25.898 1.00 36.48 C ANISOU 488 CB ASN A 82 6145 5324 2392 170 -1 -1568 C ATOM 489 CG ASN A 82 -3.396 -1.832 -25.299 1.00 36.50 C ANISOU 489 CG ASN A 82 6127 5329 2413 224 -40 -1568 C ATOM 490 OD1 ASN A 82 -3.200 -0.774 -25.897 1.00 34.06 O ANISOU 490 OD1 ASN A 82 5747 5016 2177 203 -25 -1567 O ATOM 491 ND2 ASN A 82 -2.859 -2.094 -24.114 1.00 37.88 N ANISOU 491 ND2 ASN A 82 6368 5504 2521 313 -98 -1566 N ATOM 492 N TYR A 83 -7.044 -3.939 -27.373 1.00 34.22 N ANISOU 492 N TYR A 83 5751 5110 2141 27 110 -1585 N ATOM 493 CA TYR A 83 -7.763 -4.939 -28.155 1.00 45.11 C ANISOU 493 CA TYR A 83 7135 6478 3525 40 118 -1594 C ATOM 494 C TYR A 83 -8.081 -4.358 -29.527 1.00 42.93 C ANISOU 494 C TYR A 83 6720 6219 3373 -3 141 -1591 C ATOM 495 O TYR A 83 -7.865 -4.999 -30.565 1.00 42.24 O ANISOU 495 O TYR A 83 6639 6096 3315 3 140 -1603 O ATOM 496 CB TYR A 83 -9.046 -5.383 -27.446 1.00 46.96 C ANISOU 496 CB TYR A 83 7420 6726 3697 60 130 -1579 C ATOM 497 CG TYR A 83 -8.861 -6.557 -26.508 1.00 48.97 C ANISOU 497 CG TYR A 83 7861 6887 3858 102 115 -1536 C ATOM 498 CD1 TYR A 83 -8.733 -7.849 -27.001 1.00 49.70 C ANISOU 498 CD1 TYR A 83 8060 6887 3935 127 110 -1520 C ATOM 499 CD2 TYR A 83 -8.827 -6.375 -25.132 1.00 50.71 C ANISOU 499 CD2 TYR A 83 8155 7108 4004 120 108 -1510 C ATOM 500 CE1 TYR A 83 -8.567 -8.926 -26.151 1.00 51.17 C ANISOU 500 CE1 TYR A 83 8426 6983 4033 168 99 -1478 C ATOM 501 CE2 TYR A 83 -8.662 -7.446 -24.273 1.00 52.63 C ANISOU 501 CE2 TYR A 83 8578 7262 4156 165 95 -1467 C ATOM 502 CZ TYR A 83 -8.533 -8.719 -24.789 1.00 53.18 C ANISOU 502 CZ TYR A 83 8756 7238 4212 190 92 -1450 C ATOM 503 OH TYR A 83 -8.369 -9.789 -23.939 1.00 56.18 O ANISOU 503 OH TYR A 83 9323 7523 4498 237 81 -1405 O ATOM 504 N PHE A 84 -8.587 -3.128 -29.521 1.00 40.94 N ANISOU 504 N PHE A 84 6346 6020 3190 -47 163 -1576 N ATOM 505 CA PHE A 84 -8.845 -2.412 -30.762 1.00 31.65 C ANISOU 505 CA PHE A 84 5047 4854 2123 -100 191 -1568 C ATOM 506 C PHE A 84 -7.563 -2.235 -31.569 1.00 31.34 C ANISOU 506 C PHE A 84 5147 4660 2100 -169 223 -1527 C ATOM 507 O PHE A 84 -7.539 -2.511 -32.766 1.00 30.98 O ANISOU 507 O PHE A 84 5097 4573 2100 -183 237 -1521 O ATOM 508 CB PHE A 84 -9.482 -1.055 -30.473 1.00 35.15 C ANISOU 508 CB PHE A 84 5367 5363 2624 -135 208 -1553 C ATOM 509 CG PHE A 84 -10.953 -1.129 -30.187 1.00 36.10 C ANISOU 509 CG PHE A 84 5583 5444 2688 280 41 -1502 C ATOM 510 CD1 PHE A 84 -11.786 -1.898 -30.983 1.00 35.99 C ANISOU 510 CD1 PHE A 84 5665 5353 2659 262 62 -1488 C ATOM 511 CD2 PHE A 84 -11.502 -0.439 -29.119 1.00 36.14 C ANISOU 511 CD2 PHE A 84 5671 5414 2647 317 37 -1459 C ATOM 512 CE1 PHE A 84 -13.140 -1.971 -30.726 1.00 36.23 C ANISOU 512 CE1 PHE A 84 5798 5327 2642 211 106 -1464 C ATOM 513 CE2 PHE A 84 -12.857 -0.510 -28.855 1.00 36.53 C ANISOU 513 CE2 PHE A 84 5826 5407 2649 257 86 -1433 C ATOM 514 CZ PHE A 84 -13.676 -1.278 -29.660 1.00 36.70 C ANISOU 514 CZ PHE A 84 5889 5392 2665 195 124 -1443 C ATOM 515 N ILE A 85 -6.501 -1.786 -30.905 1.00 31.54 N ANISOU 515 N ILE A 85 5263 4635 2084 -119 192 -1516 N ATOM 516 CA ILE A 85 -5.199 -1.619 -31.548 1.00 31.36 C ANISOU 516 CA ILE A 85 5282 4558 2076 -40 154 -1525 C ATOM 517 C ILE A 85 -4.745 -2.921 -32.208 1.00 31.75 C ANISOU 517 C ILE A 85 5341 4609 2112 -3 133 -1566 C ATOM 518 O ILE A 85 -4.173 -2.911 -33.303 1.00 36.05 O ANISOU 518 O ILE A 85 5881 5115 2702 23 128 -1569 O ATOM 519 CB ILE A 85 -4.138 -1.139 -30.534 1.00 31.75 C ANISOU 519 CB ILE A 85 5359 4626 2079 42 102 -1552 C ATOM 520 CG1 ILE A 85 -4.337 0.348 -30.234 1.00 31.18 C ANISOU 520 CG1 ILE A 85 5264 4544 2039 39 111 -1519 C ATOM 521 CG2 ILE A 85 -2.730 -1.378 -31.054 1.00 31.88 C ANISOU 521 CG2 ILE A 85 5353 4625 2137 160 39 -1571 C ATOM 522 CD1 ILE A 85 -3.292 0.933 -29.312 1.00 31.53 C ANISOU 522 CD1 ILE A 85 5275 4623 2082 139 49 -1537 C ATOM 523 N VAL A 86 -5.022 -4.041 -31.548 1.00 32.52 N ANISOU 523 N VAL A 86 5470 4744 2143 17 116 -1596 N ATOM 524 CA VAL A 86 -4.750 -5.351 -32.124 1.00 48.52 C ANISOU 524 CA VAL A 86 7541 6745 4151 64 92 -1621 C ATOM 525 C VAL A 86 -5.564 -5.553 -33.395 1.00 45.41 C ANISOU 525 C VAL A 86 7074 6356 3825 7 133 -1620 C ATOM 526 O VAL A 86 -5.027 -5.991 -34.409 1.00 45.64 O ANISOU 526 O VAL A 86 7114 6344 3883 25 127 -1631 O ATOM 527 CB VAL A 86 -5.055 -6.490 -31.129 1.00 51.28 C ANISOU 527 CB VAL A 86 7981 7085 4418 119 61 -1615 C ATOM 528 CG1 VAL A 86 -5.318 -7.799 -31.865 1.00 34.21 C ANISOU 528 CG1 VAL A 86 5867 4878 2253 140 58 -1621 C ATOM 529 CG2 VAL A 86 -3.910 -6.651 -30.154 1.00 34.65 C ANISOU 529 CG2 VAL A 86 5962 4937 2265 216 -3 -1598 C ATOM 530 N ASN A 87 -6.853 -5.227 -33.341 1.00 45.47 N ANISOU 530 N ASN A 87 6994 6422 3862 -39 162 -1610 N ATOM 531 CA ASN A 87 -7.710 -5.333 -34.523 1.00 31.60 C ANISOU 531 CA ASN A 87 5138 4693 2177 -58 179 -1616 C ATOM 532 C ASN A 87 -7.145 -4.547 -35.709 1.00 30.84 C ANISOU 532 C ASN A 87 5050 4518 2152 -135 224 -1576 C ATOM 533 O ASN A 87 -7.092 -5.040 -36.844 1.00 31.30 O ANISOU 533 O ASN A 87 5100 4549 2243 -136 230 -1584 O ATOM 534 CB ASN A 87 -9.124 -4.845 -34.203 1.00 31.39 C ANISOU 534 CB ASN A 87 5003 4756 2168 5 152 -1618 C ATOM 535 CG ASN A 87 -10.102 -5.124 -35.324 1.00 31.06 C ANISOU 535 CG ASN A 87 4934 4705 2163 116 106 -1614 C ATOM 536 OD1 ASN A 87 -10.014 -6.151 -35.995 1.00 31.32 O ANISOU 536 OD1 ASN A 87 5020 4694 2187 96 117 -1633 O ATOM 537 ND2 ASN A 87 -11.043 -4.211 -35.532 1.00 33.78 N ANISOU 537 ND2 ASN A 87 5316 5000 2519 253 50 -1552 N ATOM 538 N LEU A 88 -6.719 -3.321 -35.423 1.00 36.71 N ANISOU 538 N LEU A 88 5873 5179 2896 -157 241 -1514 N ATOM 539 CA LEU A 88 -6.098 -2.447 -36.409 1.00 29.77 C ANISOU 539 CA LEU A 88 5059 4199 2051 -101 230 -1465 C ATOM 540 C LEU A 88 -4.840 -3.082 -36.995 1.00 42.55 C ANISOU 540 C LEU A 88 6660 5832 3673 -32 194 -1519 C ATOM 541 O LEU A 88 -4.621 -3.064 -38.213 1.00 42.84 O ANISOU 541 O LEU A 88 6691 5837 3750 -10 196 -1513 O ATOM 542 CB LEU A 88 -5.764 -1.098 -35.770 1.00 29.44 C ANISOU 542 CB LEU A 88 5026 4153 2008 -41 204 -1441 C ATOM 543 CG LEU A 88 -5.070 -0.052 -36.638 1.00 28.81 C ANISOU 543 CG LEU A 88 4891 4080 1977 42 179 -1449 C ATOM 544 CD1 LEU A 88 -5.922 0.277 -37.843 1.00 28.22 C ANISOU 544 CD1 LEU A 88 4807 3972 1941 51 192 -1411 C ATOM 545 CD2 LEU A 88 -4.784 1.199 -35.826 1.00 28.96 C ANISOU 545 CD2 LEU A 88 4865 4141 1998 83 161 -1456 C ATOM 546 N SER A 89 -4.021 -3.652 -36.117 1.00 30.66 N ANISOU 546 N SER A 89 5169 4362 2118 18 154 -1568 N ATOM 547 CA SER A 89 -2.782 -4.292 -36.534 1.00 30.98 C ANISOU 547 CA SER A 89 5221 4390 2163 107 106 -1604 C ATOM 548 C SER A 89 -3.046 -5.503 -37.418 1.00 31.17 C ANISOU 548 C SER A 89 5259 4399 2187 87 118 -1627 C ATOM 549 O SER A 89 -2.307 -5.747 -38.363 1.00 31.08 O ANISOU 549 O SER A 89 5237 4356 2216 138 99 -1632 O ATOM 550 CB SER A 89 -1.952 -4.701 -35.317 1.00 36.02 C ANISOU 550 CB SER A 89 5890 5040 2757 193 42 -1618 C ATOM 551 OG SER A 89 -1.399 -3.565 -34.677 1.00 36.64 O ANISOU 551 OG SER A 89 5933 5136 2851 238 17 -1609 O ATOM 552 N LEU A 90 -4.096 -6.258 -37.111 1.00 39.90 N ANISOU 552 N LEU A 90 6362 5532 3264 35 139 -1635 N ATOM 553 CA LEU A 90 -4.465 -7.419 -37.915 1.00 38.81 C ANISOU 553 CA LEU A 90 6225 5387 3133 33 142 -1660 C ATOM 554 C LEU A 90 -4.956 -6.982 -39.288 1.00 37.96 C ANISOU 554 C LEU A 90 6058 5264 3102 -23 185 -1634 C ATOM 555 O LEU A 90 -4.651 -7.623 -40.296 1.00 31.00 O ANISOU 555 O LEU A 90 5185 4353 2241 -5 181 -1651 O ATOM 556 CB LEU A 90 -5.537 -8.255 -37.214 1.00 39.62 C ANISOU 556 CB LEU A 90 6336 5530 3189 31 138 -1678 C ATOM 557 CG LEU A 90 -5.101 -9.058 -35.987 1.00 41.59 C ANISOU 557 CG LEU A 90 6701 5750 3353 100 94 -1677 C ATOM 558 CD1 LEU A 90 -6.293 -9.774 -35.374 1.00 41.74 C ANISOU 558 CD1 LEU A 90 6763 5775 3321 100 99 -1675 C ATOM 559 CD2 LEU A 90 -4.008 -10.051 -36.353 1.00 42.13 C ANISOU 559 CD2 LEU A 90 6850 5739 3418 177 49 -1674 C ATOM 560 N ALA A 91 -5.722 -5.894 -39.320 1.00 36.43 N ANISOU 560 N ALA A 91 5829 5072 2941 -89 225 -1587 N ATOM 561 CA ALA A 91 -6.140 -5.306 -40.588 1.00 36.44 C ANISOU 561 CA ALA A 91 5852 5004 2990 -123 260 -1533 C ATOM 562 C ALA A 91 -4.916 -4.980 -41.442 1.00 36.80 C ANISOU 562 C ALA A 91 5917 5012 3055 -37 229 -1536 C ATOM 563 O ALA A 91 -4.812 -5.392 -42.610 1.00 37.32 O ANISOU 563 O ALA A 91 5981 5053 3146 -26 234 -1542 O ATOM 564 CB ALA A 91 -6.974 -4.056 -40.348 1.00 34.58 C ANISOU 564 CB ALA A 91 5694 4694 2751 -133 274 -1443 C ATOM 565 N ASP A 92 -3.979 -4.256 -40.837 1.00 39.46 N ANISOU 565 N ASP A 92 6247 5363 3382 26 198 -1546 N ATOM 566 CA ASP A 92 -2.748 -3.878 -41.521 1.00 41.85 C ANISOU 566 CA ASP A 92 6519 5667 3716 110 169 -1572 C ATOM 567 C ASP A 92 -1.928 -5.093 -41.960 1.00 40.80 C ANISOU 567 C ASP A 92 6391 5526 3587 151 141 -1611 C ATOM 568 O ASP A 92 -1.268 -5.056 -42.995 1.00 38.91 O ANISOU 568 O ASP A 92 6117 5275 3393 199 129 -1616 O ATOM 569 CB ASP A 92 -1.905 -2.970 -40.626 1.00 47.77 C ANISOU 569 CB ASP A 92 7219 6450 4480 177 129 -1572 C ATOM 570 CG ASP A 92 -2.545 -1.611 -40.412 1.00 51.83 C ANISOU 570 CG ASP A 92 7702 6979 5011 163 146 -1535 C ATOM 571 OD1 ASP A 92 -3.407 -1.226 -41.231 1.00 51.96 O ANISOU 571 OD1 ASP A 92 7722 6977 5043 135 175 -1506 O ATOM 572 OD2 ASP A 92 -2.182 -0.929 -39.431 1.00 55.90 O ANISOU 572 OD2 ASP A 92 8187 7528 5526 192 123 -1537 O ATOM 573 N VAL A 93 -1.977 -6.163 -41.173 1.00 30.46 N ANISOU 573 N VAL A 93 5122 4221 2229 144 125 -1637 N ATOM 574 CA VAL A 93 -1.285 -7.403 -41.509 1.00 31.01 C ANISOU 574 CA VAL A 93 5216 4269 2296 201 88 -1667 C ATOM 575 C VAL A 93 -1.897 -8.015 -42.760 1.00 33.05 C ANISOU 575 C VAL A 93 5475 4510 2574 150 126 -1677 C ATOM 576 O VAL A 93 -1.185 -8.448 -43.665 1.00 33.06 O ANISOU 576 O VAL A 93 5471 4484 2606 199 107 -1688 O ATOM 577 CB VAL A 93 -1.345 -8.428 -40.353 1.00 34.76 C ANISOU 577 CB VAL A 93 5752 4746 2710 223 55 -1682 C ATOM 578 CG1 VAL A 93 -1.040 -9.833 -40.856 1.00 35.92 C ANISOU 578 CG1 VAL A 93 5946 4852 2849 264 29 -1704 C ATOM 579 CG2 VAL A 93 -0.382 -8.041 -39.247 1.00 35.09 C ANISOU 579 CG2 VAL A 93 5805 4793 2733 306 -1 -1678 C ATOM 580 N LEU A 94 -3.226 -8.043 -42.793 1.00 30.66 N ANISOU 580 N LEU A 94 5162 4225 2264 60 173 -1667 N ATOM 581 CA LEU A 94 -3.974 -8.523 -43.948 1.00 30.51 C ANISOU 581 CA LEU A 94 5121 4194 2278 15 203 -1663 C ATOM 582 C LEU A 94 -3.531 -7.779 -45.204 1.00 38.93 C ANISOU 582 C LEU A 94 6182 5222 3386 40 212 -1636 C ATOM 583 O LEU A 94 -3.060 -8.388 -46.178 1.00 30.07 O ANISOU 583 O LEU A 94 5065 4081 2281 68 206 -1661 O ATOM 584 CB LEU A 94 -5.477 -8.342 -43.708 1.00 30.35 C ANISOU 584 CB LEU A 94 5051 4212 2269 -69 240 -1644 C ATOM 585 CG LEU A 94 -6.516 -9.085 -44.550 1.00 34.84 C ANISOU 585 CG LEU A 94 5558 4811 2867 -106 256 -1673 C ATOM 586 CD1 LEU A 94 -7.830 -9.131 -43.789 1.00 35.71 C ANISOU 586 CD1 LEU A 94 5549 5036 2982 -88 230 -1710 C ATOM 587 CD2 LEU A 94 -6.719 -8.430 -45.908 1.00 34.50 C ANISOU 587 CD2 LEU A 94 5569 4685 2855 -145 298 -1609 C ATOM 588 N VAL A 95 -3.676 -6.456 -45.159 1.00 39.00 N ANISOU 588 N VAL A 95 6181 5227 3409 44 221 -1591 N ATOM 589 CA VAL A 95 -3.286 -5.592 -46.272 1.00 38.22 C ANISOU 589 CA VAL A 95 6057 5117 3347 93 220 -1577 C ATOM 590 C VAL A 95 -1.847 -5.820 -46.725 1.00 38.91 C ANISOU 590 C VAL A 95 6109 5213 3463 172 187 -1615 C ATOM 591 O VAL A 95 -1.573 -5.970 -47.918 1.00 29.00 O ANISOU 591 O VAL A 95 4834 3946 2239 195 189 -1620 O ATOM 592 CB VAL A 95 -3.436 -4.111 -45.896 1.00 42.38 C ANISOU 592 CB VAL A 95 6554 5664 3884 115 218 -1545 C ATOM 593 CG1 VAL A 95 -3.076 -3.239 -47.056 1.00 40.60 C ANISOU 593 CG1 VAL A 95 6257 5456 3712 168 214 -1537 C ATOM 594 CG2 VAL A 95 -4.836 -3.822 -45.476 1.00 47.12 C ANISOU 594 CG2 VAL A 95 7187 6247 4469 68 233 -1493 C ATOM 595 N THR A 96 -0.936 -5.838 -45.757 1.00 38.99 N ANISOU 595 N THR A 96 6104 5241 3469 221 148 -1632 N ATOM 596 CA THR A 96 0.492 -5.983 -46.015 1.00 29.66 C ANISOU 596 CA THR A 96 4883 4065 2323 311 103 -1659 C ATOM 597 C THR A 96 0.816 -7.313 -46.684 1.00 31.67 C ANISOU 597 C THR A 96 5172 4287 2573 326 92 -1687 C ATOM 598 O THR A 96 1.629 -7.378 -47.607 1.00 32.17 O ANISOU 598 O THR A 96 5202 4344 2677 377 79 -1702 O ATOM 599 CB THR A 96 1.304 -5.866 -44.710 1.00 38.40 C ANISOU 599 CB THR A 96 5983 5192 3416 367 56 -1673 C ATOM 600 OG1 THR A 96 1.132 -4.555 -44.156 1.00 38.88 O ANISOU 600 OG1 THR A 96 5997 5287 3489 362 63 -1652 O ATOM 601 CG2 THR A 96 2.781 -6.114 -44.965 1.00 30.41 C ANISOU 601 CG2 THR A 96 4934 4182 2440 463 5 -1708 C ATOM 602 N ALA A 97 0.170 -8.372 -46.214 1.00 30.52 N ANISOU 602 N ALA A 97 5088 4125 2382 283 97 -1698 N ATOM 603 CA ALA A 97 0.405 -9.703 -46.746 1.00 36.72 C ANISOU 603 CA ALA A 97 5910 4879 3163 302 82 -1726 C ATOM 604 C ALA A 97 -0.115 -9.823 -48.169 1.00 37.97 C ANISOU 604 C ALA A 97 6057 5023 3347 262 122 -1725 C ATOM 605 O ALA A 97 0.634 -10.157 -49.086 1.00 38.83 O ANISOU 605 O ALA A 97 6153 5115 3487 310 106 -1740 O ATOM 606 CB ALA A 97 -0.247 -10.753 -45.856 1.00 38.68 C ANISOU 606 CB ALA A 97 6217 5120 3358 271 77 -1740 C ATOM 607 N ILE A 98 -1.398 -9.533 -48.351 1.00 36.50 N ANISOU 607 N ILE A 98 5877 4845 3146 175 171 -1710 N ATOM 608 CA ILE A 98 -2.062 -9.857 -49.608 1.00 36.71 C ANISOU 608 CA ILE A 98 5909 4855 3186 135 205 -1713 C ATOM 609 C ILE A 98 -2.001 -8.749 -50.658 1.00 29.66 C ANISOU 609 C ILE A 98 4981 3960 2327 157 219 -1680 C ATOM 610 O ILE A 98 -1.658 -9.000 -51.814 1.00 30.05 O ANISOU 610 O ILE A 98 5018 3996 2403 186 218 -1690 O ATOM 611 CB ILE A 98 -3.534 -10.223 -49.355 1.00 30.27 C ANISOU 611 CB ILE A 98 5093 4048 2360 50 235 -1697 C ATOM 612 CG1 ILE A 98 -3.610 -11.456 -48.452 1.00 41.32 C ANISOU 612 CG1 ILE A 98 6507 5464 3730 49 213 -1745 C ATOM 613 CG2 ILE A 98 -4.263 -10.470 -50.667 1.00 34.50 C ANISOU 613 CG2 ILE A 98 5628 4562 2919 20 260 -1686 C ATOM 614 CD1 ILE A 98 -5.013 -11.886 -48.111 1.00 41.51 C ANISOU 614 CD1 ILE A 98 6491 5528 3753 -14 231 -1755 C ATOM 615 N CYS A 99 -2.322 -7.526 -50.255 1.00 31.08 N ANISOU 615 N CYS A 99 5142 4157 2509 153 227 -1644 N ATOM 616 CA CYS A 99 -2.526 -6.445 -51.214 1.00 29.79 C ANISOU 616 CA CYS A 99 4938 4003 2376 176 237 -1614 C ATOM 617 C CYS A 99 -1.247 -5.694 -51.581 1.00 28.54 C ANISOU 617 C CYS A 99 4703 3872 2267 252 215 -1621 C ATOM 618 O CYS A 99 -1.089 -5.261 -52.723 1.00 28.34 O ANISOU 618 O CYS A 99 4640 3855 2273 276 224 -1618 O ATOM 619 CB CYS A 99 -3.564 -5.466 -50.670 1.00 29.30 C ANISOU 619 CB CYS A 99 4883 3950 2300 147 250 -1572 C ATOM 620 SG CYS A 99 -5.149 -6.242 -50.273 1.00 29.16 S ANISOU 620 SG CYS A 99 4929 3898 2252 72 263 -1537 S ATOM 621 N LEU A 100 -0.344 -5.538 -50.618 1.00 28.70 N ANISOU 621 N LEU A 100 4701 3910 2293 287 187 -1634 N ATOM 622 CA LEU A 100 0.906 -4.816 -50.851 1.00 28.64 C ANISOU 622 CA LEU A 100 4618 3931 2334 356 167 -1649 C ATOM 623 C LEU A 100 1.744 -5.410 -51.996 1.00 28.90 C ANISOU 623 C LEU A 100 4638 3949 2395 396 162 -1677 C ATOM 624 O LEU A 100 2.180 -4.664 -52.874 1.00 28.70 O ANISOU 624 O LEU A 100 4555 3941 2407 422 174 -1678 O ATOM 625 CB LEU A 100 1.736 -4.753 -49.557 1.00 28.91 C ANISOU 625 CB LEU A 100 4638 3983 2365 393 130 -1666 C ATOM 626 CG LEU A 100 3.023 -3.919 -49.543 1.00 28.92 C ANISOU 626 CG LEU A 100 4554 4019 2416 461 106 -1689 C ATOM 627 CD1 LEU A 100 3.261 -3.353 -48.153 1.00 30.98 C ANISOU 627 CD1 LEU A 100 4793 4308 2669 477 80 -1690 C ATOM 628 CD2 LEU A 100 4.234 -4.733 -49.985 1.00 32.89 C ANISOU 628 CD2 LEU A 100 5049 4506 2939 520 76 -1731 C ATOM 629 N PRO A 101 1.982 -6.739 -51.999 1.00 29.40 N ANISOU 629 N PRO A 101 4751 3980 2439 401 144 -1703 N ATOM 630 CA PRO A 101 2.790 -7.261 -53.110 1.00 29.65 C ANISOU 630 CA PRO A 101 4769 3998 2500 442 138 -1730 C ATOM 631 C PRO A 101 2.100 -7.099 -54.463 1.00 29.39 C ANISOU 631 C PRO A 101 4735 3957 2473 413 176 -1715 C ATOM 632 O PRO A 101 2.755 -6.772 -55.456 1.00 29.38 O ANISOU 632 O PRO A 101 4694 3963 2506 448 184 -1726 O ATOM 633 CB PRO A 101 2.955 -8.745 -52.762 1.00 30.23 C ANISOU 633 CB PRO A 101 4904 4036 2546 448 111 -1756 C ATOM 634 CG PRO A 101 2.701 -8.829 -51.297 1.00 30.36 C ANISOU 634 CG PRO A 101 4950 4058 2527 435 92 -1749 C ATOM 635 CD PRO A 101 1.651 -7.802 -51.032 1.00 29.81 C ANISOU 635 CD PRO A 101 4869 4010 2446 377 128 -1712 C ATOM 636 N ALA A 102 0.790 -7.323 -54.490 1.00 33.88 N ANISOU 636 N ALA A 102 5349 4513 3009 352 200 -1694 N ATOM 637 CA ALA A 102 0.008 -7.167 -55.711 1.00 34.23 C ANISOU 637 CA ALA A 102 5397 4553 3055 329 229 -1681 C ATOM 638 C ALA A 102 0.052 -5.723 -56.197 1.00 34.02 C ANISOU 638 C ALA A 102 5309 4561 3058 349 244 -1658 C ATOM 639 O ALA A 102 0.196 -5.463 -57.393 1.00 28.55 O ANISOU 639 O ALA A 102 4593 3871 2384 367 260 -1661 O ATOM 640 CB ALA A 102 -1.428 -7.609 -55.482 1.00 33.41 C ANISOU 640 CB ALA A 102 5352 4431 2911 261 247 -1666 C ATOM 641 N SER A 103 -0.068 -4.789 -55.259 1.00 33.32 N ANISOU 641 N SER A 103 5193 4497 2971 345 241 -1637 N ATOM 642 CA SER A 103 0.011 -3.369 -55.575 1.00 32.58 C ANISOU 642 CA SER A 103 5033 4440 2907 362 255 -1619 C ATOM 643 C SER A 103 1.383 -3.013 -56.130 1.00 28.02 C ANISOU 643 C SER A 103 4400 3875 2371 413 254 -1645 C ATOM 644 O SER A 103 1.501 -2.189 -57.036 1.00 29.18 O ANISOU 644 O SER A 103 4509 4037 2541 425 278 -1641 O ATOM 645 CB SER A 103 -0.288 -2.525 -54.338 1.00 27.58 C ANISOU 645 CB SER A 103 4376 3831 2270 350 247 -1598 C ATOM 646 OG SER A 103 -0.048 -1.150 -54.587 1.00 27.24 O ANISOU 646 OG SER A 103 4261 3827 2262 368 260 -1588 O ATOM 647 N LEU A 104 2.417 -3.640 -55.577 1.00 28.38 N ANISOU 647 N LEU A 104 4446 3913 2425 444 228 -1676 N ATOM 648 CA LEU A 104 3.778 -3.437 -56.053 1.00 28.63 C ANISOU 648 CA LEU A 104 4428 3953 2497 494 224 -1709 C ATOM 649 C LEU A 104 3.915 -3.902 -57.496 1.00 33.83 C ANISOU 649 C LEU A 104 5102 4590 3162 502 245 -1720 C ATOM 650 O LEU A 104 4.392 -3.156 -58.354 1.00 34.35 O ANISOU 650 O LEU A 104 5129 4668 3255 519 272 -1726 O ATOM 651 CB LEU A 104 4.779 -4.176 -55.162 1.00 29.07 C ANISOU 651 CB LEU A 104 4486 4004 2557 532 182 -1743 C ATOM 652 CG LEU A 104 6.223 -4.220 -55.666 1.00 29.47 C ANISOU 652 CG LEU A 104 4491 4057 2649 587 172 -1787 C ATOM 653 CD1 LEU A 104 6.783 -2.817 -55.833 1.00 29.28 C ANISOU 653 CD1 LEU A 104 4387 4070 2666 598 194 -1792 C ATOM 654 CD2 LEU A 104 7.096 -5.040 -54.731 1.00 30.50 C ANISOU 654 CD2 LEU A 104 4629 4182 2780 631 120 -1822 C ATOM 655 N LEU A 105 3.490 -5.135 -57.757 1.00 29.06 N ANISOU 655 N LEU A 105 4558 3954 2531 488 236 -1726 N ATOM 656 CA LEU A 105 3.569 -5.703 -59.099 1.00 32.02 C ANISOU 656 CA LEU A 105 4950 4307 2909 496 253 -1740 C ATOM 657 C LEU A 105 2.797 -4.876 -60.119 1.00 31.94 C ANISOU 657 C LEU A 105 4932 4309 2896 476 290 -1715 C ATOM 658 O LEU A 105 3.303 -4.596 -61.205 1.00 32.51 O ANISOU 658 O LEU A 105 4987 4379 2986 498 314 -1727 O ATOM 659 CB LEU A 105 3.056 -7.143 -59.102 1.00 29.60 C ANISOU 659 CB LEU A 105 4708 3966 2572 475 237 -1751 C ATOM 660 CG LEU A 105 4.024 -8.166 -58.509 1.00 34.12 C ANISOU 660 CG LEU A 105 5295 4519 3150 510 200 -1785 C ATOM 661 CD1 LEU A 105 3.462 -9.570 -58.638 1.00 34.37 C ANISOU 661 CD1 LEU A 105 5392 4515 3154 486 190 -1797 C ATOM 662 CD2 LEU A 105 5.381 -8.061 -59.187 1.00 34.95 C ANISOU 662 CD2 LEU A 105 5358 4626 3294 566 197 -1817 C ATOM 663 N VAL A 106 1.575 -4.485 -59.770 1.00 30.83 N ANISOU 663 N VAL A 106 4805 4177 2732 437 296 -1683 N ATOM 664 CA VAL A 106 0.765 -3.672 -60.671 1.00 28.39 C ANISOU 664 CA VAL A 106 4488 3882 2419 425 324 -1660 C ATOM 665 C VAL A 106 1.422 -2.322 -60.935 1.00 28.22 C ANISOU 665 C VAL A 106 4410 3886 2427 449 348 -1654 C ATOM 666 O VAL A 106 1.549 -1.902 -62.082 1.00 28.32 O ANISOU 666 O VAL A 106 4417 3897 2445 462 377 -1656 O ATOM 667 CB VAL A 106 -0.652 -3.440 -60.116 1.00 28.07 C ANISOU 667 CB VAL A 106 4467 3850 2350 383 320 -1629 C ATOM 668 CG1 VAL A 106 -1.409 -2.449 -60.987 1.00 27.85 C ANISOU 668 CG1 VAL A 106 4418 3841 2321 381 343 -1608 C ATOM 669 CG2 VAL A 106 -1.402 -4.752 -60.033 1.00 31.98 C ANISOU 669 CG2 VAL A 106 5023 4314 2813 352 307 -1637 C ATOM 670 N ASP A 107 1.854 -1.651 -59.873 1.00 38.36 N ANISOU 670 N ASP A 107 5655 5191 3728 454 337 -1651 N ATOM 671 CA ASP A 107 2.430 -0.318 -60.012 1.00 38.89 C ANISOU 671 CA ASP A 107 5667 5283 3826 469 362 -1648 C ATOM 672 C ASP A 107 3.762 -0.314 -60.761 1.00 37.71 C ANISOU 672 C ASP A 107 5499 5124 3706 505 381 -1682 C ATOM 673 O ASP A 107 4.106 0.673 -61.412 1.00 37.37 O ANISOU 673 O ASP A 107 5431 5088 3681 514 419 -1681 O ATOM 674 CB ASP A 107 2.603 0.331 -58.636 1.00 41.16 C ANISOU 674 CB ASP A 107 5912 5600 4128 466 343 -1643 C ATOM 675 CG ASP A 107 1.320 0.969 -58.129 1.00 44.09 C ANISOU 675 CG ASP A 107 6284 5989 4481 432 342 -1605 C ATOM 676 OD1 ASP A 107 0.402 1.187 -58.950 1.00 43.87 O ANISOU 676 OD1 ASP A 107 6276 5958 4436 417 361 -1585 O ATOM 677 OD2 ASP A 107 1.237 1.263 -56.917 1.00 43.93 O ANISOU 677 OD2 ASP A 107 6242 5988 4462 422 323 -1599 O ATOM 678 N ILE A 108 4.509 -1.411 -60.677 1.00 38.61 N ANISOU 678 N ILE A 108 5628 5219 3825 526 358 -1714 N ATOM 679 CA ILE A 108 5.782 -1.503 -61.390 1.00 39.58 C ANISOU 679 CA ILE A 108 5732 5331 3977 561 375 -1751 C ATOM 680 C ILE A 108 5.596 -1.910 -62.848 1.00 41.01 C ANISOU 680 C ILE A 108 5953 5486 4144 563 406 -1752 C ATOM 681 O ILE A 108 6.150 -1.285 -63.754 1.00 40.55 O ANISOU 681 O ILE A 108 5885 5422 4100 577 448 -1762 O ATOM 682 CB ILE A 108 6.742 -2.509 -60.719 1.00 44.83 C ANISOU 682 CB ILE A 108 6392 5987 4656 590 333 -1789 C ATOM 683 CG1 ILE A 108 7.409 -1.879 -59.498 1.00 46.41 C ANISOU 683 CG1 ILE A 108 6533 6217 4882 604 310 -1804 C ATOM 684 CG2 ILE A 108 7.818 -2.968 -61.698 1.00 45.53 C ANISOU 684 CG2 ILE A 108 6478 6055 4767 623 349 -1828 C ATOM 685 CD1 ILE A 108 8.576 -2.679 -58.985 1.00 50.08 C ANISOU 685 CD1 ILE A 108 6982 6677 5369 646 270 -1851 C ATOM 686 N THR A 109 4.807 -2.956 -63.068 1.00 38.64 N ANISOU 686 N THR A 109 5700 5167 3812 547 387 -1746 N ATOM 687 CA THR A 109 4.716 -3.577 -64.384 1.00 36.91 C ANISOU 687 CA THR A 109 5518 4925 3582 553 406 -1758 C ATOM 688 C THR A 109 3.504 -3.111 -65.187 1.00 36.86 C ANISOU 688 C THR A 109 5534 4923 3547 529 431 -1728 C ATOM 689 O THR A 109 3.330 -3.513 -66.338 1.00 37.87 O ANISOU 689 O THR A 109 5690 5036 3662 534 448 -1738 O ATOM 690 CB THR A 109 4.661 -5.110 -64.261 1.00 35.99 C ANISOU 690 CB THR A 109 5437 4785 3452 554 370 -1778 C ATOM 691 OG1 THR A 109 3.353 -5.511 -63.837 1.00 35.93 O ANISOU 691 OG1 THR A 109 5462 4778 3413 516 351 -1754 O ATOM 692 CG2 THR A 109 5.689 -5.595 -63.249 1.00 30.15 C ANISOU 692 CG2 THR A 109 4678 4042 2734 579 335 -1805 C ATOM 693 N GLU A 110 2.675 -2.268 -64.575 1.00 29.03 N ANISOU 693 N GLU A 110 4528 3954 2546 506 429 -1696 N ATOM 694 CA GLU A 110 1.449 -1.767 -65.201 1.00 49.63 C ANISOU 694 CA GLU A 110 7154 6573 5130 487 444 -1670 C ATOM 695 C GLU A 110 0.541 -2.895 -65.688 1.00 44.68 C ANISOU 695 C GLU A 110 6568 5933 4474 471 425 -1676 C ATOM 696 O GLU A 110 -0.231 -2.715 -66.627 1.00 41.44 O ANISOU 696 O GLU A 110 6173 5527 4044 467 439 -1671 O ATOM 697 CB GLU A 110 1.781 -0.827 -66.365 1.00 53.76 C ANISOU 697 CB GLU A 110 7676 7093 5656 505 495 -1669 C ATOM 698 CG GLU A 110 2.440 0.479 -65.950 1.00 56.72 C ANISOU 698 CG GLU A 110 8014 7480 6056 514 522 -1659 C ATOM 699 CD GLU A 110 2.548 1.470 -67.096 1.00 59.98 C ANISOU 699 CD GLU A 110 8444 7884 6463 526 581 -1653 C ATOM 700 OE1 GLU A 110 2.637 1.028 -68.262 1.00 59.22 O ANISOU 700 OE1 GLU A 110 8383 7767 6353 537 605 -1668 O ATOM 701 OE2 GLU A 110 2.535 2.691 -66.830 1.00 64.35 O ANISOU 701 OE2 GLU A 110 8977 8448 7024 524 605 -1634 O ATOM 702 N SER A 111 0.629 -4.054 -65.041 1.00 29.12 N ANISOU 702 N SER A 111 4617 3947 2501 463 393 -1691 N ATOM 703 CA SER A 111 -0.151 -5.212 -65.460 1.00 34.56 C ANISOU 703 CA SER A 111 5346 4619 3165 445 376 -1704 C ATOM 704 C SER A 111 -0.685 -6.010 -64.278 1.00 29.28 C ANISOU 704 C SER A 111 4702 3939 2482 414 346 -1701 C ATOM 705 O SER A 111 -0.169 -5.917 -63.163 1.00 29.36 O ANISOU 705 O SER A 111 4701 3951 2502 413 333 -1697 O ATOM 706 CB SER A 111 0.691 -6.124 -66.354 1.00 34.90 C ANISOU 706 CB SER A 111 5405 4640 3217 472 379 -1739 C ATOM 707 OG SER A 111 1.749 -6.724 -65.625 1.00 34.72 O ANISOU 707 OG SER A 111 5377 4601 3213 488 361 -1758 O ATOM 708 N TRP A 112 -1.724 -6.797 -64.535 1.00 31.67 N ANISOU 708 N TRP A 112 5043 4231 2760 386 337 -1706 N ATOM 709 CA TRP A 112 -2.278 -7.688 -63.527 1.00 29.47 C ANISOU 709 CA TRP A 112 4803 3932 2461 348 318 -1708 C ATOM 710 C TRP A 112 -1.779 -9.110 -63.761 1.00 33.75 C ANISOU 710 C TRP A 112 5378 4442 3003 351 307 -1745 C ATOM 711 O TRP A 112 -2.094 -9.729 -64.777 1.00 30.26 O ANISOU 711 O TRP A 112 4953 3990 2554 353 309 -1765 O ATOM 712 CB TRP A 112 -3.806 -7.647 -63.544 1.00 29.38 C ANISOU 712 CB TRP A 112 4815 3925 2422 310 318 -1695 C ATOM 713 CG TRP A 112 -4.413 -8.399 -62.411 1.00 29.43 C ANISOU 713 CG TRP A 112 4868 3908 2405 264 308 -1694 C ATOM 714 CD1 TRP A 112 -4.960 -9.645 -62.453 1.00 29.82 C ANISOU 714 CD1 TRP A 112 4972 3925 2433 230 305 -1719 C ATOM 715 CD2 TRP A 112 -4.520 -7.958 -61.053 1.00 42.23 C ANISOU 715 CD2 TRP A 112 6493 5533 4019 243 304 -1671 C ATOM 716 NE1 TRP A 112 -5.409 -10.008 -61.205 1.00 42.14 N ANISOU 716 NE1 TRP A 112 6569 5468 3975 186 302 -1709 N ATOM 717 CE2 TRP A 112 -5.150 -8.987 -60.328 1.00 42.37 C ANISOU 717 CE2 TRP A 112 6573 5518 4008 194 302 -1681 C ATOM 718 CE3 TRP A 112 -4.148 -6.790 -60.382 1.00 28.72 C ANISOU 718 CE3 TRP A 112 4739 3850 2324 259 304 -1644 C ATOM 719 CZ2 TRP A 112 -5.413 -8.885 -58.964 1.00 42.78 C ANISOU 719 CZ2 TRP A 112 6639 5566 4049 164 296 -1657 C ATOM 720 CZ3 TRP A 112 -4.411 -6.690 -59.029 1.00 44.93 C ANISOU 720 CZ3 TRP A 112 6810 5899 4361 232 297 -1627 C ATOM 721 CH2 TRP A 112 -5.038 -7.730 -58.334 1.00 44.08 C ANISOU 721 CH2 TRP A 112 6770 5758 4222 184 296 -1636 C ATOM 722 N LEU A 113 -1.001 -9.622 -62.814 1.00 34.51 N ANISOU 722 N LEU A 113 5482 4524 3107 356 291 -1756 N ATOM 723 CA LEU A 113 -0.358 -10.922 -62.971 1.00 35.70 C ANISOU 723 CA LEU A 113 5658 4645 3262 369 276 -1793 C ATOM 724 C LEU A 113 -1.072 -12.021 -62.196 1.00 37.32 C ANISOU 724 C LEU A 113 5915 4824 3441 320 267 -1806 C ATOM 725 O LEU A 113 -0.538 -13.117 -62.024 1.00 36.87 O ANISOU 725 O LEU A 113 5880 4741 3386 329 251 -1837 O ATOM 726 CB LEU A 113 1.100 -10.840 -62.522 1.00 30.64 C ANISOU 726 CB LEU A 113 4989 4004 2649 417 259 -1805 C ATOM 727 CG LEU A 113 1.957 -9.813 -63.261 1.00 30.51 C ANISOU 727 CG LEU A 113 4923 4010 2662 460 275 -1801 C ATOM 728 CD1 LEU A 113 3.275 -9.602 -62.539 1.00 31.01 C ANISOU 728 CD1 LEU A 113 4954 4076 2751 501 258 -1814 C ATOM 729 CD2 LEU A 113 2.193 -10.258 -64.695 1.00 30.85 C ANISOU 729 CD2 LEU A 113 4970 4040 2711 482 288 -1824 C ATOM 730 N PHE A 114 -2.279 -11.729 -61.730 1.00 39.71 N ANISOU 730 N PHE A 114 6239 5132 3718 269 280 -1785 N ATOM 731 CA PHE A 114 -3.024 -12.689 -60.930 1.00 41.92 C ANISOU 731 CA PHE A 114 6569 5388 3970 210 282 -1801 C ATOM 732 C PHE A 114 -4.308 -13.102 -61.636 1.00 47.75 C ANISOU 732 C PHE A 114 7334 6114 4694 171 294 -1801 C ATOM 733 O PHE A 114 -4.628 -12.590 -62.709 1.00 47.07 O ANISOU 733 O PHE A 114 7235 6040 4608 193 299 -1797 O ATOM 734 CB PHE A 114 -3.318 -12.102 -59.549 1.00 38.87 C ANISOU 734 CB PHE A 114 6184 5013 3570 180 283 -1772 C ATOM 735 CG PHE A 114 -2.099 -11.558 -58.862 1.00 35.87 C ANISOU 735 CG PHE A 114 5770 4649 3209 227 265 -1767 C ATOM 736 CD1 PHE A 114 -1.213 -12.407 -58.220 1.00 34.30 C ANISOU 736 CD1 PHE A 114 5581 4437 3015 250 240 -1795 C ATOM 737 CD2 PHE A 114 -1.829 -10.200 -58.874 1.00 34.43 C ANISOU 737 CD2 PHE A 114 5542 4497 3044 257 266 -1734 C ATOM 738 CE1 PHE A 114 -0.085 -11.911 -57.595 1.00 33.42 C ANISOU 738 CE1 PHE A 114 5438 4339 2922 303 215 -1790 C ATOM 739 CE2 PHE A 114 -0.702 -9.698 -58.251 1.00 33.67 C ANISOU 739 CE2 PHE A 114 5408 4416 2969 301 248 -1733 C ATOM 740 CZ PHE A 114 0.170 -10.555 -57.609 1.00 33.06 C ANISOU 740 CZ PHE A 114 5344 4323 2893 325 221 -1760 C ATOM 741 N GLY A 115 -5.035 -14.038 -61.037 1.00 52.67 N ANISOU 741 N GLY A 115 7987 6716 5307 117 296 -1809 N ATOM 742 CA GLY A 115 -6.227 -14.582 -61.658 1.00 58.31 C ANISOU 742 CA GLY A 115 8733 7413 6011 82 304 -1813 C ATOM 743 C GLY A 115 -7.354 -13.577 -61.781 1.00 60.11 C ANISOU 743 C GLY A 115 8968 7650 6222 80 303 -1769 C ATOM 744 O GLY A 115 -7.246 -12.444 -61.313 1.00 58.91 O ANISOU 744 O GLY A 115 8790 7523 6069 97 300 -1736 O ATOM 745 N HIS A 116 -8.438 -13.992 -62.427 1.00 62.18 N ANISOU 745 N HIS A 116 9263 7894 6470 68 299 -1776 N ATOM 746 CA HIS A 116 -9.635 -13.169 -62.502 1.00 62.33 C ANISOU 746 CA HIS A 116 9289 7924 6470 81 284 -1747 C ATOM 747 C HIS A 116 -10.293 -13.101 -61.131 1.00 31.18 C ANISOU 747 C HIS A 116 5387 3954 2507 56 275 -1708 C ATOM 748 O HIS A 116 -10.926 -12.106 -60.782 1.00 40.85 O ANISOU 748 O HIS A 116 6595 5204 3723 80 258 -1681 O ATOM 749 CB HIS A 116 -10.614 -13.725 -63.538 1.00 61.46 C ANISOU 749 CB HIS A 116 9201 7804 6348 88 271 -1778 C ATOM 750 CG HIS A 116 -10.063 -13.768 -64.928 1.00 60.79 C ANISOU 750 CG HIS A 116 9081 7742 6275 119 277 -1817 C ATOM 751 ND1 HIS A 116 -10.214 -12.729 -65.822 1.00 59.75 N ANISOU 751 ND1 HIS A 116 8902 7658 6142 157 275 -1821 N ATOM 752 CD2 HIS A 116 -9.361 -14.725 -65.581 1.00 61.78 C ANISOU 752 CD2 HIS A 116 9214 7849 6411 121 284 -1854 C ATOM 753 CE1 HIS A 116 -9.630 -13.044 -66.964 1.00 60.81 C ANISOU 753 CE1 HIS A 116 9024 7799 6283 184 280 -1855 C ATOM 754 NE2 HIS A 116 -9.105 -14.250 -66.844 1.00 62.86 N ANISOU 754 NE2 HIS A 116 9315 8019 6551 166 283 -1876 N ATOM 755 N ALA A 117 -10.131 -14.169 -60.357 1.00 36.54 N ANISOU 755 N ALA A 117 6114 4587 3180 7 289 -1710 N ATOM 756 CA ALA A 117 -10.709 -14.246 -59.021 1.00 37.26 C ANISOU 756 CA ALA A 117 6273 4640 3247 -5 276 -1668 C ATOM 757 C ALA A 117 -10.033 -13.265 -58.071 1.00 35.51 C ANISOU 757 C ALA A 117 6001 4456 3034 -16 290 -1643 C ATOM 758 O ALA A 117 -10.702 -12.506 -57.369 1.00 33.52 O ANISOU 758 O ALA A 117 5776 4200 2760 36 251 -1599 O ATOM 759 CB ALA A 117 -10.606 -15.665 -58.481 1.00 38.40 C ANISOU 759 CB ALA A 117 6447 4748 3395 -100 322 -1698 C ATOM 760 N LEU A 118 -8.703 -13.281 -58.058 1.00 38.03 N ANISOU 760 N LEU A 118 6240 4823 3387 -39 318 -1683 N ATOM 761 CA LEU A 118 -7.932 -12.387 -57.199 1.00 38.14 C ANISOU 761 CA LEU A 118 6211 4873 3409 -25 315 -1667 C ATOM 762 C LEU A 118 -8.106 -10.932 -57.624 1.00 38.18 C ANISOU 762 C LEU A 118 6195 4899 3411 38 295 -1629 C ATOM 763 O LEU A 118 -7.883 -10.012 -56.833 1.00 38.59 O ANISOU 763 O LEU A 118 6227 4972 3464 50 291 -1603 O ATOM 764 CB LEU A 118 -6.451 -12.772 -57.214 1.00 30.67 C ANISOU 764 CB LEU A 118 5212 3955 2486 1 311 -1717 C ATOM 765 CG LEU A 118 -6.125 -14.176 -56.702 1.00 33.70 C ANISOU 765 CG LEU A 118 5578 4349 2879 -27 311 -1780 C ATOM 766 CD1 LEU A 118 -4.621 -14.407 -56.678 1.00 33.88 C ANISOU 766 CD1 LEU A 118 5594 4371 2908 42 282 -1811 C ATOM 767 CD2 LEU A 118 -6.731 -14.403 -55.325 1.00 31.41 C ANISOU 767 CD2 LEU A 118 5251 4097 2585 -83 318 -1796 C ATOM 768 N CYS A 119 -8.510 -10.735 -58.876 1.00 29.97 N ANISOU 768 N CYS A 119 5143 3868 2375 70 288 -1640 N ATOM 769 CA CYS A 119 -8.816 -9.406 -59.391 1.00 32.29 C ANISOU 769 CA CYS A 119 5388 4205 2674 112 281 -1626 C ATOM 770 C CYS A 119 -10.002 -8.808 -58.646 1.00 29.32 C ANISOU 770 C CYS A 119 5023 3837 2282 113 262 -1596 C ATOM 771 O CYS A 119 -10.113 -7.593 -58.504 1.00 28.89 O ANISOU 771 O CYS A 119 4917 3825 2235 132 262 -1582 O ATOM 772 CB CYS A 119 -9.106 -9.460 -60.891 1.00 29.69 C ANISOU 772 CB CYS A 119 5041 3891 2350 134 282 -1655 C ATOM 773 SG CYS A 119 -9.527 -7.862 -61.627 1.00 46.78 S ANISOU 773 SG CYS A 119 7140 6115 4521 171 284 -1648 S ATOM 774 N LYS A 120 -10.894 -9.672 -58.175 1.00 29.68 N ANISOU 774 N LYS A 120 5130 3843 2305 101 243 -1592 N ATOM 775 CA LYS A 120 -12.026 -9.230 -57.376 1.00 47.13 C ANISOU 775 CA LYS A 120 7339 6068 4499 121 212 -1578 C ATOM 776 C LYS A 120 -11.650 -9.242 -55.901 1.00 29.49 C ANISOU 776 C LYS A 120 5141 3813 2253 123 202 -1544 C ATOM 777 O LYS A 120 -11.928 -8.292 -55.173 1.00 29.14 O ANISOU 777 O LYS A 120 5056 3806 2209 134 195 -1529 O ATOM 778 CB LYS A 120 -13.245 -10.120 -57.626 1.00 45.76 C ANISOU 778 CB LYS A 120 7195 5880 4309 136 181 -1609 C ATOM 779 CG LYS A 120 -13.523 -10.374 -59.098 1.00 44.87 C ANISOU 779 CG LYS A 120 7068 5777 4205 127 193 -1647 C ATOM 780 CD LYS A 120 -14.658 -11.368 -59.301 1.00 46.02 C ANISOU 780 CD LYS A 120 7241 5907 4338 133 164 -1689 C ATOM 781 CE LYS A 120 -16.011 -10.678 -59.308 1.00 47.06 C ANISOU 781 CE LYS A 120 7312 6097 4471 123 159 -1723 C ATOM 782 NZ LYS A 120 -16.069 -9.598 -60.335 1.00 47.82 N ANISOU 782 NZ LYS A 120 7350 6243 4578 117 182 -1729 N ATOM 783 N VAL A 121 -10.995 -10.319 -55.480 1.00 29.86 N ANISOU 783 N VAL A 121 5260 3799 2288 99 211 -1535 N ATOM 784 CA VAL A 121 -10.657 -10.530 -54.078 1.00 29.94 C ANISOU 784 CA VAL A 121 5322 3777 2278 94 204 -1504 C ATOM 785 C VAL A 121 -9.754 -9.445 -53.497 1.00 30.99 C ANISOU 785 C VAL A 121 5390 3955 2431 49 244 -1496 C ATOM 786 O VAL A 121 -10.105 -8.811 -52.503 1.00 31.42 O ANISOU 786 O VAL A 121 5448 4020 2470 87 215 -1469 O ATOM 787 CB VAL A 121 -9.965 -11.894 -53.876 1.00 34.62 C ANISOU 787 CB VAL A 121 5945 4333 2877 -52 287 -1534 C ATOM 788 CG1 VAL A 121 -9.432 -12.017 -52.457 1.00 30.59 C ANISOU 788 CG1 VAL A 121 5217 3981 2424 -231 375 -1634 C ATOM 789 CG2 VAL A 121 -10.928 -13.029 -54.190 1.00 35.59 C ANISOU 789 CG2 VAL A 121 6179 4388 2956 189 122 -1519 C ATOM 790 N ILE A 122 -8.596 -9.235 -54.113 1.00 29.32 N ANISOU 790 N ILE A 122 5104 3784 2253 21 278 -1532 N ATOM 791 CA ILE A 122 -7.578 -8.356 -53.537 1.00 32.05 C ANISOU 791 CA ILE A 122 5391 4173 2615 34 282 -1535 C ATOM 792 C ILE A 122 -8.034 -6.892 -53.367 1.00 32.45 C ANISOU 792 C ILE A 122 5405 4256 2668 80 264 -1504 C ATOM 793 O ILE A 122 -7.826 -6.310 -52.297 1.00 31.86 O ANISOU 793 O ILE A 122 5323 4195 2588 79 261 -1488 O ATOM 794 CB ILE A 122 -6.276 -8.409 -54.369 1.00 28.99 C ANISOU 794 CB ILE A 122 4949 3810 2255 65 286 -1578 C ATOM 795 CG1 ILE A 122 -5.707 -9.829 -54.349 1.00 29.55 C ANISOU 795 CG1 ILE A 122 5029 3870 2328 36 292 -1627 C ATOM 796 CG2 ILE A 122 -5.257 -7.417 -53.837 1.00 28.67 C ANISOU 796 CG2 ILE A 122 4862 3804 2227 105 278 -1579 C ATOM 797 CD1 ILE A 122 -4.439 -9.996 -55.149 1.00 29.63 C ANISOU 797 CD1 ILE A 122 5011 3889 2359 93 281 -1665 C ATOM 798 N PRO A 123 -8.662 -6.289 -54.397 1.00 33.96 N ANISOU 798 N PRO A 123 5561 4473 2870 111 258 -1506 N ATOM 799 CA PRO A 123 -9.190 -4.944 -54.135 1.00 34.61 C ANISOU 799 CA PRO A 123 5588 4603 2960 131 252 -1492 C ATOM 800 C PRO A 123 -10.301 -4.954 -53.086 1.00 38.12 C ANISOU 800 C PRO A 123 6058 5044 3380 128 230 -1473 C ATOM 801 O PRO A 123 -10.436 -3.998 -52.315 1.00 40.36 O ANISOU 801 O PRO A 123 6304 5363 3667 131 229 -1460 O ATOM 802 CB PRO A 123 -9.731 -4.505 -55.499 1.00 31.11 C ANISOU 802 CB PRO A 123 5103 4189 2529 147 258 -1509 C ATOM 803 CG PRO A 123 -8.980 -5.323 -56.486 1.00 27.94 C ANISOU 803 CG PRO A 123 4718 3762 2134 149 269 -1532 C ATOM 804 CD PRO A 123 -8.800 -6.652 -55.819 1.00 34.98 C ANISOU 804 CD PRO A 123 5680 4601 3008 120 264 -1531 C ATOM 805 N TYR A 124 -11.081 -6.031 -53.062 1.00 28.21 N ANISOU 805 N TYR A 124 4863 3754 2103 131 210 -1477 N ATOM 806 CA TYR A 124 -12.129 -6.198 -52.063 1.00 31.18 C ANISOU 806 CA TYR A 124 5252 4139 2458 149 178 -1476 C ATOM 807 C TYR A 124 -11.531 -6.227 -50.664 1.00 31.51 C ANISOU 807 C TYR A 124 5330 4160 2481 159 167 -1448 C ATOM 808 O TYR A 124 -11.974 -5.496 -49.784 1.00 31.21 O ANISOU 808 O TYR A 124 5255 4163 2440 162 161 -1444 O ATOM 809 CB TYR A 124 -12.932 -7.475 -52.325 1.00 28.92 C ANISOU 809 CB TYR A 124 5003 3831 2156 172 146 -1506 C ATOM 810 CG TYR A 124 -13.853 -7.878 -51.194 1.00 31.14 C ANISOU 810 CG TYR A 124 5267 4144 2419 193 114 -1534 C ATOM 811 CD1 TYR A 124 -15.063 -7.227 -50.990 1.00 29.10 C ANISOU 811 CD1 TYR A 124 4954 3940 2163 148 134 -1559 C ATOM 812 CD2 TYR A 124 -13.518 -8.921 -50.337 1.00 31.39 C ANISOU 812 CD2 TYR A 124 5315 4175 2438 248 68 -1553 C ATOM 813 CE1 TYR A 124 -15.910 -7.596 -49.962 1.00 29.64 C ANISOU 813 CE1 TYR A 124 5011 4037 2213 128 132 -1592 C ATOM 814 CE2 TYR A 124 -14.359 -9.297 -49.305 1.00 30.02 C ANISOU 814 CE2 TYR A 124 5098 4056 2251 230 65 -1603 C ATOM 815 CZ TYR A 124 -15.553 -8.632 -49.124 1.00 30.31 C ANISOU 815 CZ TYR A 124 5118 4118 2282 160 104 -1613 C ATOM 816 OH TYR A 124 -16.394 -9.000 -48.100 1.00 30.26 O ANISOU 816 OH TYR A 124 5107 4137 2252 114 123 -1652 O ATOM 817 N LEU A 125 -10.517 -7.064 -50.468 1.00 31.79 N ANISOU 817 N LEU A 125 5441 4131 2505 140 178 -1432 N ATOM 818 CA LEU A 125 -9.858 -7.168 -49.171 1.00 28.83 C ANISOU 818 CA LEU A 125 5116 3727 2110 113 189 -1408 C ATOM 819 C LEU A 125 -9.207 -5.847 -48.776 1.00 32.72 C ANISOU 819 C LEU A 125 5531 4276 2626 85 216 -1409 C ATOM 820 O LEU A 125 -9.176 -5.493 -47.597 1.00 33.48 O ANISOU 820 O LEU A 125 5641 4376 2706 85 210 -1392 O ATOM 821 CB LEU A 125 -8.820 -8.291 -49.182 1.00 36.15 C ANISOU 821 CB LEU A 125 6047 4639 3049 -53 281 -1446 C ATOM 822 CG LEU A 125 -9.406 -9.695 -49.336 1.00 37.45 C ANISOU 822 CG LEU A 125 6230 4786 3212 -161 330 -1478 C ATOM 823 CD1 LEU A 125 -8.352 -10.755 -49.067 1.00 37.41 C ANISOU 823 CD1 LEU A 125 5820 5088 3305 -192 322 -1714 C ATOM 824 CD2 LEU A 125 -10.600 -9.876 -48.413 1.00 36.55 C ANISOU 824 CD2 LEU A 125 5781 4978 3131 430 -53 -1623 C ATOM 825 N GLN A 126 -8.699 -5.119 -49.767 1.00 27.96 N ANISOU 825 N GLN A 126 4848 3717 2059 89 233 -1431 N ATOM 826 CA GLN A 126 -8.152 -3.789 -49.523 1.00 27.50 C ANISOU 826 CA GLN A 126 4711 3713 2023 106 238 -1435 C ATOM 827 C GLN A 126 -9.222 -2.857 -48.956 1.00 35.58 C ANISOU 827 C GLN A 126 5704 4773 3042 121 224 -1418 C ATOM 828 O GLN A 126 -9.025 -2.232 -47.909 1.00 36.19 O ANISOU 828 O GLN A 126 5767 4870 3114 119 223 -1408 O ATOM 829 CB GLN A 126 -7.570 -3.202 -50.809 1.00 27.22 C ANISOU 829 CB GLN A 126 4608 3711 2023 130 250 -1459 C ATOM 830 CG GLN A 126 -7.017 -1.795 -50.649 1.00 28.93 C ANISOU 830 CG GLN A 126 4737 3983 2272 155 253 -1459 C ATOM 831 CD GLN A 126 -5.744 -1.759 -49.825 1.00 29.00 C ANISOU 831 CD GLN A 126 4734 3997 2288 164 249 -1472 C ATOM 832 OE1 GLN A 126 -4.786 -2.477 -50.113 1.00 28.84 O ANISOU 832 OE1 GLN A 126 4725 3961 2271 173 248 -1498 O ATOM 833 NE2 GLN A 126 -5.729 -0.922 -48.793 1.00 28.79 N ANISOU 833 NE2 GLN A 126 4672 4000 2265 167 241 -1459 N ATOM 834 N ALA A 127 -10.356 -2.779 -49.650 1.00 27.13 N ANISOU 834 N ALA A 127 4612 3721 1974 127 219 -1425 N ATOM 835 CA ALA A 127 -11.468 -1.933 -49.218 1.00 26.88 C ANISOU 835 CA ALA A 127 4530 3741 1943 122 216 -1427 C ATOM 836 C ALA A 127 -11.942 -2.313 -47.817 1.00 30.19 C ANISOU 836 C ALA A 127 4990 4151 2332 124 196 -1416 C ATOM 837 O ALA A 127 -12.055 -1.458 -46.930 1.00 30.28 O ANISOU 837 O ALA A 127 4967 4196 2341 115 202 -1409 O ATOM 838 CB ALA A 127 -12.619 -2.028 -50.208 1.00 26.93 C ANISOU 838 CB ALA A 127 4500 3769 1962 111 218 -1445 C ATOM 839 N VAL A 128 -12.209 -3.603 -47.632 1.00 31.71 N ANISOU 839 N VAL A 128 5248 4303 2498 145 170 -1420 N ATOM 840 CA VAL A 128 -12.645 -4.152 -46.353 1.00 32.05 C ANISOU 840 CA VAL A 128 5318 4351 2510 171 141 -1424 C ATOM 841 C VAL A 128 -11.699 -3.777 -45.224 1.00 33.94 C ANISOU 841 C VAL A 128 5591 4571 2735 182 138 -1392 C ATOM 842 O VAL A 128 -12.131 -3.346 -44.158 1.00 27.99 O ANISOU 842 O VAL A 128 4815 3854 1966 183 133 -1393 O ATOM 843 CB VAL A 128 -12.757 -5.691 -46.409 1.00 33.08 C ANISOU 843 CB VAL A 128 5485 4463 2622 221 100 -1453 C ATOM 844 CG1 VAL A 128 -12.944 -6.268 -45.012 1.00 29.11 C ANISOU 844 CG1 VAL A 128 4955 4012 2094 255 69 -1487 C ATOM 845 CG2 VAL A 128 -13.894 -6.111 -47.320 1.00 33.49 C ANISOU 845 CG2 VAL A 128 5507 4534 2682 188 113 -1496 C ATOM 846 N SER A 129 -10.405 -3.939 -45.464 1.00 35.03 N ANISOU 846 N SER A 129 5783 4652 2877 158 159 -1370 N ATOM 847 CA SER A 129 -9.416 -3.669 -44.433 1.00 35.47 C ANISOU 847 CA SER A 129 5870 4687 2920 115 182 -1353 C ATOM 848 C SER A 129 -9.316 -2.183 -44.111 1.00 35.00 C ANISOU 848 C SER A 129 5718 4697 2885 112 192 -1360 C ATOM 849 O SER A 129 -9.116 -1.812 -42.952 1.00 34.86 O ANISOU 849 O SER A 129 5710 4686 2849 105 191 -1351 O ATOM 850 CB SER A 129 -8.057 -4.201 -44.854 1.00 36.39 C ANISOU 850 CB SER A 129 5980 4794 3053 29 232 -1382 C ATOM 851 OG SER A 129 -8.095 -5.597 -45.086 1.00 38.06 O ANISOU 851 OG SER A 129 6237 4970 3254 -48 265 -1399 O ATOM 852 N VAL A 130 -9.444 -1.334 -45.128 1.00 27.05 N ANISOU 852 N VAL A 130 4623 3738 1917 116 204 -1378 N ATOM 853 CA VAL A 130 -9.496 0.103 -44.880 1.00 29.83 C ANISOU 853 CA VAL A 130 4887 4154 2292 115 215 -1385 C ATOM 854 C VAL A 130 -10.678 0.403 -43.962 1.00 30.30 C ANISOU 854 C VAL A 130 4942 4239 2331 108 207 -1376 C ATOM 855 O VAL A 130 -10.542 1.122 -42.963 1.00 30.38 O ANISOU 855 O VAL A 130 4924 4277 2343 101 208 -1367 O ATOM 856 CB VAL A 130 -9.623 0.917 -46.182 1.00 29.54 C ANISOU 856 CB VAL A 130 4741 4166 2318 115 228 -1390 C ATOM 857 CG1 VAL A 130 -9.829 2.390 -45.866 1.00 25.67 C ANISOU 857 CG1 VAL A 130 4134 3745 1874 106 236 -1381 C ATOM 858 CG2 VAL A 130 -8.390 0.729 -47.049 1.00 30.01 C ANISOU 858 CG2 VAL A 130 4789 4213 2400 133 234 -1404 C ATOM 859 N SER A 131 -11.828 -0.180 -44.297 1.00 29.64 N ANISOU 859 N SER A 131 4869 4155 2236 106 200 -1384 N ATOM 860 CA SER A 131 -13.027 -0.064 -43.470 1.00 29.84 C ANISOU 860 CA SER A 131 4871 4217 2251 85 200 -1387 C ATOM 861 C SER A 131 -12.748 -0.450 -42.018 1.00 27.22 C ANISOU 861 C SER A 131 4605 3866 1872 112 179 -1377 C ATOM 862 O SER A 131 -12.958 0.352 -41.109 1.00 27.08 O ANISOU 862 O SER A 131 4559 3882 1848 94 188 -1373 O ATOM 863 CB SER A 131 -14.153 -0.935 -44.035 1.00 29.94 C ANISOU 863 CB SER A 131 4886 4231 2258 71 198 -1411 C ATOM 864 OG SER A 131 -15.275 -0.945 -43.170 1.00 27.35 O ANISOU 864 OG SER A 131 4531 3937 1922 29 211 -1420 O ATOM 865 N VAL A 132 -12.266 -1.675 -41.818 1.00 27.73 N ANISOU 865 N VAL A 132 4745 3882 1911 158 147 -1371 N ATOM 866 CA VAL A 132 -11.933 -2.191 -40.492 1.00 28.22 C ANISOU 866 CA VAL A 132 4855 3936 1932 206 114 -1364 C ATOM 867 C VAL A 132 -11.030 -1.241 -39.719 1.00 31.65 C ANISOU 867 C VAL A 132 5315 4347 2365 179 133 -1331 C ATOM 868 O VAL A 132 -11.282 -0.946 -38.552 1.00 32.23 O ANISOU 868 O VAL A 132 5387 4447 2412 192 123 -1329 O ATOM 869 CB VAL A 132 -11.238 -3.567 -40.583 1.00 28.78 C ANISOU 869 CB VAL A 132 4968 3979 1987 289 62 -1375 C ATOM 870 CG1 VAL A 132 -10.677 -3.978 -39.229 1.00 29.30 C ANISOU 870 CG1 VAL A 132 4977 4125 2031 377 4 -1411 C ATOM 871 CG2 VAL A 132 -12.203 -4.614 -41.108 1.00 29.12 C ANISOU 871 CG2 VAL A 132 4934 4094 2036 287 54 -1446 C ATOM 872 N ALA A 133 -9.983 -0.761 -40.383 1.00 31.56 N ANISOU 872 N ALA A 133 5293 4316 2384 130 166 -1328 N ATOM 873 CA ALA A 133 -9.041 0.169 -39.775 1.00 27.50 C ANISOU 873 CA ALA A 133 4740 3828 1879 99 185 -1336 C ATOM 874 C ALA A 133 -9.743 1.426 -39.270 1.00 43.51 C ANISOU 874 C ALA A 133 6690 5924 3920 104 186 -1340 C ATOM 875 O ALA A 133 -9.643 1.780 -38.086 1.00 42.57 O ANISOU 875 O ALA A 133 6586 5814 3776 101 182 -1333 O ATOM 876 CB ALA A 133 -7.951 0.537 -40.770 1.00 27.20 C ANISOU 876 CB ALA A 133 4634 3815 1884 93 200 -1367 C ATOM 877 N VAL A 134 -10.463 2.090 -40.171 1.00 26.62 N ANISOU 877 N VAL A 134 4462 3832 1821 95 199 -1351 N ATOM 878 CA VAL A 134 -11.122 3.344 -39.823 1.00 36.39 C ANISOU 878 CA VAL A 134 5582 5141 3104 66 213 -1345 C ATOM 879 C VAL A 134 -12.148 3.163 -38.706 1.00 36.28 C ANISOU 879 C VAL A 134 5603 5134 3047 54 210 -1340 C ATOM 880 O VAL A 134 -12.180 3.943 -37.756 1.00 26.43 O ANISOU 880 O VAL A 134 4319 3919 1803 41 215 -1334 O ATOM 881 CB VAL A 134 -11.820 3.974 -41.039 1.00 36.56 C ANISOU 881 CB VAL A 134 5493 5208 3192 39 232 -1347 C ATOM 882 CG1 VAL A 134 -12.367 5.331 -40.669 1.00 25.35 C ANISOU 882 CG1 VAL A 134 3956 3857 1820 2 248 -1342 C ATOM 883 CG2 VAL A 134 -10.851 4.109 -42.190 1.00 38.32 C ANISOU 883 CG2 VAL A 134 5681 5427 3452 60 233 -1354 C ATOM 884 N LEU A 135 -12.981 2.133 -38.822 1.00 35.66 N ANISOU 884 N LEU A 135 5581 5035 2934 60 203 -1349 N ATOM 885 CA LEU A 135 -13.984 1.843 -37.802 1.00 27.23 C ANISOU 885 CA LEU A 135 4529 3988 1830 44 206 -1354 C ATOM 886 C LEU A 135 -13.333 1.552 -36.457 1.00 34.90 C ANISOU 886 C LEU A 135 5586 4937 2738 97 178 -1348 C ATOM 887 O LEU A 135 -13.851 1.940 -35.411 1.00 35.63 O ANISOU 887 O LEU A 135 5668 5062 2808 79 187 -1349 O ATOM 888 CB LEU A 135 -14.859 0.664 -38.228 1.00 45.83 C ANISOU 888 CB LEU A 135 6909 6336 4168 36 207 -1377 C ATOM 889 CG LEU A 135 -15.855 0.962 -39.350 1.00 43.92 C ANISOU 889 CG LEU A 135 6581 6120 3987 -34 240 -1383 C ATOM 890 CD1 LEU A 135 -16.600 -0.298 -39.761 1.00 45.38 C ANISOU 890 CD1 LEU A 135 6801 6288 4153 -50 244 -1411 C ATOM 891 CD2 LEU A 135 -16.830 2.043 -38.914 1.00 44.94 C ANISOU 891 CD2 LEU A 135 6617 6303 4155 -112 276 -1376 C ATOM 892 N THR A 136 -12.193 0.871 -36.494 1.00 27.96 N ANISOU 892 N THR A 136 4776 4000 1849 147 149 -1330 N ATOM 893 CA THR A 136 -11.442 0.568 -35.283 1.00 28.95 C ANISOU 893 CA THR A 136 4978 4090 1932 189 122 -1310 C ATOM 894 C THR A 136 -10.977 1.850 -34.605 1.00 29.65 C ANISOU 894 C THR A 136 5043 4195 2030 140 148 -1301 C ATOM 895 O THR A 136 -11.164 2.030 -33.399 1.00 31.01 O ANISOU 895 O THR A 136 5239 4379 2165 154 139 -1294 O ATOM 896 CB THR A 136 -10.223 -0.322 -35.583 1.00 28.80 C ANISOU 896 CB THR A 136 5069 3972 1900 189 116 -1284 C ATOM 897 OG1 THR A 136 -10.669 -1.606 -36.037 1.00 29.19 O ANISOU 897 OG1 THR A 136 5075 4071 1945 310 51 -1322 O ATOM 898 CG2 THR A 136 -9.378 -0.500 -34.338 1.00 29.33 C ANISOU 898 CG2 THR A 136 5248 3976 1922 79 161 -1262 C ATOM 899 N LEU A 137 -10.380 2.744 -35.388 1.00 28.67 N ANISOU 899 N LEU A 137 4842 4097 1955 103 172 -1317 N ATOM 900 CA LEU A 137 -9.952 4.036 -34.861 1.00 27.26 C ANISOU 900 CA LEU A 137 4587 3974 1796 86 183 -1333 C ATOM 901 C LEU A 137 -11.141 4.819 -34.312 1.00 27.05 C ANISOU 901 C LEU A 137 4486 4005 1788 65 194 -1325 C ATOM 902 O LEU A 137 -11.018 5.550 -33.326 1.00 27.08 O ANISOU 902 O LEU A 137 4462 4039 1788 57 194 -1324 O ATOM 903 CB LEU A 137 -9.237 4.843 -35.943 1.00 26.69 C ANISOU 903 CB LEU A 137 4378 3950 1814 81 191 -1346 C ATOM 904 CG LEU A 137 -7.919 4.232 -36.418 1.00 28.60 C ANISOU 904 CG LEU A 137 4650 4162 2055 98 183 -1366 C ATOM 905 CD1 LEU A 137 -7.394 4.971 -37.637 1.00 28.95 C ANISOU 905 CD1 LEU A 137 4558 4253 2186 113 187 -1379 C ATOM 906 CD2 LEU A 137 -6.893 4.245 -35.298 1.00 27.33 C ANISOU 906 CD2 LEU A 137 4510 4009 1865 106 169 -1386 C ATOM 907 N SER A 138 -12.292 4.650 -34.954 1.00 32.42 N ANISOU 907 N SER A 138 5124 4704 2491 41 207 -1323 N ATOM 908 CA SER A 138 -13.518 5.321 -34.539 1.00 32.72 C ANISOU 908 CA SER A 138 5079 4797 2554 -13 232 -1320 C ATOM 909 C SER A 138 -14.000 4.817 -33.186 1.00 33.95 C ANISOU 909 C SER A 138 5319 4945 2637 -1 225 -1320 C ATOM 910 O SER A 138 -14.443 5.600 -32.350 1.00 33.97 O ANISOU 910 O SER A 138 5272 4987 2646 -35 240 -1315 O ATOM 911 CB SER A 138 -14.616 5.133 -35.587 1.00 34.51 C ANISOU 911 CB SER A 138 5248 5043 2823 -60 255 -1326 C ATOM 912 OG SER A 138 -14.284 5.789 -36.797 1.00 38.35 O ANISOU 912 OG SER A 138 5644 5549 3377 -68 261 -1327 O ATOM 913 N PHE A 139 -13.919 3.508 -32.975 1.00 27.92 N ANISOU 913 N PHE A 139 4669 4139 1801 55 200 -1329 N ATOM 914 CA PHE A 139 -14.339 2.927 -31.708 1.00 47.31 C ANISOU 914 CA PHE A 139 7186 6607 4182 82 189 -1338 C ATOM 915 C PHE A 139 -13.350 3.259 -30.603 1.00 45.60 C ANISOU 915 C PHE A 139 7017 6368 3939 130 161 -1315 C ATOM 916 O PHE A 139 -13.735 3.407 -29.444 1.00 45.65 O ANISOU 916 O PHE A 139 7035 6406 3905 134 163 -1317 O ATOM 917 CB PHE A 139 -14.513 1.415 -31.836 1.00 29.22 C ANISOU 917 CB PHE A 139 4932 4313 1857 117 171 -1359 C ATOM 918 CG PHE A 139 -15.892 1.008 -32.255 1.00 32.08 C ANISOU 918 CG PHE A 139 5261 4693 2233 23 221 -1375 C ATOM 919 CD1 PHE A 139 -16.237 0.958 -33.594 1.00 32.19 C ANISOU 919 CD1 PHE A 139 5233 4691 2307 -17 237 -1375 C ATOM 920 CD2 PHE A 139 -16.852 0.696 -31.309 1.00 32.87 C ANISOU 920 CD2 PHE A 139 5374 4814 2302 -42 259 -1379 C ATOM 921 CE1 PHE A 139 -17.509 0.593 -33.983 1.00 28.97 C ANISOU 921 CE1 PHE A 139 4795 4287 1925 -112 284 -1384 C ATOM 922 CE2 PHE A 139 -18.127 0.334 -31.691 1.00 32.71 C ANISOU 922 CE2 PHE A 139 5335 4784 2310 -151 315 -1382 C ATOM 923 CZ PHE A 139 -18.455 0.279 -33.031 1.00 31.80 C ANISOU 923 CZ PHE A 139 5175 4655 2254 -182 324 -1388 C ATOM 924 N ILE A 140 -12.076 3.374 -30.963 1.00 46.24 N ANISOU 924 N ILE A 140 7137 6392 4041 144 147 -1296 N ATOM 925 CA ILE A 140 -11.075 3.848 -30.017 1.00 28.95 C ANISOU 925 CA ILE A 140 4996 4172 1830 130 146 -1283 C ATOM 926 C ILE A 140 -11.430 5.260 -29.565 1.00 28.50 C ANISOU 926 C ILE A 140 4843 4191 1795 95 167 -1301 C ATOM 927 O ILE A 140 -11.501 5.548 -28.364 1.00 29.33 O ANISOU 927 O ILE A 140 4977 4304 1861 100 163 -1295 O ATOM 928 CB ILE A 140 -9.662 3.850 -30.622 1.00 30.73 C ANISOU 928 CB ILE A 140 5221 4372 2082 82 159 -1296 C ATOM 929 CG1 ILE A 140 -9.185 2.421 -30.868 1.00 31.55 C ANISOU 929 CG1 ILE A 140 5433 4397 2157 46 168 -1281 C ATOM 930 CG2 ILE A 140 -8.698 4.563 -29.700 1.00 28.98 C ANISOU 930 CG2 ILE A 140 4969 4192 1849 56 161 -1324 C ATOM 931 CD1 ILE A 140 -7.761 2.330 -31.371 1.00 29.36 C ANISOU 931 CD1 ILE A 140 5085 4163 1905 -5 182 -1336 C ATOM 932 N ALA A 141 -11.663 6.130 -30.543 1.00 27.76 N ANISOU 932 N ALA A 141 4615 4151 1781 58 188 -1314 N ATOM 933 CA ALA A 141 -12.019 7.518 -30.278 1.00 29.92 C ANISOU 933 CA ALA A 141 4743 4503 2122 16 207 -1316 C ATOM 934 C ALA A 141 -13.279 7.624 -29.431 1.00 32.00 C ANISOU 934 C ALA A 141 5008 4792 2360 -16 225 -1309 C ATOM 935 O ALA A 141 -13.351 8.441 -28.521 1.00 30.19 O ANISOU 935 O ALA A 141 4739 4600 2133 -31 230 -1309 O ATOM 936 CB ALA A 141 -12.202 8.271 -31.579 1.00 26.54 C ANISOU 936 CB ALA A 141 4168 4122 1795 -19 226 -1320 C ATOM 937 N LEU A 142 -14.269 6.794 -29.741 1.00 30.63 N ANISOU 937 N LEU A 142 4867 4605 2165 -31 237 -1307 N ATOM 938 CA LEU A 142 -15.533 6.795 -29.014 1.00 31.01 C ANISOU 938 CA LEU A 142 4902 4685 2197 -83 265 -1306 C ATOM 939 C LEU A 142 -15.325 6.372 -27.567 1.00 32.93 C ANISOU 939 C LEU A 142 5254 4914 2344 -29 245 -1306 C ATOM 940 O LEU A 142 -15.808 7.026 -26.639 1.00 31.12 O ANISOU 940 O LEU A 142 4996 4720 2110 -64 263 -1303 O ATOM 941 CB LEU A 142 -16.544 5.866 -29.689 1.00 28.08 C ANISOU 941 CB LEU A 142 4538 4305 1828 -124 288 -1313 C ATOM 942 CG LEU A 142 -17.952 5.901 -29.096 1.00 29.62 C ANISOU 942 CG LEU A 142 4704 4528 2022 -213 334 -1315 C ATOM 943 CD1 LEU A 142 -18.544 7.292 -29.248 1.00 29.32 C ANISOU 943 CD1 LEU A 142 4532 4542 2064 -289 362 -1311 C ATOM 944 CD2 LEU A 142 -18.841 4.856 -29.749 1.00 28.59 C ANISOU 944 CD2 LEU A 142 4593 4378 1891 -263 361 -1327 C ATOM 945 N ASP A 143 -14.601 5.271 -27.390 1.00 32.82 N ANISOU 945 N ASP A 143 5362 4855 2253 63 204 -1313 N ATOM 946 CA ASP A 143 -14.299 4.735 -26.069 1.00 30.07 C ANISOU 946 CA ASP A 143 5091 4507 1829 131 174 -1309 C ATOM 947 C ASP A 143 -13.592 5.771 -25.202 1.00 40.14 C ANISOU 947 C ASP A 143 6384 5765 3101 133 166 -1293 C ATOM 948 O ASP A 143 -13.983 6.011 -24.057 1.00 30.45 O ANISOU 948 O ASP A 143 5171 4569 1829 139 170 -1293 O ATOM 949 CB ASP A 143 -13.437 3.476 -26.195 1.00 41.67 C ANISOU 949 CB ASP A 143 6605 5953 3275 227 121 -1310 C ATOM 950 CG ASP A 143 -13.215 2.783 -24.866 1.00 42.22 C ANISOU 950 CG ASP A 143 6654 6112 3276 300 86 -1341 C ATOM 951 OD1 ASP A 143 -12.271 3.169 -24.143 1.00 42.77 O ANISOU 