HEADER VIRAL PROTEIN/SIGNALLING PROTEIN 22-JAN-15 4XT1 TITLE STRUCTURE OF A NANOBODY-BOUND VIRAL GPCR BOUND TO HUMAN CHEMOKINE TITLE 2 CX3CL1 COMPND MOL_ID: 1; COMPND 2 MOLECULE: G-PROTEIN COUPLED RECEPTOR HOMOLOG US28; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: HHRF3; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: FRACTALKINE; COMPND 8 CHAIN: B; COMPND 9 FRAGMENT: UNP RESIDUES 25-101; COMPND 10 SYNONYM: C-X3-C MOTIF CHEMOKINE 1,CX3C MEMBRANE-ANCHORED CHEMOKINE, COMPND 11 NEUROTACTIN,SMALL-INDUCIBLE CYTOKINE D1; COMPND 12 ENGINEERED: YES; COMPND 13 MUTATION: YES; COMPND 14 MOL_ID: 3; COMPND 15 MOLECULE: NANOBODY 7; COMPND 16 CHAIN: C; COMPND 17 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: CYTOMEGALOVIRUS; SOURCE 3 ORGANISM_TAXID: 10358; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 7 EXPRESSION_SYSTEM_CELL_LINE: HEK293S GNTI-; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 10 ORGANISM_COMMON: HUMAN; SOURCE 11 ORGANISM_TAXID: 9606; SOURCE 12 GENE: CX3CL1, FKN, NTT, SCYD1, A-152E5.2; SOURCE 13 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 14 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 15 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 16 EXPRESSION_SYSTEM_CELL_LINE: HEK293S GNTI-; SOURCE 17 MOL_ID: 3; SOURCE 18 ORGANISM_SCIENTIFIC: VICUGNA PACOS; SOURCE 19 ORGANISM_TAXID: 30538; SOURCE 20 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 21 EXPRESSION_SYSTEM_TAXID: 511693; SOURCE 22 EXPRESSION_SYSTEM_STRAIN: BL21 KEYWDS GPCR, CHEMOKINE, MEMBRANE PROTEIN, COMPLEX, VIRAL PROTEIN-SIGNALLING KEYWDS 2 PROTEIN COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR J.S.BURG,K.M.JUDE,D.WAGHRAY,K.C.GARCIA REVDAT 2 18-MAR-15 4XT1 1 JRNL REVDAT 1 04-MAR-15 4XT1 0 JRNL AUTH J.S.BURG,J.R.INGRAM,A.J.VENKATAKRISHNAN,K.M.JUDE, JRNL AUTH 2 A.DUKKIPATI,E.N.FEINBERG,A.ANGELINI,D.WAGHRAY,R.O.DROR, JRNL AUTH 3 H.L.PLOEGH,K.C.GARCIA JRNL TITL STRUCTURAL BIOLOGY. STRUCTURAL BASIS FOR CHEMOKINE JRNL TITL 2 RECOGNITION AND ACTIVATION OF A VIRAL G PROTEIN-COUPLED JRNL TITL 3 RECEPTOR. JRNL REF SCIENCE V. 347 1113 2015 JRNL REFN ESSN 1095-9203 JRNL PMID 25745166 JRNL DOI 10.1126/SCIENCE.AAA5026 REMARK 2 REMARK 2 RESOLUTION. 2.89 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX DEV_1839 REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.89 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.23 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6 REMARK 3 NUMBER OF REFLECTIONS : 16629 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.204 REMARK 3 R VALUE (WORKING SET) : 0.199 REMARK 3 FREE R VALUE : 0.249 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.980 REMARK 3 FREE R VALUE TEST SET COUNT : 1659 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 38.2374 - 6.5960 1.00 1273 143 0.1846 0.2083 REMARK 3 2 6.5960 - 5.2397 1.00 1247 145 0.2212 0.2534 REMARK 3 3 5.2397 - 4.5786 