951 OD1 ASP A 143 6771 6148 3333 376 43 -1319 O ATOM 952 OD2 ASP A 143 -13.982 1.850 -24.548 1.00 41.12 O ANISOU 952 OD2 ASP A 143 6485 6052 3085 239 124 -1383 O ATOM 953 N ARG A 144 -12.555 6.389 -25.759 1.00 39.52 N ANISOU 953 N ARG A 144 6292 5657 3068 108 166 -1290 N ATOM 954 CA ARG A 144 -11.814 7.418 -25.038 1.00 39.80 C ANISOU 954 CA ARG A 144 6304 5712 3106 83 168 -1301 C ATOM 955 C ARG A 144 -12.687 8.633 -24.761 1.00 29.03 C ANISOU 955 C ARG A 144 4804 4432 1795 38 194 -1309 C ATOM 956 O ARG A 144 -12.569 9.271 -23.718 1.00 32.21 O ANISOU 956 O ARG A 144 5201 4860 2177 35 192 -1313 O ATOM 957 CB ARG A 144 -10.571 7.832 -25.824 1.00 29.07 C ANISOU 957 CB ARG A 144 4877 4365 1803 66 164 -1326 C ATOM 958 CG ARG A 144 -9.534 6.731 -25.971 1.00 29.58 C ANISOU 958 CG ARG A 144 5038 4366 1835 62 153 -1325 C ATOM 959 CD ARG A 144 -8.902 6.369 -24.633 1.00 31.15 C ANISOU 959 CD ARG A 144 5315 4555 1965 31 150 -1331 C ATOM 960 NE ARG A 144 -9.660 5.350 -23.911 1.00 31.18 N ANISOU 960 NE ARG A 144 5461 4482 1904 -1 167 -1282 N ATOM 961 CZ ARG A 144 -9.772 5.300 -22.588 1.00 31.88 C ANISOU 961 CZ ARG A 144 5608 4576 1931 -50 182 -1278 C ATOM 962 NH1 ARG A 144 -9.179 6.217 -21.837 1.00 36.67 N ANISOU 962 NH1 ARG A 144 6144 5261 2530 -40 165 -1318 N ATOM 963 NH2 ARG A 144 -10.481 4.337 -22.015 1.00 37.84 N ANISOU 963 NH2 ARG A 144 6478 5269 2631 -125 220 -1241 N ATOM 964 N TRP A 145 -13.570 8.944 -25.703 1.00 29.26 N ANISOU 964 N TRP A 145 4715 4501 1902 -13 222 -1306 N ATOM 965 CA TRP A 145 -14.456 10.090 -25.570 1.00 27.97 C ANISOU 965 CA TRP A 145 4410 4410 1808 -85 254 -1307 C ATOM 966 C TRP A 145 -15.430 9.891 -24.419 1.00 37.30 C ANISOU 966 C TRP A 145 5645 5598 2927 -105 271 -1301 C ATOM 967 O TRP A 145 -15.755 10.835 -23.709 1.00 37.14 O ANISOU 967 O TRP A 145 5558 5625 2928 -141 285 -1304 O ATOM 968 CB TRP A 145 -15.218 10.337 -26.871 1.00 27.32 C ANISOU 968 CB TRP A 145 4214 4354 1812 -146 282 -1306 C ATOM 969 CG TRP A 145 -16.167 11.486 -26.794 1.00 26.88 C ANISOU 969 CG TRP A 145 4023 4365 1825 -225 315 -1308 C ATOM 970 CD1 TRP A 145 -15.853 12.812 -26.827 1.00 26.36 C ANISOU 970 CD1 TRP A 145 3828 4358 1831 -241 315 -1316 C ATOM 971 CD2 TRP A 145 -17.592 11.414 -26.675 1.00 26.95 C ANISOU 971 CD2 TRP A 145 4009 4390 1841 -303 352 -1305 C ATOM 972 NE1 TRP A 145 -16.993 13.572 -26.734 1.00 28.22 N ANISOU 972 NE1 TRP A 145 3969 4641 2112 -317 347 -1317 N ATOM 973 CE2 TRP A 145 -18.076 12.735 -26.640 1.00 28.52 C ANISOU 973 CE2 TRP A 145 4071 4654 2113 -361 371 -1310 C ATOM 974 CE3 TRP A 145 -18.507 10.359 -26.596 1.00 27.42 C ANISOU 974 CE3 TRP A 145 4145 4418 1854 -333 374 -1303 C ATOM 975 CZ2 TRP A 145 -19.431 13.033 -26.528 1.00 28.08 C ANISOU 975 CZ2 TRP A 145 3959 4626 2084 -448 409 -1313 C ATOM 976 CZ3 TRP A 145 -19.852 10.655 -26.485 1.00 27.39 C ANISOU 976 CZ3 TRP A 145 4081 4445 1881 -428 417 -1307 C ATOM 977 CH2 TRP A 145 -20.302 11.980 -26.453 1.00 26.89 C ANISOU 977 CH2 TRP A 145 3887 4442 1889 -484 432 -1311 C ATOM 978 N TYR A 146 -15.897 8.664 -24.230 1.00 36.94 N ANISOU 978 N TYR A 146 5710 5517 2809 -80 271 -1298 N ATOM 979 CA TYR A 146 -16.756 8.384 -23.091 1.00 36.42 C ANISOU 979 CA TYR A 146 5692 5467 2679 -98 290 -1297 C ATOM 980 C TYR A 146 -15.943 8.391 -21.804 1.00 34.55 C ANISOU 980 C TYR A 146 5558 5217 2351 -10 253 -1298 C ATOM 981 O TYR A 146 -16.334 9.020 -20.828 1.00 35.35 O ANISOU 981 O TYR A 146 5643 5351 2438 -35 268 -1297 O ATOM 982 CB TYR A 146 -17.484 7.052 -23.264 1.00 38.92 C ANISOU 982 CB TYR A 146 6070 5768 2951 -108 308 -1302 C ATOM 983 CG TYR A 146 -18.799 7.185 -23.997 1.00 39.87 C ANISOU 983 CG TYR A 146 6100 5902 3146 -235 366 -1301 C ATOM 984 CD1 TYR A 146 -19.950 7.582 -23.328 1.00 40.97 C ANISOU 984 CD1 TYR A 146 6204 6068 3294 -330 416 -1299 C ATOM 985 CD2 TYR A 146 -18.890 6.924 -25.356 1.00 39.32 C ANISOU 985 CD2 TYR A 146 5985 5818 3136 -259 370 -1304 C ATOM 986 CE1 TYR A 146 -21.155 7.712 -23.992 1.00 40.72 C ANISOU 986 CE1 TYR A 146 6095 6047 3330 -444 466 -1304 C ATOM 987 CE2 TYR A 146 -20.090 7.049 -26.029 1.00 39.24 C ANISOU 987 CE2 TYR A 146 5898 5821 3190 -367 418 -1308 C ATOM 988 CZ TYR A 146 -21.219 7.444 -25.342 1.00 40.56 C ANISOU 988 CZ TYR A 146 6031 6014 3366 -460 465 -1310 C ATOM 989 OH TYR A 146 -22.414 7.569 -26.012 1.00 39.66 O ANISOU 989 OH TYR A 146 5840 5912 3315 -565 510 -1320 O ATOM 990 N ALA A 147 -14.801 7.708 -21.817 1.00 33.19 N ANISOU 990 N ALA A 147 5495 4992 2123 88 204 -1299 N ATOM 991 CA ALA A 147 -13.949 7.615 -20.633 1.00 31.47 C ANISOU 991 CA ALA A 147 5367 4739 1851 151 168 -1281 C ATOM 992 C ALA A 147 -13.545 8.982 -20.087 1.00 31.16 C ANISOU 992 C ALA A 147 5289 4719 1831 100 180 -1291 C ATOM 993 O ALA A 147 -13.481 9.182 -18.874 1.00 33.78 O ANISOU 993 O ALA A 147 5674 5050 2110 116 173 -1285 O ATOM 994 CB ALA A 147 -12.709 6.796 -20.948 1.00 31.77 C ANISOU 994 CB ALA A 147 5508 4684 1881 193 132 -1258 C ATOM 995 N ILE A 148 -13.284 9.920 -20.989 1.00 30.27 N ANISOU 995 N ILE A 148 5040 4648 1814 46 194 -1309 N ATOM 996 CA ILE A 148 -12.786 11.236 -20.605 1.00 29.94 C ANISOU 996 CA ILE A 148 4872 4669 1834 17 194 -1326 C ATOM 997 C ILE A 148 -13.915 12.255 -20.445 1.00 29.49 C ANISOU 997 C ILE A 148 4675 4687 1842 -46 228 -1325 C ATOM 998 O ILE A 148 -13.991 12.951 -19.431 1.00 32.36 O ANISOU 998 O ILE A 148 5017 5086 2191 -52 229 -1332 O ATOM 999 CB ILE A 148 -11.757 11.766 -21.637 1.00 40.45 C ANISOU 999 CB ILE A 148 6075 6033 3263 15 182 -1347 C ATOM 1000 CG1 ILE A 148 -10.362 11.193 -21.359 1.00 29.84 C ANISOU 1000 CG1 ILE A 148 4816 4652 1868 55 148 -1366 C ATOM 1001 CG2 ILE A 148 -11.683 13.284 -21.606 1.00 40.60 C ANISOU 1001 CG2 ILE A 148 5899 6147 3382 -10 188 -1367 C ATOM 1002 CD1 ILE A 148 -10.163 9.754 -21.788 1.00 30.25 C ANISOU 1002 CD1 ILE A 148 5032 4614 1849 61 146 -1352 C ATOM 1003 N CYS A 149 -14.800 12.328 -21.435 1.00 28.91 N ANISOU 1003 N CYS A 149 4510 4634 1839 -102 258 -1318 N ATOM 1004 CA CYS A 149 -15.806 13.387 -21.478 1.00 31.00 C ANISOU 1004 CA CYS A 149 4628 4967 2182 -185 294 -1320 C ATOM 1005 C CYS A 149 -17.128 13.012 -20.809 1.00 28.83 C ANISOU 1005 C CYS A 149 4399 4691 1862 -236 329 -1310 C ATOM 1006 O CYS A 149 -17.897 13.891 -20.422 1.00 28.63 O ANISOU 1006 O CYS A 149 4282 4717 1878 -302 356 -1314 O ATOM 1007 CB CYS A 149 -16.061 13.806 -22.927 1.00 27.55 C ANISOU 1007 CB CYS A 149 4060 4557 1852 -232 311 -1322 C ATOM 1008 SG CYS A 149 -14.591 14.408 -23.785 1.00 41.75 S ANISOU 1008 SG CYS A 149 5770 6374 3719 -183 280 -1339 S ATOM 1009 N HIS A 150 -17.401 11.719 -20.674 1.00 29.44 N ANISOU 1009 N HIS A 150 4611 4717 1858 -207 329 -1301 N ATOM 1010 CA HIS A 150 -18.598 11.283 -19.957 1.00 29.99 C ANISOU 1010 CA HIS A 150 4721 4791 1881 -258 367 -1296 C ATOM 1011 C HIS A 150 -18.307 10.087 -19.056 1.00 31.01 C ANISOU 1011 C HIS A 150 5018 4883 1881 -172 346 -1293 C ATOM 1012 O HIS A 150 -18.819 8.994 -19.294 1.00 34.16 O ANISOU 1012 O HIS A 150 5470 5263 2245 -183 364 -1293 O ATOM 1013 CB HIS A 150 -19.718 10.943 -20.942 1.00 38.46 C ANISOU 1013 CB HIS A 150 5734 5865 3013 -353 411 -1296 C ATOM 1014 CG HIS A 150 -20.132 12.094 -21.803 1.00 37.79 C ANISOU 1014 CG HIS A 150 5484 5827 3047 -429 429 -1302 C ATOM 1015 ND1 HIS A 150 -20.765 13.210 -21.300 1.00 36.48 N ANISOU 1015 ND1 HIS A 150 5219 5715 2927 -495 452 -1308 N ATOM 1016 CD2 HIS A 150 -19.998 12.307 -23.135 1.00 37.44 C ANISOU 1016 CD2 HIS A 150 5356 5789 3081 -442 425 -1305 C ATOM 1017 CE1 HIS A 150 -21.005 14.060 -22.283 1.00 35.82 C ANISOU 1017 CE1 HIS A 150 4996 5670 2944 -542 459 -1315 C ATOM 1018 NE2 HIS A 150 -20.549 13.534 -23.407 1.00 36.28 N ANISOU 1018 NE2 HIS A 150 5062 5700 3022 -510 444 -1313 N ATOM 1019 N PRO A 151 -17.482 10.298 -18.015 1.00 31.49 N ANISOU 1019 N PRO A 151 5155 4941 1871 -87 309 -1296 N ATOM 1020 CA PRO A 151 -16.985 9.225 -17.145 1.00 32.53 C ANISOU 1020 CA PRO A 151 5437 5053 1870 30 272 -1300 C ATOM 1021 C PRO A 151 -18.098 8.378 -16.538 1.00 33.29 C ANISOU 1021 C PRO A 151 5558 5182 1907 -13 317 -1301 C ATOM 1022 O PRO A 151 -17.938 7.167 -16.392 1.00 34.00 O ANISOU 1022 O PRO A 151 5710 5287 1922 39 305 -1313 O ATOM 1023 CB PRO A 151 -16.231 9.984 -16.047 1.00 32.84 C ANISOU 1023 CB PRO A 151 5531 5086 1862 86 240 -1301 C ATOM 1024 CG PRO A 151 -15.877 11.291 -16.662 1.00 31.87 C ANISOU 1024 CG PRO A 151 5275 4976 1858 9 250 -1304 C ATOM 1025 CD PRO A 151 -17.024 11.622 -17.560 1.00 31.14 C ANISOU 1025 CD PRO A 151 5038 4926 1869 -100 300 -1301 C ATOM 1026 N LEU A 152 -19.213 9.015 -16.195 1.00 33.16 N ANISOU 1026 N LEU A 152 5484 5185 1932 -129 375 -1293 N ATOM 1027 CA LEU A 152 -20.323 8.327 -15.548 1.00 33.92 C ANISOU 1027 CA LEU A 152 5623 5288 1978 -206 435 -1288 C ATOM 1028 C LEU A 152 -20.957 7.267 -16.445 1.00 39.94 C ANISOU 1028 C LEU A 152 6398 6014 2764 -279 475 -1285 C ATOM 1029 O LEU A 152 -21.398 6.222 -15.965 1.00 39.79 O ANISOU 1029 O LEU A 152 6464 5978 2675 -308 512 -1281 O ATOM 1030 CB LEU A 152 -21.384 9.337 -15.109 1.00 33.69 C ANISOU 1030 CB LEU A 152 5521 5279 2002 -322 488 -1284 C ATOM 1031 CG LEU A 152 -21.010 10.212 -13.913 1.00 33.98 C ANISOU 1031 CG LEU A 152 5567 5350 1994 -269 465 -1286 C ATOM 1032 CD1 LEU A 152 -22.087 11.249 -13.644 1.00 33.64 C ANISOU 1032 CD1 LEU A 152 5427 5335 2020 -394 518 -1287 C ATOM 1033 CD2 LEU A 152 -20.772 9.348 -12.684 1.00 35.23 C ANISOU 1033 CD2 LEU A 152 5853 5521 2012 -187 456 -1285 C ATOM 1034 N LEU A 153 -21.000 7.535 -17.745 1.00 41.26 N ANISOU 1034 N LEU A 153 6484 6164 3028 -317 473 -1287 N ATOM 1035 CA LEU A 153 -21.628 6.618 -18.689 1.00 42.20 C ANISOU 1035 CA LEU A 153 6609 6248 3179 -389 509 -1289 C ATOM 1036 C LEU A 153 -20.623 5.624 -19.259 1.00 43.90 C ANISOU 1036 C LEU A 153 6882 6443 3356 -288 461 -1295 C ATOM 1037 O LEU A 153 -20.970 4.783 -20.088 1.00 44.90 O ANISOU 1037 O LEU A 153 7021 6536 3504 -333 483 -1297 O ATOM 1038 CB LEU A 153 -22.291 7.395 -19.828 1.00 40.71 C ANISOU 1038 CB LEU A 153 6292 6065 3113 -483 533 -1293 C ATOM 1039 CG LEU A 153 -23.268 8.497 -19.417 1.00 38.40 C ANISOU 1039 CG LEU A 153 5907 5808 2874 -585 574 -1296 C ATOM 1040 CD1 LEU A 153 -23.890 9.143 -20.645 1.00 37.21 C ANISOU 1040 CD1 LEU A 153 5621 5677 2841 -668 592 -1307 C ATOM 1041 CD2 LEU A 153 -24.342 7.949 -18.489 1.00 38.73 C ANISOU 1041 CD2 LEU A 153 6017 5835 2864 -670 638 -1296 C ATOM 1042 N PHE A 154 -19.379 5.725 -18.806 1.00 88.35 N ANISOU 1042 N PHE A 154 13607 14146 5817 734 2816 -3260 N ATOM 1043 CA PHE A 154 -18.299 4.917 -19.359 1.00 83.77 C ANISOU 1043 CA PHE A 154 13122 13366 5341 485 2450 -3096 C ATOM 1044 C PHE A 154 -18.446 3.433 -19.037 1.00 91.13 C ANISOU 1044 C PHE A 154 14187 14525 5914 255 2700 -2587 C ATOM 1045 O PHE A 154 -18.155 2.990 -17.925 1.00 96.62 O ANISOU 1045 O PHE A 154 15222 15436 6055 453 2717 -2450 O ATOM 1046 CB PHE A 154 -16.947 5.428 -18.859 1.00 84.81 C ANISOU 1046 CB PHE A 154 13656 13213 5356 640 1920 -3379 C ATOM 1047 CG PHE A 154 -15.780 4.613 -19.330 1.00 80.06 C ANISOU 1047 CG PHE A 154 13165 12451 4802 483 1538 -3156 C ATOM 1048 CD1 PHE A 154 -15.494 4.502 -20.680 1.00 74.04 C ANISOU 1048 CD1 PHE A 154 12084 11445 4604 237 1381 -3097 C ATOM 1049 CD2 PHE A 154 -14.961 3.964 -18.421 1.00 82.79 C ANISOU 1049 CD2 PHE A 154 13888 12881 4687 533 1365 -2948 C ATOM 1050 CE1 PHE A 154 -14.417 3.755 -21.114 1.00 70.85 C ANISOU 1050 CE1 PHE A 154 11829 10849 4242 87 1075 -2855 C ATOM 1051 CE2 PHE A 154 -13.882 3.216 -18.851 1.00 79.57 C ANISOU 1051 CE2 PHE A 154 13361 12536 4336 323 1062 -2758 C ATOM 1052 CZ PHE A 154 -13.610 3.112 -20.198 1.00 73.61 C ANISOU 1052 CZ PHE A 154 12510 11340 4117 176 915 -2649 C ATOM 1053 N LYS A 155 -18.911 2.677 -20.026 1.00 86.19 N ANISOU 1053 N LYS A 155 13293 13823 5634 -184 2907 -2293 N ATOM 1054 CA LYS A 155 -18.936 1.223 -19.955 1.00 87.75 C ANISOU 1054 CA LYS A 155 13669 14003 5669 -526 3122 -1792 C ATOM 1055 C LYS A 155 -18.001 0.661 -21.014 1.00 77.60 C ANISOU 1055 C LYS A 155 12494 12262 4728 -821 2833 -1714 C ATOM 1056 O LYS A 155 -18.132 0.987 -22.194 1.00 76.14 O ANISOU 1056 O LYS A 155 11988 11917 5023 -1016 2751 -1867 O ATOM 1057 CB LYS A 155 -20.347 0.681 -20.169 1.00 90.33 C ANISOU 1057 CB LYS A 155 13661 14550 6109 -842 3633 -1476 C ATOM 1058 CG LYS A 155 -21.358 1.084 -19.119 1.00 96.36 C ANISOU 1058 CG LYS A 155 14320 15786 6507 -521 3987 -1423 C ATOM 1059 CD LYS A 155 -22.701 0.473 -19.457 1.00 97.89 C ANISOU 1059 CD LYS A 155 14120 16175 6899 -886 4433 -1029 C ATOM 1060 CE LYS A 155 -23.737 0.751 -18.392 1.00103.59 C ANISOU 1060 CE LYS A 155 14755 17361 7243 -541 4839 -859 C ATOM 1061 NZ LYS A 155 -25.007 0.067 -18.745 1.00105.80 N ANISOU 1061 NZ LYS A 155 14618 17813 7767 -935 5225 -403 N ATOM 1062 N SER A 156 -17.061 -0.181 -20.602 1.00 78.22 N ANISOU 1062 N SER A 156 13003 12167 4551 -805 2690 -1441 N ATOM 1063 CA SER A 156 -16.080 -0.709 -21.540 1.00 73.71 C ANISOU 1063 CA SER A 156 12597 11138 4271 -969 2401 -1325 C ATOM 1064 C SER A 156 -15.427 -1.991 -21.037 1.00 76.07 C ANISOU 1064 C SER A 156 13366 11256 4279 -999 2473 -830 C ATOM 1065 O SER A 156 -14.289 -1.975 -20.569 1.00 76.16 O ANISOU 1065 O SER A 156 13627 11234 4078 -701 2127 -760 O ATOM 1066 CB SER A 156 -15.009 0.344 -21.825 1.00 75.96 C ANISOU 1066 CB SER A 156 12819 11296 4744 -660 1823 -1676 C ATOM 1067 OG SER A 156 -14.200 -0.028 -22.926 1.00 71.86 O ANISOU 1067 OG SER A 156 12258 10372 4673 -749 1515 -1530 O ATOM 1068 N THR A 157 -16.151 -3.100 -21.138 1.00 78.48 N ANISOU 1068 N THR A 157 13735 11446 4639 -1360 2913 -456 N ATOM 1069 CA THR A 157 -15.603 -4.399 -20.769 1.00 81.20 C ANISOU 1069 CA THR A 157 14493 11510 4849 -1395 3036 71 C ATOM 1070 C THR A 157 -15.047 -5.107 -21.999 1.00 78.80 C ANISOU 1070 C THR A 157 14316 10612 5014 -1621 2904 171 C ATOM 1071 O THR A 157 -15.340 -4.721 -23.131 1.00 74.60 O ANISOU 1071 O THR A 157 13442 9954 4950 -1816 2760 -131 O ATOM 1072 CB THR A 157 -16.659 -5.295 -20.094 1.00 89.13 C ANISOU 1072 CB THR A 157 15479 12644 5743 -1632 3569 478 C ATOM 1073 OG1 THR A 157 -16.068 -6.553 -19.747 1.00 92.31 O ANISOU 1073 OG1 THR A 157 16258 12713 6103 -1626 3684 1013 O ATOM 1074 CG2 THR A 157 -17.833 -5.534 -21.027 1.00 88.55 C ANISOU 1074 CG2 THR A 157 15096 12445 6105 -2182 3861 409 C ATOM 1075 N ALA A 158 -14.243 -6.141 -21.770 1.00 80.86 N ANISOU 1075 N ALA A 158 15022 10536 5165 -1536 2946 613 N ATOM 1076 CA ALA A 158 -13.625 -6.890 -22.859 1.00 78.24 C ANISOU 1076 CA ALA A 158 14854 9610 5265 -1647 2825 724 C ATOM 1077 C ALA A 158 -14.676 -7.591 -23.714 1.00 79.45 C ANISOU 1077 C ALA A 158 14887 9446 5853 -2220 3153 680 C ATOM 1078 O ALA A 158 -14.484 -7.787 -24.916 1.00 74.70 O ANISOU 1078 O ALA A 158 14219 8491 5671 -2371 2986 498 O ATOM 1079 CB ALA A 158 -12.631 -7.900 -22.308 1.00 79.87 C ANISOU 1079 CB ALA A 158 15511 9536 5302 -1371 2857 1253 C ATOM 1080 N ARG A 159 -15.786 -7.964 -23.083 1.00 84.80 N ANISOU 1080 N ARG A 159 15515 10299 6406 -2542 3610 853 N ATOM 1081 CA ARG A 159 -16.887 -8.617 -23.781 1.00 87.12 C ANISOU 1081 CA ARG A 159 15645 10366 7092 -3170 3922 826 C ATOM 1082 C ARG A 159 -17.482 -7.696 -24.842 1.00 82.75 C ANISOU 1082 C ARG A 159 14517 10070 6854 -3357 3693 301 C ATOM 1083 O ARG A 159 -17.863 -8.146 -25.923 1.00 82.27 O ANISOU 1083 O ARG A 159 14328 9736 7193 -3781 3696 142 O ATOM 1084 CB ARG A 159 -17.966 -9.058 -22.787 1.00 91.07 C ANISOU 1084 CB ARG A 159 16009 11126 7466 -3367 4342 1146 C ATOM 1085 CG ARG A 159 -17.502 -10.131 -21.808 1.00 98.66 C ANISOU 1085 CG ARG A 159 17357 11839 8291 -3154 4527 1715 C ATOM 1086 CD ARG A 159 -18.584 -10.492 -20.799 1.00105.38 C ANISOU 1086 CD ARG A 159 17981 13045 9015 -3290 4919 2083 C ATOM 1087 NE ARG A 159 -18.126 -11.503 -19.849 1.00111.12 N ANISOU 1087 NE ARG A 159 19005 13602 9614 -3060 5103 2679 N ATOM 1088 CZ ARG A 159 -18.836 -11.936 -18.811 1.00118.05 C ANISOU 1088 CZ ARG A 159 19727 14809 10318 -3070 5442 3147 C ATOM 1089 NH1 ARG A 159 -20.045 -11.445 -18.580 1.00119.86 N ANISOU 1089 NH1 ARG A 159 19520 15549 10473 -3273 5636 3088 N ATOM 1090 NH2 ARG A 159 -18.335 -12.859 -18.001 1.00123.21 N ANISOU 1090 NH2 ARG A 159 20613 15330 10872 -2849 5586 3715 N ATOM 1091 N ARG A 160 -17.552 -6.404 -24.532 1.00 77.52 N ANISOU 1091 N ARG A 160 13512 9939 6002 -3025 3500 31 N ATOM 1092 CA ARG A 160 -18.048 -5.418 -25.485 1.00 73.48 C ANISOU 1092 CA ARG A 160 12425 9702 5790 -3097 3299 -400 C ATOM 1093 C ARG A 160 -17.119 -5.296 -26.685 1.00 71.50 C ANISOU 1093 C ARG A 160 12152 9132 5883 -2965 2864 -605 C ATOM 1094 O ARG A 160 -17.571 -5.316 -27.828 1.00 66.61 O ANISOU 1094 O ARG A 160 11196 8499 5612 -3263 2812 -808 O ATOM 1095 CB ARG A 160 -18.214 -4.052 -24.818 1.00 72.47 C ANISOU 1095 CB ARG A 160 12015 10110 5412 -2697 3210 -629 C ATOM 1096 CG ARG A 160 -19.403 -3.956 -23.884 1.00 77.48 C ANISOU 1096 CG ARG A 160 12489 11210 5740 -2815 3667 -505 C ATOM 1097 CD ARG A 160 -19.512 -2.565 -23.288 1.00 82.93 C ANISOU 1097 CD ARG A 160 12954 12367 6189 -2357 3577 -813 C ATOM 1098 NE ARG A 160 -20.614 -2.468 -22.335 1.00 88.55 N ANISOU 1098 NE ARG A 160 13472 13520 6651 -2300 3942 -651 N ATOM 1099 CZ ARG A 160 -21.867 -2.180 -22.670 1.00 89.65 C ANISOU 1099 CZ ARG A 160 13081 13968 7013 -2483 4161 -653 C ATOM 1100 NH1 ARG A 160 -22.182 -1.960 -23.939 1.00 86.35 N ANISOU 1100 NH1 ARG A 160 12255 13502 7054 -2763 4046 -829 N ATOM 1101 NH2 ARG A 160 -22.805 -2.113 -21.735 1.00 94.73 N ANISOU 1101 NH2 ARG A 160 13574 15016 7404 -2339 4480 -439 N ATOM 1102 N ALA A 161 -15.823 -5.168 -26.416 1.00 69.59 N ANISOU 1102 N ALA A 161 12234 8701 5507 -2506 2552 -522 N ATOM 1103 CA ALA A 161 -14.821 -5.055 -27.472 1.00 64.87 C ANISOU 1103 CA ALA A 161 11617 7838 5194 -2298 2145 -626 C ATOM 1104 C ALA A 161 -14.829 -6.290 -28.366 1.00 62.81 C ANISOU 1104 C ALA A 161 11592 7093 5180 -2628 2274 -539 C ATOM 1105 O ALA A 161 -15.188 -6.210 -29.541 1.00 60.86 O ANISOU 1105 O ALA A 161 11014 6862 5248 -2847 2181 -796 O ATOM 1106 CB ALA A 161 -13.441 -4.840 -26.874 1.00 60.42 C ANISOU 1106 CB ALA A 161 11371 7191 4395 -1779 1829 -449 C ATOM 1107 N ARG A 162 -14.435 -7.430 -27.807 1.00 78.46 N ANISOU 1107 N ARG A 162 14150 8651 7012 -2649 2497 -182 N ATOM 1108 CA ARG A 162 -14.508 -8.692 -28.535 1.00 80.09 C ANISOU 1108 CA ARG A 162 14677 8290 7465 -2989 2688 -120 C ATOM 1109 C ARG A 162 -15.967 -9.068 -28.760 1.00 81.64 C ANISOU 1109 C ARG A 162 14631 8555 7833 -3675 3024 -268 C ATOM 1110 O ARG A 162 -16.514 -9.935 -28.080 1.00 86.29 O ANISOU 1110 O ARG A 162 15497 8921 8367 -4008 3426 13 O ATOM 1111 CB ARG A 162 -13.774 -9.802 -27.782 1.00 83.67 C ANISOU 1111 CB ARG A 162 15806 8240 7743 -2814 2911 365 C ATOM 1112 CG ARG A 162 -12.267 -9.617 -27.725 1.00 81.55 C ANISOU 1112 CG ARG A 162 15772 7887 7326 -2164 2576 568 C ATOM 1113 CD ARG A 162 -11.614 -10.680 -26.860 1.00 86.09 C ANISOU 1113 CD ARG A 162 16963 8068 7681 -1950 2850 1133 C ATOM 1114 NE ARG A 162 -12.161 -10.683 -25.507 1.00 89.78 N ANISOU 1114 NE ARG A 162 17445 8849 7820 -2009 3126 1398 N ATOM 1115 CZ ARG A 162 -11.708 -11.445 -24.517 1.00 93.68 C ANISOU 1115 CZ ARG A 162 18120 9276 8196 -1709 3249 1838 C ATOM 1116 NH1 ARG A 162 -10.691 -12.270 -24.726 1.00 94.18 N ANISOU 1116 NH1 ARG A 162 18419 8948 8416 -1359 3176 2080 N ATOM 1117 NH2 ARG A 162 -12.270 -11.381 -23.318 1.00 98.31 N ANISOU 1117 NH2 ARG A 162 18597 10257 8498 -1730 3457 2050 N ATOM 1118 N GLY A 163 -16.583 -8.397 -29.726 1.00 78.66 N ANISOU 1118 N GLY A 163 13689 8529 7669 -3879 2857 -660 N ATOM 1119 CA GLY A 163 -17.999 -8.532 -30.007 1.00 81.41 C ANISOU 1119 CA GLY A 163 13646 9129 8158 -4517 3108 -812 C ATOM 1120 C GLY A 163 -18.415 -7.317 -30.809 1.00 76.11 C ANISOU 1120 C GLY A 163 12251 9067 7601 -4443 2850 -1156 C ATOM 1121 O GLY A 163 -19.343 -7.365 -31.616 1.00 76.74 O ANISOU 1121 O GLY A 163 11902 9395 7863 -4912 2900 -1374 O ATOM 1122 N SER A 164 -17.706 -6.218 -30.574 1.00 69.95 N ANISOU 1122 N SER A 164 11322 8536 6722 -3853 2572 -1182 N ATOM 1123 CA SER A 164 -17.862 -5.004 -31.361 1.00 64.67 C ANISOU 1123 CA SER A 164 10001 8351 6221 -3658 2308 -1445 C ATOM 1124 C SER A 164 -16.933 -5.076 -32.565 1.00 60.90 C ANISOU 1124 C SER A 164 9521 7665 5951 -3436 1948 -1572 C ATOM 1125 O SER A 164 -17.276 -4.640 -33.665 1.00 58.81 O ANISOU 1125 O SER A 164 8731 7727 5889 -3509 1804 -1785 O ATOM 1126 CB SER A 164 -17.556 -3.768 -30.516 1.00 57.40 C ANISOU 1126 CB SER A 164 8935 7725 5149 -3154 2191 -1426 C ATOM 1127 OG SER A 164 -17.773 -2.583 -31.252 1.00 55.59 O ANISOU 1127 OG SER A 164 8066 7906 5150 -2968 1993 -1635 O ATOM 1128 N ILE A 165 -15.748 -5.633 -32.331 1.00 60.19 N ANISOU 1128 N ILE A 165 10001 7091 5779 -3124 1823 -1391 N ATOM 1129 CA ILE A 165 -14.781 -5.909 -33.386 1.00 57.61 C ANISOU 1129 CA ILE A 165 9777 6516 5596 -2867 1538 -1438 C ATOM 1130 C ILE A 165 -15.399 -6.820 -34.442 1.00 60.42 C ANISOU 1130 C ILE A 165 10130 6733 6095 -3358 1657 -1679 C ATOM 1131 O ILE A 165 -15.230 -6.609 -35.648 1.00 58.64 O ANISOU 1131 O ILE A 165 9583 6690 6007 -3266 1428 -1887 O ATOM 1132 CB ILE A 165 -13.508 -6.562 -32.810 1.00 53.67 C ANISOU 1132 CB ILE A 165 9948 5505 4939 -2482 1484 -1120 C ATOM 1133 CG1 ILE A 165 -12.814 -5.600 -31.842 1.00 51.26 C ANISOU 1133 CG1 ILE A 165 9598 5413 4465 -2013 1279 -933 C ATOM 1134 CG2 ILE A 165 -12.568 -6.990 -33.923 1.00 52.10 C ANISOU 1134 CG2 ILE A 165 9890 5040 4864 -2203 1260 -1136 C ATOM 1135 CD1 ILE A 165 -11.595 -6.183 -31.164 1.00 52.26 C ANISOU 1135 CD1 ILE A 165 10308 5176 4375 -1634 1220 -560 C ATOM 1136 N LEU A 166 -16.127 -7.828 -33.972 1.00 66.04 N ANISOU 1136 N LEU A 166 11185 7142 6767 -3890 2014 -1649 N ATOM 1137 CA LEU A 166 -16.841 -8.748 -34.847 1.00 69.47 C ANISOU 1137 CA LEU A 166 11646 7405 7347 -4489 2141 -1926 C ATOM 1138 C LEU A 166 -17.860 -8.001 -35.702 1.00 68.41 C ANISOU 1138 C LEU A 166 10696 7989 7307 -4784 2041 -2226 C ATOM 1139 O LEU A 166 -18.065 -8.333 -36.868 1.00 69.09 O ANISOU 1139 O LEU A 166 10547 8229 7474 -4813 1895 -2431 O ATOM 1140 CB LEU A 166 -17.537 -9.835 -34.027 1.00 76.84 C ANISOU 1140 CB LEU A 166 13014 7905 8275 -5058 2563 -1769 C ATOM 1141 CG LEU A 166 -16.666 -10.574 -33.008 1.00 78.74 C ANISOU 1141 CG LEU A 166 14012 7506 8400 -4760 2745 -1358 C ATOM 1142 CD1 LEU A 166 -17.485 -11.602 -32.242 1.00 85.97 C ANISOU 1142 CD1 LEU A 166 15190 8121 9352 -5241 3151 -1142 C ATOM 1143 CD2 LEU A 166 -15.477 -11.231 -33.691 1.00 78.63 C ANISOU 1143 CD2 LEU A 166 14511 6920 8444 -4388 2593 -1387 C ATOM 1144 N GLY A 167 -18.494 -6.992 -35.114 1.00 62.78 N ANISOU 1144 N GLY A 167 9484 7825 6545 -4740 2105 -2124 N ATOM 1145 CA GLY A 167 -19.453 -6.172 -35.831 1.00 61.94 C ANISOU 1145 CA GLY A 167 8553 8468 6513 -4858 2038 -2287 C ATOM 1146 C GLY A 167 -18.770 -5.331 -36.889 1.00 56.87 C ANISOU 1146 C GLY A 167 7498 8134 5978 -4370 1673 -2402 C ATOM 1147 O GLY A 167 -19.296 -5.142 -37.990 1.00 57.11 O ANISOU 1147 O GLY A 167 7023 8621 6054 -4312 1553 -2500 O ATOM 1148 N ILE A 168 -17.588 -4.826 -36.549 1.00 52.76 N ANISOU 1148 N ILE A 168 7205 7382 5458 -3784 1472 -2251 N ATOM 1149 CA ILE A 168 -16.783 -4.054 -37.485 1.00 48.20 C ANISOU 1149 CA ILE A 168 6263 7036 5013 -3257 1117 -2263 C ATOM 1150 C ILE A 168 -16.415 -4.903 -38.694 1.00 54.26 C ANISOU 1150 C ILE A 168 7173 7663 5780 -3330 982 -2461 C ATOM 1151 O ILE A 168 -16.576 -4.470 -39.834 1.00 53.42 O ANISOU 1151 O ILE A 168 6497 8045 5755 -3180 815 -2537 O ATOM 1152 CB ILE A 168 -15.502 -3.516 -36.820 1.00 44.59 C ANISOU 1152 CB ILE A 168 6094 6289 4558 -2630 909 -2004 C ATOM 1153 CG1 ILE A 168 -15.852 -2.404 -35.831 1.00 44.03 C ANISOU 1153 CG1 ILE A 168 5761 6469 4500 -2482 971 -1913 C ATOM 1154 CG2 ILE A 168 -14.525 -3.002 -37.867 1.00 40.76 C ANISOU 1154 CG2 ILE A 168 5319 5938 4230 -2117 546 -1946 C ATOM 1155 CD1 ILE A 168 -14.650 -1.776 -35.169 1.00 41.86 C ANISOU 1155 CD1 ILE A 168 5708 5968 4228 -1936 717 -1720 C ATOM 1156 N TRP A 169 -15.938 -6.118 -38.442 1.00 56.63 N ANISOU 1156 N TRP A 169 8238 7295 5985 -3455 1084 -2471 N ATOM 1157 CA TRP A 169 -15.585 -7.028 -39.527 1.00 58.06 C ANISOU 1157 CA TRP A 169 8633 7260 6167 -3416 993 -2627 C ATOM 1158 C TRP A 169 -16.804 -7.459 -40.335 1.00 58.61 C ANISOU 1158 C TRP A 169 8321 7684 6266 -3875 1081 -2845 C ATOM 1159 O TRP A 169 -16.711 -7.658 -41.542 1.00 59.41 O ANISOU 1159 O TRP A 169 8227 7989 6360 -3767 913 -3028 O ATOM 1160 CB TRP A 169 -14.862 -8.260 -38.983 1.00 57.38 C ANISOU 1160 CB TRP A 169 9466 6323 6011 -3399 1147 -2531 C ATOM 1161 CG TRP A 169 -13.418 -8.013 -38.716 1.00 53.71 C ANISOU 1161 CG TRP A 169 9354 5573 5480 -2734 975 -2264 C ATOM 1162 CD1 TRP A 169 -12.841 -7.763 -37.508 1.00 52.21 C ANISOU 1162 CD1 TRP A 169 9440 5172 5227 -2443 1010 -1881 C ATOM 1163 CD2 TRP A 169 -12.362 -7.975 -39.683 1.00 51.57 C ANISOU 1163 CD2 TRP A 169 9077 5322 5195 -2167 714 -2238 C ATOM 1164 NE1 TRP A 169 -11.488 -7.578 -37.660 1.00 49.34 N ANISOU 1164 NE1 TRP A 169 9225 4690 4831 -1774 768 -1609 N ATOM 1165 CE2 TRP A 169 -11.169 -7.703 -38.987 1.00 50.26 C ANISOU 1165 CE2 TRP A 169 9169 4937 4990 -1577 599 -1794 C ATOM 1166 CE3 TRP A 169 -12.310 -8.149 -41.069 1.00 52.19 C ANISOU 1166 CE3 TRP A 169 8935 5642 5255 -2088 567 -2535 C ATOM 1167 CZ2 TRP A 169 -9.937 -7.599 -39.629 1.00 46.59 C ANISOU 1167 CZ2 TRP A 169 8723 4474 4505 -920 354 -1585 C ATOM 1168 CZ3 TRP A 169 -11.086 -8.045 -41.705 1.00 49.94 C ANISOU 1168 CZ3 TRP A 169 8693 5358 4922 -1388 344 -2344 C ATOM 1169 CH2 TRP A 169 -9.916 -7.773 -40.985 1.00 47.12 C ANISOU 1169 CH2 TRP A 169 8572 4766 4565 -816 246 -1847 C ATOM 1170 N ALA A 170 -17.944 -7.603 -39.667 1.00 43.24 N ANISOU 1170 N ALA A 170 3707 6641 6080 -524 31 -3450 N ATOM 1171 CA ALA A 170 -19.174 -8.004 -40.340 1.00 44.14 C ANISOU 1171 CA ALA A 170 3862 6750 6158 -625 -30 -3431 C ATOM 1172 C ALA A 170 -19.630 -6.930 -41.322 1.00 42.99 C ANISOU 1172 C ALA A 170 3592 6733 6011 -589 52 -3454 C ATOM 1173 O ALA A 170 -19.809 -7.197 -42.515 1.00 43.75 O ANISOU 1173 O ALA A 170 3748 6807 6067 -565 -9 -3480 O ATOM 1174 CB ALA A 170 -20.266 -8.293 -39.322 1.00 44.84 C ANISOU 1174 CB ALA A 170 3952 6858 6228 -829 -51 -3360 C ATOM 1175 N VAL A 171 -19.812 -5.715 -40.812 1.00 42.37 N ANISOU 1175 N VAL A 171 3388 6757 5954 -581 155 -3449 N ATOM 1176 CA VAL A 171 -20.224 -4.592 -41.646 1.00 42.77 C ANISOU 1176 CA VAL A 171 3383 6881 5988 -539 170 -3471 C ATOM 1177 C VAL A 171 -19.200 -4.336 -42.752 1.00 43.49 C ANISOU 1177 C VAL A 171 3540 6963 6023 -493 179 -3480 C ATOM 1178 O VAL A 171 -19.565 -4.057 -43.893 1.00 44.31 O ANISOU 1178 O VAL A 171 3697 7071 6069 -496 133 -3492 O ATOM 1179 CB VAL A 171 -20.421 -3.309 -40.809 1.00 38.80 C ANISOU 1179 CB VAL A 171 2798 6444 5498 -504 222 -3485 C ATOM 1180 CG1 VAL A 171 -20.688 -2.113 -41.710 1.00 39.10 C ANISOU 1180 CG1 VAL A 171 2869 6490 5498 -446 162 -3504 C ATOM 1181 CG2 VAL A 171 -21.559 -3.496 -39.816 1.00 40.06 C ANISOU 1181 CG2 VAL A 171 2842 6705 5673 -553 238 -3532 C ATOM 1182 N SER A 172 -17.920 -4.456 -42.414 1.00 44.28 N ANISOU 1182 N SER A 172 3628 7076 6121 -466 230 -3488 N ATOM 1183 CA SER A 172 -16.854 -4.233 -43.385 1.00 44.10 C ANISOU 1183 CA SER A 172 3607 7138 6012 -457 270 -3536 C ATOM 1184 C SER A 172 -16.855 -5.287 -44.489 1.00 46.06 C ANISOU 1184 C SER A 172 3931 7369 6200 -401 217 -3602 C ATOM 1185 O SER A 172 -16.514 -4.995 -45.635 1.00 47.17 O ANISOU 1185 O SER A 172 4107 7596 6221 -418 252 -3646 O ATOM 1186 CB SER A 172 -15.491 -4.211 -42.691 1.00 44.02 C ANISOU 1186 CB SER A 172 3501 7205 6019 -441 321 -3575 C ATOM 1187 OG SER A 172 -15.439 -3.191 -41.707 1.00 42.99 O ANISOU 1187 OG SER A 172 3353 7063 5917 -499 353 -3513 O ATOM 1188 N LEU A 173 -17.241 -6.510 -44.144 1.00 41.03 N ANISOU 1188 N LEU A 173 3368 6609 5612 -351 120 -3611 N ATOM 1189 CA LEU A 173 -17.289 -7.595 -45.119 1.00 42.46 C ANISOU 1189 CA LEU A 173 3697 6716 5719 -278 21 -3677 C ATOM 1190 C LEU A 173 -18.607 -7.579 -45.884 1.00 48.58 C ANISOU 1190 C LEU A 173 4572 7423 6463 -369 -59 -3634 C ATOM 1191 O LEU A 173 -18.757 -8.273 -46.889 1.00 50.01 O ANISOU 1191 O LEU A 173 4913 7533 6556 -333 -152 -3680 O ATOM 1192 CB LEU A 173 -17.097 -8.950 -44.433 1.00 43.29 C ANISOU 1192 CB LEU A 173 3930 6660 5857 -200 -118 -3706 C ATOM 1193 CG LEU A 173 -15.665 -9.325 -44.030 1.00 44.10 C ANISOU 1193 CG LEU A 173 3978 6811 5969 -26 -116 -3804 C ATOM 1194 CD1 LEU A 173 -15.645 -10.613 -43.218 1.00 45.14 C ANISOU 1194 CD1 LEU A 173 4316 6710 6125 42 -318 -3818 C ATOM 1195 CD2 LEU A 173 -14.779 -9.449 -45.257 1.00 45.83 C ANISOU 1195 CD2 LEU A 173 4167 7176 6070 130 -72 -3934 C ATOM 1196 N ALA A 174 -19.559 -6.781 -45.407 1.00 48.54 N ANISOU 1196 N ALA A 174 4475 7447 6523 -469 -43 -3562 N ATOM 1197 CA ALA A 174 -20.873 -6.707 -46.039 1.00 49.76 C ANISOU 1197 CA ALA A 174 4665 7573 6670 -549 -150 -3534 C ATOM 1198 C ALA A 174 -20.984 -5.565 -47.051 1.00 49.64 C ANISOU 1198 C ALA A 174 4669 7606 6585 -541 -139 -3540 C ATOM 1199 O ALA A 174 -21.511 -5.754 -48.146 1.00 51.82 O ANISOU 1199 O ALA A 174 5070 7827 6792 -567 -249 -3548 O ATOM 1200 CB ALA A 174 -21.954 -6.573 -44.978 1.00 50.15 C ANISOU 1200 CB ALA A 174 4573 7670 6810 -640 -166 -3486 C ATOM 1201 N ILE A 175 -20.491 -4.385 -46.685 1.00 46.91 N ANISOU 1201 N ILE A 175 4253 7332 6237 -528 -44 -3527 N ATOM 1202 CA ILE A 175 -20.687 -3.190 -47.504 1.00 46.44 C ANISOU 1202 CA ILE A 175 4284 7271 6089 -554 -93 -3515 C ATOM 1203 C ILE A 175 -19.654 -3.032 -48.618 1.00 46.06 C ANISOU 1203 C ILE A 175 4377 7263 5859 -609 -33 -3540 C ATOM 1204 O ILE A 175 -19.719 -2.082 -49.399 1.00 43.84 O ANISOU 1204 O ILE A 175 4245 6963 5451 -687 -92 -3520 O ATOM 1205 CB ILE A 175 -20.659 -1.905 -46.646 1.00 46.36 C ANISOU 1205 CB ILE A 175 4221 7280 6114 -537 -77 -3490 C ATOM 1206 CG1 ILE A 175 -19.224 -1.566 -46.235 1.00 41.09 C ANISOU 1206 CG1 ILE A 175 3548 6674 5389 -585 61 -3475 C ATOM 1207 CG2 ILE A 175 -21.564 -2.050 -45.434 1.00 41.13 C ANISOU 1207 CG2 ILE A 175 3379 6652 5596 -475 -88 -3512 C ATOM 1208 CD1 ILE A 175 -19.100 -0.264 -45.474 1.00 40.85 C ANISOU 1208 CD1 ILE A 175 3552 6615 5355 -594 36 -3439 C ATOM 1209 N MET A 176 -18.700 -3.954 -48.690 1.00 45.49 N ANISOU 1209 N MET A 176 4272 7262 5752 -571 68 -3602 N ATOM 1210 CA MET A 176 -17.655 -3.876 -49.707 1.00 46.27 C ANISOU 1210 CA MET A 176 4437 7495 5649 -615 167 -3674 C ATOM 1211 C MET A 176 -17.869 -4.877 -50.834 1.00 46.25 C ANISOU 1211 C MET A 176 4591 7442 5539 -553 107 -3740 C ATOM 1212 O MET A 176 -17.058 -4.961 -51.756 1.00 53.90 O ANISOU 1212 O MET A 176 5618 8553 6309 -562 203 -3824 O ATOM 1213 CB MET A 176 -16.278 -4.092 -49.081 1.00 45.60 C ANISOU 1213 CB MET A 176 4167 7591 5567 -575 320 -3743 C ATOM 1214 CG MET A 176 -15.836 -2.953 -48.191 1.00 44.73 C ANISOU 1214 CG MET A 176 3955 7550 5489 -686 381 -3692 C ATOM 1215 SD MET A 176 -16.049 -1.360 -49.006 1.00 50.90 S ANISOU 1215 SD MET A 176 4941 8334 6065 -922 338 -3623 S ATOM 1216 CE MET A 176 -15.620 -0.245 -47.674 1.00 43.97 C ANISOU 1216 CE MET A 176 4003 7446 5257 -1007 337 -3548 C ATOM 1217 N VAL A 177 -18.963 -5.627 -50.766 1.00 56.11 N ANISOU 1217 N VAL A 177 5915 8511 6892 -508 -55 -3707 N ATOM 1218 CA VAL A 177 -19.278 -6.579 -51.826 1.00 57.95 C ANISOU 1218 CA VAL A 177 6363 8643 7014 -465 -165 -3760 C ATOM 1219 C VAL A 177 -19.599 -5.937 -53.194 1.00 60.66 C ANISOU 1219 C VAL A 177 6911 8971 7164 -566 -217 -3757 C ATOM 1220 O VAL A 177 -19.401 -6.593 -54.220 1.00 63.44 O ANISOU 1220 O VAL A 177 7462 9299 7345 -523 -242 -3831 O ATOM 1221 CB VAL A 177 -20.449 -7.519 -51.416 1.00 59.24 C ANISOU 1221 CB VAL A 177 6580 8616 7313 -472 -367 -3711 C ATOM 1222 CG1 VAL A 177 -20.073 -8.319 -50.175 1.00 59.28 C ANISOU 1222 CG1 VAL A 177 6481 8598 7443 -404 -348 -3718 C ATOM 1223 CG2 VAL A 177 -21.738 -6.750 -51.184 1.00 57.47 C ANISOU 1223 CG2 VAL A 177 6271 8363 7202 -587 -477 -3617 C ATOM 1224 N PRO A 178 -20.076 -4.669 -53.237 1.00 48.38 N ANISOU 1224 N PRO A 178 5362 7410 5612 -687 -263 -3677 N ATOM 1225 CA PRO A 178 -20.220 -4.147 -54.602 1.00 54.12 C ANISOU 1225 CA PRO A 178 6354 8100 6109 -798 -340 -3678 C ATOM 1226 C PRO A 178 -18.886 -3.971 -55.325 1.00 55.35 C ANISOU 1226 C PRO A 178 6569 8472 5988 -867 -127 -3763 C ATOM 1227 O PRO A 178 -18.824 -4.150 -56.543 1.00 56.80 O ANISOU 1227 O PRO A 178 6989 8658 5935 -918 -147 -3808 O ATOM 1228 CB PRO A 178 -20.900 -2.787 -54.392 1.00 49.67 C ANISOU 1228 CB PRO A 178 5820 7457 5598 -890 -479 -3579 C ATOM 1229 CG PRO A 178 -20.609 -2.426 -52.984 1.00 47.86 C ANISOU 1229 CG PRO A 178 5330 7305 5552 -836 -370 -3555 C ATOM 1230 CD PRO A 178 -20.637 -3.722 -52.252 1.00 46.91 C ANISOU 1230 CD PRO A 178 5028 7202 5595 -712 -307 -3594 C ATOM 1231 N GLN A 179 -17.833 -3.632 -54.588 1.00 55.40 N ANISOU 1231 N GLN A 179 6352 8691 6007 -885 75 -3790 N ATOM 1232 CA GLN A 179 -16.529 -3.450 -55.208 1.00 60.49 C ANISOU 1232 CA GLN A 179 6963 9643 6376 -984 304 -3883 C ATOM 1233 C GLN A 179 -15.971 -4.781 -55.689 1.00 61.86 C ANISOU 1233 C GLN A 179 7111 9914 6480 -763 395 -4025 C ATOM 1234 O GLN A 179 -15.367 -4.855 -56.757 1.00 63.94 O ANISOU 1234 O GLN A 179 7469 10371 6455 -808 518 -4108 O ATOM 1235 CB GLN A 179 -15.546 -2.790 -54.249 1.00 63.57 C ANISOU 1235 CB GLN A 179 7088 10260 6804 -1075 470 -3880 C ATOM 1236 CG GLN A 179 -14.226 -2.450 -54.908 1.00 70.25 C ANISOU 1236 CG GLN A 179 7849 11511 7330 -1260 714 -3962 C ATOM 1237 CD GLN A 179 -13.317 -1.662 -54.003 1.00 74.36 C ANISOU 1237 CD GLN A 179 8131 12266 7855 -1431 839 -3944 C ATOM 1238 OE1 GLN A 179 -12.345 -2.193 -53.472 1.00 77.30 O ANISOU 1238 OE1 GLN A 179 8191 12886 8295 -1303 991 -4038 O ATOM 1239 NE2 GLN A 179 -13.626 -0.384 -53.819 1.00 75.00 N ANISOU 1239 NE2 GLN A 179 8391 12237 7869 -1714 724 -3807 N ATOM 1240 N ALA A 180 -16.172 -5.829 -54.895 1.00 55.75 N ANISOU 1240 N ALA A 180 6254 10554 4375 -200 160 -2531 N ATOM 1241 CA ALA A 180 -15.802 -7.173 -55.314 1.00 48.43 C ANISOU 1241 CA ALA A 180 5406 9513 3481 -505 189 -2451 C ATOM 1242 C ALA A 180 -16.566 -7.530 -56.580 1.00 49.72 C ANISOU 1242 C ALA A 180 5395 9918 3579 -533 138 -2501 C ATOM 1243 O ALA A 180 -16.017 -8.138 -57.497 1.00 48.56 O ANISOU 1243 O ALA A 180 5394 9587 3469 -629 110 -2417 O ATOM 1244 CB ALA A 180 -16.087 -8.181 -54.214 1.00 48.98 C ANISOU 1244 CB ALA A 180 5428 9652 3531 -806 292 -2460 C ATOM 1245 N ALA A 181 -17.831 -7.124 -56.626 1.00 54.17 N ANISOU 1245 N ALA A 181 5635 10912 4035 -430 122 -2641 N ATOM 1246 CA ALA A 181 -18.699 -7.420 -57.758 1.00 54.02 C ANISOU 1246 CA ALA A 181 5393 11201 3930 -454 73 -2704 C ATOM 1247 C ALA A 181 -18.223 -6.761 -59.053 1.00 68.66 C ANISOU 1247 C ALA A 181 7383 12888 5816 -200 -41 -2656 C ATOM 1248 O ALA A 181 -18.087 -7.428 -60.078 1.00 68.45 O ANISOU 1248 O ALA A 181 7409 12802 5796 -337 -68 -2604 O ATOM 1249 CB ALA A 181 -20.126 -6.990 -57.448 1.00 57.29 C ANISOU 1249 CB ALA A 181 5399 12162 4206 -341 72 -2872 C ATOM 1250 N VAL A 182 -17.965 -5.457 -59.005 1.00 52.90 N ANISOU 1250 N VAL A 182 5473 10795 3831 160 -106 -2667 N ATOM 1251 CA VAL A 182 -17.648 -4.707 -60.219 1.00 52.52 C ANISOU 1251 CA VAL A 182 5551 10616 3787 419 -220 -2633 C ATOM 1252 C VAL A 182 -16.216 -4.908 -60.711 1.00 57.57 C ANISOU 1252 C VAL A 182 6550 10779 4544 318 -228 -2479 C ATOM 1253 O VAL A 182 -15.873 -4.482 -61.814 1.00 57.98 O ANISOU 1253 O VAL A 182 6725 10702 4602 455 -314 -2437 O ATOM 1254 CB VAL A 182 -17.877 -3.198 -60.022 1.00 56.53 C ANISOU 1254 CB VAL A 182 6085 11151 4242 851 -290 -2691 C ATOM 1255 CG1 VAL A 182 -19.324 -2.928 -59.645 1.00 59.64 C ANISOU 1255 CG1 VAL A 182 6097 12065 4500 1024 -299 -2852 C ATOM 1256 CG2 VAL A 182 -16.929 -2.651 -58.967 1.00 55.58 C ANISOU 1256 CG2 VAL A 182 6236 10682 4198 873 -236 -2623 C ATOM 1257 N MET A 183 -15.381 -5.550 -59.900 1.00 55.30 N ANISOU 1257 N MET A 183 6425 10247 4339 92 -143 -2395 N ATOM 1258 CA MET A 183 -13.999 -5.792 -60.298 1.00 52.38 C ANISOU 1258 CA MET A 183 6360 9477 4065 11 -148 -2254 C ATOM 1259 C MET A 183 -13.921 -6.772 -61.460 1.00 44.95 C ANISOU 1259 C MET A 183 5438 8512 3129 -151 -171 -2206 C ATOM 1260 O MET A 183 -14.403 -7.901 -61.371 1.00 45.58 O ANISOU 1260 O MET A 183 5417 8718 3181 -390 -119 -2221 O ATOM 1261 CB MET A 183 -13.174 -6.311 -59.121 1.00 50.28 C ANISOU 1261 CB MET A 183 6237 9000 3866 -159 -60 -2180 C ATOM 1262 CG MET A 183 -12.648 -5.212 -58.223 1.00 43.37 C ANISOU 1262 CG MET A 183 5486 7982 3013 1 -51 -2169 C ATOM 1263 SD MET A 183 -11.916 -3.874 -59.181 1.00 42.79 S ANISOU 1263 SD MET A 183 5629 7689 2941 246 -144 -2120 S ATOM 1264 CE MET A 183 -11.662 -2.654 -57.900 1.00 44.94 C ANISOU 1264 CE MET A 183 6022 7856 3197 390 -113 -2136 C ATOM 1265 N GLU A 184 -13.316 -6.324 -62.555 1.00 44.10 N ANISOU 1265 N GLU A 184 5481 8231 3043 -34 -246 -2147 N ATOM 1266 CA GLU A 184 -13.167 -7.152 -63.744 1.00 52.29 C ANISOU 1266 CA GLU A 184 6566 9217 4084 -160 -275 -2098 C ATOM 1267 C GLU A 184 -11.750 -7.080 -64.306 1.00 48.57 C ANISOU 1267 C GLU A 184 6377 8393 3685 -147 -294 -1972 C ATOM 1268 O GLU A 184 -11.067 -6.053 -64.201 1.00 40.93 O ANISOU 1268 O GLU A 184 5544 7267 2740 1 -320 -1939 O ATOM 1269 CB GLU A 184 -14.176 -6.741 -64.817 1.00 56.15 C ANISOU 1269 CB GLU A 184 6879 9965 4493 -27 -362 -2177 C ATOM 1270 CG GLU A 184 -15.633 -6.849 -64.388 1.00 60.47 C ANISOU 1270 CG GLU A 184 7090 10943 4942 -34 -347 -2312 C ATOM 1271 CD GLU A 184 -16.041 -8.269 -64.040 1.00 62.22 C ANISOU 1271 CD GLU A 184 7218 11279 5142 -384 -257 -2315 C ATOM 1272 OE1 GLU A 184 -15.575 -9.208 -64.721 1.00 62.93 O ANISOU 1272 OE1 GLU A 184 7460 11194 5257 -573 -247 -2235 O ATOM 1273 OE2 GLU A 184 -16.825 -8.443 -63.082 1.00 62.70 O ANISOU 1273 OE2 GLU A 184 7074 11599 5150 -470 -193 -2399 O ATOM 1274 N CYS A 185 -11.325 -8.188 -64.904 1.00 40.91 N ANISOU 1274 N CYS A 185 5499 7313 2733 -311 -279 -1907 N ATOM 1275 CA CYS A 185 -9.992 -8.314 -65.478 1.00 43.99 C ANISOU 1275 CA CYS A 185 6122 7417 3176 -304 -291 -1796 C ATOM 1276 C CYS A 185 -10.063 -8.301 -67.001 1.00 39.40 C ANISOU 1276 C CYS A 185 5574 6827 2569 -274 -362 -1782 C ATOM 1277 O CYS A 185 -10.368 -9.317 -67.625 1.00 40.52 O ANISOU 1277 O CYS A 185 5704 7005 2687 -400 -359 -1778 O ATOM 1278 CB CYS A 185 -9.323 -9.599 -64.983 1.00 38.35 C ANISOU 1278 CB CYS A 185 5516 6567 2490 -455 -223 -1730 C ATOM 1279 SG CYS A 185 -7.644 -9.871 -65.588 1.00 85.89 S ANISOU 1279 SG CYS A 185 11773 12306 8555 -403 -234 -1609 S ATOM 1280 N SER A 186 -9.787 -7.145 -67.595 1.00 39.29 N ANISOU 1280 N SER A 186 5623 6754 2550 -117 -426 -1773 N ATOM 1281 CA SER A 186 -9.867 -7.001 -69.044 1.00 61.28 C ANISOU 1281 CA SER A 186 8449 9528 5306 -78 -501 -1760 C ATOM 1282 C SER A 186 -8.538 -6.525 -69.612 1.00 55.81 C ANISOU 1282 C SER A 186 7980 8584 4643 -56 -512 -1665 C ATOM 1283 O SER A 186 -7.666 -6.078 -68.875 1.00 53.93 O ANISOU 1283 O SER A 186 7841 8215 4434 -49 -473 -1622 O ATOM 1284 CB SER A 186 -10.989 -6.036 -69.428 1.00 64.18 C ANISOU 1284 CB SER A 186 8670 10111 5607 101 -584 -1852 C ATOM 1285 OG SER A 186 -12.257 -6.575 -69.099 1.00 65.16 O ANISOU 1285 OG SER A 186 8543 10534 5681 56 -574 -1947 O ATOM 1286 N SER A 187 -8.387 -6.620 -70.927 1.00 54.67 N ANISOU 1286 N SER A 187 7905 8390 4476 -65 -563 -1635 N ATOM 1287 CA SER A 187 -7.115 -6.298 -71.558 1.00 50.84 C ANISOU 1287 CA SER A 187 7612 7701 4005 -88 -560 -1548 C ATOM 1288 C SER A 187 -7.280 -5.358 -72.742 1.00 53.02 C ANISOU 1288 C SER A 187 7934 7979 4234 -18 -636 -1552 C ATOM 1289 O SER A 187 -7.161 -4.140 -72.608 1.00 53.13 O ANISOU 1289 O SER A 187 7995 7966 4226 78 -660 -1562 O ATOM 1290 CB SER A 187 -6.417 -7.577 -72.013 1.00 49.54 C ANISOU 1290 CB SER A 187 7530 7434 3861 -177 -529 -1488 C ATOM 1291 OG SER A 187 -7.223 -8.291 -72.935 1.00 49.48 O ANISOU 1291 OG SER A 187 7468 7511 3821 -212 -569 -1519 O ATOM 1292 N VAL A 188 -7.549 -5.939 -73.906 1.00 53.34 N ANISOU 1292 N VAL A 188 7978 8039 4251 -57 -676 -1545 N ATOM 1293 CA VAL A 188 -7.684 -5.170 -75.132 1.00 54.26 C ANISOU 1293 CA VAL A 188 8142 8154 4320 7 -752 -1543 C ATOM 1294 C VAL A 188 -8.993 -4.385 -75.123 1.00 58.54 C ANISOU 1294 C VAL A 188 8563 8870 4810 213 -846 -1630 C ATOM 1295 O VAL A 188 -9.913 -4.702 -74.366 1.00 60.23 O ANISOU 1295 O VAL A 188 8604 9264 5018 257 -843 -1701 O ATOM 1296 CB VAL A 188 -7.619 -6.087 -76.377 1.00 47.67 C ANISOU 1296 CB VAL A 188 7353 7293 3469 -98 -769 -1511 C ATOM 1297 CG1 VAL A 188 -8.962 -6.761 -76.618 1.00 44.26 C ANISOU 1297 CG1 VAL A 188 6768 7047 3002 -79 -823 -1578 C ATOM 1298 CG2 VAL A 188 -7.175 -5.305 -77.606 1.00 50.50 C ANISOU 1298 CG2 VAL A 188 7798 7597 3794 -87 -809 -1480 C ATOM 1299 N LEU A 189 -9.052 -3.349 -75.954 1.00 60.12 N ANISOU 1299 N LEU A 189 8854 9028 4961 353 -927 -1626 N ATOM 1300 CA LEU A 189 -10.238 -2.515 -76.107 1.00 62.93 C ANISOU 1300 CA LEU A 189 9138 9531 5243 619 -1038 -1703 C ATOM 1301 C LEU A 189 -11.462 -3.368 -76.431 1.00 64.18 C ANISOU 1301 C LEU A 189 9059 9961 5365 618 -1080 -1773 C ATOM 1302 O LEU A 189 -11.411 -4.211 -77.324 1.00 63.02 O ANISOU 1302 O LEU A 189 8909 9816 5220 461 -1081 -1743 O ATOM 1303 CB LEU A 189 -9.999 -1.475 -77.208 1.00 66.81 C ANISOU 1303 CB LEU A 189 9824 9882 5679 751 -1126 -1665 C ATOM 1304 CG LEU A 189 -10.708 -0.119 -77.167 1.00 70.93 C ANISOU 1304 CG LEU A 189 10432 10406 6112 1089 -1235 -1711 C ATOM 1305 CD1 LEU A 189 -9.977 0.866 -78.065 1.00 73.06 C ANISOU 1305 CD1 LEU A 189 10997 10420 6344 1128 -1281 -1637 C ATOM 1306 CD2 LEU A 189 -12.160 -0.238 -77.594 1.00 72.89 C ANISOU 1306 CD2 LEU A 189 10475 10938 6282 1303 -1341 -1800 C ATOM 1307 N PRO A 190 -12.566 -3.158 -75.694 1.00 65.66 N ANISOU 1307 N PRO A 190 9038 10400 5509 781 -1107 -1871 N ATOM 1308 CA PRO A 190 -13.811 -3.909 -75.901 1.00 67.28 C ANISOU 1308 CA PRO A 190 8961 10942 5661 755 -1135 -1951 C ATOM 1309 C PRO A 190 -14.354 -3.771 -77.321 1.00 68.02 C ANISOU 1309 C PRO A 190 9041 11123 5681 842 -1248 -1954 C ATOM 1310 O PRO A 190 -13.925 -2.880 -78.055 1.00 65.74 O ANISOU 1310 O PRO A 190 8961 10647 5372 993 -1320 -1909 O ATOM 1311 CB PRO A 190 -14.775 -3.277 -74.892 1.00 69.79 C ANISOU 1311 CB PRO A 190 9074 11520 5922 991 -1153 -2059 C ATOM 1312 CG PRO A 190 -13.895 -2.699 -73.840 1.00 67.71 C ANISOU 1312 CG PRO A 190 8988 11019 5720 1018 -1088 -2023 C ATOM 1313 CD PRO A 190 -12.670 -2.223 -74.560 1.00 65.88 C ANISOU 1313 CD PRO A 190 9076 10429 5526 977 -1099 -1913 C ATOM 1314 N GLU A 191 -15.283 -4.649 -77.692 1.00 69.30 N ANISOU 1314 N GLU A 191 8970 11563 5797 724 -1258 -2004 N ATOM 1315 CA GLU A 191 -15.926 -4.611 -79.004 1.00 70.41 C ANISOU 1315 CA GLU A 191 9057 11837 5858 789 -1365 -2013 C ATOM 1316 C GLU A 191 -14.904 -4.686 -80.137 1.00 66.51 C ANISOU 1316 C GLU A 191 8855 11014 5401 676 -1381 -1905 C ATOM 1317 O GLU A 191 -15.084 -4.081 -81.195 1.00 68.18 O ANISOU 1317 O GLU A 191 9144 11208 5555 825 -1486 -1891 O ATOM 1318 CB GLU A 191 -16.784 -3.348 -79.140 1.00 72.76 C ANISOU 1318 CB GLU A 191 9266 12325 6056 1199 -1490 -2085 C ATOM 1319 CG GLU A 191 -17.773 -3.154 -77.998 1.00 76.16 C ANISOU 1319 CG GLU A 191 9397 13107 6432 1358 -1471 -2202 C ATOM 1320 CD GLU A 191 -18.586 -1.882 -78.130 1.00 81.06 C ANISOU 1320 CD GLU A 191 9959 13906 6935 1830 -1597 -2276 C ATOM 1321 OE1 GLU A 191 -18.495 -1.221 -79.186 1.00 83.50 O ANISOU 1321 OE1 GLU A 191 10453 14076 7198 2019 -1707 -2236 O ATOM 1322 OE2 GLU A 191 -19.317 -1.542 -77.175 1.00 83.61 O ANISOU 1322 OE2 GLU A 191 10065 14502 7201 2027 -1585 -2375 O ATOM 1323 N LEU A 192 -13.831 -5.434 -79.902 1.00 61.06 N ANISOU 1323 N LEU A 192 8325 10076 4797 424 -1275 -1831 N ATOM 1324 CA LEU A 192 -12.772 -5.604 -80.889 1.00 58.49 C ANISOU 1324 CA LEU A 192 8254 9468 4502 297 -1264 -1734 C ATOM 1325 C LEU A 192 -12.592 -7.084 -81.209 1.00 58.35 C ANISOU 1325 C LEU A 192 8256 9412 4502 17 -1200 -1704 C ATOM 1326 O LEU A 192 -12.425 -7.904 -80.307 1.00 58.99 O ANISOU 1326 O LEU A 192 8304 9481 4627 -113 -1107 -1709 O ATOM 1327 CB LEU A 192 -11.461 -5.003 -80.377 1.00 44.97 C ANISOU 1327 CB LEU A 192 6749 7479 2858 299 -1195 -1669 C ATOM 1328 CG LEU A 192 -10.305 -4.838 -81.364 1.00 43.83 C ANISOU 1328 CG LEU A 192 6827 7098 2730 200 -1175 -1580 C ATOM 1329 CD1 LEU A 192 -10.673 -3.850 -82.459 1.00 45.27 C ANISOU 1329 CD1 LEU A 192 7079 7280 2843 380 -1294 -1580 C ATOM 1330 CD2 LEU A 192 -9.049 -4.390 -80.636 1.00 42.31 C ANISOU 1330 CD2 LEU A 192 6752 6723 2601 154 -1080 -1531 C ATOM 1331 N ALA A 193 -12.630 -7.420 -82.495 1.00 46.35 N ANISOU 1331 N ALA A 193 6817 7856 2940 -55 -1252 -1673 N ATOM 1332 CA ALA A 193 -12.535 -8.809 -82.931 1.00 46.01 C ANISOU 1332 CA ALA A 193 6830 7756 2896 -271 -1209 -1651 C ATOM 1333 C ALA A 193 -11.186 -9.424 -82.571 1.00 43.90 C ANISOU 1333 C ALA A 193 6777 7196 2705 -352 -1107 -1583 C ATOM 1334 O ALA A 193 -11.097 -10.615 -82.274 1.00 43.62 O ANISOU 1334 O ALA A 193 6742 7138 2692 -456 -1040 -1590 O ATOM 1335 CB ALA A 193 -12.777 -8.908 -84.430 1.00 46.87 C ANISOU 1335 CB ALA A 193 7009 7860 2938 -299 -1295 -1631 C ATOM 1336 N ASN A 194 -10.141 -8.604 -82.596 1.00 42.77 N ANISOU 1336 N ASN A 194 6790 6868 2593 -301 -1086 -1523 N ATOM 1337 CA ASN A 194 -8.793 -9.067 -82.288 1.00 43.20 C ANISOU 1337 CA ASN A 194 7010 6684 2722 -329 -995 -1457 C ATOM 1338 C ASN A 194 -8.514 -9.055 -80.787 1.00 42.43 C ANISOU 1338 C ASN A 194 6862 6590 2672 -308 -924 -1473 C ATOM 1339 O ASN A 194 -8.272 -8.001 -80.200 1.00 42.23 O ANISOU 1339 O ASN A 194 6804 6580 2661 -279 -900 -1468 O ATOM 1340 CB ASN A 194 -7.760 -8.209 -83.022 1.00 40.24 C ANISOU 1340 CB ASN A 194 6667 6243 2380 -420 -922 -1381 C ATOM 1341 CG ASN A 194 -6.348 -8.741 -82.876 1.00 38.80 C ANISOU 1341 CG ASN A 194 6124 6284 2336 -309 -773 -1468 C ATOM 1342 OD1 ASN A 194 -6.144 -9.904 -82.531 1.00 38.41 O ANISOU 1342 OD1 ASN A 194 6270 6009 2315 -97 -842 -1453 O ATOM 1343 ND2 ASN A 194 -5.365 -7.891 -83.146 1.00 38.28 N ANISOU 1343 ND2 ASN A 194 6162 6117 2265 -306 -761 -1422 N ATOM 1344 N ARG A 195 -8.544 -10.235 -80.176 1.00 39.95 N ANISOU 1344 N ARG A 195 6492 6297 2392 -328 -870 -1498 N ATOM 1345 CA ARG A 195 -8.327 -10.367 -78.739 1.00 39.35 C ANISOU 1345 CA ARG A 195 6356 6229 2365 -333 -792 -1505 C ATOM 1346 C ARG A 195 -6.854 -10.579 -78.404 1.00 37.85 C ANISOU 1346 C ARG A 195 6269 5875 2237 -250 -730 -1454 C ATOM 1347 O ARG A 195 -6.522 -11.102 -77.340 1.00 39.11 O ANISOU 1347 O ARG A 195 6396 6034 2430 -261 -658 -1455 O ATOM 1348 CB ARG A 195 -9.155 -11.526 -78.181 1.00 40.44 C ANISOU 1348 CB ARG A 195 6369 6506 2489 -461 -742 -1554 C ATOM 1349 CG ARG A 195 -10.661 -11.353 -78.307 1.00 42.01 C ANISOU 1349 CG ARG A 195 6374 6964 2623 -532 -793 -1626 C ATOM 1350 CD ARG A 195 -11.228 -10.548 -77.149 1.00 45.19 C ANISOU 1350 CD ARG A 195 6605 7529 3035 -472 -786 -1678 C ATOM 1351 NE ARG A 195 -11.600 -9.191 -77.540 1.00 46.14 N ANISOU 1351 NE ARG A 195 6659 7743 3129 -302 -876 -1705 N ATOM 1352 CZ ARG A 195 -12.094 -8.285 -76.703 1.00 47.23 C ANISOU 1352 CZ ARG A 195 6653 8029 3264 -166 -890 -1762 C ATOM 1353 NH1 ARG A 195 -12.269 -8.588 -75.424 1.00 47.81 N ANISOU 1353 NH1 ARG A 195 6626 8177 3364 -216 -814 -1795 N ATOM 1354 NH2 ARG A 195 -12.408 -7.073 -77.143 1.00 47.95 N ANISOU 1354 NH2 ARG A 195 6716 8184 3318 40 -981 -1787 N ATOM 1355 N THR A 196 -5.973 -10.179 -79.315 1.00 37.34 N ANISOU 1355 N THR A 196 6237 5731 2220 -157 -741 -1408 N ATOM 1356 CA THR A 196 -4.537 -10.309 -79.094 1.00 36.24 C ANISOU 1356 CA THR A 196 6007 5614 2149 -77 -660 -1395 C ATOM 1357 C THR A 196 -4.075 -9.319 -78.033 1.00 35.69 C ANISOU 1357 C THR A 196 5952 5487 2121 -24 -650 -1363 C ATOM 1358 O THR A 196 -4.465 -8.152 -78.049 1.00 36.06 O ANISOU 1358 O THR A 196 6200 5379 2120 -238 -648 -1278 O ATOM 1359 CB THR A 196 -3.738 -10.082 -80.392 1.00 36.11 C ANISOU 1359 CB THR A 196 5908 5681 2131 -99 -633 -1397 C ATOM 1360 OG1 THR A 196 -4.222 -10.961 -81.415 1.00 36.73 O ANISOU 1360 OG1 THR A 196 6045 5752 2157 -147 -656 -1411 O ATOM 1361 CG2 THR A 196 -2.257 -10.345 -80.166 1.00 35.34 C ANISOU 1361 CG2 THR A 196 5813 5568 2045 -110 -544 -1354 C ATOM 1362 N ARG A 197 -3.244 -9.789 -77.110 1.00 34.99 N ANISOU 1362 N ARG A 197 5824 5410 2060 -24 -572 -1350 N ATOM 1363 CA ARG A 197 -2.781 -8.953 -76.013 1.00 40.28 C ANISOU 1363 CA ARG A 197 6517 6028 2758 4 -556 -1319 C ATOM 1364 C ARG A 197 -1.390 -9.355 -75.548 1.00 33.86 C ANISOU 1364 C ARG A 197 5631 5271 1963 20 -476 -1296 C ATOM 1365 O ARG A 197 -0.925 -10.461 -75.822 1.00 33.83 O ANISOU 1365 O ARG A 197 5615 5298 1939 7 -426 -1291 O ATOM 1366 CB ARG A 197 -3.755 -9.037 -74.840 1.00 43.70 C ANISOU 1366 CB ARG A 197 7023 6415 3167 -103 -541 -1324 C ATOM 1367 CG ARG A 197 -3.886 -10.441 -74.277 1.00 48.10 C ANISOU 1367 CG ARG A 197 7530 7032 3715 -119 -493 -1359 C ATOM 1368 CD ARG A 197 -4.863 -10.500 -73.122 1.00 53.68 C ANISOU 1368 CD ARG A 197 8197 7797 4401 -195 -476 -1405 C ATOM 1369 NE ARG A 197 -5.040 -11.862 -72.630 1.00 58.16 N ANISOU 1369 NE ARG A 197 8737 8398 4964 -255 -420 -1422 N ATOM 1370 CZ ARG A 197 -5.911 -12.210 -71.689 1.00 64.10 C ANISOU 1370 CZ ARG A 197 9420 9226 5710 -353 -387 -1460 C ATOM 1371 NH1 ARG A 197 -6.692 -11.293 -71.133 1.00 68.64 N ANISOU 1371 NH1 ARG A 197 9895 9892 6291 -369 -404 -1499 N ATOM 1372 NH2 ARG A 197 -6.002 -13.476 -71.306 1.00 63.86 N ANISOU 1372 NH2 ARG A 197 9415 9193 5656 -438 -331 -1464 N ATOM 1373 N LEU A 198 -0.730 -8.447 -74.839 1.00 33.56 N ANISOU 1373 N LEU A 198 5586 5226 1938 39 -467 -1273 N ATOM 1374 CA LEU A 198 0.529 -8.766 -74.186 1.00 33.16 C ANISOU 1374 CA LEU A 198 5545 5177 1877 46 -406 -1226 C ATOM 1375 C LEU A 198 0.288 -8.939 -72.694 1.00 32.91 C ANISOU 1375 C LEU A 198 5556 5088 1859 30 -378 -1215 C ATOM 1376 O LEU A 198 0.756 -9.900 -72.087 1.00 32.78 O ANISOU 1376 O LEU A 198 5544 5078 1831 43 -325 -1196 O ATOM 1377 CB LEU A 198 1.576 -7.682 -74.442 1.00 33.23 C ANISOU 1377 CB LEU A 198 5542 5227 1858 34 -408 -1203 C ATOM 1378 CG LEU A 198 2.125 -7.601 -75.868 1.00 33.57 C ANISOU 1378 CG LEU A 198 5572 5322 1861 12 -413 -1199 C ATOM 1379 CD1 LEU A 198 1.256 -6.712 -76.748 1.00 34.22 C ANISOU 1379 CD1 LEU A 198 5624 5434 1942 -44 -462 -1247 C ATOM 1380 CD2 LEU A 198 3.565 -7.120 -75.864 1.00 33.81 C ANISOU 1380 CD2 LEU A 198 5652 5370 1824 -7 -388 -1150 C ATOM 1381 N PHE A 199 -0.462 -8.013 -72.108 1.00 33.00 N ANISOU 1381 N PHE A 199 5593 5062 1885 4 -409 -1232 N ATOM 1382 CA PHE A 199 -0.772 -8.084 -70.687 1.00 32.85 C ANISOU 1382 CA PHE A 199 5578 5029 1873 -34 -372 -1240 C ATOM 1383 C PHE A 199 -2.231 -7.731 -70.410 1.00 38.55 C ANISOU 1383 C PHE A 199 6317 5747 2584 -93 -396 -1290 C ATOM 1384 O PHE A 199 -2.885 -7.058 -71.209 1.00 39.37 O ANISOU 1384 O PHE A 199 6459 5838 2663 -130 -437 -1302 O ATOM 1385 CB PHE A 199 0.158 -7.163 -69.890 1.00 32.64 C ANISOU 1385 CB PHE A 199 5537 5018 1846 -22 -359 -1217 C ATOM 1386 CG PHE A 199 0.109 -5.722 -70.319 1.00 39.05 C ANISOU 1386 CG PHE A 199 6347 5839 2650 13 -415 -1237 C ATOM 1387 CD1 PHE A 199 0.915 -5.263 -71.348 1.00 37.38 C ANISOU 1387 CD1 PHE A 199 6078 5713 2413 17 -429 -1240 C ATOM 1388 CD2 PHE A 199 -0.731 -4.823 -69.681 1.00 39.17 C ANISOU 1388 CD2 PHE A 199 6415 5803 2663 20 -441 -1262 C ATOM 1389 CE1 PHE A 199 0.876 -3.938 -71.741 1.00 37.93 C ANISOU 1389 CE1 PHE A 199 6101 5863 2449 -27 -449 -1285 C ATOM 1390 CE2 PHE A 199 -0.774 -3.496 -70.069 1.00 39.16 C ANISOU 1390 CE2 PHE A 199 6153 6072 2653 -11 -433 -1374 C ATOM 1391 CZ PHE A 199 0.030 -3.054 -71.100 1.00 38.66 C ANISOU 1391 CZ PHE A 199 6155 5998 2537 -68 -444 -1345 C ATOM 1392 N SER A 200 -2.734 -8.202 -69.275 1.00 38.43 N ANISOU 1392 N SER A 200 6259 5777 2567 -118 -361 -1327 N ATOM 1393 CA SER A 200 -4.093 -7.904 -68.843 1.00 38.57 C ANISOU 1393 CA SER A 200 6210 5873 2572 -159 -370 -1395 C ATOM 1394 C SER A 200 -4.055 -6.914 -67.686 1.00 39.20 C ANISOU 1394 C SER A 200 6278 5957 2660 -145 -349 -1407 C ATOM 1395 O SER A 200 -3.017 -6.742 -67.048 1.00 38.79 O ANISOU 1395 O SER A 200 6272 5846 2621 -127 -325 -1362 O ATOM 1396 CB SER A 200 -4.821 -9.182 -68.424 1.00 38.72 C ANISOU 1396 CB SER A 200 6146 5970 2598 -213 -336 -1431 C ATOM 1397 OG SER A 200 -4.505 -10.259 -69.289 1.00 38.31 O ANISOU 1397 OG SER A 200 6144 5882 2530 -220 -338 -1409 O ATOM 1398 N VAL A 201 -5.180 -6.259 -67.418 1.00 40.10 N ANISOU 1398 N VAL A 201 6311 6169 2755 -130 -365 -1478 N ATOM 1399 CA VAL A 201 -5.273 -5.349 -66.280 1.00 35.18 C ANISOU 1399 CA VAL A 201 5681 5558 2129 -96 -343 -1505 C ATOM 1400 C VAL A 201 -6.573 -5.543 -65.506 1.00 36.12 C ANISOU 1400 C VAL A 201 5630 5846 2247 -69 -329 -1595 C ATOM 1401 O VAL A 201 -7.574 -6.026 -66.043 1.00 40.42 O ANISOU 1401 O VAL A 201 6051 6532 2772 -69 -354 -1651 O ATOM 1402 CB VAL A 201 -5.168 -3.865 -66.709 1.00 39.17 C ANISOU 1402 CB VAL A 201 6280 6021 2582 -55 -378 -1514 C ATOM 1403 CG1 VAL A 201 -3.821 -3.582 -67.366 1.00 38.37 C ANISOU 1403 CG1 VAL A 201 6318 5790 2469 -150 -369 -1428 C ATOM 1404 CG2 VAL A 201 -6.314 -3.484 -67.632 1.00 40.65 C ANISOU 1404 CG2 VAL A 201 6390 6323 2733 55 -450 -1584 C ATOM 1405 N CYS A 202 -6.540 -5.160 -64.235 1.00 65.29 N ANISOU 1405 N CYS A 202 9312 9545 5950 -56 -287 -1612 N ATOM 1406 CA CYS A 202 -7.696 -5.268 -63.359 1.00 63.74 C ANISOU 1406 CA CYS A 202 8949 9526 5744 -35 -263 -1702 C ATOM 1407 C CYS A 202 -8.264 -3.886 -63.054 1.00 38.26 C ANISOU 1407 C CYS A 202 5713 6355 2468 124 -292 -1770 C ATOM 1408 O CYS A 202 -7.548 -3.013 -62.562 1.00 37.92 O ANISOU 1408 O CYS A 202 5818 6174 2417 147 -280 -1736 O ATOM 1409 CB CYS A 202 -7.311 -5.984 -62.063 1.00 60.01 C ANISOU 1409 CB CYS A 202 8467 9023 5310 -130 -189 -1676 C ATOM 1410 SG CYS A 202 -8.659 -6.187 -60.880 1.00 49.96 S ANISOU 1410 SG CYS A 202 6991 7977 4016 -154 -140 -1784 S ATOM 1411 N ASP A 203 -9.544 -3.682 -63.352 1.00 43.79 N ANISOU 1411 N ASP A 203 6247 7271 3120 243 -334 -1870 N ATOM 1412 CA ASP A 203 -10.181 -2.403 -63.045 1.00 41.33 C ANISOU 1412 CA ASP A 203 5928 7031 2746 469 -374 -1945 C ATOM 1413 C ASP A 203 -11.682 -2.575 -62.833 1.00 46.34 C ANISOU 1413 C ASP A 203 6286 7997 3324 581 -389 -2072 C ATOM 1414 O ASP A 203 -12.197 -3.687 -62.882 1.00 43.40 O ANISOU 1414 O ASP A 203 5732 7797 2961 426 -358 -2098 O ATOM 1415 CB ASP A 203 -9.913 -1.382 -64.155 1.00 51.65 C ANISOU 1415 CB ASP A 203 7403 8213 4007 617 -460 -1920 C ATOM 1416 CG ASP A 203 -9.972 0.051 -63.654 1.00 52.93 C ANISOU 1416 CG ASP A 203 7713 8290 4107 823 -486 -1947 C ATOM 1417 OD1 ASP A 203 -9.749 0.267 -62.443 1.00 52.55 O ANISOU 1417 OD1 ASP A 203 7697 8199 4069 786 -419 -1952 O ATOM 1418 OD2 ASP A 203 -10.242 0.960 -64.468 1.00 54.54 O ANISOU 1418 OD2 ASP A 203 8027 8451 4244 1027 -574 -1959 O ATOM 1419 N GLU A 204 -12.376 -1.467 -62.596 1.00 66.68 N ANISOU 1419 N GLU A 204 9479 9905 5950 1713 -2101 -3846 N ATOM 1420 CA GLU A 204 -13.799 -1.501 -62.281 1.00 69.48 C ANISOU 1420 CA GLU A 204 9304 10593 6504 2186 -2346 -4191 C ATOM 1421 C GLU A 204 -14.665 -1.399 -63.532 1.00 72.63 C ANISOU 1421 C GLU A 204 9954 10770 6872 2477 -2811 -4227 C ATOM 1422 O GLU A 204 -14.387 -0.600 -64.425 1.00 74.75 O ANISOU 1422 O GLU A 204 10900 10503 6997 2540 -3108 -4095 O ATOM 1423 CB GLU A 204 -14.150 -0.370 -61.313 1.00 72.59 C ANISOU 1423 CB GLU A 204 9641 10947 6991 2583 -2503 -4475 C ATOM 1424 CG GLU A 204 -13.268 -0.325 -60.079 1.00 70.03 C ANISOU 1424 CG GLU A 204 9138 10788 6682 2304 -2086 -4427 C ATOM 1425 CD GLU A 204 -13.584 0.850 -59.176 1.00 74.78 C ANISOU 1425 CD GLU A 204 9754 11300 7358 2707 -2274 -4709 C ATOM 1426 OE1 GLU A 204 -14.504 1.627 -59.507 1.00 79.36 O ANISOU 1426 OE1 GLU A 204 10470 11694 7990 3226 -2725 -4952 O ATOM 1427 OE2 GLU A 204 -12.911 0.997 -58.134 1.00 72.16 O ANISOU 1427 OE2 GLU A 204 9301 11081 7034 2512 -1982 -4686 O ATOM 1428 N ARG A 205 -15.718 -2.209 -63.590 1.00 73.13 N ANISOU 1428 N ARG A 205 9454 11257 7076 2640 -2890 -4382 N ATOM 1429 CA ARG A 205 -16.647 -2.157 -64.713 1.00 76.37 C ANISOU 1429 CA ARG A 205 10032 11504 7481 2924 -3346 -4423 C ATOM 1430 C ARG A 205 -18.085 -1.925 -64.250 1.00 80.04 C ANISOU 1430 C ARG A 205 9964 12307 8143 3469 -3653 -4783 C ATOM 1431 O ARG A 205 -18.711 -2.798 -63.646 1.00 79.13 O ANISOU 1431 O ARG A 205 9112 12760 8193 3474 -3501 -4891 O ATOM 1432 CB ARG A 205 -16.548 -3.432 -65.548 1.00 79.76 C ANISOU 1432 CB ARG A 205 10384 12048 7871 2569 -3219 -4204 C ATOM 1433 CG ARG A 205 -15.517 -3.332 -66.667 1.00 80.48 C ANISOU 1433 CG ARG A 205 11232 11650 7698 2256 -3192 -3871 C ATOM 1434 CD ARG A 205 -15.334 -4.654 -67.386 1.00 78.24 C ANISOU 1434 CD ARG A 205 10858 11505 7363 1909 -3016 -3687 C ATOM 1435 NE ARG A 205 -16.607 -5.242 -67.789 1.00 81.10 N ANISOU 1435 NE ARG A 205 10834 12092 7890 2132 -3308 -3836 N ATOM 1436 CZ ARG A 205 -16.741 -6.479 -68.253 1.00 79.94 C ANISOU 1436 CZ ARG A 205 10461 12127 7787 1891 -3216 -3749 C ATOM 1437 NH1 ARG A 205 -15.678 -7.263 -68.370 1.00 77.01 N ANISOU 1437 NH1 ARG A 205 10211 11753 7297 1450 -2830 -3540 N ATOM 1438 NH2 ARG A 205 -17.938 -6.933 -68.597 1.00 82.62 N ANISOU 1438 NH2 ARG A 205 10457 12635 8298 2094 -3513 -3865 N ATOM 1439 N TRP A 206 -18.591 -0.731 -64.547 1.00 84.45 N ANISOU 1439 N TRP A 206 10891 12511 8684 3928 -4095 -4944 N ATOM 1440 CA TRP A 206 -19.934 -0.315 -64.156 1.00 90.57 C ANISOU 1440 CA TRP A 206 11240 13554 9618 4521 -4431 -5299 C ATOM 1441 C TRP A 206 -20.865 -0.207 -65.363 1.00 92.20 C ANISOU 1441 C TRP A 206 11641 13549 9843 4784 -4911 -5273 C ATOM 1442 O TRP A 206 -20.414 -0.222 -66.507 1.00 91.89 O ANISOU 1442 O TRP A 206 12169 13085 9658 4554 -5027 -5009 O ATOM 1443 CB TRP A 206 -19.887 1.035 -63.435 1.00 93.64 C ANISOU 1443 CB TRP A 206 11860 13712 10008 4922 -4586 -5556 C ATOM 1444 CG TRP A 206 -18.966 1.093 -62.252 1.00 90.71 C ANISOU 1444 CG TRP A 206 11362 13476 9628 4674 -4132 -5556 C ATOM 1445 CD1 TRP A 206 -17.637 1.404 -62.260 1.00 88.11 C ANISOU 1445 CD1 TRP A 206 11558 12738 9183 4251 -3900 -5283 C ATOM 1446 CD2 TRP A 206 -19.314 0.859 -60.883 1.00 90.15 C ANISOU 1446 CD2 TRP A 206 10579 14012 9663 4832 -3867 -5816 C ATOM 1447 NE1 TRP A 206 -17.134 1.367 -60.982 1.00 84.35 N ANISOU 1447 NE1 TRP A 206 10751 12547 8751 4116 -3512 -5346 N ATOM 1448 CE2 TRP A 206 -18.145 1.035 -60.118 1.00 85.67 C ANISOU 1448 CE2 TRP A 206 10159 13342 9051 4468 -3475 -5666 C ATOM 1449 CE3 TRP A 206 -20.500 0.511 -60.231 1.00 90.56 C ANISOU 1449 CE3 TRP A 206 9858 14722 9828 5240 -3927 -6135 C ATOM 1450 CZ2 TRP A 206 -18.128 0.875 -58.735 1.00 84.82 C ANISOU 1450 CZ2 TRP A 206 9470 13745 9014 4487 -3142 -5811 C ATOM 1451 CZ3 TRP A 206 -20.482 0.355 -58.858 1.00 89.79 C ANISOU 1451 CZ3 TRP A 206 9172 15167 9775 5289 -3579 -6307 C ATOM 1452 CH2 TRP A 206 -19.304 0.535 -58.125 1.00 86.92 C ANISOU 1452 CH2 TRP A 206 8984 14664 9379 4897 -3193 -6117 C ATOM 1453 N ALA A 207 -22.163 -0.079 -65.097 1.00 99.76 N ANISOU 1453 N ALA A 207 12114 14812 10976 5265 -5161 -5522 N ATOM 1454 CA ALA A 207 -23.154 0.116 -66.153 1.00103.79 C ANISOU 1454 CA ALA A 207 12774 15122 11541 5543 -5601 -5498 C ATOM 1455 C ALA A 207 -23.457 1.601 -66.353 1.00107.75 C ANISOU 1455 C ALA A 207 13757 15173 12011 6071 -6074 -5691 C ATOM 1456 O ALA A 207 -22.860 2.251 -67.211 1.00107.85 O ANISOU 1456 O ALA A 207 14507 14605 11867 5992 -6306 -5527 O ATOM 1457 CB ALA A 207 -24.428 -0.649 -65.836 1.00104.94 C ANISOU 1457 CB ALA A 207 12156 15796 11921 5674 -5518 -5569 C ATOM 1458 N ASP A 208 -24.384 2.133 -65.561 1.00112.79 N ANISOU 1458 N ASP A 208 13983 16067 12804 6595 -6188 -6013 N ATOM 1459 CA ASP A 208 -24.704 3.559 -65.608 1.00117.76 C ANISOU 1459 CA ASP A 208 15026 16281 13436 7149 -6641 -6245 C ATOM 1460 C ASP A 208 -23.615 4.372 -64.916 1.00118.65 C ANISOU 1460 C ASP A 208 15552 16112 13418 7139 -6601 -6369 C ATOM 1461 O ASP A 208 -23.097 3.963 -63.879 1.00115.67 O ANISOU 1461 O ASP A 208 14827 16088 13033 6931 -6157 -6439 O ATOM 1462 CB ASP A 208 -26.061 3.835 -64.954 1.00122.39 C ANISOU 1462 CB ASP A 208 15069 17235 14197 7641 -6667 -6546 C ATOM 1463 CG ASP A 208 -27.206 3.136 -65.664 1.00123.30 C ANISOU 1463 CG ASP A 208 14867 17562 14418 7570 -6703 -6395 C ATOM 1464 OD1 ASP A 208 -27.059 2.816 -66.863 1.00121.97 O ANISOU 1464 OD1 ASP A 208 15044 17093 14205 7338 -6900 -6130 O ATOM 1465 OD2 ASP A 208 -28.254 2.912 -65.023 1.00125.62 O ANISOU 1465 OD2 ASP A 208 14594 18325 14812 7711 -6533 -6513 O ATOM 1466 N ASP A 209 -23.272 5.524 -65.489 1.00 81.85 N ANISOU 1466 N ASP A 209 11988 12349 6764 2626 -3613 -2293 N ATOM 1467 CA ASP A 209 -22.181 6.349 -64.969 1.00 81.26 C ANISOU 1467 CA ASP A 209 11946 12117 6813 2886 -3397 -2242 C ATOM 1468 C ASP A 209 -22.509 6.986 -63.622 1.00 82.14 C ANISOU 1468 C ASP A 209 11813 12222 7175 3098 -3358 -2188 C ATOM 1469 O ASP A 209 -21.651 7.615 -63.001 1.00 78.97 O ANISOU 1469 O ASP A 209 11429 11690 6888 3292 -3180 -2157 O ATOM 1470 CB ASP A 209 -21.809 7.439 -65.976 1.00 82.70 C ANISOU 1470 CB ASP A 209 12238 12326 6858 2954 -3416 -2114 C ATOM 1471 CG ASP A 209 -21.046 6.895 -67.167 1.00 86.04 C ANISOU 1471 CG ASP A 209 12944 12703 7042 2793 -3359 -2178 C ATOM 1472 OD1 ASP A 209 -20.404 5.833 -67.029 1.00 86.30 O ANISOU 1472 OD1 ASP A 209 13114 12612 7065 2707 -3213 -2317 O ATOM 1473 OD2 ASP A 209 -21.086 7.532 -68.240 1.00 88.15 O ANISOU 1473 OD2 ASP A 209 13301 13058 7132 2753 -3449 -2086 O ATOM 1474 N LEU A 210 -23.750 6.827 -63.177 1.00 86.10 N ANISOU 1474 N LEU A 210 12087 12873 7752 3047 -3521 -2173 N ATOM 1475 CA LEU A 210 -24.132 7.266 -61.845 1.00 87.29 C ANISOU 1475 CA LEU A 210 12007 13027 8131 3223 -3467 -2146 C ATOM 1476 C LEU A 210 -23.535 6.333 -60.799 1.00 87.81 C ANISOU 1476 C LEU A 210 12085 12961 8320 3219 -3303 -2282 C ATOM 1477 O LEU A 210 -23.080 6.782 -59.751 1.00 89.09 O ANISOU 1477 O LEU A 210 12184 13033 8635 3395 -3151 -2275 O ATOM 1478 CB LEU A 210 -25.654 7.322 -61.705 1.00 87.81 C ANISOU 1478 CB LEU A 210 11805 13312 8249 3161 -3684 -2067 C ATOM 1479 CG LEU A 210 -26.361 8.419 -62.504 1.00 87.66 C ANISOU 1479 CG LEU A 210 11703 13439 8163 3210 -3846 -1879 C ATOM 1480 CD1 LEU A 210 -27.864 8.370 -62.278 1.00 89.09 C ANISOU 1480 CD1 LEU A 210 11578 13844 8427 3143 -4052 -1771 C ATOM 1481 CD2 LEU A 210 -25.806 9.787 -62.135 1.00 85.32 C ANISOU 1481 CD2 LEU A 210 11428 13035 7956 3482 -3694 -1790 C ATOM 1482 N TYR A 211 -23.527 5.037 -61.099 1.00 87.10 N ANISOU 1482 N TYR A 211 12090 12854 8150 3003 -3335 -2402 N ATOM 1483 CA TYR A 211 -23.040 4.024 -60.162 1.00 83.60 C ANISOU 1483 CA TYR A 211 11656 12289 7820 2970 -3197 -2522 C ATOM 1484 C TYR A 211 -21.600 4.247 -59.659 1.00 62.76 C ANISOU 1484 C TYR A 211 9136 9455 5257 3131 -2948 -2513 C ATOM 1485 O TYR A 211 -21.371 4.210 -58.450 1.00 61.97 O ANISOU 1485 O TYR A 211 8920 9303 5324 3231 -2842 -2522 O ATOM 1486 CB TYR A 211 -23.150 2.626 -60.785 1.00 84.36 C ANISOU 1486 CB TYR A 211 11904 12364 7785 2696 -3253 -2656 C ATOM 1487 CG TYR A 211 -24.565 2.118 -60.963 1.00 86.20 C ANISOU 1487 CG TYR A 211 11988 12785 7978 2487 -3500 -2676 C ATOM 1488 CD1 TYR A 211 -25.405 1.942 -59.869 1.00 86.55 C ANISOU 1488 CD1 TYR A 211 11762 12925 8200 2502 -3563 -2671 C ATOM 1489 CD2 TYR A 211 -25.051 1.789 -62.222 1.00 87.75 C ANISOU 1489 CD2 TYR A 211 12312 13078 7953 2255 -3670 -2688 C ATOM 1490 CE1 TYR A 211 -26.696 1.470 -60.028 1.00 89.48 C ANISOU 1490 CE1 TYR A 211 11968 13483 8545 2295 -3795 -2660 C ATOM 1491 CE2 TYR A 211 -26.339 1.316 -62.390 1.00 90.79 C ANISOU 1491 CE2 TYR A 211 12550 13652 8296 2032 -3913 -2681 C ATOM 1492 CZ TYR A 211 -27.156 1.158 -61.291 1.00 92.29 C ANISOU 1492 CZ TYR A 211 12449 13935 8683 2055 -3977 -2659 C ATOM 1493 OH TYR A 211 -28.439 0.687 -61.456 1.00 97.70 O ANISOU 1493 OH TYR A 211 12961 14822 9338 1820 -4224 -2624 O ATOM 1494 N PRO A 212 -20.625 4.474 -60.566 1.00 66.54 N ANISOU 1494 N PRO A 212 9834 9840 5610 3141 -2857 -2481 N ATOM 1495 CA PRO A 212 -19.267 4.644 -60.032 1.00 64.15 C ANISOU 1495 CA PRO A 212 9608 9374 5394 3271 -2633 -2439 C ATOM 1496 C PRO A 212 -19.097 5.930 -59.228 1.00 62.03 C ANISOU 1496 C PRO A 212 9214 9100 5254 3491 -2580 -2329 C ATOM 1497 O PRO A 212 -18.417 5.922 -58.199 1.00 60.28 O ANISOU 1497 O PRO A 212 8945 8792 5167 3574 -2441 -2304 O ATOM 1498 CB PRO A 212 -18.396 4.673 -61.292 1.00 61.18 C ANISOU 1498 CB PRO A 212 9474 8932 4839 3223 -2567 -2416 C ATOM 1499 CG PRO A 212 -19.302 5.153 -62.362 1.00 66.15 C ANISOU 1499 CG PRO A 212 10123 9705 5308 3151 -2763 -2397 C ATOM 1500 CD PRO A 212 -20.641 4.565 -62.039 1.00 68.33 C ANISOU 1500 CD PRO A 212 10239 10110 5613 3026 -2943 -2469 C ATOM 1501 N LYS A 213 -19.708 7.015 -59.695 1.00 63.62 N ANISOU 1501 N LYS A 213 9374 9393 5405 3569 -2688 -2258 N ATOM 1502 CA LYS A 213 -19.649 8.292 -58.994 1.00 62.81 C ANISOU 1502 CA LYS A 213 9189 9273 5403 3764 -2631 -2174 C ATOM 1503 C LYS A 213 -20.237 8.164 -57.595 1.00 63.71 C ANISOU 1503 C LYS A 213 9105 9420 5682 3817 -2611 -2221 C ATOM 1504 O LYS A 213 -19.607 8.545 -56.605 1.00 60.51 O ANISOU 1504 O LYS A 213 8684 8926 5381 3923 -2469 -2203 O ATOM 1505 CB LYS A 213 -20.394 9.372 -59.782 1.00 65.26 C ANISOU 1505 CB LYS A 213 9483 9686 5626 3814 -2766 -2089 C ATOM 1506 CG LYS A 213 -19.811 9.645 -61.157 1.00 65.89 C ANISOU 1506 CG LYS A 213 9759 9746 5530 3766 -2786 -2031 C ATOM 1507 CD LYS A 213 -20.525 10.797 -61.840 1.00 63.15 C ANISOU 1507 CD LYS A 213 9380 9502 5111 3824 -2920 -1918 C ATOM 1508 CE LYS A 213 -19.852 11.157 -63.153 1.00 79.87 C ANISOU 1508 CE LYS A 213 11697 11598 7049 3781 -2927 -1850 C ATOM 1509 NZ LYS A 213 -20.551 12.274 -63.846 1.00 82.14 N ANISOU 1509 NZ LYS A 213 11950 11992 7267 3829 -3070 -1717 N ATOM 1510 N ILE A 214 -21.445 7.614 -57.527 1.00 66.44 N ANISOU 1510 N ILE A 214 9300 9905 6039 3724 -2758 -2273 N ATOM 1511 CA ILE A 214 -22.135 7.398 -56.262 1.00 67.86 C ANISOU 1511 CA ILE A 214 9274 10147 6364 3750 -2752 -2318 C ATOM 1512 C ILE A 214 -21.326 6.510 -55.325 1.00 66.68 C ANISOU 1512 C ILE A 214 9141 9889 6306 3719 -2611 -2387 C ATOM 1513 O ILE A 214 -21.094 6.871 -54.170 1.00 67.53 O ANISOU 1513 O ILE A 214 9175 9961 6521 3819 -2499 -2383 O ATOM 1514 CB ILE A 214 -23.524 6.764 -56.479 1.00 60.16 C ANISOU 1514 CB ILE A 214 8123 9352 5382 3610 -2951 -2343 C ATOM 1515 CG1 ILE A 214 -24.482 7.783 -57.099 1.00 72.56 C ANISOU 1515 CG1 ILE A 214 9597 11062 6912 3667 -3092 -2221 C ATOM 1516 CG2 ILE A 214 -24.091 6.249 -55.164 1.00 59.41 C ANISOU 1516 CG2 ILE A 214 7820 9313 5439 3598 -2926 -2397 C ATOM 1517 CD1 ILE A 214 -25.897 7.273 -57.254 1.00 75.67 C ANISOU 1517 CD1 ILE A 214 9769 11661 7322 3529 -3299 -2193 C ATOM 1518 N TYR A 215 -20.889 5.357 -55.823 1.00 66.96 N ANISOU 1518 N TYR A 215 9285 9870 6288 3566 -2612 -2445 N ATOM 1519 CA TYR A 215 -20.179 4.407 -54.974 1.00 63.79 C ANISOU 1519 CA TYR A 215 8890 9371 5977 3514 -2488 -2489 C ATOM 1520 C TYR A 215 -18.853 4.953 -54.465 1.00 62.37 C ANISOU 1520 C TYR A 215 8782 9064 5852 3629 -2312 -2385 C ATOM 1521 O TYR A 215 -18.489 4.710 -53.321 1.00 58.24 O ANISOU 1521 O TYR A 215 8176 8511 5442 3643 -2224 -2368 O ATOM 1522 CB TYR A 215 -19.918 3.085 -55.698 1.00 66.14 C ANISOU 1522 CB TYR A 215 9333 9607 6189 3321 -2495 -2573 C ATOM 1523 CG TYR A 215 -19.050 2.161 -54.872 1.00 53.70 C ANISOU 1523 CG TYR A 215 7784 7910 4708 3274 -2340 -2592 C ATOM 1524 CD1 TYR A 215 -19.586 1.440 -53.814 1.00 53.33 C ANISOU 1524 CD1 TYR A 215 7587 7899 4776 3216 -2356 -2667 C ATOM 1525 CD2 TYR A 215 -17.689 2.035 -55.127 1.00 52.67 C ANISOU 1525 CD2 TYR A 215 7816 7641 4554 3285 -2175 -2518 C ATOM 1526 CE1 TYR A 215 -18.799 0.608 -53.044 1.00 53.08 C ANISOU 1526 CE1 TYR A 215 7579 7758 4833 3168 -2213 -2670 C ATOM 1527 CE2 TYR A 215 -16.893 1.205 -54.360 1.00 51.39 C ANISOU 1527 CE2 TYR A 215 7667 7378 4483 3235 -2027 -2507 C ATOM 1528 CZ TYR A 215 -17.454 0.493 -53.320 1.00 51.06 C ANISOU 1528 CZ TYR A 215 7484 7362 4554 3177 -2046 -2583 C ATOM 1529 OH TYR A 215 -16.669 -0.337 -52.553 1.00 49.96 O ANISOU 1529 OH TYR A 215 7359 7118 4507 3125 -1895 -2564 O ATOM 1530 N HIS A 216 -18.119 5.667 -55.311 1.00 62.75 N ANISOU 1530 N HIS A 216 8978 9051 5812 3687 -2272 -2298 N ATOM 1531 CA HIS A 216 -16.807 6.158 -54.904 1.00 62.14 C ANISOU 1531 CA HIS A 216 8965 8869 5775 3757 -2125 -2169 C ATOM 1532 C HIS A 216 -16.917 7.378 -53.998 1.00 61.07 C ANISOU 1532 C HIS A 216 8739 8743 5721 3909 -2099 -2109 C ATOM 1533 O HIS A 216 -16.105 7.554 -53.085 1.00 60.09 O ANISOU 1533 O HIS A 216 8592 8572 5668 3919 -2010 -2009 O ATOM 1534 CB HIS A 216 -15.949 6.475 -56.125 1.00 50.41 C ANISOU 1534 CB HIS A 216 7672 7321 4162 3754 -2086 -2099 C ATOM 1535 CG HIS A 216 -15.234 5.281 -56.677 1.00 53.60 C ANISOU 1535 CG HIS A 216 8205 7660 4500 3616 -2009 -2129 C ATOM 1536 ND1 HIS A 216 -14.013 4.859 -56.197 1.00 49.44 N ANISOU 1536 ND1 HIS A 216 7718 7049 4016 3587 -1854 -2046 N ATOM 1537 CD2 HIS A 216 -15.569 4.418 -57.665 1.00 55.50 C ANISOU 1537 CD2 HIS A 216 8560 7905 4625 3492 -2052 -2237 C ATOM 1538 CE1 HIS A 216 -13.625 3.788 -56.866 1.00 50.54 C ANISOU 1538 CE1 HIS A 216 7993 7128 4083 3477 -1782 -2112 C ATOM 1539 NE2 HIS A 216 -14.552 3.500 -57.763 1.00 55.14 N ANISOU 1539 NE2 HIS A 216 8633 7754 4563 3413 -1899 -2235 N ATOM 1540 N SER A 217 -17.921 8.214 -54.242 1.00 62.47 N ANISOU 1540 N SER A 217 8880 8990 5866 3996 -2176 -2162 N ATOM 1541 CA SER A 217 -18.185 9.334 -53.348 1.00 54.53 C ANISOU 1541 CA SER A 217 7828 7985 4904 4115 -2118 -2159 C ATOM 1542 C SER A 217 -18.583 8.804 -51.974 1.00 55.64 C ANISOU 1542 C SER A 217 7814 8180 5147 4004 -2074 -2183 C ATOM 1543 O SER A 217 -18.120 9.300 -50.946 1.00 51.75 O ANISOU 1543 O SER A 217 7313 7651 4697 3896 -1959 -2078 O ATOM 1544 CB SER A 217 -19.277 10.244 -53.914 1.00 62.67 C ANISOU 1544 CB SER A 217 8854 9109 5848 4175 -2215 -2190 C ATOM 1545 OG SER A 217 -20.461 9.517 -54.191 1.00 63.57 O ANISOU 1545 OG SER A 217 8825 9365 5966 4094 -2364 -2243 O ATOM 1546 N CYS A 218 -19.427 7.777 -51.965 1.00 49.23 N ANISOU 1546 N CYS A 218 6884 7457 4364 4008 -2176 -2316 N ATOM 1547 CA CYS A 218 -19.861 7.158 -50.718 1.00 52.48 C ANISOU 1547 CA CYS A 218 7142 7930 4869 3946 -2148 -2376 C ATOM 1548 C CYS A 218 -18.729 6.384 -50.047 1.00 50.23 C ANISOU 1548 C CYS A 218 6862 7566 4655 3800 -2060 -2261 C ATOM 1549 O CYS A 218 -18.728 6.210 -48.832 1.00 49.42 O ANISOU 1549 O CYS A 218 6666 7495 4616 3699 -2001 -2226 O ATOM 1550 CB CYS A 218 -21.057 6.236 -50.965 1.00 54.99 C ANISOU 1550 CB CYS A 218 7319 8380 5196 3849 -2295 -2471 C ATOM 1551 SG CYS A 218 -22.603 7.105 -51.323 1.00 91.04 S ANISOU 1551 SG CYS A 218 11747 13114 9730 3887 -2429 -2449 S ATOM 1552 N PHE A 219 -17.766 5.923 -50.839 1.00 46.48 N ANISOU 1552 N PHE A 219 6508 7011 4143 3808 -2067 -2208 N ATOM 1553 CA PHE A 219 -16.610 5.218 -50.300 1.00 44.99 C ANISOU 1553 CA PHE A 219 6360 6761 3974 3671 -1972 -2108 C ATOM 1554 C PHE A 219 -15.711 6.213 -49.588 1.00 43.38 C ANISOU 1554 C PHE A 219 6200 6523 3760 3609 -1863 -1935 C ATOM 1555 O PHE A 219 -15.240 5.958 -48.477 1.00 42.13 O ANISOU 1555 O PHE A 219 5998 6372 3637 3509 -1794 -1880 O ATOM 1556 CB PHE A 219 -15.837 4.490 -51.405 1.00 45.56 C ANISOU 1556 CB PHE A 219 6599 6739 3974 3587 -1919 -2104 C ATOM 1557 CG PHE A 219 -14.667 3.686 -50.902 1.00 44.80 C ANISOU 1557 CG PHE A 219 6553 6564 3905 3466 -1775 -2028 C ATOM 1558 CD1 PHE A 219 -14.829 2.361 -50.529 1.00 44.71 C ANISOU 1558 CD1 PHE A 219 6513 6521 3954 3357 -1732 -2124 C ATOM 1559 CD2 PHE A 219 -13.407 4.254 -50.803 1.00 43.56 C ANISOU 1559 CD2 PHE A 219 6477 6360 3713 3465 -1674 -1868 C ATOM 1560 CE1 PHE A 219 -13.756 1.621 -50.066 1.00 43.88 C ANISOU 1560 CE1 PHE A 219 6455 6327 3890 3272 -1575 -2056 C ATOM 1561 CE2 PHE A 219 -12.332 3.518 -50.339 1.00 42.39 C ANISOU 1561 CE2 PHE A 219 6366 6149 3593 3371 -1527 -1802 C ATOM 1562 CZ PHE A 219 -12.507 2.200 -49.971 1.00 42.75 C ANISOU 1562 CZ PHE A 219 6377 6151 3713 3285 -1470 -1893 C ATOM 1563 N PHE A 220 -15.479 7.350 -50.239 1.00 46.49 N ANISOU 1563 N PHE A 220 6692 6874 4097 3655 -1843 -1864 N ATOM 1564 CA PHE A 220 -14.701 8.423 -49.636 1.00 44.54 C ANISOU 1564 CA PHE A 220 6506 6586 3832 3583 -1746 -1722 C ATOM 1565 C PHE A 220 -15.371 8.926 -48.365 1.00 44.77 C ANISOU 1565 C PHE A 220 6447 6677 3888 3530 -1736 -1735 C ATOM 1566 O PHE A 220 -14.706 9.165 -47.360 1.00 44.14 O ANISOU 1566 O PHE A 220 6377 6578 3815 3449 -1658 -1658 O ATOM 1567 CB PHE A 220 -14.512 9.582 -50.616 1.00 45.21 C ANISOU 1567 CB PHE A 220 6711 6614 3854 3664 -1743 -1673 C ATOM 1568 CG PHE A 220 -13.883 10.797 -49.994 1.00 42.25 C ANISOU 1568 CG PHE A 220 6403 6194 3457 3610 -1668 -1553 C ATOM 1569 CD1 PHE A 220 -12.514 10.859 -49.799 1.00 42.23 C ANISOU 1569 CD1 PHE A 220 6477 6129 3439 3542 -1576 -1439 C ATOM 1570 CD2 PHE A 220 -14.662 11.873 -49.598 1.00 42.83 C ANISOU 1570 CD2 PHE A 220 6480 6298 3496 3641 -1701 -1568 C ATOM 1571 CE1 PHE A 220 -11.931 11.972 -49.222 1.00 40.57 C ANISOU 1571 CE1 PHE A 220 6337 5867 3209 3508 -1517 -1349 C ATOM 1572 CE2 PHE A 220 -14.085 12.989 -49.020 1.00 42.31 C ANISOU 1572 CE2 PHE A 220 6511 6180 3384 3608 -1645 -1483 C ATOM 1573 CZ PHE A 220 -12.717 13.038 -48.833 1.00 41.16 C ANISOU 1573 CZ PHE A 220 6429 5953 3258 3544 -1555 -1371 C ATOM 1574 N ILE A 221 -16.689 9.088 -48.415 1.00 43.32 N ANISOU 1574 N ILE A 221 6185 6576 3699 3597 -1816 -1848 N ATOM 1575 CA ILE A 221 -17.432 9.557 -47.252 1.00 43.35 C ANISOU 1575 CA ILE A 221 6126 6656 3691 3583 -1803 -1898 C ATOM 1576 C ILE A 221 -17.337 8.565 -46.096 1.00 42.41 C ANISOU 1576 C ILE A 221 5888 6573 3651 3495 -1768 -1917 C ATOM 1577 O ILE A 221 -16.893 8.916 -45.003 1.00 41.45 O ANISOU 1577 O ILE A 221 5770 6442 3536 3443 -1700 -1851 O ATOM 1578 CB ILE A 221 -18.915 9.806 -47.588 1.00 45.23 C ANISOU 1578 CB ILE A 221 6304 6993 3887 3710 -1880 -2062 C ATOM 1579 CG1 ILE A 221 -19.059 11.061 -48.450 1.00 48.11 C ANISOU 1579 CG1 ILE A 221 6797 7325 4160 3834 -1896 -2050 C ATOM 1580 CG2 ILE A 221 -19.733 9.957 -46.315 1.00 45.44 C ANISOU 1580 CG2 ILE A 221 6212 7123 3931 3736 -1876 -2117 C ATOM 1581 CD1 ILE A 221 -20.482 11.355 -48.869 1.00 48.43 C ANISOU 1581 CD1 ILE A 221 6766 7483 4154 4026 -1998 -2195 C ATOM 1582 N VAL A 222 -17.737 7.323 -46.351 1.00 42.85 N ANISOU 1582 N VAL A 222 5847 6669 3763 3492 -1822 -2014 N ATOM 1583 CA VAL A 222 -17.822 6.312 -45.302 1.00 42.28 C ANISOU 1583 CA VAL A 222 5655 6647 3763 3422 -1802 -2063 C ATOM 1584 C VAL A 222 -16.460 5.919 -44.727 1.00 45.68 C ANISOU 1584 C VAL A 222 6141 7006 4209 3334 -1714 -1946 C ATOM 1585 O VAL A 222 -16.308 5.828 -43.512 1.00 39.95 O ANISOU 1585 O VAL A 222 5359 6296 3526 3258 -1634 -1921 O ATOM 1586 CB VAL A 222 -18.536 5.041 -45.814 1.00 43.39 C ANISOU 1586 CB VAL A 222 5691 6832 3963 3455 -1895 -2212 C ATOM 1587 CG1 VAL A 222 -18.360 3.888 -44.836 1.00 42.75 C ANISOU 1587 CG1 VAL A 222 5512 6772 3959 3374 -1863 -2253 C ATOM 1588 CG2 VAL A 222 -20.013 5.323 -46.048 1.00 45.14 C ANISOU 1588 CG2 VAL A 222 5823 7165 4163 3540 -1971 -2369 C ATOM 1589 N THR A 223 -15.469 5.692 -45.584 1.00 45.89 N ANISOU 1589 N THR A 223 6279 6948 4209 3339 -1698 -1873 N ATOM 1590 CA THR A 223 -14.178 5.202 -45.103 1.00 44.70 C ANISOU 1590 CA THR A 223 6179 6723 4080 3242 -1571 -1771 C ATOM 1591 C THR A 223 -13.178 6.306 -44.771 1.00 38.24 C ANISOU 1591 C THR A 223 5461 5871 3197 3233 -1511 -1630 C ATOM 1592 O THR A 223 -12.034 6.018 -44.424 1.00 37.43 O ANISOU 1592 O THR A 223 5403 5721 3097 3172 -1407 -1540 O ATOM 1593 CB THR A 223 -13.514 4.260 -46.125 1.00 46.55 C ANISOU 1593 CB THR A 223 6496 6876 4317 3238 -1537 -1772 C ATOM 1594 OG1 THR A 223 -13.336 4.947 -47.369 1.00 46.90 O ANISOU 1594 OG1 THR A 223 6651 6897 4273 3335 -1597 -1741 O ATOM 1595 CG2 THR A 223 -14.368 3.023 -46.344 1.00 48.70 C ANISOU 1595 CG2 THR A 223 6694 7149 4660 3225 -1576 -1925 C ATOM 1596 N TYR A 224 -13.592 7.563 -44.872 1.00 38.55 N ANISOU 1596 N TYR A 224 5538 5909 3199 3270 -1533 -1612 N ATOM 1597 CA TYR A 224 -12.663 8.656 -44.611 1.00 55.63 C ANISOU 1597 CA TYR A 224 7810 8008 5320 3252 -1463 -1491 C ATOM 1598 C TYR A 224 -13.339 9.880 -44.001 1.00 55.79 C ANISOU 1598 C TYR A 224 7841 8037 5319 3286 -1476 -1502 C ATOM 1599 O TYR A 224 -13.016 10.276 -42.886 1.00 55.69 O ANISOU 1599 O TYR A 224 7835 8020 5302 3264 -1432 -1464 O ATOM 1600 CB TYR A 224 -11.939 9.050 -45.902 1.00 38.14 C ANISOU 1600 CB TYR A 224 5716 5719 3055 3288 -1453 -1424 C ATOM 1601 CG TYR A 224 -10.735 9.940 -45.691 1.00 37.51 C ANISOU 1601 CG TYR A 224 5747 5570 2937 3265 -1371 -1301 C ATOM 1602 CD1 TYR A 224 -10.868 11.321 -45.627 1.00 37.84 C ANISOU 1602 CD1 TYR A 224 5867 5563 2949 3297 -1376 -1271 C ATOM 1603 CD2 TYR A 224 -9.462 9.399 -45.563 1.00 36.83 C ANISOU 1603 CD2 TYR A 224 5694 5467 2834 3232 -1293 -1221 C ATOM 1604 CE1 TYR A 224 -9.769 12.138 -45.435 1.00 37.48 C ANISOU 1604 CE1 TYR A 224 5930 5438 2871 3289 -1310 -1174 C ATOM 1605 CE2 TYR A 224 -8.357 10.208 -45.371 1.00 36.48 C ANISOU 1605 CE2 TYR A 224 5741 5365 2754 3225 -1220 -1117 C ATOM 1606 CZ TYR A 224 -8.517 11.576 -45.308 1.00 36.78 C ANISOU 1606 CZ TYR A 224 5858 5340 2779 3251 -1231 -1100 C ATOM 1607 OH TYR A 224 -7.423 12.386 -45.118 1.00 36.62 O ANISOU 1607 OH TYR A 224 5946 5246 2723 3261 -1162 -1021 O ATOM 1608 N LEU A 225 -14.275 10.473 -44.736 1.00 55.46 N ANISOU 1608 N LEU A 225 7813 8011 5248 3364 -1543 -1560 N ATOM 1609 CA LEU A 225 -14.864 11.755 -44.351 1.00 54.43 C ANISOU 1609 CA LEU A 225 7736 7882 5064 3438 -1559 -1569 C ATOM 1610 C LEU A 225 -15.587 11.725 -43.004 1.00 52.38 C ANISOU 1610 C LEU A 225 7383 7702 4815 3456 -1560 -1630 C ATOM 1611 O LEU A 225 -15.164 12.384 -42.051 1.00 50.50 O ANISOU 1611 O LEU A 225 7200 7407 4580 3431 -1483 -1576 O ATOM 1612 CB LEU A 225 -15.832 12.231 -45.435 1.00 57.76 C ANISOU 1612 CB LEU A 225 8180 8332 5435 3543 -1636 -1641 C ATOM 1613 CG LEU A 225 -16.590 13.524 -45.135 1.00 60.85 C ANISOU 1613 CG LEU A 225 8635 8738 5748 3669 -1663 -1669 C ATOM 1614 CD1 LEU A 225 -15.626 14.681 -44.932 1.00 59.90 C ANISOU 1614 CD1 LEU A 225 8683 8497 5578 3671 -1613 -1554 C ATOM 1615 CD2 LEU A 225 -17.577 13.833 -46.250 1.00 65.70 C ANISOU 1615 CD2 LEU A 225 9259 9402 6303 3795 -1741 -1761 C ATOM 1616 N ALA A 226 -16.677 10.968 -42.935 1.00 41.00 N ANISOU 1616 N ALA A 226 5800 6366 3410 3475 -1605 -1747 N ATOM 1617 CA ALA A 226 -17.506 10.919 -41.733 1.00 44.26 C ANISOU 1617 CA ALA A 226 6092 6823 3902 3453 -1526 -1802 C ATOM 1618 C ALA A 226 -16.746 10.468 -40.477 1.00 44.18 C ANISOU 1618 C ALA A 226 6052 6781 3954 3327 -1414 -1751 C ATOM 1619 O ALA A 226 -16.835 11.132 -39.443 1.00 44.29 O ANISOU 1619 O ALA A 226 6085 6765 3976 3316 -1320 -1739 O ATOM 1620 CB ALA A 226 -18.722 10.019 -41.966 1.00 44.85 C ANISOU 1620 CB ALA A 226 5999 7014 4027 3484 -1583 -1933 C ATOM 1621 N PRO A 227 -15.995 9.351 -40.548 1.00 44.03 N ANISOU 1621 N PRO A 227 5997 6763 3969 3241 -1410 -1729 N ATOM 1622 CA PRO A 227 -15.372 8.934 -39.288 1.00 43.67 C ANISOU 1622 CA PRO A 227 5916 6708 3967 3138 -1302 -1694 C ATOM 1623 C PRO A 227 -14.228 9.837 -38.845 1.00 43.56 C ANISOU 1623 C PRO A 227 6050 6604 3895 3111 -1236 -1589 C ATOM 1624 O PRO A 227 -14.024 9.984 -37.648 1.00 42.61 O ANISOU 1624 O PRO A 227 5932 6486 3774 3047 -1144 -1587 O ATOM 1625 CB PRO A 227 -14.845 7.528 -39.599 1.00 37.71 C ANISOU 1625 CB PRO A 227 5102 5966 3260 3075 -1309 -1694 C ATOM 1626 CG PRO A 227 -15.521 7.116 -40.852 1.00 38.42 C ANISOU 1626 CG PRO A 227 5169 6079 3350 3137 -1416 -1768 C ATOM 1627 CD PRO A 227 -15.732 8.375 -41.618 1.00 39.01 C ANISOU 1627 CD PRO A 227 5351 6134 3336 3237 -1483 -1746 C ATOM 1628 N LEU A 228 -13.490 10.421 -39.783 1.00 45.23 N ANISOU 1628 N LEU A 228 6390 6745 4049 3155 -1280 -1512 N ATOM 1629 CA LEU A 228 -12.390 11.303 -39.407 1.00 47.42 C ANISOU 1629 CA LEU A 228 6815 6931 4271 3130 -1219 -1421 C ATOM 1630 C LEU A 228 -12.927 12.634 -38.908 1.00 50.35 C ANISOU 1630 C LEU A 228 7285 7243 4604 3162 -1186 -1447 C ATOM 1631 O LEU A 228 -12.303 13.289 -38.076 1.00 53.40 O ANISOU 1631 O LEU A 228 7788 7561 4942 3089 -1104 -1419 O ATOM 1632 CB LEU A 228 -11.429 11.519 -40.576 1.00 36.86 C ANISOU 1632 CB LEU A 228 5582 5535 2889 3179 -1264 -1332 C ATOM 1633 CG LEU A 228 -10.226 10.574 -40.628 1.00 40.52 C ANISOU 1633 CG LEU A 228 6029 6007 3359 3131 -1219 -1264 C ATOM 1634 CD1 LEU A 228 -10.659 9.115 -40.643 1.00 39.61 C ANISOU 1634 CD1 LEU A 228 5772 5977 3303 3094 -1229 -1325 C ATOM 1635 CD2 LEU A 228 -9.363 10.886 -41.836 1.00 41.21 C ANISOU 1635 CD2 LEU A 228 6222 6029 3407 3177 -1226 -1184 C ATOM 1636 N GLY A 229 -14.088 13.030 -39.419 1.00 47.39 N ANISOU 1636 N GLY A 229 7812 6989 3205 427 -714 107 N ATOM 1637 CA GLY A 229 -14.769 14.203 -38.906 1.00 46.67 C ANISOU 1637 CA GLY A 229 7806 6548 3379 614 -1188 282 C ATOM 1638 C GLY A 229 -15.216 13.957 -37.477 1.00 41.68 C ANISOU 1638 C GLY A 229 6750 5811 3273 989 -1042 95 C ATOM 1639 O GLY A 229 -14.910 14.739 -36.570 1.00 39.98 O ANISOU 1639 O GLY A 229 6506 5457 3227 1066 -1039 222 O ATOM 1640 N LEU A 230 -15.931 12.852 -37.280 1.00 39.82 N ANISOU 1640 N LEU A 230 6157 5656 3318 1136 -879 -219 N ATOM 1641 CA LEU A 230 -16.412 12.460 -35.958 1.00 38.08 C ANISOU 1641 CA LEU A 230 5508 5395 3566 1326 -651 -415 C ATOM 1642 C LEU A 230 -15.272 12.346 -34.954 1.00 33.56 C ANISOU 1642 C LEU A 230 4883 4869 2998 1250 -215 -265 C ATOM 1643 O LEU A 230 -15.377 12.830 -33.830 1.00 32.95 O ANISOU 1643 O LEU A 230 4663 4709 3149 1344 -167 -260 O ATOM 1644 CB LEU A 230 -17.169 11.131 -36.032 1.00 39.90 C ANISOU 1644 CB LEU A 230 5448 5720 3990 1343 -495 -726 C ATOM 1645 CG LEU A 230 -18.546 11.146 -36.698 1.00 45.38 C ANISOU 1645 CG LEU A 230 6029 6369 4844 1469 -925 -989 C ATOM 1646 CD1 LEU A 230 -19.171 9.759 -36.668 1.00 45.48 C ANISOU 1646 CD1 LEU A 230 5747 6484 5050 1412 -700 -1288 C ATOM 1647 CD2 LEU A 230 -19.455 12.162 -36.026 1.00 47.97 C ANISOU 1647 CD2 LEU A 230 6134 6552 5541 1699 -1254 -1150 C ATOM 1648 N MET A 231 -14.184 11.706 -35.367 1.00 33.10 N ANISOU 1648 N MET A 231 4916 4957 2702 1085 78 -201 N ATOM 1649 CA MET A 231 -13.027 11.517 -34.504 1.00 30.60 C ANISOU 1649 CA MET A 231 4526 4667 2432 1041 414 -105 C ATOM 1650 C MET A 231 -12.316 12.837 -34.238 1.00 31.95 C ANISOU 1650 C MET A 231 4888 4793 2460 973 335 159 C ATOM 1651 O MET A 231 -11.740 13.031 -33.169 1.00 32.06 O ANISOU 1651 O MET A 231 4811 4753 2619 1007 488 241 O ATOM 1652 CB MET A 231 -12.057 10.506 -35.117 1.00 30.15 C ANISOU 1652 CB MET A 231 4421 4762 2274 910 671 -234 C ATOM 1653 CG MET A 231 -12.519 9.065 -34.999 1.00 29.15 C ANISOU 1653 CG MET A 231 4096 4573 2406 985 754 -481 C ATOM 1654 SD MET A 231 -11.291 7.881 -35.576 1.00 44.59 S ANISOU 1654 SD MET A 231 5926 6561 4453 855 942 -712 S ATOM 1655 CE MET A 231 -11.674 7.806 -37.323 1.00 32.77 C ANISOU 1655 CE MET A 231 4576 5317 2559 732 901 -907 C ATOM 1656 N ALA A 232 -12.358 13.741 -35.211 1.00 32.20 N ANISOU 1656 N ALA A 232 5233 4817 2186 837 50 311 N ATOM 1657 CA ALA A 232 -11.827 15.082 -35.009 1.00 31.59 C ANISOU 1657 CA ALA A 232 5333 4592 2077 683 -122 563 C ATOM 1658 C ALA A 232 -12.611 15.773 -33.901 1.00 30.26 C ANISOU 1658 C ALA A 232 5103 4190 2205 1011 -357 554 C ATOM 1659 O ALA A 232 -12.027 16.382 -33.007 1.00 27.92 O ANISOU 1659 O ALA A 232 4753 3810 2046 989 -270 641 O ATOM 1660 CB ALA A 232 -11.885 15.891 -36.294 1.00 30.46 C ANISOU 1660 CB ALA A 232 5483 4432 1658 385 -451 737 C ATOM 1661 N MET A 233 -13.935 15.661 -33.960 1.00 33.31 N ANISOU 1661 N MET A 233 5346 4474 2835 1232 -631 332 N ATOM 1662 CA MET A 233 -14.793 16.219 -32.917 1.00 34.44 C ANISOU 1662 CA MET A 233 5239 4460 3388 1496 -797 127 C ATOM 1663 C MET A 233 -14.491 15.605 -31.554 1.00 33.06 C ANISOU 1663 C MET A 233 4762 4421 3377 1493 -316 23 C ATOM 1664 O MET A 233 -14.300 16.318 -30.563 1.00 33.02 O ANISOU 1664 O MET A 233 4704 4343 3500 1551 -300 21 O ATOM 1665 CB MET A 233 -16.270 16.006 -33.259 1.00 38.29 C ANISOU 1665 CB MET A 233 5500 4902 4146 1706 -1110 -219 C ATOM 1666 CG MET A 233 -16.788 16.876 -34.389 1.00 44.47 C ANISOU 1666 CG MET A 233 6604 5430 4864 1784 -1802 -143 C ATOM 1667 SD MET A 233 -18.580 16.767 -34.562 1.00 91.88 S ANISOU 1667 SD MET A 233 12203 11349 11359 2085 -2217 -678 S ATOM 1668 CE MET A 233 -19.109 17.236 -32.916 1.00 52.02 C ANISOU 1668 CE MET A 233 6633 6333 6798 2225 -1975 -1095 C ATOM 1669 N ALA A 234 -14.449 14.277 -31.522 1.00 31.61 N ANISOU 1669 N ALA A 234 4431 4404 3175 1403 22 -59 N ATOM 1670 CA ALA A 234 -14.243 13.529 -30.289 1.00 19.87 C ANISOU 1670 CA ALA A 234 2759 2991 1799 1333 387 -114 C ATOM 1671 C ALA A 234 -12.922 13.901 -29.632 1.00 27.54 C ANISOU 1671 C ALA A 234 3868 3934 2663 1262 530 134 C ATOM 1672 O ALA A 234 -12.875 14.163 -28.434 1.00 28.37 O ANISOU 1672 O ALA A 234 3901 4025 2853 1250 631 117 O ATOM 1673 CB ALA A 234 -14.297 12.034 -30.561 1.00 19.54 C ANISOU 1673 CB ALA A 234 2648 3024 1753 1229 595 -188 C ATOM 1674 N TYR A 235 -11.853 13.937 -30.418 1.00 24.97 N ANISOU 1674 N TYR A 235 3717 3635 2133 1178 550 318 N ATOM 1675 CA TYR A 235 -10.545 14.279 -29.876 1.00 24.81 C ANISOU 1675 CA TYR A 235 3700 3554 2174 1035 608 457 C ATOM 1676 C TYR A 235 -10.444 15.762 -29.553 1.00 25.96 C ANISOU 1676 C TYR A 235 3983 3606 2273 1060 444 574 C ATOM 1677 O TYR A 235 -9.652 16.157 -28.704 1.00 26.12 O ANISOU 1677 O TYR A 235 3951 3572 2403 978 487 609 O ATOM 1678 CB TYR A 235 -9.435 13.861 -30.839 1.00 17.84 C ANISOU 1678 CB TYR A 235 2808 2753 1219 834 666 448 C ATOM 1679 CG TYR A 235 -9.152 12.382 -30.770 1.00 23.47 C ANISOU 1679 CG TYR A 235 3370 3483 2062 838 786 307 C ATOM 1680 CD1 TYR A 235 -8.610 11.818 -29.624 1.00 23.51 C ANISOU 1680 CD1 TYR A 235 3307 3385 2242 874 816 327 C ATOM 1681 CD2 TYR A 235 -9.441 11.547 -31.839 1.00 25.32 C ANISOU 1681 CD2 TYR A 235 3584 3822 2216 818 835 153 C ATOM 1682 CE1 TYR A 235 -8.358 10.466 -29.546 1.00 24.56 C ANISOU 1682 CE1 TYR A 235 3376 3481 2473 930 882 217 C ATOM 1683 CE2 TYR A 235 -9.193 10.192 -31.771 1.00 26.75 C ANISOU 1683 CE2 TYR A 235 3641 3974 2549 854 912 -14 C ATOM 1684 CZ TYR A 235 -8.651 9.657 -30.622 1.00 26.52 C ANISOU 1684 CZ TYR A 235 3567 3805 2706 930 922 24 C ATOM 1685 OH TYR A 235 -8.401 8.307 -30.550 1.00 27.23 O ANISOU 1685 OH TYR A 235 3587 3796 2962 1043 951 -145 O ATOM 1686 N PHE A 236 -11.248 16.582 -30.221 1.00 27.99 N ANISOU 1686 N PHE A 236 4417 3779 2437 1161 136 605 N ATOM 1687 CA PHE A 236 -11.311 17.996 -29.875 1.00 29.29 C ANISOU 1687 CA PHE A 236 4685 3731 2714 1171 -161 647 C ATOM 1688 C PHE A 236 -11.872 18.154 -28.468 1.00 27.70 C ANISOU 1688 C PHE A 236 4280 3507 2737 1407 -108 453 C ATOM 1689 O PHE A 236 -11.305 18.867 -27.636 1.00 26.30 O ANISOU 1689 O PHE A 236 4133 3258 2602 1380 -102 504 O ATOM 1690 CB PHE A 236 -12.163 18.777 -30.875 1.00 32.10 C ANISOU 1690 CB PHE A 236 5214 3889 3093 1204 -638 640 C ATOM 1691 CG PHE A 236 -12.397 20.206 -30.479 1.00 36.21 C ANISOU 1691 CG PHE A 236 5785 4136 3838 1244 -991 609 C ATOM 1692 CD1 PHE A 236 -11.439 21.172 -30.729 1.00 38.11 C ANISOU 1692 CD1 PHE A 236 6207 4289 3983 957 -1051 857 C ATOM 1693 CD2 PHE A 236 -13.574 20.582 -29.852 1.00 37.99 C ANISOU 1693 CD2 PHE A 236 5802 4234 4399 1560 -1231 258 C ATOM 1694 CE1 PHE A 236 -11.650 22.488 -30.363 1.00 40.52 C ANISOU 1694 CE1 PHE A 236 6598 4315 4482 1020 -1379 805 C ATOM 1695 CE2 PHE A 236 -13.790 21.896 -29.483 1.00 41.39 C ANISOU 1695 CE2 PHE A 236 6262 4411 5053 1605 -1554 149 C ATOM 1696 CZ PHE A 236 -12.827 22.850 -29.739 1.00 41.76 C ANISOU 1696 CZ PHE A 236 6595 4302 4969 1353 -1653 447 C ATOM 1697 N GLN A 237 -12.985 17.476 -28.207 1.00 28.70 N ANISOU 1697 N GLN A 237 4137 3735 3033 1513 -28 147 N ATOM 1698 CA GLN A 237 -13.606 17.527 -26.889 1.00 20.52 C ANISOU 1698 CA GLN A 237 2829 2785 2185 1565 125 -159 C ATOM 1699 C GLN A 237 -12.693 16.903 -25.836 1.00 28.02 C ANISOU 1699 C GLN A 237 3813 3853 2982 1368 492 -2 C ATOM 1700 O GLN A 237 -12.570 17.420 -24.724 1.00 28.32 O ANISOU 1700 O GLN A 237 3809 3910 3040 1343 558 -91 O ATOM 1701 CB GLN A 237 -14.968 16.828 -26.908 1.00 27.70 C ANISOU 1701 CB GLN A 237 3418 3842 3264 1583 191 -539 C ATOM 1702 CG GLN A 237 -15.979 17.500 -27.826 1.00 31.59 C ANISOU 1702 CG GLN A 237 3829 4187 3985 1798 -270 -764 C ATOM 1703 CD GLN A 237 -17.397 17.001 -27.616 1.00 34.97 C ANISOU 1703 CD GLN A 237 3864 4778 4644 1715 -200 -1187 C ATOM 1704 OE1 GLN A 237 -17.618 15.942 -27.029 1.00 34.21 O ANISOU 1704 OE1 GLN A 237 3632 4886 4480 1459 202 -1234 O ATOM 1705 NE2 GLN A 237 -18.369 17.770 -28.095 1.00 38.81 N ANISOU 1705 NE2 GLN A 237 4215 5141 5391 1888 -636 -1473 N ATOM 1706 N ILE A 238 -12.042 15.801 -26.200 1.00 27.14 N ANISOU 1706 N ILE A 238 3784 3785 2743 1222 655 205 N ATOM 1707 CA ILE A 238 -11.122 15.117 -25.297 1.00 25.82 C ANISOU 1707 CA ILE A 238 3647 3576 2588 984 742 349 C ATOM 1708 C ILE A 238 -9.963 16.019 -24.892 1.00 24.36 C ANISOU 1708 C ILE A 238 3559 3309 2387 1011 684 497 C ATOM 1709 O ILE A 238 -9.693 16.195 -23.705 1.00 24.85 O ANISOU 1709 O ILE A 238 3628 3364 2450 924 711 485 O ATOM 1710 CB ILE A 238 -10.559 13.829 -25.930 1.00 15.03 C ANISOU 1710 CB ILE A 238 2286 2162 1261 896 751 422 C ATOM 1711 CG1 ILE A 238 -11.627 12.736 -25.943 1.00 18.50 C ANISOU 1711 CG1 ILE A 238 2654 2661 1715 804 843 280 C ATOM 1712 CG2 ILE A 238 -9.338 13.344 -25.165 1.00 14.55 C ANISOU 1712 CG2 ILE A 238 2269 2015 1246 825 750 518 C ATOM 1713 CD1 ILE A 238 -11.207 11.482 -26.677 1.00 19.29 C ANISOU 1713 CD1 ILE A 238 2787 2710 1832 806 866 316 C ATOM 1714 N PHE A 239 -9.284 16.595 -25.879 1.00 23.85 N ANISOU 1714 N PHE A 239 3553 3204 2304 1025 595 578 N ATOM 1715 CA PHE A 239 -8.144 17.458 -25.605 1.00 25.02 C ANISOU 1715 CA PHE A 239 3730 3297 2479 899 520 638 C ATOM 1716 C PHE A 239 -8.580 18.714 -24.866 1.00 26.61 C ANISOU 1716 C PHE A 239 4040 3424 2647 1011 415 640 C ATOM 1717 O PHE A 239 -7.836 19.243 -24.041 1.00 25.84 O ANISOU 1717 O PHE A 239 3952 3290 2578 934 395 664 O ATOM 1718 CB PHE A 239 -7.415 17.822 -26.899 1.00 29.49 C ANISOU 1718 CB PHE A 239 4354 3876 2974 730 438 718 C ATOM 1719 CG PHE A 239 -6.508 16.736 -27.396 1.00 35.07 C ANISOU 1719 CG PHE A 239 4956 4688 3680 653 567 695 C ATOM 1720 CD1 PHE A 239 -5.501 16.243 -26.586 1.00 37.33 C ANISOU 1720 CD1 PHE A 239 5149 4983 4052 675 635 692 C ATOM 1721 CD2 PHE A 239 -6.661 16.207 -28.665 1.00 39.03 C ANISOU 1721 CD2 PHE A 239 5477 5288 4063 591 610 672 C ATOM 1722 CE1 PHE A 239 -4.667 15.241 -27.030 1.00 39.67 C ANISOU 1722 CE1 PHE A 239 5353 5381 4338 702 759 665 C ATOM 1723 CE2 PHE A 239 -5.830 15.206 -29.113 1.00 39.77 C ANISOU 1723 CE2 PHE A 239 5457 5512 4141 552 757 588 C ATOM 1724 CZ PHE A 239 -4.830 14.723 -28.294 1.00 40.27 C ANISOU 1724 CZ PHE A 239 5402 5581 4319 633 836 572 C ATOM 1725 N ARG A 240 -9.791 19.179 -25.152 1.00 28.35 N ANISOU 1725 N ARG A 240 4324 3586 2861 1256 260 569 N ATOM 1726 CA ARG A 240 -10.341 20.318 -24.429 1.00 30.60 C ANISOU 1726 CA ARG A 240 4575 3740 3310 1408 52 358 C ATOM 1727 C ARG A 240 -10.559 19.965 -22.959 1.00 27.13 C ANISOU 1727 C ARG A 240 3962 3483 2861 1354 320 128 C ATOM 1728 O ARG A 240 -10.406 20.813 -22.080 1.00 26.34 O ANISOU 1728 O ARG A 240 3862 3335 2812 1380 253 -2 O ATOM 1729 CB ARG A 240 -11.650 20.783 -25.067 1.00 37.57 C ANISOU 1729 CB ARG A 240 5363 4502 4411 1626 -265 81 C ATOM 1730 CG ARG A 240 -12.171 22.101 -24.522 1.00 42.87 C ANISOU 1730 CG ARG A 240 5953 4980 5357 1761 -588 -221 C ATOM 1731 CD ARG A 240 -13.278 22.654 -25.400 1.00 48.44 C ANISOU 1731 CD ARG A 240 6591 5514 6300 1855 -997 -426 C ATOM 1732 NE ARG A 240 -13.891 23.846 -24.820 1.00 54.83 N ANISOU 1732 NE ARG A 240 7262 6169 7400 1978 -1301 -794 N ATOM 1733 CZ ARG A 240 -13.383 25.070 -24.916 1.00 60.58 C ANISOU 1733 CZ ARG A 240 8239 6594 8183 1943 -1649 -668 C ATOM 1734 NH1 ARG A 240 -12.245 25.270 -25.565 1.00 60.55 N ANISOU 1734 NH1 ARG A 240 8602 6465 7942 1703 -1663 -172 N ATOM 1735 NH2 ARG A 240 -14.012 26.096 -24.357 1.00 64.62 N ANISOU 1735 NH2 ARG A 240 8598 6972 8984 2091 -1961 -1074 N ATOM 1736 N LYS A 241 -10.906 18.709 -22.698 1.00 24.72 N ANISOU 1736 N LYS A 241 3556 3381 2454 1228 605 85 N ATOM 1737 CA LYS A 241 -11.131 18.253 -21.331 1.00 18.85 C ANISOU 1737 CA LYS A 241 2740 2816 1608 1004 833 -71 C ATOM 1738 C LYS A 241 -9.814 17.950 -20.615 1.00 22.17 C ANISOU 1738 C LYS A 241 3352 3168 1904 820 829 235 C ATOM 1739 O LYS A 241 -9.745 17.994 -19.389 1.00 24.79 O ANISOU 1739 O LYS A 241 3717 3590 2114 631 899 151 O ATOM 1740 CB LYS A 241 -12.036 17.016 -21.326 1.00 32.90 C ANISOU 1740 CB LYS A 241 4373 4727 3399 748 976 -200 C ATOM 1741 CG LYS A 241 -12.486 16.566 -19.943 1.00 35.50 C ANISOU 1741 CG LYS A 241 4654 5271 3565 368 1191 -405 C ATOM 1742 CD LYS A 241 -13.201 17.684 -19.197 1.00 38.67 C ANISOU 1742 CD LYS A 241 4966 5693 4035 503 1302 -734 C ATOM 1743 CE LYS A 241 -13.546 17.266 -17.774 1.00 43.40 C ANISOU 1743 CE LYS A 241 5570 6539 4380 218 1436 -788 C ATOM 1744 NZ LYS A 241 -14.111 18.392 -16.979 1.00 47.68 N ANISOU 1744 NZ LYS A 241 5898 7214 5003 209 1461 -1231 N ATOM 1745 N LEU A 242 -8.769 17.658 -21.385 1.00 15.96 N ANISOU 1745 N LEU A 242 2624 2230 1209 843 704 488 N ATOM 1746 CA LEU A 242 -7.473 17.287 -20.819 1.00 15.44 C ANISOU 1746 CA LEU A 242 2583 2091 1193 690 612 595 C ATOM 1747 C LEU A 242 -6.493 18.452 -20.756 1.00 16.01 C ANISOU 1747 C LEU A 242 2686 2102 1296 724 509 653 C ATOM 1748 O LEU A 242 -5.447 18.354 -20.115 1.00 15.53 O ANISOU 1748 O LEU A 242 2636 2017 1249 617 430 710 O ATOM 1749 CB LEU A 242 -6.840 16.154 -21.628 1.00 14.68 C ANISOU 1749 CB LEU A 242 2418 1952 1206 664 577 643 C ATOM 1750 CG LEU A 242 -7.534 14.795 -21.652 1.00 15.59 C ANISOU 1750 CG LEU A 242 2556 2075 1291 598 633 634 C ATOM 1751 CD1 LEU A 242 -6.636 13.775 -22.329 1.00 15.03 C ANISOU 1751 CD1 LEU A 242 2473 1939 1299 671 604 699 C ATOM 1752 CD2 LEU A 242 -7.896 14.351 -20.247 1.00 16.70 C ANISOU 1752 CD2 LEU A 242 2824 2256 1265 363 640 657 C ATOM 1753 N TRP A 243 -6.827 19.547 -21.431 1.00 17.27 N ANISOU 1753 N TRP A 243 2894 2214 1453 855 456 658 N ATOM 1754 CA TRP A 243 -5.911 20.677 -21.553 1.00 16.32 C ANISOU 1754 CA TRP A 243 2822 1993 1384 779 295 733 C ATOM 1755 C TRP A 243 -5.573 21.303 -20.208 1.00 17.12 C ANISOU 1755 C TRP A 243 3026 2062 1416 805 258 731 C ATOM 1756 O TRP A 243 -6.458 21.572 -19.395 1.00 18.18 O ANISOU 1756 O TRP A 243 3257 2230 1421 959 305 597 O ATOM 1757 CB TRP A 243 -6.499 21.744 -22.475 1.00 17.64 C ANISOU 1757 CB TRP A 243 3096 2016 1590 856 100 752 C ATOM 1758 CG TRP A 243 -5.570 22.896 -22.720 1.00 18.95 C ANISOU 1758 CG TRP A 243 3335 2049 1815 679 -101 888 C ATOM 1759 CD1 TRP A 243 -4.721 23.052 -23.777 1.00 22.39 C ANISOU 1759 CD1 TRP A 243 3761 2524 2221 423 -140 1062 C ATOM 1760 CD2 TRP A 243 -5.390 24.049 -21.887 1.00 20.42 C ANISOU 1760 CD2 TRP A 243 3639 2060 2058 747 -274 874 C ATOM 1761 NE1 TRP A 243 -4.026 24.230 -23.655 1.00 21.54 N ANISOU 1761 NE1 TRP A 243 3728 2309 2146 330 -265 1211 N ATOM 1762 CE2 TRP A 243 -4.417 24.860 -22.504 1.00 39.57 C ANISOU 1762 CE2 TRP A 243 6102 4420 4512 516 -382 1077 C ATOM 1763 CE3 TRP A 243 -5.957 24.474 -20.681 1.00 40.01 C ANISOU 1763 CE3 TRP A 243 6219 4440 4541 1013 -345 677 C ATOM 1764 CZ2 TRP A 243 -3.999 26.071 -21.955 1.00 41.39 C ANISOU 1764 CZ2 TRP A 243 6484 4439 4804 507 -572 1085 C ATOM 1765 CZ3 TRP A 243 -5.539 25.674 -20.138 1.00 41.20 C ANISOU 1765 CZ3 TRP A 243 6495 4369 4789 1019 -591 637 C ATOM 1766 CH2 TRP A 243 -4.571 26.460 -20.775 1.00 40.86 C ANISOU 1766 CH2 TRP A 243 6498 4224 4804 743 -711 857 C ATOM 1767 N GLY A 244 -4.286 21.547 -19.987 1.00 17.18 N ANISOU 1767 N GLY A 244 2999 2045 1483 646 172 818 N ATOM 1768 CA GLY A 244 -3.834 22.220 -18.785 1.00 24.23 C ANISOU 1768 CA GLY A 244 4011 2890 2307 657 92 831 C ATOM 1769 C GLY A 244 -3.823 21.323 -17.566 1.00 24.28 C ANISOU 1769 C GLY A 244 4057 3004 2162 597 162 803 C ATOM 1770 O GLY A 244 -3.699 21.796 -16.436 1.00 25.42 O ANISOU 1770 O GLY A 244 4373 3156 2131 587 115 775 O ATOM 1771 N ARG A 245 -3.950 20.021 -17.794 1.00 17.70 N ANISOU 1771 N ARG A 245 3125 2235 1365 518 225 808 N ATOM 1772 CA ARG A 245 -3.995 19.060 -16.701 1.00 18.79 C ANISOU 1772 CA ARG A 245 3352 2430 1358 366 205 838 C ATOM 1773 C ARG A 245 -2.824 18.095 -16.785 1.00 30.77 C ANISOU 1773 C ARG A 245 4813 3864 3013 324 28 974 C ATOM 1774 O ARG A 245 -2.987 16.925 -17.131 1.00 30.83 O ANISOU 1774 O ARG A 245 4803 3843 3067 307 16 1005 O ATOM 1775 CB ARG A 245 -5.320 18.303 -16.719 1.00 19.05 C ANISOU 1775 CB ARG A 245 3395 2571 1273 296 374 746 C ATOM 1776 CG ARG A 245 -6.521 19.223 -16.638 1.00 19.81 C ANISOU 1776 CG ARG A 245 3521 2790 1216 395 577 528 C ATOM 1777 CD ARG A 245 -7.803 18.498 -16.979 1.00 47.74 C ANISOU 1777 CD ARG A 245 6943 6467 4729 323 758 370 C ATOM 1778 NE ARG A 245 -8.923 19.424 -17.103 1.00 47.86 N ANISOU 1778 NE ARG A 245 6838 6617 4727 499 921 1 N ATOM 1779 CZ ARG A 245 -9.741 19.742 -16.106 1.00 50.25 C ANISOU 1779 CZ ARG A 245 7032 7170 4890 332 1092 -401 C ATOM 1780 NH1 ARG A 245 -9.567 19.203 -14.907 1.00 53.81 N ANISOU 1780 NH1 ARG A 245 7576 7793 5077 50 1123 -310 N ATOM 1781 NH2 ARG A 245 -10.736 20.596 -16.309 1.00 50.14 N ANISOU 1781 NH2 ARG A 245 6759 7211 5082 544 1130 -878 N ATOM 1782 N GLN A 246 -1.640 18.598 -16.458 1.00 32.21 N ANISOU 1782 N GLN A 246 4992 3988 3259 352 -129 1056 N ATOM 1783 CA GLN A 246 -0.419 17.815 -16.569 1.00 33.08 C ANISOU 1783 CA GLN A 246 5046 3995 3529 429 -325 1167 C ATOM 1784 C GLN A 246 -0.010 17.229 -15.223 1.00 35.84 C ANISOU 1784 C GLN A 246 5525 4302 3792 414 -510 1275 C ATOM 1785 O GLN A 246 0.980 16.505 -15.126 1.00 38.72 O ANISOU 1785 O GLN A 246 5891 4516 4305 545 -750 1307 O ATOM 1786 CB GLN A 246 0.709 18.678 -17.134 1.00 34.25 C ANISOU 1786 CB GLN A 246 5100 4118 3794 550 -366 1180 C ATOM 1787 CG GLN A 246 0.328 19.422 -18.403 1.00 35.41 C ANISOU 1787 CG GLN A 246 5156 4359 3939 553 -112 1129 C ATOM 1788 CD GLN A 246 1.523 20.037 -19.098 1.00 42.37 C ANISOU 1788 CD GLN A 246 5867 5312 4918 576 -74 1222 C ATOM 1789 OE1 GLN A 246 2.669 19.778 -18.731 1.00 46.93 O ANISOU 1789 OE1 GLN A 246 6253 5891 5689 591 -242 1137 O ATOM 1790 NE2 GLN A 246 1.262 20.855 -20.111 1.00 43.46 N ANISOU 1790 NE2 GLN A 246 6012 5515 4987 441 96 1254 N ATOM 1791 N GLY A1001 -0.780 17.544 -14.188 1.00 31.05 N ANISOU 1791 N GLY A1001 3687 5270 2840 -157 -980 0 N ATOM 1792 CA GLY A1001 -0.473 17.081 -12.848 1.00 30.10 C ANISOU 1792 CA GLY A1001 3497 5218 2720 -192 -893 -4 C ATOM 1793 C GLY A1001 0.471 18.029 -12.144 1.00 30.43 C ANISOU 1793 C GLY A1001 3545 5235 2782 -165 -889 5 C ATOM 1794 O GLY A1001 0.727 19.134 -12.622 1.00 31.61 O ANISOU 1794 O GLY A1001 3752 5320 2939 -131 -965 9 O ATOM 1795 N ILE A1002 0.989 17.599 -11.000 1.00 31.13 N ANISOU 1795 N ILE A1002 3588 5375 2864 -190 -814 10 N ATOM 1796 CA ILE A1002 1.925 18.416 -10.242 1.00 20.62 C ANISOU 1796 CA ILE A1002 2252 4038 1545 -179 -807 14 C ATOM 1797 C ILE A1002 3.243 17.683 -10.030 1.00 31.53 C ANISOU 1797 C ILE A1002 3646 5435 2898 -202 -733 65 C ATOM 1798 O ILE A1002 3.319 16.463 -10.180 1.00 31.59 O ANISOU 1798 O ILE A1002 3675 5453 2874 -211 -692 88 O ATOM 1799 CB ILE A1002 1.350 18.816 -8.872 1.00 20.93 C ANISOU 1799 CB ILE A1002 2209 4146 1596 -165 -800 -46 C ATOM 1800 CG1 ILE A1002 1.186 17.582 -7.984 1.00 20.77 C ANISOU 1800 CG1 ILE A1002 2141 4212 1540 -211 -714 -41 C ATOM 1801 CG2 ILE A1002 0.025 19.542 -9.040 1.00 23.65 C ANISOU 1801 CG2 ILE A1002 2517 4510 1960 -114 -878 -115 C ATOM 1802 CD1 ILE A1002 0.699 17.895 -6.589 1.00 23.53 C ANISOU 1802 CD1 ILE A1002 2404 4658 1877 -209 -689 -99 C ATOM 1803 N ASP A1003 4.280 18.436 -9.682 1.00 20.18 N ANISOU 1803 N ASP A1003 2201 4005 1460 -208 -731 75 N ATOM 1804 CA ASP A1003 5.584 17.854 -9.403 1.00 20.04 C ANISOU 1804 CA ASP A1003 2164 4041 1411 -215 -669 108 C ATOM 1805 C ASP A1003 5.559 17.153 -8.051 1.00 26.07 C ANISOU 1805 C ASP A1003 2890 4849 2166 -199 -629 93 C ATOM 1806 O ASP A1003 5.787 17.776 -7.014 1.00 26.67 O ANISOU 1806 O ASP A1003 2924 4959 2252 -203 -628 68 O ATOM 1807 CB ASP A1003 6.672 18.931 -9.431 1.00 37.16 C ANISOU 1807 CB ASP A1003 4313 6242 3565 -256 -682 119 C ATOM 1808 CG ASP A1003 8.074 18.351 -9.502 1.00 36.67 C ANISOU 1808 CG ASP A1003 4200 6279 3455 -261 -621 148 C ATOM 1809 OD1 ASP A1003 8.273 17.191 -9.085 1.00 36.15 O ANISOU 1809 OD1 ASP A1003 4123 6241 3374 -200 -584 147 O ATOM 1810 OD2 ASP A1003 8.985 19.061 -9.975 1.00 35.95 O ANISOU 1810 OD2 ASP A1003 4082 6254 3325 -327 -621 167 O ATOM 1811 N CYS A1004 5.289 15.851 -8.069 1.00 25.31 N ANISOU 1811 N CYS A1004 2832 4748 2037 -185 -607 108 N ATOM 1812 CA CYS A1004 5.220 15.065 -6.843 1.00 24.68 C ANISOU 1812 CA CYS A1004 2757 4700 1920 -182 -584 104 C ATOM 1813 C CYS A1004 6.578 14.953 -6.156 1.00 24.49 C ANISOU 1813 C CYS A1004 2716 4718 1872 -135 -567 114 C ATOM 1814 O CYS A1004 6.654 14.645 -4.966 1.00 24.93 O ANISOU 1814 O CYS A1004 2771 4801 1899 -126 -559 107 O ATOM 1815 CB CYS A1004 4.668 13.668 -7.134 1.00 25.26 C ANISOU 1815 CB CYS A1004 2927 4735 1934 -193 -588 125 C ATOM 1816 SG CYS A1004 2.913 13.630 -7.566 1.00 47.58 S ANISOU 1816 SG CYS A1004 5736 7576 4767 -279 -602 99 S ATOM 1817 N SER A1005 7.649 15.205 -6.903 1.00 23.08 N ANISOU 1817 N SER A1005 2513 4567 1691 -109 -562 128 N ATOM 1818 CA SER A1005 8.993 15.132 -6.343 1.00 20.85 C ANISOU 1818 CA SER A1005 2176 4372 1374 -61 -546 126 C ATOM 1819 C SER A1005 9.296 16.367 -5.500 1.00 35.01 C ANISOU 1819 C SER A1005 3885 6219 3196 -111 -545 101 C ATOM 1820 O SER A1005 10.112 16.316 -4.580 1.00 36.31 O ANISOU 1820 O SER A1005 4003 6460 3335 -83 -538 89 O ATOM 1821 CB SER A1005 10.036 14.982 -7.451 1.00 25.21 C ANISOU 1821 CB SER A1005 2694 4995 1890 -27 -532 138 C ATOM 1822 OG SER A1005 10.254 16.213 -8.116 1.00 26.78 O ANISOU 1822 OG SER A1005 2831 5234 2109 -114 -527 141 O ATOM 1823 N PHE A1006 8.636 17.476 -5.822 1.00 20.66 N ANISOU 1823 N PHE A1006 2069 4358 1424 -177 -567 90 N ATOM 1824 CA PHE A1006 8.763 18.694 -5.031 1.00 31.50 C ANISOU 1824 CA PHE A1006 3405 5749 2813 -224 -590 58 C ATOM 1825 C PHE A1006 7.755 18.688 -3.891 1.00 32.64 C ANISOU 1825 C PHE A1006 3561 5868 2974 -206 -597 21 C ATOM 1826 O PHE A1006 8.112 18.867 -2.727 1.00 31.60 O ANISOU 1826 O PHE A1006 3397 5783 2825 -202 -592 -3 O ATOM 1827 CB PHE A1006 8.563 19.939 -5.900 1.00 21.14 C ANISOU 1827 CB PHE A1006 2126 4388 1518 -290 -642 57 C ATOM 1828 CG PHE A1006 8.511 21.222 -5.115 1.00 21.65 C ANISOU 1828 CG PHE A1006 2201 4436 1589 -332 -700 14 C ATOM 1829 CD1 PHE A1006 9.674 21.907 -4.806 1.00 34.41 C ANISOU 1829 CD1 PHE A1006 3781 6126 3168 -410 -707 13 C ATOM 1830 CD2 PHE A1006 7.299 21.741 -4.684 1.00 23.11 C ANISOU 1830 CD2 PHE A1006 2428 4550 1805 -295 -754 -36 C ATOM 1831 CE1 PHE A1006 9.630 23.084 -4.081 1.00 34.86 C ANISOU 1831 CE1 PHE A1006 3873 6152 3219 -458 -777 -33 C ATOM 1832 CE2 PHE A1006 7.249 22.916 -3.958 1.00 22.33 C ANISOU 1832 CE2 PHE A1006 2357 4429 1698 -314 -826 -89 C ATOM 1833 CZ PHE A1006 8.416 23.587 -3.657 1.00 35.10 C ANISOU 1833 CZ PHE A1006 3969 6087 3280 -398 -844 -87 C ATOM 1834 N TRP A1007 6.488 18.488 -4.241 1.00 33.48 N ANISOU 1834 N TRP A1007 3698 5924 3100 -201 -606 11 N ATOM 1835 CA TRP A1007 5.410 18.505 -3.263 1.00 34.86 C ANISOU 1835 CA TRP A1007 3852 6124 3270 -198 -603 -33 C ATOM 1836 C TRP A1007 5.311 17.192 -2.498 1.00 36.15 C ANISOU 1836 C TRP A1007 4023 6332 3379 -198 -558 -12 C ATOM 1837 O TRP A1007 4.429 16.375 -2.764 1.00 37.82 O ANISOU 1837 O TRP A1007 4258 6545 3566 -224 -546 -2 O ATOM 1838 CB TRP A1007 4.072 18.804 -3.942 1.00 20.70 C ANISOU 1838 CB TRP A1007 2059 4305 1502 -196 -633 -64 C ATOM 1839 CG TRP A1007 4.006 20.154 -4.582 1.00 26.23 C ANISOU 