1.00 1265 134 0.1699 0.2022 REMARK 3 4 4.5786 - 4.1606 1.00 1261 135 0.1573 0.2179 REMARK 3 5 4.1606 - 3.8627 1.00 1251 137 0.1999 0.2280 REMARK 3 6 3.8627 - 3.6351 1.00 1260 142 0.1904 0.2472 REMARK 3 7 3.6351 - 3.4532 1.00 1233 145 0.2020 0.3041 REMARK 3 8 3.4532 - 3.3029 1.00 1264 140 0.2338 0.2984 REMARK 3 9 3.3029 - 3.1759 1.00 1245 139 0.2307 0.3373 REMARK 3 10 3.1759 - 3.0663 1.00 1253 137 0.2341 0.2838 REMARK 3 11 3.0663 - 2.9705 1.00 1237 137 0.2562 0.3219 REMARK 3 12 2.9705 - 2.8856 0.95 1181 125 0.2723 0.3354 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) : 0.430 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.330 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 58.12 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 67.00 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 : 0.002 4044 REMARK 3 ANGLE : 0.605 5461 REMARK 3 CHIRALITY : 0.021 630 REMARK 3 PLANARITY : 0.003 649 REMARK 3 DIHEDRAL : 12.801 1462 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 14 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 66 ) REMARK 3 ORIGIN FOR THE GROUP (A): 97.8340 17.9238 277.5957 REMARK 3 T TENSOR REMARK 3 T11: 0.7263 T22: 0.7106 REMARK 3 T33: 0.4480 T12: -0.1552 REMARK 3 T13: 0.1093 T23: -0.0240 REMARK 3 L TENSOR REMARK 3 L11: 3.6181 L22: 7.7641 REMARK 3 L33: 4.4286 L12: 0.2164 REMARK 3 L13: -0.4889 L23: -4.0143 REMARK 3 S TENSOR REMARK 3 S11: 0.2541 S12: -1.0191 S13: -0.1501 REMARK 3 S21: 0.5337 S22: -0.2781 S23: -0.0937 REMARK 3 S31: 0.7752 S32: -0.2718 S33: 0.0552 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 67 THROUGH 72 ) REMARK 3 ORIGIN FOR THE GROUP (A): 90.1610 21.1182 275.9458 REMARK 3 T TENSOR REMARK 3 T11: 0.6665 T22: 0.9599 REMARK 3 T33: 0.4348 T12: -0.1040 REMARK 3 T13: 0.2870 T23: -0.0122 REMARK 3 L TENSOR REMARK 3 L11: 9.5434 L22: 7.0106 REMARK 3 L33: 4.0699 L12: -5.9422 REMARK 3 L13: 2.6683 L23: 1.5195 REMARK 3 S TENSOR REMARK 3 S11: 0.8410 S12: 0.3912 S13: 0.4446 REMARK 3 S21: 0.2966 S22: -0.2147 S23: 0.9728 REMARK 3 S31: -0.9919 S32: -1.3048 S33: -1.0979 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 73 THROUGH 116 ) REMARK 3 ORIGIN FOR THE GROUP (A): 99.5792 18.4164 278.1598 REMARK 3 T TENSOR REMARK 3 T11: 0.8674 T22: 0.6620 REMARK 3 T33: 0.2987 T12: -0.1589 REMARK 3 T13: 0.0638 T23: 0.0675 REMARK 3 L TENSOR REMARK 3 L11: 6.6941 L22: 3.7743 REMARK 3 L33: 7.1639 L12: 2.0050 REMARK 3 L13: -4.2132 L23: -3.4989 REMARK 3 S TENSOR REMARK 3 S11: 0.0082 S12: -0.6647 S13: -0.6379 REMARK 3 S21: 0.6593 S22: 0.0400 S23: -0.0901 REMARK 3 S31: 0.7415 S32: -0.5307 S33: 0.0046 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 16 THROUGH 33 ) REMARK 3 ORIGIN FOR THE GROUP (A): 110.2833 23.3554 207.6492 REMARK 3 T TENSOR REMARK 3 T11: 0.6672 T22: 0.6745 REMARK 3 T33: 0.5254 T12: -0.0585 REMARK 3 T13: 0.1004 T23: 0.0131 REMARK 3 L TENSOR REMARK 3 L11: 6.0571 L22: 3.2809 REMARK 3 L33: 