1839 CG TRP A1007 2787 4940 2237 -180 -714 -91 C ATOM 1840 CD1 TRP A1007 4.154 20.441 -5.908 1.00 20.91 C ANISOU 1840 CD1 TRP A1007 2171 4194 1578 -187 -759 -59 C ATOM 1841 CD2 TRP A1007 3.774 21.405 -3.924 1.00 21.63 C ANISOU 1841 CD2 TRP A1007 2205 4353 1660 -156 -779 -157 C ATOM 1842 NE1 TRP A1007 4.029 21.794 -6.116 1.00 25.44 N ANISOU 1842 NE1 TRP A1007 2797 4711 2160 -176 -859 -92 N ATOM 1843 CE2 TRP A1007 3.796 22.408 -4.914 1.00 27.09 C ANISOU 1843 CE2 TRP A1007 2976 4954 2364 -152 -880 -156 C ATOM 1844 CE3 TRP A1007 3.553 21.775 -2.594 1.00 30.66 C ANISOU 1844 CE3 TRP A1007 3304 5562 2784 -136 -773 -220 C ATOM 1845 CZ2 TRP A1007 3.603 23.755 -4.616 1.00 29.34 C ANISOU 1845 CZ2 TRP A1007 3318 5195 2636 -126 -992 -217 C ATOM 1846 CZ3 TRP A1007 3.362 23.113 -2.300 1.00 30.57 C ANISOU 1846 CZ3 TRP A1007 3327 5518 2770 -101 -869 -289 C ATOM 1847 CH2 TRP A1007 3.388 24.087 -3.307 1.00 30.34 C ANISOU 1847 CH2 TRP A1007 3397 5381 2748 -96 -986 -287 C ATOM 1848 N ASN A1008 6.222 16.987 -1.553 1.00 38.35 N ANISOU 1848 N ASN A1008 4298 6648 3626 -180 -547 -5 N ATOM 1849 CA ASN A1008 6.094 15.877 -0.619 1.00 41.17 C ANISOU 1849 CA ASN A1008 4698 7033 3912 -179 -531 13 C ATOM 1850 C ASN A1008 6.653 16.234 0.753 1.00 39.98 C ANISOU 1850 C ASN A1008 4518 6941 3731 -165 -531 -11 C ATOM 1851 O ASN A1008 7.444 17.166 0.895 1.00 38.15 O ANISOU 1851 O ASN A1008 4237 6728 3532 -151 -545 -34 O ATOM 1852 CB ASN A1008 6.767 14.610 -1.166 1.00 46.82 C ANISOU 1852 CB ASN A1008 5510 7695 4583 -133 -543 68 C ATOM 1853 CG ASN A1008 8.213 14.829 -1.567 1.00 51.65 C ANISOU 1853 CG ASN A1008 6088 8324 5210 -67 -553 76 C ATOM 1854 OD1 ASN A1008 8.897 15.701 -1.038 1.00 52.63 O ANISOU 1854 OD1 ASN A1008 6133 8510 5353 -67 -552 50 O ATOM 1855 ND2 ASN A1008 8.688 14.023 -2.510 1.00 52.85 N ANISOU 1855 ND2 ASN A1008 6297 8443 5339 -14 -564 105 N ATOM 1856 N GLU A1009 6.227 15.479 1.759 1.00 38.58 N ANISOU 1856 N GLU A1009 4386 6796 3479 -185 -520 -4 N ATOM 1857 CA GLU A1009 6.539 15.778 3.150 1.00 39.92 C ANISOU 1857 CA GLU A1009 4536 7027 3604 -180 -521 -30 C ATOM 1858 C GLU A1009 7.995 15.479 3.497 1.00 40.86 C ANISOU 1858 C GLU A1009 4687 7138 3701 -105 -555 -6 C ATOM 1859 O GLU A1009 8.477 15.854 4.566 1.00 40.89 O ANISOU 1859 O GLU A1009 4666 7194 3676 -92 -566 -31 O ATOM 1860 CB GLU A1009 5.604 14.984 4.063 1.00 43.47 C ANISOU 1860 CB GLU A1009 5042 7521 3956 -244 -497 -23 C ATOM 1861 CG GLU A1009 5.539 15.476 5.494 1.00 47.37 C ANISOU 1861 CG GLU A1009 5496 8104 4399 -258 -486 -68 C ATOM 1862 CD GLU A1009 4.516 14.717 6.313 1.00 49.94 C ANISOU 1862 CD GLU A1009 5869 8495 4609 -356 -448 -61 C ATOM 1863 OE1 GLU A1009 3.545 14.201 5.718 1.00 51.28 O ANISOU 1863 OE1 GLU A1009 6044 8681 4761 -439 -418 -49 O ATOM 1864 OE2 GLU A1009 4.686 14.633 7.548 1.00 50.03 O ANISOU 1864 OE2 GLU A1009 5917 8553 4540 -365 -446 -68 O ATOM 1865 N SER A1010 8.694 14.813 2.583 1.00 35.84 N ANISOU 1865 N SER A1010 4095 6453 3069 -49 -573 34 N ATOM 1866 CA SER A1010 10.076 14.405 2.812 1.00 23.88 C ANISOU 1866 CA SER A1010 2590 4966 1517 44 -608 46 C ATOM 1867 C SER A1010 10.997 15.589 3.094 1.00 29.85 C ANISOU 1867 C SER A1010 3208 5819 2315 39 -605 2 C ATOM 1868 O SER A1010 11.972 15.460 3.832 1.00 33.52 O ANISOU 1868 O SER A1010 3650 6353 2734 96 -632 -8 O ATOM 1869 CB SER A1010 10.602 13.617 1.611 1.00 35.31 C ANISOU 1869 CB SER A1010 4081 6375 2959 114 -621 77 C ATOM 1870 OG SER A1010 9.916 12.386 1.468 1.00 36.44 O ANISOU 1870 OG SER A1010 4404 6411 3033 120 -644 119 O ATOM 1871 N TYR A1011 10.682 16.743 2.518 1.00 28.32 N ANISOU 1871 N TYR A1011 2942 5626 2193 -35 -584 -25 N ATOM 1872 CA TYR A1011 11.537 17.914 2.670 1.00 28.55 C ANISOU 1872 CA TYR A1011 2881 5726 2242 -74 -593 -62 C ATOM 1873 C TYR A1011 11.181 18.727 3.907 1.00 29.67 C ANISOU 1873 C TYR A1011 3018 5882 2374 -113 -609 -111 C ATOM 1874 O TYR A1011 11.763 19.783 4.158 1.00 31.02 O ANISOU 1874 O TYR A1011 3142 6093 2553 -164 -633 -149 O ATOM 1875 CB TYR A1011 11.466 18.778 1.414 1.00 26.30 C ANISOU 1875 CB TYR A1011 2569 5411 2011 -142 -588 -62 C ATOM 1876 CG TYR A1011 12.120 18.103 0.235 1.00 23.61 C ANISOU 1876 CG TYR A1011 2206 5102 1662 -106 -569 -25 C ATOM 1877 CD1 TYR A1011 13.503 18.045 0.129 1.00 37.73 C ANISOU 1877 CD1 TYR A1011 3901 7030 3405 -84 -564 -32 C ATOM 1878 CD2 TYR A1011 11.360 17.497 -0.755 1.00 26.04 C ANISOU 1878 CD2 TYR A1011 2576 5327 1993 -89 -557 7 C ATOM 1879 CE1 TYR A1011 14.112 17.417 -0.938 1.00 37.56 C ANISOU 1879 CE1 TYR A1011 3841 7074 3357 -35 -542 -13 C ATOM 1880 CE2 TYR A1011 11.959 16.865 -1.828 1.00 22.80 C ANISOU 1880 CE2 TYR A1011 2150 4950 1561 -46 -543 32 C ATOM 1881 CZ TYR A1011 13.335 16.828 -1.913 1.00 37.03 C ANISOU 1881 CZ TYR A1011 3853 6902 3315 -12 -534 20 C ATOM 1882 OH TYR A1011 13.937 16.202 -2.977 1.00 38.68 O ANISOU 1882 OH TYR A1011 4029 7180 3486 48 -516 31 O ATOM 1883 N LEU A1012 10.231 18.221 4.684 1.00 24.06 N ANISOU 1883 N LEU A1012 2361 5149 1631 -101 -599 -112 N ATOM 1884 CA LEU A1012 9.873 18.837 5.954 1.00 24.58 C ANISOU 1884 CA LEU A1012 2420 5254 1665 -124 -608 -165 C ATOM 1885 C LEU A1012 10.558 18.111 7.104 1.00 37.39 C ANISOU 1885 C LEU A1012 4069 6931 3207 -76 -628 -151 C ATOM 1886 O LEU A1012 10.728 16.892 7.067 1.00 38.34 O ANISOU 1886 O LEU A1012 4260 7029 3279 -23 -635 -98 O ATOM 1887 CB LEU A1012 8.358 18.826 6.149 1.00 24.48 C ANISOU 1887 CB LEU A1012 2425 5232 1643 -151 -578 -189 C ATOM 1888 CG LEU A1012 7.540 19.453 5.021 1.00 25.90 C ANISOU 1888 CG LEU A1012 2587 5362 1893 -172 -574 -209 C ATOM 1889 CD1 LEU A1012 6.060 19.295 5.300 1.00 26.09 C ANISOU 1889 CD1 LEU A1012 2593 5433 1887 -189 -539 -246 C ATOM 1890 CD2 LEU A1012 7.905 20.916 4.848 1.00 23.96 C ANISOU 1890 CD2 LEU A1012 2328 5086 1690 -189 -627 -263 C ATOM 1891 N THR A1013 10.953 18.864 8.125 1.00 26.15 N ANISOU 1891 N THR A1013 2615 5564 1758 -91 -652 -201 N ATOM 1892 CA THR A1013 11.619 18.281 9.283 1.00 30.22 C ANISOU 1892 CA THR A1013 3159 6134 2187 -42 -684 -193 C ATOM 1893 C THR A1013 10.669 18.174 10.469 1.00 31.52 C ANISOU 1893 C THR A1013 3382 6315 2280 -65 -670 -215 C ATOM 1894 O THR A1013 9.626 18.825 10.501 1.00 31.35 O ANISOU 1894 O THR A1013 3336 6299 2278 -115 -637 -261 O ATOM 1895 CB THR A1013 12.851 19.102 9.701 1.00 27.99 C ANISOU 1895 CB THR A1013 2798 5932 1904 -49 -726 -236 C ATOM 1896 OG1 THR A1013 12.434 20.396 10.153 1.00 29.89 O ANISOU 1896 OG1 THR A1013 3022 6173 2163 -123 -735 -306 O ATOM 1897 CG2 THR A1013 13.808 19.260 8.529 1.00 27.87 C ANISOU 1897 CG2 THR A1013 2704 5947 1938 -52 -725 -223 C ATOM 1898 N GLY A1014 11.034 17.343 11.439 1.00 34.74 N ANISOU 1898 N GLY A1014 3870 6741 2587 -23 -701 -185 N ATOM 1899 CA GLY A1014 10.256 17.189 12.653 1.00 35.35 C ANISOU 1899 CA GLY A1014 4014 6851 2566 -58 -686 -201 C ATOM 1900 C GLY A1014 8.904 16.536 12.441 1.00 36.39 C ANISOU 1900 C GLY A1014 4207 6959 2661 -119 -626 -173 C ATOM 1901 O GLY A1014 8.613 16.016 11.364 1.00 36.00 O ANISOU 1901 O GLY A1014 4176 6846 2656 -124 -610 -130 O ATOM 1902 N SER A1015 8.080 16.561 13.484 1.00 36.43 N ANISOU 1902 N SER A1015 4238 7033 2573 -177 -591 -202 N ATOM 1903 CA SER A1015 6.730 16.017 13.420 1.00 36.39 C ANISOU 1903 CA SER A1015 4258 7057 2510 -270 -519 -190 C ATOM 1904 C SER A1015 5.758 17.084 12.937 1.00 29.68 C ANISOU 1904 C SER A1015 3237 6295 1744 -305 -465 -281 C ATOM 1905 O SER A1015 6.056 18.275 13.008 1.00 29.45 O ANISOU 1905 O SER A1015 3119 6291 1780 -258 -487 -360 O ATOM 1906 CB SER A1015 6.301 15.486 14.787 1.00 37.96 C ANISOU 1906 CB SER A1015 4562 7314 2546 -332 -496 -181 C ATOM 1907 OG SER A1015 6.353 16.510 15.766 1.00 39.75 O ANISOU 1907 OG SER A1015 4699 7647 2757 -320 -493 -271 O ATOM 1908 N ARG A1016 4.596 16.659 12.452 1.00 35.79 N ANISOU 1908 N ARG A1016 3982 7115 2503 -385 -404 -278 N ATOM 1909 CA ARG A1016 3.633 17.601 11.892 1.00 37.19 C ANISOU 1909 CA ARG A1016 3998 7385 2749 -389 -366 -373 C ATOM 1910 C ARG A1016 3.080 18.559 12.943 1.00 40.14 C ANISOU 1910 C ARG A1016 4272 7909 3071 -377 -340 -497 C ATOM 1911 O ARG A1016 3.030 19.765 12.717 1.00 40.99 O ANISOU 1911 O ARG A1016 4300 8027 3248 -295 -367 -594 O ATOM 1912 CB ARG A1016 2.475 16.867 11.216 1.00 36.00 C ANISOU 1912 CB ARG A1016 3815 7289 2575 -489 -308 -352 C ATOM 1913 CG ARG A1016 1.517 17.817 10.518 1.00 29.34 C ANISOU 1913 CG ARG A1016 2802 6546 1801 -457 -285 -460 C ATOM 1914 CD ARG A1016 0.377 17.098 9.829 1.00 29.68 C ANISOU 1914 CD ARG A1016 2786 6674 1815 -567 -231 -448 C ATOM 1915 NE ARG A1016 -0.419 18.032 9.038 1.00 29.92 N ANISOU 1915 NE ARG A1016 2664 6786 1916 -492 -229 -556 N ATOM 1916 CZ ARG A1016 -0.181 18.314 7.761 1.00 28.75 C ANISOU 1916 CZ ARG A1016 2541 6504 1878 -420 -276 -532 C ATOM 1917 NH1 ARG A1016 0.825 17.728 7.128 1.00 27.13 N ANISOU 1917 NH1 ARG A1016 2474 6107 1725 -422 -317 -412 N ATOM 1918 NH2 ARG A1016 -0.951 19.179 7.114 1.00 28.75 N ANISOU 1918 NH2 ARG A1016 2434 6564 1927 -333 -290 -635 N ATOM 1919 N ASP A1017 2.666 18.021 14.087 1.00 45.26 N ANISOU 1919 N ASP A1017 4948 8662 3586 -456 -294 -497 N ATOM 1920 CA ASP A1017 2.083 18.839 15.147 1.00 50.76 C ANISOU 1920 CA ASP A1017 5547 9527 4214 -444 -260 -623 C ATOM 1921 C ASP A1017 3.073 19.870 15.682 1.00 51.39 C ANISOU 1921 C ASP A1017 5654 9543 4329 -334 -333 -678 C ATOM 1922 O ASP A1017 2.675 20.937 16.152 1.00 50.40 O ANISOU 1922 O ASP A1017 5445 9509 4194 -272 -335 -812 O ATOM 1923 CB ASP A1017 1.584 17.955 16.291 1.00 58.94 C ANISOU 1923 CB ASP A1017 6638 10672 5085 -574 -196 -593 C ATOM 1924 CG ASP A1017 2.694 17.139 16.921 1.00 66.23 C ANISOU 1924 CG ASP A1017 7775 11449 5940 -579 -247 -473 C ATOM 1925 OD1 ASP A1017 3.650 16.785 16.199 1.00 72.04 O ANISOU 1925 OD1 ASP A1017 8607 12012 6751 -515 -316 -388 O ATOM 1926 OD2 ASP A1017 2.610 16.853 18.135 1.00 69.84 O ANISOU 1926 OD2 ASP A1017 8306 11972 6260 -634 -222 -472 O ATOM 1927 N GLU A1018 4.361 19.554 15.610 1.00 52.37 N ANISOU 1927 N GLU A1018 5896 9518 4486 -308 -400 -584 N ATOM 1928 CA GLU A1018 5.384 20.480 16.078 1.00 56.66 C ANISOU 1928 CA GLU A1018 6459 10011 5056 -238 -474 -630 C ATOM 1929 C GLU A1018 5.658 21.547 15.024 1.00 31.47 C ANISOU 1929 C GLU A1018 3224 6734 2000 -181 -525 -678 C ATOM 1930 O GLU A1018 6.038 22.672 15.352 1.00 31.93 O ANISOU 1930 O GLU A1018 3284 6773 2074 -143 -582 -764 O ATOM 1931 CB GLU A1018 6.671 19.739 16.436 1.00 61.84 C ANISOU 1931 CB GLU A1018 7231 10581 5682 -229 -531 -528 C ATOM 1932 CG GLU A1018 7.602 20.546 17.325 1.00 69.06 C ANISOU 1932 CG GLU A1018 8160 11504 6577 -191 -598 -583 C ATOM 1933 CD GLU A1018 8.803 19.751 17.792 1.00 76.72 C ANISOU 1933 CD GLU A1018 9227 12430 7495 -167 -660 -497 C ATOM 1934 OE1 GLU A1018 9.053 18.665 17.227 1.00 82.59 O ANISOU 1934 OE1 GLU A1018 10036 13105 8238 -155 -664 -397 O ATOM 1935 OE2 GLU A1018 9.494 20.214 18.725 1.00 78.09 O ANISOU 1935 OE2 GLU A1018 9416 12637 7617 -148 -713 -537 O ATOM 1936 N ARG A1019 5.464 21.190 13.758 1.00 33.27 N ANISOU 1936 N ARG A1019 3436 6895 2310 -188 -513 -621 N ATOM 1937 CA ARG A1019 5.546 22.168 12.682 1.00 29.60 C ANISOU 1937 CA ARG A1019 2951 6340 1955 -148 -561 -661 C ATOM 1938 C ARG A1019 4.363 23.121 12.780 1.00 30.41 C ANISOU 1938 C ARG A1019 2986 6522 2045 -94 -555 -802 C ATOM 1939 O ARG A1019 4.483 24.309 12.484 1.00 39.96 O ANISOU 1939 O ARG A1019 4225 7658 3300 -41 -631 -882 O ATOM 1940 CB ARG A1019 5.574 21.485 11.313 1.00 28.33 C ANISOU 1940 CB ARG A1019 2795 6095 1872 -165 -547 -566 C ATOM 1941 CG ARG A1019 6.823 20.655 11.057 1.00 32.64 C ANISOU 1941 CG ARG A1019 3402 6563 2435 -176 -569 -452 C ATOM 1942 CD ARG A1019 6.967 20.296 9.586 1.00 26.61 C ANISOU 1942 CD ARG A1019 2644 5708 1757 -176 -569 -385 C ATOM 1943 NE ARG A1019 5.855 19.489 9.093 1.00 26.33 N ANISOU 1943 NE ARG A1019 2600 5697 1708 -203 -514 -358 N ATOM 1944 CZ ARG A1019 5.841 18.160 9.082 1.00 26.34 C ANISOU 1944 CZ ARG A1019 2665 5686 1656 -232 -491 -275 C ATOM 1945 NH1 ARG A1019 6.881 17.478 9.544 1.00 27.65 N ANISOU 1945 NH1 ARG A1019 2913 5813 1780 -203 -524 -216 N ATOM 1946 NH2 ARG A1019 4.786 17.510 8.610 1.00 26.31 N ANISOU 1946 NH2 ARG A1019 2656 5709 1631 -287 -446 -258 N ATOM 1947 N LYS A1020 3.220 22.593 13.206 1.00 31.13 N ANISOU 1947 N LYS A1020 2994 6772 2061 -110 -473 -840 N ATOM 1948 CA LYS A1020 2.031 23.407 13.402 1.00 32.31 C ANISOU 1948 CA LYS A1020 3041 7056 2181 -31 -459 -1000 C ATOM 1949 C LYS A1020 2.229 24.341 14.586 1.00 33.66 C ANISOU 1949 C LYS A1020 3235 7267 2288 30 -498 -1118 C ATOM 1950 O LYS A1020 1.893 25.520 14.517 1.00 34.47 O ANISOU 1950 O LYS A1020 3338 7354 2406 145 -562 -1257 O ATOM 1951 CB LYS A1020 0.794 22.534 13.621 1.00 33.11 C ANISOU 1951 CB LYS A1020 3013 7367 2199 -94 -351 -1015 C ATOM 1952 CG LYS A1020 -0.499 23.330 13.718 1.00 34.61 C ANISOU 1952 CG LYS A1020 3046 7748 2357 13 -333 -1202 C ATOM 1953 CD LYS A1020 -1.714 22.428 13.829 1.00 35.62 C ANISOU 1953 CD LYS A1020 3010 8124 2401 -90 -223 -1215 C ATOM 1954 CE LYS A1020 -1.771 21.723 15.172 1.00 39.05 C ANISOU 1954 CE LYS A1020 3443 8694 2702 -226 -149 -1185 C ATOM 1955 NZ LYS A1020 -2.997 20.885 15.296 1.00 40.55 N ANISOU 1955 NZ LYS A1020 3475 9136 2796 -376 -48 -1202 N ATOM 1956 N LYS A1021 2.780 23.802 15.670 1.00 34.16 N ANISOU 1956 N LYS A1021 3340 7368 2270 -38 -471 -1066 N ATOM 1957 CA LYS A1021 3.050 24.591 16.866 1.00 35.44 C ANISOU 1957 CA LYS A1021 3538 7567 2360 5 -507 -1168 C ATOM 1958 C LYS A1021 4.028 25.720 16.551 1.00 36.45 C ANISOU 1958 C LYS A1021 3776 7514 2561 47 -631 -1199 C ATOM 1959 O LYS A1021 3.816 26.871 16.946 1.00 36.40 O ANISOU 1959 O LYS A1021 3801 7500 2530 130 -693 -1343 O ATOM 1960 CB LYS A1021 3.601 23.698 17.980 1.00 35.88 C ANISOU 1960 CB LYS A1021 3647 7670 2316 -84 -471 -1081 C ATOM 1961 CG LYS A1021 3.498 24.296 19.373 1.00 37.67 C ANISOU 1961 CG LYS A1021 3882 7999 2431 -52 -473 -1196 C ATOM 1962 CD LYS A1021 3.903 23.283 20.432 1.00 39.34 C ANISOU 1962 CD LYS A1021 4161 8259 2526 -143 -436 -1099 C ATOM 1963 CE LYS A1021 3.650 23.813 21.835 1.00 41.56 C ANISOU 1963 CE LYS A1021 4447 8666 2679 -120 -423 -1215 C ATOM 1964 NZ LYS A1021 4.413 25.063 22.101 1.00 42.11 N ANISOU 1964 NZ LYS A1021 4580 8639 2781 -41 -530 -1310 N ATOM 1965 N SER A1022 5.090 25.382 15.824 1.00 35.70 N ANISOU 1965 N SER A1022 3743 7276 2545 -16 -672 -1068 N ATOM 1966 CA SER A1022 6.086 26.363 15.409 1.00 36.25 C ANISOU 1966 CA SER A1022 3909 7188 2676 -29 -787 -1077 C ATOM 1967 C SER A1022 5.469 27.434 14.519 1.00 38.53 C ANISOU 1967 C SER A1022 4232 7389 3019 37 -856 -1172 C ATOM 1968 O SER A1022 5.719 28.626 14.704 1.00 40.24 O ANISOU 1968 O SER A1022 4553 7517 3221 56 -962 -1270 O ATOM 1969 CB SER A1022 7.241 25.678 14.677 1.00 32.42 C ANISOU 1969 CB SER A1022 3441 6617 2261 -106 -798 -925 C ATOM 1970 OG SER A1022 8.206 26.625 14.252 1.00 32.61 O ANISOU 1970 OG SER A1022 3538 6522 2331 -154 -903 -934 O ATOM 1971 N LEU A1023 4.662 26.999 13.556 1.00 38.39 N ANISOU 1971 N LEU A1023 4146 7387 3052 71 -809 -1146 N ATOM 1972 CA LEU A1023 3.994 27.909 12.633 1.00 33.45 C ANISOU 1972 CA LEU A1023 3555 6681 2473 159 -884 -1232 C ATOM 1973 C LEU A1023 3.113 28.903 13.378 1.00 38.68 C ANISOU 1973 C LEU A1023 4221 7412 3065 306 -924 -1433 C ATOM 1974 O LEU A1023 3.240 30.115 13.203 1.00 40.48 O ANISOU 1974 O LEU A1023 4586 7500 3293 365 -1053 -1530 O ATOM 1975 CB LEU A1023 3.152 27.126 11.625 1.00 32.46 C ANISOU 1975 CB LEU A1023 3329 6605 2398 181 -813 -1179 C ATOM 1976 CG LEU A1023 2.509 27.965 10.522 1.00 40.90 C ANISOU 1976 CG LEU A1023 4438 7582 3520 283 -903 -1251 C ATOM 1977 CD1 LEU A1023 3.586 28.590 9.650 1.00 39.71 C ANISOU 1977 CD1 LEU A1023 4451 7208 3430 198 -1020 -1172 C ATOM 1978 CD2 LEU A1023 1.552 27.129 9.686 1.00 41.39 C ANISOU 1978 CD2 LEU A1023 4375 7736 3616 307 -823 -1216 C ATOM 1979 N LEU A1024 2.225 28.374 14.213 1.00 39.20 N ANISOU 1979 N LEU A1024 4142 7694 3057 360 -817 -1499 N ATOM 1980 CA LEU A1024 1.285 29.190 14.971 1.00 42.98 C ANISOU 1980 CA LEU A1024 4578 8293 3459 527 -833 -1707 C ATOM 1981 C LEU A1024 1.991 30.156 15.912 1.00 47.25 C ANISOU 1981 C LEU A1024 5271 8737 3944 538 -923 -1789 C ATOM 1982 O LEU A1024 1.611 31.323 16.008 1.00 47.62 O ANISOU 1982 O LEU A1024 5407 8718 3968 692 -1025 -1956 O ATOM 1983 CB LEU A1024 0.330 28.299 15.766 1.00 42.50 C ANISOU 1983 CB LEU A1024 4314 8522 3310 525 -685 -1740 C ATOM 1984 CG LEU A1024 -0.640 27.469 14.926 1.00 38.37 C ANISOU 1984 CG LEU A1024 3624 8140 2815 515 -599 -1705 C ATOM 1985 CD1 LEU A1024 -1.468 26.554 15.812 1.00 41.93 C ANISOU 1985 CD1 LEU A1024 3889 8886 3155 440 -456 -1722 C ATOM 1986 CD2 LEU A1024 -1.533 28.377 14.098 1.00 39.32 C ANISOU 1986 CD2 LEU A1024 3706 8257 2977 724 -680 -1860 C ATOM 1987 N SER A1025 3.016 29.674 16.608 1.00 50.46 N ANISOU 1987 N SER A1025 5720 9131 4324 389 -898 -1680 N ATOM 1988 CA SER A1025 3.746 30.531 17.533 1.00 54.92 C ANISOU 1988 CA SER A1025 6424 9615 4826 373 -984 -1752 C ATOM 1989 C SER A1025 4.529 31.598 16.771 1.00 52.13 C ANISOU 1989 C SER A1025 6270 9012 4526 328 -1143 -1755 C ATOM 1990 O SER A1025 4.789 32.679 17.298 1.00 53.83 O ANISOU 1990 O SER A1025 6640 9127 4686 351 -1249 -1873 O ATOM 1991 CB SER A1025 4.686 29.709 18.417 1.00 59.00 C ANISOU 1991 CB SER A1025 6929 10189 5298 232 -931 -1631 C ATOM 1992 OG SER A1025 5.798 29.228 17.684 1.00 62.40 O ANISOU 1992 OG SER A1025 7395 10503 5809 101 -959 -1463 O ATOM 1993 N LYS A1026 4.900 31.292 15.531 1.00 50.27 N ANISOU 1993 N LYS A1026 6043 8673 4385 248 -1162 -1627 N ATOM 1994 CA LYS A1026 5.631 32.244 14.702 1.00 50.04 C ANISOU 1994 CA LYS A1026 6203 8420 4390 163 -1309 -1614 C ATOM 1995 C LYS A1026 4.731 33.409 14.294 1.00 49.92 C ANISOU 1995 C LYS A1026 6315 8291 4360 332 -1416 -1783 C ATOM 1996 O LYS A1026 5.204 34.525 14.076 1.00 49.36 O ANISOU 1996 O LYS A1026 6470 8022 4264 282 -1561 -1840 O ATOM 1997 CB LYS A1026 6.202 31.547 13.464 1.00 50.84 C ANISOU 1997 CB LYS A1026 6264 8466 4586 43 -1289 -1435 C ATOM 1998 CG LYS A1026 7.216 32.369 12.685 1.00 53.31 C ANISOU 1998 CG LYS A1026 6756 8585 4915 -114 -1429 -1390 C ATOM 1999 CD LYS A1026 8.045 31.477 11.772 1.00 53.62 C ANISOU 1999 CD LYS A1026 6707 8630 5036 -237 -1379 -1209 C ATOM 2000 CE LYS A1026 8.982 32.288 10.893 1.00 56.60 C ANISOU 2000 CE LYS A1026 7241 8844 5420 -400 -1513 -1173 C ATOM 2001 NZ LYS A1026 8.234 33.070 9.870 1.00 60.12 N ANISOU 2001 NZ LYS A1026 7836 9146 5859 -367 -1607 -1223 N ATOM 2002 N PHE A1027 3.431 33.144 14.202 1.00 49.78 N ANISOU 2002 N PHE A1027 6159 8403 4351 536 -1350 -1871 N ATOM 2003 CA PHE A1027 2.458 34.173 13.852 1.00 52.35 C ANISOU 2003 CA PHE A1027 6579 8644 4667 774 -1455 -2051 C ATOM 2004 C PHE A1027 1.857 34.817 15.098 1.00 55.02 C ANISOU 2004 C PHE A1027 6925 9068 4913 960 -1465 -2255 C ATOM 2005 O PHE A1027 0.969 35.665 15.004 1.00 56.61 O ANISOU 2005 O PHE A1027 7189 9224 5096 1218 -1552 -2434 O ATOM 2006 CB PHE A1027 1.346 33.588 12.981 1.00 55.76 C ANISOU 2006 CB PHE A1027 6834 9196 5157 918 -1394 -2052 C ATOM 2007 CG PHE A1027 1.823 33.076 11.654 1.00 54.54 C ANISOU 2007 CG PHE A1027 6696 8934 5092 769 -1400 -1870 C ATOM 2008 CD1 PHE A1027 2.877 33.689 10.996 1.00 54.83 C ANISOU 2008 CD1 PHE A1027 6957 8727 5147 609 -1521 -1785 C ATOM 2009 CD2 PHE A1027 1.219 31.979 11.065 1.00 55.77 C ANISOU 2009 CD2 PHE A1027 6647 9245 5299 768 -1281 -1786 C ATOM 2010 CE1 PHE A1027 3.316 33.218 9.773 1.00 54.10 C ANISOU 2010 CE1 PHE A1027 6868 8562 5125 472 -1520 -1622 C ATOM 2011 CE2 PHE A1027 1.654 31.504 9.844 1.00 54.59 C ANISOU 2011 CE2 PHE A1027 6520 8993 5228 641 -1284 -1622 C ATOM 2012 CZ PHE A1027 2.704 32.122 9.197 1.00 53.68 C ANISOU 2012 CZ PHE A1027 6614 8648 5133 502 -1403 -1540 C ATOM 2013 N GLY A1028 2.342 34.404 16.265 1.00 55.06 N ANISOU 2013 N GLY A1028 6869 9197 4854 848 -1382 -2230 N ATOM 2014 CA GLY A1028 1.885 34.965 17.522 1.00 58.74 C ANISOU 2014 CA GLY A1028 7342 9755 5220 995 -1382 -2412 C ATOM 2015 C GLY A1028 0.626 34.311 18.058 1.00 61.20 C ANISOU 2015 C GLY A1028 7378 10385 5489 1159 -1240 -2501 C ATOM 2016 O GLY A1028 -0.035 34.854 18.943 1.00 67.20 O ANISOU 2016 O GLY A1028 8113 11255 6166 1340 -1243 -2684 O ATOM 2017 N MET A1029 0.291 33.141 17.524 1.00 57.85 N ANISOU 2017 N MET A1029 6747 10121 5113 1080 -1116 -2375 N ATOM 2018 CA MET A1029 -0.886 32.409 17.976 1.00 55.85 C ANISOU 2018 CA MET A1029 6215 10199 4805 1165 -971 -2441 C ATOM 2019 C MET A1029 -0.493 31.156 18.752 1.00 54.67 C ANISOU 2019 C MET A1029 5954 10214 4606 940 -820 -2289 C ATOM 2020 O MET A1029 0.646 30.696 18.674 1.00 51.53 O ANISOU 2020 O MET A1029 5664 9674 4242 748 -825 -2115 O ATOM 2021 CB MET A1029 -1.775 32.035 16.789 1.00 53.36 C ANISOU 2021 CB MET A1029 5751 9963 4560 1250 -950 -2436 C ATOM 2022 CG MET A1029 -2.425 33.225 16.103 1.00 53.67 C ANISOU 2022 CG MET A1029 5879 9883 4630 1536 -1106 -2613 C ATOM 2023 SD MET A1029 -3.346 32.762 14.624 1.00 79.04 S ANISOU 2023 SD MET A1029 8931 13173 7926 1625 -1099 -2591 S ATOM 2024 CE MET A1029 -2.028 32.122 13.595 1.00 91.73 C ANISOU 2024 CE MET A1029 10705 14509 9639 1320 -1103 -2306 C ATOM 2025 N ASP A1030 -1.442 30.613 19.505 1.00 57.44 N ANISOU 2025 N ASP A1030 7394 9781 4651 -184 -285 -2374 N ATOM 2026 CA ASP A1030 -1.212 29.389 20.260 1.00 58.41 C ANISOU 2026 CA ASP A1030 7274 10166 4755 -152 -283 -2229 C ATOM 2027 C ASP A1030 -1.772 28.192 19.502 1.00 51.79 C ANISOU 2027 C ASP A1030 6299 9331 4049 -27 -260 -2014 C ATOM 2028 O ASP A1030 -2.432 28.360 18.477 1.00 49.27 O ANISOU 2028 O ASP A1030 6056 8838 3826 37 -249 -1990 O ATOM 2029 CB ASP A1030 -1.839 29.489 21.651 1.00 66.77 C ANISOU 2029 CB ASP A1030 8321 11354 5696 -101 -241 -2335 C ATOM 2030 CG ASP A1030 -1.177 30.550 22.513 1.00 76.08 C ANISOU 2030 CG ASP A1030 9614 12564 6729 -243 -260 -2547 C ATOM 2031 OD1 ASP A1030 0.043 30.766 22.355 1.00 82.71 O ANISOU 2031 OD1 ASP A1030 10432 13454 7542 -397 -316 -2562 O ATOM 2032 OD2 ASP A1030 -1.875 31.167 23.346 1.00 78.51 O ANISOU 2032 OD2 ASP A1030 10028 12854 6949 -208 -213 -2707 O ATOM 2033 N GLU A1031 -1.501 26.990 20.005 1.00 49.36 N ANISOU 2033 N GLU A1031 5795 9225 3736 6 -250 -1868 N ATOM 2034 CA GLU A1031 -1.975 25.765 19.369 1.00 39.67 C ANISOU 2034 CA GLU A1031 4428 8023 2621 110 -218 -1680 C ATOM 2035 C GLU A1031 -3.488 25.772 19.186 1.00 43.26 C ANISOU 2035 C GLU A1031 4928 8376 3133 235 -170 -1692 C ATOM 2036 O GLU A1031 -4.229 26.281 20.027 1.00 45.29 O ANISOU 2036 O GLU A1031 5244 8649 3316 278 -141 -1815 O ATOM 2037 CB GLU A1031 -1.554 24.538 20.179 1.00 70.28 C ANISOU 2037 CB GLU A1031 8101 12158 6443 142 -203 -1562 C ATOM 2038 CG GLU A1031 -0.179 23.996 19.822 1.00 68.31 C ANISOU 2038 CG GLU A1031 7741 12014 6201 74 -232 -1459 C ATOM 2039 CD GLU A1031 0.225 22.818 20.690 1.00 66.69 C ANISOU 2039 CD GLU A1031 7360 12061 5919 134 -216 -1344 C ATOM 2040 OE1 GLU A1031 0.134 22.937 21.931 1.00 68.20 O ANISOU 2040 OE1 GLU A1031 7531 12407 5975 142 -218 -1417 O ATOM 2041 OE2 GLU A1031 0.626 21.774 20.132 1.00 65.96 O ANISOU 2041 OE2 GLU A1031 7166 12004 5890 178 -198 -1182 O ATOM 2042 N GLY A1032 -3.931 25.211 18.068 1.00 41.22 N ANISOU 2042 N GLY A1032 4634 8026 3002 289 -157 -1571 N ATOM 2043 CA GLY A1032 -5.338 25.169 17.726 1.00 38.83 C ANISOU 2043 CA GLY A1032 4342 7651 2759 404 -118 -1574 C ATOM 2044 C GLY A1032 -5.494 24.583 16.339 1.00 36.76 C ANISOU 2044 C GLY A1032 4042 7296 2630 423 -121 -1437 C ATOM 2045 O GLY A1032 -4.523 24.502 15.587 1.00 35.76 O ANISOU 2045 O GLY A1032 3932 7111 2546 343 -152 -1370 O ATOM 2046 N VAL A1033 -6.709 24.171 15.999 1.00 35.69 N ANISOU 2046 N VAL A1033 3848 7159 2553 519 -88 -1402 N ATOM 2047 CA VAL A1033 -6.958 23.558 14.701 1.00 32.99 C ANISOU 2047 CA VAL A1033 3460 6748 2326 531 -88 -1278 C ATOM 2048 C VAL A1033 -6.797 24.580 13.586 1.00 33.60 C ANISOU 2048 C VAL A1033 3675 6657 2435 525 -130 -1337 C ATOM 2049 O VAL A1033 -7.627 25.473 13.418 1.00 31.97 O ANISOU 2049 O VAL A1033 3533 6407 2206 622 -140 -1462 O ATOM 2050 CB VAL A1033 -8.353 22.935 14.636 1.00 32.98 C ANISOU 2050 CB VAL A1033 3354 6818 2361 623 -52 -1249 C ATOM 2051 CG1 VAL A1033 -8.549 22.226 13.307 1.00 28.78 C ANISOU 2051 CG1 VAL A1033 2769 6232 1935 611 -53 -1123 C ATOM 2052 CG2 VAL A1033 -8.528 21.967 15.789 1.00 34.05 C ANISOU 2052 CG2 VAL A1033 3371 7131 2434 622 -14 -1210 C ATOM 2053 N THR A1034 -5.720 24.432 12.824 1.00 31.04 N ANISOU 2053 N THR A1034 3391 6251 2153 424 -156 -1254 N ATOM 2054 CA THR A1034 -5.322 25.440 11.854 1.00 29.84 C ANISOU 2054 CA THR A1034 3396 5940 2003 383 -206 -1315 C ATOM 2055 C THR A1034 -5.933 25.217 10.472 1.00 30.40 C ANISOU 2055 C THR A1034 3462 5931 2159 434 -211 -1238 C ATOM 2056 O THR A1034 -5.778 24.155 9.867 1.00 28.83 O ANISOU 2056 O THR A1034 3168 5744 2041 397 -186 -1085 O ATOM 2057 CB THR A1034 -3.789 25.495 11.719 1.00 37.03 C ANISOU 2057 CB THR A1034 4357 6812 2903 230 -239 -1278 C ATOM 2058 OG1 THR A1034 -3.196 25.517 13.023 1.00 39.40 O ANISOU 2058 OG1 THR A1034 4617 7237 3117 187 -237 -1334 O ATOM 2059 CG2 THR A1034 -3.366 26.737 10.952 1.00 30.54 C ANISOU 2059 CG2 THR A1034 3739 5814 2050 161 -296 -1382 C ATOM 2060 N PHE A1035 -6.634 26.238 9.993 1.00 29.51 N ANISOU 2060 N PHE A1035 3460 5735 2018 528 -242 -1355 N ATOM 2061 CA PHE A1035 -7.186 26.266 8.647 1.00 29.92 C ANISOU 2061 CA PHE A1035 3529 5719 2121 593 -267 -1307 C ATOM 2062 C PHE A1035 -6.415 27.297 7.842 1.00 29.26 C ANISOU 2062 C PHE A1035 3667 5446 2003 517 -327 -1367 C ATOM 2063 O PHE A1035 -5.955 28.291 8.395 1.00 32.58 O ANISOU 2063 O PHE A1035 4245 5783 2350 475 -344 -1510 O ATOM 2064 CB PHE A1035 -8.676 26.611 8.670 1.00 29.84 C ANISOU 2064 CB PHE A1035 3461 5784 2093 808 -266 -1398 C ATOM 2065 CG PHE A1035 -9.508 25.650 9.463 1.00 35.96 C ANISOU 2065 CG PHE A1035 4027 6747 2889 856 -211 -1354 C ATOM 2066 CD1 PHE A1035 -9.597 25.759 10.841 1.00 37.09 C ANISOU 2066 CD1 PHE A1035 4147 6971 2975 864 -180 -1436 C ATOM 2067 CD2 PHE A1035 -10.209 24.640 8.829 1.00 35.52 C ANISOU 2067 CD2 PHE A1035 3815 6783 2899 874 -190 -1236 C ATOM 2068 CE1 PHE A1035 -10.363 24.873 11.572 1.00 36.91 C ANISOU 2068 CE1 PHE A1035 3958 7108 2958 890 -135 -1395 C ATOM 2069 CE2 PHE A1035 -10.977 23.753 9.552 1.00 35.85 C ANISOU 2069 CE2 PHE A1035 3693 6981 2949 884 -146 -1204 C ATOM 2070 CZ PHE A1035 -11.056 23.869 10.927 1.00 36.54 C ANISOU 2070 CZ PHE A1035 3770 7138 2976 894 -120 -1280 C ATOM 2071 N MET A1036 -6.267 27.072 6.543 1.00 27.97 N ANISOU 2071 N MET A1036 3534 5205 1888 482 -356 -1264 N ATOM 2072 CA MET A1036 -5.490 27.998 5.731 1.00 29.34 C ANISOU 2072 CA MET A1036 3933 5191 2024 383 -416 -1312 C ATOM 2073 C MET A1036 -6.054 28.190 4.333 1.00 29.23 C ANISOU 2073 C MET A1036 3983 5101 2023 471 -465 -1271 C ATOM 2074 O MET A1036 -6.368 27.231 3.636 1.00 27.51 O ANISOU 2074 O MET A1036 3627 4954 1872 473 -449 -1120 O ATOM 2075 CB MET A1036 -4.043 27.521 5.634 1.00 27.44 C ANISOU 2075 CB MET A1036 3696 4917 1811 164 -417 -1210 C ATOM 2076 CG MET A1036 -3.185 28.335 4.684 1.00 27.95 C ANISOU 2076 CG MET A1036 3980 4795 1844 28 -478 -1241 C ATOM 2077 SD MET A1036 -1.880 27.308 4.000 1.00 37.10 S ANISOU 2077 SD MET A1036 5042 5962 3093 -134 -476 -1053 S ATOM 2078 CE MET A1036 -2.828 25.833 3.648 1.00 54.60 C ANISOU 2078 CE MET A1036 7033 8299 5412 -22 -404 -882 C ATOM 2079 N PHE A1037 -6.172 29.448 3.931 1.00 30.96 N ANISOU 2079 N PHE A1037 4432 5156 2174 554 -521 -1413 N ATOM 2080 CA PHE A1037 -6.563 29.789 2.575 1.00 30.30 C ANISOU 2080 CA PHE A1037 4466 4967 2080 664 -593 -1376 C ATOM 2081 C PHE A1037 -5.343 30.287 1.817 1.00 34.65 C ANISOU 2081 C PHE A1037 5236 5318 2611 438 -629 -1370 C ATOM 2082 O PHE A1037 -4.511 30.990 2.376 1.00 34.47 O ANISOU 2082 O PHE A1037 5362 5181 2555 284 -608 -1497 O ATOM 2083 CB PHE A1037 -7.667 30.849 2.589 1.00 32.82 C ANISOU 2083 CB PHE A1037 4938 5190 2343 1004 -639 -1529 C ATOM 2084 CG PHE A1037 -7.957 31.454 1.243 1.00 33.66 C ANISOU 2084 CG PHE A1037 5277 5106 2408 1170 -738 -1496 C ATOM 2085 CD1 PHE A1037 -8.819 30.830 0.358 1.00 33.32 C ANISOU 2085 CD1 PHE A1037 5084 5217 2359 1322 -789 -1357 C ATOM 2086 CD2 PHE A1037 -7.381 32.658 0.871 1.00 35.60 C ANISOU 2086 CD2 PHE A1037 5891 4981 2655 1140 -759 -1562 C ATOM 2087 CE1 PHE A1037 -9.090 31.389 -0.877 1.00 35.05 C ANISOU 2087 CE1 PHE A1037 5477 5227 2614 1434 -858 -1232 C ATOM 2088 CE2 PHE A1037 -7.648 33.219 -0.362 1.00 36.61 C ANISOU 2088 CE2 PHE A1037 6215 4860 2835 1246 -809 -1421 C ATOM 2089 CZ PHE A1037 -8.503 32.584 -1.236 1.00 36.25 C ANISOU 2089 CZ PHE A1037 5990 4983 2800 1405 -867 -1251 C ATOM 2090 N ILE A1038 -5.218 29.901 0.555 1.00 34.33 N ANISOU 2090 N ILE A1038 5208 5248 2589 388 -673 -1226 N ATOM 2091 CA ILE A1038 -4.194 30.477 -0.306 1.00 37.13 C ANISOU 2091 CA ILE A1038 5796 5393 2920 198 -714 -1228 C ATOM 2092 C ILE A1038 -4.790 30.750 -1.672 1.00 34.07 C ANISOU 2092 C ILE A1038 5585 4851 2510 359 -808 -1130 C ATOM 2093 O ILE A1038 -5.268 29.834 -2.342 1.00 32.30 O ANISOU 2093 O ILE A1038 5163 4795 2315 390 -813 -969 O ATOM 2094 CB ILE A1038 -2.962 29.564 -0.464 1.00 40.40 C ANISOU 2094 CB ILE A1038 6074 5902 3375 -130 -662 -1098 C ATOM 2095 CG1 ILE A1038 -2.167 29.497 0.841 1.00 49.48 C ANISOU 2095 CG1 ILE A1038 7192 7070 4536 -216 -632 -1157 C ATOM 2096 CG2 ILE A1038 -2.064 30.079 -1.580 1.00 41.13 C ANISOU 2096 CG2 ILE A1038 6302 5846 3480 -266 -698 -1101 C ATOM 2097 CD1 ILE A1038 -0.885 28.699 0.735 1.00 55.64 C ANISOU 2097 CD1 ILE A1038 7820 7901 5419 -321 -628 -1045 C ATOM 2098 N GLY A1039 -4.777 32.012 -2.084 1.00 35.49 N ANISOU 2098 N GLY A1039 6090 4677 2718 414 -821 -1158 N ATOM 2099 CA GLY A1039 -5.278 32.334 -3.407 1.00 35.89 C ANISOU 2099 CA GLY A1039 6286 4546 2802 535 -873 -989 C ATOM 2100 C GLY A1039 -5.463 33.810 -3.672 1.00 39.58 C ANISOU 2100 C GLY A1039 7145 4605 3290 677 -874 -1026 C ATOM 2101 O GLY A1039 -5.266 34.640 -2.788 1.00 41.28 O ANISOU 2101 O GLY A1039 7532 4655 3497 686 -822 -1207 O ATOM 2102 N ARG A1040 -5.839 34.133 -4.904 1.00 40.15 N ANISOU 2102 N ARG A1040 7375 4506 3375 789 -925 -852 N ATOM 2103 CA ARG A1040 -6.114 35.511 -5.276 1.00 40.22 C ANISOU 2103 CA ARG A1040 7785 4102 3393 975 -922 -846 C ATOM 2104 C ARG A1040 -7.336 36.010 -4.526 1.00 42.25 C ANISOU 2104 C ARG A1040 8025 4380 3649 1391 -926 -944 C ATOM 2105 O ARG A1040 -8.328 35.294 -4.397 1.00 42.23 O ANISOU 2105 O ARG A1040 7705 4708 3633 1616 -976 -909 O ATOM 2106 CB ARG A1040 -6.342 35.636 -6.781 1.00 53.32 C ANISOU 2106 CB ARG A1040 9589 5627 5044 1040 -987 -610 C ATOM 2107 CG ARG A1040 -5.552 34.649 -7.610 1.00 50.99 C ANISOU 2107 CG ARG A1040 9140 5494 4742 707 -1001 -481 C ATOM 2108 CD ARG A1040 -5.769 34.892 -9.090 1.00 52.62 C ANISOU 2108 CD ARG A1040 9528 5546 4920 765 -1061 -259 C ATOM 2109 NE ARG A1040 -7.110 34.534 -9.540 1.00 53.78 N ANISOU 2109 NE ARG A1040 9481 5920 5031 1115 -1159 -140 N ATOM 2110 CZ ARG A1040 -7.410 33.385 -10.137 1.00 52.33 C ANISOU 2110 CZ ARG A1040 8991 6075 4818 1055 -1208 -31 C ATOM 2111 NH1 ARG A1040 -6.461 32.485 -10.353 1.00 50.43 N ANISOU 2111 NH1 ARG A1040 8619 5954 4588 688 -1161 -16 N ATOM 2112 NH2 ARG A1040 -8.655 33.137 -10.519 1.00 52.59 N ANISOU 2112 NH2 ARG A1040 8844 6334 4803 1361 -1297 55 N ATOM 2113 N PHE A1041 -7.262 37.236 -4.026 1.00 45.25 N ANISOU 2113 N PHE A1041 8748 4408 4039 1483 -860 -1078 N ATOM 2114 CA PHE A1041 -8.409 37.834 -3.364 1.00 61.12 C ANISOU 2114 CA PHE A1041 10783 6391 6049 1906 -848 -1175 C ATOM 2115 C PHE A1041 -9.379 38.362 -4.412 1.00 63.90 C ANISOU 2115 C PHE A1041 11281 6597 6399 2294 -920 -983 C ATOM 2116 O PHE A1041 -9.315 39.524 -4.812 1.00 65.49 O ANISOU 2116 O PHE A1041 11914 6362 6607 2417 -883 -951 O ATOM 2117 CB PHE A1041 -7.967 38.939 -2.406 1.00 50.31 C ANISOU 2117 CB PHE A1041 9742 4689 4684 1858 -732 -1406 C ATOM 2118 CG PHE A1041 -7.247 38.426 -1.190 1.00 49.45 C ANISOU 2118 CG PHE A1041 9434 4806 4549 1557 -677 -1616 C ATOM 2119 CD1 PHE A1041 -7.358 37.098 -0.816 1.00 46.47 C ANISOU 2119 CD1 PHE A1041 8601 4906 4150 1481 -724 -1596 C ATOM 2120 CD2 PHE A1041 -6.462 39.267 -0.422 1.00 51.12 C ANISOU 2120 CD2 PHE A1041 9922 4759 4742 1345 -573 -1834 C ATOM 2121 CE1 PHE A1041 -6.702 36.618 0.301 1.00 44.89 C ANISOU 2121 CE1 PHE A1041 8225 4924 3907 1233 -680 -1766 C ATOM 2122 CE2 PHE A1041 -5.802 38.793 0.696 1.00 49.10 C ANISOU 2122 CE2 PHE A1041 9466 4752 4438 1077 -538 -2022 C ATOM 2123 CZ PHE A1041 -5.923 37.466 1.058 1.00 45.85 C ANISOU 2123 CZ PHE A1041 8599 4820 4001 1038 -596 -1977 C ATOM 2124 N ASP A1042 -10.272 37.484 -4.858 1.00 65.33 N ANISOU 2124 N ASP A1042 11104 7158 6559 2479 -1017 -853 N ATOM 2125 CA ASP A1042 -11.193 37.794 -5.944 1.00 70.08 C ANISOU 2125 CA ASP A1042 11763 7730 7133 2831 -1113 -650 C ATOM 2126 C ASP A1042 -12.647 37.811 -5.488 1.00 69.85 C ANISOU 2126 C ASP A1042 11491 7962 7085 3307 -1151 -694 C ATOM 2127 O ASP A1042 -13.018 37.135 -4.529 1.00 66.46 O ANISOU 2127 O ASP A1042 10725 7869 6656 3303 -1122 -842 O ATOM 2128 CB ASP A1042 -11.031 36.779 -7.079 1.00 72.57 C ANISOU 2128 CB ASP A1042 11865 8295 7415 2631 -1204 -448 C ATOM 2129 CG ASP A1042 -9.705 36.915 -7.801 1.00 76.93 C ANISOU 2129 CG ASP A1042 12695 8560 7976 2228 -1172 -366 C ATOM 2130 OD1 ASP A1042 -8.846 37.691 -7.334 1.00 83.09 O ANISOU 2130 OD1 ASP A1042 13792 8991 8787 2051 -1076 -484 O ATOM 2131 OD2 ASP A1042 -9.522 36.238 -8.836 1.00 73.89 O ANISOU 2131 OD2 ASP A1042 12204 8312 7558 2071 -1235 -195 O ATOM 2132 N ARG A1043 -13.463 38.589 -6.190 1.00 71.97 N ANISOU 2132 N ARG A1043 11933 8085 7328 3722 -1212 -561 N ATOM 2133 CA ARG A1043 -14.905 38.578 -5.983 1.00 72.34 C ANISOU 2133 CA ARG A1043 11709 8433 7344 4205 -1269 -570 C ATOM 2134 C ARG A1043 -15.584 37.742 -7.058 1.00 70.73 C ANISOU 2134 C ARG A1043 11176 8630 7067 4278 -1412 -370 C ATOM 2135 O ARG A1043 -15.987 38.263 -8.098 1.00 73.12 O ANISOU 2135 O ARG A1043 11638 8825 7318 4538 -1504 -174 O ATOM 2136 CB ARG A1043 -15.468 40.000 -5.992 1.00 76.17 C ANISOU 2136 CB ARG A1043 12573 8534 7833 4685 -1241 -558 C ATOM 2137 CG ARG A1043 -15.402 40.711 -4.656 1.00 63.73 C ANISOU 2137 CG ARG A1043 11170 6734 6311 4769 -1095 -817 C ATOM 2138 CD ARG A1043 -16.569 40.333 -3.753 1.00 72.10 C ANISOU 2138 CD ARG A1043 11802 8235 7359 5048 -1087 -959 C ATOM 2139 NE ARG A1043 -16.619 41.177 -2.562 1.00 74.40 N ANISOU 2139 NE ARG A1043 12265 8313 7688 5104 -938 -1172 N ATOM 2140 CZ ARG A1043 -17.550 41.090 -1.617 1.00 75.14 C ANISOU 2140 CZ ARG A1043 12057 8715 7778 5272 -893 -1306 C ATOM 2141 NH1 ARG A1043 -18.520 40.192 -1.716 1.00 74.63 N ANISOU 2141 NH1 ARG A1043 11503 9188 7665 5378 -974 -1264 N ATOM 2142 NH2 ARG A1043 -17.510 41.904 -0.570 1.00 76.69 N ANISOU 2142 NH2 ARG A1043 12441 8686 8014 5291 -755 -1485 N ATOM 2143 N GLY A1044 -15.696 36.442 -6.810 1.00 66.94 N ANISOU 2143 N GLY A1044 10252 8610 6572 4039 -1425 -420 N ATOM 2144 CA GLY A1044 -16.388 35.558 -7.728 1.00 65.33 C ANISOU 2144 CA GLY A1044 9703 8831 6290 4067 -1542 -272 C ATOM 2145 C GLY A1044 -15.484 34.583 -8.456 1.00 61.71 C ANISOU 2145 C GLY A1044 9185 8443 5819 3586 -1554 -169 C ATOM 2146 O GLY A1044 -15.789 34.169 -9.574 1.00 48.61 O ANISOU 2146 O GLY A1044 7396 6946 4129 3497 -1599 -21 O ATOM 2147 N GLN A1045 -14.370 34.218 -7.829 1.00 59.20 N ANISOU 2147 N GLN A1045 8933 7996 5565 3191 -1451 -274 N ATOM 2148 CA GLN A1045 -13.469 33.219 -8.398 1.00 55.16 C ANISOU 2148 CA GLN A1045 8342 7568 5050 2741 -1440 -197 C ATOM 2149 C GLN A1045 -12.900 32.298 -7.321 1.00 39.89 C ANISOU 2149 C GLN A1045 6196 5806 3156 2434 -1334 -357 C ATOM 2150 O GLN A1045 -13.327 31.151 -7.190 1.00 42.51 O ANISOU 2150 O GLN A1045 6169 6526 3455 2339 -1322 -374 O ATOM 2151 CB GLN A1045 -12.329 33.891 -9.170 1.00 55.21 C ANISOU 2151 CB GLN A1045 8769 7131 5077 2535 -1433 -84 C ATOM 2152 CG GLN A1045 -12.776 34.625 -10.427 1.00 58.63 C ANISOU 2152 CG GLN A1045 9426 7405 5446 2784 -1539 121 C ATOM 2153 CD GLN A1045 -11.628 34.951 -11.359 1.00 58.74 C ANISOU 2153 CD GLN A1045 9792 7068 5459 2488 -1523 253 C ATOM 2154 OE1 GLN A1045 -11.185 34.105 -12.136 1.00 56.34 O ANISOU 2154 OE1 GLN A1045 9369 6915 5123 2195 -1542 351 O ATOM 2155 NE2 GLN A1045 -11.140 36.185 -11.289 1.00 62.05 N ANISOU 2155 NE2 GLN A1045 10659 7010 5908 2552 -1474 248 N ATOM 2156 N LYS A1046 -11.939 32.803 -6.553 1.00 46.10 N ANISOU 2156 N LYS A1046 7210 6305 3999 2276 -1251 -473 N ATOM 2157 CA LYS A1046 -11.296 32.007 -5.512 1.00 43.13 C ANISOU 2157 CA LYS A1046 6661 6083 3644 1999 -1158 -612 C ATOM 2158 C LYS A1046 -12.127 31.972 -4.234 1.00 44.19 C ANISOU 2158 C LYS A1046 6596 6427 3769 2219 -1112 -791 C ATOM 2159 O LYS A1046 -11.862 31.178 -3.331 1.00 42.75 O ANISOU 2159 O LYS A1046 6213 6453 3578 2044 -1041 -895 O ATOM 2160 CB LYS A1046 -9.896 32.546 -5.218 1.00 42.85 C ANISOU 2160 CB LYS A1046 6921 5709 3651 1717 -1096 -674 C ATOM 2161 CG LYS A1046 -8.913 32.327 -6.352 1.00 41.17 C ANISOU 2161 CG LYS A1046 6844 5354 3444 1415 -1113 -520 C ATOM 2162 CD LYS A1046 -8.854 30.859 -6.737 1.00 32.26 C ANISOU 2162 CD LYS A1046 5389 4574 2293 1212 -1111 -435 C ATOM 2163 CE LYS A1046 -7.884 30.623 -7.881 1.00 32.45 C ANISOU 2163 CE LYS A1046 5541 4467 2320 918 -1115 -290 C ATOM 2164 NZ LYS A1046 -7.837 29.187 -8.272 1.00 29.91 N ANISOU 2164 NZ LYS A1046 4927 4460 1977 727 -1092 -215 N ATOM 2165 N GLY A1047 -13.127 32.844 -4.164 1.00 46.01 N ANISOU 2165 N GLY A1047 6890 6600 3992 2617 -1148 -821 N ATOM 2166 CA GLY A1047 -14.093 32.825 -3.082 1.00 49.22 C ANISOU 2166 CA GLY A1047 7081 7240 4380 2870 -1105 -983 C ATOM 2167 C GLY A1047 -13.550 33.145 -1.704 1.00 50.33 C ANISOU 2167 C GLY A1047 7316 7266 4540 2781 -1000 -1193 C ATOM 2168 O GLY A1047 -14.053 32.632 -0.705 1.00 41.33 O ANISOU 2168 O GLY A1047 5924 6410 3370 2824 -942 -1327 O ATOM 2169 N VAL A1048 -12.535 34.000 -1.639 1.00 42.60 N ANISOU 2169 N VAL A1048 6703 5886 3598 2642 -971 -1230 N ATOM 2170 CA VAL A1048 -11.994 34.424 -0.353 1.00 43.51 C ANISOU 2170 CA VAL A1048 6931 5886 3713 2547 -875 -1446 C ATOM 2171 C VAL A1048 -13.062 35.190 0.430 1.00 45.99 C ANISOU 2171 C VAL A1048 7263 6190 4020 2947 -834 -1599 C ATOM 2172 O VAL A1048 -13.066 35.186 1.662 1.00 46.20 O ANISOU 2172 O VAL A1048 7224 6310 4019 2928 -752 -1796 O ATOM 2173 CB VAL A1048 -10.727 35.293 -0.522 1.00 43.68 C ANISOU 2173 CB VAL A1048 7359 5472 3765 2303 -845 -1471 C ATOM 2174 CG1 VAL A1048 -11.050 36.582 -1.257 1.00 47.01 C ANISOU 2174 CG1 VAL A1048 8158 5485 4219 2569 -863 -1407 C ATOM 2175 CG2 VAL A1048 -10.089 35.585 0.830 1.00 44.04 C ANISOU 2175 CG2 VAL A1048 7476 5470 3786 2139 -750 -1709 C ATOM 2176 N ASP A1049 -13.980 35.826 -0.294 1.00 51.38 N ANISOU 2176 N ASP A1049 8024 6781 4717 3322 -890 -1505 N ATOM 2177 CA ASP A1049 -15.081 36.550 0.331 1.00 54.67 C ANISOU 2177 CA ASP A1049 8438 7205 5128 3759 -851 -1633 C ATOM 2178 C ASP A1049 -16.010 35.588 1.065 1.00 54.60 C ANISOU 2178 C ASP A1049 7964 7709 5071 3846 -830 -1723 C ATOM 2179 O ASP A1049 -16.534 35.911 2.134 1.00 56.38 O ANISOU 2179 O ASP A1049 8138 8002 5284 4020 -747 -1909 O ATOM 2180 CB ASP A1049 -15.861 37.357 -0.711 1.00 56.91 C ANISOU 2180 CB ASP A1049 8880 7317 5424 4170 -928 -1477 C ATOM 2181 CG ASP A1049 -16.277 36.524 -1.909 1.00 56.70 C ANISOU 2181 CG ASP A1049 8592 7584 5366 4165 -1056 -1251 C ATOM 2182 OD1 ASP A1049 -15.457 35.708 -2.381 1.00 53.39 O ANISOU 2182 OD1 ASP A1049 8111 7231 4945 3769 -1083 -1156 O ATOM 2183 OD2 ASP A1049 -17.424 36.685 -2.377 1.00 58.12 O ANISOU 2183 OD2 ASP A1049 8622 7945 5515 4560 -1127 -1174 O ATOM 2184 N VAL A1050 -16.207 34.405 0.489 1.00 51.70 N ANISOU 2184 N VAL A1050 7272 7698 4675 3694 -891 -1590 N ATOM 2185 CA VAL A1050 -17.001 33.367 1.134 1.00 50.01 C ANISOU 2185 CA VAL A1050 6626 7971 4405 3698 -852 -1669 C ATOM 2186 C VAL A1050 -16.338 32.955 2.442 1.00 45.41 C ANISOU 2186 C VAL A1050 6014 7442 3798 3429 -742 -1838 C ATOM 2187 O VAL A1050 -17.008 32.766 3.459 1.00 47.43 O ANISOU 2187 O VAL A1050 6060 7896 4065 3430 -690 -1903 O ATOM 2188 CB VAL A1050 -17.172 32.129 0.233 1.00 44.56 C ANISOU 2188 CB VAL A1050 5644 7607 3682 3507 -916 -1500 C ATOM 2189 CG1 VAL A1050 -18.087 31.112 0.897 1.00 43.94 C ANISOU 2189 CG1 VAL A1050 5143 8018 3536 3512 -852 -1593 C ATOM 2190 CG2 VAL A1050 -17.718 32.533 -1.126 1.00 46.99 C ANISOU 2190 CG2 VAL A1050 5991 7873 3992 3738 -1040 -1319 C ATOM 2191 N LEU A1051 -15.015 32.828 2.409 1.00 45.77 N ANISOU 2191 N LEU A1051 6249 7281 3860 3075 -737 -1807 N ATOM 2192 CA LEU A1051 -14.250 32.467 3.596 1.00 44.31 C ANISOU 2192 CA LEU A1051 6026 7123 3687 2761 -655 -1892 C ATOM 2193 C LEU A1051 -14.384 33.514 4.692 1.00 48.13 C ANISOU 2193 C LEU A1051 6671 7419 4199 2873 -584 -2058 C ATOM 2194 O LEU A1051 -14.705 33.188 5.831 1.00 48.62 O ANISOU 2194 O LEU A1051 6541 7662 4271 2798 -517 -2118 O ATOM 2195 CB LEU A1051 -12.773 32.279 3.257 1.00 41.12 C ANISOU 2195 CB LEU A1051 5799 6534 3289 2397 -669 -1831 C ATOM 2196 CG LEU A1051 -11.915 32.122 4.514 1.00 40.47 C ANISOU 2196 CG LEU A1051 5691 6440 3245 2089 -584 -1894 C ATOM 2197 CD1 LEU A1051 -12.202 30.793 5.198 1.00 37.24 C ANISOU 2197 CD1 LEU A1051 4913 6365 2872 1933 -529 -1802 C ATOM 2198 CD2 LEU A1051 -10.440 32.271 4.200 1.00 39.90 C ANISOU 2198 CD2 LEU A1051 5827 6154 3180 1769 -595 -1864 C ATOM 2199 N LEU A1052 -14.123 34.769 4.338 1.00 47.12 N ANISOU 2199 N LEU A1052 6919 6901 4085 3033 -589 -2124 N ATOM 2200 CA LEU A1052 -14.213 35.874 5.287 1.00 50.11 C ANISOU 2200 CA LEU A1052 7499 7045 4495 3121 -503 -2281 C ATOM 2201 C LEU A1052 -15.605 35.958 5.901 1.00 52.18 C ANISOU 2201 C LEU A1052 7534 7526 4766 3416 -470 -2322 C ATOM 2202 O LEU A1052 -15.751 36.095 7.120 1.00 53.85 O ANISOU 2202 O LEU A1052 7685 7798 4979 3346 -381 -2444 O ATOM 2203 CB LEU A1052 -13.851 37.191 4.599 1.00 56.30 C ANISOU 2203 CB LEU A1052 8746 7335 5311 3264 -505 -2297 C ATOM 2204 CG LEU A1052 -12.412 37.253 4.082 1.00 54.59 C ANISOU 2204 CG LEU A1052 8797 6864 5083 2913 -526 -2277 C ATOM 2205 CD1 LEU A1052 -12.196 38.462 3.189 1.00 57.55 C ANISOU 2205 CD1 LEU A1052 9638 6735 5493 3058 -532 -2239 C ATOM 2206 CD2 LEU A1052 -11.442 37.270 5.248 1.00 53.72 C ANISOU 2206 CD2 LEU A1052 8692 6756 4963 2526 -439 -2415 C ATOM 2207 N LYS A1053 -16.624 35.863 5.050 1.00 52.99 N ANISOU 2207 N LYS A1053 7501 7768 4865 3726 -544 -2214 N ATOM 2208 CA LYS A1053 -18.010 35.855 5.503 1.00 57.72 C ANISOU 2208 CA LYS A1053 7843 8632 5458 3975 -530 -2232 C ATOM 2209 C LYS A1053 -18.248 34.712 6.483 1.00 53.05 C ANISOU 2209 C LYS A1053 6893 8427 4835 3726 -488 -2263 C ATOM 2210 O LYS A1053 -18.931 34.879 7.495 1.00 54.80 O ANISOU 2210 O LYS A1053 7008 8758 5054 3784 -419 -2361 O ATOM 2211 CB LYS A1053 -18.965 35.732 4.314 1.00 58.87 C ANISOU 2211 CB LYS A1053 7846 8941 5582 4260 -636 -2081 C ATOM 2212 CG LYS A1053 -20.411 36.087 4.631 1.00 62.11 C ANISOU 2212 CG LYS A1053 8075 9548 5976 4553 -626 -2102 C ATOM 2213 CD LYS A1053 -20.523 37.560 4.970 1.00 66.01 C ANISOU 2213 CD LYS A1053 8904 9654 6524 4819 -559 -2182 C ATOM 2214 CE LYS A1053 -21.960 38.049 5.005 1.00 70.11 C ANISOU 2214 CE LYS A1053 9279 10334 7027 5172 -560 -2172 C ATOM 2215 NZ LYS A1053 -22.018 39.533 5.129 1.00 74.93 N ANISOU 2215 NZ LYS A1053 10259 10516 7696 5455 -491 -2217 N ATOM 2216 N ALA A1054 -17.673 33.553 6.177 1.00 49.55 N ANISOU 2216 N ALA A1054 6289 8166 4373 3441 -520 -2168 N ATOM 2217 CA ALA A1054 -17.825 32.370 7.017 1.00 47.60 C ANISOU 2217 CA ALA A1054 5738 8236 4112 3179 -478 -2149 C ATOM 2218 C ALA A1054 -17.159 32.565 8.375 1.00 49.28 C ANISOU 2218 C ALA A1054 6045 8341 4339 2975 -381 -2260 C ATOM 2219 O ALA A1054 -17.654 32.079 9.393 1.00 49.48 O ANISOU 2219 O ALA A1054 5882 8566 4350 2897 -325 -2294 O ATOM 2220 CB ALA A1054 -17.253 31.148 6.317 1.00 44.12 C ANISOU 2220 CB ALA A1054 5155 7940 3671 2916 -518 -1998 C ATOM 2221 N ILE A1055 -16.034 33.273 8.387 1.00 47.76 N ANISOU 2221 N ILE A1055 6153 7833 4159 2871 -362 -2318 N ATOM 2222 CA ILE A1055 -15.347 33.586 9.632 1.00 54.28 C ANISOU 2222 CA ILE A1055 7091 8557 4976 2669 -272 -2438 C ATOM 2223 C ILE A1055 -16.203 34.539 10.456 1.00 58.32 C ANISOU 2223 C ILE A1055 7671 9005 5483 2904 -195 -2599 C ATOM 2224 O ILE A1055 -16.308 34.396 11.676 1.00 52.37 O ANISOU 2224 O ILE A1055 6837 8359 4704 2797 -116 -2681 O ATOM 2225 CB ILE A1055 -13.957 34.207 9.384 1.00 53.50 C ANISOU 2225 CB ILE A1055 7309 8142 4877 2470 -270 -2479 C ATOM 2226 CG1 ILE A1055 -13.062 33.218 8.635 1.00 49.77 C ANISOU 2226 CG1 ILE A1055 6753 7746 4411 2212 -334 -2313 C ATOM 2227 CG2 ILE A1055 -13.305 34.607 10.698 1.00 54.77 C ANISOU 2227 CG2 ILE A1055 7577 8228 5004 2260 -174 -2621 C ATOM 2228 CD1 ILE A1055 -11.647 33.707 8.431 1.00 44.23 C ANISOU 2228 CD1 ILE A1055 6321 6785 3700 1956 -336 -2344 C ATOM 2229 N GLU A1056 -16.822 35.505 9.781 1.00 61.63 N ANISOU 2229 N GLU A1056 8247 9241 5930 3235 -215 -2629 N ATOM 2230 CA GLU A1056 -17.761 36.406 10.442 1.00 58.06 C ANISOU 2230 CA GLU A1056 7845 8726 5488 3501 -137 -2758 C ATOM 2231 C GLU A1056 -18.919 35.623 11.055 1.00 61.19 C ANISOU 2231 C GLU A1056 7877 9517 5856 3557 -126 -2743 C ATOM 2232 O GLU A1056 -19.398 35.957 12.138 1.00 63.68 O ANISOU 2232 O GLU A1056 8169 9868 6158 3596 -29 -2870 O ATOM 2233 CB GLU A1056 -18.291 37.456 9.464 1.00 76.01 C ANISOU 2233 CB GLU A1056 10329 10748 7804 3876 -172 -2733 C ATOM 2234 CG GLU A1056 -17.321 38.593 9.183 1.00 77.45 C ANISOU 2234 CG GLU A1056 10961 10444 8022 3846 -131 -2799 C ATOM 2235 CD GLU A1056 -17.950 39.709 8.370 1.00 81.08 C ANISOU 2235 CD GLU A1056 11660 10615 8531 4243 -143 -2754 C ATOM 2236 OE1 GLU A1056 -18.794 39.410 7.500 1.00 81.17 O ANISOU 2236 OE1 GLU A1056 11497 10806 8537 4499 -244 -2606 O ATOM 2237 OE2 GLU A1056 -17.605 40.886 8.608 1.00 84.61 O ANISOU 2237 OE2 GLU A1056 12471 10660 9017 4285 -47 -2859 O ATOM 2238 N ILE A1057 -19.362 34.579 10.361 1.00 58.55 N ANISOU 2238 N ILE A1057 7271 9471 5505 3535 -216 -2595 N ATOM 2239 CA ILE A1057 -20.406 33.704 10.885 1.00 57.82 C ANISOU 2239 CA ILE A1057 6841 9753 5376 3513 -207 -2575 C ATOM 2240 C ILE A1057 -19.901 32.955 12.116 1.00 56.44 C ANISOU 2240 C ILE A1057 6581 9682 5179 3190 -132 -2604 C ATOM 2241 O ILE A1057 -20.639 32.751 13.081 1.00 59.53 O ANISOU 2241 O ILE A1057 6829 10248 5542 3191 -66 -2671 O ATOM 2242 CB ILE A1057 -20.885 32.691 9.823 1.00 54.07 C ANISOU 2242 CB ILE A1057 6122 9546 4875 3490 -310 -2416 C ATOM 2243 CG1 ILE A1057 -21.518 33.423 8.639 1.00 56.90 C ANISOU 2243 CG1 ILE A1057 6543 9845 5232 3833 -389 -2373 C ATOM 2244 CG2 ILE A1057 -21.880 31.707 10.420 1.00 54.01 C ANISOU 2244 CG2 ILE A1057 5798 9902 4820 3389 -287 -2406 C ATOM 2245 CD1 ILE A1057 -21.964 32.506 7.522 1.00 54.56 C ANISOU 2245 CD1 ILE A1057 6029 9816 4886 3798 -487 -2230 C ATOM 2246 N LEU A1058 -18.631 32.566 12.084 1.00 51.73 N ANISOU 2246 N LEU A1058 6086 8976 4594 2920 -140 -2546 N ATOM 2247 CA LEU A1058 -18.040 31.809 13.180 1.00 54.17 C ANISOU 2247 CA LEU A1058 6327 9376 4880 2621 -81 -2535 C ATOM 2248 C LEU A1058 -17.542 32.698 14.316 1.00 57.18 C ANISOU 2248 C LEU A1058 6917 9579 5230 2579 14 -2703 C ATOM 2249 O LEU A1058 -17.007 32.196 15.296 1.00 55.32 O ANISOU 2249 O LEU A1058 6652 9412 4956 2351 61 -2701 O ATOM 2250 CB LEU A1058 -16.884 30.948 12.668 1.00 46.79 C ANISOU 2250 CB LEU A1058 5391 8420 3967 2350 -128 -2382 C ATOM 2251 CG LEU A1058 -17.242 29.802 11.722 1.00 44.56 C ANISOU 2251 CG LEU A1058 4890 8329 3712 2301 -195 -2208 C ATOM 2252 CD1 LEU A1058 -15.986 29.080 11.267 1.00 41.49 C ANISOU 2252 CD1 LEU A1058 4539 7864 3361 2042 -216 -2067 C ATOM 2253 CD2 LEU A1058 -18.211 28.838 12.390 1.00 45.28 C ANISOU 2253 CD2 LEU A1058 4729 8695 3781 2245 -161 -2175 C ATOM 2254 N SER A1059 -17.717 34.011 14.183 1.00 61.47 N ANISOU 2254 N SER A1059 7685 9885 5787 2798 48 -2843 N ATOM 2255 CA SER A1059 -17.228 34.956 15.188 1.00 65.81 C ANISOU 2255 CA SER A1059 8472 10230 6303 2741 155 -3025 C ATOM 2256 C SER A1059 -17.812 34.678 16.571 1.00 68.92 C ANISOU 2256 C SER A1059 8728 10820 6640 2698 247 -3106 C ATOM 2257 O SER A1059 -17.161 34.914 17.589 1.00 71.46 O ANISOU 2257 O SER A1059 9171 11079 6899 2518 322 -3206 O ATOM 2258 CB SER A1059 -17.544 36.392 14.769 1.00 67.64 C ANISOU 2258 CB SER A1059 8971 10153 6577 3022 197 -3154 C ATOM 2259 OG SER A1059 -16.904 36.714 13.547 1.00 66.53 O ANISOU 2259 OG SER A1059 9011 9787 6479 3044 118 -3082 O ATOM 2260 N SER A1060 -19.043 34.180 16.603 1.00 70.08 N ANISOU 2260 N SER A1060 8624 11210 6793 2853 239 -3066 N ATOM 2261 CA SER A1060 -19.646 33.736 17.851 1.00 69.71 C ANISOU 2261 CA SER A1060 8423 11375 6688 2791 320 -3121 C ATOM 2262 C SER A1060 -19.293 32.272 18.087 1.00 67.74 C ANISOU 2262 C SER A1060 7975 11349 6413 2519 276 -2956 C ATOM 2263 O SER A1060 -18.205 31.832 17.714 1.00 65.68 O ANISOU 2263 O SER A1060 7771 11021 6165 2324 221 -2848 O ATOM 2264 CB SER A1060 -21.162 33.935 17.827 1.00 69.97 C ANISOU 2264 CB SER A1060 8291 11562 6733 3071 346 -3172 C ATOM 2265 OG SER A1060 -21.771 33.133 16.831 1.00 67.65 O ANISOU 2265 OG SER A1060 7772 11468 6464 3122 241 -3021 O ATOM 2266 N LYS A1061 -20.210 31.530 18.707 1.00 68.07 N ANISOU 2266 N LYS A1061 7800 11640 6423 2506 310 -2937 N ATOM 2267 CA LYS A1061 -20.029 30.105 19.003 1.00 66.11 C ANISOU 2267 CA LYS A1061 7383 11579 6155 2265 291 -2782 C ATOM 2268 C LYS A1061 -18.871 29.838 19.969 1.00 63.65 C ANISOU 2268 C LYS A1061 7185 11210 5790 2030 326 -2767 C ATOM 2269 O LYS A1061 -17.939 30.633 20.083 1.00 63.98 O ANISOU 2269 O LYS A1061 7433 11061 5816 1995 332 -2843 O ATOM 2270 CB LYS A1061 -19.816 29.304 17.712 1.00 63.76 C ANISOU 2270 CB LYS A1061 6990 11314 5921 2204 186 -2600 C ATOM 2271 CG LYS A1061 -20.901 29.493 16.666 1.00 66.45 C ANISOU 2271 CG LYS A1061 7211 11745 6291 2424 130 -2598 C ATOM 2272 CD LYS A1061 -20.589 28.701 15.406 1.00 63.70 C ANISOU 2272 CD LYS A1061 6790 11426 5988 2334 33 -2425 C ATOM 2273 CE LYS A1061 -21.679 28.877 14.362 1.00 64.09 C ANISOU 2273 CE LYS A1061 6715 11599 6037 2548 -32 -2424 C ATOM 2274 NZ LYS A1061 -21.874 30.310 14.006 1.00 65.97 N ANISOU 2274 NZ LYS A1061 7106 11674 6287 2855 -44 -2543 N ATOM 2275 N LYS A1062 -18.939 28.711 20.668 1.00 63.57 N ANISOU 2275 N LYS A1062 7047 11364 5741 1867 351 -2671 N ATOM 2276 CA LYS A1062 -17.875 28.329 21.589 1.00 65.09 C ANISOU 2276 CA LYS A1062 7324 11537 5871 1666 373 -2632 C ATOM 2277 C LYS A1062 -16.663 27.831 20.813 1.00 61.23 C ANISOU 2277 C LYS A1062 6877 10953 5435 1525 290 -2472 C ATOM 2278 O LYS A1062 -15.519 28.012 21.231 1.00 60.21 O ANISOU 2278 O LYS A1062 6872 10743 5263 1404 281 -2473 O ATOM 2279 CB LYS A1062 -18.351 27.244 22.559 1.00 69.08 C ANISOU 2279 CB LYS A1062 7701 12230 6316 1560 431 -2568 C ATOM 2280 CG LYS A1062 -19.814 27.347 22.952 1.00 74.53 C ANISOU 2280 CG LYS A1062 8271 13066 6981 1689 503 -2673 C ATOM 2281 CD LYS A1062 -20.176 26.333 24.030 1.00 77.19 C ANISOU 2281 CD LYS A1062 8527 13563 7240 1560 578 -2625 C ATOM 2282 CE LYS A1062 -19.570 26.714 25.374 1.00 79.72 C ANISOU 2282 CE LYS A1062 8976 13867 7446 1497 640 -2718 C ATOM 2283 NZ LYS A1062 -20.140 25.913 26.494 1.00 82.16 N ANISOU 2283 NZ LYS A1062 9217 14340 7661 1418 730 -2708 N ATOM 2284 N GLU A1063 -16.933 27.212 19.670 1.00 58.71 N ANISOU 2284 N GLU A1063 6451 10655 5201 1539 232 -2340 N ATOM 2285 CA GLU A1063 -15.917 26.498 18.907 1.00 55.09 C ANISOU 2285 CA GLU A1063 6000 10129 4802 1400 171 -2167 C ATOM 2286 C GLU A1063 -14.855 27.393 18.266 1.00 54.69 C ANISOU 2286 C GLU A1063 6121 9885 4775 1396 121 -2203 C ATOM 2287 O GLU A1063 -13.753 26.931 17.969 1.00 55.39 O ANISOU 2287 O GLU A1063 6245 9913 4887 1252 86 -2086 O ATOM 2288 CB GLU A1063 -16.593 25.657 17.820 1.00 42.68 C ANISOU 2288 CB GLU A1063 4280 8629 3307 1414 133 -2038 C ATOM 2289 CG GLU A1063 -17.316 24.418 18.336 1.00 62.12 C ANISOU 2289 CG GLU A1063 6603 11250 5750 1323 183 -1954 C ATOM 2290 CD GLU A1063 -18.745 24.699 18.761 1.00 63.52 C ANISOU 2290 CD GLU A1063 6678 11577 5881 1447 229 -2080 C ATOM 2291 OE1 GLU A1063 -19.140 25.884 18.789 1.00 64.25 O ANISOU 2291 OE1 GLU A1063 6812 11646 5956 1624 228 -2236 O ATOM 2292 OE2 GLU A1063 -19.476 23.731 19.062 1.00 63.51 O ANISOU 2292 OE2 GLU A1063 6567 11706 5860 1369 275 -2027 O ATOM 2293 N PHE A1064 -15.180 28.667 18.063 1.00 53.82 N ANISOU 2293 N PHE A1064 6132 9664 4654 1552 126 -2370 N ATOM 2294 CA PHE A1064 -14.307 29.566 17.308 1.00 52.78 C ANISOU 2294 CA PHE A1064 6194 9315 4542 1552 84 -2416 C ATOM 2295 C PHE A1064 -12.918 29.732 17.914 1.00 45.60 C ANISOU 2295 C PHE A1064 5429 8322 3576 1347 86 -2430 C ATOM 2296 O PHE A1064 -11.939 29.915 17.190 1.00 46.37 O ANISOU 2296 O PHE A1064 5634 8288 3699 1250 36 -2384 O ATOM 2297 CB PHE A1064 -14.951 30.943 17.164 1.00 54.32 C ANISOU 2297 CB PHE A1064 6537 9373 4731 1771 114 -2611 C ATOM 2298 CG PHE A1064 -14.130 31.907 16.352 1.00 53.72 C ANISOU 2298 CG PHE A1064 6703 9034 4674 1771 81 -2670 C ATOM 2299 CD1 PHE A1064 -13.951 31.709 14.992 1.00 50.25 C ANISOU 2299 CD1 PHE A1064 6258 8534 4303 1804 2 -2555 C ATOM 2300 CD2 PHE A1064 -13.533 33.006 16.948 1.00 55.23 C ANISOU 2300 CD2 PHE A1064 7147 9033 4806 1719 138 -2846 C ATOM 2301 CE1 PHE A1064 -13.195 32.589 14.242 1.00 50.14 C ANISOU 2301 CE1 PHE A1064 6489 8263 4301 1791 -25 -2609 C ATOM 2302 CE2 PHE A1064 -12.776 33.891 16.202 1.00 55.14 C ANISOU 2302 CE2 PHE A1064 7387 8756 4808 1686 119 -2908 C ATOM 2303 CZ PHE A1064 -12.607 33.682 14.848 1.00 49.71 C ANISOU 2303 CZ PHE A1064 6694 8001 4191 1725 35 -2787 C ATOM 2304 N GLN A1065 -12.829 29.675 19.237 1.00 46.92 N ANISOU 2304 N GLN A1065 5595 8579 3653 1278 139 -2495 N ATOM 2305 CA GLN A1065 -11.547 29.855 19.906 1.00 67.65 C ANISOU 2305 CA GLN A1065 8339 11167 6200 1092 130 -2519 C ATOM 2306 C GLN A1065 -10.658 28.627 19.745 1.00 44.61 C ANISOU 2306 C GLN A1065 5299 8341 3310 943 78 -2305 C ATOM 2307 O GLN A1065 -9.447 28.698 19.954 1.00 44.47 O ANISOU 2307 O GLN A1065 5352 8297 3249 796 44 -2289 O ATOM 2308 CB GLN A1065 -11.751 30.173 21.389 1.00 70.36 C ANISOU 2308 CB GLN A1065 8716 11596 6422 1077 199 -2658 C ATOM 2309 CG GLN A1065 -12.494 31.479 21.658 1.00 74.07 C ANISOU 2309 CG GLN A1065 9343 11941 6858 1219 274 -2891 C ATOM 2310 CD GLN A1065 -11.666 32.723 21.354 1.00 76.22 C ANISOU 2310 CD GLN A1065 9893 11967 7101 1155 274 -3039 C ATOM 2311 OE1 GLN A1065 -10.641 32.662 20.672 1.00 75.10 O ANISOU 2311 OE1 GLN A1065 9812 11741 6981 1023 203 -2960 O ATOM 2312 NE2 GLN A1065 -12.111 33.863 21.871 1.00 80.37 N ANISOU 2312 NE2 GLN A1065 10602 12360 7574 1242 366 -3259 N ATOM 2313 N GLU A1066 -11.261 27.505 19.367 1.00 42.80 N ANISOU 2313 N GLU A1066 4890 8217 3154 980 77 -2147 N ATOM 2314 CA GLU A1066 -10.502 26.287 19.112 1.00 62.67 C ANISOU 2314 CA GLU A1066 7311 10786 5716 864 49 -1942 C ATOM 2315 C GLU A1066 -9.877 26.320 17.723 1.00 58.47 C ANISOU 2315 C GLU A1066 6818 10121 5277 829 -7 -1855 C ATOM 2316 O GLU A1066 -9.096 25.441 17.362 1.00 59.40 O ANISOU 2316 O GLU A1066 6881 10246 5441 734 -27 -1696 O ATOM 2317 CB GLU A1066 -11.393 25.053 19.248 1.00 61.22 C ANISOU 2317 CB GLU A1066 6963 10732 5566 892 85 -1818 C ATOM 2318 CG GLU A1066 -12.030 24.879 20.612 1.00 61.37 C ANISOU 2318 CG GLU A1066 6945 10887 5486 910 147 -1887 C ATOM 2319 CD GLU A1066 -12.860 23.614 20.700 1.00 59.26 C ANISOU 2319 CD GLU A1066 6525 10757 5236 913 181 -1776 C ATOM 2320 OE1 GLU A1066 -14.103 23.719 20.747 1.00 61.09 O ANISOU 2320 OE1 GLU A1066 6702 11040 5470 994 220 -1840 O ATOM 2321 OE2 GLU A1066 -12.268 22.514 20.718 1.00 56.44 O ANISOU 2321 OE2 GLU A1066 6104 10460 4879 834 173 -1632 O ATOM 2322 N MET A1067 -10.225 27.342 16.949 1.00 55.50 N ANISOU 2322 N MET A1067 6549 9615 4924 917 -25 -1963 N ATOM 2323 CA MET A1067 -9.796 27.428 15.559 1.00 50.11 C ANISOU 2323 CA MET A1067 5916 8803 4320 899 -76 -1888 C ATOM 2324 C MET A1067 -8.719 28.481 15.330 1.00 49.74 C ANISOU 2324 C MET A1067 6082 8584 4231 803 -109 -1985 C ATOM 2325 O MET A1067 -8.698 29.523 15.982 1.00 51.35 O ANISOU 2325 O MET A1067 6436 8719 4355 812 -88 -2166 O ATOM 2326 CB MET A1067 -10.993 27.728 14.657 1.00 49.81 C ANISOU 2326 CB MET A1067 5846 8744 4334 1082 -85 -1920 C ATOM 2327 CG MET A1067 -12.079 26.672 14.683 1.00 48.86 C ANISOU 2327 CG MET A1067 5512 8798 4253 1145 -62 -1824 C ATOM 2328 SD MET A1067 -13.612 27.282 13.960 1.00 39.30 S ANISOU 2328 SD MET A1067 4248 7626 3057 1396 -81 -1918 S ATOM 2329 CE MET A1067 -14.637 25.820 14.068 1.00 50.99 C ANISOU 2329 CE MET A1067 5477 9331 4566 1364 -57 -1788 C ATOM 2330 N ARG A1068 -7.825 28.186 14.393 1.00 44.77 N ANISOU 2330 N ARG A1068 5478 7878 3656 695 -154 -1869 N ATOM 2331 CA ARG A1068 -6.842 29.146 13.911 1.00 44.98 C ANISOU 2331 CA ARG A1068 5715 7725 3651 582 -193 -1948 C ATOM 2332 C ARG A1068 -7.049 29.336 12.415 1.00 45.56 C ANISOU 2332 C ARG A1068 5853 7662 3796 634 -229 -1899 C ATOM 2333 O ARG A1068 -7.426 28.398 11.718 1.00 43.49 O ANISOU 2333 O ARG A1068 5440 7470 3614 678 -234 -1745 O ATOM 2334 CB ARG A1068 -5.415 28.675 14.205 1.00 45.14 C ANISOU 2334 CB ARG A1068 5707 7792 3651 389 -222 -1860 C ATOM 2335 CG ARG A1068 -4.818 29.232 15.490 1.00 47.90 C ANISOU 2335 CG ARG A1068 6121 8197 3884 299 -217 -1994 C ATOM 2336 CD ARG A1068 -5.581 28.764 16.716 1.00 48.57 C ANISOU 2336 CD ARG A1068 6075 8456 3922 390 -166 -2014 C ATOM 2337 NE ARG A1068 -5.093 29.398 17.938 1.00 51.02 N ANISOU 2337 NE ARG A1068 6462 8818 4105 309 -161 -2162 N ATOM 2338 CZ ARG A1068 -5.649 29.240 19.134 1.00 43.48 C ANISOU 2338 CZ ARG A1068 5442 8002 3077 364 -116 -2220 C ATOM 2339 NH1 ARG A1068 -6.718 28.468 19.273 1.00 50.94 N ANISOU 2339 NH1 ARG A1068 6244 9042 4068 494 -74 -2141 N ATOM 2340 NH2 ARG A1068 -5.137 29.855 20.191 1.00 53.56 N ANISOU 2340 NH2 ARG A1068 6798 9326 4228 276 -115 -2362 N ATOM 2341 N PHE A1069 -6.818 30.546 11.920 1.00 37.96 N ANISOU 2341 N PHE A1069 5129 6494 2799 624 -248 -2038 N ATOM 2342 CA PHE A1069 -7.020 30.826 10.503 1.00 37.31 C ANISOU 2342 CA PHE A1069 5136 6271 2768 690 -288 -2006 C ATOM 2343 C PHE A1069 -5.845 31.580 9.902 1.00 37.83 C ANISOU 2343 C PHE A1069 5442 6128 2805 497 -322 -2053 C ATOM 2344 O PHE A1069 -5.407 32.592 10.439 1.00 40.10 O ANISOU 2344 O PHE A1069 5937 6277 3021 411 -298 -2225 O ATOM 2345 CB PHE A1069 -8.309 31.622 10.292 1.00 39.15 C ANISOU 2345 CB PHE A1069 5440 6431 3003 969 -276 -2140 C ATOM 2346 CG PHE A1069 -9.555 30.859 10.634 1.00 38.66 C ANISOU 2346 CG PHE A1069 5127 6590 2972 1159 -256 -2082 C ATOM 2347 CD1 PHE A1069 -10.185 30.073 9.683 1.00 37.14 C ANISOU 2347 CD1 PHE A1069 4772 6500 2841 1258 -292 -1938 C ATOM 2348 CD2 PHE A1069 -10.098 30.929 11.905 1.00 45.00 C ANISOU 2348 CD2 PHE A1069 5860 7502 3733 1217 -197 -2177 C ATOM 2349 CE1 PHE A1069 -11.334 29.370 9.995 1.00 36.76 C ANISOU 2349 CE1 PHE A1069 4490 6663 2812 1393 -270 -1896 C ATOM 2350 CE2 PHE A1069 -11.246 30.230 12.221 1.00 39.88 C ANISOU 2350 CE2 PHE A1069 4985 7059 3108 1360 -177 -2129 C ATOM 2351 CZ PHE A1069 -11.864 29.449 11.265 1.00 40.93 C ANISOU 2351 CZ PHE A1069 4952 7296 3301 1441 -214 -1991 C ATOM 2352 N ILE A1070 -5.339 31.075 8.784 1.00 37.05 N ANISOU 2352 N ILE A1070 5321 5999 2759 411 -368 -1904 N ATOM 2353 CA ILE A1070 -4.251 31.726 8.069 1.00 38.09 C ANISOU 2353 CA ILE A1070 5673 5935 2866 215 -404 -1935 C ATOM 2354 C ILE A1070 -4.684 32.033 6.641 1.00 38.15 C ANISOU 2354 C ILE A1070 5789 5795 2911 311 -442 -1913 C ATOM 2355 O ILE A1070 -4.732 31.147 5.789 1.00 36.36 O ANISOU 2355 O ILE A1070 5425 5650 2740 314 -474 -1733 O ATOM 2356 CB ILE A1070 -2.980 30.858 8.051 1.00 34.57 C ANISOU 2356 CB ILE A1070 5107 5584 2446 11 -437 -1774 C ATOM 2357 CG1 ILE A1070 -2.653 30.361 9.461 1.00 34.84 C ANISOU 2357 CG1 ILE A1070 4975 5810 2453 -15 -411 -1772 C ATOM 2358 CG2 ILE A1070 -1.811 31.641 7.471 1.00 35.55 C ANISOU 2358 CG2 ILE A1070 5453 5516 2539 -183 -486 -1832 C ATOM 2359 CD1 ILE A1070 -1.366 29.574 9.548 1.00 35.47 C ANISOU 2359 CD1 ILE A1070 4909 6002 2565 -159 -435 -1643 C ATOM 2360 N ILE A1071 -5.004 33.297 6.392 1.00 38.46 N ANISOU 2360 N ILE A1071 6091 5595 2926 411 -434 -2094 N ATOM 2361 CA ILE A1071 -5.499 33.732 5.093 1.00 38.75 C ANISOU 2361 CA ILE A1071 6289 5438 2997 595 -494 -2072 C ATOM 2362 C ILE A1071 -4.391 34.366 4.262 1.00 39.32 C ANISOU 2362 C ILE A1071 6612 5257 3069 356 -513 -2094 C ATOM 2363 O ILE A1071 -3.965 35.487 4.529 1.00 44.62 O ANISOU 2363 O ILE A1071 7537 5681 3733 265 -465 -2264 O ATOM 2364 CB ILE A1071 -6.653 34.731 5.251 1.00 41.47 C ANISOU 2364 CB ILE A1071 6819 5594 3344 950 -482 -2210 C ATOM 2365 CG1 ILE A1071 -7.763 34.113 6.103 1.00 41.13 C ANISOU 2365 CG1 ILE A1071 6492 5834 3302 1165 -453 -2202 C ATOM 2366 CG2 ILE A1071 -7.181 35.155 3.889 1.00 42.46 C ANISOU 2366 CG2 ILE A1071 7165 5481 3487 1196 -561 -2134 C ATOM 2367 CD1 ILE A1071 -8.870 35.071 6.445 1.00 44.07 C ANISOU 2367 CD1 ILE A1071 7003 6065 3677 1510 -419 -2344 C ATOM 2368 N ILE A1072 -3.942 33.639 3.246 1.00 37.12 N ANISOU 2368 N ILE A1072 6251 5039 2814 243 -569 -1919 N ATOM 2369 CA ILE A1072 -2.823 34.059 2.413 1.00 43.46 C ANISOU 2369 CA ILE A1072 7227 5650 3634 -15 -583 -1907 C ATOM 2370 C ILE A1072 -3.242 34.366 0.977 1.00 43.58 C ANISOU 2370 C ILE A1072 7507 5382 3670 125 -655 -1775 C ATOM 2371 O ILE A1072 -3.906 33.559 0.307 1.00 42.90 O ANISOU 2371 O ILE A1072 7281 5436 3581 288 -719 -1619 O ATOM 2372 CB ILE A1072 -1.719 32.985 2.381 1.00 34.96 C ANISOU 2372 CB ILE A1072 5830 4883 2571 -294 -574 -1811 C ATOM 2373 CG1 ILE A1072 -1.302 32.605 3.802 1.00 34.95 C ANISOU 2373 CG1 ILE A1072 5826 4933 2519 -311 -596 -1766 C ATOM 2374 CG2 ILE A1072 -0.520 33.471 1.579 1.00 35.54 C ANISOU 2374 CG2 ILE A1072 6041 4746 2714 -484 -608 -1778 C ATOM 2375 CD1 ILE A1072 -0.264 31.514 3.854 1.00 32.90 C ANISOU 2375 CD1 ILE A1072 5284 4878 2340 -395 -630 -1606 C ATOM 2376 N GLY A1073 -2.837 35.539 0.504 1.00 45.14 N ANISOU 2376 N GLY A1073 8083 5183 3885 39 -628 -1827 N ATOM 2377 CA GLY A1073 -3.123 35.935 -0.859 1.00 40.46 C ANISOU 2377 CA GLY A1073 7749 4296 3328 133 -667 -1662 C ATOM 2378 C GLY A1073 -3.036 37.428 -1.074 1.00 44.02 C ANISOU 2378 C GLY A1073 8674 4258 3793 146 -604 -1747 C ATOM 2379 O GLY A1073 -2.667 38.177 -0.170 1.00 46.08 O ANISOU 2379 O GLY A1073 9033 4418 4057 39 -516 -1936 O ATOM 2380 N LYS A1074 -3.380 37.858 -2.282 1.00 60.55 N ANISOU 2380 N LYS A1074 10996 6080 5929 273 -627 -1565 N ATOM 2381 CA LYS A1074 -3.331 39.268 -2.638 1.00 62.33 C ANISOU 2381 CA LYS A1074 11723 5794 6165 310 -555 -1603 C ATOM 2382 C LYS A1074 -4.203 39.538 -3.859 1.00 59.97 C ANISOU 2382 C LYS A1074 11587 5302 5896 631 -613 -1360 C ATOM 2383 O LYS A1074 -4.045 38.900 -4.900 1.00 56.45 O ANISOU 2383 O LYS A1074 11029 4964 5456 548 -679 -1154 O ATOM 2384 CB LYS A1074 -1.887 39.701 -2.904 1.00 65.23 C ANISOU 2384 CB LYS A1074 12247 5996 6540 -170 -471 -1636 C ATOM 2385 CG LYS A1074 -1.682 41.206 -2.951 1.00 71.95 C ANISOU 2385 CG LYS A1074 13509 6400 7430 -207 -343 -1682 C ATOM 2386 CD LYS A1074 -0.220 41.554 -3.182 1.00 74.82 C ANISOU 2386 CD LYS A1074 13876 6733 7820 -689 -249 -1686 C ATOM 2387 CE LYS A1074 0.005 43.059 -3.168 1.00 81.47 C ANISOU 2387 CE LYS A1074 15117 7159 8680 -749 -107 -1745 C ATOM 2388 NZ LYS A1074 -0.241 43.655 -1.825 1.00 84.84 N ANISOU 2388 NZ LYS A1074 15539 7581 9117 -677 -37 -1982 N ATOM 2389 N GLY A1075 -5.129 40.481 -3.724 1.00 52.64 N ANISOU 2389 N GLY A1075 10919 4104 4979 1012 -585 -1384 N ATOM 2390 CA GLY A1075 -6.021 40.831 -4.814 1.00 58.75 C ANISOU 2390 CA GLY A1075 11853 4707 5761 1374 -648 -1154 C ATOM 2391 C GLY A1075 -6.696 42.173 -4.607 1.00 64.10 C ANISOU 2391 C GLY A1075 12954 4957 6446 1734 -573 -1212 C ATOM 2392 O GLY A1075 -6.027 43.199 -4.482 1.00 66.10 O ANISOU 2392 O GLY A1075 13645 4775 6695 1555 -447 -1320 O ATOM 2393 N ASP A1076 -8.025 42.163 -4.574 1.00 67.19 N ANISOU 2393 N ASP A1076 13208 5479 6841 2240 -638 -1144 N ATOM 2394 CA ASP A1076 -8.799 43.383 -4.373 1.00 71.94 C ANISOU 2394 CA ASP A1076 14180 5705 7450 2668 -567 -1186 C ATOM 2395 C ASP A1076 -8.507 44.008 -3.014 1.00 72.47 C ANISOU 2395 C ASP A1076 14326 5671 7539 2535 -418 -1468 C ATOM 2396 O ASP A1076 -8.498 43.314 -1.998 1.00 69.14 O ANISOU 2396 O ASP A1076 13583 5580 7107 2448 -423 -1657 O ATOM 2397 CB ASP A1076 -10.297 43.100 -4.503 1.00 75.86 C ANISOU 2397 CB ASP A1076 14393 6487 7941 3228 -675 -1073 C ATOM 2398 CG ASP A1076 -10.692 42.684 -5.905 1.00 78.20 C ANISOU 2398 CG ASP A1076 14597 6909 8205 3366 -818 -764 C ATOM 2399 OD1 ASP A1076 -9.993 43.077 -6.862 1.00 79.96 O ANISOU 2399 OD1 ASP A1076 15155 6816 8411 3171 -808 -615 O ATOM 2400 OD2 ASP A1076 -11.704 41.967 -6.049 1.00 79.83 O ANISOU 2400 OD2 ASP A1076 14395 7543 8393 3653 -934 -679 O ATOM 2401 N PRO A1077 -8.264 45.327 -2.999 1.00 72.61 N ANISOU 2401 N PRO A1077 14725 5280 7582 2486 -278 -1474 N ATOM 2402 CA PRO A1077 -7.971 46.082 -1.776 1.00 73.60 C ANISOU 2402 CA PRO A1077 14929 5295 7740 2329 -120 -1721 C ATOM 2403 C PRO A1077 -9.087 45.970 -0.740 1.00 72.62 C ANISOU 2403 C PRO A1077 14558 5404 7630 2712 -120 -1857 C ATOM 2404 O PRO A1077 -8.807 45.925 0.458 1.00 72.36 O ANISOU 2404 O PRO A1077 14381 5506 7605 2521 -43 -2095 O ATOM 2405 CB PRO A1077 -7.838 47.524 -2.276 1.00 78.68 C ANISOU 2405 CB PRO A1077 16053 5442 8400 2352 12 -1636 C ATOM 2406 CG PRO A1077 -7.483 47.393 -3.718 1.00 78.14 C ANISOU 2406 CG PRO A1077 16144 5249 8297 2274 -61 -1375 C ATOM 2407 CD PRO A1077 -8.221 46.183 -4.197 1.00 74.56 C ANISOU 2407 CD PRO A1077 15355 5155 7819 2558 -255 -1242 C ATOM 2408 N GLU A1078 -10.332 45.927 -1.205 1.00 73.59 N ANISOU 2408 N GLU A1078 14600 5612 7751 3234 -205 -1703 N ATOM 2409 CA GLU A1078 -11.482 45.820 -0.315 1.00 83.41 C ANISOU 2409 CA GLU A1078 15566 7120 9006 3613 -204 -1809 C ATOM 2410 C GLU A1078 -11.431 44.524 0.484 1.00 76.83 C ANISOU 2410 C GLU A1078 14268 6780 8145 3468 -270 -1957 C ATOM 2411 O GLU A1078 -11.690 44.511 1.689 1.00 75.88 O ANISOU 2411 O GLU A1078 13968 6831 8031 3466 -197 -2157 O ATOM 2412 CB GLU A1078 -12.787 45.899 -1.111 1.00 87.44 C ANISOU 2412 CB GLU A1078 15994 7724 9505 4164 -305 -1587 C ATOM 2413 CG GLU A1078 -14.037 45.933 -0.245 1.00 90.07 C ANISOU 2413 CG GLU A1078 16040 8332 9850 4554 -288 -1685 C ATOM 2414 CD GLU A1078 -15.311 46.081 -1.058 1.00 92.26 C ANISOU 2414 CD GLU A1078 16204 8746 10103 5064 -388 -1464 C ATOM 2415 OE1 GLU A1078 -16.288 46.656 -0.531 1.00 95.25 O ANISOU 2415 OE1 GLU A1078 16524 9169 10498 5401 -330 -1513 O ATOM 2416 OE2 GLU A1078 -15.336 45.621 -2.219 1.00 90.50 O ANISOU 2416 OE2 GLU A1078 15935 8611 9841 5112 -522 -1244 O ATOM 2417 N LEU A1079 -11.084 43.437 -0.196 1.00 71.55 N ANISOU 2417 N LEU A1079 13409 6338 7437 3333 -399 -1853 N ATOM 2418 CA LEU A1079 -10.990 42.131 0.441 1.00 65.76 C ANISOU 2418 CA LEU A1079 12233 6091 6661 3177 -460 -1964 C ATOM 2419 C LEU A1079 -9.791 42.059 1.380 1.00 64.87 C ANISOU 2419 C LEU A1079 12119 5992 6536 2662 -372 -2160 C ATOM 2420 O LEU A1079 -9.844 41.394 2.414 1.00 63.34 O ANISOU 2420 O LEU A1079 11593 6157 6314 2565 -360 -2301 O ATOM 2421 CB LEU A1079 -10.905 41.029 -0.616 1.00 60.95 C ANISOU 2421 CB LEU A1079 11345 5771 6043 3070 -604 -1727 C ATOM 2422 CG LEU A1079 -12.119 40.945 -1.543 1.00 62.76 C ANISOU 2422 CG LEU A1079 11449 6121 6275 3525 -712 -1507 C ATOM 2423 CD1 LEU A1079 -11.927 39.869 -2.598 1.00 58.35 C ANISOU 2423 CD1 LEU A1079 10619 5848 5702 3331 -839 -1277 C ATOM 2424 CD2 LEU A1079 -13.383 40.690 -0.738 1.00 62.10 C ANISOU 2424 CD2 LEU A1079 11034 6382 6179 3914 -712 -1615 C ATOM 2425 N GLU A1080 -8.712 42.746 1.017 1.00 62.25 N ANISOU 2425 N GLU A1080 12128 5300 6222 2319 -306 -2155 N ATOM 2426 CA GLU A1080 -7.522 42.788 1.858 1.00 66.31 C ANISOU 2426 CA GLU A1080 12613 5854 6729 1817 -221 -2335 C ATOM 2427 C GLU A1080 -7.808 43.535 3.153 1.00 68.95 C ANISOU 2427 C GLU A1080 12967 6147 7083 1865 -89 -2559 C ATOM 2428 O GLU A1080 -7.373 43.118 4.224 1.00 63.39 O ANISOU 2428 O GLU A1080 12018 5721 6347 1618 -57 -2733 O ATOM 2429 CB GLU A1080 -6.353 43.439 1.118 1.00 67.75 C ANISOU 2429 CB GLU A1080 13122 5687 6932 1441 -167 -2274 C ATOM 2430 CG GLU A1080 -5.877 42.656 -0.091 1.00 65.21 C ANISOU 2430 CG GLU A1080 12765 5426 6587 1296 -281 -2072 C ATOM 2431 CD GLU A1080 -4.573 43.183 -0.653 1.00 66.55 C ANISOU 2431 CD GLU A1080 13162 5350 6775 838 -211 -2033 C ATOM 2432 OE1 GLU A1080 -4.240 42.836 -1.806 1.00 65.63 O ANISOU 2432 OE1 GLU A1080 13113 5176 6648 743 -277 -1844 O ATOM 2433 OE2 GLU A1080 -3.879 43.940 0.058 1.00 68.58 O ANISOU 2433 OE2 GLU A1080 13508 5496 7052 569 -87 -2197 O ATOM 2434 N GLY A1081 -8.540 44.639 3.049 1.00 68.50 N ANISOU 2434 N GLY A1081 13200 5753 7073 2187 -10 -2546 N ATOM 2435 CA GLY A1081 -8.958 45.380 4.223 1.00 71.56 C ANISOU 2435 CA GLY A1081 13621 6085 7483 2282 122 -2755 C ATOM 2436 C GLY A1081 -9.896 44.541 5.068 1.00 69.88 C ANISOU 2436 C GLY A1081 12992 6316 7242 2523 78 -2825 C ATOM 2437 O GLY A1081 -9.765 44.481 6.293 1.00 70.85 O ANISOU 2437 O GLY A1081 12957 6620 7343 2365 156 -3034 O ATOM 2438 N TRP A1082 -10.838 43.882 4.399 1.00 68.38 N ANISOU 2438 N TRP A1082 12608 6327 7045 2889 -45 -2645 N ATOM 2439 CA TRP A1082 -11.798 43.000 5.054 1.00 66.76 C ANISOU 2439 CA TRP A1082 11966 6587 6813 3113 -93 -2676 C ATOM 2440 C TRP A1082 -11.082 41.893 5.825 1.00 65.70 C ANISOU 2440 C TRP A1082 11501 6845 6618 2727 -115 -2772 C ATOM 2441 O TRP A1082 -11.555 41.440 6.868 1.00 62.63 O ANISOU 2441 O TRP A1082 10821 6772 6203 2752 -80 -2876 O ATOM 2442 CB TRP A1082 -12.753 42.402 4.017 1.00 65.61 C ANISOU 2442 CB TRP A1082 11639 6628 6663 3493 -234 -2455 C ATOM 2443 CG TRP A1082 -13.930 41.673 4.597 1.00 66.21 C ANISOU 2443 CG TRP A1082 11270 7166 6721 3756 -266 -2471 C ATOM 2444 CD1 TRP A1082 -14.327 41.655 5.902 1.00 66.84 C ANISOU 2444 CD1 TRP A1082 11161 7441 6796 3742 -174 -2644 C ATOM 2445 CD2 TRP A1082 -14.864 40.855 3.883 1.00 64.71 C ANISOU 2445 CD2 TRP A1082 10758 7318 6510 4036 -392 -2307 C ATOM 2446 NE1 TRP A1082 -15.448 40.875 6.046 1.00 66.03 N ANISOU 2446 NE1 TRP A1082 10647 7767 6673 3979 -232 -2589 N ATOM 2447 CE2 TRP A1082 -15.798 40.373 4.821 1.00 64.71 C ANISOU 2447 CE2 TRP A1082 10378 7712 6495 4154 -365 -2389 C ATOM 2448 CE3 TRP A1082 -15.002 40.484 2.542 1.00 63.48 C ANISOU 2448 CE3 TRP A1082 10593 7185 6342 4174 -520 -2100 C ATOM 2449 CZ2 TRP A1082 -16.853 39.538 4.461 1.00 62.56 C ANISOU 2449 CZ2 TRP A1082 9710 7865 6196 4371 -457 -2277 C ATOM 2450 CZ3 TRP A1082 -16.050 39.655 2.187 1.00 62.58 C ANISOU 2450 CZ3 TRP A1082 10070 7508 6200 4411 -614 -1994 C ATOM 2451 CH2 TRP A1082 -16.962 39.192 3.143 1.00 62.68 C ANISOU 2451 CH2 TRP A1082 9701 7918 6196 4490 -580 -2086 C ATOM 2452 N ALA A1083 -9.934 41.468 5.310 1.00 64.34 N ANISOU 2452 N ALA A1083 11373 6653 6421 2362 -167 -2719 N ATOM 2453 CA ALA A1083 -9.130 40.446 5.968 1.00 61.39 C ANISOU 2453 CA ALA A1083 10692 6644 5988 1981 -188 -2775 C ATOM 2454 C ALA A1083 -8.365 41.024 7.156 1.00 63.81 C ANISOU 2454 C ALA A1083 11070 6900 6274 1659 -60 -3002 C ATOM 2455 O ALA A1083 -8.371 40.452 8.247 1.00 62.61 O ANISOU 2455 O ALA A1083 10644 7076 6068 1543 -28 -3096 O ATOM 2456 CB ALA A1083 -8.168 39.812 4.976 1.00 58.03 C ANISOU 2456 CB ALA A1083 10267 6235 5546 1708 -284 -2630 C ATOM 2457 N ARG A1084 -7.711 42.161 6.934 1.00 66.59 N ANISOU 2457 N ARG A1084 11791 6847 6664 1503 18 -3083 N ATOM 2458 CA ARG A1084 -6.901 42.807 7.963 1.00 64.02 C ANISOU 2458 CA ARG A1084 11532 6474 6319 1172 135 -3326 C ATOM 2459 C ARG A1084 -7.735 43.194 9.182 1.00 70.45 C ANISOU 2459 C ARG A1084 12292 7356 7121 1359 244 -3509 C ATOM 2460 O ARG A1084 -7.246 43.158 10.314 1.00 70.78 O ANISOU 2460 O ARG A1084 12199 7592 7101 1098 311 -3707 O ATOM 2461 CB ARG A1084 -6.203 44.046 7.395 1.00 67.13 C ANISOU 2461 CB ARG A1084 12341 6395 6771 1015 203 -3359 C ATOM 2462 CG ARG A1084 -5.133 43.747 6.354 1.00 65.23 C ANISOU 2462 CG ARG A1084 12148 6100 6535 716 125 -3208 C ATOM 2463 CD ARG A1084 -3.950 43.005 6.957 1.00 66.61 C ANISOU 2463 CD ARG A1084 11997 6661 6652 296 77 -3299 C ATOM 2464 NE ARG A1084 -2.933 42.694 5.956 1.00 65.63 N ANISOU 2464 NE ARG A1084 11883 6511 6542 24 9 -3143 N ATOM 2465 CZ ARG A1084 -1.814 42.023 6.209 1.00 64.32 C ANISOU 2465 CZ ARG A1084 11432 6668 6341 -299 -59 -3156 C ATOM 2466 NH1 ARG A1084 -1.561 41.590 7.436 1.00 58.90 N ANISOU 2466 NH1 ARG A1084 10446 6347 5588 -363 -93 -3309 N ATOM 2467 NH2 ARG A1084 -0.945 41.785 5.235 1.00 63.37 N ANISOU 2467 NH2 ARG A1084 11325 6508 6245 -523 -102 -2997 N ATOM 2468 N SER A1085 -8.991 43.562 8.946 1.00 72.39 N ANISOU 2468 N SER A1085 12624 7464 7418 1814 260 -3442 N ATOM 2469 CA SER A1085 -9.904 43.899 10.034 1.00 74.46 C ANISOU 2469 CA SER A1085 12814 7801 7676 2028 365 -3595 C ATOM 2470 C SER A1085 -10.121 42.693 10.942 1.00 71.07 C ANISOU 2470 C SER A1085 11962 7880 7162 1949 333 -3604 C ATOM 2471 O SER A1085 -10.198 42.826 12.164 1.00 72.46 O ANISOU 2471 O SER A1085 12067 8178 7285 1848 441 -3783 O ATOM 2472 CB SER A1085 -11.242 44.398 9.483 1.00 76.19 C ANISOU 2472 CB SER A1085 13138 7844 7968 2561 364 -3480 C ATOM 2473 OG SER A1085 -11.874 43.403 8.699 1.00 73.28 O ANISOU 2473 OG SER A1085 12511 7739 7593 2798 212 -3255 O ATOM 2474 N LEU A1086 -10.213 41.515 10.335 1.00 66.93 N ANISOU 2474 N LEU A1086 11171 7640 6619 1982 192 -3398 N ATOM 2475 CA LEU A1086 -10.331 40.276 11.091 1.00 65.85 C ANISOU 2475 CA LEU A1086 10642 7967 6410 1878 155 -3351 C ATOM 2476 C LEU A1086 -8.998 39.919 11.739 1.00 62.72 C ANISOU 2476 C LEU A1086 10208 7701 5923 1397 178 -3415 C ATOM 2477 O LEU A1086 -8.960 39.270 12.785 1.00 58.59 O ANISOU 2477 O LEU A1086 9479 7465 5316 1272 199 -3424 O ATOM 2478 CB LEU A1086 -10.807 39.135 10.191 1.00 60.54 C ANISOU 2478 CB LEU A1086 9697 7546 5758 2040 9 -3112 C ATOM 2479 CG LEU A1086 -12.230 39.268 9.646 1.00 62.25 C ANISOU 2479 CG LEU A1086 9853 7767 6031 2516 -27 -3031 C ATOM 2480 CD1 LEU A1086 -12.582 38.082 8.761 1.00 58.88 C ANISOU 2480 CD1 LEU A1086 9138 7628 5605 2600 -161 -2820 C ATOM 2481 CD2 LEU A1086 -13.226 39.404 10.787 1.00 64.47 C ANISOU 2481 CD2 LEU A1086 9985 8208 6304 2693 65 -3144 C ATOM 2482 N GLU A1087 -7.907 40.351 11.114 1.00 59.62 N ANISOU 2482 N GLU A1087 10016 7097 5540 1135 168 -3442 N ATOM 2483 CA GLU A1087 -6.575 40.099 11.648 1.00 71.02 C ANISOU 2483 CA GLU A1087 11421 8676 6887 668 190 -3505 C ATOM 2484 C GLU A1087 -6.301 40.975 12.866 1.00 73.57 C ANISOU 2484 C GLU A1087 11894 8923 7136 481 344 -3773 C ATOM 2485 O GLU A1087 -5.436 40.660 13.686 1.00 71.94 O ANISOU 2485 O GLU A1087 11718 8845 6771 177 342 -3736 O ATOM 2486 CB GLU A1087 -5.504 40.338 10.582 1.00 58.28 C ANISOU 2486 CB GLU A1087 9909 6906 5327 439 131 -3485 C ATOM 2487 CG GLU A1087 -4.138 39.776 10.948 1.00 65.41 C ANISOU 2487 CG GLU A1087 10647 8062 6145 -8 112 -3464 C ATOM 2488 CD GLU A1087 -3.018 40.383 10.130 1.00 65.59 C ANISOU 2488 CD GLU A1087 10680 7963 6280 -51 -69 -3568 C ATOM 2489 OE1 GLU A1087 -3.127 41.571 9.762 1.00 67.74 O ANISOU 2489 OE1 GLU A1087 11322 7806 6610 -19 4 -3652 O ATOM 2490 OE2 GLU A1087 -2.029 39.673 9.855 1.00 63.45 O ANISOU 2490 OE2 GLU A1087 10300 7837 5972 -126 -265 -3397 O ATOM 2491 N GLU A1088 -7.058 42.060 13.003 1.00 76.91 N ANISOU 2491 N GLU A1088 12498 9080 7646 728 435 -3945 N ATOM 2492 CA GLU A1088 -6.918 42.937 14.163 1.00 69.00 C ANISOU 2492 CA GLU A1088 11597 8019 6600 583 586 -4243 C ATOM 2493 C GLU A1088 -8.104 42.807 15.122 1.00 73.43 C ANISOU 2493 C GLU A1088 12128 8668 7103 847 675 -4242 C ATOM 2494 O GLU A1088 -8.115 43.423 16.188 1.00 75.85 O ANISOU 2494 O GLU A1088 12545 8936 7340 738 820 -4461 O ATOM 2495 CB GLU A1088 -6.765 44.391 13.723 1.00 90.04 C ANISOU 2495 CB GLU A1088 14543 10265 9404 687 592 -4433 C ATOM 2496 CG GLU A1088 -7.971 44.951 12.994 1.00 90.37 C ANISOU 2496 CG GLU A1088 14836 9949 9552 1138 637 -4295 C ATOM 2497 CD GLU A1088 -7.843 46.432 12.702 1.00 93.23 C ANISOU 2497 CD GLU A1088 15609 9810 10005 1197 713 -4411 C ATOM 2498 OE1 GLU A1088 -7.083 47.117 13.418 1.00 96.26 O ANISOU 2498 OE1 GLU A1088 16075 10140 10358 943 749 -4654 O ATOM 2499 OE2 GLU A1088 -8.503 46.910 11.754 1.00 93.22 O ANISOU 2499 OE2 GLU A1088 15855 9474 10090 1515 721 -4239 O ATOM 2500 N LYS A1089 -9.096 42.001 14.744 1.00 72.07 N ANISOU 2500 N LYS A1089 11750 8659 6973 1192 573 -4023 N ATOM 2501 CA LYS A1089 -10.260 41.765 15.599 1.00 73.29 C ANISOU 2501 CA LYS A1089 11749 8991 7108 1460 619 -4032 C ATOM 2502 C LYS A1089 -10.143 40.449 16.371 1.00 65.53 C ANISOU 2502 C LYS A1089 10455 8433 6011 1332 538 -3890 C ATOM 2503 O LYS A1089 -10.181 40.437 17.601 1.00 66.74 O ANISOU 2503 O LYS A1089 10596 8707 6055 1247 606 -3983 O ATOM 2504 CB LYS A1089 -11.544 41.770 14.768 1.00 68.63 C ANISOU 2504 CB LYS A1089 11075 8356 6646 1936 561 -3909 C ATOM 2505 CG LYS A1089 -12.820 41.688 15.590 1.00 71.05 C ANISOU 2505 CG LYS A1089 11211 8834 6949 2221 624 -3948 C ATOM 2506 CD LYS A1089 -14.039 42.029 14.747 1.00 72.47 C ANISOU 2506 CD LYS A1089 11380 8909 7245 2694 589 -3858 C ATOM 2507 CE LYS A1089 -15.274 42.218 15.614 1.00 75.00 C ANISOU 2507 CE LYS A1089 11573 9355 7568 2962 684 -3945 C ATOM 2508 NZ LYS A1089 -16.447 42.672 14.819 1.00 75.91 N ANISOU 2508 NZ LYS A1089 11689 9370 7784 3431 655 -3858 N ATOM 2509 N HIS A1090 -9.994 39.346 15.641 1.00 68.49 N ANISOU 2509 N HIS A1090 10586 9019 6418 1330 389 -3658 N ATOM 2510 CA HIS A1090 -9.876 38.021 16.249 1.00 64.96 C ANISOU 2510 CA HIS A1090 9818 8954 5908 1228 307 -3496 C ATOM 2511 C HIS A1090 -8.414 37.605 16.386 1.00 62.32 C ANISOU 2511 C HIS A1090 9511 8682 5486 868 237 -3424 C ATOM 2512 O HIS A1090 -7.658 37.651 15.415 1.00 61.08 O ANISOU 2512 O HIS A1090 9446 8400 5360 740 179 -3359 O ATOM 2513 CB HIS A1090 -10.639 36.986 15.422 1.00 61.35 C ANISOU 2513 CB HIS A1090 9061 8701 5547 1439 204 -3282 C ATOM 2514 CG HIS A1090 -12.062 37.361 15.153 1.00 63.65 C ANISOU 2514 CG HIS A1090 9311 8957 5916 1822 235 -3319 C ATOM 2515 ND1 HIS A1090 -13.066 37.179 16.079 1.00 65.57 N ANISOU 2515 ND1 HIS A1090 9389 9385 6139 1975 295 -3366 N ATOM 2516 CD2 HIS A1090 -12.647 37.914 14.066 1.00 65.38 C ANISOU 2516 CD2 HIS A1090 9632 8983 6225 2097 207 -3302 C ATOM 2517 CE1 HIS A1090 -14.210 37.602 15.572 1.00 68.10 C ANISOU 2517 CE1 HIS A1090 9694 9647 6535 2321 303 -3380 C ATOM 2518 NE2 HIS A1090 -13.984 38.053 14.352 1.00 68.04 N ANISOU 2518 NE2 HIS A1090 9848 9409 6592 2418 245 -3332 N ATOM 2519 N GLY A1091 -8.017 37.205 17.589 1.00 63.00 N ANISOU 2519 N GLY A1091 9508 8966 5462 728 231 -3428 N ATOM 2520 CA GLY A1091 -6.627 36.885 17.864 1.00 62.05 C ANISOU 2520 CA GLY A1091 9393 8925 5256 446 140 -3364 C ATOM 2521 C GLY A1091 -6.132 35.608 17.212 1.00 58.61 C ANISOU 2521 C GLY A1091 8683 8696 4890 386 23 -3107 C ATOM 2522 O GLY A1091 -4.945 35.289 17.283 1.00 58.40 O ANISOU 2522 O GLY A1091 8619 8744 4826 185 -58 -3034 O ATOM 2523 N ASN A1092 -7.038 34.876 16.574 1.00 51.05 N ANISOU 2523 N ASN A1092 7523 7834 4041 574 15 -2971 N ATOM 2524 CA ASN A1092 -6.687 33.611 15.942 1.00 51.74 C ANISOU 2524 CA ASN A1092 7365 8095 4201 532 -70 -2726 C ATOM 2525 C ASN A1092 -6.739 33.674 14.418 1.00 50.65 C ANISOU 2525 C ASN A1092 7283 7805 4157 581 -110 -2648 C ATOM 2526 O ASN A1092 -6.890 32.651 13.752 1.00 48.20 O ANISOU 2526 O ASN A1092 6769 7621 3925 622 -158 -2456 O ATOM 2527 CB ASN A1092 -7.607 32.498 16.447 1.00 46.27 C ANISOU 2527 CB ASN A1092 6377 7658 3544 675 -57 -2605 C ATOM 2528 CG ASN A1092 -9.073 32.888 16.406 1.00 47.65 C ANISOU 2528 CG ASN A1092 6540 7808 3755 935 2 -2698 C ATOM 2529 OD1 ASN A1092 -9.448 33.881 15.781 1.00 49.02 O ANISOU 2529 OD1 ASN A1092 6903 7768 3955 1056 26 -2820 O ATOM 2530 ND2 ASN A1092 -9.911 32.105 17.075 1.00 47.10 N ANISOU 2530 ND2 ASN A1092 6250 7955 3690 1033 27 -2640 N ATOM 2531 N VAL A1093 -6.614 34.880 13.871 1.00 52.30 N ANISOU 2531 N VAL A1093 7787 7729 4357 573 -81 -2803 N ATOM 2532 CA VAL A1093 -6.618 35.064 12.424 1.00 51.11 C ANISOU 2532 CA VAL A1093 7724 7409 4285 621 -120 -2748 C ATOM 2533 C VAL A1093 -5.408 35.878 11.964 1.00 52.06 C ANISOU 2533 C VAL A1093 8134 7283 4364 363 -124 -2827 C ATOM 2534 O VAL A1093 -5.214 37.018 12.384 1.00 55.59 O ANISOU 2534 O VAL A1093 8861 7507 4754 290 -46 -3032 O ATOM 2535 CB VAL A1093 -7.912 35.756 11.944 1.00 48.85 C ANISOU 2535 CB VAL A1093 7521 6975 4066 956 -84 -2842 C ATOM 2536 CG1 VAL A1093 -7.816 36.096 10.465 1.00 48.42 C ANISOU 2536 CG1 VAL A1093 7614 6703 4081 1027 -143 -2791 C ATOM 2537 CG2 VAL A1093 -9.122 34.873 12.216 1.00 47.70 C ANISOU 2537 CG2 VAL A1093 7072 7095 3957 1201 -98 -2740 C ATOM 2538 N LYS A1094 -4.599 35.272 11.101 1.00 48.89 N ANISOU 2538 N LYS A1094 7673 6913 3991 216 -207 -2664 N ATOM 2539 CA LYS A1094 -3.415 35.911 10.541 1.00 46.90 C ANISOU 2539 CA LYS A1094 7677 6440 3701 -27 -238 -2704 C ATOM 2540 C LYS A1094 -3.570 36.077 9.033 1.00 47.02 C ANISOU 2540 C LYS A1094 7766 6295 3804 -6 -240 -2664 C ATOM 2541 O LYS A1094 -3.975 35.145 8.344 1.00 44.60 O ANISOU 2541 O LYS A1094 7241 6139 3565 121 -303 -2483 O ATOM 2542 CB LYS A1094 -2.163 35.089 10.859 1.00 45.34 C ANISOU 2542 CB LYS A1094 7291 6448 3489 -195 -352 -2560 C ATOM 2543 CG LYS A1094 -0.882 35.615 10.230 1.00 59.47 C ANISOU 2543 CG LYS A1094 9207 8094 5294 -363 -446 -2594 C ATOM 2544 CD LYS A1094 -0.546 37.004 10.744 1.00 62.26 C ANISOU 2544 CD LYS A1094 9804 8247 5606 -405 -444 -2862 C ATOM 2545 CE LYS A1094 0.786 37.495 10.201 1.00 65.84 C ANISOU 2545 CE LYS A1094 10225 8658 6133 -652 -482 -2916 C ATOM 2546 NZ LYS A1094 1.078 38.894 10.615 1.00 71.32 N ANISOU 2546 NZ LYS A1094 11131 9145 6822 -767 -424 -3179 N ATOM 2547 N VAL A1095 -3.250 37.262 8.523 1.00 48.44 N ANISOU 2547 N VAL A1095 8173 6209 4022 -123 -165 -2860 N ATOM 2548 CA VAL A1095 -3.379 37.533 7.094 1.00 48.11 C ANISOU 2548 CA VAL A1095 8208 5968 4104 21 -241 -2806 C ATOM 2549 C VAL A1095 -2.022 37.812 6.451 1.00 52.85 C ANISOU 2549 C VAL A1095 8828 6494 4758 -224 -316 -2821 C ATOM 2550 O VAL A1095 -1.252 38.638 6.939 1.00 55.91 O ANISOU 2550 O VAL A1095 9335 6758 5148 -356 -323 -2964 O ATOM 2551 CB VAL A1095 -4.321 38.725 6.832 1.00 52.02 C ANISOU 2551 CB VAL A1095 9051 6057 4658 334 -204 -2883 C ATOM 2552 CG1 VAL A1095 -4.362 39.061 5.349 1.00 51.14 C ANISOU 2552 CG1 VAL A1095 9208 5613 4611 433 -265 -2721 C ATOM 2553 CG2 VAL A1095 -5.717 38.417 7.353 1.00 51.07 C ANISOU 2553 CG2 VAL A1095 8815 6062 4526 708 -196 -2861 C ATOM 2554 N ILE A1096 -1.740 37.116 5.353 1.00 45.84 N ANISOU 2554 N ILE A1096 7886 5630 3900 -271 -384 -2607 N ATOM 2555 CA ILE A1096 -0.464 37.248 4.660 1.00 58.12 C ANISOU 2555 CA ILE A1096 9491 7087 5504 -527 -429 -2525 C ATOM 2556 C ILE A1096 -0.635 37.751 3.227 1.00 58.68 C ANISOU 2556 C ILE A1096 9888 6780 5629 -536 -405 -2385 C ATOM 2557 O ILE A1096 -1.100 37.019 2.346 1.00 57.93 O ANISOU 2557 O ILE A1096 9752 6725 5535 -423 -461 -2202 O ATOM 2558 CB ILE A1096 0.294 35.908 4.620 1.00 42.63 C ANISOU 2558 CB ILE A1096 7190 5470 3538 -599 -529 -2348 C ATOM 2559 CG1 ILE A1096 0.272 35.234 5.992 1.00 42.02 C ANISOU 2559 CG1 ILE A1096 6957 5638 3371 -499 -586 -2333 C ATOM 2560 CG2 ILE A1096 1.725 36.121 4.149 1.00 43.10 C ANISOU 2560 CG2 ILE A1096 7263 5467 3645 -916 -516 -2281 C ATOM 2561 CD1 ILE A1096 1.096 35.950 7.030 1.00 46.58 C ANISOU 2561 CD1 ILE A1096 7574 6215 3910 -675 -559 -2481 C ATOM 2562 N THR A1097 -0.257 39.006 3.004 1.00 59.55 N ANISOU 2562 N THR A1097 10337 6517 5774 -656 -330 -2460 N ATOM 2563 CA THR A1097 -0.217 39.572 1.661 1.00 58.22 C ANISOU 2563 CA THR A1097 10508 5965 5647 -686 -309 -2312 C ATOM 2564 C THR A1097 1.225 39.583 1.167 1.00 59.15 C ANISOU 2564 C THR A1097 10565 6114 5797 -1069 -289 -2251 C ATOM 2565 O THR A1097 1.541 40.176 0.136 1.00 58.17 O ANISOU 2565 O THR A1097 10716 5684 5700 -1181 -244 -2146 O ATOM 2566 CB THR A1097 -0.793 41.000 1.620 1.00 61.09 C ANISOU 2566 CB THR A1097 11323 5856 6032 -535 -214 -2393 C ATOM 2567 OG1 THR A1097 -0.003 41.863 2.446 1.00 62.76 O ANISOU 2567 OG1 THR A1097 11590 6007 6250 -778 -122 -2586 O ATOM 2568 CG2 THR A1097 -2.233 41.009 2.112 1.00 60.85 C ANISOU 2568 CG2 THR A1097 11330 5810 5981 -100 -228 -2443 C ATOM 2569 N GLU A1098 2.092 38.917 1.924 1.00 59.41 N ANISOU 2569 N GLU A1098 10233 6524 5814 -1237 -321 -2301 N ATOM 2570 CA GLU A1098 3.510 38.819 1.604 1.00 61.15 C ANISOU 2570 CA GLU A1098 10335 6844 6056 -1561 -303 -2242 C ATOM 2571 C GLU A1098 3.755 37.772 0.521 1.00 56.08 C ANISOU 2571 C GLU A1098 9524 6337 5446 -1589 -350 -2014 C ATOM 2572 O GLU A1098 3.066 36.753 0.465 1.00 51.92 O ANISOU 2572 O GLU A1098 8806 6007 4914 -1388 -423 -1922 O ATOM 2573 CB GLU A1098 4.308 38.482 2.870 1.00 63.39 C ANISOU 2573 CB GLU A1098 10319 7469 6296 -1666 -329 -2353 C ATOM 2574 CG GLU A1098 5.796 38.251 2.659 1.00 65.16 C ANISOU 2574 CG GLU A1098 10373 7861 6526 -1967 -305 -2287 C ATOM 2575 CD GLU A1098 6.508 37.845 3.938 1.00 65.15 C ANISOU 2575 CD GLU A1098 10092 8202 6462 -2031 -336 -2366 C ATOM 2576 OE1 GLU A1098 6.212 38.438 4.998 1.00 66.56 O ANISOU 2576 OE1 GLU A1098 10345 8361 6584 -1992 -331 -2543 O ATOM 2577 OE2 GLU A1098 7.356 36.929 3.884 1.00 62.69 O ANISOU 2577 OE2 GLU A1098 9496 8173 6151 -2111 -356 -2245 O ATOM 2578 N MET A1099 4.731 38.032 -0.345 1.00 57.11 N ANISOU 2578 N MET A1099 9728 6367 5604 -1843 -295 -1924 N ATOM 2579 CA MET A1099 5.100 37.087 -1.392 1.00 54.00 C ANISOU 2579 CA MET A1099 9175 6100 5242 -1897 -320 -1715 C ATOM 2580 C MET A1099 5.932 35.946 -0.813 1.00 41.55 C ANISOU 2580 C MET A1099 7167 4949 3672 -1946 -351 -1677 C ATOM 2581 O MET A1099 6.996 36.173 -0.238 1.00 46.11 O ANISOU 2581 O MET A1099 7636 5655 4231 -2135 -310 -1756 O ATOM 2582 CB MET A1099 5.873 37.793 -2.508 1.00 45.26 C ANISOU 2582 CB MET A1099 8303 4748 4147 -2141 -233 -1633 C ATOM 2583 CG MET A1099 5.168 39.011 -3.096 1.00 47.90 C ANISOU 2583 CG MET A1099 9119 4611 4468 -2084 -185 -1640 C ATOM 2584 SD MET A1099 3.665 38.621 -4.018 1.00 58.64 S ANISOU 2584 SD MET A1099 10677 5782 5821 -1754 -277 -1476 S ATOM 2585 CE MET A1099 2.400 38.963 -2.796 1.00 54.82 C ANISOU 2585 CE MET A1099 10272 5246 5313 -1426 -314 -1657 C ATOM 2586 N LEU A1100 5.443 34.721 -0.970 1.00 38.46 N ANISOU 2586 N LEU A1100 6548 4767 3300 -1766 -413 -1548 N ATOM 2587 CA LEU A1100 6.096 33.559 -0.380 1.00 36.60 C ANISOU 2587 CA LEU A1100 5941 4891 3073 -1749 -430 -1483 C ATOM 2588 C LEU A1100 6.801 32.709 -1.432 1.00 40.53 C ANISOU 2588 C LEU A1100 6299 5481 3620 -1846 -393 -1294 C ATOM 2589 O LEU A1100 6.568 32.866 -2.630 1.00 40.78 O ANISOU 2589 O LEU A1100 6495 5325 3673 -1890 -376 -1197 O ATOM 2590 CB LEU A1100 5.076 32.707 0.377 1.00 34.73 C ANISOU 2590 CB LEU A1100 5546 4829 2822 -1462 -500 -1468 C ATOM 2591 CG LEU A1100 4.166 33.459 1.351 1.00 36.40 C ANISOU 2591 CG LEU A1100 5900 4957 2972 -1316 -532 -1650 C ATOM 2592 CD1 LEU A1100 3.266 32.494 2.107 1.00 34.53 C ANISOU 2592 CD1 LEU A1100 5485 4928 2708 -1048 -584 -1606 C ATOM 2593 CD2 LEU A1100 4.985 34.307 2.313 1.00 39.48 C ANISOU 2593 CD2 LEU A1100 6331 5349 3322 -1484 -501 -1820 C ATOM 2594 N SER A1101 7.667 31.812 -0.974 1.00 38.50 N ANISOU 2594 N SER A1101 5754 5507 3369 -1872 -371 -1240 N ATOM 2595 CA SER A1101 8.332 30.868 -1.862 1.00 35.79 C ANISOU 2595 CA SER A1101 5255 5277 3066 -1930 -318 -1072 C ATOM 2596 C SER A1101 7.566 29.553 -1.884 1.00 34.23 C ANISOU 2596 C SER A1101 4890 5204 2911 -1697 -344 -937 C ATOM 2597 O SER A1101 6.814 29.254 -0.957 1.00 33.04 O ANISOU 2597 O SER A1101 4676 5128 2748 -1508 -394 -974 O ATOM 2598 CB SER A1101 9.779 30.632 -1.423 1.00 36.56 C ANISOU 2598 CB SER A1101 5153 5608 3130 -2092 -256 -1093 C ATOM 2599 OG SER A1101 9.832 30.069 -0.123 1.00 36.54 O ANISOU 2599 OG SER A1101 4945 5841 3096 -1972 -285 -1133 O ATOM 2600 N ARG A1102 7.755 28.773 -2.944 1.00 32.65 N ANISOU 2600 N ARG A1102 4630 5018 2756 -1718 -296 -783 N ATOM 2601 CA ARG A1102 7.100 27.475 -3.067 1.00 31.02 C ANISOU 2601 CA ARG A1102 4274 4913 2600 -1528 -291 -651 C ATOM 2602 C ARG A1102 7.496 26.554 -1.926 1.00 31.04 C ANISOU 2602 C ARG A1102 4035 5159 2599 -1431 -266 -643 C ATOM 2603 O ARG A1102 6.685 25.768 -1.445 1.00 28.57 O ANISOU 2603 O ARG A1102 3640 4903 2311 -1241 -277 -595 O ATOM 2604 CB ARG A1102 7.446 26.817 -4.400 1.00 30.30 C ANISOU 2604 CB ARG A1102 4164 4801 2550 -1611 -220 -500 C ATOM 2605 CG ARG A1102 7.029 27.616 -5.608 1.00 32.72 C ANISOU 2605 CG ARG A1102 4720 4866 2846 -1705 -239 -472 C ATOM 2606 CD ARG A1102 5.541 27.501 -5.875 1.00 34.05 C ANISOU 2606 CD ARG A1102 4974 4936 3029 -1522 -311 -439 C ATOM 2607 NE ARG A1102 5.104 28.528 -6.813 1.00 36.63 N ANISOU 2607 NE ARG A1102 5595 5010 3311 -1607 -353 -437 N ATOM 2608 CZ ARG A1102 5.341 28.499 -8.121 1.00 40.23 C ANISOU 2608 CZ ARG A1102 6163 5358 3765 -1735 -316 -316 C ATOM 2609 NH1 ARG A1102 6.011 27.487 -8.658 1.00 40.26 N ANISOU 2609 NH1 ARG A1102 5993 5497 3808 -1794 -228 -202 N ATOM 2610 NH2 ARG A1102 4.907 29.485 -8.893 1.00 41.63 N ANISOU 2610 NH2 ARG A1102 6657 5279 3884 -1797 -363 -305 N ATOM 2611 N GLU A1103 8.752 26.650 -1.505 1.00 34.17 N ANISOU 2611 N GLU A1103 4324 5705 2952 -1571 -225 -688 N ATOM 2612 CA GLU A1103 9.247 25.854 -0.391 1.00 36.05 C ANISOU 2612 CA GLU A1103 4340 6196 3161 -1494 -201 -685 C ATOM 2613 C GLU A1103 8.469 26.181 0.879 1.00 34.50 C ANISOU 2613 C GLU A1103 4167 6009 2932 -1360 -270 -779 C ATOM 2614 O GLU A1103 8.099 25.287 1.645 1.00 33.49 O ANISOU 2614 O GLU A1103 3909 6007 2809 -1200 -259 -726 O ATOM 2615 CB GLU A1103 10.745 26.093 -0.176 1.00 38.54 C ANISOU 2615 CB GLU A1103 4544 6695 3405 -1680 -154 -742 C ATOM 2616 CG GLU A1103 11.638 25.585 -1.305 1.00 39.05 C ANISOU 2616 CG GLU A1103 4552 6813 3472 -1796 -66 -646 C ATOM 2617 CD GLU A1103 11.656 26.508 -2.511 1.00 40.14 C ANISOU 2617 CD GLU A1103 4909 6718 3625 -1964 -57 -656 C ATOM 2618 OE1 GLU A1103 11.118 27.631 -2.413 1.00 40.98 O ANISOU 2618 OE1 GLU A1103 5208 6628 3734 -2010 -116 -753 O ATOM 2619 OE2 GLU A1103 12.211 26.109 -3.557 1.00 39.27 O ANISOU 2619 OE2 GLU A1103 4793 6617 3508 -2045 16 -568 O ATOM 2620 N PHE A1104 8.207 27.467 1.089 1.00 34.05 N ANISOU 2620 N PHE A1104 4291 5808 2838 -1431 -330 -921 N ATOM 2621 CA PHE A1104 7.486 27.898 2.278 1.00 34.01 C ANISOU 2621 CA PHE A1104 4334 5805 2784 -1319 -388 -1031 C ATOM 2622 C PHE A1104 6.004 27.549 2.199 1.00 31.30 C ANISOU 2622 C PHE A1104 4065 5354 2472 -1100 -423 -979 C ATOM 2623 O PHE A1104 5.386 27.237 3.216 1.00 30.91 O ANISOU 2623 O PHE A1104 3964 5385 2394 -960 -435 -994 O ATOM 2624 CB PHE A1104 7.651 29.400 2.503 1.00 37.69 C ANISOU 2624 CB PHE A1104 4994 6133 3194 -1467 -424 -1218 C ATOM 2625 CG PHE A1104 7.039 29.878 3.785 1.00 37.94 C ANISOU 2625 CG PHE A1104 5075 6181 3158 -1372 -470 -1350 C ATOM 2626 CD1 PHE A1104 7.712 29.720 4.985 1.00 39.25 C ANISOU 2626 CD1 PHE A1104 5081 6574 3257 -1412 -459 -1405 C ATOM 2627 CD2 PHE A1104 5.786 30.466 3.795 1.00 37.84 C ANISOU 2627 CD2 PHE A1104 5265 5979 3135 -1237 -519 -1423 C ATOM 2628 CE1 PHE A1104 7.151 30.149 6.170 1.00 40.59 C ANISOU 2628 CE1 PHE A1104 5301 6766 3356 -1337 -492 -1525 C ATOM 2629 CE2 PHE A1104 5.219 30.897 4.978 1.00 39.28 C ANISOU 2629 CE2 PHE A1104 5501 6179 3243 -1148 -546 -1550 C ATOM 2630 CZ PHE A1104 5.902 30.738 6.167 1.00 40.54 C ANISOU 2630 CZ PHE A1104 5507 6552 3343 -1207 -531 -1597 C ATOM 2631 N VAL A1105 5.435 27.611 0.999 1.00 29.76 N ANISOU 2631 N VAL A1105 3988 4995 2325 -1082 -432 -918 N ATOM 2632 CA VAL A1105 4.048 27.205 0.794 1.00 24.93 C ANISOU 2632 CA VAL A1105 3423 4317 1733 -883 -458 -861 C ATOM 2633 C VAL A1105 3.908 25.718 1.099 1.00 22.97 C ANISOU 2633 C VAL A1105 2966 4221 1540 -773 -391 -717 C ATOM 2634 O VAL A1105 2.948 25.282 1.739 1.00 22.42 O ANISOU 2634 O VAL A1105 2864 4186 1467 -623 -387 -702 O ATOM 2635 CB VAL A1105 3.573 27.488 -0.646 1.00 24.38 C ANISOU 2635 CB VAL A1105 3495 4077 1690 -903 -475 -813 C ATOM 2636 CG1 VAL A1105 2.157 26.975 -0.850 1.00 23.09 C ANISOU 2636 CG1 VAL A1105 3343 3898 1533 -697 -498 -750 C ATOM 2637 CG2 VAL A1105 3.651 28.974 -0.952 1.00 26.62 C ANISOU 2637 CG2 VAL A1105 4021 4172 1921 -1023 -518 -957 C ATOM 2638 N ARG A1106 4.887 24.949 0.634 1.00 22.15 N ANISOU 2638 N ARG A1106 2726 4207 1482 -863 -322 -621 N ATOM 2639 CA ARG A1106 4.973 23.523 0.911 1.00 26.50 C ANISOU 2639 CA ARG A1106 3086 4902 2081 -784 -242 -503 C ATOM 2640 C ARG A1106 5.021 23.286 2.410 1.00 27.67 C ANISOU 2640 C ARG A1106 3116 5227 2172 -716 -234 -552 C ATOM 2641 O ARG A1106 4.299 22.441 2.941 1.00 27.43 O ANISOU 2641 O ARG A1106 2991 5274 2158 -595 -195 -502 O ATOM 2642 CB ARG A1106 6.209 22.920 0.239 1.00 20.33 C ANISOU 2642 CB ARG A1106 2188 4212 1324 -909 -172 -426 C ATOM 2643 CG ARG A1106 6.506 21.486 0.640 1.00 19.55 C ANISOU 2643 CG ARG A1106 1874 4307 1247 -844 -90 -331 C ATOM 2644 CD ARG A1106 7.700 20.944 -0.120 1.00 19.30 C ANISOU 2644 CD ARG A1106 1746 4356 1233 -953 -29 -264 C ATOM 2645 NE ARG A1106 8.924 21.667 0.210 1.00 21.09 N ANISOU 2645 NE ARG A1106 1941 4699 1373 -1080 -37 -342 N ATOM 2646 CZ ARG A1106 10.057 21.569 -0.477 1.00 27.54 C ANISOU 2646 CZ ARG A1106 2694 5609 2160 -1219 18 -316 C ATOM 2647 NH1 ARG A1106 10.125 20.783 -1.542 1.00 26.99 N ANISOU 2647 NH1 ARG A1106 2597 5504 2152 -1241 78 -211 N ATOM 2648 NH2 ARG A1106 11.123 22.264 -0.102 1.00 29.24 N ANISOU 2648 NH2 ARG A1106 2871 5959 2281 -1347 15 -405 N ATOM 2649 N GLU A1107 5.875 24.050 3.084 1.00 29.30 N ANISOU 2649 N GLU A1107 3323 5500 2308 -807 -270 -655 N ATOM 2650 CA GLU A1107 6.002 23.966 4.533 1.00 29.81 C ANISOU 2650 CA GLU A1107 3281 5746 2300 -759 -271 -715 C ATOM 2651 C GLU A1107 4.675 24.274 5.221 1.00 29.53 C ANISOU 2651 C GLU A1107 3340 5634 2246 -629 -306 -770 C ATOM 2652 O GLU A1107 4.349 23.683 6.250 1.00 30.46 O ANISOU 2652 O GLU A1107 3339 5902 2334 -536 -275 -760 O ATOM 2653 CB GLU A1107 7.092 24.918 5.025 1.00 26.88 C ANISOU 2653 CB GLU A1107 2915 5449 1848 -911 -308 -842 C ATOM 2654 CG GLU A1107 7.468 24.732 6.480 1.00 64.60 C ANISOU 2654 CG GLU A1107 7547 10462 6535 -882 -305 -895 C ATOM 2655 CD GLU A1107 8.872 25.220 6.776 1.00 63.64 C ANISOU 2655 CD GLU A1107 7338 10508 6336 -1053 -308 -978 C ATOM 2656 OE1 GLU A1107 9.179 25.475 7.959 1.00 63.95 O ANISOU 2656 OE1 GLU A1107 7303 10715 6280 -1067 -328 -1068 O ATOM 2657 OE2 GLU A1107 9.670 25.342 5.821 1.00 61.43 O ANISOU 2657 OE2 GLU A1107 7051 10212 6078 -1185 -284 -958 O ATOM 2658 N LEU A1108 3.908 25.193 4.643 1.00 29.20 N ANISOU 2658 N LEU A1108 3504 5381 2209 -622 -365 -832 N ATOM 2659 CA LEU A1108 2.588 25.521 5.165 1.00 25.04 C ANISOU 2659 CA LEU A1108 3068 4792 1652 -495 -389 -888 C ATOM 2660 C LEU A1108 1.636 24.340 5.023 1.00 23.16 C ANISOU 2660 C LEU A1108 2726 4591 1484 -363 -326 -761 C ATOM 2661 O LEU A1108 0.993 23.938 5.991 1.00 27.78 O ANISOU 2661 O LEU A1108 3220 5288 2047 -269 -293 -773 O ATOM 2662 CB LEU A1108 2.018 26.746 4.453 1.00 30.39 C ANISOU 2662 CB LEU A1108 3985 5264 2297 -510 -459 -990 C ATOM 2663 CG LEU A1108 2.717 28.070 4.761 1.00 33.36 C ANISOU 2663 CG LEU A1108 4504 5573 2598 -641 -511 -1165 C ATOM 2664 CD1 LEU A1108 2.393 29.098 3.695 1.00 34.22 C ANISOU 2664 CD1 LEU A1108 4852 5451 2697 -672 -563 -1244 C ATOM 2665 CD2 LEU A1108 2.320 28.578 6.140 1.00 36.01 C ANISOU 2665 CD2 LEU A1108 4870 5966 2847 -592 -518 -1300 C ATOM 2666 N TYR A1109 1.558 23.783 3.817 1.00 27.86 N ANISOU 2666 N TYR A1109 3313 5120 2155 -374 -299 -655 N ATOM 2667 CA TYR A1109 0.669 22.654 3.550 1.00 20.22 C ANISOU 2667 CA TYR A1109 2230 4201 1250 -285 -229 -554 C ATOM 2668 C TYR A1109 0.992 21.455 4.438 1.00 29.86 C ANISOU 2668 C TYR A1109 3236 5626 2481 -251 -153 -496 C ATOM 2669 O TYR A1109 0.124 20.631 4.725 1.00 27.84 O ANISOU 2669 O TYR A1109 2890 5432 2256 -164 -108 -453 O ATOM 2670 CB TYR A1109 0.748 22.239 2.079 1.00 24.31 C ANISOU 2670 CB TYR A1109 2770 4624 1841 -337 -209 -457 C ATOM 2671 CG TYR A1109 0.177 23.247 1.108 1.00 23.94 C ANISOU 2671 CG TYR A1109 2936 4380 1781 -332 -290 -491 C ATOM 2672 CD1 TYR A1109 -0.762 24.180 1.517 1.00 26.83 C ANISOU 2672 CD1 TYR A1109 3422 4698 2075 -252 -354 -592 C ATOM 2673 CD2 TYR A1109 0.575 23.260 -0.223 1.00 25.38 C ANISOU 2673 CD2 TYR A1109 3178 4461 2002 -408 -298 -431 C ATOM 2674 CE1 TYR A1109 -1.288 25.102 0.631 1.00 29.65 C ANISOU 2674 CE1 TYR A1109 3957 4927 2382 -241 -431 -635 C ATOM 2675 CE2 TYR A1109 0.054 24.178 -1.117 1.00 18.89 C ANISOU 2675 CE2 TYR A1109 2529 3509 1139 -402 -377 -467 C ATOM 2676 CZ TYR A1109 -0.876 25.097 -0.683 1.00 29.85 C ANISOU 2676 CZ TYR A1109 4044 4859 2438 -311 -451 -569 C ATOM 2677 OH TYR A1109 -1.400 26.014 -1.564 1.00 31.70 O ANISOU 2677 OH TYR A1109 4465 4977 2601 -287 -536 -612 O ATOM 2678 N GLY A1110 2.244 21.361 4.872 1.00 33.19 N ANISOU 2678 N GLY A1110 3581 6161 2870 -319 -148 -498 N ATOM 2679 CA GLY A1110 2.666 20.277 5.737 1.00 36.76 C ANISOU 2679 CA GLY A1110 3846 6811 3309 -269 -97 -442 C ATOM 2680 C GLY A1110 2.664 20.657 7.205 1.00 37.27 C ANISOU 2680 C GLY A1110 3875 7007 3279 -223 -121 -529 C ATOM 2681 O GLY A1110 3.255 19.968 8.035 1.00 36.75 O ANISOU 2681 O GLY A1110 3669 7125 3171 -188 -98 -496 O ATOM 2682 N SER A1111 1.999 21.760 7.529 1.00 38.55 N ANISOU 2682 N SER A1111 4172 7075 3399 -217 -173 -643 N ATOM 2683 CA SER A1111 1.911 22.215 8.911 1.00 25.03 C ANISOU 2683 CA SER A1111 2444 5474 1592 -186 -196 -744 C ATOM 2684 C SER A1111 0.458 22.366 9.344 1.00 29.66 C ANISOU 2684 C SER A1111 3081 6013 2176 -77 -192 -788 C ATOM 2685 O SER A1111 0.045 21.817 10.365 1.00 29.18 O ANISOU 2685 O SER A1111 2917 6090 2079 1 -164 -784 O ATOM 2686 CB SER A1111 2.653 23.539 9.090 1.00 26.68 C ANISOU 2686 CB SER A1111 2774 5633 1729 -303 -267 -877 C ATOM 2687 OG SER A1111 4.020 23.409 8.738 1.00 34.87 O ANISOU 2687 OG SER A1111 3735 6752 2760 -414 -265 -847 O ATOM 2688 N VAL A1112 -0.310 23.109 8.555 1.00 24.60 N ANISOU 2688 N VAL A1112 2596 5185 1565 -69 -223 -828 N ATOM 2689 CA VAL A1112 -1.723 23.337 8.837 1.00 24.74 C ANISOU 2689 CA VAL A1112 2654 5168 1577 41 -217 -877 C ATOM 2690 C VAL A1112 -2.505 22.028 8.908 1.00 23.66 C ANISOU 2690 C VAL A1112 2351 5140 1498 125 -149 -774 C ATOM 2691 O VAL A1112 -2.046 20.992 8.426 1.00 22.54 O ANISOU 2691 O VAL A1112 2111 5039 1416 97 -111 -657 O ATOM 2692 CB VAL A1112 -2.367 24.240 7.770 1.00 24.52 C ANISOU 2692 CB VAL A1112 2808 4942 1567 50 -262 -917 C ATOM 2693 CG1 VAL A1112 -1.665 25.590 7.724 1.00 26.18 C ANISOU 2693 CG1 VAL A1112 3197 5052 1699 -41 -334 -1048 C ATOM 2694 CG2 VAL A1112 -2.319 23.562 6.412 1.00 22.70 C ANISOU 2694 CG2 VAL A1112 2558 4640 1429 22 -244 -787 C ATOM 2695 N ASP A1113 -3.683 22.078 9.520 1.00 24.19 N ANISOU 2695 N ASP A1113 2395 5252 1544 222 -136 -825 N ATOM 2696 CA ASP A1113 -4.551 20.910 9.593 1.00 23.48 C ANISOU 2696 CA ASP A1113 2166 5256 1499 282 -85 -744 C ATOM 2697 C ASP A1113 -5.421 20.819 8.350 1.00 29.55 C ANISOU 2697 C ASP A1113 2955 5932 2341 302 -79 -706 C ATOM 2698 O ASP A1113 -5.482 19.779 7.694 1.00 21.22 O ANISOU 2698 O ASP A1113 1823 4889 1352 270 -48 -601 O ATOM 2699 CB ASP A1113 -5.435 20.961 10.839 1.00 34.94 C ANISOU 2699 CB ASP A1113 3568 6822 2884 364 -74 -819 C ATOM 2700 CG ASP A1113 -4.635 20.983 12.122 1.00 36.89 C ANISOU 2700 CG ASP A1113 3788 7186 3042 346 -78 -855 C ATOM 2701 OD1 ASP A1113 -3.977 19.967 12.431 1.00 36.62 O ANISOU 2701 OD1 ASP A1113 3659 7249 3004 326 -58 -758 O ATOM 2702 OD2 ASP A1113 -4.679 22.013 12.829 1.00 38.13 O ANISOU 2702 OD2 ASP A1113 4025 7339 3123 356 -104 -984 O ATOM 2703 N PHE A1114 -6.095 21.919 8.037 1.00 29.90 N ANISOU 2703 N PHE A1114 3112 5885 2363 355 -116 -797 N ATOM 2704 CA PHE A1114 -6.990 21.962 6.891 1.00 27.81 C ANISOU 2704 CA PHE A1114 2863 5559 2145 394 -122 -772 C ATOM 2705 C PHE A1114 -6.671 23.129 5.971 1.00 26.28 C ANISOU 2705 C PHE A1114 2832 5234 1921 389 -188 -827 C ATOM 2706 O PHE A1114 -6.174 24.167 6.409 1.00 29.74 O ANISOU 2706 O PHE A1114 3393 5619 2288 382 -235 -933 O ATOM 2707 CB PHE A1114 -8.445 22.053 7.351 1.00 28.45 C ANISOU 2707 CB PHE A1114 2847 5767 2195 525 -116 -847 C ATOM 2708 CG PHE A1114 -8.892 20.887 8.182 1.00 28.49 C ANISOU 2708 CG PHE A1114 2703 5911 2210 513 -69 -798 C ATOM 2709 CD1 PHE A1114 -9.377 19.740 7.582 1.00 26.52 C ANISOU 2709 CD1 PHE A1114 2346 5718 2013 468 -43 -705 C ATOM 2710 CD2 PHE A1114 -8.831 20.940 9.564 1.00 24.37 C ANISOU 2710 CD2 PHE A1114 2156 5480 1622 537 -60 -857 C ATOM 2711 CE1 PHE A1114 -9.789 18.663 8.342 1.00 25.36 C ANISOU 2711 CE1 PHE A1114 2099 5694 1845 441 -19 -671 C ATOM 2712 CE2 PHE A1114 -9.243 19.867 10.329 1.00 24.66 C ANISOU 2712 CE2 PHE A1114 2077 5654 1640 525 -28 -814 C ATOM 2713 CZ PHE A1114 -9.722 18.727 9.716 1.00 23.84 C ANISOU 2713 CZ PHE A1114 1895 5582 1580 474 -10 -721 C ATOM 2714 N VAL A1115 -6.964 22.949 4.690 1.00 23.58 N ANISOU 2714 N VAL A1115 2502 4835 1621 381 -196 -761 N ATOM 2715 CA VAL A1115 -6.800 24.016 3.717 1.00 22.39 C ANISOU 2715 CA VAL A1115 2519 4559 1428 386 -274 -803 C ATOM 2716 C VAL A1115 -8.127 24.264 3.007 1.00 23.09 C ANISOU 2716 C VAL A1115 2565 4712 1498 541 -301 -832 C ATOM 2717 O VAL A1115 -8.721 23.352 2.436 1.00 22.01 O ANISOU 2717 O VAL A1115 2299 4648 1416 534 -256 -744 O ATOM 2718 CB VAL A1115 -5.694 23.688 2.696 1.00 21.01 C ANISOU 2718 CB VAL A1115 2427 4252 1304 226 -282 -689 C ATOM 2719 CG1 VAL A1115 -5.825 22.253 2.206 1.00 19.22 C ANISOU 2719 CG1 VAL A1115 2061 4066 1178 177 -200 -554 C ATOM 2720 CG2 VAL A1115 -5.721 24.678 1.538 1.00 22.04 C ANISOU 2720 CG2 VAL A1115 2733 4259 1384 227 -371 -713 C ATOM 2721 N ILE A1116 -8.594 25.505 3.061 1.00 24.93 N ANISOU 2721 N ILE A1116 2907 4923 1644 697 -376 -968 N ATOM 2722 CA ILE A1116 -9.900 25.851 2.525 1.00 28.85 C ANISOU 2722 CA ILE A1116 3347 5513 2099 922 -419 -1017 C ATOM 2723 C ILE A1116 -9.802 26.434 1.120 1.00 30.18 C ANISOU 2723 C ILE A1116 3673 5560 2234 954 -510 -976 C ATOM 2724 O ILE A1116 -9.104 27.420 0.883 1.00 31.13 O ANISOU 2724 O ILE A1116 4030 5498 2298 942 -581 -1034 O ATOM 2725 CB ILE A1116 -10.627 26.843 3.446 1.00 28.47 C ANISOU 2725 CB ILE A1116 3329 5516 1972 1157 -450 -1202 C ATOM 2726 CG1 ILE A1116 -10.760 26.244 4.847 1.00 30.53 C ANISOU 2726 CG1 ILE A1116 3436 5906 2258 1107 -368 -1227 C ATOM 2727 CG2 ILE A1116 -11.993 27.197 2.881 1.00 30.37 C ANISOU 2727 CG2 ILE A1116 3497 5882 2159 1448 -505 -1253 C ATOM 2728 CD1 ILE A1116 -11.364 27.182 5.858 1.00 33.35 C ANISOU 2728 CD1 ILE A1116 3831 6296 2545 1296 -380 -1408 C ATOM 2729 N ILE A1117 -10.511 25.796 0.195 1.00 30.05 N ANISOU 2729 N ILE A1117 3532 5639 2245 978 -504 -877 N ATOM 2730 CA ILE A1117 -10.560 26.209 -1.199 1.00 26.04 C ANISOU 2730 CA ILE A1117 3146 5044 1705 1012 -595 -804 C ATOM 2731 C ILE A1117 -11.999 26.553 -1.573 1.00 27.88 C ANISOU 2731 C ILE A1117 3279 5443 1870 1311 -655 -847 C ATOM 2732 O ILE A1117 -12.714 25.732 -2.151 1.00 27.34 O ANISOU 2732 O ILE A1117 3023 5528 1838 1276 -606 -770 O ATOM 2733 CB ILE A1117 -10.025 25.105 -2.127 1.00 23.83 C ANISOU 2733 CB ILE A1117 2816 4720 1518 745 -534 -634 C ATOM 2734 CG1 ILE A1117 -8.764 24.478 -1.528 1.00 22.10 C ANISOU 2734 CG1 ILE A1117 2621 4403 1374 510 -453 -594 C ATOM 2735 CG2 ILE A1117 -9.762 25.650 -3.521 1.00 24.19 C ANISOU 2735 CG2 ILE A1117 3033 4632 1524 724 -637 -548 C ATOM 2736 CD1 ILE A1117 -8.287 23.252 -2.259 1.00 23.76 C ANISOU 2736 CD1 ILE A1117 2774 4569 1684 315 -374 -455 C ATOM 2737 N PRO A1118 -12.432 27.774 -1.228 1.00 30.31 N ANISOU 2737 N PRO A1118 3728 5718 2070 1620 -753 -984 N ATOM 2738 CA PRO A1118 -13.811 28.227 -1.426 1.00 32.60 C ANISOU 2738 CA PRO A1118 3925 6186 2275 1985 -823 -1041 C ATOM 2739 C PRO A1118 -14.066 28.750 -2.835 1.00 33.74 C ANISOU 2739 C PRO A1118 4198 6241 2379 2123 -956 -913 C ATOM 2740 O PRO A1118 -14.813 29.714 -2.999 1.00 36.44 O ANISOU 2740 O PRO A1118 4629 6553 2662 2486 -1055 -943 O ATOM 2741 CB PRO A1118 -13.946 29.349 -0.400 1.00 34.83 C ANISOU 2741 CB PRO A1118 4383 6392 2460 2260 -855 -1248 C ATOM 2742 CG PRO A1118 -12.575 29.937 -0.343 