6.4363 L12: 0.0943 REMARK 3 L13: 0.5272 L23: 1.0416 REMARK 3 S TENSOR REMARK 3 S11: -0.1704 S12: 0.9867 S13: 0.5568 REMARK 3 S21: -0.4851 S22: 0.4170 S23: 0.1129 REMARK 3 S31: -0.7431 S32: -0.4589 S33: -0.0335 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 34 THROUGH 103 ) REMARK 3 ORIGIN FOR THE GROUP (A): 103.0991 10.5731 240.6328 REMARK 3 T TENSOR REMARK 3 T11: 0.3570 T22: 0.2609 REMARK 3 T33: 0.4665 T12: -0.0585 REMARK 3 T13: 0.0052 T23: -0.0455 REMARK 3 L TENSOR REMARK 3 L11: 2.3303 L22: 1.7464 REMARK 3 L33: 3.9634 L12: -0.6707 REMARK 3 L13: -1.7244 L23: 0.1946 REMARK 3 S TENSOR REMARK 3 S11: -0.2586 S12: 0.1193 S13: -0.4502 REMARK 3 S21: -0.0147 S22: 0.0722 S23: 0.1727 REMARK 3 S31: 0.7907 S32: -0.3102 S33: 0.1915 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 104 THROUGH 169 ) REMARK 3 ORIGIN FOR THE GROUP (A): 92.4756 22.3415 242.3529 REMARK 3 T TENSOR REMARK 3 T11: 0.1923 T22: 0.3210 REMARK 3 T33: 0.4229 T12: 0.0114 REMARK 3 T13: -0.0223 T23: 0.0353 REMARK 3 L TENSOR REMARK 3 L11: 2.9439 L22: 1.4595 REMARK 3 L33: 8.8955 L12: 0.3258 REMARK 3 L13: -0.3839 L23: 1.6012 REMARK 3 S TENSOR REMARK 3 S11: -0.2236 S12: 0.2217 S13: 0.0628 REMARK 3 S21: -0.1167 S22: -0.1545 S23: 0.4046 REMARK 3 S31: -0.0129 S32: -0.6211 S33: 0.3990 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 170 THROUGH 183 ) REMARK 3 ORIGIN FOR THE GROUP (A): 92.3407 20.5767 214.9800 REMARK 3 T TENSOR REMARK 3 T11: 0.8177 T22: 1.0753 REMARK 3 T33: 0.6612 T12: -0.0693 REMARK 3 T13: -0.1480 T23: -0.2003 REMARK 3 L TENSOR REMARK 3 L11: 3.4908 L22: 8.5694 REMARK 3 L33: 8.4630 L12: -2.8670 REMARK 3 L13: -1.4758 L23: 5.6972 REMARK 3 S TENSOR REMARK 3 S11: 0.3479 S12: 1.4016 S13: -0.1867 REMARK 3 S21: -1.3734 S22: -1.3732 S23: 1.9016 REMARK 3 S31: -0.4287 S32: -0.8483 S33: 1.0144 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 184 THROUGH 290 ) REMARK 3 ORIGIN FOR THE GROUP (A): 106.3190 29.7905 237.0153 REMARK 3 T TENSOR REMARK 3 T11: 0.3088 T22: 0.2787 REMARK 3 T33: 0.3940 T12: -0.0511 REMARK 3 T13: 0.0069 T23: 0.0360 REMARK 3 L TENSOR REMARK 3 L11: 0.9490 L22: 0.5389 REMARK 3 L33: 5.3558 L12: -0.0388 REMARK 3 L13: -0.0274 L23: 0.1635 REMARK 3 S TENSOR REMARK 3 S11: -0.0709 S12: 0.0897 S13: -0.0460 REMARK 3 S21: -0.1062 S22: 0.0317 S23: 0.0247 REMARK 3 S31: -0.1538 S32: -0.0703 S33: 0.0276 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 291 THROUGH 310 ) REMARK 3 ORIGIN FOR THE GROUP (A): 109.6962 9.3779 257.7165 REMARK 3 T TENSOR REMARK 3 T11: 0.3843 T22: 0.4173 REMARK 3 T33: 0.6507 T12: 0.0627 REMARK 3 T13: -0.0727 T23: -0.0791 REMARK 3 L TENSOR REMARK 3 L11: 7.7503 L22: 5.3358 REMARK 3 L33: 8.0326 L12: -1.3482 REMARK 3 L13: 3.2667 L23: -4.8988 REMARK 3 S TENSOR REMARK 3 S11: 0.4807 S12: -0.1203 S13: -0.6189 REMARK 3 S21: -0.2217 S22: -0.5434 S23: -0.6009 REMARK 3 S31: 0.8659 S32: 0.4113 S33: 0.1423 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 