1.00 34.36 C ANISOU 2742 CG PRO A1118 4637 5980 2437 2058 -855 -1256 C ATOM 2743 CD PRO A1118 -11.608 28.803 -0.569 1.00 31.30 C ANISOU 2743 CD PRO A1118 4131 5619 2144 1646 -787 -1113 C ATOM 2744 N SER A1119 -13.461 28.111 -3.833 1.00 31.89 N ANISOU 2744 N SER A1119 3970 5925 2221 1827 -931 -749 N ATOM 2745 CA SER A1119 -13.537 28.573 -5.217 1.00 32.86 C ANISOU 2745 CA SER A1119 4235 5928 2321 1893 -1043 -602 C ATOM 2746 C SER A1119 -14.963 28.621 -5.760 1.00 37.28 C ANISOU 2746 C SER A1119 4603 6700 2861 2142 -1074 -571 C ATOM 2747 O SER A1119 -15.889 28.081 -5.158 1.00 35.17 O ANISOU 2747 O SER A1119 4063 6706 2595 2201 -988 -665 O ATOM 2748 CB SER A1119 -12.682 27.680 -6.115 1.00 30.37 C ANISOU 2748 CB SER A1119 3913 5537 2090 1493 -981 -455 C ATOM 2749 OG SER A1119 -11.325 27.690 -5.707 1.00 31.40 O ANISOU 2749 OG SER A1119 4211 5480 2241 1262 -948 -474 O ATOM 2750 N TYR A1120 -15.128 29.270 -6.908 1.00 40.37 N ANISOU 2750 N TYR A1120 5146 6966 3226 2273 -1185 -440 N ATOM 2751 CA TYR A1120 -16.441 29.410 -7.528 1.00 45.31 C ANISOU 2751 CA TYR A1120 5604 7785 3827 2498 -1215 -401 C ATOM 2752 C TYR A1120 -16.605 28.532 -8.772 1.00 48.18 C ANISOU 2752 C TYR A1120 5828 8258 4219 2221 -1187 -266 C ATOM 2753 O TYR A1120 -17.725 28.161 -9.123 1.00 50.44 O ANISOU 2753 O TYR A1120 5879 8806 4480 2281 -1163 -273 O ATOM 2754 CB TYR A1120 -16.706 30.876 -7.891 1.00 42.27 C ANISOU 2754 CB TYR A1120 5495 7176 3389 2910 -1351 -346 C ATOM 2755 CG TYR A1120 -17.324 31.706 -6.780 1.00 44.64 C ANISOU 2755 CG TYR A1120 5821 7479 3662 3310 -1362 -497 C ATOM 2756 CD1 TYR A1120 -18.697 31.701 -6.564 1.00 46.89 C ANISOU 2756 CD1 TYR A1120 5842 8055 3920 3533 -1323 -570 C ATOM 2757 CD2 TYR A1120 -16.538 32.507 -5.962 1.00 46.49 C ANISOU 2757 CD2 TYR A1120 6362 7406 3897 3438 -1393 -577 C ATOM 2758 CE1 TYR A1120 -19.267 32.463 -5.556 1.00 49.24 C ANISOU 2758 CE1 TYR A1120 6164 8345 4200 3878 -1309 -714 C ATOM 2759 CE2 TYR A1120 -17.101 33.273 -4.953 1.00 47.23 C ANISOU 2759 CE2 TYR A1120 6489 7442 4014 3756 -1344 -735 C ATOM 2760 CZ TYR A1120 -18.465 33.246 -4.755 1.00 49.37 C ANISOU 2760 CZ TYR A1120 6477 8032 4250 4023 -1328 -794 C ATOM 2761 OH TYR A1120 -19.031 34.004 -3.755 1.00 51.86 O ANISOU 2761 OH TYR A1120 6828 8300 4575 4331 -1273 -951 O ATOM 2762 N PHE A1121 -15.501 28.201 -9.439 1.00 51.14 N ANISOU 2762 N PHE A1121 6355 8441 4633 1915 -1187 -157 N ATOM 2763 CA PHE A1121 -15.573 27.379 -10.652 1.00 55.10 C ANISOU 2763 CA PHE A1121 6763 9016 5157 1652 -1168 -40 C ATOM 2764 C PHE A1121 -14.286 26.604 -10.946 1.00 55.10 C ANISOU 2764 C PHE A1121 6861 8851 5222 1252 -1101 18 C ATOM 2765 O PHE A1121 -14.122 26.071 -12.044 1.00 57.99 O ANISOU 2765 O PHE A1121 7234 9200 5599 1043 -1102 117 O ATOM 2766 CB PHE A1121 -15.937 28.250 -11.862 1.00 59.44 C ANISOU 2766 CB PHE A1121 7452 9492 5642 1838 -1307 99 C ATOM 2767 CG PHE A1121 -14.935 29.334 -12.164 1.00 61.03 C ANISOU 2767 CG PHE A1121 8037 9336 5814 1913 -1399 194 C ATOM 2768 CD1 PHE A1121 -15.036 30.579 -11.563 1.00 64.34 C ANISOU 2768 CD1 PHE A1121 8681 9571 6193 2287 -1467 153 C ATOM 2769 CD2 PHE A1121 -13.903 29.114 -13.064 1.00 60.41 C ANISOU 2769 CD2 PHE A1121 8127 9084 5742 1612 -1403 316 C ATOM 2770 CE1 PHE A1121 -14.121 31.578 -11.843 1.00 65.89 C ANISOU 2770 CE1 PHE A1121 9302 9377 6356 2347 -1532 234 C ATOM 2771 CE2 PHE A1121 -12.985 30.108 -13.348 1.00 61.85 C ANISOU 2771 CE2 PHE A1121 8691 8926 5885 1662 -1462 395 C ATOM 2772 CZ PHE A1121 -13.094 31.342 -12.737 1.00 64.92 C ANISOU 2772 CZ PHE A1121 9344 9089 6233 2022 -1526 355 C ATOM 2773 N GLU A1122 -13.401 26.544 -9.949 1.00 52.00 N ANISOU 2773 N GLU A1122 6542 8347 4868 1159 -1040 -56 N ATOM 2774 CA GLU A1122 -12.076 25.904 -10.026 1.00 47.49 C ANISOU 2774 CA GLU A1122 6072 7611 4360 815 -967 -18 C ATOM 2775 C GLU A1122 -11.955 24.729 -11.001 1.00 40.43 C ANISOU 2775 C GLU A1122 5103 6732 3527 541 -895 56 C ATOM 2776 O GLU A1122 -12.445 23.636 -10.726 1.00 36.47 O ANISOU 2776 O GLU A1122 4392 6383 3083 463 -770 4 O ATOM 2777 CB GLU A1122 -11.670 25.429 -8.630 1.00 50.66 C ANISOU 2777 CB GLU A1122 6391 8039 4820 750 -854 -136 C ATOM 2778 CG GLU A1122 -10.276 24.837 -8.542 1.00 51.38 C ANISOU 2778 CG GLU A1122 6581 7959 4982 452 -776 -106 C ATOM 2779 CD GLU A1122 -9.187 25.892 -8.573 1.00 55.09 C ANISOU 2779 CD GLU A1122 7318 8231 5383 428 -861 -97 C ATOM 2780 OE1 GLU A1122 -9.155 26.744 -7.660 1.00 55.29 O ANISOU 2780 OE1 GLU A1122 7426 8229 5352 604 -901 -205 O ATOM 2781 OE2 GLU A1122 -8.362 25.866 -9.510 1.00 59.68 O ANISOU 2781 OE2 GLU A1122 8044 8676 5956 237 -879 -1 O ATOM 2782 N PRO A1123 -11.278 24.951 -12.139 1.00 34.48 N ANISOU 2782 N PRO A1123 4687 5439 2975 433 -1058 503 N ATOM 2783 CA PRO A1123 -11.207 23.930 -13.189 1.00 34.36 C ANISOU 2783 CA PRO A1123 4776 5491 2787 293 -1102 416 C ATOM 2784 C PRO A1123 -10.061 22.930 -13.024 1.00 30.33 C ANISOU 2784 C PRO A1123 4383 4888 2252 170 -934 274 C ATOM 2785 O PRO A1123 -10.133 21.838 -13.587 1.00 30.42 O ANISOU 2785 O PRO A1123 4455 4942 2161 90 -951 144 O ATOM 2786 CB PRO A1123 -11.019 24.761 -14.464 1.00 28.29 C ANISOU 2786 CB PRO A1123 4137 4752 1859 319 -1197 579 C ATOM 2787 CG PRO A1123 -10.459 26.097 -14.003 1.00 35.79 C ANISOU 2787 CG PRO A1123 5094 5583 2921 422 -1138 754 C ATOM 2788 CD PRO A1123 -10.509 26.155 -12.496 1.00 34.20 C ANISOU 2788 CD PRO A1123 4754 5311 2929 494 -1039 672 C ATOM 2789 N PHE A1124 -9.030 23.287 -12.264 1.00 27.41 N ANISOU 2789 N PHE A1124 4028 4405 1980 176 -785 288 N ATOM 2790 CA PHE A1124 -7.862 22.423 -12.127 1.00 20.07 C ANISOU 2790 CA PHE A1124 3181 3398 1046 82 -634 180 C ATOM 2791 C PHE A1124 -7.676 21.923 -10.698 1.00 25.07 C ANISOU 2791 C PHE A1124 3717 3971 1839 107 -535 102 C ATOM 2792 O PHE A1124 -7.466 20.730 -10.474 1.00 23.98 O ANISOU 2792 O PHE A1124 3602 3807 1702 54 -476 -1 O ATOM 2793 CB PHE A1124 -6.607 23.159 -12.596 1.00 24.13 C ANISOU 2793 CB PHE A1124 3783 3879 1508 58 -549 261 C ATOM 2794 CG PHE A1124 -6.710 23.691 -13.995 1.00 22.82 C ANISOU 2794 CG PHE A1124 3733 3773 1163 56 -623 365 C ATOM 2795 CD1 PHE A1124 -6.517 22.857 -15.083 1.00 26.15 C ANISOU 2795 CD1 PHE A1124 4282 4237 1418 9 -605 272 C ATOM 2796 CD2 PHE A1124 -7.009 25.024 -14.222 1.00 25.93 C ANISOU 2796 CD2 PHE A1124 4130 4183 1538 137 -713 567 C ATOM 2797 CE1 PHE A1124 -6.616 23.343 -16.372 1.00 28.73 C ANISOU 2797 CE1 PHE A1124 4734 4655 1528 36 -672 369 C ATOM 2798 CE2 PHE A1124 -7.108 25.516 -15.509 1.00 28.85 C ANISOU 2798 CE2 PHE A1124 4628 4614 1721 154 -785 698 C ATOM 2799 CZ PHE A1124 -6.911 24.675 -16.586 1.00 29.97 C ANISOU 2799 CZ PHE A1124 4895 4833 1660 100 -762 594 C ATOM 2800 N GLY A1125 -7.749 22.838 -9.737 1.00 24.76 N ANISOU 2800 N GLY A1125 3589 3909 1908 215 -521 151 N ATOM 2801 CA GLY A1125 -7.629 22.484 -8.334 1.00 22.60 C ANISOU 2801 CA GLY A1125 3240 3599 1746 265 -439 82 C ATOM 2802 C GLY A1125 -6.251 21.982 -7.950 1.00 23.18 C ANISOU 2802 C GLY A1125 3355 3595 1856 216 -323 37 C ATOM 2803 O GLY A1125 -6.123 21.034 -7.176 1.00 23.55 O ANISOU 2803 O GLY A1125 3376 3626 1945 211 -270 -13 O ATOM 2804 N LEU A1126 -5.218 22.622 -8.487 1.00 21.79 N ANISOU 2804 N LEU A1126 3234 3396 1650 198 -292 71 N ATOM 2805 CA LEU A1126 -3.847 22.225 -8.192 1.00 21.07 C ANISOU 2805 CA LEU A1126 3154 3267 1586 174 -197 29 C ATOM 2806 C LEU A1126 -3.490 22.475 -6.730 1.00 19.56 C ANISOU 2806 C LEU A1126 2892 3049 1490 257 -174 -3 C ATOM 2807 O LEU A1126 -2.621 21.804 -6.183 1.00 20.20 O ANISOU 2807 O LEU A1126 2951 3120 1604 261 -121 -36 O ATOM 2808 CB LEU A1126 -2.863 22.959 -9.105 1.00 20.39 C ANISOU 2808 CB LEU A1126 3135 3200 1413 146 -164 81 C ATOM 2809 CG LEU A1126 -2.892 22.573 -10.585 1.00 21.52 C ANISOU 2809 CG LEU A1126 3368 3397 1410 50 -158 99 C ATOM 2810 CD1 LEU A1126 -1.739 23.226 -11.331 1.00 17.03 C ANISOU 2810 CD1 LEU A1126 2866 2864 739 25 -79 164 C ATOM 2811 CD2 LEU A1126 -2.859 21.061 -10.749 1.00 15.82 C ANISOU 2811 CD2 LEU A1126 2665 2670 674 -2 -108 -17 C ATOM 2812 N VAL A1127 -4.156 23.438 -6.100 1.00 19.82 N ANISOU 2812 N VAL A1127 2894 3093 1545 346 -221 2 N ATOM 2813 CA VAL A1127 -3.942 23.693 -4.679 1.00 19.39 C ANISOU 2813 CA VAL A1127 2781 3049 1537 423 -207 -60 C ATOM 2814 C VAL A1127 -4.413 22.497 -3.859 1.00 19.07 C ANISOU 2814 C VAL A1127 2680 3033 1531 413 -175 -69 C ATOM 2815 O VAL A1127 -3.768 22.113 -2.885 1.00 18.38 O ANISOU 2815 O VAL A1127 2557 2966 1460 433 -146 -87 O ATOM 2816 CB VAL A1127 -4.664 24.977 -4.208 1.00 13.30 C ANISOU 2816 CB VAL A1127 2009 2300 744 561 -264 -95 C ATOM 2817 CG1 VAL A1127 -4.940 24.936 -2.708 1.00 13.34 C ANISOU 2817 CG1 VAL A1127 1935 2368 767 634 -244 -186 C ATOM 2818 CG2 VAL A1127 -3.842 26.203 -4.568 1.00 14.20 C ANISOU 2818 CG2 VAL A1127 2227 2368 801 615 -304 -100 C ATOM 2819 N ALA A1128 -5.527 21.900 -4.270 1.00 19.58 N ANISOU 2819 N ALA A1128 2739 3123 1578 391 -193 -47 N ATOM 2820 CA ALA A1128 -6.035 20.708 -3.603 1.00 12.24 C ANISOU 2820 CA ALA A1128 1776 2237 639 387 -162 -39 C ATOM 2821 C ALA A1128 -5.011 19.580 -3.671 1.00 15.06 C ANISOU 2821 C ALA A1128 2180 2550 992 347 -116 -29 C ATOM 2822 O ALA A1128 -4.714 18.952 -2.664 1.00 15.70 O ANISOU 2822 O ALA A1128 2236 2663 1068 394 -80 -2 O ATOM 2823 CB ALA A1128 -7.355 20.270 -4.217 1.00 13.02 C ANISOU 2823 CB ALA A1128 1860 2404 684 362 -208 -32 C ATOM 2824 N LEU A1129 -4.460 19.342 -4.857 1.00 13.68 N ANISOU 2824 N LEU A1129 2074 2330 794 285 -114 -47 N ATOM 2825 CA LEU A1129 -3.462 18.291 -5.043 1.00 12.29 C ANISOU 2825 CA LEU A1129 1940 2138 593 297 -56 -61 C ATOM 2826 C LEU A1129 -2.191 18.555 -4.241 1.00 16.86 C ANISOU 2826 C LEU A1129 2468 2725 1211 377 -33 -43 C ATOM 2827 O LEU A1129 -1.720 17.691 -3.497 1.00 19.92 O ANISOU 2827 O LEU A1129 2844 3143 1583 468 -2 -8 O ATOM 2828 CB LEU A1129 -3.108 18.147 -6.524 1.00 12.86 C ANISOU 2828 CB LEU A1129 2088 2196 603 224 -38 -114 C ATOM 2829 CG LEU A1129 -4.209 17.641 -7.455 1.00 16.80 C ANISOU 2829 CG LEU A1129 2651 2722 1011 138 -76 -166 C ATOM 2830 CD1 LEU A1129 -3.723 17.633 -8.895 1.00 18.75 C ANISOU 2830 CD1 LEU A1129 2976 2983 1163 58 -50 -227 C ATOM 2831 CD2 LEU A1129 -4.658 16.255 -7.034 1.00 16.78 C ANISOU 2831 CD2 LEU A1129 2687 2731 956 167 -45 -224 C ATOM 2832 N GLU A1130 -1.642 19.754 -4.406 1.00 15.82 N ANISOU 2832 N GLU A1130 2318 2591 1103 361 -53 -57 N ATOM 2833 CA GLU A1130 -0.392 20.140 -3.761 1.00 16.51 C ANISOU 2833 CA GLU A1130 2351 2728 1192 425 -50 -67 C ATOM 2834 C GLU A1130 -0.510 20.083 -2.241 1.00 16.20 C ANISOU 2834 C GLU A1130 2239 2754 1161 494 -78 -56 C ATOM 2835 O GLU A1130 0.397 19.607 -1.559 1.00 12.72 O ANISOU 2835 O GLU A1130 1743 2399 690 579 -78 -39 O ATOM 2836 CB GLU A1130 0.028 21.542 -4.217 1.00 17.91 C ANISOU 2836 CB GLU A1130 2544 2910 1352 387 -68 -93 C ATOM 2837 CG GLU A1130 0.450 21.608 -5.679 1.00 18.94 C ANISOU 2837 CG GLU A1130 2748 3025 1424 327 -17 -81 C ATOM 2838 CD GLU A1130 0.453 23.024 -6.233 1.00 20.93 C ANISOU 2838 CD GLU A1130 3054 3283 1618 296 -34 -59 C ATOM 2839 OE1 GLU A1130 -0.255 23.889 -5.673 1.00 21.21 O ANISOU 2839 OE1 GLU A1130 3088 3301 1669 331 -100 -66 O ATOM 2840 OE2 GLU A1130 1.165 23.272 -7.231 1.00 21.57 O ANISOU 2840 OE2 GLU A1130 3186 3396 1612 258 34 -26 O ATOM 2841 N ALA A1131 -1.636 20.553 -1.717 1.00 14.78 N ANISOU 2841 N ALA A1131 2052 2570 995 478 -98 -63 N ATOM 2842 CA ALA A1131 -1.892 20.501 -0.282 1.00 13.89 C ANISOU 2842 CA ALA A1131 1880 2547 850 537 -106 -60 C ATOM 2843 C ALA A1131 -2.065 19.062 0.195 1.00 13.08 C ANISOU 2843 C ALA A1131 1778 2482 710 580 -68 33 C ATOM 2844 O ALA A1131 -1.471 18.663 1.195 1.00 16.10 O ANISOU 2844 O ALA A1131 2116 2964 1037 654 -69 78 O ATOM 2845 CB ALA A1131 -3.118 21.324 0.069 1.00 13.15 C ANISOU 2845 CB ALA A1131 1774 2472 751 544 -115 -99 C ATOM 2846 N MET A1132 -2.876 18.291 -0.526 1.00 12.89 N ANISOU 2846 N MET A1132 1809 2400 688 543 -39 70 N ATOM 2847 CA MET A1132 -3.146 16.900 -0.167 1.00 13.87 C ANISOU 2847 CA MET A1132 1964 2552 753 590 13 182 C ATOM 2848 C MET A1132 -1.876 16.061 -0.116 1.00 18.27 C ANISOU 2848 C MET A1132 2540 3113 1288 703 40 254 C ATOM 2849 O MET A1132 -1.734 15.200 0.751 1.00 19.83 O ANISOU 2849 O MET A1132 2734 3359 1440 796 78 401 O ATOM 2850 CB MET A1132 -4.137 16.272 -1.149 1.00 15.11 C ANISOU 2850 CB MET A1132 2196 2660 883 525 39 182 C ATOM 2851 CG MET A1132 -5.592 16.647 -0.899 1.00 16.43 C ANISOU 2851 CG MET A1132 2316 2898 1029 473 32 180 C ATOM 2852 SD MET A1132 -6.652 16.320 -2.322 1.00 19.42 S ANISOU 2852 SD MET A1132 2746 3281 1353 378 3 117 S ATOM 2853 CE MET A1132 -6.709 14.531 -2.303 1.00 16.14 C ANISOU 2853 CE MET A1132 2412 2794 927 352 120 217 C ATOM 2854 N CYS A1133 -0.953 16.319 -1.040 1.00 17.81 N ANISOU 2854 N CYS A1133 2497 3015 1255 714 32 178 N ATOM 2855 CA CYS A1133 0.324 15.608 -1.058 1.00 20.27 C ANISOU 2855 CA CYS A1133 2810 3361 1531 874 69 242 C ATOM 2856 C CYS A1133 1.115 15.846 0.223 1.00 22.07 C ANISOU 2856 C CYS A1133 2914 3736 1736 959 18 301 C ATOM 2857 O CYS A1133 2.018 15.081 0.562 1.00 23.68 O ANISOU 2857 O CYS A1133 3085 4001 1911 1122 35 422 O ATOM 2858 CB CYS A1133 1.162 16.029 -2.268 1.00 14.68 C ANISOU 2858 CB CYS A1133 2116 2630 830 860 87 129 C ATOM 2859 SG CYS A1133 0.637 15.301 -3.835 1.00 34.61 S ANISOU 2859 SG CYS A1133 4807 5009 3335 797 188 31 S ATOM 2860 N LEU A1134 0.763 16.912 0.931 1.00 22.52 N ANISOU 2860 N LEU A1134 2909 3849 1798 860 -41 221 N ATOM 2861 CA LEU A1134 1.454 17.290 2.153 1.00 23.11 C ANISOU 2861 CA LEU A1134 2884 4088 1808 911 -96 226 C ATOM 2862 C LEU A1134 0.594 17.068 3.390 1.00 25.72 C ANISOU 2862 C LEU A1134 3215 4488 2069 907 -90 299 C ATOM 2863 O LEU A1134 0.891 17.587 4.466 1.00 28.76 O ANISOU 2863 O LEU A1134 3536 5025 2366 924 -141 268 O ATOM 2864 CB LEU A1134 1.895 18.747 2.067 1.00 21.10 C ANISOU 2864 CB LEU A1134 2578 3869 1568 833 -158 64 C ATOM 2865 CG LEU A1134 3.148 18.896 1.209 1.00 23.30 C ANISOU 2865 CG LEU A1134 2805 4190 1857 870 -172 25 C ATOM 2866 CD1 LEU A1134 3.221 20.267 0.577 1.00 23.38 C ANISOU 2866 CD1 LEU A1134 2822 4155 1904 753 -201 -109 C ATOM 2867 CD2 LEU A1134 4.374 18.624 2.063 1.00 26.75 C ANISOU 2867 CD2 LEU A1134 3107 4842 2215 980 -234 60 C ATOM 2868 N GLY A1135 -0.474 16.296 3.228 1.00 17.77 N ANISOU 2868 N GLY A1135 2278 3396 1076 887 -25 395 N ATOM 2869 CA GLY A1135 -1.308 15.913 4.351 1.00 19.25 C ANISOU 2869 CA GLY A1135 2461 3674 1177 895 7 507 C ATOM 2870 C GLY A1135 -2.365 16.930 4.731 1.00 30.85 C ANISOU 2870 C GLY A1135 3912 5189 2622 817 3 386 C ATOM 2871 O GLY A1135 -3.222 16.649 5.568 1.00 32.57 O ANISOU 2871 O GLY A1135 4120 5504 2752 825 52 471 O ATOM 2872 N ALA A1136 -2.304 18.116 4.133 1.00 17.29 N ANISOU 2872 N ALA A1136 2185 3410 976 761 -42 212 N ATOM 2873 CA ALA A1136 -3.323 19.130 4.376 1.00 23.38 C ANISOU 2873 CA ALA A1136 2938 4208 1737 729 -40 109 C ATOM 2874 C ALA A1136 -4.669 18.640 3.859 1.00 23.63 C ANISOU 2874 C ALA A1136 2990 4193 1794 691 20 168 C ATOM 2875 O ALA A1136 -4.812 18.334 2.676 1.00 23.38 O ANISOU 2875 O ALA A1136 3005 4034 1844 639 19 170 O ATOM 2876 CB ALA A1136 -2.942 20.447 3.717 1.00 22.08 C ANISOU 2876 CB ALA A1136 2775 3965 1649 696 -93 -43 C ATOM 2877 N ILE A1137 -5.649 18.553 4.751 1.00 18.19 N ANISOU 2877 N ILE A1137 2259 3644 1009 718 74 213 N ATOM 2878 CA ILE A1137 -6.972 18.071 4.376 1.00 18.41 C ANISOU 2878 CA ILE A1137 2271 3691 1034 684 143 282 C ATOM 2879 C ILE A1137 -7.804 19.192 3.761 1.00 23.16 C ANISOU 2879 C ILE A1137 2825 4293 1683 690 114 144 C ATOM 2880 O ILE A1137 -7.995 20.242 4.375 1.00 23.91 O ANISOU 2880 O ILE A1137 2872 4476 1737 756 101 36 O ATOM 2881 CB ILE A1137 -7.719 17.477 5.582 1.00 20.81 C ANISOU 2881 CB ILE A1137 2526 4177 1203 709 245 420 C ATOM 2882 CG1 ILE A1137 -6.912 16.329 6.193 1.00 29.10 C ANISOU 2882 CG1 ILE A1137 3627 5229 2200 729 274 609 C ATOM 2883 CG2 ILE A1137 -9.105 17.003 5.172 1.00 21.42 C ANISOU 2883 CG2 ILE A1137 2548 4307 1283 652 344 505 C ATOM 2884 CD1 ILE A1137 -7.578 15.681 7.387 1.00 33.03 C ANISOU 2884 CD1 ILE A1137 4093 5898 2560 743 389 798 C ATOM 2885 N PRO A1138 -8.295 18.969 2.533 1.00 21.64 N ANISOU 2885 N PRO A1138 2647 4022 1553 638 99 147 N ATOM 2886 CA PRO A1138 -9.036 19.985 1.781 1.00 20.14 C ANISOU 2886 CA PRO A1138 2407 3848 1397 670 52 45 C ATOM 2887 C PRO A1138 -10.487 20.161 2.220 1.00 21.09 C ANISOU 2887 C PRO A1138 2383 4198 1433 733 114 51 C ATOM 2888 O PRO A1138 -11.237 19.193 2.356 1.00 22.48 O ANISOU 2888 O PRO A1138 2492 4497 1553 673 201 167 O ATOM 2889 CB PRO A1138 -8.974 19.460 0.346 1.00 15.32 C ANISOU 2889 CB PRO A1138 1863 3118 838 581 3 62 C ATOM 2890 CG PRO A1138 -8.901 17.985 0.503 1.00 15.92 C ANISOU 2890 CG PRO A1138 1979 3203 866 513 69 183 C ATOM 2891 CD PRO A1138 -8.075 17.748 1.738 1.00 22.52 C ANISOU 2891 CD PRO A1138 2834 4039 1684 559 114 242 C ATOM 2892 N ILE A1139 -10.861 21.414 2.446 1.00 20.99 N ANISOU 2892 N ILE A1139 2310 4257 1409 855 90 -71 N ATOM 2893 CA ILE A1139 -12.252 21.805 2.602 1.00 22.49 C ANISOU 2893 CA ILE A1139 2333 4675 1538 953 147 -107 C ATOM 2894 C ILE A1139 -12.584 22.714 1.433 1.00 22.09 C ANISOU 2894 C ILE A1139 2260 4613 1520 1059 46 -193 C ATOM 2895 O ILE A1139 -12.272 23.901 1.461 1.00 22.28 O ANISOU 2895 O ILE A1139 2337 4555 1574 1188 -3 -317 O ATOM 2896 CB ILE A1139 -12.506 22.533 3.930 1.00 25.12 C ANISOU 2896 CB ILE A1139 2622 5111 1811 1050 219 -204 C ATOM 2897 CG1 ILE A1139 -11.986 21.699 5.101 1.00 22.69 C ANISOU 2897 CG1 ILE A1139 2367 4833 1420 966 290 -106 C ATOM 2898 CG2 ILE A1139 -13.988 22.843 4.094 1.00 24.17 C ANISOU 2898 CG2 ILE A1139 2303 5191 1689 1140 320 -244 C ATOM 2899 CD1 ILE A1139 -12.248 22.323 6.447 1.00 27.87 C ANISOU 2899 CD1 ILE A1139 2991 5636 1964 1043 365 -208 C ATOM 2900 N ALA A1140 -13.200 22.161 0.396 1.00 19.73 N ANISOU 2900 N ALA A1140 1894 4347 1256 979 -20 -114 N ATOM 2901 CA ALA A1140 -13.333 22.899 -0.852 1.00 19.55 C ANISOU 2901 CA ALA A1140 1886 4204 1337 1021 -194 -124 C ATOM 2902 C ALA A1140 -14.752 22.928 -1.398 1.00 27.43 C ANISOU 2902 C ALA A1140 2640 5318 2464 1033 -262 -85 C ATOM 2903 O ALA A1140 -15.571 22.057 -1.101 1.00 28.95 O ANISOU 2903 O ALA A1140 2655 5655 2690 921 -187 -44 O ATOM 2904 CB ALA A1140 -12.395 22.319 -1.892 1.00 17.89 C ANISOU 2904 CB ALA A1140 1865 3793 1139 852 -268 -73 C ATOM 2905 N SER A1141 -15.031 23.947 -2.205 1.00 22.20 N ANISOU 2905 N SER A1141 1953 4592 1889 1168 -407 -78 N ATOM 2906 CA SER A1141 -16.307 24.041 -2.894 1.00 24.37 C ANISOU 2906 CA SER A1141 2005 4966 2290 1180 -514 -22 C ATOM 2907 C SER A1141 -16.435 22.908 -3.903 1.00 29.70 C ANISOU 2907 C SER A1141 2687 5678 2919 931 -629 30 C ATOM 2908 O SER A1141 -15.492 22.609 -4.633 1.00 28.31 O ANISOU 2908 O SER A1141 2757 5341 2658 808 -672 39 O ATOM 2909 CB SER A1141 -16.448 25.392 -3.595 1.00 49.50 C ANISOU 2909 CB SER A1141 5247 7973 5589 1340 -621 19 C ATOM 2910 OG SER A1141 -16.383 26.463 -2.669 1.00 49.04 O ANISOU 2910 OG SER A1141 5181 7837 5615 1567 -513 -75 O ATOM 2911 N ALA A1142 -17.601 22.275 -3.938 1.00 32.13 N ANISOU 2911 N ALA A1142 2713 6187 3307 840 -658 38 N ATOM 2912 CA ALA A1142 -17.843 21.198 -4.885 1.00 26.90 C ANISOU 2912 CA ALA A1142 2024 5575 2621 587 -788 31 C ATOM 2913 C ALA A1142 -18.081 21.758 -6.283 1.00 28.21 C ANISOU 2913 C ALA A1142 2277 5654 2788 597 -989 66 C ATOM 2914 O ALA A1142 -19.199 21.716 -6.798 1.00 31.51 O ANISOU 2914 O ALA A1142 2475 6206 3292 563 -1119 77 O ATOM 2915 CB ALA A1142 -19.023 20.352 -4.440 1.00 33.68 C ANISOU 2915 CB ALA A1142 2524 6665 3610 440 -743 17 C ATOM 2916 N VAL A1143 -17.022 22.284 -6.892 1.00 27.16 N ANISOU 2916 N VAL A1143 2446 5311 2563 634 -1008 99 N ATOM 2917 CA VAL A1143 -17.091 22.790 -8.257 1.00 29.10 C ANISOU 2917 CA VAL A1143 2793 5495 2769 629 -1180 172 C ATOM 2918 C VAL A1143 -15.893 22.331 -9.081 1.00 26.75 C ANISOU 2918 C VAL A1143 2793 5046 2326 486 -1169 146 C ATOM 2919 O VAL A1143 -14.768 22.281 -8.583 1.00 24.30 O ANISOU 2919 O VAL A1143 2656 4586 1993 480 -1020 123 O ATOM 2920 CB VAL A1143 -17.161 24.332 -8.297 1.00 28.80 C ANISOU 2920 CB VAL A1143 2769 5359 2816 865 -1211 298 C ATOM 2921 CG1 VAL A1143 -18.535 24.818 -7.862 1.00 31.49 C ANISOU 2921 CG1 VAL A1143 2795 5842 3327 1023 -1259 326 C ATOM 2922 CG2 VAL A1143 -16.064 24.943 -7.435 1.00 26.39 C ANISOU 2922 CG2 VAL A1143 2629 4878 2519 970 -1043 279 C ATOM 2923 N GLY A1144 -16.152 21.989 -10.339 1.00 28.30 N ANISOU 2923 N GLY A1144 3032 5296 2426 377 -1325 138 N ATOM 2924 CA GLY A1144 -15.111 21.649 -11.292 1.00 27.70 C ANISOU 2924 CA GLY A1144 3223 5102 2199 270 -1314 109 C ATOM 2925 C GLY A1144 -14.121 20.592 -10.842 1.00 32.73 C ANISOU 2925 C GLY A1144 3993 5629 2813 153 -1151 -17 C ATOM 2926 O GLY A1144 -14.500 19.578 -10.247 1.00 33.09 O ANISOU 2926 O GLY A1144 3919 5755 2898 55 -1123 -128 O ATOM 2927 N GLY A1145 -12.846 20.849 -11.126 1.00 31.77 N ANISOU 2927 N GLY A1145 4098 5334 2640 155 -1048 13 N ATOM 2928 CA GLY A1145 -11.768 19.922 -10.830 1.00 30.66 C ANISOU 2928 CA GLY A1145 4093 5069 2487 74 -899 -85 C ATOM 2929 C GLY A1145 -11.775 19.393 -9.411 1.00 29.70 C ANISOU 2929 C GLY A1145 3872 4946 2468 89 -786 -123 C ATOM 2930 O GLY A1145 -11.495 18.214 -9.183 1.00 30.73 O ANISOU 2930 O GLY A1145 4031 5070 2577 -4 -729 -230 O ATOM 2931 N LEU A1146 -12.107 20.265 -8.463 1.00 19.84 N ANISOU 2931 N LEU A1146 2508 3723 1308 216 -754 -42 N ATOM 2932 CA LEU A1146 -12.182 19.890 -7.056 1.00 18.86 C ANISOU 2932 CA LEU A1146 2283 3648 1235 258 -644 -58 C ATOM 2933 C LEU A1146 -13.050 18.651 -6.857 1.00 26.91 C ANISOU 2933 C LEU A1146 3142 4860 2220 123 -687 -131 C ATOM 2934 O LEU A1146 -12.636 17.703 -6.183 1.00 26.27 O ANISOU 2934 O LEU A1146 3091 4772 2117 49 -584 -156 O ATOM 2935 CB LEU A1146 -12.721 21.054 -6.220 1.00 18.96 C ANISOU 2935 CB LEU A1146 2163 3727 1312 434 -629 -1 C ATOM 2936 CG LEU A1146 -11.832 22.300 -6.182 1.00 17.96 C ANISOU 2936 CG LEU A1146 2163 3436 1224 540 -586 38 C ATOM 2937 CD1 LEU A1146 -12.485 23.417 -5.385 1.00 18.77 C ANISOU 2937 CD1 LEU A1146 2137 3621 1375 747 -590 47 C ATOM 2938 CD2 LEU A1146 -10.462 21.962 -5.616 1.00 16.06 C ANISOU 2938 CD2 LEU A1146 2057 3048 999 491 -454 5 C ATOM 2939 N ARG A1147 -14.232 18.652 -7.471 1.00 22.44 N ANISOU 2939 N ARG A1147 2396 4459 1673 61 -838 -156 N ATOM 2940 CA ARG A1147 -15.161 17.529 -7.349 1.00 29.77 C ANISOU 2940 CA ARG A1147 3105 5555 2650 -152 -888 -246 C ATOM 2941 C ARG A1147 -14.500 16.224 -7.756 1.00 30.40 C ANISOU 2941 C ARG A1147 3366 5453 2732 -361 -823 -379 C ATOM 2942 O ARG A1147 -14.730 15.179 -7.147 1.00 31.33 O ANISOU 2942 O ARG A1147 3432 5447 3024 -518 -690 -396 O ATOM 2943 CB ARG A1147 -16.407 17.751 -8.206 1.00 32.77 C ANISOU 2943 CB ARG A1147 3279 6098 3074 -202 -1084 -275 C ATOM 2944 CG ARG A1147 -17.165 19.020 -7.898 1.00 33.63 C ANISOU 2944 CG ARG A1147 3224 6290 3264 26 -1115 -142 C ATOM 2945 CD ARG A1147 -18.335 19.200 -8.851 1.00 37.47 C ANISOU 2945 CD ARG A1147 3533 6907 3795 -8 -1318 -149 C ATOM 2946 NE ARG A1147 -19.407 18.241 -8.600 1.00 40.49 N ANISOU 2946 NE ARG A1147 3600 7470 4312 -222 -1355 -243 N ATOM 2947 CZ ARG A1147 -20.483 18.108 -9.369 1.00 45.84 C ANISOU 2947 CZ ARG A1147 4087 8280 5051 -310 -1539 -288 C ATOM 2948 NH1 ARG A1147 -20.629 18.869 -10.445 1.00 49.06 N ANISOU 2948 NH1 ARG A1147 4591 8691 5357 -183 -1721 -229 N ATOM 2949 NH2 ARG A1147 -21.412 17.213 -9.065 1.00 47.62 N ANISOU 2949 NH2 ARG A1147 4015 8629 5450 -540 -1541 -380 N ATOM 2950 N ASP A1148 -13.672 16.297 -8.791 1.00 24.17 N ANISOU 2950 N ASP A1148 2796 4605 1783 -347 -885 -456 N ATOM 2951 CA ASP A1148 -12.999 15.118 -9.308 1.00 49.30 C ANISOU 2951 CA ASP A1148 6150 7640 4940 -517 -830 -637 C ATOM 2952 C ASP A1148 -11.903 14.663 -8.358 1.00 22.84 C ANISOU 2952 C ASP A1148 2950 4036 1693 -441 -594 -560 C ATOM 2953 O ASP A1148 -11.672 13.466 -8.192 1.00 23.83 O ANISOU 2953 O ASP A1148 3139 3946 1968 -569 -476 -638 O ATOM 2954 CB ASP A1148 -12.419 15.401 -10.694 1.00 48.18 C ANISOU 2954 CB ASP A1148 6207 7423 4678 -449 -885 -681 C ATOM 2955 CG ASP A1148 -13.457 15.944 -11.659 1.00 50.32 C ANISOU 2955 CG ASP A1148 6373 7843 4902 -450 -1084 -662 C ATOM 2956 OD1 ASP A1148 -14.650 15.605 -11.501 1.00 51.86 O ANISOU 2956 OD1 ASP A1148 6334 8192 5178 -582 -1197 -724 O ATOM 2957 OD2 ASP A1148 -13.080 16.713 -12.569 1.00 52.97 O ANISOU 2957 OD2 ASP A1148 6848 8153 5126 -337 -1127 -576 O ATOM 2958 N ILE A1149 -11.238 15.622 -7.724 1.00 25.91 N ANISOU 2958 N ILE A1149 3384 4442 2018 -230 -537 -406 N ATOM 2959 CA ILE A1149 -10.095 15.310 -6.878 1.00 23.73 C ANISOU 2959 CA ILE A1149 3232 3990 1794 -135 -359 -329 C ATOM 2960 C ILE A1149 -10.530 14.835 -5.502 1.00 23.70 C ANISOU 2960 C ILE A1149 3119 3939 1948 -140 -231 -193 C ATOM 2961 O ILE A1149 -10.133 13.763 -5.045 1.00 25.04 O ANISOU 2961 O ILE A1149 3352 3920 2243 -192 -99 -156 O ATOM 2962 CB ILE A1149 -9.171 16.524 -6.714 1.00 16.94 C ANISOU 2962 CB ILE A1149 2449 3109 878 50 -344 -231 C ATOM 2963 CG1 ILE A1149 -8.648 16.979 -8.078 1.00 17.12 C ANISOU 2963 CG1 ILE A1149 2595 3028 882 23 -391 -266 C ATOM 2964 CG2 ILE A1149 -8.024 16.190 -5.778 1.00 15.79 C ANISOU 2964 CG2 ILE A1149 2376 2860 765 138 -203 -165 C ATOM 2965 CD1 ILE A1149 -7.900 18.287 -8.041 1.00 18.45 C ANISOU 2965 CD1 ILE A1149 2781 3104 1126 83 -356 -152 C ATOM 2966 N ILE A1150 -11.349 15.644 -4.843 1.00 19.08 N ANISOU 2966 N ILE A1150 2367 3527 1354 -70 -256 -106 N ATOM 2967 CA ILE A1150 -11.801 15.339 -3.497 1.00 19.64 C ANISOU 2967 CA ILE A1150 2324 3627 1513 -59 -111 35 C ATOM 2968 C ILE A1150 -12.989 14.387 -3.518 1.00 38.20 C ANISOU 2968 C ILE A1150 4507 5965 4041 -280 -79 33 C ATOM 2969 O ILE A1150 -14.086 14.753 -3.937 1.00 37.45 O ANISOU 2969 O ILE A1150 4218 6032 3979 -345 -187 -27 O ATOM 2970 CB ILE A1150 -12.180 16.619 -2.746 1.00 18.99 C ANISOU 2970 CB ILE A1150 2124 3746 1347 120 -117 86 C ATOM 2971 CG1 ILE A1150 -10.980 17.565 -2.702 1.00 16.97 C ANISOU 2971 CG1 ILE A1150 2024 3465 958 296 -149 65 C ATOM 2972 CG2 ILE A1150 -12.661 16.288 -1.347 1.00 21.68 C ANISOU 2972 CG2 ILE A1150 2347 4175 1717 132 58 221 C ATOM 2973 CD1 ILE A1150 -11.352 19.010 -2.563 1.00 16.72 C ANISOU 2973 CD1 ILE A1150 1914 3494 947 435 -202 30 C ATOM 2974 N THR A1151 -12.755 13.159 -3.071 1.00 42.76 N ANISOU 2974 N THR A1151 5148 6338 4760 -396 68 112 N ATOM 2975 CA THR A1151 -13.803 12.150 -3.020 1.00 47.86 C ANISOU 2975 CA THR A1151 5643 6911 5632 -649 133 125 C ATOM 2976 C THR A1151 -14.239 11.909 -1.579 1.00 55.21 C ANISOU 2976 C THR A1151 6456 7905 6617 -637 343 382 C ATOM 2977 O THR A1151 -13.969 12.722 -0.698 1.00 55.26 O ANISOU 2977 O THR A1151 6458 8095 6444 -425 396 494 O ATOM 2978 CB THR A1151 -13.340 10.818 -3.646 1.00 46.25 C ANISOU 2978 CB THR A1151 5600 6363 5609 -827 172 25 C ATOM 2979 OG1 THR A1151 -12.388 10.179 -2.787 1.00 43.72 O ANISOU 2979 OG1 THR A1151 5442 5827 5344 -722 351 226 O ATOM 2980 CG2 THR A1151 -12.708 11.062 -5.003 1.00 42.65 C ANISOU 2980 CG2 THR A1151 5296 5882 5026 -804 5 -233 C ATOM 2981 N ASN A1152 -14.918 10.792 -1.348 1.00 59.37 N ANISOU 2981 N ASN A1152 6888 8284 7386 -878 470 466 N ATOM 2982 CA ASN A1152 -15.308 10.427 0.003 1.00 62.67 C ANISOU 2982 CA ASN A1152 7208 8758 7844 -890 707 761 C ATOM 2983 C ASN A1152 -14.095 9.901 0.761 1.00 61.31 C ANISOU 2983 C ASN A1152 7282 8402 7611 -741 835 984 C ATOM 2984 O ASN A1152 -13.203 9.291 0.168 1.00 60.29 O ANISOU 2984 O ASN A1152 7357 7978 7574 -737 792 915 O ATOM 2985 CB ASN A1152 -16.433 9.388 -0.011 1.00 68.74 C ANISOU 2985 CB ASN A1152 7782 9406 8931 -1229 820 813 C ATOM 2986 CG ASN A1152 -15.957 8.009 -0.429 1.00 69.74 C ANISOU 2986 CG ASN A1152 8095 9069 9334 -1422 877 809 C ATOM 2987 OD1 ASN A1152 -15.801 7.724 -1.617 1.00 67.44 O ANISOU 2987 OD1 ASN A1152 7883 8603 9139 -1537 715 516 O ATOM 2988 ND2 ASN A1152 -15.731 7.141 0.552 1.00 73.52 N ANISOU 2988 ND2 ASN A1152 8651 9346 9938 -1448 1116 1138 N ATOM 2989 N GLU A1153 -14.062 10.162 2.067 1.00 60.04 N ANISOU 2989 N GLU A1153 7088 8449 7276 -599 988 1241 N ATOM 2990 CA GLU A1153 -12.972 9.733 2.945 1.00 59.51 C ANISOU 2990 CA GLU A1153 7215 8300 7098 -429 1088 1502 C ATOM 2991 C GLU A1153 -11.636 10.378 2.555 1.00 51.62 C ANISOU 2991 C GLU A1153 6396 7296 5920 -193 916 1350 C ATOM 2992 O GLU A1153 -10.575 9.784 2.747 1.00 49.15 O ANISOU 2992 O GLU A1153 6251 6800 5626 -84 935 1484 O ATOM 2993 CB GLU A1153 -12.852 8.202 2.935 1.00 68.43 C ANISOU 2993 CB GLU A1153 8444 9014 8543 -598 1228 1709 C ATOM 2994 CG GLU A1153 -12.186 7.595 4.166 1.00 75.04 C ANISOU 2994 CG GLU A1153 9398 9819 9294 -451 1394 2130 C ATOM 2995 CD GLU A1153 -12.158 6.079 4.118 1.00 81.53 C ANISOU 2995 CD GLU A1153 10318 10160 10500 -617 1547 2362 C ATOM 2996 OE1 GLU A1153 -12.848 5.498 3.253 1.00 85.48 O ANISOU 2996 OE1 GLU A1153 10762 10381 11337 -899 1552 2174 O ATOM 2997 OE2 GLU A1153 -11.445 5.469 4.942 1.00 82.87 O ANISOU 2997 OE2 GLU A1153 10622 10233 10633 -460 1604 2647 O ATOM 2998 N THR A1154 -11.686 11.598 2.025 1.00 46.23 N ANISOU 2998 N THR A1154 5664 6811 5088 -108 755 1091 N ATOM 2999 CA THR A1154 -10.459 12.308 1.661 1.00 39.85 C ANISOU 2999 CA THR A1154 5000 6013 4127 84 611 954 C ATOM 3000 C THR A1154 -10.653 13.817 1.509 1.00 35.11 C ANISOU 3000 C THR A1154 4326 5668 3349 196 488 758 C ATOM 3001 O THR A1154 -9.882 14.483 0.816 1.00 30.04 O ANISOU 3001 O THR A1154 3774 4992 2649 281 354 599 O ATOM 3002 CB THR A1154 -9.863 11.762 0.349 1.00 39.50 C ANISOU 3002 CB THR A1154 5086 5670 4250 9 522 786 C ATOM 3003 OG1 THR A1154 -8.646 12.456 0.050 1.00 35.97 O ANISOU 3003 OG1 THR A1154 4750 5257 3659 187 417 683 O ATOM 3004 CG2 THR A1154 -10.831 11.953 -0.792 1.00 23.25 C ANISOU 3004 CG2 THR A1154 2936 3610 2289 -170 418 557 C ATOM 3005 N GLY A1155 -11.675 14.358 2.162 1.00 34.34 N ANISOU 3005 N GLY A1155 4056 5808 3184 203 554 778 N ATOM 3006 CA GLY A1155 -11.902 15.790 2.132 1.00 31.11 C ANISOU 3006 CA GLY A1155 3574 5597 2648 340 463 599 C ATOM 3007 C GLY A1155 -13.339 16.175 2.419 1.00 31.26 C ANISOU 3007 C GLY A1155 3352 5816 2710 309 536 579 C ATOM 3008 O GLY A1155 -14.221 15.321 2.499 1.00 33.35 O ANISOU 3008 O GLY A1155 3480 6075 3116 137 644 692 O ATOM 3009 N ILE A1156 -13.571 17.472 2.578 1.00 30.64 N ANISOU 3009 N ILE A1156 3202 5899 2540 475 487 429 N ATOM 3010 CA ILE A1156 -14.910 17.979 2.841 1.00 33.75 C ANISOU 3010 CA ILE A1156 3338 6496 2991 502 560 385 C ATOM 3011 C ILE A1156 -15.354 18.884 1.697 1.00 35.20 C ANISOU 3011 C ILE A1156 3442 6633 3300 558 365 224 C ATOM 3012 O ILE A1156 -14.649 19.822 1.325 1.00 32.65 O ANISOU 3012 O ILE A1156 3256 6226 2924 697 239 112 O ATOM 3013 CB ILE A1156 -14.969 18.743 4.177 1.00 34.33 C ANISOU 3013 CB ILE A1156 3417 6665 2962 657 630 330 C ATOM 3014 CG1 ILE A1156 -14.459 17.852 5.313 1.00 26.96 C ANISOU 3014 CG1 ILE A1156 2605 5689 1950 596 730 496 C ATOM 3015 CG2 ILE A1156 -16.384 19.214 4.461 1.00 36.80 C ANISOU 3015 CG2 ILE A1156 3461 7182 3338 701 736 281 C ATOM 3016 CD1 ILE A1156 -14.373 18.545 6.650 1.00 28.49 C ANISOU 3016 CD1 ILE A1156 2827 5982 2015 716 766 419 C ATOM 3017 N LEU A1157 -16.521 18.587 1.135 1.00 34.27 N ANISOU 3017 N LEU A1157 3090 6576 3356 440 333 234 N ATOM 3018 CA LEU A1157 -17.023 19.329 -0.015 1.00 32.19 C ANISOU 3018 CA LEU A1157 2727 6306 3196 493 118 131 C ATOM 3019 C LEU A1157 -18.226 20.190 0.350 1.00 33.67 C ANISOU 3019 C LEU A1157 2608 6711 3472 655 163 86 C ATOM 3020 O LEU A1157 -19.102 19.771 1.106 1.00 35.18 O ANISOU 3020 O LEU A1157 2562 7086 3718 597 347 140 O ATOM 3021 CB LEU A1157 -17.378 18.369 -1.151 1.00 32.00 C ANISOU 3021 CB LEU A1157 2657 6207 3293 242 -22 137 C ATOM 3022 CG LEU A1157 -16.170 17.748 -1.855 1.00 29.28 C ANISOU 3022 CG LEU A1157 2620 5626 2880 138 -104 119 C ATOM 3023 CD1 LEU A1157 -16.607 16.669 -2.831 1.00 30.71 C ANISOU 3023 CD1 LEU A1157 2749 5738 3180 -133 -203 70 C ATOM 3024 CD2 LEU A1157 -15.358 18.821 -2.566 1.00 22.36 C ANISOU 3024 CD2 LEU A1157 1925 4682 1889 312 -262 52 C ATOM 3025 N VAL A1158 -18.252 21.401 -0.196 1.00 34.09 N ANISOU 3025 N VAL A1158 2662 6733 3556 867 12 3 N ATOM 3026 CA VAL A1158 -19.241 22.402 0.180 1.00 35.16 C ANISOU 3026 CA VAL A1158 2552 7007 3801 1090 59 -57 C ATOM 3027 C VAL A1158 -19.965 22.966 -1.038 1.00 35.64 C ANISOU 3027 C VAL A1158 2509 7014 4018 1136 -182 -39 C ATOM 3028 O VAL A1158 -19.370 23.117 -2.105 1.00 33.93 O ANISOU 3028 O VAL A1158 2469 6661 3761 1112 -387 -9 O ATOM 3029 CB VAL A1158 -18.580 23.572 0.948 1.00 36.04 C ANISOU 3029 CB VAL A1158 2875 6987 3831 1318 140 -178 C ATOM 3030 CG1 VAL A1158 -19.632 24.474 1.571 1.00 38.60 C ANISOU 3030 CG1 VAL A1158 3041 7343 4283 1482 239 -262 C ATOM 3031 CG2 VAL A1158 -17.631 23.049 2.012 1.00 35.45 C ANISOU 3031 CG2 VAL A1158 2995 6930 3542 1250 306 -190 C ATOM 3032 N LYS A1159 -21.252 23.263 -0.880 1.00 34.54 N ANISOU 3032 N LYS A1159 2098 6979 4045 1193 -148 -41 N ATOM 3033 CA LYS A1159 -21.982 24.033 -1.879 1.00 36.51 C ANISOU 3033 CA LYS A1159 2245 7174 4452 1303 -361 -7 C ATOM 3034 C LYS A1159 -21.286 25.378 -2.063 1.00 35.63 C ANISOU 3034 C LYS A1159 2373 6823 4343 1545 -418 -26 C ATOM 3035 O LYS A1159 -21.170 26.156 -1.116 1.00 39.13 O ANISOU 3035 O LYS A1159 2857 7195 4815 1724 -253 -124 O ATOM 3036 CB LYS A1159 -23.440 24.230 -1.458 1.00 44.59 C ANISOU 3036 CB LYS A1159 2913 8350 5681 1371 -277 -15 C ATOM 3037 CG LYS A1159 -24.234 25.179 -2.345 1.00 46.66 C ANISOU 3037 CG LYS A1159 3039 8556 6132 1545 -484 40 C ATOM 3038 CD LYS A1159 -25.636 25.394 -1.797 1.00 50.37 C ANISOU 3038 CD LYS A1159 3131 9179 6829 1639 -373 19 C ATOM 3039 CE LYS A1159 -26.367 26.497 -2.547 1.00 53.28 C ANISOU 3039 CE LYS A1159 3359 9470 7413 1875 -564 87 C ATOM 3040 NZ LYS A1159 -27.703 26.781 -1.950 1.00 57.42 N ANISOU 3040 NZ LYS A1159 3496 10134 8189 2001 -434 54 N ATOM 3041 N ALA A1160 -20.809 25.635 -3.276 1.00 34.76 N ANISOU 3041 N ALA A1160 2432 6574 4200 1523 -640 62 N ATOM 3042 CA ALA A1160 -20.048 26.847 -3.560 1.00 34.14 C ANISOU 3042 CA ALA A1160 2589 6237 4144 1703 -690 85 C ATOM 3043 C ALA A1160 -20.886 28.103 -3.357 1.00 44.38 C ANISOU 3043 C ALA A1160 3732 7444 5685 1969 -676 91 C ATOM 3044 O ALA A1160 -22.081 28.119 -3.652 1.00 47.61 O ANISOU 3044 O ALA A1160 3869 7976 6243 2009 -749 151 O ATOM 3045 CB ALA A1160 -19.502 26.805 -4.977 1.00 33.31 C ANISOU 3045 CB ALA A1160 2677 6030 3951 1591 -907 219 C ATOM 3046 N GLY A1161 -20.252 29.152 -2.845 1.00 45.09 N ANISOU 3046 N GLY A1161 3986 7305 5842 2147 -582 16 N ATOM 3047 CA GLY A1161 -20.916 30.429 -2.666 1.00 50.90 C ANISOU 3047 CA GLY A1161 4609 7879 6853 2411 -554 9 C ATOM 3048 C GLY A1161 -21.489 30.641 -1.279 1.00 55.26 C ANISOU 3048 C GLY A1161 5008 8501 7488 2525 -301 -199 C ATOM 3049 O GLY A1161 -21.391 31.735 -0.726 1.00 55.06 O ANISOU 3049 O GLY A1161 5037 8258 7626 2720 -189 -318 O ATOM 3050 N ASP A1162 -22.088 29.595 -0.718 1.00 59.50 N ANISOU 3050 N ASP A1162 5360 9332 7917 2388 -195 -244 N ATOM 3051 CA ASP A1162 -22.742 29.688 0.585 1.00 64.16 C ANISOU 3051 CA ASP A1162 5790 10039 8548 2464 65 -412 C ATOM 3052 C ASP A1162 -21.723 29.689 1.721 1.00 60.21 C ANISOU 3052 C ASP A1162 5542 9502 7835 2421 249 -603 C ATOM 3053 O ASP A1162 -21.064 28.679 1.970 1.00 59.10 O ANISOU 3053 O ASP A1162 5516 9496 7445 2219 272 -587 O ATOM 3054 CB ASP A1162 -23.734 28.533 0.764 1.00 67.77 C ANISOU 3054 CB ASP A1162 5956 10820 8974 2301 124 -354 C ATOM 3055 CG ASP A1162 -24.775 28.811 1.836 1.00 73.27 C ANISOU 3055 CG ASP A1162 6403 11641 9795 2419 372 -469 C ATOM 3056 OD1 ASP A1162 -24.438 29.444 2.859 1.00 75.74 O ANISOU 3056 OD1 ASP A1162 6846 11871 10061 2535 569 -648 O ATOM 3057 OD2 ASP A1162 -25.939 28.393 1.652 1.00 75.00 O ANISOU 3057 OD2 ASP A1162 6287 12048 10159 2385 370 -393 O ATOM 3058 N PRO A1163 -21.597 30.828 2.421 1.00 64.66 N ANISOU 3058 N PRO A1163 6322 12484 5763 1698 1107 -730 N ATOM 3059 CA PRO A1163 -20.657 30.958 3.538 1.00 59.19 C ANISOU 3059 CA PRO A1163 5892 11449 5149 1459 1232 -757 C ATOM 3060 C PRO A1163 -21.089 30.117 4.732 1.00 58.19 C ANISOU 3060 C PRO A1163 5698 11248 5162 1286 1237 -871 C ATOM 3061 O PRO A1163 -20.253 29.682 5.524 1.00 55.90 O ANISOU 3061 O PRO A1163 5538 10780 4920 1061 1240 -948 O ATOM 3062 CB PRO A1163 -20.709 32.455 3.879 1.00 50.50 C ANISOU 3062 CB PRO A1163 5094 10133 3960 1648 1479 -605 C ATOM 3063 CG PRO A1163 -21.414 33.108 2.719 1.00 67.39 C ANISOU 3063 CG PRO A1163 7153 12472 5979 1997 1483 -449 C ATOM 3064 CD PRO A1163 -22.350 32.072 2.199 1.00 67.17 C ANISOU 3064 CD PRO A1163 6729 12816 5976 2044 1256 -542 C ATOM 3065 N GLY A1164 -22.395 29.894 4.847 1.00 60.90 N ANISOU 3065 N GLY A1164 5827 11750 5563 1412 1249 -865 N ATOM 3066 CA GLY A1164 -22.953 29.132 5.947 1.00 49.43 C ANISOU 3066 CA GLY A1164 4301 10220 4259 1283 1318 -928 C ATOM 3067 C GLY A1164 -22.561 27.668 5.913 1.00 52.65 C ANISOU 3067 C GLY A1164 4551 10685 4769 1014 1170 -1091 C ATOM 3068 O GLY A1164 -22.105 27.120 6.917 1.00 51.43 O ANISOU 3068 O GLY A1164 4533 10326 4681 847 1239 -1131 O ATOM 3069 N GLU A1165 -22.738 27.033 4.758 1.00 53.98 N ANISOU 3069 N GLU A1165 4456 11137 4916 998 976 -1194 N ATOM 3070 CA GLU A1165 -22.390 25.624 4.610 1.00 55.39 C ANISOU 3070 CA GLU A1165 4510 11364 5173 759 855 -1377 C ATOM 3071 C GLU A1165 -20.881 25.441 4.738 1.00 51.17 C ANISOU 3071 C GLU A1165 4227 10630 4586 628 823 -1381 C ATOM 3072 O GLU A1165 -20.408 24.400 5.198 1.00 48.99 O ANISOU 3072 O GLU A1165 3975 10252 4388 445 816 -1472 O ATOM 3073 CB GLU A1165 -22.891 25.073 3.272 1.00 61.22 C ANISOU 3073 CB GLU A1165 4942 12474 5847 796 649 -1533 C ATOM 3074 CG GLU A1165 -22.772 23.558 3.149 1.00 66.56 C ANISOU 3074 CG GLU A1165 5472 13196 6623 547 563 -1771 C ATOM 3075 CD GLU A1165 -23.460 23.007 1.913 1.00 73.67 C ANISOU 3075 CD GLU A1165 6044 14480 7469 572 351 -1992 C ATOM 3076 OE1 GLU A1165 -24.558 23.497 1.572 1.00 78.82 O ANISOU 3076 OE1 GLU A1165 6468 15353 8126 719 291 -1959 O ATOM 3077 OE2 GLU A1165 -22.902 22.082 1.284 1.00 74.92 O ANISOU 3077 OE2 GLU A1165 6173 14721 7571 462 237 -2205 O ATOM 3078 N LEU A1166 -20.128 26.462 4.338 1.00 44.70 N ANISOU 3078 N LEU A1166 3584 9753 3649 733 826 -1265 N ATOM 3079 CA LEU A1166 -18.682 26.458 4.521 1.00 44.78 C ANISOU 3079 CA LEU A1166 3787 9588 3638 608 816 -1242 C ATOM 3080 C LEU A1166 -18.340 26.490 6.006 1.00 44.47 C ANISOU 3080 C LEU A1166 3938 9306 3653 493 931 -1234 C ATOM 3081 O LEU A1166 -17.475 25.745 6.468 1.00 43.67 O ANISOU 3081 O LEU A1166 3888 9125 3578 348 890 -1283 O ATOM 3082 CB LEU A1166 -18.034 27.644 3.803 1.00 44.56 C ANISOU 3082 CB LEU A1166 3883 9551 3496 728 855 -1112 C ATOM 3083 CG LEU A1166 -16.526 27.808 4.016 1.00 42.34 C ANISOU 3083 CG LEU A1166 3747 9136 3205 584 877 -1079 C ATOM 3084 CD1 LEU A1166 -15.781 26.544 3.613 1.00 41.34 C ANISOU 3084 CD1 LEU A1166 3513 9080 3115 473 742 -1155 C ATOM 3085 CD2 LEU A1166 -16.000 29.012 3.250 1.00 43.45 C ANISOU 3085 CD2 LEU A1166 3986 9277 3245 694 982 -939 C ATOM 3086 N ALA A1167 -19.025 27.355 6.747 1.00 45.56 N ANISOU 3086 N ALA A1167 4193 9344 3774 599 1083 -1169 N ATOM 3087 CA ALA A1167 -18.824 27.463 8.187 1.00 45.09 C ANISOU 3087 CA ALA A1167 4358 9073 3702 545 1202 -1177 C ATOM 3088 C ALA A1167 -19.146 26.143 8.877 1.00 44.37 C ANISOU 3088 C ALA A1167 4184 8956 3717 449 1214 -1235 C ATOM 3089 O ALA A1167 -18.422 25.708 9.774 1.00 44.05 O ANISOU 3089 O ALA A1167 4299 8793 3645 361 1222 -1263 O ATOM 3090 CB ALA A1167 -19.674 28.586 8.762 1.00 44.58 C ANISOU 3090 CB ALA A1167 4455 8908 3577 730 1393 -1099 C ATOM 3091 N ASN A1168 -20.232 25.506 8.449 1.00 43.53 N ANISOU 3091 N ASN A1168 3827 8986 3726 471 1224 -1257 N ATOM 3092 CA ASN A1168 -20.609 24.205 8.984 1.00 43.81 C ANISOU 3092 CA ASN A1168 3763 8994 3890 359 1287 -1315 C ATOM 3093 C ASN A1168 -19.559 23.149 8.655 1.00 42.48 C ANISOU 3093 C ASN A1168 3597 8826 3718 207 1156 -1410 C ATOM 3094 O ASN A1168 -19.270 22.272 9.472 1.00 42.34 O ANISOU 3094 O ASN A1168 3671 8681 3736 137 1241 -1421 O ATOM 3095 CB ASN A1168 -21.978 23.782 8.448 1.00 48.24 C ANISOU 3095 CB ASN A1168 3991 9742 4596 370 1315 -1353 C ATOM 3096 CG ASN A1168 -23.095 24.695 8.920 1.00 50.21 C ANISOU 3096 CG ASN A1168 4212 9988 4877 555 1489 -1222 C ATOM 3097 OD1 ASN A1168 -23.007 25.300 9.989 1.00 47.62 O ANISOU 3097 OD1 ASN A1168 4153 9456 4486 652 1663 -1123 O ATOM 3098 ND2 ASN A1168 -24.154 24.797 8.125 1.00 52.29 N ANISOU 3098 ND2 ASN A1168 4155 10495 5219 627 1439 -1230 N ATOM 3099 N ALA A1169 -18.986 23.244 7.458 1.00 41.85 N ANISOU 3099 N ALA A1169 3435 8887 3579 198 980 -1456 N ATOM 3100 CA ALA A1169 -17.911 22.345 7.053 1.00 40.87 C ANISOU 3100 CA ALA A1169 3328 8766 3434 104 875 -1521 C ATOM 3101 C ALA A1169 -16.693 22.525 7.954 1.00 44.05 C ANISOU 3101 C ALA A1169 3949 9014 3774 82 889 -1445 C ATOM 3102 O ALA A1169 -16.023 21.556 8.315 1.00 44.24 O ANISOU 3102 O ALA A1169 4023 8982 3804 31 891 -1468 O ATOM 3103 CB ALA A1169 -17.538 22.583 5.601 1.00 40.83 C ANISOU 3103 CB ALA A1169 3222 8943 3349 155 722 -1549 C ATOM 3104 N ILE A1170 -16.417 23.774 8.316 1.00 39.73 N ANISOU 3104 N ILE A1170 3527 8421 3147 130 907 -1373 N ATOM 3105 CA ILE A1170 -15.316 24.088 9.218 1.00 42.15 C ANISOU 3105 CA ILE A1170 4008 8648 3357 89 898 -1355 C ATOM 3106 C ILE A1170 -15.591 23.522 10.610 1.00 42.81 C ANISOU 3106 C ILE A1170 4249 8598 3421 108 1005 -1359 C ATOM 3107 O ILE A1170 -14.690 22.992 11.268 1.00 43.43 O ANISOU 3107 O ILE A1170 4416 8659 3425 87 966 -1367 O ATOM 3108 CB ILE A1170 -15.079 25.611 9.304 1.00 40.02 C ANISOU 3108 CB ILE A1170 3861 8361 2982 108 921 -1330 C ATOM 3109 CG1 ILE A1170 -14.597 26.146 7.954 1.00 39.91 C ANISOU 3109 CG1 ILE A1170 3722 8475 2967 106 862 -1289 C ATOM 3110 CG2 ILE A1170 -14.068 25.945 10.389 1.00 40.52 C ANISOU 3110 CG2 ILE A1170 4109 8383 2903 32 889 -1380 C ATOM 3111 CD1 ILE A1170 -14.283 27.625 7.958 1.00 40.95 C ANISOU 3111 CD1 ILE A1170 3988 8584 2987 104 940 -1265 C ATOM 3112 N LEU A1171 -16.843 23.623 11.047 1.00 40.77 N ANISOU 3112 N LEU A1171 4014 8265 3212 181 1158 -1334 N ATOM 3113 CA LEU A1171 -17.254 23.060 12.329 1.00 41.69 C ANISOU 3113 CA LEU A1171 4288 8243 3308 237 1327 -1304 C ATOM 3114 C LEU A1171 -17.055 21.548 12.353 1.00 41.61 C ANISOU 3114 C LEU A1171 4209 8223 3378 181 1360 -1320 C ATOM 3115 O LEU A1171 -16.559 20.992 13.339 1.00 42.09 O ANISOU 3115 O LEU A1171 4455 8193 3344 230 1427 -1289 O ATOM 3116 CB LEU A1171 -18.715 23.405 12.624 1.00 55.52 C ANISOU 3116 CB LEU A1171 6011 9947 5139 335 1532 -1247 C ATOM 3117 CG LEU A1171 -19.008 24.875 12.924 1.00 56.22 C ANISOU 3117 CG LEU A1171 6272 9981 5110 457 1586 -1212 C ATOM 3118 CD1 LEU A1171 -20.497 25.095 13.136 1.00 57.23 C ANISOU 3118 CD1 LEU A1171 6317 10090 5339 590 1814 -1127 C ATOM 3119 CD2 LEU A1171 -18.222 25.335 14.141 1.00 57.07 C ANISOU 3119 CD2 LEU A1171 6746 9948 4992 503 1590 -1235 C ATOM 3120 N LYS A1172 -17.438 20.885 11.265 1.00 41.43 N ANISOU 3120 N LYS A1172 3948 8297 3498 97 1321 -1382 N ATOM 3121 CA LYS A1172 -17.237 19.446 11.166 1.00 47.99 C ANISOU 3121 CA LYS A1172 4739 9099 4398 34 1379 -1432 C ATOM 3122 C LYS A1172 -15.753 19.115 11.174 1.00 47.17 C ANISOU 3122 C LYS A1172 4747 9006 4172 56 1250 -1418 C ATOM 3123 O LYS A1172 -15.335 18.129 11.779 1.00 48.62 O ANISOU 3123 O LYS A1172 5048 9104 4321 98 1352 -1393 O ATOM 3124 CB LYS A1172 -17.886 18.874 9.907 1.00 42.27 C ANISOU 3124 CB LYS A1172 3747 8505 3809 -75 1335 -1566 C ATOM 3125 CG LYS A1172 -17.666 17.376 9.781 1.00 43.11 C ANISOU 3125 CG LYS A1172 3846 8556 3979 -154 1432 -1662 C ATOM 3126 CD LYS A1172 -18.218 16.812 8.495 1.00 59.18 C ANISOU 3126 CD LYS A1172 5628 10748 6109 -282 1366 -1875 C ATOM 3127 CE LYS A1172 -17.962 15.317 8.428 1.00 59.26 C ANISOU 3127 CE LYS A1172 5681 10660 6175 -370 1514 -2010 C ATOM 3128 NZ LYS A1172 -18.391 14.638 9.684 1.00 59.06 N ANISOU 3128 NZ LYS A1172 5760 10414 6267 -398 1830 -1923 N ATOM 3129 N ALA A1173 -14.963 19.942 10.496 1.00 45.29 N ANISOU 3129 N ALA A1173 4456 8884 3869 47 1055 -1418 N ATOM 3130 CA ALA A1173 -13.516 19.778 10.496 1.00 39.45 C ANISOU 3130 CA ALA A1173 3750 8213 3027 69 939 -1390 C ATOM 3131 C ALA A1173 -12.982 19.828 11.921 1.00 42.42 C ANISOU 3131 C ALA A1173 4321 8540 3255 142 970 -1343 C ATOM 3132 O ALA A1173 -12.103 19.051 12.291 1.00 42.76 O ANISOU 3132 O ALA A1173 4414 8618 3214 211 956 -1313 O ATOM 3133 CB ALA A1173 -12.858 20.842 9.645 1.00 38.83 C ANISOU 3133 CB ALA A1173 3560 8276 2916 33 788 -1381 C ATOM 3134 N LEU A1174 -13.527 20.741 12.719 1.00 40.62 N ANISOU 3134 N LEU A1174 4227 8243 2963 162 1014 -1338 N ATOM 3135 CA LEU A1174 -13.138 20.839 14.120 1.00 41.84 C ANISOU 3135 CA LEU A1174 4625 8350 2924 259 1029 -1318 C ATOM 3136 C LEU A1174 -13.544 19.588 14.891 1.00 45.80 C ANISOU 3136 C LEU A1174 5264 8718 3418 374 1235 -1252 C ATOM 3137 O LEU A1174 -12.786 19.092 15.724 1.00 46.80 O ANISOU 3137 O LEU A1174 5544 8865 3373 492 1216 -1215 O ATOM 3138 CB LEU A1174 -13.755 22.076 14.771 1.00 45.64 C ANISOU 3138 CB LEU A1174 5283 8743 3316 284 1065 -1340 C ATOM 3139 CG LEU A1174 -13.482 22.214 16.270 1.00 50.26 C ANISOU 3139 CG LEU A1174 6191 9252 3654 413 1073 -1342 C ATOM 3140 CD1 LEU A1174 -11.994 22.177 16.557 1.00 45.10 C ANISOU 3140 CD1 LEU A1174 5540 8772 2825 395 817 -1396 C ATOM 3141 CD2 LEU A1174 -14.080 23.491 16.804 1.00 53.75 C ANISOU 3141 CD2 LEU A1174 6854 9577 3990 448 1115 -1385 C ATOM 3142 N GLU A1175 -14.739 19.076 14.609 1.00 42.95 N ANISOU 3142 N GLU A1175 4836 8244 3237 346 1445 -1235 N ATOM 3143 CA GLU A1175 -15.220 17.881 15.295 1.00 44.41 C ANISOU 3143 CA GLU A1175 5141 8282 3450 427 1720 -1168 C ATOM 3144 C GLU A1175 -14.438 16.632 14.887 1.00 44.51 C ANISOU 3144 C GLU A1175 5126 8311 3473 439 1722 -1171 C ATOM 3145 O GLU A1175 -14.440 15.630 15.602 1.00 46.08 O ANISOU 3145 O GLU A1175 5495 8388 3624 552 1947 -1097 O ATOM 3146 CB GLU A1175 -16.713 17.677 15.032 1.00 76.21 C ANISOU 3146 CB GLU A1175 9024 12227 7703 353 1956 -1167 C ATOM 3147 CG GLU A1175 -17.596 18.741 15.661 1.00 75.07 C ANISOU 3147 CG GLU A1175 8954 12034 7534 421 2054 -1114 C ATOM 3148 CD GLU A1175 -17.453 18.801 17.172 1.00 73.59 C ANISOU 3148 CD GLU A1175 9123 11709 7127 606 2216 -1019 C ATOM 3149 OE1 GLU A1175 -17.296 17.731 17.801 1.00 74.71 O ANISOU 3149 OE1 GLU A1175 9401 11751 7233 677 2410 -953 O ATOM 3150 OE2 GLU A1175 -17.491 19.918 17.730 1.00 71.95 O ANISOU 3150 OE2 GLU A1175 9087 11487 6765 682 2156 -1025 O ATOM 3151 N LEU A1176 -13.769 16.696 13.741 1.00 43.18 N ANISOU 3151 N LEU A1176 4772 8282 3354 352 1510 -1242 N ATOM 3152 CA LEU A1176 -12.938 15.589 13.281 1.00 43.50 C ANISOU 3152 CA LEU A1176 4805 8342 3379 403 1514 -1241 C ATOM 3153 C LEU A1176 -11.528 15.706 13.842 1.00 43.83 C ANISOU 3153 C LEU A1176 4922 8526 3204 553 1353 -1167 C ATOM 3154 O LEU A1176 -10.802 14.716 13.941 1.00 45.92 O ANISOU 3154 O LEU A1176 5257 8797 3392 693 1413 -1109 O ATOM 3155 CB LEU A1176 -12.892 15.545 11.753 1.00 46.00 C ANISOU 3155 CB LEU A1176 4905 8750 3824 281 1388 -1345 C ATOM 3156 CG LEU A1176 -14.200 15.221 11.030 1.00 45.95 C ANISOU 3156 CG LEU A1176 4766 8688 4006 130 1500 -1474 C ATOM 3157 CD1 LEU A1176 -13.980 15.174 9.526 1.00 42.31 C ANISOU 3157 CD1 LEU A1176 4139 8354 3582 63 1337 -1594 C ATOM 3158 CD2 LEU A1176 -14.784 13.910 11.533 1.00 48.01 C ANISOU 3158 CD2 LEU A1176 5127 8769 4344 124 1817 -1502 C ATOM 3159 N SER A1177 -11.149 16.925 14.214 1.00 48.30 N ANISOU 3159 N SER A1177 5464 9227 3660 530 1156 -1178 N ATOM 3160 CA SER A1177 -9.806 17.198 14.712 1.00 49.61 C ANISOU 3160 CA SER A1177 5619 9619 3611 633 953 -1151 C ATOM 3161 C SER A1177 -9.605 16.679 16.132 1.00 51.57 C ANISOU 3161 C SER A1177 6132 9825 3636 853 1020 -1071 C ATOM 3162 O SER A1177 -8.486 16.676 16.647 1.00 53.28 O ANISOU 3162 O SER A1177 6342 10262 3640 992 839 -1041 O ATOM 3163 CB SER A1177 -9.517 18.697 14.660 1.00 43.88 C ANISOU 3163 CB SER A1177 4797 9042 2833 496 736 -1233 C ATOM 3164 OG SER A1177 -10.437 19.415 15.463 1.00 44.20 O ANISOU 3164 OG SER A1177 5045 8915 2833 483 800 -1263 O ATOM 3165 N ARG A1178 -10.690 16.237 16.761 1.00 52.08 N ANISOU 3165 N ARG A1178 6415 9634 3738 901 1286 -1025 N ATOM 3166 CA ARG A1178 -10.612 15.638 18.088 1.00 53.75 C ANISOU 3166 CA ARG A1178 6919 9764 3741 1141 1413 -915 C ATOM 3167 C ARG A1178 -10.303 14.150 17.971 1.00 50.49 C ANISOU 3167 C ARG A1178 6561 9272 3350 1294 1612 -807 C ATOM 3168 O ARG A1178 -10.610 13.364 18.867 1.00 52.56 O ANISOU 3168 O ARG A1178 7072 9364 3535 1471 1851 -687 O ATOM 3169 CB ARG A1178 -11.914 15.855 18.858 1.00 50.09 C ANISOU 3169 CB ARG A1178 6663 9060 3308 1136 1669 -888 C ATOM 3170 CG ARG A1178 -12.463 17.265 18.746 1.00 48.97 C ANISOU 3170 CG ARG A1178 6477 8931 3199 988 1552 -990 C ATOM 3171 CD ARG A1178 -13.752 17.417 19.533 1.00 56.17 C ANISOU 3171 CD ARG A1178 7580 9625 4137 1028 1847 -936 C ATOM 3172 NE ARG A1178 -14.547 18.544 19.056 1.00 54.31 N ANISOU 3172 NE ARG A1178 7241 9369 4024 890 1828 -1011 N ATOM 3173 CZ ARG A1178 -14.344 19.808 19.413 1.00 52.92 C ANISOU 3173 CZ ARG A1178 7183 9235 3690 895 1640 -1086 C ATOM 3174 NH1 ARG A1178 -13.365 20.114 20.253 1.00 53.20 N ANISOU 3174 NH1 ARG A1178 7422 9351 3439 1000 1417 -1124 N ATOM 3175 NH2 ARG A1178 -15.120 20.767 18.926 1.00 51.34 N ANISOU 3175 NH2 ARG A1178 6901 8998 3608 804 1669 -1130 N ATOM 3176 N SER A1179 -9.703 13.774 16.847 1.00 49.44 N ANISOU 3176 N SER A1179 6215 9244 3325 1236 1533 -842 N ATOM 3177 CA SER A1179 -9.277 12.405 16.603 1.00 50.73 C ANISOU 3177 CA SER A1179 6449 9327 3499 1399 1710 -754 C ATOM 3178 C SER A1179 -7.941 12.419 15.865 1.00 57.76 C ANISOU 3178 C SER A1179 7117 10506 4325 1480 1468 -744 C ATOM 3179 O SER A1179 -7.409 13.488 15.564 1.00 57.25 O ANISOU 3179 O SER A1179 6823 10705 4224 1374 1187 -811 O ATOM 3180 CB SER A1179 -10.337 11.642 15.809 1.00 50.34 C ANISOU 3180 CB SER A1179 6406 9010 3711 1226 2012 -832 C ATOM 3181 OG SER A1179 -11.579 11.646 16.495 1.00 51.06 O ANISOU 3181 OG SER A1179 6628 8892 3880 1152 2271 -825 O ATOM 3182 N ASP A1180 -7.408 11.238 15.567 1.00 51.87 N ANISOU 3182 N ASP A1180 6438 9703 3568 1672 1612 -654 N ATOM 3183 CA ASP A1180 -6.042 11.115 15.058 1.00 66.55 C ANISOU 3183 CA ASP A1180 8100 11861 5326 1849 1433 -585 C ATOM 3184 C ASP A1180 -5.807 11.828 13.725 1.00 64.45 C ANISOU 3184 C ASP A1180 7522 11755 5210 1623 1267 -698 C ATOM 3185 O ASP A1180 -4.753 12.434 13.524 1.00 67.00 O ANISOU 3185 O ASP A1180 7578 12446 5435 1675 1042 -663 O ATOM 3186 CB ASP A1180 -5.666 9.640 14.917 1.00 67.11 C ANISOU 3186 CB ASP A1180 8358 11759 5380 2120 1680 -457 C ATOM 3187 CG ASP A1180 -4.200 9.444 14.588 1.00 65.68 C ANISOU 3187 CG ASP A1180 7980 11916 5059 2399 1528 -329 C ATOM 3188 OD1 ASP A1180 -3.380 10.287 15.009 1.00 64.77 O ANISOU 3188 OD1 ASP A1180 7620 12221 4768 2471 1246 -295 O ATOM 3189 OD2 ASP A1180 -3.866 8.451 13.909 1.00 65.75 O ANISOU 3189 OD2 ASP A1180 8070 11791 5123 2551 1701 -270 O ATOM 3190 N LEU A1181 -6.776 11.729 12.817 1.00 41.41 N ANISOU 3190 N LEU A1181 6504 6063 3168 313 -245 995 N ATOM 3191 CA LEU A1181 -6.725 12.380 11.500 1.00 38.90 C ANISOU 3191 CA LEU A1181 6127 5738 2916 303 -260 960 C ATOM 3192 C LEU A1181 -5.601 11.898 10.575 1.00 40.55 C ANISOU 3192 C LEU A1181 6291 5926 3190 311 -287 973 C ATOM 3193 O LEU A1181 -5.576 12.264 9.401 1.00 39.84 O ANISOU 3193 O LEU A1181 6161 5822 3154 298 -295 951 O ATOM 3194 CB LEU A1181 -6.602 13.903 11.654 1.00 36.21 C ANISOU 3194 CB LEU A1181 5765 5435 2557 320 -291 903 C ATOM 3195 CG LEU A1181 -7.847 14.722 11.992 1.00 35.21 C ANISOU 3195 CG LEU A1181 5675 5319 2384 311 -268 870 C ATOM 3196 CD1 LEU A1181 -7.565 16.205 11.795 1.00 28.21 C ANISOU 3196 CD1 LEU A1181 4734 4486 1498 333 -302 821 C ATOM 3197 CD2 LEU A1181 -9.029 14.280 11.145 1.00 34.25 C ANISOU 3197 CD2 LEU A1181 5567 5162 2287 267 -229 881 C ATOM 3198 N SER A1182 -4.681 11.087 11.089 1.00 41.66 N ANISOU 3198 N SER A1182 6446 