2 THROUGH 16 ) REMARK 3 ORIGIN FOR THE GROUP (A): 102.8725 21.5940 212.1990 REMARK 3 T TENSOR REMARK 3 T11: 0.5954 T22: 0.8527 REMARK 3 T33: 0.5501 T12: 0.0365 REMARK 3 T13: -0.0628 T23: -0.0573 REMARK 3 L TENSOR REMARK 3 L11: 4.5598 L22: 6.5817 REMARK 3 L33: 9.6518 L12: 2.3673 REMARK 3 L13: -3.1025 L23: -1.9082 REMARK 3 S TENSOR REMARK 3 S11: 0.3271 S12: 0.9673 S13: -0.0434 REMARK 3 S21: -0.6332 S22: -0.3916 S23: 1.6379 REMARK 3 S31: -0.8714 S32: 0.1197 S33: -0.1066 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 17 THROUGH 23 ) REMARK 3 ORIGIN FOR THE GROUP (A): 101.4834 24.0413 188.1388 REMARK 3 T TENSOR REMARK 3 T11: 1.2398 T22: 1.6698 REMARK 3 T33: 0.7576 T12: -0.1170 REMARK 3 T13: -0.1320 T23: -0.0828 REMARK 3 L TENSOR REMARK 3 L11: 0.4372 L22: 2.0615 REMARK 3 L33: 4.7053 L12: -0.8465 REMARK 3 L13: -1.4104 L23: 2.9888 REMARK 3 S TENSOR REMARK 3 S11: -1.0461 S12: 0.9625 S13: -0.1861 REMARK 3 S21: 1.7639 S22: 0.0976 S23: 0.8073 REMARK 3 S31: 0.9873 S32: -3.3418 S33: 1.1414 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 24 THROUGH 29 ) REMARK 3 ORIGIN FOR THE GROUP (A): 102.3993 14.3923 196.3178 REMARK 3 T TENSOR REMARK 3 T11: 1.8237 T22: 1.6473 REMARK 3 T33: 0.8598 T12: -0.4539 REMARK 3 T13: -0.1482 T23: -0.3401 REMARK 3 L TENSOR REMARK 3 L11: 3.7392 L22: 1.2740 REMARK 3 L33: 5.7859 L12: -1.8308 REMARK 3 L13: -3.6685 L23: 0.8875 REMARK 3 S TENSOR REMARK 3 S11: -0.7249 S12: 1.4117 S13: -1.2002 REMARK 3 S21: 0.5817 S22: 1.1974 S23: -0.7236 REMARK 3 S31: 2.0070 S32: -2.3345 S33: -0.1025 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 30 THROUGH 57 ) REMARK 3 ORIGIN FOR THE GROUP (A): 100.9478 20.6617 199.6775 REMARK 3 T TENSOR REMARK 3 T11: 1.0706 T22: 1.9454 REMARK 3 T33: 0.4560 T12: -0.0774 REMARK 3 T13: -0.1322 T23: -0.0630 REMARK 3 L TENSOR REMARK 3 L11: 1.9495 L22: 2.9397 REMARK 3 L33: 3.0594 L12: 1.8877 REMARK 3 L13: -1.5929 L23: -1.1735 REMARK 3 S TENSOR REMARK 3 S11: -0.4506 S12: 0.2093 S13: -0.2632 REMARK 3 S21: -1.1037 S22: 0.2179 S23: 0.1150 REMARK 3 S31: 0.5901 S32: -0.1105 S33: -0.3604 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 58 THROUGH 69 ) REMARK 3 ORIGIN FOR THE GROUP (A): 96.0353 13.8865 190.4050 REMARK 3 T TENSOR REMARK 3 T11: 1.2548 T22: 2.1225 REMARK 3 T33: 1.1028 T12: -0.7648 REMARK 3 T13: -0.0630 T23: -0.0347 REMARK 3 L TENSOR REMARK 3 L11: 9.6854 L22: 5.9922 REMARK 3 L33: 6.3853 L12: -7.6140 REMARK 3 L13: -1.4100 L23: 1.3203 REMARK 3 S TENSOR REMARK 3 S11: 0.1889 S12: 3.4295 S13: -2.5020 REMARK 3 S21: -0.6080 S22: -0.3263 S23: 2.1531 REMARK 3 S31: 1.5941 S32: -2.3030 S33: 0.6776 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 4XT1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-JAN-15. REMARK 100 THE DEPOSITION ID IS D_1000206261. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 13-OCT-13 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 6.3 REMARK 200 NUMBER OF CRYSTALS USED : 2 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 23-ID-B 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 : CCD REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16648 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.880 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.7 REMARK 200 DATA REDUNDANCY : 8.500 REMARK 200 R MERGE (I) : 0.20000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 5.2000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.88 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.93 REMARK 200 COMPLETENESS FOR SHELL (%) : 74.8 REMARK 200 DATA REDUNDANCY IN SHELL : 6.80 REMARK 200 R MERGE FOR SHELL (I) : 0.87200 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: 4MBS, 1F2L, 3ONA, 4B41 REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 56.80 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.85 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 300, MES, SODIUM SUCCINATE, REMARK 280 POLYPROPYLENE GLYCOL 400, PH 6.3, LIPIDIC CUBIC PHASE, REMARK 280 TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z REMARK 290 3555 -Y,X,Z REMARK 290 4555 Y,-X,Z REMARK 290 5555 X+1/2,Y+1/2,Z+1/2 REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2 REMARK 290 7555 -Y+1/2,X+1/2,Z+1/2 REMARK 290 8555 Y+1/2,-X+1/2,Z+1/2 REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 40.51200 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 40.51200 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 115.65150 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 40.51200 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 40.51200 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 115.65150 REMARK 290 SMTRY1 7 0.000000 -1.000000 0.000000 40.51200 REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 40.51200 REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 115.65150 REMARK 290 SMTRY1 8 0.000000 1.000000 0.000000 40.51200 REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 40.51200 REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 115.65150 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: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 7910 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 23920 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -40.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C 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 THR A 2 REMARK 465 PRO A 3 REMARK 465 THR A 4 REMARK 465 THR A 5 REMARK 465 THR A 6 REMARK 465 THR A 7 REMARK 465 ALA A 8 REMARK 465 GLU A 9 REMARK 465 LEU A 10 REMARK 465 THR A 11 REMARK 465 THR A 12 REMARK 465 GLU A 13 REMARK 465 PHE A 14 REMARK 465 HIS A 96 REMARK 465 ASN A 97 REMARK 465 SER A 98 REMARK 465 LEU A 99 REMARK 465 ALA A 100 REMARK 465 GLN A 311 REMARK 465 ARG A 312 REMARK 465 LEU A 313 REMARK 465 PHE A 314 REMARK 465 SER A 315 REMARK 465 ARG A 316 REMARK 465 ASP A 317 