6061 3322 333 -301 1008 N ATOM 3199 CA SER A1182 -3.506 10.685 10.315 1.00 43.02 C ANISOU 3199 CA SER A1182 6589 6212 3544 346 -331 1017 C ATOM 3200 C SER A1182 -3.873 9.868 9.075 1.00 44.19 C ANISOU 3200 C SER A1182 6715 6326 3749 325 -304 1038 C ATOM 3201 O SER A1182 -3.346 10.109 7.982 1.00 45.73 O ANISOU 3201 O SER A1182 6876 6505 3993 324 -322 1018 O ATOM 3202 CB SER A1182 -2.534 9.892 11.193 1.00 44.87 C ANISOU 3202 CB SER A1182 6856 6445 3748 378 -351 1054 C ATOM 3203 OG SER A1182 -3.116 8.684 11.647 1.00 47.32 O ANISOU 3203 OG SER A1182 7199 6743 4037 377 -311 1112 O ATOM 3204 N LYS A1183 -4.781 8.909 9.243 1.00 42.68 N ANISOU 3204 N LYS A1183 6546 6126 3544 306 -262 1083 N ATOM 3205 CA LYS A1183 -5.209 8.066 8.130 1.00 41.54 C ANISOU 3205 CA LYS A1183 6383 5957 3444 280 -240 1110 C ATOM 3206 C LYS A1183 -5.941 8.889 7.075 1.00 39.19 C ANISOU 3206 C LYS A1183 6058 5656 3176 251 -237 1064 C ATOM 3207 O LYS A1183 -5.886 8.579 5.884 1.00 36.61 O ANISOU 3207 O LYS A1183 5705 5311 2894 239 -239 1065 O ATOM 3208 CB LYS A1183 -6.100 6.920 8.623 1.00 44.12 C ANISOU 3208 CB LYS A1183 6744 6278 3742 252 -198 1175 C ATOM 3209 CG LYS A1183 -7.420 7.356 9.241 1.00 46.93 C ANISOU 3209 CG LYS A1183 7131 6651 4050 219 -166 1168 C ATOM 3210 CD LYS A1183 -8.300 6.158 9.554 1.00 50.33 C ANISOU 3210 CD LYS A1183 7596 7074 4455 177 -121 1242 C ATOM 3211 CE LYS A1183 -7.589 5.184 10.481 1.00 53.42 C ANISOU 3211 CE LYS A1183 8015 7460 4822 206 -119 1303 C ATOM 3212 NZ LYS A1183 -8.428 3.993 10.786 1.00 55.57 N ANISOU 3212 NZ LYS A1183 8324 7719 5071 159 -74 1386 N ATOM 3213 N PHE A1184 -6.621 9.941 7.521 1.00 38.92 N ANISOU 3213 N PHE A1184 6033 5643 3113 244 -234 1026 N ATOM 3214 CA PHE A1184 -7.304 10.853 6.616 1.00 25.95 C ANISOU 3214 CA PHE A1184 4366 4001 1492 225 -236 983 C ATOM 3215 C PHE A1184 -6.283 11.544 5.724 1.00 32.74 C ANISOU 3215 C PHE A1184 5185 4853 2400 244 -272 948 C ATOM 3216 O PHE A1184 -6.458 11.640 4.507 1.00 32.19 O ANISOU 3216 O PHE A1184 5090 4769 2371 231 -273 934 O ATOM 3217 CB PHE A1184 -8.113 11.885 7.403 1.00 65.01 C ANISOU 3217 CB PHE A1184 9336 8975 6391 223 -229 952 C ATOM 3218 CG PHE A1184 -9.435 12.220 6.781 1.00 62.39 C ANISOU 3218 CG PHE A1184 9006 8645 6056 189 -208 937 C ATOM 3219 CD1 PHE A1184 -9.523 13.162 5.769 1.00 59.89 C ANISOU 3219 CD1 PHE A1184 8657 8324 5773 191 -228 895 C ATOM 3220 CD2 PHE A1184 -10.592 11.593 7.210 1.00 60.49 C ANISOU 3220 CD2 PHE A1184 8797 8414 5771 150 -168 972 C ATOM 3221 CE1 PHE A1184 -10.742 13.471 5.195 1.00 61.03 C ANISOU 3221 CE1 PHE A1184 8805 8474 5909 162 -214 884 C ATOM 3222 CE2 PHE A1184 -11.813 11.898 6.641 1.00 61.18 C ANISOU 3222 CE2 PHE A1184 8882 8517 5848 113 -152 963 C ATOM 3223 CZ PHE A1184 -11.888 12.838 5.632 1.00 63.87 C ANISOU 3223 CZ PHE A1184 9193 8852 6222 121 -178 917 C ATOM 3224 N ARG A1185 -5.205 12.011 6.346 1.00 33.13 N ANISOU 3224 N ARG A1185 5233 4916 2439 272 -303 937 N ATOM 3225 CA ARG A1185 -4.136 12.687 5.627 1.00 32.51 C ANISOU 3225 CA ARG A1185 5123 4833 2395 282 -338 911 C ATOM 3226 C ARG A1185 -3.449 11.743 4.644 1.00 31.75 C ANISOU 3226 C ARG A1185 5016 4705 2342 287 -339 933 C ATOM 3227 O ARG A1185 -3.162 12.123 3.506 1.00 31.19 O ANISOU 3227 O ARG A1185 4921 4622 2309 281 -349 913 O ATOM 3228 CB ARG A1185 -3.114 13.266 6.607 1.00 25.47 C ANISOU 3228 CB ARG A1185 4239 3967 1471 302 -376 904 C ATOM 3229 CG ARG A1185 -3.711 14.210 7.641 1.00 25.85 C ANISOU 3229 CG ARG A1185 4297 4056 1466 303 -379 882 C ATOM 3230 CD ARG A1185 -2.626 14.972 8.380 1.00 26.24 C ANISOU 3230 CD ARG A1185 4344 4141 1484 314 -428 869 C ATOM 3231 NE ARG A1185 -3.148 15.689 9.540 1.00 26.80 N ANISOU 3231 NE ARG A1185 4429 4262 1492 320 -430 852 N ATOM 3232 CZ ARG A1185 -3.672 16.910 9.494 1.00 31.02 C ANISOU 3232 CZ ARG A1185 4943 4832 2010 308 -436 819 C ATOM 3233 NH1 ARG A1185 -3.755 17.558 8.340 1.00 30.17 N ANISOU 3233 NH1 ARG A1185 4805 4709 1948 289 -443 801 N ATOM 3234 NH2 ARG A1185 -4.118 17.483 10.603 1.00 32.42 N ANISOU 3234 NH2 ARG A1185 5131 5065 2121 316 -437 804 N ATOM 3235 N GLU A1186 -3.192 10.512 5.079 1.00 25.26 N ANISOU 3235 N GLU A1186 4215 3874 1510 299 -328 977 N ATOM 3236 CA GLU A1186 -2.552 9.530 4.207 1.00 48.34 C ANISOU 3236 CA GLU A1186 7130 6772 4465 310 -327 1002 C ATOM 3237 C GLU A1186 -3.459 9.211 3.015 1.00 41.61 C ANISOU 3237 C GLU A1186 6257 5909 3642 282 -303 1003 C ATOM 3238 O GLU A1186 -2.983 8.996 1.891 1.00 39.53 O ANISOU 3238 O GLU A1186 5975 5631 3411 288 -309 1000 O ATOM 3239 CB GLU A1186 -2.208 8.258 4.985 1.00 53.93 C ANISOU 3239 CB GLU A1186 7863 7477 5151 332 -319 1058 C ATOM 3240 CG GLU A1186 -1.131 7.406 4.329 1.00 57.48 C ANISOU 3240 CG GLU A1186 8307 7908 5624 362 -332 1084 C ATOM 3241 CD GLU A1186 0.202 8.128 4.223 1.00 59.69 C ANISOU 3241 CD GLU A1186 8605 8169 5905 385 -380 1046 C ATOM 3242 OE1 GLU A1186 0.815 8.408 5.276 1.00 59.15 O ANISOU 3242 OE1 GLU A1186 8567 8105 5802 397 -412 1044 O ATOM 3243 OE2 GLU A1186 0.632 8.421 3.087 1.00 61.51 O ANISOU 3243 OE2 GLU A1186 8823 8380 6166 381 -393 1022 O ATOM 3244 N ASN A1187 -4.766 9.198 3.265 1.00 36.73 N ANISOU 3244 N ASN A1187 5650 5298 3006 250 -278 1008 N ATOM 3245 CA ASN A1187 -5.746 9.037 2.196 1.00 31.95 C ANISOU 3245 CA ASN A1187 5035 4685 2418 216 -263 1005 C ATOM 3246 C ASN A1187 -5.697 10.202 1.216 1.00 29.06 C ANISOU 3246 C ASN A1187 4641 4320 2080 218 -280 952 C ATOM 3247 O ASN A1187 -5.833 10.011 0.005 1.00 27.22 O ANISOU 3247 O ASN A1187 4392 4077 1873 208 -280 947 O ATOM 3248 CB ASN A1187 -7.158 8.898 2.768 1.00 30.67 C ANISOU 3248 CB ASN A1187 4900 4534 2219 179 -237 1020 C ATOM 3249 CG ASN A1187 -7.390 7.556 3.431 1.00 32.21 C ANISOU 3249 CG ASN A1187 5128 4721 2389 161 -215 1087 C ATOM 3250 OD1 ASN A1187 -6.628 6.610 3.227 1.00 33.02 O ANISOU 3250 OD1 ASN A1187 5230 4808 2507 174 -221 1124 O ATOM 3251 ND2 ASN A1187 -8.451 7.464 4.225 1.00 33.27 N ANISOU 3251 ND2 ASN A1187 5293 4869 2480 130 -188 1107 N ATOM 3252 N CYS A1188 -5.505 11.407 1.746 1.00 23.74 N ANISOU 3252 N CYS A1188 3963 3659 1397 230 -295 918 N ATOM 3253 CA CYS A1188 -5.355 12.590 0.905 1.00 25.45 C ANISOU 3253 CA CYS A1188 4155 3877 1638 232 -313 877 C ATOM 3254 C CYS A1188 -4.133 12.459 -0.001 1.00 26.34 C ANISOU 3254 C CYS A1188 4252 3973 1784 248 -330 876 C ATOM 3255 O CYS A1188 -4.216 12.707 -1.208 1.00 26.82 O ANISOU 3255 O CYS A1188 4296 4024 1870 243 -331 861 O ATOM 3256 CB CYS A1188 -5.247 13.854 1.761 1.00 25.40 C ANISOU 3256 CB CYS A1188 4150 3894 1609 240 -330 851 C ATOM 3257 SG CYS A1188 -6.755 14.273 2.667 1.00 37.43 S ANISOU 3257 SG CYS A1188 5696 5441 3086 228 -309 842 S ATOM 3258 N LYS A1189 -3.005 12.064 0.585 1.00 23.31 N ANISOU 3258 N LYS A1189 3880 3585 1393 269 -345 893 N ATOM 3259 CA LYS A1189 -1.778 11.841 -0.178 1.00 26.30 C ANISOU 3259 CA LYS A1189 4257 3944 1792 286 -363 895 C ATOM 3260 C LYS A1189 -1.991 10.839 -1.309 1.00 27.25 C ANISOU 3260 C LYS A1189 4371 4051 1933 288 -343 911 C ATOM 3261 O LYS A1189 -1.700 11.131 -2.477 1.00 27.17 O ANISOU 3261 O LYS A1189 4350 4029 1943 289 -348 894 O ATOM 3262 CB LYS A1189 -0.654 11.344 0.731 1.00 23.77 C ANISOU 3262 CB LYS A1189 3961 3619 1450 309 -386 917 C ATOM 3263 CG LYS A1189 -0.052 12.387 1.652 1.00 23.97 C ANISOU 3263 CG LYS A1189 3991 3666 1452 305 -421 903 C ATOM 3264 CD LYS A1189 1.048 11.755 2.489 1.00 29.20 C ANISOU 3264 CD LYS A1189 4683 4322 2089 326 -451 928 C ATOM 3265 CE LYS A1189 1.763 12.771 3.358 1.00 29.64 C ANISOU 3265 CE LYS A1189 4737 4411 2114 318 -497 919 C ATOM 3266 NZ LYS A1189 2.934 12.151 4.041 1.00 29.81 N ANISOU 3266 NZ LYS A1189 4787 4427 2110 335 -538 945 N ATOM 3267 N LYS A1190 -2.498 9.659 -0.955 1.00 26.41 N ANISOU 3267 N LYS A1190 4270 3949 1815 286 -322 949 N ATOM 3268 CA LYS A1190 -2.728 8.607 -1.942 1.00 23.50 C ANISOU 3268 CA LYS A1190 3890 3581 1459 280 -308 977 C ATOM 3269 C LYS A1190 -3.651 9.079 -3.063 1.00 23.06 C ANISOU 3269 C LYS A1190 3819 3526 1415 252 -303 949 C ATOM 3270 O LYS A1190 -3.361 8.873 -4.246 1.00 22.92 O ANISOU 3270 O LYS A1190 3787 3509 1411 258 -306 945 O ATOM 3271 CB LYS A1190 -3.308 7.358 -1.274 1.00 24.04 C ANISOU 3271 CB LYS A1190 3971 3654 1507 260 -293 1033 C ATOM 3272 CG LYS A1190 -2.312 6.602 -0.412 1.00 45.61 C ANISOU 3272 CG LYS A1190 6710 6391 4230 293 -298 1076 C ATOM 3273 CD LYS A1190 -2.946 5.386 0.245 1.00 44.23 C ANISOU 3273 CD LYS A1190 6558 6213 4035 263 -285 1142 C ATOM 3274 CE LYS A1190 -2.012 4.783 1.283 1.00 42.23 C ANISOU 3274 CE LYS A1190 6305 5971 3769 298 -293 1189 C ATOM 3275 NZ LYS A1190 -2.674 3.710 2.075 1.00 41.82 N ANISOU 3275 NZ LYS A1190 6290 5906 3694 265 -280 1255 N ATOM 3276 N ARG A1191 -4.751 9.725 -2.687 1.00 22.91 N ANISOU 3276 N ARG A1191 3806 3513 1385 225 -298 930 N ATOM 3277 CA ARG A1191 -5.716 10.225 -3.661 1.00 22.58 C ANISOU 3277 CA ARG A1191 3755 3474 1349 202 -298 904 C ATOM 3278 C ARG A1191 -5.076 11.219 -4.626 1.00 22.16 C ANISOU 3278 C ARG A1191 3682 3418 1321 222 -311 868 C ATOM 3279 O ARG A1191 -5.246 11.109 -5.842 1.00 22.01 O ANISOU 3279 O ARG A1191 3653 3399 1310 219 -312 860 O ATOM 3280 CB ARG A1191 -6.906 10.873 -2.951 1.00 22.60 C ANISOU 3280 CB ARG A1191 3769 3488 1330 179 -292 891 C ATOM 3281 CG ARG A1191 -7.941 11.477 -3.886 1.00 22.35 C ANISOU 3281 CG ARG A1191 3730 3463 1298 160 -296 865 C ATOM 3282 CD ARG A1191 -8.457 10.457 -4.888 1.00 30.35 C ANISOU 3282 CD ARG A1191 4752 4476 2305 132 -297 884 C ATOM 3283 NE ARG A1191 -9.449 11.042 -5.785 1.00 30.34 N ANISOU 3283 NE ARG A1191 4744 4486 2296 115 -308 859 N ATOM 3284 CZ ARG A1191 -9.809 10.514 -6.950 1.00 30.86 C ANISOU 3284 CZ ARG A1191 4810 4553 2361 92 -320 858 C ATOM 3285 NH1 ARG A1191 -9.254 9.386 -7.372 1.00 32.19 N ANISOU 3285 NH1 ARG A1191 4990 4710 2530 84 -322 882 N ATOM 3286 NH2 ARG A1191 -10.721 11.119 -7.700 1.00 22.26 N ANISOU 3286 NH2 ARG A1191 3713 3479 1267 77 -334 832 N ATOM 3287 N ALA A1192 -4.333 12.178 -4.080 1.00 22.08 N ANISOU 3287 N ALA A1192 3670 3404 1315 238 -323 851 N ATOM 3288 CA ALA A1192 -3.680 13.198 -4.897 1.00 21.81 C ANISOU 3288 CA ALA A1192 3625 3362 1298 247 -338 827 C ATOM 3289 C ALA A1192 -2.686 12.581 -5.879 1.00 21.85 C ANISOU 3289 C ALA A1192 3636 3352 1314 264 -340 835 C ATOM 3290 O ALA A1192 -2.686 12.913 -7.072 1.00 27.43 O ANISOU 3290 O ALA A1192 4339 4054 2031 265 -341 821 O ATOM 3291 CB ALA A1192 -2.982 14.218 -4.009 1.00 21.88 C ANISOU 3291 CB ALA A1192 3637 3376 1301 248 -359 820 C ATOM 3292 N MET A1193 -1.848 11.677 -5.378 1.00 22.18 N ANISOU 3292 N MET A1193 3695 3385 1348 282 -343 859 N ATOM 3293 CA MET A1193 -0.842 11.041 -6.223 1.00 34.80 C ANISOU 3293 CA MET A1193 5314 4961 2946 304 -349 866 C ATOM 3294 C MET A1193 -1.477 10.213 -7.340 1.00 34.26 C ANISOU 3294 C MET A1193 5223 4915 2879 309 -327 877 C ATOM 3295 O MET A1193 -1.100 10.347 -8.509 1.00 34.26 O ANISOU 3295 O MET A1193 5236 4903 2880 318 -330 862 O ATOM 3296 CB MET A1193 0.093 10.170 -5.380 1.00 36.29 C ANISOU 3296 CB MET A1193 5537 5132 3121 324 -361 891 C ATOM 3297 CG MET A1193 0.953 10.968 -4.412 1.00 37.84 C ANISOU 3297 CG MET A1193 5750 5319 3309 310 -397 887 C ATOM 3298 SD MET A1193 2.136 9.963 -3.495 1.00 80.14 S ANISOU 3298 SD MET A1193 11160 10645 8643 321 -433 918 S ATOM 3299 CE MET A1193 2.814 11.188 -2.377 1.00 45.10 C ANISOU 3299 CE MET A1193 6700 6244 4192 304 -470 918 C ATOM 3300 N SER A1194 -2.446 9.373 -6.984 1.00 32.13 N ANISOU 3300 N SER A1194 4928 4677 2602 286 -313 907 N ATOM 3301 CA SER A1194 -3.108 8.526 -7.974 1.00 30.11 C ANISOU 3301 CA SER A1194 4654 4448 2338 258 -311 927 C ATOM 3302 C SER A1194 -3.838 9.363 -9.022 1.00 30.36 C ANISOU 3302 C SER A1194 4683 4480 2372 248 -314 887 C ATOM 3303 O SER A1194 -3.834 9.026 -10.207 1.00 30.79 O ANISOU 3303 O SER A1194 4725 4556 2419 243 -317 889 O ATOM 3304 CB SER A1194 -4.089 7.563 -7.302 1.00 29.36 C ANISOU 3304 CB SER A1194 4586 4347 2223 214 -312 962 C ATOM 3305 OG SER A1194 -5.283 8.225 -6.926 1.00 29.17 O ANISOU 3305 OG SER A1194 4577 4314 2192 190 -309 936 O ATOM 3306 N PHE A1195 -4.458 10.454 -8.579 1.00 28.14 N ANISOU 3306 N PHE A1195 4409 4184 2099 240 -316 857 N ATOM 3307 CA PHE A1195 -5.157 11.357 -9.487 1.00 26.27 C ANISOU 3307 CA PHE A1195 4166 3950 1865 232 -322 825 C ATOM 3308 C PHE A1195 -4.183 11.971 -10.489 1.00 25.27 C ANISOU 3308 C PHE A1195 4039 3812 1749 261 -324 808 C ATOM 3309 O PHE A1195 -4.417 11.938 -11.704 1.00 26.08 O ANISOU 3309 O PHE A1195 4137 3928 1845 264 -325 799 O ATOM 3310 CB PHE A1195 -5.877 12.457 -8.701 1.00 21.45 C ANISOU 3310 CB PHE A1195 3558 3335 1259 220 -326 805 C ATOM 3311 CG PHE A1195 -6.829 13.272 -9.530 1.00 21.29 C ANISOU 3311 CG PHE A1195 3532 3321 1236 211 -335 781 C ATOM 3312 CD1 PHE A1195 -8.123 12.834 -9.752 1.00 21.43 C ANISOU 3312 CD1 PHE A1195 3557 3354 1231 183 -341 782 C ATOM 3313 CD2 PHE A1195 -6.432 14.479 -10.080 1.00 21.09 C ANISOU 3313 CD2 PHE A1195 3500 3289 1226 228 -341 762 C ATOM 3314 CE1 PHE A1195 -9.002 13.582 -10.513 1.00 21.37 C ANISOU 3314 CE1 PHE A1195 3546 3356 1217 180 -354 760 C ATOM 3315 CE2 PHE A1195 -7.307 15.231 -10.843 1.00 21.53 C ANISOU 3315 CE2 PHE A1195 3551 3351 1277 226 -351 745 C ATOM 3316 CZ PHE A1195 -8.594 14.782 -11.059 1.00 21.16 C ANISOU 3316 CZ PHE A1195 3509 3321 1210 206 -359 741 C ATOM 3317 N SER A1196 -3.086 12.519 -9.970 1.00 23.96 N ANISOU 3317 N SER A1196 3892 3620 1593 275 -330 805 N ATOM 3318 CA SER A1196 -2.061 13.135 -10.809 1.00 21.54 C ANISOU 3318 CA SER A1196 3612 3284 1288 282 -341 795 C ATOM 3319 C SER A1196 -1.514 12.150 -11.846 1.00 22.31 C ANISOU 3319 C SER A1196 3741 3366 1368 299 -339 798 C ATOM 3320 O SER A1196 -1.439 12.461 -13.046 1.00 22.40 O ANISOU 3320 O SER A1196 3777 3362 1371 292 -345 783 O ATOM 3321 CB SER A1196 -0.924 13.675 -9.939 1.00 30.07 C ANISOU 3321 CB SER A1196 4710 4347 2371 271 -362 804 C ATOM 3322 OG SER A1196 0.027 14.381 -10.714 1.00 31.24 O ANISOU 3322 OG SER A1196 4873 4482 2514 252 -379 810 O ATOM 3323 N LYS A 288 -1.146 10.959 -11.378 1.00 22.12 N ANISOU 3323 N LYS A 288 3723 3347 1334 319 -332 819 N ATOM 3324 CA LYS A 288 -0.633 9.914 -12.260 1.00 34.99 C ANISOU 3324 CA LYS A 288 5392 4962 2940 340 -332 824 C ATOM 3325 C LYS A 288 -1.654 9.521 -13.324 1.00 33.42 C ANISOU 3325 C LYS A 288 4999 4955 2743 313 -305 879 C ATOM 3326 O LYS A 288 -1.297 9.270 -14.479 1.00 30.42 O ANISOU 3326 O LYS A 288 4506 4682 2369 132 -354 940 O ATOM 3327 CB LYS A 288 -0.228 8.677 -11.456 1.00 40.49 C ANISOU 3327 CB LYS A 288 5914 5824 3646 352 -303 921 C ATOM 3328 CG LYS A 288 1.071 8.821 -10.681 1.00 43.73 C ANISOU 3328 CG LYS A 288 6643 5923 4050 146 -455 863 C ATOM 3329 CD LYS A 288 1.534 7.473 -10.154 1.00 48.18 C ANISOU 3329 CD LYS A 288 7043 6629 4635 -21 -508 994 C ATOM 3330 CE LYS A 288 2.837 7.592 -9.384 1.00 52.57 C ANISOU 3330 CE LYS A 288 7685 7121 5168 64 -521 984 C ATOM 3331 NZ LYS A 288 3.236 6.291 -8.776 1.00 57.64 N ANISOU 3331 NZ LYS A 288 8270 7826 5804 62 -533 1066 N ATOM 3332 N GLN A 289 -2.922 9.471 -12.927 1.00 41.07 N ANISOU 3332 N GLN A 289 6309 6403 2894 -120 -252 -764 N ATOM 3333 CA GLN A 289 -3.990 9.103 -13.848 1.00 42.50 C ANISOU 3333 CA GLN A 289 6491 6477 3182 -68 -181 -799 C ATOM 3334 C GLN A 289 -4.153 10.141 -14.948 1.00 37.67 C ANISOU 3334 C GLN A 289 5808 5739 2766 -101 -202 -899 C ATOM 3335 O GLN A 289 -4.336 9.789 -16.112 1.00 35.00 O ANISOU 3335 O GLN A 289 5470 5300 2527 -76 -200 -880 O ATOM 3336 CB GLN A 289 -5.316 8.923 -13.108 1.00 50.16 C ANISOU 3336 CB GLN A 289 7470 7516 4071 -10 -84 -865 C ATOM 3337 CG GLN A 289 -6.491 8.647 -14.034 1.00 55.08 C ANISOU 3337 CG GLN A 289 8095 8034 4798 30 -20 -928 C ATOM 3338 CD GLN A 289 -7.767 8.323 -13.284 1.00 61.12 C ANISOU 3338 CD GLN A 289 8988 8803 5432 89 94 -967 C ATOM 3339 OE1 GLN A 289 -7.777 8.245 -12.056 1.00 66.68 O ANISOU 3339 OE1 GLN A 289 9780 9600 5956 90 142 -937 O ATOM 3340 NE2 GLN A 289 -8.855 8.130 -14.024 1.00 60.42 N ANISOU 3340 NE2 GLN A 289 8920 8628 5409 70 166 -1041 N ATOM 3341 N MET A 290 -4.088 11.419 -14.587 1.00 27.68 N ANISOU 3341 N MET A 290 4520 4466 1531 -164 -216 -1002 N ATOM 3342 CA MET A 290 -4.252 12.464 -15.590 1.00 26.85 C ANISOU 3342 CA MET A 290 4416 4221 1565 -169 -236 -1077 C ATOM 3343 C MET A 290 -3.037 12.505 -16.518 1.00 31.47 C ANISOU 3343 C MET A 290 4981 4769 2207 -152 -320 -1012 C ATOM 3344 O MET A 290 -3.167 12.806 -17.709 1.00 31.35 O ANISOU 3344 O MET A 290 4975 4648 2288 -129 -336 -1017 O ATOM 3345 CB MET A 290 -4.489 13.826 -14.929 1.00 28.22 C ANISOU 3345 CB MET A 290 4640 4357 1724 -220 -224 -1216 C ATOM 3346 CG MET A 290 -3.247 14.661 -14.683 1.00 28.90 C ANISOU 3346 CG MET A 290 4705 4478 1799 -256 -300 -1261 C ATOM 3347 SD MET A 290 -3.654 16.288 -14.026 1.00 86.66 S ANISOU 3347 SD MET A 290 12111 11709 9109 -304 -273 -1469 S ATOM 3348 CE MET A 290 -4.147 15.866 -12.360 1.00 32.67 C ANISOU 3348 CE MET A 290 5489 4854 2070 -406 -199 -1419 C ATOM 3349 N ARG A 291 -1.863 12.177 -15.981 1.00 26.41 N ANISOU 3349 N ARG A 291 4321 4228 1484 -173 -371 -950 N ATOM 3350 CA ARG A 291 -0.659 12.121 -16.806 1.00 25.85 C ANISOU 3350 CA ARG A 291 4225 4149 1449 -174 -436 -898 C ATOM 3351 C ARG A 291 -0.757 10.991 -17.834 1.00 24.58 C ANISOU 3351 C ARG A 291 4086 3926 1327 -120 -419 -800 C ATOM 3352 O ARG A 291 -0.521 11.194 -19.036 1.00 23.70 O ANISOU 3352 O ARG A 291 3962 3731 1313 -111 -430 -795 O ATOM 3353 CB ARG A 291 0.581 11.938 -15.931 1.00 50.71 C ANISOU 3353 CB ARG A 291 7356 7433 4476 -232 -499 -853 C ATOM 3354 CG ARG A 291 1.891 12.203 -16.649 1.00 49.46 C ANISOU 3354 CG ARG A 291 7149 7298 4345 -271 -564 -847 C ATOM 3355 CD ARG A 291 3.072 12.004 -15.718 1.00 49.04 C ANISOU 3355 CD ARG A 291 7303 7190 4141 -378 -690 -748 C ATOM 3356 NE ARG A 291 2.884 12.701 -14.449 1.00 52.97 N ANISOU 3356 NE ARG A 291 7998 7575 4553 -349 -762 -803 N ATOM 3357 CZ ARG A 291 3.184 13.979 -14.245 1.00 56.86 C ANISOU 3357 CZ ARG A 291 8550 7973 5080 -183 -883 -974 C ATOM 3358 NH1 ARG A 291 3.688 14.710 -15.230 1.00 55.05 N ANISOU 3358 NH1 ARG A 291 8180 7772 4966 -119 -920 -1098 N ATOM 3359 NH2 ARG A 291 2.979 14.528 -13.055 1.00 62.53 N ANISOU 3359 NH2 ARG A 291 9316 8748 5692 -194 -908 -1069 N ATOM 3360 N ALA A 292 -1.115 9.803 -17.350 1.00 26.44 N ANISOU 3360 N ALA A 292 4374 4182 1491 -75 -386 -721 N ATOM 3361 CA ALA A 292 -1.306 8.637 -18.207 1.00 24.09 C ANISOU 3361 CA ALA A 292 4130 3784 1240 -10 -354 -643 C ATOM 3362 C ALA A 292 -2.359 8.919 -19.274 1.00 40.75 C ANISOU 3362 C ALA A 292 6207 5795 3481 -19 -306 -710 C ATOM 3363 O ALA A 292 -2.209 8.537 -20.442 1.00 40.70 O ANISOU 3363 O ALA A 292 6200 5715 3548 -4 -305 -690 O ATOM 3364 CB ALA A 292 -1.705 7.427 -17.373 1.00 25.11 C ANISOU 3364 CB ALA A 292 4374 3922 1246 41 -308 -560 C ATOM 3365 N ARG A 293 -3.420 9.601 -18.854 1.00 23.26 N ANISOU 3365 N ARG A 293 3964 3600 1273 -44 -272 -799 N ATOM 3366 CA ARG A 293 -4.506 9.989 -19.743 1.00 22.76 C ANISOU 3366 CA ARG A 293 3870 3475 1301 -48 -244 -869 C ATOM 3367 C ARG A 293 -3.978 10.848 -20.880 1.00 25.34 C ANISOU 3367 C ARG A 293 4192 3723 1715 -43 -303 -858 C ATOM 3368 O ARG A 293 -4.231 10.576 -22.062 1.00 24.24 O ANISOU 3368 O ARG A 293 4043 3537 1631 -31 -304 -841 O ATOM 3369 CB ARG A 293 -5.580 10.748 -18.966 1.00 27.77 C ANISOU 3369 CB ARG A 293 4502 4147 1902 -75 -203 -981 C ATOM 3370 CG ARG A 293 -6.923 10.804 -19.658 1.00 30.47 C ANISOU 3370 CG ARG A 293 4843 4443 2292 -77 -160 -1048 C ATOM 3371 CD ARG A 293 -7.974 10.097 -18.825 1.00 33.99 C ANISOU 3371 CD ARG A 293 5294 4946 2675 -122 -56 -1092 C ATOM 3372 NE ARG A 293 -8.078 10.671 -17.487 1.00 38.34 N ANISOU 3372 NE ARG A 293 5908 5520 3141 -150 -19 -1128 N ATOM 3373 CZ ARG A 293 -8.947 10.267 -16.567 1.00 42.23 C ANISOU 3373 CZ ARG A 293 6631 5902 3513 -102 51 -1109 C ATOM 3374 NH1 ARG A 293 -9.792 9.283 -16.840 1.00 43.13 N ANISOU 3374 NH1 ARG A 293 6718 6080 3590 87 54 -1143 N ATOM 3375 NH2 ARG A 293 -8.969 10.849 -15.376 1.00 44.54 N ANISOU 3375 NH2 ARG A 293 6999 6217 3708 -45 55 -1149 N ATOM 3376 N ARG A 294 -3.238 11.884 -20.503 1.00 22.57 N ANISOU 3376 N ARG A 294 3856 3369 1351 -60 -350 -879 N ATOM 3377 CA ARG A 294 -2.612 12.779 -21.460 1.00 22.48 C ANISOU 3377 CA ARG A 294 3879 3278 1385 -62 -405 -872 C ATOM 3378 C ARG A 294 -1.785 12.010 -22.485 1.00 21.75 C ANISOU 3378 C ARG A 294 3760 3197 1308 -67 -411 -794 C ATOM 3379 O ARG A 294 -1.982 12.165 -23.695 1.00 21.44 O ANISOU 3379 O ARG A 294 3745 3098 1305 -55 -420 -774 O ATOM 3380 CB ARG A 294 -1.740 13.789 -20.724 1.00 31.56 C ANISOU 3380 CB ARG A 294 5054 4444 2493 -106 -448 -932 C ATOM 3381 CG ARG A 294 -1.514 15.082 -21.465 1.00 33.07 C ANISOU 3381 CG ARG A 294 5361 4490 2715 -119 -498 -966 C ATOM 3382 CD ARG A 294 -0.941 16.105 -20.518 1.00 34.65 C ANISOU 3382 CD ARG A 294 5604 4687 2876 -179 -529 -1078 C ATOM 3383 NE ARG A 294 -0.623 17.351 -21.211 1.00 36.07 N ANISOU 3383 NE ARG A 294 5962 4669 3074 -228 -575 -1107 N ATOM 3384 CZ ARG A 294 -1.438 18.392 -21.254 1.00 38.36 C ANISOU 3384 CZ ARG A 294 6421 4765 3390 -182 -588 -1170 C ATOM 3385 NH1 ARG A 294 -2.612 18.335 -20.639 1.00 38.62 N ANISOU 3385 NH1 ARG A 294 6420 4818 3437 -78 -557 -1232 N ATOM 3386 NH2 ARG A 294 -1.068 19.478 -21.904 1.00 40.20 N ANISOU 3386 NH2 ARG A 294 6880 4773 3623 -245 -629 -1176 N ATOM 3387 N LYS A 295 -0.871 11.172 -21.997 1.00 21.81 N ANISOU 3387 N LYS A 295 3733 3290 1264 -77 -411 -755 N ATOM 3388 CA LYS A 295 -0.015 10.389 -22.889 1.00 21.51 C ANISOU 3388 CA LYS A 295 3681 3269 1221 -71 -412 -706 C ATOM 3389 C LYS A 295 -0.825 9.541 -23.876 1.00 25.51 C ANISOU 3389 C LYS A 295 4198 3714 1781 -42 -364 -693 C ATOM 3390 O LYS A 295 -0.565 9.559 -25.091 1.00 25.48 O ANISOU 3390 O LYS A 295 4186 3700 1796 -52 -363 -692 O ATOM 3391 CB LYS A 295 0.928 9.494 -22.078 1.00 22.15 C ANISOU 3391 CB LYS A 295 3766 3438 1211 -54 -432 -663 C ATOM 3392 CG LYS A 295 2.043 10.254 -21.372 1.00 41.99 C ANISOU 3392 CG LYS A 295 6234 6079 3643 -113 -498 -695 C ATOM 3393 CD LYS A 295 2.951 9.325 -20.578 1.00 41.61 C ANISOU 3393 CD LYS A 295 6215 6118 3476 -82 -552 -625 C ATOM 3394 CE LYS A 295 3.970 10.117 -19.770 1.00 41.87 C ANISOU 3394 CE LYS A 295 6228 6254 3427 -186 -636 -650 C ATOM 3395 NZ LYS A 295 4.769 9.247 -18.861 1.00 44.60 N ANISOU 3395 NZ LYS A 295 6611 6695 3639 -71 -742 -577 N ATOM 3396 N THR A 296 -1.813 8.816 -23.355 1.00 25.38 N ANISOU 3396 N THR A 296 4200 3677 1764 -18 -322 -702 N ATOM 3397 CA THR A 296 -2.660 7.967 -24.192 1.00 20.57 C ANISOU 3397 CA THR A 296 3594 3032 1189 -11 -275 -730 C ATOM 3398 C THR A 296 -3.350 8.761 -25.303 1.00 20.35 C ANISOU 3398 C THR A 296 3521 3004 1206 -32 -293 -767 C ATOM 3399 O THR A 296 -3.261 8.404 -26.491 1.00 20.27 O ANISOU 3399 O THR A 296 3496 3002 1205 -41 -287 -776 O ATOM 3400 CB THR A 296 -3.732 7.244 -23.355 1.00 21.03 C ANISOU 3400 CB THR A 296 3685 3089 1217 -7 -221 -764 C ATOM 3401 OG1 THR A 296 -3.102 6.290 -22.492 1.00 28.77 O ANISOU 3401 OG1 THR A 296 4779 4038 2116 29 -201 -698 O ATOM 3402 CG2 THR A 296 -4.720 6.524 -24.259 1.00 21.15 C ANISOU 3402 CG2 THR A 296 3679 3095 1263 -27 -175 -842 C ATOM 3403 N ALA A 297 -4.025 9.842 -24.916 1.00 20.59 N ANISOU 3403 N ALA A 297 3557 3026 1241 -27 -320 -792 N ATOM 3404 CA ALA A 297 -4.736 10.676 -25.880 1.00 21.67 C ANISOU 3404 CA ALA A 297 3714 3137 1384 -6 -363 -810 C ATOM 3405 C ALA A 297 -3.788 11.234 -26.939 1.00 23.00 C ANISOU 3405 C ALA A 297 3927 3278 1536 -7 -408 -754 C ATOM 3406 O ALA A 297 -4.135 11.295 -28.120 1.00 22.44 O ANISOU 3406 O ALA A 297 3869 3220 1438 3 -433 -747 O ATOM 3407 CB ALA A 297 -5.463 11.806 -25.173 1.00 21.62 C ANISOU 3407 CB ALA A 297 3759 3085 1369 46 -399 -854 C ATOM 3408 N LYS A 298 -2.593 11.635 -26.512 1.00 24.62 N ANISOU 3408 N LYS A 298 4158 3467 1731 -32 -420 -723 N ATOM 3409 CA LYS A 298 -1.581 12.125 -27.443 1.00 21.33 C ANISOU 3409 CA LYS A 298 3794 3037 1272 -66 -445 -684 C ATOM 3410 C LYS A 298 -1.240 11.070 -28.489 1.00 23.26 C ANISOU 3410 C LYS A 298 3974 3363 1501 -78 -405 -679 C ATOM 3411 O LYS A 298 -1.238 11.353 -29.695 1.00 25.22 O ANISOU 3411 O LYS A 298 4263 3621 1697 -88 -419 -658 O ATOM 3412 CB LYS A 298 -0.312 12.543 -26.698 1.00 21.69 C ANISOU 3412 CB LYS A 298 3852 3096 1293 -118 -458 -688 C ATOM 3413 CG LYS A 298 0.887 12.751 -27.610 1.00 22.31 C ANISOU 3413 CG LYS A 298 3968 3202 1308 -186 -463 -666 C ATOM 3414 CD LYS A 298 2.109 13.234 -26.846 1.00 49.54 C ANISOU 3414 CD LYS A 298 7420 6688 4715 -262 -489 -701 C ATOM 3415 CE LYS A 298 3.295 13.420 -27.782 1.00 49.11 C ANISOU 3415 CE LYS A 298 7405 6676 4577 -378 -476 -690 C ATOM 3416 NZ LYS A 298 4.440 14.090 -27.107 1.00 47.58 N ANISOU 3416 NZ LYS A 298 7220 6524 4335 -522 -504 -742 N ATOM 3417 N MET A 299 -0.961 9.853 -28.025 1.00 22.75 N ANISOU 3417 N MET A 299 3842 3346 1458 -73 -357 -701 N ATOM 3418 CA MET A 299 -0.618 8.769 -28.942 1.00 20.71 C ANISOU 3418 CA MET A 299 3553 3136 1180 -75 -312 -730 C ATOM 3419 C MET A 299 -1.735 8.499 -29.947 1.00 20.85 C ANISOU 3419 C MET A 299 3548 3174 1199 -81 -302 -771 C ATOM 3420 O MET A 299 -1.495 8.476 -31.157 1.00 21.36 O ANISOU 3420 O MET A 299 3604 3303 1210 -92 -300 -787 O ATOM 3421 CB MET A 299 -0.299 7.486 -28.177 1.00 20.68 C ANISOU 3421 CB MET A 299 3564 3111 1183 -47 -270 -747 C ATOM 3422 CG MET A 299 0.178 6.354 -29.074 1.00 21.19 C ANISOU 3422 CG MET A 299 3645 3186 1221 -35 -214 -804 C ATOM 3423 SD MET A 299 0.099 4.739 -28.282 1.00 50.18 S ANISOU 3423 SD MET A 299 7434 6735 4895 49 -158 -831 S ATOM 3424 CE MET A 299 -1.668 4.578 -28.040 1.00 21.42 C ANISOU 3424 CE MET A 299 3776 3050 1312 6 -138 -868 C ATOM 3425 N LEU A 300 -2.953 8.301 -29.447 1.00 20.70 N ANISOU 3425 N LEU A 300 3514 3134 1217 -78 -297 -803 N ATOM 3426 CA LEU A 300 -4.087 8.010 -30.326 1.00 21.21 C ANISOU 3426 CA LEU A 300 3543 3256 1259 -110 -294 -870 C ATOM 3427 C LEU A 300 -4.331 9.138 -31.329 1.00 21.87 C ANISOU 3427 C LEU A 300 3669 3373 1270 -102 -368 -824 C ATOM 3428 O LEU A 300 -4.704 8.894 -32.485 1.00 34.66 O ANISOU 3428 O LEU A 300 5274 5070 2825 -138 -375 -852 O ATOM 3429 CB LEU A 300 -5.344 7.754 -29.499 1.00 21.32 C ANISOU 3429 CB LEU A 300 3544 3249 1306 -127 -274 -919 C ATOM 3430 CG LEU A 300 -5.234 6.522 -28.602 1.00 25.46 C ANISOU 3430 CG LEU A 300 4060 3740 1874 -107 -209 -966 C ATOM 3431 CD1 LEU A 300 -6.426 6.426 -27.673 1.00 21.60 C ANISOU 3431 CD1 LEU A 300 3551 3260 1397 -122 -183 -1019 C ATOM 3432 CD2 LEU A 300 -5.097 5.262 -29.441 1.00 21.76 C ANISOU 3432 CD2 LEU A 300 3581 3267 1422 -86 -176 -1047 C ATOM 3433 N MET A 301 -4.105 10.369 -30.882 1.00 21.93 N ANISOU 3433 N MET A 301 3757 3301 1273 -48 -428 -751 N ATOM 3434 CA MET A 301 -4.212 11.527 -31.760 1.00 23.01 C ANISOU 3434 CA MET A 301 4009 3414 1320 -3 -514 -687 C ATOM 3435 C MET A 301 -3.207 11.441 -32.898 1.00 23.82 C ANISOU 3435 C MET A 301 4130 3584 1339 -51 -493 -649 C ATOM 3436 O MET A 301 -3.560 11.637 -34.063 1.00 24.65 O ANISOU 3436 O MET A 301 4269 3762 1333 -45 -534 -626 O ATOM 3437 CB MET A 301 -3.994 12.822 -30.984 1.00 23.32 C ANISOU 3437 CB MET A 301 4193 3301 1366 51 -572 -636 C ATOM 3438 CG MET A 301 -4.094 14.070 -31.844 1.00 25.32 C ANISOU 3438 CG MET A 301 4658 3460 1504 111 -673 -553 C ATOM 3439 SD MET A 301 -5.715 14.228 -32.618 1.00102.94 S ANISOU 3439 SD MET A 301 14495 13359 11260 268 -789 -571 S ATOM 3440 CE MET A 301 -5.521 15.769 -33.507 1.00 67.71 C ANISOU 3440 CE MET A 301 10361 8732 6633 366 -921 -420 C ATOM 3441 N VAL A 302 -1.954 11.151 -32.556 1.00 20.56 N ANISOU 3441 N VAL A 302 4584 1570 1658 -27 848 -253 N ATOM 3442 CA VAL A 302 -0.912 11.044 -33.571 1.00 20.05 C ANISOU 3442 CA VAL A 302 4616 1442 1559 -40 870 -180 C ATOM 3443 C VAL A 302 -1.226 9.922 -34.560 1.00 23.10 C ANISOU 3443 C VAL A 302 4995 1854 1929 -27 844 -217 C ATOM 3444 O VAL A 302 -1.055 10.092 -35.766 1.00 20.88 O ANISOU 3444 O VAL A 302 4813 1533 1589 13 824 -199 O ATOM 3445 CB VAL A 302 0.475 10.807 -32.943 1.00 19.20 C ANISOU 3445 CB VAL A 302 4500 1291 1505 -127 939 -100 C ATOM 3446 CG1 VAL A 302 1.513 10.539 -34.023 1.00 19.28 C ANISOU 3446 CG1 VAL A 302 4594 1232 1497 -142 964 -45 C ATOM 3447 CG2 VAL A 302 0.883 12.006 -32.103 1.00 19.04 C ANISOU 3447 CG2 VAL A 302 4506 1236 1494 -141 964 -62 C ATOM 3448 N VAL A 303 -1.697 8.785 -34.051 1.00 23.16 N ANISOU 3448 N VAL A 303 4893 1922 1985 -60 846 -268 N ATOM 3449 CA VAL A 303 -2.088 7.668 -34.910 1.00 20.32 C ANISOU 3449 CA VAL A 303 4518 1590 1612 -50 821 -314 C ATOM 3450 C VAL A 303 -3.173 8.083 -35.900 1.00 23.02 C ANISOU 3450 C VAL A 303 4906 1945 1894 40 743 -392 C ATOM 3451 O VAL A 303 -3.063 7.825 -37.103 1.00 23.88 O ANISOU 3451 O VAL A 303 5089 2032 1952 70 719 -388 O ATOM 3452 CB VAL A 303 -2.593 6.465 -34.088 1.00 19.95 C ANISOU 3452 CB VAL A 303 4349 1603 1627 -99 835 -368 C ATOM 3453 CG1 VAL A 303 -3.328 5.474 -34.982 1.00 20.52 C ANISOU 3453 CG1 VAL A 303 4404 1709 1682 -75 795 -444 C ATOM 3454 CG2 VAL A 303 -1.439 5.789 -33.371 1.00 20.13 C ANISOU 3454 CG2 VAL A 303 4346 1601 1701 -184 903 -289 C ATOM 3455 N LEU A 304 -4.215 8.733 -35.388 1.00 24.06 N ANISOU 3455 N LEU A 304 4999 2110 2034 86 702 -465 N ATOM 3456 CA LEU A 304 -5.299 9.213 -36.239 1.00 22.89 C ANISOU 3456 CA LEU A 304 4893 1969 1836 181 619 -549 C ATOM 3457 C LEU A 304 -4.787 10.176 -37.308 1.00 23.43 C ANISOU 3457 C LEU A 304 5121 1964 1819 238 596 -480 C ATOM 3458 O LEU A 304 -5.188 10.106 -38.474 1.00 24.28 O ANISOU 3458 O LEU A 304 5302 2059 1866 300 537 -511 O ATOM 3459 CB LEU A 304 -6.375 9.899 -35.402 1.00 23.25 C ANISOU 3459 CB LEU A 304 4872 2049 1913 222 586 -636 C ATOM 3460 CG LEU A 304 -7.560 10.395 -36.228 1.00 24.51 C ANISOU 3460 CG LEU A 304 5071 2213 2030 327 491 -735 C ATOM 3461 CD1 LEU A 304 -8.270 9.215 -36.873 1.00 29.64 C ANISOU 3461 CD1 LEU A 304 5667 2909 2688 329 451 -830 C ATOM 3462 CD2 LEU A 304 -8.517 11.216 -35.382 1.00 27.79 C ANISOU 3462 CD2 LEU A 304 5427 2650 2481 371 464 -815 C ATOM 3463 N LEU A 305 -3.891 11.066 -36.898 1.00 23.01 N ANISOU 3463 N LEU A 305 5127 1857 1759 216 644 -387 N ATOM 3464 CA LEU A 305 -3.337 12.080 -37.787 1.00 23.55 C ANISOU 3464 CA LEU A 305 5358 1843 1749 262 636 -314 C ATOM 3465 C LEU A 305 -2.534 11.451 -38.925 1.00 28.88 C ANISOU 3465 C LEU A 305 6112 2476 2384 243 657 -260 C ATOM 3466 O LEU A 305 -2.756 11.754 -40.103 1.00 31.83 O ANISOU 3466 O LEU A 305 6604 2810 2680 312 607 -260 O ATOM 3467 CB LEU A 305 -2.466 13.049 -36.986 1.00 23.03 C ANISOU 3467 CB LEU A 305 5325 1728 1698 222 697 -232 C ATOM 3468 CG LEU A 305 -2.039 14.357 -37.650 1.00 25.33 C ANISOU 3468 CG LEU A 305 5787 1927 1912 272 692 -165 C ATOM 3469 CD1 LEU A 305 -2.063 15.481 -36.630 1.00 25.02 C ANISOU 3469 CD1 LEU A 305 5744 1875 1888 272 707 -150 C ATOM 3470 CD2 LEU A 305 -0.653 14.223 -38.253 1.00 25.21 C ANISOU 3470 CD2 LEU A 305 5859 1834 1885 214 761 -69 C ATOM 3471 N VAL A 306 -1.604 10.574 -38.558 1.00 22.75 N ANISOU 3471 N VAL A 306 5275 1704 1664 153 727 -216 N ATOM 3472 CA VAL A 306 -0.786 9.849 -39.524 1.00 32.93 C ANISOU 3472 CA VAL A 306 6620 2956 2936 127 756 -173 C ATOM 3473 C VAL A 306 -1.674 9.051 -40.475 1.00 34.39 C ANISOU 3473 C VAL A 306 6803 3182 3080 176 690 -249 C ATOM 3474 O VAL A 306 -1.396 8.962 -41.674 1.00 24.08 O ANISOU 3474 O VAL A 306 5603 1833 1714 206 678 -227 O ATOM 3475 CB VAL A 306 0.219 8.913 -38.811 1.00 31.56 C ANISOU 3475 CB VAL A 306 6358 2788 2844 28 832 -133 C ATOM 3476 CG1 VAL A 306 0.790 7.880 -39.772 1.00 31.94 C ANISOU 3476 CG1 VAL A 306 6433 2818 2885 7 850 -120 C ATOM 3477 CG2 VAL A 306 1.334 9.728 -38.172 1.00 31.04 C ANISOU 3477 CG2 VAL A 306 6325 2655 2815 -20 895 -56 C ATOM 3478 N PHE A 307 -2.754 8.491 -39.939 1.00 23.47 N ANISOU 3478 N PHE A 307 5304 1880 1734 185 649 -344 N ATOM 3479 CA PHE A 307 -3.737 7.793 -40.760 1.00 24.26 C ANISOU 3479 CA PHE A 307 5392 2022 1803 233 578 -437 C ATOM 3480 C PHE A 307 -4.316 8.721 -41.827 1.00 26.30 C ANISOU 3480 C PHE A 307 5784 2241 1969 338 496 -454 C ATOM 3481 O PHE A 307 -4.261 8.422 -43.028 1.00 26.73 O ANISOU 3481 O PHE A 307 5928 2270 1960 372 463 -451 O ATOM 3482 CB PHE A 307 -4.861 7.233 -39.887 1.00 24.18 C ANISOU 3482 CB PHE A 307 5235 2094 1858 224 550 -548 C ATOM 3483 CG PHE A 307 -5.779 6.298 -40.613 1.00 24.91 C ANISOU 3483 CG PHE A 307 5293 2231 1940 250 489 -653 C ATOM 3484 CD1 PHE A 307 -5.511 4.941 -40.651 1.00 25.89 C ANISOU 3484 CD1 PHE A 307 5355 2383 2101 186 524 -663 C ATOM 3485 CD2 PHE A 307 -6.907 6.773 -41.263 1.00 26.08 C ANISOU 3485 CD2 PHE A 307 5477 2389 2042 341 391 -744 C ATOM 3486 CE1 PHE A 307 -6.349 4.075 -41.318 1.00 26.22 C ANISOU 3486 CE1 PHE A 307 5367 2463 2134 205 469 -765 C ATOM 3487 CE2 PHE A 307 -7.749 5.911 -41.934 1.00 26.83 C ANISOU 3487 CE2 PHE A 307 5540 2524 2130 361 331 -848 C ATOM 3488 CZ PHE A 307 -7.467 4.560 -41.962 1.00 26.54 C ANISOU 3488 CZ PHE A 307 5437 2516 2130 289 372 -860 C ATOM 3489 N ALA A 308 -4.862 9.846 -41.372 1.00 27.21 N ANISOU 3489 N ALA A 308 5918 2347 2073 393 460 -471 N ATOM 3490 CA ALA A 308 -5.484 10.831 -42.253 1.00 27.03 C ANISOU 3490 CA ALA A 308 6028 2281 1962 506 371 -487 C ATOM 3491 C ALA A 308 -4.539 11.286 -43.361 1.00 27.44 C ANISOU 3491 C ALA A 308 6259 2240 1929 525 390 -384 C ATOM 3492 O ALA A 308 -4.909 11.301 -44.541 1.00 28.50 O ANISOU 3492 O ALA A 308 6500 2346 1983 600 319 -401 O ATOM 3493 CB ALA A 308 -5.960 12.030 -41.444 1.00 27.17 C ANISOU 3493 CB ALA A 308 6044 2290 1989 551 349 -499 C ATOM 3494 N LEU A 309 -3.318 11.648 -42.979 1.00 26.69 N ANISOU 3494 N LEU A 309 6197 2090 1854 457 485 -281 N ATOM 3495 CA LEU A 309 -2.328 12.100 -43.949 1.00 44.13 C ANISOU 3495 CA LEU A 309 8572 4197 3999 461 522 -187 C ATOM 3496 C LEU A 309 -1.954 10.987 -44.925 1.00 44.75 C ANISOU 3496 C LEU A 309 8665 4276 4062 437 534 -188 C ATOM 3497 O LEU A 309 -1.722 11.245 -46.105 1.00 47.23 O ANISOU 3497 O LEU A 309 9129 4519 4298 483 516 -157 O ATOM 3498 CB LEU A 309 -1.078 12.622 -43.239 1.00 44.52 C ANISOU 3498 CB LEU A 309 8631 4188 4097 380 626 -96 C ATOM 3499 CG LEU A 309 -1.251 13.904 -42.419 1.00 45.36 C ANISOU 3499 CG LEU A 309 8762 4271 4203 403 624 -77 C ATOM 3500 CD1 LEU A 309 0.081 14.354 -41.839 1.00 44.72 C ANISOU 3500 CD1 LEU A 309 8699 4121 4171 316 728 8 C ATOM 3501 CD2 LEU A 309 -1.871 15.006 -43.265 1.00 46.35 C ANISOU 3501 CD2 LEU A 309 9057 4332 4223 519 546 -75 C ATOM 3502 N CYS A 310 -1.906 9.752 -44.434 1.00 40.72 N ANISOU 3502 N CYS A 310 8007 3840 3624 367 564 -225 N ATOM 3503 CA CYS A 310 -1.557 8.617 -45.283 1.00 39.40 C ANISOU 3503 CA CYS A 310 7844 3678 3448 340 578 -231 C ATOM 3504 C CYS A 310 -2.618 8.339 -46.344 1.00 27.71 C ANISOU 3504 C CYS A 310 6415 2221 1891 426 475 -308 C ATOM 3505 O CYS A 310 -2.287 8.097 -47.505 1.00 35.40 O ANISOU 3505 O CYS A 310 7496 3151 2804 447 468 -286 O ATOM 3506 CB CYS A 310 -1.328 7.362 -44.439 1.00 25.46 C ANISOU 3506 CB CYS A 310 5914 1983 1777 252 629 -255 C ATOM 3507 SG CYS A 310 0.340 7.223 -43.756 1.00 31.33 S ANISOU 3507 SG CYS A 310 6631 2674 2599 146 752 -155 S ATOM 3508 N TYR A 311 -3.888 8.375 -45.953 1.00 28.04 N ANISOU 3508 N TYR A 311 6381 2331 1943 475 392 -404 N ATOM 3509 CA TYR A 311 -4.963 8.068 -46.896 1.00 29.23 C ANISOU 3509 CA TYR A 311 6566 2509 2033 556 282 -494 C ATOM 3510 C TYR A 311 -5.470 9.286 -47.667 1.00 30.52 C ANISOU 3510 C TYR A 311 6890 2610 2095 677 190 -486 C ATOM 3511 O TYR A 311 -6.336 9.153 -48.530 1.00 31.68 O ANISOU 3511 O TYR A 311 7086 2768 2181 760 84 -555 O ATOM 3512 CB TYR A 311 -6.135 7.406 -46.170 1.00 29.15 C ANISOU 3512 CB TYR A 311 6390 2596 2091 550 233 -622 C ATOM 3513 CG TYR A 311 -5.937 5.933 -45.890 1.00 32.42 C ANISOU 3513 CG TYR A 311 6676 3067 2574 458 286 -658 C ATOM 3514 CD1 TYR A 311 -5.293 5.507 -44.738 1.00 27.14 C ANISOU 3514 CD1 TYR A 311 5897 2420 1995 363 382 -621 C ATOM 3515 CD2 TYR A 311 -6.401 4.968 -46.776 1.00 33.03 C ANISOU 3515 CD2 TYR A 311 6753 3172 2625 469 236 -728 C ATOM 3516 CE1 TYR A 311 -5.112 4.162 -44.476 1.00 26.57 C ANISOU 3516 CE1 TYR A 311 5722 2391 1982 287 426 -647 C ATOM 3517 CE2 TYR A 311 -6.225 3.620 -46.521 1.00 31.62 C ANISOU 3517 CE2 TYR A 311 6467 3038 2508 388 285 -760 C ATOM 3518 CZ TYR A 311 -5.580 3.224 -45.368 1.00 29.38 C ANISOU 3518 CZ TYR A 311 6080 2770 2311 300 380 -717 C ATOM 3519 OH TYR A 311 -5.400 1.886 -45.107 1.00 29.24 O ANISOU 3519 OH TYR A 311 5971 2788 2351 227 424 -743 O ATOM 3520 N LEU A 312 -4.939 10.466 -47.360 1.00 32.60 N ANISOU 3520 N LEU A 312 7242 2805 2342 691 225 -404 N ATOM 3521 CA LEU A 312 -5.363 11.683 -48.057 1.00 33.68 C ANISOU 3521 CA LEU A 312 7549 2868 2379 811 141 -386 C ATOM 3522 C LEU A 312 -5.102 11.668 -49.579 1.00 32.80 C ANISOU 3522 C LEU A 312 7617 2682 2164 868 106 -350 C ATOM 3523 O LEU A 312 -6.033 11.908 -50.356 1.00 36.80 O ANISOU 3523 O LEU A 312 8203 3184 2595 981 -19 -405 O ATOM 3524 CB LEU A 312 -4.697 12.914 -47.430 1.00 33.85 C ANISOU 3524 CB LEU A 312 7639 2817 2404 800 203 -297 C ATOM 3525 CG LEU A 312 -5.039 14.260 -48.072 1.00 34.91 C ANISOU 3525 CG LEU A 312 7968 2860 2437 924 126 -266 C ATOM 3526 CD1 LEU A 312 -6.505 14.607 -47.858 1.00 33.40 C ANISOU 3526 CD1 LEU A 312 7733 2724 2232 1036 -12 -371 C ATOM 3527 CD2 LEU A 312 -4.136 15.358 -47.535 1.00 32.16 C ANISOU 3527 CD2 LEU A 312 7700 2426 2094 888 213 -167 C ATOM 3528 N PRO A 313 -3.854 11.390 -50.019 1.00 32.41 N ANISOU 3528 N PRO A 313 7630 2571 2113 794 211 -265 N ATOM 3529 CA PRO A 313 -3.606 11.490 -51.465 1.00 34.61 C ANISOU 3529 CA PRO A 313 8091 2766 2292 851 184 -232 C ATOM 3530 C PRO A 313 -4.406 10.491 -52.299 1.00 34.40 C ANISOU 3530 C PRO A 313 8041 2802 2226 893 92 -318 C ATOM 3531 O PRO A 313 -4.927 10.851 -53.358 1.00 39.08 O ANISOU 3531 O PRO A 313 8778 3350 2721 998 -6 -334 O ATOM 3532 CB PRO A 313 -2.104 11.201 -51.587 1.00 32.90 C ANISOU 3532 CB PRO A 313 7899 2486 2113 744 327 -147 C ATOM 3533 CG PRO A 313 -1.547 11.451 -50.234 1.00 32.32 C ANISOU 3533 CG PRO A 313 7710 2432 2139 659 414 -114 C ATOM 3534 CD PRO A 313 -2.624 11.018 -49.295 1.00 31.66 C ANISOU 3534 CD PRO A 313 7454 2470 2105 666 350 -200 C ATOM 3535 N ILE A 314 -4.505 9.252 -51.830 1.00 42.31 N ANISOU 3535 N ILE A 314 8870 3902 3305 814 119 -376 N ATOM 3536 CA ILE A 314 -5.228 8.233 -52.580 1.00 41.97 C ANISOU 3536 CA ILE A 314 8795 3917 3234 841 40 -464 C ATOM 3537 C ILE A 314 -6.710 8.584 -52.665 1.00 44.19 C ANISOU 3537 C ILE A 314 9066 4242 3481 954 -116 -568 C ATOM 3538 O ILE A 314 -7.379 8.244 -53.639 1.00 47.37 O ANISOU 3538 O ILE A 314 9525 4655 3818 1025 -219 -629 O ATOM 3539 CB ILE A 314 -5.057 6.827 -51.959 1.00 40.74 C ANISOU 3539 CB ILE A 314 8453 3850 3176 730 106 -511 C ATOM 3540 CG1 ILE A 314 -5.572 5.757 -52.923 1.00 33.96 C ANISOU 3540 CG1 ILE A 314 7594 3031 2280 748 41 -588 C ATOM 3541 CG2 ILE A 314 -5.766 6.728 -50.614 1.00 39.36 C ANISOU 3541 CG2 ILE A 314 8100 3759 3097 701 96 -582 C ATOM 3542 CD1 ILE A 314 -5.007 5.874 -54.324 1.00 34.98 C ANISOU 3542 CD1 ILE A 314 7908 3078 2306 788 39 -530 C ATOM 3543 N SER A 315 -7.214 9.287 -51.656 1.00 34.97 N ANISOU 3543 N SER A 315 7829 3099 2360 975 -137 -592 N ATOM 3544 CA SER A 315 -8.620 9.659 -51.623 1.00 36.00 C ANISOU 3544 CA SER A 315 7933 3272 2475 1085 -285 -699 C ATOM 3545 C SER A 315 -8.891 10.849 -52.530 1.00 37.49 C ANISOU 3545 C SER A 315 8330 3370 2546 1228 -388 -662 C ATOM 3546 O SER A 315 -9.911 10.885 -53.218 1.00 43.85 O ANISOU 3546 O SER A 315 9174 4191 3297 1341 -536 -743 O ATOM 3547 CB SER A 315 -9.063 9.970 -50.194 1.00 37.53 C ANISOU 3547 CB SER A 315 7972 3521 2765 1056 -265 -744 C ATOM 3548 OG SER A 315 -9.111 8.790 -49.411 1.00 34.08 O ANISOU 3548 OG SER A 315 7343 3172 2435 943 -198 -806 O ATOM 3549 N VAL A 316 -7.984 11.823 -52.537 1.00 37.30 N ANISOU 3549 N VAL A 316 8441 3246 2485 1227 -314 -543 N ATOM 3550 CA VAL A 316 -8.169 12.981 -53.402 1.00 61.24 C ANISOU 3550 CA VAL A 316 11692 6173 5403 1362 -401 -500 C ATOM 3551 C VAL A 316 -8.060 12.524 -54.862 1.00 61.56 C ANISOU 3551 C VAL A 316 11870 6168 5352 1403 -446 -493 C ATOM 3552 O VAL A 316 -8.819 12.978 -55.729 1.00 66.20 O ANISOU 3552 O VAL A 316 12585 6719 5850 1542 -586 -527 O ATOM 3553 CB VAL A 316 -7.157 14.125 -53.069 1.00 39.80 C ANISOU 3553 CB VAL A 316 9099 3347 2675 1336 -296 -375 C ATOM 3554 CG1 VAL A 316 -5.744 13.805 -53.540 1.00 37.80 C ANISOU 3554 CG1 VAL A 316 8920 3020 2421 1231 -151 -277 C ATOM 3555 CG2 VAL A 316 -7.628 15.444 -53.656 1.00 41.37 C ANISOU 3555 CG2 VAL A 316 9502 3444 2773 1490 -403 -352 C ATOM 3556 N LEU A 317 -7.164 11.575 -55.120 1.00 56.58 N ANISOU 3556 N LEU A 317 11205 5545 4747 1289 -333 -458 N ATOM 3557 CA LEU A 317 -7.001 11.046 -56.467 1.00 53.40 C ANISOU 3557 CA LEU A 317 10921 5105 4263 1315 -360 -455 C ATOM 3558 C LEU A 317 -8.199 10.205 -56.893 1.00 51.97 C ANISOU 3558 C LEU A 317 10659 5019 4069 1373 -502 -582 C ATOM 3559 O LEU A 317 -8.703 10.365 -58.001 1.00 51.76 O ANISOU 3559 O LEU A 317 10767 4954 3945 1481 -617 -606 O ATOM 3560 CB LEU A 317 -5.717 10.224 -56.573 1.00 39.23 C ANISOU 3560 CB LEU A 317 9099 3297 2509 1178 -202 -392 C ATOM 3561 CG LEU A 317 -4.436 11.060 -56.595 1.00 38.90 C ANISOU 3561 CG LEU A 317 9185 3133 2461 1132 -72 -271 C ATOM 3562 CD1 LEU A 317 -3.227 10.191 -56.904 1.00 38.21 C ANISOU 3562 CD1 LEU A 317 9079 3030 2410 1015 65 -226 C ATOM 3563 CD2 LEU A 317 -4.558 12.199 -57.597 1.00 40.55 C ANISOU 3563 CD2 LEU A 317 9639 3214 2555 1252 -136 -233 C ATOM 3564 N ASN A 318 -8.656 9.316 -56.015 1.00 53.57 N ANISOU 3564 N ASN A 318 10644 5339 4372 1301 -493 -667 N ATOM 3565 CA ASN A 318 -9.808 8.474 -56.324 1.00 59.04 C ANISOU 3565 CA ASN A 318 11240 6122 5071 1340 -620 -803 C ATOM 3566 C ASN A 318 -11.072 9.293 -56.545 1.00 56.78 C ANISOU 3566 C ASN A 318 11000 5838 4738 1500 -804 -879 C ATOM 3567 O ASN A 318 -11.876 8.987 -57.428 1.00 56.86 O ANISOU 3567 O ASN A 318 11044 5866 4692 1587 -942 -958 O ATOM 3568 CB ASN A 318 -10.047 7.451 -55.213 1.00 62.84 C ANISOU 3568 CB ASN A 318 11481 6715 5682 1224 -561 -883 C ATOM 3569 CG ASN A 318 -9.120 6.257 -55.311 1.00 68.76 C ANISOU 3569 CG ASN A 318 12176 7481 6468 1093 -432 -851 C ATOM 3570 OD1 ASN A 318 -8.553 5.984 -56.368 1.00 70.44 O ANISOU 3570 OD1 ASN A 318 12512 7643 6608 1097 -415 -803 O ATOM 3571 ND2 ASN A 318 -8.970 5.532 -54.210 1.00 69.11 N ANISOU 3571 ND2 ASN A 318 12038 7593 6627 980 -342 -880 N ATOM 3572 N ILE A 319 -11.242 10.338 -55.741 1.00 57.33 N ANISOU 3572 N ILE A 319 11066 5886 4830 1544 -811 -857 N ATOM 3573 CA ILE A 319 -12.419 11.182 -55.862 1.00 60.57 C ANISOU 3573 CA ILE A 319 11514 6295 5204 1707 -988 -930 C ATOM 3574 C ILE A 319 -12.307 12.057 -57.112 1.00 65.70 C ANISOU 3574 C ILE A 319 12421 6826 5715 1842 -1072 -863 C ATOM 3575 O ILE A 319 -13.322 12.466 -57.675 1.00 68.84 O ANISOU 3575 O ILE A 319 12876 7221 6058 1995 -1250 -935 O ATOM 3576 CB ILE A 319 -12.635 12.059 -54.599 1.00 45.28 C ANISOU 3576 CB ILE A 319 9499 4370 3335 1717 -968 -930 C ATOM 3577 CG1 ILE A 319 -14.107 12.458 -54.466 1.00 47.56 C ANISOU 3577 CG1 ILE A 319 9722 4711 3636 1861 -1157 -1063 C ATOM 3578 CG2 ILE A 319 -11.728 13.281 -54.604 1.00 45.10 C ANISOU 3578 CG2 ILE A 319 9660 4225 3253 1738 -894 -788 C ATOM 3579 CD1 ILE A 319 -15.033 11.289 -54.201 1.00 48.73 C ANISOU 3579 CD1 ILE A 319 9656 4985 3874 1821 -1214 -1217 C ATOM 3580 N LEU A 320 -11.081 12.323 -57.561 1.00 67.59 N ANISOU 3580 N LEU A 320 12815 6964 5903 1786 -944 -731 N ATOM 3581 CA LEU A 320 -10.897 13.085 -58.796 1.00 70.36 C ANISOU 3581 CA LEU A 320 13423 7187 6125 1899 -1003 -668 C ATOM 3582 C LEU A 320 -10.889 12.210 -60.052 1.00 73.54 C ANISOU 3582 C LEU A 320 13892 7590 6462 1905 -1041 -693 C ATOM 3583 O LEU A 320 -10.962 12.720 -61.169 1.00 76.04 O ANISOU 3583 O LEU A 320 14413 7811 6668 2013 -1117 -668 O ATOM 3584 CB LEU A 320 -9.605 13.899 -58.735 1.00 45.84 C ANISOU 3584 CB LEU A 320 10466 3954 2998 1841 -846 -525 C ATOM 3585 CG LEU A 320 -9.701 15.181 -57.907 1.00 47.72 C ANISOU 3585 CG LEU A 320 10742 4140 3250 1895 -850 -488 C ATOM 3586 CD1 LEU A 320 -8.402 15.964 -57.983 1.00 47.38 C ANISOU 3586 CD1 LEU A 320 10860 3957 3185 1834 -696 -355 C ATOM 3587 CD2 LEU A 320 -10.876 16.029 -58.372 1.00 49.36 C ANISOU 3587 CD2 LEU A 320 11058 4314 3382 2096 -1051 -548 C ATOM 3588 N LYS A 321 -10.832 10.894 -59.866 1.00 69.50 N ANISOU 3588 N LYS A 321 13212 7181 6015 1791 -991 -748 N ATOM 3589 CA LYS A 321 -10.776 9.956 -60.984 1.00 69.80 C ANISOU 3589 CA LYS A 321 13297 7227 5998 1779 -1014 -774 C ATOM 3590 C LYS A 321 -12.123 9.275 -61.230 1.00 71.90 C ANISOU 3590 C LYS A 321 13449 7596 6272 1849 -1189 -925 C ATOM 3591 O LYS A 321 -12.476 8.964 -62.368 1.00 75.55 O ANISOU 3591 O LYS A 321 14009 8045 6653 1918 -1288 -961 O ATOM 3592 CB LYS A 321 -9.697 8.897 -60.732 1.00 71.86 C ANISOU 3592 CB LYS A 321 13465 7519 6321 1604 -834 -731 C ATOM 3593 CG LYS A 321 -9.654 7.783 -61.768 1.00 67.50 C ANISOU 3593 CG LYS A 321 12933 6990 5724 1579 -850 -770 C ATOM 3594 CD LYS A 321 -8.655 6.699 -61.408 1.00 61.86 C ANISOU 3594 CD LYS A 321 12107 6312 5083 1414 -680 -739 C ATOM 3595 CE LYS A 321 -8.606 5.627 -62.485 1.00 56.61 C ANISOU 3595 CE LYS A 321 11477 5664 4368 1396 -697 -777 C ATOM 3596 NZ LYS A 321 -9.954 5.060 -62.766 1.00 56.47 N ANISOU 3596 NZ LYS A 321 11380 5734 4343 1462 -866 -917 N ATOM 3597 N ARG A 322 -12.885 9.071 -60.159 1.00 47.73 N ANISOU 3597 N ARG A 322 10184 4637 3314 1830 -1227 -1018 N ATOM 3598 CA ARG A 322 -14.086 8.242 -60.229 1.00 58.90 C ANISOU 3598 CA ARG A 322 11448 6161 4770 1859 -1364 -1174 C ATOM 3599 C ARG A 322 -15.412 9.005 -60.169 1.00 59.82 C ANISOU 3599 C ARG A 322 11546 6301 4883 2026 -1567 -1274 C ATOM 3600 O ARG A 322 -16.462 8.449 -60.492 1.00 59.91 O ANISOU 3600 O ARG A 322 11464 6388 4911 2080 -1712 -1407 O ATOM 3601 CB ARG A 322 -14.052 7.212 -59.104 1.00 46.82 C ANISOU 3601 CB ARG A 322 9678 4736 3377 1702 -1257 -1235 C ATOM 3602 CG ARG A 322 -12.943 6.188 -59.239 1.00 45.65 C ANISOU 3602 CG ARG A 322 9516 4585 3244 1549 -1089 -1172 C ATOM 3603 CD ARG A 322 -13.145 5.341 -60.481 1.00 65.75 C ANISOU 3603 CD ARG A 322 12123 7139 5720 1567 -1159 -1220 C ATOM 3604 NE ARG A 322 -12.192 4.238 -60.555 1.00 64.43 N ANISOU 3604 NE ARG A 322 11919 6982 5581 1423 -1007 -1181 N ATOM 3605 CZ ARG A 322 -12.201 3.309 -61.504 1.00 64.49 C ANISOU 3605 CZ ARG A 322 11958 7002 5543 1405 -1031 -1220 C ATOM 3606 NH1 ARG A 322 -13.116 3.350 -62.463 1.00 65.13 N ANISOU 3606 NH1 ARG A 322 12109 7089 5549 1520 -1203 -1298 N ATOM 3607 NH2 ARG A 322 -11.296 2.340 -61.495 1.00 62.99 N ANISOU 3607 NH2 ARG A 322 11731 6819 5384 1279 -889 -1184 N ATOM 3608 N VAL A 323 -15.372 10.265 -59.748 1.00 60.08 N ANISOU 3608 N VAL A 323 11660 6270 4899 2108 -1580 -1215 N ATOM 3609 CA VAL A 323 -16.586 11.074 -59.649 1.00 62.77 C ANISOU 3609 CA VAL A 323 11984 6626 5238 2280 -1773 -1307 C ATOM 3610 C VAL A 323 -16.489 12.319 -60.529 1.00 63.99 C ANISOU 3610 C VAL A 323 12402 6647 5263 2443 -1859 -1226 C ATOM 3611 O VAL A 323 -17.216 12.453 -61.513 1.00 66.01 O ANISOU 3611 O VAL A 323 12749 6885 5447 2586 -2031 -1284 O ATOM 3612 CB VAL A 323 -16.862 11.501 -58.196 1.00 62.27 C ANISOU 3612 CB VAL A 323 11758 6616 5286 2251 -1733 -1340 C ATOM 3613 CG1 VAL A 323 -18.155 12.298 -58.115 1.00 64.23 C ANISOU 3613 CG1 VAL A 323 11976 6886 5541 2437 -1940 -1448 C ATOM 3614 CG2 VAL A 323 -16.921 10.285 -57.287 1.00 61.49 C ANISOU 3614 CG2 VAL A 323 11412 6634 5319 2083 -1632 -1418 C ATOM 3615 N PHE A 324 -15.583 13.224 -60.170 1.00 62.03 N ANISOU 3615 N PHE A 324 12278 6300 4989 2420 -1736 -1094 N ATOM 3616 CA PHE A 324 -15.383 14.459 -60.923 1.00 65.26 C ANISOU 3616 CA PHE A 324 12952 6562 5282 2559 -1789 -1009 C ATOM 3617 C PHE A 324 -14.366 14.279 -62.048 1.00 67.33 C ANISOU 3617 C PHE A 324 13416 6718 5446 2511 -1693 -905 C ATOM 3618 O PHE A 324 -13.200 14.643 -61.901 1.00 66.14 O ANISOU 3618 O PHE A 324 13365 6480 5285 2419 -1522 -781 O ATOM 3619 CB PHE A 324 -14.928 15.586 -59.992 1.00 61.71 C ANISOU 3619 CB PHE A 324 12545 6046 4856 2556 -1704 -926 C ATOM 3620 CG PHE A 324 -15.954 15.986 -58.970 1.00 61.59 C ANISOU 3620 CG PHE A 324 12365 6114 4921 2632 -1809 -1026 C ATOM 3621 CD1 PHE A 324 -17.283 16.147 -59.326 1.00 62.31 C ANISOU 3621 CD1 PHE A 324 12423 6249 5004 2806 -2034 -1157 C ATOM 3622 CD2 PHE A 324 -15.588 16.199 -57.651 1.00 61.13 C ANISOU 3622 CD2 PHE A 324 12181 6092 4954 2529 -1684 -998 C ATOM 3623 CE1 PHE A 324 -18.228 16.517 -58.384 1.00 62.28 C ANISOU 3623 CE1 PHE A 324 12255 6323 5084 2878 -2130 -1260 C ATOM 3624 CE2 PHE A 324 -16.526 16.567 -56.705 1.00 60.75 C ANISOU 3624 CE2 PHE A 324 11979 6119 4984 2595 -1773 -1097 C ATOM 3625 CZ PHE A 324 -17.848 16.725 -57.072 1.00 61.57 C ANISOU 3625 CZ PHE A 324 12044 6266 5082 2770 -1996 -1230 C ATOM 3626 N GLY A 325 -14.812 13.720 -63.169 1.00 74.59 N ANISOU 3626 N GLY A 325 14394 7647 6301 2573 -1804 -961 N ATOM 3627 CA GLY A 325 -13.943 13.511 -64.314 1.00 77.60 C ANISOU 3627 CA GLY A 325 14967 7932 6585 2538 -1726 -878 C ATOM 3628 C GLY A 325 -12.867 12.475 -64.049 1.00 77.87 C ANISOU 3628 C GLY A 325 14905 8009 6674 2333 -1525 -824 C ATOM 3629 O GLY A 325 -13.010 11.641 -63.156 1.00 82.06 O ANISOU 3629 O GLY A 325 15206 8662 7312 2227 -1479 -881 O ATOM 3630 N MET A 326 -11.784 12.531 -64.819 1.00116.24 N ANISOU 3630 N MET A 326 20951 11170 12044 1893 -1116 116 N ATOM 3631 CA MET A 326 -10.726 11.531 -64.708 1.00109.72 C ANISOU 3631 CA MET A 326 20016 10131 11544 1715 -931 -225 C ATOM 3632 C MET A 326 -9.400 12.026 -65.296 1.00108.93 C ANISOU 3632 C MET A 326 20055 10165 11170 1693 -696 -29 C ATOM 3633 O MET A 326 -9.316 13.137 -65.819 1.00100.14 O ANISOU 3633 O MET A 326 19152 9296 9601 1808 -642 370 O ATOM 3634 CB MET A 326 -11.161 10.231 -65.404 1.00108.47 C ANISOU 3634 CB MET A 326 19549 10265 11400 1662 -993 -914 C ATOM 3635 CG MET A 326 -10.427 8.975 -64.939 1.00104.89 C ANISOU 3635 CG MET A 326 18963 9425 11464 1490 -816 -1313 C ATOM 3636 SD MET A 326 -10.863 7.464 -65.823 1.00133.73 S ANISOU 3636 SD MET A 326 22271 13402 15139 1395 -804 -2150 S ATOM 3637 CE MET A 326 -12.392 7.010 -65.008 1.00102.52 C ANISOU 3637 CE MET A 326 18182 9183 11588 1363 -961 -2381 C ATOM 3638 N PHE A 327 -8.368 11.194 -65.184 1.00108.20 N ANISOU 3638 N PHE A 327 19851 9883 11377 1553 -524 -315 N ATOM 3639 CA PHE A 327 -7.093 11.427 -65.845 1.00110.18 C ANISOU 3639 CA PHE A 327 20155 10292 11418 1504 -276 -277 C ATOM 3640 C PHE A 327 -6.895 10.400 -66.965 1.00112.35 C ANISOU 3640 C PHE A 327 20221 10964 11502 1469 -218 -833 C ATOM 3641 O PHE A 327 -6.136 9.441 -66.813 1.00103.62 O ANISOU 3641 O PHE A 327 18958 9669 10745 1357 -85 -1176 O ATOM 3642 CB PHE A 327 -5.935 11.353 -64.847 1.00110.19 C ANISOU 3642 CB PHE A 327 20167 9789 11909 1386 -114 -171 C ATOM 3643 CG PHE A 327 -6.100 12.253 -63.650 1.00109.08 C ANISOU 3643 CG PHE A 327 20215 9233 11999 1396 -171 310 C ATOM 3644 CD1 PHE A 327 -5.728 13.587 -63.707 1.00109.62 C ANISOU 3644 CD1 PHE A 327 20508 9328 11815 1400 -36 784 C ATOM 3645 CD2 PHE A 327 -6.611 11.756 -62.462 1.00107.93 C ANISOU 3645 CD2 PHE A 327 20042 8642 12325 1392 -319 277 C ATOM 3646 CE1 PHE A 327 -5.875 14.411 -62.603 1.00107.88 C ANISOU 3646 CE1 PHE A 327 20455 8720 11814 1387 -67 1197 C ATOM 3647 CE2 PHE A 327 -6.760 12.573 -61.357 1.00106.16 C ANISOU 3647 CE2 PHE A 327 20000 8037 12296 1396 -365 703 C ATOM 3648 CZ PHE A 327 -6.391 13.902 -61.427 1.00106.95 C ANISOU 3648 CZ PHE A 327 20299 8190 12149 1386 -249 1154 C ATOM 3649 N ARG A 328 -7.577 10.611 -68.089 1.00114.55 N ANISOU 3649 N ARG A 328 20506 11804 11214 1587 -316 -923 N ATOM 3650 CA ARG A 328 -7.636 9.630 -69.173 1.00117.89 C ANISOU 3650 CA ARG A 328 20721 12662 11412 1560 -308 -1498 C ATOM 3651 C ARG A 328 -7.146 10.183 -70.514 1.00122.57 C ANISOU 3651 C ARG A 328 21459 13784 11329 1648 -162 -1424 C ATOM 3652 O ARG A 328 -6.880 9.422 -71.443 1.00126.42 O ANISOU 3652 O ARG A 328 21808 14606 11619 1601 -81 -1881 O ATOM 3653 CB ARG A 328 -9.071 9.129 -69.324 1.00119.07 C ANISOU 3653 CB ARG A 328 20679 13062 11500 1627 -601 -1836 C ATOM 3654 CG ARG A 328 -10.092 10.217 -69.034 1.00119.09 C ANISOU 3654 CG ARG A 328 20832 13143 11274 1815 -833 -1384 C ATOM 3655 CD ARG A 328 -11.542 9.799 -69.233 1.00121.82 C ANISOU 3655 CD ARG A 328 20944 13798 11544 1896 -1137 -1745 C ATOM 3656 NE ARG A 328 -12.429 10.665 -68.456 1.00120.25 N ANISOU 3656 NE ARG A 328 20858 13412 11421 2024 -1322 -1311 N ATOM 3657 CZ ARG A 328 -12.829 11.874 -68.842 1.00120.81 C ANISOU 3657 CZ ARG A 328 21140 13785 10975 2275 -1432 -838 C ATOM 3658 NH1 ARG A 328 -12.452 12.361 -70.018 1.00123.84 N ANISOU 3658 NH1 ARG A 328 21672 14685 10696 2440 -1374 -733 N ATOM 3659 NH2 ARG A 328 -13.614 12.596 -68.054 1.00118.66 N ANISOU 3659 NH2 ARG A 328 20958 13284 10843 2376 -1572 -462 N ATOM 3660 N GLN A 329 -7.016 11.504 -70.608 1.00122.50 N ANISOU 3660 N GLN A 329 21755 13822 10966 1776 -89 -852 N ATOM 3661 CA GLN A 329 -6.787 12.154 -71.898 1.00126.61 C ANISOU 3661 CA GLN A 329 22493 14854 10759 1924 53 -717 C ATOM 3662 C GLN A 329 -5.312 12.346 -72.252 1.00128.29 C ANISOU 3662 C GLN A 329 22828 14957 10961 1785 474 -649 C ATOM 3663 O GLN A 329 -4.562 12.981 -71.511 1.00125.23 O ANISOU 3663 O GLN A 329 22561 14142 10878 1684 678 -298 O ATOM 3664 CB GLN A 329 -7.502 13.506 -71.929 1.00127.70 C ANISOU 3664 CB GLN A 329 22942 15118 10461 2178 -39 -128 C ATOM 3665 CG GLN A 329 -7.590 14.133 -73.311 1.00133.28 C ANISOU 3665 CG GLN A 329 23908 16416 10316 2430 45 10 C ATOM 3666 CD GLN A 329 -8.671 15.193 -73.396 1.00134.44 C ANISOU 3666 CD GLN A 329 24289 16782 10007 2767 -162 474 C ATOM 3667 OE1 GLN A 329 -9.617 15.194 -72.608 1.00131.47 O ANISOU 3667 OE1 GLN A 329 23776 16259 9916 2814 -461 520 O ATOM 3668 NE2 GLN A 329 -8.536 16.102 -74.354 1.00138.70 N ANISOU 3668 NE2 GLN A 329 25203 17663 9836 3023 22 825 N ATOM 3669 N ALA A 330 -4.921 11.786 -73.396 1.00132.12 N ANISOU 3669 N ALA A 330 23261 15844 11095 1771 608 -1025 N ATOM 3670 CA ALA A 330 -3.605 12.001 -74.003 1.00134.51 C ANISOU 3670 CA ALA A 330 23695 16148 11266 1664 1039 -999 C ATOM 3671 C ALA A 330 -2.435 11.766 -73.050 1.00132.19 C ANISOU 3671 C ALA A 330 23258 15293 11676 1418 1263 -1016 C ATOM 3672 O ALA A 330 -2.488 10.892 -72.185 1.00129.67 O ANISOU 3672 O ALA A 330 22664 14662 11941 1315 1102 -1279 O ATOM 3673 CB ALA A 330 -3.527 13.409 -74.580 1.00136.16 C ANISOU 3673 CB ALA A 330 24340 16524 10871 1841 1255 -442 C ATOM 3674 N SER A 331 -1.381 12.560 -73.220 1.00133.23 N ANISOU 3674 N SER A 331 23580 15302 11738 1342 1652 -746 N ATOM 3675 CA SER A 331 -0.173 12.434 -72.412 1.00130.08 C ANISOU 3675 CA SER A 331 23020 14446 11959 1125 1877 -789 C ATOM 3676 C SER A 331 -0.320 13.132 -71.064 1.00124.98 C ANISOU 3676 C SER A 331 22418 13346 11722 1107 1757 -387 C ATOM 3677 O SER A 331 0.579 13.847 -70.621 1.00124.77 O ANISOU 3677 O SER A 331 22453 13044 11909 985 2026 -162 O ATOM 3678 CB SER A 331 1.034 13.000 -73.161 1.00132.93 C ANISOU 3678 CB SER A 331 23529 14868 12110 1017 2380 -730 C ATOM 3679 OG SER A 331 2.199 12.950 -72.357 1.00130.81 O ANISOU 3679 OG SER A 331 23059 14192 12449 817 2580 -795 O ATOM 3680 N ASP A 332 -1.461 12.923 -70.421 1.00122.29 N ANISOU 3680 N ASP A 332 22037 12934 11495 1215 1368 -329 N ATOM 3681 CA ASP A 332 -1.689 13.426 -69.074 1.00117.84 C ANISOU 3681 CA ASP A 332 21501 11923 11348 1198 1223 1 C ATOM 3682 C ASP A 332 -1.705 12.235 -68.119 1.00115.81 C ANISOU 3682 C ASP A 332 20942 11352 11710 1138 1002 -347 C ATOM 3683 O ASP A 332 -2.348 12.258 -67.071 1.00111.12 O ANISOU 3683 O ASP A 332 20348 10453 11419 1175 765 -194 O ATOM 3684 CB ASP A 332 -2.997 14.211 -69.004 1.00117.21 C ANISOU 3684 CB ASP A 332 21651 11949 10932 1384 993 388 C ATOM 3685 CG ASP A 332 -3.181 14.929 -67.681 1.00112.79 C ANISOU 3685 CG ASP A 332 21182 10926 10747 1355 912 786 C ATOM 3686 OD1 ASP A 332 -2.167 15.351 -67.088 1.00111.45 O ANISOU 3686 OD1 ASP A 332 21018 10443 10886 1203 1138 911 O ATOM 3687 OD2 ASP A 332 -4.339 15.055 -67.229 1.00111.17 O ANISOU 3687 OD2 ASP A 332 21022 10680 10536 1477 623 940 O ATOM 3688 N ARG A 333 -0.970 11.194 -68.492 1.00119.30 N ANISOU 3688 N ARG A 333 21151 11846 12330 1058 1117 -808 N ATOM 3689 CA ARG A 333 -1.047 9.918 -67.796 1.00119.10 C ANISOU 3689 CA ARG A 333 20872 11562 12819 1045 953 -1183 C ATOM 3690 C ARG A 333 0.271 9.534 -67.114 1.00114.96 C ANISOU 3690 C ARG A 333 20169 10703 12809 965 1113 -1311 C ATOM 3691 O ARG A 333 0.267 8.842 -66.098 1.00111.57 O ANISOU 3691 O ARG A 333 19619 9910 12863 1006 970 -1417 O ATOM 3692 CB ARG A 333 -1.476 8.832 -68.787 1.00127.86 C ANISOU 3692 CB ARG A 333 21834 13016 13729 1055 927 -1686 C ATOM 3693 CG ARG A 333 -2.078 7.595 -68.157 1.00131.42 C ANISOU 3693 CG ARG A 333 22095 13225 14612 1067 745 -2045 C ATOM 3694 CD ARG A 333 -3.361 7.889 -67.390 1.00133.76 C ANISOU 3694 CD ARG A 333 22486 13362 14976 1146 454 -1819 C ATOM 3695 NE ARG A 333 -3.551 6.974 -66.263 1.00135.78 N ANISOU 3695 NE ARG A 333 22636 13131 15823 1148 371 -1989 N ATOM 3696 CZ ARG A 333 -4.217 5.824 -66.324 1.00137.99 C ANISOU 3696 CZ ARG A 333 22768 13376 16287 1132 327 -2438 C ATOM 3697 NH1 ARG A 333 -4.769 5.431 -67.464 1.00143.43 N ANISOU 3697 NH1 ARG A 333 23350 14531 16616 1097 319 -2805 N ATOM 3698 NH2 ARG A 333 -4.331 5.065 -65.242 1.00134.76 N ANISOU 3698 NH2 ARG A 333 22329 12459 16414 1154 314 -2536 N ATOM 3699 N GLU A 334 1.391 9.999 -67.664 1.00114.60 N ANISOU 3699 N GLU A 334 20112 10777 12652 871 1419 -1301 N ATOM 3700 CA GLU A 334 2.715 9.587 -67.194 1.00113.45 C ANISOU 3700 CA GLU A 334 19733 10406 12968 806 1580 -1506 C ATOM 3701 C GLU A 334 3.023 9.996 -65.751 1.00110.50 C ANISOU 3701 C GLU A 334 19333 9615 13039 829 1447 -1259 C ATOM 3702 O GLU A 334 3.570 9.203 -64.984 1.00111.22 O ANISOU 3702 O GLU A 334 19215 9449 13593 892 1371 -1473 O ATOM 3703 CB GLU A 334 3.793 10.142 -68.127 1.00116.50 C ANISOU 3703 CB GLU A 334 20116 11022 13126 675 1974 -1546 C ATOM 3704 CG GLU A 334 3.716 9.592 -69.541 1.00120.68 C ANISOU 3704 CG GLU A 334 20650 11955 13247 657 2140 -1860 C ATOM 3705 CD GLU A 334 4.799 10.144 -70.445 1.00124.85 C ANISOU 3705 CD GLU A 334 21211 12670 13558 524 2580 -1896 C ATOM 3706 OE1 GLU A 334 5.639 10.930 -69.957 1.00123.86 O ANISOU 3706 OE1 GLU A 334 21067 12351 13645 426 2771 -1713 O ATOM 3707 OE2 GLU A 334 4.811 9.791 -71.643 1.00128.74 O ANISOU 3707 OE2 GLU A 334 21746 13500 13669 507 2755 -2131 O ATOM 3708 N ALA A 335 2.682 11.226 -65.383 1.00 75.14 N ANISOU 3708 N ALA A 335 16164 7840 4546 -275 536 -279 N ATOM 3709 CA ALA A 335 2.916 11.697 -64.019 1.00 72.93 C ANISOU 3709 CA ALA A 335 16059 7106 4544 -523 626 -244 C ATOM 3710 C ALA A 335 1.802 11.226 -63.087 1.00 71.47 C ANISOU 3710 C ALA A 335 15744 6878 4532 -522 372 -352 C ATOM 3711 O ALA A 335 2.003 11.062 -61.877 1.00 69.78 O ANISOU 3711 O ALA A 335 15517 6414 4580 -713 342 -432 O ATOM 3712 CB ALA A 335 3.033 13.213 -63.991 1.00 70.11 C ANISOU 3712 CB ALA A 335 16044 6464 4130 -470 1008 94 C ATOM 3713 N VAL A 336 0.626 11.004 -63.665 1.00 67.22 N ANISOU 3713 N VAL A 336 15067 6652 3822 -277 206 -376 N ATOM 3714 CA VAL A 336 -0.534 10.544 -62.911 1.00 70.54 C ANISOU 3714 CA VAL A 336 15357 7061 4385 -278 4 -515 C ATOM 3715 C VAL A 336 -0.297 9.145 -62.337 1.00 69.71 C ANISOU 3715 C VAL A 336 15031 6863 4591 -502 -98 -832 C ATOM 3716 O VAL A 336 -0.628 8.881 -61.176 1.00 67.80 O ANISOU 3716 O VAL A 336 14783 6367 4609 -602 -126 -844 O ATOM 3717 CB VAL A 336 -1.804 10.557 -63.790 1.00 72.81 C ANISOU 3717 CB VAL A 336 15465 7832 4367 37 -136 -581 C ATOM 3718 CG1 VAL A 336 -2.894 9.684 -63.191 1.00 71.59 C ANISOU 3718 CG1 VAL A 336 15086 7725 4389 -49 -330 -909 C ATOM 3719 CG2 VAL A 336 -2.297 11.984 -63.967 1.00 70.47 C ANISOU 3719 CG2 VAL A 336 15372 7548 3854 346 6 -166 C ATOM 3720 N TYR A 337 0.288 8.260 -63.143 1.00 70.52 N ANISOU 3720 N TYR A 337 14954 7167 4674 -543 -103 -1057 N ATOM 3721 CA TYR A 337 0.691 6.942 -62.658 1.00 69.06 C ANISOU 3721 CA TYR A 337 14595 6831 4813 -713 -88 -1301 C ATOM 3722 C TYR A 337 1.622 7.078 -61.463 1.00 65.97 C ANISOU 3722 C TYR A 337 14324 6113 4628 -818 12 -1112 C ATOM 3723 O TYR A 337 1.491 6.346 -60.493 1.00 64.28 O ANISOU 3723 O TYR A 337 14062 5704 4659 -846 46 -1156 O ATOM 3724 CB TYR A 337 1.386 6.126 -63.751 1.00 65.52 C ANISOU 3724 CB TYR A 337 13968 6627 4299 -734 -66 -1549 C ATOM 3725 CG TYR A 337 0.464 5.285 -64.604 1.00 84.48 C ANISOU 3725 CG TYR A 337 16073 9365 6660 -696 -147 -1985 C ATOM 3726 CD1 TYR A 337 -0.107 5.804 -65.752 1.00 85.44 C ANISOU 3726 CD1 TYR A 337 16086 10013 6364 -484 -258 -2065 C ATOM 3727 CD2 TYR A 337 0.181 3.963 -64.274 1.00 86.26 C ANISOU 3727 CD2 TYR A 337 16095 9418 7264 -845 -60 -2352 C ATOM 3728 CE1 TYR A 337 -0.938 5.043 -66.540 1.00 89.40 C ANISOU 3728 CE1 TYR A 337 16215 10964 6788 -443 -344 -2587 C ATOM 3729 CE2 TYR A 337 -0.657 3.192 -65.066 1.00 89.72 C ANISOU 3729 CE2 TYR A 337 16185 10174 7731 -867 -85 -2890 C ATOM 3730 CZ TYR A 337 -1.213 3.744 -66.199 1.00 90.73 C ANISOU 3730 CZ TYR A 337 16146 10931 7398 -674 -261 -3053 C ATOM 3731 OH TYR A 337 -2.049 3.005 -67.004 1.00 94.24 O ANISOU 3731 OH TYR A 337 16152 11839 7818 -673 -311 -3702 O ATOM 3732 N ALA A 338 2.558 8.019 -61.539 1.00 61.49 N ANISOU 3732 N ALA A 338 13901 5523 3937 -852 100 -935 N ATOM 3733 CA ALA A 338 3.518 8.235 -60.461 1.00 60.17 C ANISOU 3733 CA ALA A 338 13751 5200 3911 -947 189 -871 C ATOM 3734 C ALA A 338 2.812 8.683 -59.184 1.00 59.51 C ANISOU 3734 C ALA A 338 13724 4943 3946 -926 157 -766 C ATOM 3735 O ALA A 338 3.137 8.216 -58.084 1.00 58.85 O ANISOU 3735 O ALA A 338 13552 4816 3993 -901 167 -790 O ATOM 3736 CB ALA A 338 4.564 9.256 -60.879 1.00 61.22 C ANISOU 3736 CB ALA A 338 14007 5346 3906 -1048 350 -815 C ATOM 3737 N CYS A 339 1.843 9.583 -59.337 1.00 59.85 N ANISOU 3737 N CYS A 339 13928 4923 3889 -881 130 -646 N ATOM 3738 CA CYS A 339 1.024 10.019 -58.209 1.00 57.99 C ANISOU 3738 CA CYS A 339 13743 4534 3756 -852 84 -556 C ATOM 3739 C CYS A 339 0.292 8.843 -57.573 1.00 57.06 C ANISOU 3739 C CYS A 339 13478 4388 3815 -788 -9 -634 C ATOM 3740 O CYS A 339 0.237 8.719 -56.347 1.00 61.97 O ANISOU 3740 O CYS A 339 14076 4912 4558 -753 2 -589 O ATOM 3741 CB CYS A 339 0.010 11.082 -58.647 1.00 58.95 C ANISOU 3741 CB CYS A 339 14085 4617 3697 -757 82 -411 C ATOM 3742 SG CYS A 339 0.699 12.706 -59.035 1.00 68.16 S ANISOU 3742 SG CYS A 339 15593 5627 4680 -807 383 -241 S ATOM 3743 N PHE A 340 -0.267 7.977 -58.413 1.00 58.05 N ANISOU 3743 N PHE A 340 13505 4607 3943 -766 -53 -794 N ATOM 3744 CA PHE A 340 -1.023 6.831 -57.920 1.00 58.11 C ANISOU 3744 CA PHE A 340 13394 4503 4183 -753 -27 -939 C ATOM 3745 C PHE A 340 -0.133 5.802 -57.223 1.00 57.92 C ANISOU 3745 C PHE A 340 13353 4323 4332 -728 136 -955 C ATOM 3746 O PHE A 340 -0.509 5.257 -56.185 1.00 57.74 O ANISOU 3746 O PHE A 340 13357 4090 4492 -643 247 -904 O ATOM 3747 CB PHE A 340 -1.798 6.173 -59.063 1.00 60.17 C ANISOU 3747 CB PHE A 340 13481 4943 4438 -780 -64 -1247 C ATOM 3748 CG PHE A 340 -3.177 6.738 -59.258 1.00 60.94 C ANISOU 3748 CG PHE A 340 13551 5190 4415 -716 -198 -1309 C ATOM 3749 CD1 PHE A 340 -3.383 7.842 -60.068 1.00 61.86 C ANISOU 3749 CD1 PHE A 340 13763 5584 4158 -579 -315 -1191 C ATOM 3750 CD2 PHE A 340 -4.267 6.167 -58.623 1.00 61.27 C ANISOU 3750 CD2 PHE A 340 13472 5102 4707 -754 -161 -1468 C ATOM 3751 CE1 PHE A 340 -4.652 8.363 -60.244 1.00 63.06 C ANISOU 3751 CE1 PHE A 340 13880 5952 4130 -434 -435 -1228 C ATOM 3752 CE2 PHE A 340 -5.537 6.682 -58.795 1.00 62.25 C ANISOU 3752 CE2 PHE A 340 13540 5425 4686 -683 -299 -1569 C ATOM 3753 CZ PHE A 340 -5.730 7.782 -59.606 1.00 63.13 C ANISOU 3753 CZ PHE A 340 13739 5884 4362 -500 -458 -1448 C ATOM 3754 N THR A 341 1.043 5.544 -57.787 1.00 58.37 N ANISOU 3754 N THR A 341 13393 4483 4303 -752 182 -1009 N ATOM 3755 CA THR A 341 1.991 4.615 -57.182 1.00 58.71 C ANISOU 3755 CA THR A 341 13478 4415 4415 -651 353 -1025 C ATOM 3756 C THR A 341 2.446 5.140 -55.829 1.00 64.45 C ANISOU 3756 C THR A 341 14310 5148 5031 -509 360 -864 C ATOM 3757 O THR A 341 2.519 4.385 -54.852 1.00 65.55 O ANISOU 3757 O THR A 341 14409 5206 5289 -278 519 -742 O ATOM 3758 CB THR A 341 3.232 4.377 -58.071 1.00 59.44 C ANISOU 3758 CB THR A 341 13511 4687 4385 -696 374 -1126 C ATOM 3759 OG1 THR A 341 3.921 5.616 -58.281 1.00 58.80 O ANISOU 3759 OG1 THR A 341 13406 4819 4115 -775 271 -1031 O ATOM 3760 CG2 THR A 341 2.835 3.783 -59.412 1.00 60.87 C ANISOU 3760 CG2 THR A 341 13557 4935 4634 -802 368 -1355 C ATOM 3761 N PHE A 342 2.746 6.436 -55.768 1.00 27.81 N ANISOU 3761 N PHE A 342 4275 3645 2647 478 594 -1106 N ATOM 3762 CA PHE A 342 3.148 7.030 -54.500 1.00 27.48 C ANISOU 3762 CA PHE A 342 4221 3605 2614 443 594 -1155 C ATOM 3763 C PHE A 342 2.033 6.931 -53.468 1.00 27.19 C ANISOU 3763 C PHE A 342 4203 3553 2575 438 557 -1129 C ATOM 3764 O PHE A 342 2.275 6.534 -52.330 1.00 27.03 O ANISOU 3764 O PHE A 342 4188 3524 2557 401 540 -1148 O ATOM 3765 CB PHE A 342 3.554 8.493 -54.662 1.00 28.66 C ANISOU 3765 CB PHE A 342 4350 3770 2769 435 643 -1207 C ATOM 3766 CG PHE A 342 3.798 9.185 -53.352 1.00 29.66 C ANISOU 3766 CG PHE A 342 4473 3882 2915 370 650 -1246 C ATOM 3767 CD1 PHE A 342 4.945 8.920 -52.622 1.00 31.22 C ANISOU 3767 CD1 PHE A 342 4641 4092 3128 298 654 -1287 C ATOM 3768 CD2 PHE A 342 2.870 10.075 -52.836 1.00 30.33 C ANISOU 3768 CD2 PHE A 342 4573 3954 2998 383 650 -1247 C ATOM 3769 CE1 PHE A 342 5.170 9.541 -51.409 1.00 31.94 C ANISOU 3769 CE1 PHE A 342 4723 4181 3233 233 658 -1328 C ATOM 3770 CE2 PHE A 342 3.089 10.700 -51.623 1.00 30.98 C ANISOU 3770 CE2 PHE A 342 4662 4014 3095 323 658 -1281 C ATOM 3771 CZ PHE A 342 4.241 10.432 -50.909 1.00 31.75 C ANISOU 3771 CZ PHE A 342 4733 4121 3208 244 661 -1322 C ATOM 3772 N SER A 343 0.818 7.298 -53.868 1.00 26.61 N ANISOU 3772 N SER A 343 4132 3491 2489 479 549 -1091 N ATOM 3773 CA SER A 343 -0.333 7.255 -52.970 1.00 21.25 C ANISOU 3773 CA SER A 343 3476 2802 1796 474 530 -1062 C ATOM 3774 C SER A 343 -0.557 5.849 -52.419 1.00 30.54 C ANISOU 3774 C SER A 343 4685 3947 2971 413 516 -1046 C ATOM 3775 O SER A 343 -0.781 5.668 -51.216 1.00 31.05 O ANISOU 3775 O SER A 343 4753 4008 3036 385 495 -1055 O ATOM 3776 CB SER A 343 -1.593 7.745 -53.688 1.00 32.85 C ANISOU 3776 CB SER A 343 4946 4297 3237 529 539 -1019 C ATOM 3777 OG SER A 343 -1.484 9.117 -54.030 1.00 33.76 O ANISOU 3777 OG SER A 343 4915 4533 3379 562 529 -1106 O ATOM 3778 N HIS A 344 -0.486 4.859 -53.304 1.00 20.79 N ANISOU 3778 N HIS A 344 3463 2704 1733 394 523 -1033 N ATOM 3779 CA HIS A 344 -0.599 3.462 -52.903 1.00 20.62 C ANISOU 3779 CA HIS A 344 3455 2675 1705 349 497 -1038 C ATOM 3780 C HIS A 344 0.460 3.126 -51.859 1.00 21.45 C ANISOU 3780 C HIS A 344 3551 2775 1824 338 478 -1069 C ATOM 3781 O HIS A 344 0.137 2.661 -50.751 1.00 21.15 O ANISOU 3781 O HIS A 344 3520 2736 1780 315 453 -1073 O ATOM 3782 CB HIS A 344 -0.465 2.538 -54.117 1.00 36.44 C ANISOU 3782 CB HIS A 344 5474 4671 3701 338 509 -1031 C ATOM 3783 CG HIS A 344 -1.568 2.692 -55.118 1.00 35.24 C ANISOU 3783 CG HIS A 344 5327 4535 3528 329 534 -1013 C ATOM 3784 ND1 HIS A 344 -1.416 2.365 -56.449 1.00 35.86 N ANISOU 3784 ND1 HIS A 344 5408 4614 3603 321 563 -1011 N ATOM 3785 CD2 HIS A 344 -2.838 3.137 -54.983 1.00 34.00 C ANISOU 3785 CD2 HIS A 344 5164 4407 3348 317 545 -1003 C ATOM 3786 CE1 HIS A 344 -2.546 2.603 -57.089 1.00 34.46 C ANISOU 3786 CE1 HIS A 344 5223 4471 3401 305 586 -1006 C ATOM 3787 NE2 HIS A 344 -3.426 3.072 -56.224 1.00 33.41 N ANISOU 3787 NE2 HIS A 344 5082 4358 3252 303 578 -1001 N ATOM 3788 N TRP A 345 1.720 3.388 -52.206 1.00 20.91 N ANISOU 3788 N TRP A 345 3464 2713 1767 353 497 -1095 N ATOM 3789 CA TRP A 345 2.821 3.109 -51.291 1.00 21.12 C ANISOU 3789 CA TRP A 345 3473 2754 1795 338 492 -1136 C ATOM 3790 C TRP A 345 2.587 3.734 -49.925 1.00 26.47 C ANISOU 3790 C TRP A 345 4141 3442 2475 325 474 -1154 C ATOM 3791 O TRP A 345 2.864 3.113 -48.909 1.00 26.80 O ANISOU 3791 O TRP A 345 4181 3492 2509 307 458 -1171 O ATOM 3792 CB TRP A 345 4.159 3.609 -51.834 1.00 21.53 C ANISOU 3792 CB TRP A 345 3494 2836 1849 353 524 -1177 C ATOM 3793 CG TRP A 345 5.242 3.431 -50.811 1.00 21.99 C ANISOU 3793 CG TRP A 345 3505 2942 1909 331 516 -1225 C ATOM 3794 CD1 TRP A 345 5.987 2.310 -50.600 1.00 23.27 C ANISOU 3794 CD1 TRP A 345 3655 3130 2057 337 512 -1239 C ATOM 3795 CD2 TRP A 345 5.667 4.385 -49.827 1.00 22.18 C ANISOU 3795 CD2 TRP A 345 3477 3004 1947 299 511 -1267 C ATOM 3796 NE1 TRP A 345 6.860 2.511 -49.560 1.00 23.77 N ANISOU 3796 NE1 TRP A 345 3651 3262 2119 325 499 -1286 N ATOM 3797 CE2 TRP A 345 6.684 3.777 -49.067 1.00 24.69 C ANISOU 3797 CE2 TRP A 345 3741 3385 2254 290 499 -1306 C ATOM 3798 CE3 TRP A 345 5.291 5.697 -49.521 1.00 22.27 C ANISOU 3798 CE3 TRP A 345 3483 3004 1973 276 521 -1281 C ATOM 3799 CZ2 TRP A 345 7.331 4.433 -48.022 1.00 26.38 C ANISOU 3799 CZ2 TRP A 345 3889 3662 2472 249 493 -1361 C ATOM 3800 CZ3 TRP A 345 5.934 6.347 -48.482 1.00 22.72 C ANISOU 3800 CZ3 TRP A 345 3490 3104 2040 224 522 -1335 C ATOM 3801 CH2 TRP A 345 6.943 5.714 -47.746 1.00 26.63 C ANISOU 3801 CH2 TRP A 345 3923 3671 2524 206 506 -1377 C ATOM 3802 N LEU A 346 2.093 4.967 -49.915 1.00 21.12 N ANISOU 3802 N LEU A 346 3458 2764 1803 338 482 -1153 N ATOM 3803 CA LEU A 346 1.818 5.684 -48.676 1.00 21.18 C ANISOU 3803 CA LEU A 346 3462 2775 1811 325 471 -1172 C ATOM 3804 C LEU A 346 0.771 4.947 -47.850 1.00 26.35 C ANISOU 3804 C LEU A 346 4136 3419 2455 311 442 -1139 C ATOM 3805 O LEU A 346 0.948 4.723 -46.638 1.00 27.13 O ANISOU 3805 O LEU A 346 4232 3527 2551 290 426 -1159 O ATOM 3806 CB LEU A 346 1.350 7.107 -48.981 1.00 22.56 C ANISOU 3806 CB LEU A 346 3636 2946 1988 351 491 -1174 C ATOM 3807 CG LEU A 346 1.249 8.060 -47.793 1.00 24.87 C ANISOU 3807 CG LEU A 346 3931 3238 2280 337 489 -1208 C ATOM 3808 CD1 LEU A 346 2.599 8.186 -47.109 1.00 24.17 C ANISOU 3808 CD1 LEU A 346 3799 3171 2213 273 495 -1265 C ATOM 3809 CD2 LEU A 346 0.749 9.420 -48.247 1.00 24.28 C ANISOU 3809 CD2 LEU A 346 3858 3163 2204 372 515 -1215 C ATOM 3810 N VAL A 347 -0.316 4.571 -48.522 1.00 24.63 N ANISOU 3810 N VAL A 347 3936 3192 2228 318 442 -1096 N ATOM 3811 CA VAL A 347 -1.385 3.800 -47.896 1.00 22.95 C ANISOU 3811 CA VAL A 347 3739 2984 1998 293 421 -1076 C ATOM 3812 C VAL A 347 -0.823 2.576 -47.191 1.00 20.42 C ANISOU 3812 C VAL A 347 3426 2659 1674 269 399 -1090 C ATOM 3813 O VAL A 347 -1.181 2.289 -46.049 1.00 27.37 O ANISOU 3813 O VAL A 347 4310 3545 2544 252 381 -1093 O ATOM 3814 CB VAL A 347 -2.441 3.351 -48.922 1.00 20.32 C ANISOU 3814 CB VAL A 347 3418 2659 1643 291 428 -1048 C ATOM 3815 CG1 VAL A 347 -3.385 2.327 -48.306 1.00 20.27 C ANISOU 3815 CG1 VAL A 347 3425 2670 1608 263 398 -1044 C ATOM 3816 CG2 VAL A 347 -3.211 4.547 -49.438 1.00 23.57 C ANISOU 3816 CG2 VAL A 347 3829 3081 2047 312 464 -1029 C ATOM 3817 N TYR A 348 0.078 1.867 -47.863 1.00 26.99 N ANISOU 3817 N TYR A 348 4264 3482 2510 271 407 -1098 N ATOM 3818 CA TYR A 348 0.688 0.697 -47.237 1.00 26.41 C ANISOU 3818 CA TYR A 348 4204 3403 2426 254 402 -1112 C ATOM 3819 C TYR A 348 1.695 1.081 -46.154 1.00 25.67 C ANISOU 3819 C TYR A 348 4080 3339 2334 259 403 -1153 C ATOM 3820 O TYR A 348 1.947 0.310 -45.227 1.00 25.27 O ANISOU 3820 O TYR A 348 4034 3299 2268 250 397 -1168 O ATOM 3821 CB TYR A 348 1.351 -0.183 -48.295 1.00 20.92 C ANISOU 3821 CB TYR A 348 3525 2694 1730 253 424 -1114 C ATOM 3822 CG TYR A 348 0.347 -0.758 -49.258 1.00 20.82 C ANISOU 3822 CG TYR A 348 3550 2658 1704 241 418 -1082 C ATOM 3823 CD1 TYR A 348 -0.519 -1.762 -48.863 1.00 23.74 C ANISOU 3823 CD1 TYR A 348 3964 3010 2046 218 397 -1068 C ATOM 3824 CD2 TYR A 348 0.250 -0.287 -50.557 1.00 20.76 C ANISOU 3824 CD2 TYR A 348 3534 2651 1701 261 431 -1071 C ATOM 3825 CE1 TYR A 348 -1.446 -2.286 -49.736 1.00 24.01 C ANISOU 3825 CE1 TYR A 348 4032 3040 2049 242 364 -1049 C ATOM 3826 CE2 TYR A 348 -0.681 -0.802 -51.435 1.00 20.77 C ANISOU 3826 CE2 TYR A 348 3564 2648 1679 260 419 -1052 C ATOM 3827 CZ TYR A 348 -1.527 -1.805 -51.017 1.00 22.97 C ANISOU 3827 CZ TYR A 348 3882 2921 1922 258 377 -1045 C ATOM 3828 OH TYR A 348 -2.459 -2.337 -51.878 1.00 24.82 O ANISOU 3828 OH TYR A 348 4126 3184 2120 290 335 -1045 O ATOM 3829 N ALA A 349 2.250 2.283 -46.264 1.00 21.06 N ANISOU 3829 N ALA A 349 3465 2774 1762 272 413 -1179 N ATOM 3830 CA ALA A 349 3.268 2.755 -45.335 1.00 21.78 C ANISOU 3830 CA ALA A 349 3498 2915 1862 265 406 -1224 C ATOM 3831 C ALA A 349 2.651 3.067 -43.985 1.00 22.95 C ANISOU 3831 C ALA A 349 3646 3068 2007 250 385 -1225 C ATOM 3832 O ALA A 349 3.333 3.026 -42.962 1.00 23.73 O ANISOU 3832 O ALA A 349 3701 3214 2101 243 371 -1259 O ATOM 3833 CB ALA A 349 3.978 3.980 -45.892 1.00 21.72 C ANISOU 3833 CB ALA A 349 3447 2931 1875 259 425 -1256 C ATOM 3834 N ASN A 350 1.361 3.390 -43.987 1.00 23.43 N ANISOU 3834 N ASN A 350 3748 3093 2064 249 382 -1191 N ATOM 3835 CA ASN A 350 0.629 3.569 -42.732 1.00 24.31 C ANISOU 3835 CA ASN A 350 3864 3209 2165 237 366 -1186 C ATOM 3836 C ASN A 350 0.728 2.336 -41.826 1.00 25.05 C ANISOU 3836 C ASN A 350 3961 3317 2239 228 350 -1189 C ATOM 3837 O ASN A 350 0.947 2.445 -40.605 1.00 21.20 O ANISOU 3837 O ASN A 350 3447 2861 1747 223 335 -1209 O ATOM 3838 CB ASN A 350 -0.839 3.888 -43.018 1.00 20.63 C ANISOU 3838 CB ASN A 350 3426 2721 1692 241 369 -1145 C ATOM 3839 CG ASN A 350 -1.623 4.194 -41.759 1.00 31.01 C ANISOU 3839 CG ASN A 350 4743 4046 2993 231 359 -1142 C ATOM 3840 OD1 ASN A 350 -1.562 5.304 -41.229 1.00 31.86 O ANISOU 3840 OD1 ASN A 350 4848 4153 3103 238 366 -1159 O ATOM 3841 ND2 ASN A 350 -2.372 3.209 -41.274 1.00 29.40 N ANISOU 3841 ND2 ASN A 350 4550 3852 2769 215 343 -1124 N ATOM 3842 N SER A 351 0.578 1.166 -42.445 1.00 25.48 N ANISOU 3842 N SER A 351 4051 3350 2279 227 356 -1170 N ATOM 3843 CA SER A 351 0.633 -0.117 -41.751 1.00 26.73 C ANISOU 3843 CA SER A 351 4229 3513 2414 217 353 -1173 C ATOM 3844 C SER A 351 1.970 -0.327 -41.050 1.00 26.35 C ANISOU 3844 C SER A 351 4135 3518 2358 243 351 -1216 C ATOM 3845 O SER A 351 2.042 -0.990 -40.016 1.00 27.72 O ANISOU 3845 O SER A 351 4305 3717 2509 252 342 -1227 O ATOM 3846 CB SER A 351 0.376 -1.262 -42.733 1.00 28.15 C ANISOU 3846 CB SER A 351 4448 3658 2590 199 367 -1150 C ATOM 3847 OG SER A 351 -0.920 -1.167 -43.300 1.00 29.40 O ANISOU 3847 OG SER A 351 4634 3792 2745 188 353 -1110 O ATOM 3848 N ALA A 352 3.028 0.233 -41.625 1.00 24.92 N ANISOU 3848 N ALA A 352 3905 3369 2194 264 353 -1240 N ATOM 3849 CA ALA A 352 4.343 0.180 -41.007 1.00 25.62 C ANISOU 3849 CA ALA A 352 3921 3542 2272 297 340 -1285 C ATOM 3850 C ALA A 352 4.478 1.288 -39.972 1.00 26.51 C ANISOU 3850 C ALA A 352 3977 3702 2394 280 319 -1314 C ATOM 3851 O ALA A 352 5.228 1.164 -39.004 1.00 27.30 O ANISOU 3851 O ALA A 352 4017 3883 2472 303 299 -1351 O ATOM 3852 CB ALA A 352 5.433 0.297 -42.059 1.00 25.35 C ANISOU 3852 CB ALA A 352 3848 3543 2243 318 354 -1307 C ATOM 3853 N ALA A 353 3.732 2.368 -40.180 1.00 26.26 N ANISOU 3853 N ALA A 353 3965 3625 2388 246 326 -1300 N ATOM 3854 CA ALA A 353 3.843 3.556 -39.344 1.00 22.41 C ANISOU 3854 CA ALA A 353 3438 3167 1911 220 317 -1334 C ATOM 3855 C ALA A 353 3.284 3.329 -37.947 1.00 25.34 C ANISOU 3855 C ALA A 353 3812 3551 2263 223 295 -1329 C ATOM 3856 O ALA A 353 3.928 3.681 -36.958 1.00 25.64 O ANISOU 3856 O ALA A 353 3792 3657 2291 218 278 -1374 O ATOM 3857 CB ALA A 353 3.141 4.733 -40.003 1.00 22.15 C ANISOU 3857 CB ALA A 353 3442 3074 1901 199 337 -1318 C ATOM 3858 N ASN A 354 2.090 2.746 -37.865 1.00 24.37 N ANISOU 3858 N ASN A 354 3752 3376 2132 226 296 -1280 N ATOM 3859 CA ASN A 354 1.431 2.567 -36.566 1.00 24.05 C ANISOU 3859 CA ASN A 354 3717 3349 2073 225 279 -1274 C ATOM 3860 C ASN A 354 2.280 1.868 -35.482 1.00 25.35 C ANISOU 3860 C ASN A 354 3833 3589 2210 255 257 -1306 C ATOM 3861 O ASN A 354 2.364 2.375 -34.358 1.00 26.57 O ANISOU 3861 O ASN A 354 3951 3789 2356 255 239 -1330 O ATOM 3862 CB ASN A 354 0.107 1.817 -36.747 1.00 21.53 C ANISOU 3862 CB ASN A 354 3463 2980 1738 216 287 -1226 C ATOM 3863 CG ASN A 354 -0.939 2.651 -37.454 1.00 24.61 C ANISOU 3863 CG ASN A 354 3884 3327 2141 202 300 -1197 C ATOM 3864 OD1 ASN A 354 -0.956 3.877 -37.333 1.00 24.32 O ANISOU 3864 OD1 ASN A 354 3835 3288 2118 202 305 -1209 O ATOM 3865 ND2 ASN A 354 -1.819 1.992 -38.199 1.00 24.27 N ANISOU 3865 ND2 ASN A 354 3884 3253 2083 195 308 -1165 N ATOM 3866 N PRO A 355 2.914 0.719 -35.803 1.00 28.01 N ANISOU 3866 N PRO A 355 4172 3946 2526 291 260 -1307 N ATOM 3867 CA PRO A 355 3.746 0.096 -34.763 1.00 28.80 C ANISOU 3867 CA PRO A 355 4222 4134 2586 346 237 -1336 C ATOM 3868 C PRO A 355 4.885 0.997 -34.288 1.00 23.90 C ANISOU 3868 C PRO A 355 3501 3616 1965 351 216 -1396 C ATOM 3869 O PRO A 355 5.235 0.976 -33.107 1.00 28.11 O ANISOU 3869 O PRO A 355 3982 4230 2468 380 190 -1423 O ATOM 3870 CB PRO A 355 4.301 -1.152 -35.458 1.00 23.59 C ANISOU 3870 CB PRO A 355 3588 3475 1902 396 250 -1328 C ATOM 3871 CG PRO A 355 3.318 -1.454 -36.528 1.00 28.43 C ANISOU 3871 CG PRO A 355 4285 3982 2536 347 281 -1289 C ATOM 3872 CD PRO A 355 2.861 -0.116 -37.018 1.00 27.43 C ANISOU 3872 CD PRO A 355 4149 3822 2452 295 284 -1283 C ATOM 3873 N ILE A 356 5.448 1.782 -35.202 1.00 25.47 N ANISOU 3873 N ILE A 356 3669 3819 2191 317 229 -1421 N ATOM 3874 CA ILE A 356 6.513 2.718 -34.860 1.00 27.38 C ANISOU 3874 CA ILE A 356 3811 4163 2430 291 218 -1491 C ATOM 3875 C ILE A 356 5.989 3.799 -33.916 1.00 28.31 C ANISOU 3875 C ILE A 356 3927 4270 2561 240 212 -1510 C ATOM 3876 O ILE A 356 6.636 4.139 -32.916 1.00 28.83 O ANISOU 3876 O ILE A 356 3916 4437 2602 234 190 -1566 O ATOM 3877 CB ILE A 356 7.110 3.369 -36.123 1.00 27.51 C ANISOU 3877 CB ILE A 356 3805 4174 2472 250 244 -1516 C ATOM 3878 CG1 ILE A 356 7.577 2.288 -37.101 1.00 28.40 C ANISOU 3878 CG1 ILE A 356 3929 4293 2569 308 253 -1493 C ATOM 3879 CG2 ILE A 356 8.257 4.298 -35.756 1.00 25.60 C ANISOU 3879 CG2 ILE A 356 3453 4054 2219 200 241 -1603 C ATOM 3880 CD1 ILE A 356 8.097 2.827 -38.414 1.00 29.08 C ANISOU 3880 CD1 ILE A 356 3998 4373 2680 275 281 -1511 C ATOM 3881 N ILE A 357 4.810 4.324 -34.238 1.00 28.11 N ANISOU 3881 N ILE A 357 3985 4129 2565 209 230 -1466 N ATOM 3882 CA ILE A 357 4.141 5.301 -33.387 1.00 27.65 C ANISOU 3882 CA ILE A 357 3949 4045 2513 177 228 -1473 C ATOM 3883 C ILE A 357 3.967 4.750 -31.978 1.00 29.74 C ANISOU 3883 C ILE A 357 4190 4365 2745 210 198 -1474 C ATOM 3884 O ILE A 357 4.327 5.406 -31.000 1.00 30.22 O ANISOU 3884 O ILE A 357 4204 4485 2792 191 184 -1522 O ATOM 3885 CB ILE A 357 2.761 5.699 -33.944 1.00 27.27 C ANISOU 3885 CB ILE A 357 3996 3881 2484 171 250 -1412 C ATOM 3886 CG1 ILE A 357 2.908 6.388 -35.301 1.00 25.91 C ANISOU 3886 CG1 ILE A 357 3848 3658 2339 150 280 -1412 C ATOM 3887 CG2 ILE A 357 2.041 6.613 -32.966 1.00 27.88 C ANISOU 3887 CG2 ILE A 357 4100 3938 2554 157 249 -1417 C ATOM 3888 CD1 ILE A 357 1.588 6.811 -35.914 1.00 25.12 C ANISOU 3888 CD1 ILE A 357 3831 3467 2245 163 300 -1356 C ATOM 3889 N TYR A 358 3.421 3.539 -31.887 1.00 29.46 N ANISOU 3889 N TYR A 358 4190 4311 2693 257 192 -1425 N ATOM 3890 CA TYR A 358 3.262 2.861 -30.603 1.00 29.02 C ANISOU 3890 CA TYR A 358 4117 4309 2599 300 168 -1422 C ATOM 3891 C TYR A 358 4.593 2.739 -29.874 1.00 24.93 C ANISOU 3891 C TYR A 358 3499 3926 2046 337 139 -1482 C ATOM 3892 O TYR A 358 4.667 2.911 -28.658 1.00 25.35 O ANISOU 3892 O TYR A 358 3512 4047 2073 353 116 -1507 O ATOM 3893 CB TYR A 358 2.663 1.468 -30.791 1.00 23.74 C ANISOU 3893 CB TYR A 358 3509 3600 1911 339 175 -1370 C ATOM 3894 CG TYR A 358 1.326 1.445 -31.488 1.00 33.21 C ANISOU 3894 CG TYR A 358 4791 4696 3132 298 201 -1318 C ATOM 3895 CD1 TYR A 358 0.410 2.473 -31.318 1.00 32.92 C ANISOU 3895 CD1 TYR A 358 4773 4621 3114 260 207 -1307 C ATOM 3896 CD2 TYR A 358 0.979 0.388 -32.318 1.00 34.64 C ANISOU 3896 CD2 TYR A 358 5030 4827 3306 300 220 -1285 C ATOM 3897 CE1 TYR A 358 -0.815 2.449 -31.958 1.00 32.79 C ANISOU 3897 CE1 TYR A 358 4816 4538 3105 236 227 -1262 C ATOM 3898 CE2 TYR A 358 -0.240 0.355 -32.962 1.00 33.54 C ANISOU 3898 CE2 TYR A 358 4953 4616 3177 258 241 -1246 C ATOM 3899 CZ TYR A 358 -1.134 1.386 -32.778 1.00 35.74 C ANISOU 3899 CZ TYR A 358 5233 4876 3469 232 241 -1234 C ATOM 3900 OH TYR A 358 -2.351 1.354 -33.419 1.00 39.46 O ANISOU 3900 OH TYR A 358 5752 5303 3939 205 256 -1198 O ATOM 3901 N ASN A 359 5.645 2.437 -30.629 1.00 25.28 N ANISOU 3901 N ASN A 359 3498 4025 2083 356 141 -1507 N ATOM 3902 CA ASN A 359 6.964 2.240 -30.046 1.00 34.91 C ANISOU 3902 CA ASN A 359 4606 5404 3255 403 114 -1566 C ATOM 3903 C ASN A 359 7.578 3.534 -29.531 1.00 37.29 C ANISOU 3903 C ASN A 359 4821 5789 3561 330 106 -1644 C ATOM 3904 O ASN A 359 8.453 3.509 -28.672 1.00 38.08 O ANISOU 3904 O ASN A 359 4817 6039 3614 357 78 -1698 O ATOM 3905 CB ASN A 359 7.909 1.593 -31.059 1.00 26.55 C ANISOU 3905 CB ASN A 359 3516 4393 2180 447 121 -1572 C ATOM 3906 CG ASN A 359 9.316 1.426 -30.516 1.00 35.04 C ANISOU 3906 CG ASN A 359 4458 5664 3193 505 92 -1633 C ATOM 3907 OD1 ASN A 359 9.619 0.447 -29.833 1.00 35.77 O ANISOU 3907 OD1 ASN A 359 4532 5834 3224 614 68 -1616 O ATOM 3908 ND2 ASN A 359 10.180 2.391 -30.807 1.00 28.29 N ANISOU 3908 ND2 ASN A 359 3505 4900 2343 431 96 -1706 N ATOM 3909 N PHE A 360 7.133 4.670 -30.053 1.00 37.77 N ANISOU 3909 N PHE A 360 4925 5757 3670 239 134 -1652 N ATOM 3910 CA PHE A 360 7.674 5.937 -29.571 1.00 39.91 C ANISOU 3910 CA PHE A 360 5135 6087 3941 155 137 -1731 C ATOM 3911 C PHE A 360 6.799 6.602 -28.510 1.00 38.22 C ANISOU 3911 C PHE A 360 4971 5821 3731 133 131 -1725 C ATOM 3912 O PHE A 360 7.293 7.391 -27.705 1.00 39.72 O ANISOU 3912 O PHE A 360 5105 6085 3902 82 124 -1795 O ATOM 3913 CB PHE A 360 7.894 6.902 -30.736 1.00 41.79 C ANISOU 3913 CB PHE A 360 5396 6264 4220 68 177 -1756 C ATOM 3914 CG PHE A 360 9.225 6.739 -31.411 1.00 45.16 C ANISOU 3914 CG PHE A 360 5718 6813 4629 50 183 -1813 C ATOM 3915 CD1 PHE A 360 10.358 7.343 -30.890 1.00 48.52 C ANISOU 3915 CD1 PHE A 360 6020 7394 5021 -18 180 -1912 C ATOM 3916 CD2 PHE A 360 9.345 5.982 -32.563 1.00 44.92 C ANISOU 3916 CD2 PHE A 360 5707 6754 4607 97 194 -1771 C ATOM 3917 CE1 PHE A 360 11.585 7.196 -31.506 1.00 49.89 C ANISOU 3917 CE1 PHE A 360 6081 7707 5167 -39 187 -1967 C ATOM 3918 CE2 PHE A 360 10.570 5.831 -33.185 1.00 46.78 C ANISOU 3918 CE2 PHE A 360 5841 7114 4818 89 200 -1823 C ATOM 3919 CZ PHE A 360 11.692 6.439 -32.655 1.00 49.06 C ANISOU 3919 CZ PHE A 360 5998 7572 5071 21 196 -1921 C ATOM 3920 N LEU A 361 5.510 6.279 -28.494 1.00 37.39 N ANISOU 3920 N LEU A 361 4967 5598 3642 168 136 -1647 N ATOM 3921 CA LEU A 361 4.574 7.021 -27.655 1.00 32.50 C ANISOU 3921 CA LEU A 361 4405 4920 3024 149 138 -1637 C ATOM 3922 C LEU A 361 3.799 6.171 -26.646 1.00 32.54 C ANISOU 3922 C LEU A 361 4424 4937 3004 216 115 -1591 C ATOM 3923 O LEU A 361 2.852 6.656 -26.027 1.00 32.82 O ANISOU 3923 O LEU A 361 4513 4920 3038 210 119 -1570 O ATOM 3924 CB LEU A 361 3.588 7.781 -28.543 1.00 28.32 C ANISOU 3924 CB LEU A 361 3983 4246 2530 120 175 -1594 C ATOM 3925 CG LEU A 361 4.218 8.819 -29.474 1.00 26.09 C ANISOU 3925 CG LEU A 361 3707 3936 2271 53 206 -1640 C ATOM 3926 CD1 LEU A 361 3.166 9.449 -30.372 1.00 25.38 C ANISOU 3926 CD1 LEU A 361 3729 3711 2205 57 240 -1587 C ATOM 3927 CD2 LEU A 361 4.958 9.883 -28.676 1.00 27.04 C ANISOU 3927 CD2 LEU A 361 3785 4115 2375 -16 206 -1729 C ATOM 3928 N SER A 362 4.196 4.915 -26.473 1.00 25.98 N ANISOU 3928 N SER A 362 3552 4176 2145 284 93 -1575 N ATOM 3929 CA SER A 362 3.574 4.062 -25.462 1.00 34.10 C ANISOU 3929 CA SER A 362 4593 5224 3141 349 74 -1537 C ATOM 3930 C SER A 362 4.619 3.270 -24.688 1.00 34.92 C ANISOU 3930 C SER A 362 4606 5473 3189 426 39 -1569 C ATOM 3931 O SER A 362 5.274 2.393 -25.246 1.00 34.77 O ANISOU 3931 O SER A 362 4568 5491 3151 478 37 -1561 O ATOM 3932 CB SER A 362 2.566 3.107 -26.101 1.00 25.10 C ANISOU 3932 CB SER A 362 3538 3987 2010 370 93 -1461 C ATOM 3933 OG SER A 362 2.004 2.246 -25.126 1.00 26.28 O ANISOU 3933 OG SER A 362 3703 4161 2122 426 79 -1430 O ATOM 3934 N GLY A 363 4.760 3.577 -23.401 1.00 33.69 N ANISOU 3934 N GLY A 363 4397 5404 3000 443 13 -1603 N ATOM 3935 CA GLY A 363 5.773 2.958 -22.564 1.00 34.02 C ANISOU 3935 CA GLY A 363 4339 5608 2978 527 -22 -1637 C ATOM 3936 C GLY A 363 5.708 1.443 -22.512 1.00 34.21 C ANISOU 3936 C GLY A 363 4396 5643 2960 644 -28 -1577 C ATOM 3937 O GLY A 363 6.732 0.761 -22.618 1.00 36.27 O ANISOU 3937 O GLY A 363 4597 6011 3173 724 -43 -1590 O ATOM 3938 N LYS A 364 4.498 0.917 -22.358 1.00 64.53 N ANISOU 3938 N LYS A 364 10945 8595 4979 -111 -1905 -2967 N ATOM 3939 CA LYS A 364 4.294 -0.521 -22.249 1.00 65.97 C ANISOU 3939 CA LYS A 364 11170 8903 4994 186 -2200 -2504 C ATOM 3940 C LYS A 364 4.663 -1.237 -23.549 1.00 63.96 C ANISOU 3940 C LYS A 364 10897 8375 5032 348 -2307 -2330 C ATOM 3941 O LYS A 364 5.285 -2.307 -23.531 1.00 66.09 O ANISOU 3941 O LYS A 364 11062 8796 5254 577 -2631 -2167 O ATOM 3942 CB LYS A 364 2.845 -0.816 -21.859 1.00 64.15 C ANISOU 3942 CB LYS A 364 11217 8594 4564 301 -2107 -2121 C ATOM 3943 CG LYS A 364 2.457 -0.253 -20.499 1.00 65.46 C ANISOU 3943 CG LYS A 364 11360 9163 4347 232 -2026 -2283 C ATOM 3944 CD LYS A 364 1.010 -0.556 -20.144 1.00 66.68 C ANISOU 3944 CD LYS A 364 11721 9356 4258 370 -1924 -1836 C ATOM 3945 CE LYS A 364 0.637 0.066 -18.805 1.00 70.94 C ANISOU 3945 CE LYS A 364 12193 10389 4374 344 -1815 -2047 C ATOM 3946 NZ LYS A 364 -0.801 -0.134 -18.474 1.00 70.90 N ANISOU 3946 NZ LYS A 364 12306 10525 4110 487 -1669 -1583 N ATOM 3947 N PHE A 365 4.291 -0.636 -24.676 1.00 60.51 N ANISOU 3947 N PHE A 365 10545 7555 4890 256 -2029 -2372 N ATOM 3948 CA PHE A 365 4.656 -1.181 -25.978 1.00 55.66 C ANISOU 3948 CA PHE A 365 9858 6768 4523 398 -2084 -2276 C ATOM 3949 C PHE A 365 6.166 -1.138 -26.182 1.00 58.14 C ANISOU 3949 C PHE A 365 9800 7407 4885 408 -2262 -2571 C ATOM 3950 O PHE A 365 6.731 -2.039 -26.793 1.00 58.18 O ANISOU 3950 O PHE A 365 9679 7486 4941 685 -2462 -2483 O ATOM 3951 CB PHE A 365 3.948 -0.430 -27.108 1.00 53.63 C ANISOU 3951 CB PHE A 365 9647 6157 4572 254 -1680 -2194 C ATOM 3952 CG PHE A 365 2.550 -0.913 -27.373 1.00 49.90 C ANISOU 3952 CG PHE A 365 9463 5422 4076 337 -1569 -1771 C ATOM 3953 CD1 PHE A 365 2.330 -2.127 -28.004 1.00 48.56 C ANISOU 3953 CD1 PHE A 365 9376 5142 3931 540 -1780 -1494 C ATOM 3954 CD2 PHE A 365 1.457 -0.152 -26.997 1.00 49.27 C ANISOU 3954 CD2 PHE A 365 9564 5214 3941 214 -1266 -1660 C ATOM 3955 CE1 PHE A 365 1.046 -2.574 -28.249 1.00 46.56 C ANISOU 3955 CE1 PHE A 365 9367 4675 3647 536 -1715 -1085 C ATOM 3956 CE2 PHE A 365 0.170 -0.593 -27.240 1.00 47.10 C ANISOU 3956 CE2 PHE A 365 9493 4800 3604 268 -1169 -1212 C ATOM 3957 CZ PHE A 365 -0.036 -1.805 -27.867 1.00 45.70 C ANISOU 3957 CZ PHE A 365 9381 4533 3451 386 -1405 -910 C ATOM 3958 N ARG A 366 6.814 -0.092 -25.674 1.00 60.81 N ANISOU 3958 N ARG A 366 9957 7951 5196 111 -2198 -2930 N ATOM 3959 CA ARG A 366 8.271 -0.010 -25.718 1.00 63.97 C ANISOU 3959 CA ARG A 366 9948 8782 5578 58 -2396 -3171 C ATOM 3960 C ARG A 366 8.876 -1.190 -24.974 1.00 70.60 C ANISOU 3960 C ARG A 366 10679 10016 6131 376 -2774 -3038 C ATOM 3961 O ARG A 366 9.708 -1.925 -25.519 1.00 70.76 O ANISOU 3961 O ARG A 366 10468 10259 6160 673 -2984 -2996 O ATOM 3962 CB ARG A 366 8.772 1.300 -25.107 1.00 78.68 C ANISOU 3962 CB ARG A 366 11679 10779 7438 -401 -2317 -3578 C ATOM 3963 CG ARG A 366 8.286 2.545 -25.815 1.00 77.91 C ANISOU 3963 CG ARG A 366 11660 10220 7723 -731 -1931 -3659 C ATOM 3964 CD ARG A 366 9.083 3.772 -25.410 1.00 83.01 C ANISOU 3964 CD ARG A 366 12122 10954 8464 -1219 -1933 -4077 C ATOM 3965 NE ARG A 366 8.753 4.240 -24.067 1.00 87.49 N ANISOU 3965 NE ARG A 366 12954 11485 8803 -1348 -1945 -4287 N ATOM 3966 CZ ARG A 366 8.057 5.342 -23.809 1.00 90.18 C ANISOU 3966 CZ ARG A 366 13583 11349 9332 -1525 -1700 -4452 C ATOM 3967 NH1 ARG A 366 7.617 6.098 -24.806 1.00 89.54 N ANISOU 3967 NH1 ARG A 366 13544 10776 9700 -1668 -1396 -4427 N ATOM 3968 NH2 ARG A 366 7.806 5.694 -22.555 1.00 94.49 N ANISOU 3968 NH2 ARG A 366 14344 11933 9624 -1524 -1752 -4630 N ATOM 3969 N GLU A 367 8.442 -1.361 -23.727 1.00 73.34 N ANISOU 3969 N GLU A 367 11162 10478 6225 341 -2836 -2942 N ATOM 3970 CA GLU A 367 8.897 -2.467 -22.890 1.00 77.22 C ANISOU 3970 CA GLU A 367 11548 11333 6458 622 -3175 -2717 C ATOM 3971 C GLU A 367 8.751 -3.809 -23.600 1.00 76.61 C ANISOU 3971 C GLU A 367 11595 11004 6511 1091 -3378 -2379 C ATOM 3972 O GLU A 367 9.688 -4.611 -23.636 1.00 79.83 O ANISOU 3972 O GLU A 367 11785 11666 6879 1410 -3648 -2317 O ATOM 3973 CB GLU A 367 8.120 -2.495 -21.572 1.00 79.42 C ANISOU 3973 CB GLU A 367 11988 11747 6441 531 -3177 -2573 C ATOM 3974 CG GLU A 367 8.297 -1.257 -20.711 1.00 83.18 C ANISOU 3974 CG GLU A 367 12384 12478 6742 111 -3018 -2960 C ATOM 3975 CD GLU A 367 7.439 -1.295 -19.460 1.00 84.63 C ANISOU 3975 CD GLU A 367 12716 12860 6579 80 -2999 -2833 C ATOM 3976 OE1 GLU A 367 6.676 -2.269 -19.290 1.00 82.76 O ANISOU 3976 OE1 GLU A 367 12610 12582 6254 348 -3108 -2382 O ATOM 3977 OE2 GLU A 367 7.529 -0.351 -18.645 1.00 88.27 O ANISOU 3977 OE2 GLU A 367 13175 13506 6857 -212 -2894 -3166 O ATOM 3978 N GLN A 368 7.577 -4.045 -24.177 1.00 72.59 N ANISOU 3978 N GLN A 368 11439 9981 6159 1137 -3248 -2165 N ATOM 3979 CA GLN A 368 7.309 -5.320 -24.833 1.00 64.21 C ANISOU 3979 CA GLN A 368 10576 8576 5244 1520 -3460 -1868 C ATOM 3980 C GLN A 368 8.101 -5.504 -26.129 1.00 63.98 C ANISOU 3980 C GLN A 368 10379 8518 5412 1761 -3483 -2083 C ATOM 3981 O GLN A 368 8.467 -6.625 -26.482 1.00 65.60 O ANISOU 3981 O GLN A 368 10623 8621 5682 2191 -3757 -1981 O ATOM 3982 CB GLN A 368 5.814 -5.463 -25.112 1.00 62.15 C ANISOU 3982 CB GLN A 368 10712 7831 5072 1417 -3317 -1569 C ATOM 3983 CG GLN A 368 4.972 -5.638 -23.859 1.00 63.32 C ANISOU 3983 CG GLN A 368 10996 8074 4990 1299 -3356 -1234 C ATOM 3984 CD GLN A 368 5.361 -6.869 -23.062 1.00 67.15 C ANISOU 3984 CD GLN A 368 11423 8695 5397 1553 -3728 -901 C ATOM 3985 OE1 GLN A 368 5.774 -7.884 -23.624 1.00 68.32 O ANISOU 3985 OE1 GLN A 368 11626 8581 5752 1865 -3970 -796 O ATOM 3986 NE2 GLN A 368 5.233 -6.784 -21.743 1.00 69.76 N ANISOU 3986 NE2 GLN A 368 11624 9448 5432 1436 -3760 -738 N ATOM 3987 N PHE A 369 8.365 -4.407 -26.833 1.00 63.97 N ANISOU 3987 N PHE A 369 10170 8614 5523 1501 -3184 -2362 N ATOM 3988 CA PHE A 369 9.139 -4.467 -28.070 1.00 62.84 C ANISOU 3988 CA PHE A 369 9740 8595 5542 1692 -3130 -2517 C ATOM 3989 C PHE A 369 10.604 -4.750 -27.767 1.00 69.63 C ANISOU 3989 C PHE A 369 10179 10035 6243 1934 -3384 -2665 C ATOM 3990 O PHE A 369 11.304 -5.371 -28.568 1.00 70.71 O ANISOU 3990 O PHE A 369 10111 10333 6422 2341 -3484 -2718 O ATOM 3991 CB PHE A 369 9.009 -3.166 -28.868 1.00 61.02 C ANISOU 3991 CB PHE A 369 9338 8356 5492 1295 -2732 -2658 C ATOM 3992 CG PHE A 369 7.651 -2.958 -29.483 1.00 57.05 C ANISOU 3992 CG PHE A 369 9160 7356 5158 1155 -2454 -2470 C ATOM 3993 CD1 PHE A 369 6.701 -3.966 -29.471 1.00 55.32 C ANISOU 3993 CD1 PHE A 369 9332 6765 4924 1362 -2585 -2217 C ATOM 3994 CD2 PHE A 369 7.328 -1.750 -30.078 1.00 55.16 C ANISOU 3994 CD2 PHE A 369 8817 7036 5107 797 -2075 -2500 C ATOM 3995 CE1 PHE A 369 5.454 -3.769 -30.037 1.00 52.67 C ANISOU 3995 CE1 PHE A 369 9243 6067 4701 1202 -2339 -2008 C ATOM 3996 CE2 PHE A 369 6.085 -1.548 -30.646 1.00 51.89 C ANISOU 3996 CE2 PHE A 369 8653 6241 4823 695 -1807 -2277 C ATOM 3997 CZ PHE A 369 5.147 -2.558 -30.625 1.00 50.26 C ANISOU 3997 CZ PHE A 369 8802 5751 4545 893 -1937 -2037 C ATOM 3998 N LYS A 370 11.067 -4.284 -26.611 1.00 72.87 N ANISOU 3998 N LYS A 370 10436 10820 6432 1701 -3485 -2745 N ATOM 3999 CA LYS A 370 12.420 -4.593 -26.165 1.00 74.23 C ANISOU 3999 CA LYS A 370 10176 11624 6405 1906 -3740 -2809 C ATOM 4000 C LYS A 370 12.517 -6.049 -25.719 1.00 76.48 C ANISOU 4000 C LYS A 370 10593 11833 6631 2455 -4052 -2519 C ATOM 4001 O LYS A 370 13.413 -6.779 -26.141 1.00 79.42 O ANISOU 4001 O LYS A 370 10723 12451 7001 2937 -4222 -2514 O ATOM 4002 CB LYS A 370 12.846 -3.668 -25.023 1.00 76.76 C ANISOU 4002 CB LYS A 370 10284 12355 6527 1415 -3713 -2942 C ATOM 4003 CG LYS A 370 13.013 -2.208 -25.413 1.00 80.30 C ANISOU 4003 CG LYS A 370 10554 12877 7080 860 -3471 -3260 C ATOM 4004 CD LYS A 370 13.385 -1.362 -24.203 1.00 83.72 C ANISOU 4004 CD LYS A 370 10869 13612 7330 369 -3483 -3431 C ATOM 4005 CE LYS A 370 13.415 0.120 -24.543 1.00 83.09 C ANISOU 4005 CE LYS A 370 10716 13414 7442 -224 -3260 -3753 C ATOM 4006 NZ LYS A 370 13.613 0.962 -23.330 1.00 85.50 N ANISOU 4006 NZ LYS A 370 11042 13841 7602 -693 -3271 -3962 N ATOM 4007 N ALA A 371 11.579 -6.463 -24.871 1.00 76.90 N ANISOU 4007 N ALA A 371 11017 11553 6650 2394 -4120 -2251 N ATOM 4008 CA ALA A 371 11.595 -7.803 -24.288 1.00 80.10 C ANISOU 4008 CA ALA A 371 11555 11840 7038 2826 -4430 -1891 C ATOM 4009 C ALA A 371 11.453 -8.907 -25.334 1.00 80.53 C ANISOU 4009 C ALA A 371 11859 11377 7363 3352 -4576 -1820 C ATOM 4010 O ALA A 371 11.868 -10.044 -25.106 1.00 85.64 O ANISOU 4010 O ALA A 371 12529 11933 8077 3812 -4833 -1607 O ATOM 4011 CB ALA A 371 10.495 -7.931 -23.244 1.00 78.99 C ANISOU 4011 CB ALA A 371 11720 11486 6807 2572 -4438 -1563 C ATOM 4012 N ALA A 372 10.875 -8.566 -26.481 1.00 76.74 N ANISOU 4012 N ALA A 372 11562 10549 7047 3276 -4396 -2010 N ATOM 4013 CA ALA A 372 10.654 -9.536 -27.550 1.00 76.86 C ANISOU 4013 CA ALA A 372 11840 10072 7290 3728 -4528 -2030 C ATOM 4014 C ALA A 372 11.962 -9.986 -28.200 1.00 80.85 C ANISOU 4014 C ALA A 372 11982 10954 7784 4300 -4638 -2270 C ATOM 4015 O ALA A 372 11.967 -10.883 -29.042 1.00 82.21 O ANISOU 4015 O ALA A 372 12341 10769 8128 4786 -4765 -2363 O ATOM 4016 CB ALA A 372 9.721 -8.953 -28.600 1.00 70.18 C ANISOU 4016 CB ALA A 372 11177 8881 6607 3410 -4193 -2147 C ATOM 4017 N PHE A 373 13.066 -9.360 -27.804 1.00 83.02 N ANISOU 4017 N PHE A 373 11725 11970 7850 4230 -4573 -2378 N ATOM 4018 CA PHE A 373 14.373 -9.675 -28.367 1.00 85.20 C ANISOU 4018 CA PHE A 373 11546 12768 8060 4737 -4615 -2554 C ATOM 4019 C PHE A 373 15.325 -10.207 -27.302 1.00 90.45 C ANISOU 4019 C PHE A 373 11942 13843 8583 4976 -4798 -2341 C ATOM 4020 O PHE A 373 16.520 -9.911 -27.319 1.00 93.80 O ANISOU 4020 O PHE A 373 11815 15003 8824 5077 -4750 -2427 O ATOM 4021 CB PHE A 373 14.970 -8.438 -29.038 1.00 84.04 C ANISOU 4021 CB PHE A 373 10885 13260 7785 4407 -4346 -2814 C ATOM 4022 CG PHE A 373 14.120 -7.881 -30.143 1.00 83.27 C ANISOU 4022 CG PHE A 373 10965 12810 7864 4130 -4052 -2950 C ATOM 4023 CD1 PHE A 373 13.424 -8.726 -30.992 1.00 81.79 C ANISOU 4023 CD1 PHE A 373 11175 12041 7860 4487 -4081 -2993 C ATOM 4024 CD2 PHE A 373 14.007 -6.513 -30.327 1.00 81.30 C ANISOU 4024 CD2 PHE A 373 10484 12780 7624 3482 -3734 -3015 C ATOM 4025 CE1 PHE A 373 12.638 -8.218 -32.008 1.00 74.71 C ANISOU 4025 CE1 PHE A 373 10390 10903 7094 4207 -3785 -3076 C ATOM 4026 CE2 PHE A 373 13.221 -5.998 -31.341 1.00 77.46 C ANISOU 4026 CE2 PHE A 373 10121 11992 7320 3234 -3428 -3054 C ATOM 4027 CZ PHE A 373 12.536 -6.852 -32.182 1.00 75.68 C ANISOU 4027 CZ PHE A 373 10239 11299 7216 3598 -3446 -3073 C TER 4028 PHE A 373 HETATM 4029 C1 SUV A2001 -8.067 -1.538 -55.027 1.00 33.62 C HETATM 4030 N1 SUV A2001 -9.182 -0.881 -54.761 1.00 36.05 N HETATM 4031 O1 SUV A2001 -7.428 -2.060 -53.948 1.00 32.52 O HETATM 4032 CL1 SUV A2001 -3.028 -4.353 -56.970 1.00 48.82 CL HETATM 4033 N2 SUV A2001 -7.501 -1.752 -56.177 1.00 32.61 N HETATM 4034 O2 SUV A2001 -7.773 3.002 -55.076 1.00 38.74 O HETATM 4035 C3 SUV A2001 -6.362 -2.494 -55.853 1.00 32.80 C HETATM 4036 N3 SUV A2001 -9.087 1.618 -53.907 1.00 39.78 N HETATM 4037 C4 SUV A2001 -5.347 -3.015 -56.646 1.00 33.51 C HETATM 4038 N4 SUV A2001 -7.489 2.786 -51.270 1.00 39.31 N HETATM 4039 C5 SUV A2001 -4.328 -3.705 -56.009 1.00 33.70 C HETATM 4040 N5 SUV A2001 -7.964 2.338 -50.104 1.00 40.22 N HETATM 4041 C6 SUV A2001 -4.301 -3.889 -54.631 1.00 33.35 C HETATM 4042 N6 SUV A2001 -8.002 3.951 -51.684 1.00 40.76 N HETATM 4043 C7 SUV A2001 -5.320 -3.366 -53.850 1.00 32.63 C HETATM 4044 C8 SUV A2001 -6.326 -2.677 -54.492 1.00 31.76 C HETATM 4045 C11 SUV A2001 -9.657 -0.718 -53.382 1.00 37.48 C HETATM 4046 C12 SUV A2001 -9.321 0.627 -52.853 1.00 37.68 C HETATM 4047 C14 SUV A2001 -10.246 2.003 -54.739 1.00 44.69 C HETATM 4048 C15 SUV A2001 -10.960 0.795 -55.329 1.00 41.53 C HETATM 4049 C16 SUV A2001 -9.996 -0.281 -55.825 1.00 38.25 C HETATM 4050 C17 SUV A2001 -7.893 2.178 -54.188 1.00 38.43 C HETATM 4051 C19 SUV A2001 -6.695 1.763 -53.380 1.00 36.44 C HETATM 4052 C20 SUV A2001 -6.508 2.075 -52.025 1.00 37.17 C HETATM 4053 C21 SUV A2001 -5.344 1.676 -51.379 1.00 34.59 C HETATM 4054 C22 SUV A2001 -4.378 0.972 -52.073 1.00 34.79 C HETATM 4055 C23 SUV A2001 -4.538 0.646 -53.410 1.00 35.44 C HETATM 4056 C24 SUV A2001 -5.701 1.047 -54.048 1.00 36.41 C HETATM 4057 C27 SUV A2001 -8.843 3.254 -49.720 1.00 41.06 C HETATM 4058 C28 SUV A2001 -8.867 4.295 -50.740 1.00 41.49 C HETATM 4059 C29 SUV A2001 -3.475 -0.127 -54.153 1.00 36.87 C HETATM 4060 C30 SUV A2001 -11.208 2.902 -53.983 1.00 53.89 C HETATM 4061 C1 OLA A2002 -15.069 25.641 -31.504 1.00 56.31 C HETATM 4062 O1 OLA A2002 -14.339 26.602 -31.180 1.00 57.21 O HETATM 4063 O2 OLA A2002 -16.234 25.586 -31.053 1.00 55.69 O HETATM 4064 C2 OLA A2002 -14.552 24.559 -32.423 1.00 56.01 C HETATM 4065 C3 OLA A2002 -14.665 25.000 -33.878 1.00 54.99 C HETATM 4066 C4 OLA A2002 -13.303 24.957 -34.563 1.00 53.74 C HETATM 4067 C5 OLA A2002 -13.447 24.992 -36.080 1.00 52.61 C HETATM 4068 C1 OLA A2003 -11.053 26.471 -28.369 1.00 61.66 C HETATM 4069 O1 OLA A2003 -10.808 27.319 -27.481 1.00 62.21 O HETATM 4070 O2 OLA A2003 -12.223 26.369 -28.801 1.00 64.94 O HETATM 4071 C2 OLA A2003 -9.953 25.588 -28.915 1.00 57.00 C HETATM 4072 C3 OLA A2003 -9.478 26.116 -30.265 1.00 51.81 C HETATM 4073 C4 OLA A2003 -9.408 24.990 -31.291 1.00 46.95 C HETATM 4074 C5 OLA A2003 -8.971 25.501 -32.659 1.00 42.31 C HETATM 4075 C6 OLA A2003 -9.724 24.788 -33.778 1.00 38.38 C HETATM 4076 C7 OLA A2003 -8.814 23.832 -34.541 1.00 35.96 C HETATM 4077 C1 OLA A2004 -17.363 20.549 -31.138 1.00 59.75 C HETATM 4078 O1 OLA A2004 -17.248 19.317 -31.314 1.00 63.22 O HETATM 4079 O2 OLA A2004 -18.188 20.967 -30.296 1.00 59.39 O HETATM 4080 C2 OLA A2004 -16.513 21.517 -31.926 1.00 56.60 C HETATM 4081 C3 OLA A2004 -16.120 20.888 -33.258 1.00 52.79 C HETATM 4082 C4 OLA A2004 -14.614 20.979 -33.479 1.00 48.65 C HETATM 4083 C5 OLA A2004 -14.235 20.525 -34.884 1.00 45.03 C HETATM 4084 C6 OLA A2004 -12.845 19.900 -34.903 1.00 42.44 C HETATM 4085 C1 OLA A2005 -7.668 29.697 -23.412 1.00 64.08 C HETATM 4086 O1 OLA A2005 -6.695 29.841 -22.640 1.00 67.76 O HETATM 4087 O2 OLA A2005 -8.488 30.633 -23.533 1.00 63.74 O HETATM 4088 C2 OLA A2005 -7.841 28.414 -24.192 1.00 61.08 C HETATM 4089 C3 OLA A2005 -7.260 27.259 -23.385 1.00 58.26 C HETATM 4090 C4 OLA A2005 -8.033 25.963 -23.606 1.00 56.21 C HETATM 4091 C5 OLA A2005 -7.610 25.302 -24.914 1.00 53.73 C HETATM 4092 C6 OLA A2005 -8.646 24.304 -25.422 1.00 52.23 C HETATM 4093 C7 OLA A2005 -8.089 22.886 -25.392 1.00 50.57 C HETATM 4094 C8 OLA A2005 -7.517 22.455 -26.739 1.00 50.05 C HETATM 4095 C9 OLA A2005 -8.621 21.927 -27.626 1.00 49.61 C HETATM 4096 C10 OLA A2005 -8.312 21.067 -28.782 1.00 46.76 C HETATM 4097 C11 OLA A2005 -6.976 21.182 -29.480 1.00 44.04 C HETATM 4098 C12 OLA A2005 -7.061 20.652 -30.909 1.00 43.83 C HETATM 4099 C13 OLA A2005 -7.000 19.130 -30.971 1.00 43.71 C HETATM 4100 C14 OLA A2005 -8.059 18.575 -31.917 1.00 43.91 C HETATM 4101 C1 OLA A2006 -24.222 10.849 -25.961 1.00 51.84 C HETATM 4102 O1 OLA A2006 -24.043 11.791 -25.157 1.00 51.51 O HETATM 4103 O2 OLA A2006 -24.276 9.680 -25.519 1.00 55.17 O HETATM 4104 C2 OLA A2006 -24.376 11.123 -27.440 1.00 51.02 C HETATM 4105 C3 OLA A2006 -23.906 9.918 -28.247 1.00 49.97 C HETATM 4106 C4 OLA A2006 -22.959 10.347 -29.362 1.00 48.34 C HETATM 4107 C5 OLA A2006 -22.438 9.148 -30.148 1.00 46.11 C HETATM 4108 C6 OLA A2006 -23.116 9.024 -31.509 1.00 43.62 C HETATM 4109 C7 OLA A2006 -22.080 8.819 -32.609 1.00 42.10 C HETATM 4110 C8 OLA A2006 -22.641 9.176 -33.981 1.00 42.00 C HETATM 4111 C9 OLA A2006 -23.141 7.926 -34.665 1.00 42.40 C HETATM 4112 C1 OLA A2007 9.303 -1.599 -34.428 1.00 53.87 C HETATM 4113 O1 OLA A2007 10.267 -1.431 -33.648 1.00 58.96 O HETATM 4114 O2 OLA A2007 8.335 -0.808 -34.372 1.00 52.97 O HETATM 4115 C2 OLA A2007 9.306 -2.738 -35.421 1.00 51.66 C HETATM 4116 C3 OLA A2007 10.010 -2.308 -36.704 1.00 48.93 C HETATM 4117 C4 OLA A2007 11.221 -3.190 -36.988 1.00 45.67 C HETATM 4118 C5 OLA A2007 11.996 -2.686 -38.199 1.00 42.37 C HETATM 4119 O HOH A2101 -11.484 15.225 -63.370 1.00 26.27 O HETATM 4120 O HOH A2102 -5.417 38.078 14.861 1.00 35.55 O HETATM 4121 O HOH A2103 -15.287 3.319 -89.458 1.00 30.33 O HETATM 4122 O HOH A2104 4.604 -4.580 -20.636 1.00 36.88 O HETATM 4123 O HOH A2105 -3.727 -11.975 -64.897 1.00 15.94 O HETATM 4124 O HOH A2106 9.784 23.490 1.890 1.00 36.01 O HETATM 4125 O HOH A2107 -15.486 -0.873 -92.356 1.00 36.01 O HETATM 4126 O HOH A2108 -1.246 19.438 11.623 1.00 27.83 O HETATM 4127 O HOH A2109 3.452 19.668 -13.619 1.00 31.72 O HETATM 4128 O HOH A2110 0.929 14.766 7.092 1.00 35.91 O HETATM 4129 O HOH A2111 -2.616 15.536 12.490 1.00 30.55 O HETATM 4130 O HOH A2112 -11.299 -1.491 -20.351 1.00 31.21 O HETATM 4131 O HOH A2113 -1.408 -15.369 -63.875 1.00 44.30 O HETATM 4132 O HOH A2114 -21.331 23.322 -5.251 1.00 19.86 O HETATM 4133 O HOH A2115 0.633 11.990 6.330 1.00 26.36 O HETATM 4134 O HOH A2116 2.958 12.545 -58.047 1.00 30.61 O HETATM 4135 O HOH A2117 -1.138 17.436 13.422 1.00 36.81 O HETATM 4136 O HOH A2118 -0.052 15.188 13.634 1.00 23.33 O CONECT 773 1410 CONECT 1410 773 CONECT 4029 4030 4031 4033 CONECT 4030 4029 4045 4049 CONECT 4031 4029 4044 CONECT 4032 4039 CONECT 4033 4029 4035 CONECT 4034 4050 CONECT 4035 4033 4037 4044 CONECT 4036 4046 4047 4050 CONECT 4037 4035 4039 CONECT 4038 4040 4042 4052 CONECT 4039 4032 4037 4041 CONECT 4040 4038 4057 CONECT 4041 4039 4043 CONECT 4042 4038 4058 CONECT 4043 4041 4044 CONECT 4044 4031 4035 4043 CONECT 4045 4030 4046 CONECT 4046 4036 4045 CONECT 4047 4036 4048 4060 CONECT 4048 4047 4049 CONECT 4049 4030 4048 CONECT 4050 4034 4036 4051 CONECT 4051 4050 4052 4056 CONECT 4052 4038 4051 4053 CONECT 4053 4052 4054 CONECT 4054 4053 4055 CONECT 4055 4054 4056 4059 CONECT 4056 4051 4055 CONECT 4057 4040 4058 CONECT 4058 4042 4057 CONECT 4059 4055 CONECT 4060 4047 CONECT 4061 4062 4063 4064 CONECT 4062 4061 CONECT 4063 4061 CONECT 4064 4061 4065 CONECT 4065 4064 4066 CONECT 4066 4065 4067 CONECT 4067 4066 CONECT 4068 4069 4070 4071 CONECT 4069 4068 CONECT 4070 4068 CONECT 4071 4068 4072 CONECT 4072 4071 4073 CONECT 4073 4072 4074 CONECT 4074 4073 4075 CONECT 4075 4074 4076 CONECT 4076 4075 CONECT 4077 4078 4079 4080 CONECT 4078 4077 CONECT 4079 4077 CONECT 4080 4077 4081 CONECT 4081 4080 4082 CONECT 4082 4081 4083 CONECT 4083 4082 4084 CONECT 4084 4083 CONECT 4085 4086 4087 4088 CONECT 4086 4085 CONECT 4087 4085 CONECT 4088 4085 4089 CONECT 4089 4088 4090 CONECT 4090 4089 4091 CONECT 4091 4090 4092 CONECT 4092 4091 4093 CONECT 4093 4092 4094 CONECT 4094 4093 4095 CONECT 4095 4094 4096 CONECT 4096 4095 4097 CONECT 4097 4096 4098 CONECT 4098 4097 4099 CONECT 4099 4098 4100 CONECT 4100 4099 CONECT 4101 4102 4103 4104 CONECT 4102 4101 CONECT 4103 4101 CONECT 4104 4101 4105 CONECT 4105 4104 4106 CONECT 4106 4105 4107 CONECT 4107 4106 4108 CONECT 4108 4107 4109 CONECT 4109 4108 4110 CONECT 4110 4109 4111 CONECT 4111 4110 CONECT 4112 4113 4114 4115 CONECT 4113 4112 CONECT 4114 4112 CONECT 4115 4112 4116 CONECT 4116 4115 4117 CONECT 4117 4116 4118 CONECT 4118 4117 MASTER 630 0 7 21 8 0 9 6 4135 1 92 43 END