REMARK 465 VAL A 318 REMARK 465 SER A 319 REMARK 465 TRP A 320 REMARK 465 TYR A 321 REMARK 465 HIS A 322 REMARK 465 SER A 323 REMARK 465 MET A 324 REMARK 465 SER A 325 REMARK 465 PHE A 326 REMARK 465 SER A 327 REMARK 465 ARG A 328 REMARK 465 ARG A 329 REMARK 465 SER A 330 REMARK 465 SER A 331 REMARK 465 PRO A 332 REMARK 465 SER A 333 REMARK 465 ARG A 334 REMARK 465 ARG A 335 REMARK 465 GLU A 336 REMARK 465 THR A 337 REMARK 465 SER A 338 REMARK 465 SER A 339 REMARK 465 ASP A 340 REMARK 465 THR A 341 REMARK 465 LEU A 342 REMARK 465 SER A 343 REMARK 465 ASP A 344 REMARK 465 GLU A 345 REMARK 465 VAL A 346 REMARK 465 CYS A 347 REMARK 465 ARG A 348 REMARK 465 VAL A 349 REMARK 465 SER A 350 REMARK 465 GLN A 351 REMARK 465 ILE A 352 REMARK 465 ILE A 353 REMARK 465 PRO A 354 REMARK 465 ALA B 69 REMARK 465 ALA B 70 REMARK 465 ALA B 71 REMARK 465 LEU B 72 REMARK 465 THR B 73 REMARK 465 ARG B 74 REMARK 465 ASN B 75 REMARK 465 GLY B 76 REMARK 465 GLY B 77 REMARK 465 SER B 78 REMARK 465 GLY B 79 REMARK 465 SER B 80 REMARK 465 GLY B 81 REMARK 465 SER B 82 REMARK 465 ALA B 83 REMARK 465 ALA B 84 REMARK 465 ALA B 85 REMARK 465 LEU B 86 REMARK 465 GLU B 87 REMARK 465 VAL B 88 REMARK 465 LEU B 89 REMARK 465 PHE B 90 REMARK 465 GLN B 91 REMARK 465 GLY C -3 REMARK 465 PRO C -2 REMARK 465 GLY C -1 REMARK 465 SER C 0 REMARK 465 SER C 117 REMARK 465 SER C 118 REMARK 465 ARG C 119 REMARK 465 ALA C 120 REMARK 465 ALA C 121 REMARK 465 ALA C 122 REMARK 465 HIS C 123 REMARK 465 HIS C 124 REMARK 465 HIS C 125 REMARK 465 HIS C 126 REMARK 465 HIS C 127 REMARK 465 HIS C 128 REMARK 465 HIS C 129 REMARK 465 HIS C 130 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 ARG A 62 CG CD NE CZ NH1 NH2 REMARK 470 ARG A 63 CG CD NE CZ NH1 NH2 REMARK 470 GLN A 65 CG CD OE1 NE2 REMARK 470 GLN A 91 CG CD OE1 NE2 REMARK 470 ARG A 137 CD NE CZ NH1 NH2 REMARK 470 LYS A 297 CG CD CE NZ REMARK 470 LYS B 14 CG CD CE NZ REMARK 470 LEU B 23 CG CD1 CD2 REMARK 470 HIS B 26 CG ND1 CD2 CE1 NE2 REMARK 470 LYS B 36 CG CD CE NZ REMARK 470 ARG B 37 CG CD NE CZ NH1 NH2 REMARK 470 ARG B 44 CG CD NE CZ NH1 NH2 REMARK 470 ARG B 47 CG CD NE CZ NH1 NH2 REMARK 470 LYS B 54 CG CD CE NZ REMARK 470 GLN B 56 CG CD OE1 NE2 REMARK 470 LYS B 59 CG CD CE NZ REMARK 470 MET B 62 CG SD CE REMARK 470 GLN B 63 CG CD OE1 NE2 REMARK 470 HIS B 64 CG ND1 CD2 CE1 NE2 REMARK 470 ASP B 66 CG OD1 OD2 REMARK 470 ARG B 67 CG CD NE CZ NH1 NH2 REMARK 470 GLN B 68 CG CD OE1 NE2 REMARK 470 GLN C 1 CG CD OE1 NE2 REMARK 470 ARG C 13 CG CD NE CZ NH1 NH2 REMARK 470 ASP C 61 CG OD1 OD2 REMARK 470 LYS C 64 CG CD CE NZ REMARK 470 GLN C 110 CG CD OE1 NE2 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 OH TYR A 209 O19 OLC A 407 1.26 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 ASP A 17 96.42 -54.09 REMARK 500 TRP A 60 -73.74 -60.65 REMARK 500 GLN A 65 -61.76 -96.13 REMARK 500 VAL A 102 81.35 31.07 REMARK 500 PHE A 197 -64.82 -124.15 REMARK 500 TYR A 291 -54.60 -126.12 REMARK 500 ILE B 19 102.29 -162.85 REMARK 500 LYS B 54 37.20 -91.32 REMARK 500 ALA C 74 -29.69 69.72 REMARK 500 ILE C 101 -61.95 61.47 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 OLC A 403 REMARK 610 OLC A 404 REMARK 610 OLC A 405 REMARK 610 OLC A 406 REMARK 610 OLC A 408 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue CLR A 401 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue CLR A 402 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 403 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 404 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 405 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 406 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 407 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 408 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue SIN A 416 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 4XT3 RELATED DB: PDB DBREF 4XT1 A 1 354 UNP P69332 US28_HCMVA 1 354 DBREF 4XT1 B 1 77 UNP P78423 X3CL1_HUMAN 25 101 DBREF 4XT1 C -3 130 PDB 4XT1 4XT1 -3 130 SEQADV 4XT1 ASP A -7 UNP P69332 EXPRESSION TAG SEQADV 4XT1 TYR A -6 UNP P69332 EXPRESSION TAG SEQADV 4XT1 LYS A -5 UNP P69332 EXPRESSION TAG SEQADV 4XT1 ASP A -4 UNP P69332 EXPRESSION TAG SEQADV 4XT1 ASP A -3 UNP P69332 EXPRESSION TAG SEQADV 4XT1 ASP A -2 UNP P69332 EXPRESSION TAG SEQADV 4XT1 ASP A -1 UNP P69332 EXPRESSION TAG SEQADV 4XT1 ALA A 0 UNP P69332 EXPRESSION TAG SEQADV 4XT1 ALA B 9 UNP P78423 ASN 33 ENGINEERED MUTATION SEQADV 4XT1 SER B 78 UNP P78423 EXPRESSION TAG SEQADV 4XT1 GLY B 79 UNP P78423 EXPRESSION TAG SEQADV 4XT1 SER B 80 UNP P78423 EXPRESSION TAG SEQADV 4XT1 GLY B 81 UNP P78423 EXPRESSION TAG SEQADV 4XT1 SER B 82 UNP P78423 EXPRESSION TAG SEQADV 4XT1 ALA B 83 UNP P78423 EXPRESSION TAG SEQADV 4XT1 ALA B 84 UNP P78423 EXPRESSION TAG SEQADV 4XT1 ALA B 85 UNP P78423 EXPRESSION TAG SEQADV 4XT1 LEU B 86 UNP P78423 EXPRESSION TAG SEQADV 4XT1 GLU B 87 UNP P78423 EXPRESSION TAG SEQADV 4XT1 VAL B 88 UNP P78423 EXPRESSION TAG SEQADV 4XT1 LEU B 89 UNP P78423 EXPRESSION TAG SEQADV 4XT1 PHE B 90 UNP P78423 EXPRESSION TAG SEQADV 4XT1 GLN B 91 UNP P78423 EXPRESSION TAG SEQRES 1 A 362 ASP TYR LYS ASP ASP ASP ASP ALA MET THR PRO THR THR SEQRES 2 A 362 THR THR ALA GLU LEU THR THR GLU PHE ASP TYR ASP GLU SEQRES 3 A 362 ASP ALA THR PRO CYS VAL PHE THR ASP VAL LEU ASN GLN SEQRES 4 A 362 SER LYS PRO VAL THR LEU PHE LEU TYR GLY VAL VAL PHE SEQRES 5 A 362 LEU PHE GLY SER ILE GLY ASN PHE LEU VAL ILE PHE THR SEQRES 6 A 362 ILE THR TRP ARG ARG ARG ILE GLN CYS SER GLY ASP VAL SEQRES 7 A 362 TYR PHE ILE ASN LEU ALA ALA ALA ASP LEU LEU PHE VAL SEQRES 8 A 362 CYS THR LEU PRO LEU TRP MET GLN TYR LEU LEU ASP HIS SEQRES 9 A 362 ASN SER LEU ALA SER VAL PRO CYS THR LEU LEU THR ALA SEQRES 10 A 362 CYS PHE TYR VAL ALA MET PHE ALA SER LEU CYS PHE ILE SEQRES 11 A 362 THR GLU ILE ALA LEU ASP ARG TYR TYR ALA ILE VAL TYR SEQRES 12 A 362 MET ARG TYR ARG PRO VAL LYS GLN ALA CYS LEU PHE SER SEQRES 13 A 362 ILE PHE TRP TRP ILE PHE ALA VAL ILE ILE ALA ILE PRO SEQRES 14 A 362 HIS PHE MET VAL VAL THR LYS LYS ASP ASN GLN CYS MET SEQRES 15 A 362 THR ASP TYR ASP TYR LEU GLU VAL SER TYR PRO ILE ILE SEQRES 16 A 362 LEU ASN VAL GLU LEU MET LEU GLY ALA PHE VAL ILE PRO SEQRES 17 A 362 LEU SER VAL ILE SER TYR CYS TYR TYR ARG ILE SER ARG SEQRES 18 A 362 ILE VAL ALA VAL SER GLN SER ARG HIS LYS GLY ARG ILE SEQRES 19 A 362 VAL ARG VAL LEU ILE ALA VAL VAL LEU VAL PHE ILE ILE SEQRES 20 A 362 PHE TRP LEU PRO TYR HIS LEU THR LEU PHE VAL ASP THR SEQRES 21 A 362 LEU LYS LEU LEU LYS TRP ILE SER SER SER CYS GLU PHE SEQRES 22 A 362 GLU ARG SER LEU LYS ARG ALA LEU ILE LEU THR GLU SER SEQRES 23 A 362 LEU ALA PHE CYS HIS CYS CYS LEU ASN PRO LEU LEU TYR SEQRES 24 A 362 VAL PHE VAL GLY THR LYS PHE ARG GLN GLU LEU HIS CYS SEQRES 25 A 362 LEU LEU ALA GLU PHE ARG GLN ARG LEU PHE SER ARG ASP SEQRES 26 A 362 VAL SER TRP TYR HIS SER MET SER PHE SER ARG ARG SER SEQRES 27 A 362 SER PRO SER ARG ARG GLU THR SER SER ASP THR LEU SER SEQRES 28 A 362 ASP GLU VAL CYS ARG VAL SER GLN ILE ILE PRO SEQRES 1 B 91 PCA HIS HIS GLY VAL THR LYS CYS ALA ILE THR CYS SER SEQRES 2 B 91 LYS MET THR SER LYS ILE PRO VAL ALA LEU LEU ILE HIS SEQRES 3 B 91 TYR GLN GLN ASN GLN ALA SER CYS GLY LYS ARG ALA ILE SEQRES 4 B 91 ILE LEU GLU THR ARG GLN HIS ARG LEU PHE CYS ALA ASP SEQRES 5 B 91 PRO LYS GLU GLN TRP VAL LYS ASP ALA MET GLN HIS LEU SEQRES 6 B 91 ASP ARG GLN ALA ALA ALA LEU THR ARG ASN GLY GLY SER SEQRES 7 B 91 GLY SER GLY SER ALA ALA ALA LEU GLU VAL LEU PHE GLN SEQRES 1 C 134 GLY PRO GLY SER GLN VAL GLN LEU VAL GLU SER GLY GLY SEQRES 2 C 134 GLY LEU VAL ARG PRO GLY GLY SER LEU ARG LEU SER CYS SEQRES 3 C 134 ALA ALA SER GLY SER ILE PHE THR ILE TYR ALA MET GLY SEQRES 4 C 134 TRP TYR ARG GLN ALA PRO GLY LYS GLN ARG GLU LEU VAL SEQRES 5 C 134 ALA ARG ILE THR PHE GLY GLY ASP THR ASN TYR ALA ASP SEQRES 6 C 134 SER VAL LYS GLY ARG PHE THR ILE SER ARG ASP ASN ALA SEQRES 7 C 134 LYS ASN ALA VAL TYR LEU GLN MET ASN SER LEU LYS PRO SEQRES 8 C 134 GLU ASP THR ALA VAL TYR TYR CYS ASN ALA GLU GLU THR SEQRES 9 C 134 ILE VAL GLU GLU ALA ASP TYR TRP GLY GLN GLY THR GLN SEQRES 10 C 134 VAL THR VAL SER SER ARG ALA ALA ALA HIS HIS HIS HIS SEQRES 11 C 134 HIS HIS HIS HIS MODRES 4XT1 PCA B 1 GLN MODIFIED RESIDUE HET PCA B 1 8 HET CLR A 401 28 HET CLR A 402 28 HET OLC A 403 20 HET OLC A 404 20 HET OLC A 405 16 HET OLC A 406 21 HET OLC A 407 25 HET OLC A 408 14 HET UNL A 409 7 HET UNL A 410 12 HET UNL A 411 10 HET UNL A 412 12 HET UNL A 413 10 HET UNL A 414 12 HET UNL A 415 12 HET SIN A 416 8 HETNAM PCA PYROGLUTAMIC ACID HETNAM CLR CHOLESTEROL HETNAM OLC (2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE HETNAM UNL UNKNOWN LIGAND HETNAM SIN SUCCINIC ACID HETSYN OLC 1-OLEOYL-R-GLYCEROL FORMUL 2 PCA C5 H7 N O3 FORMUL 4 CLR 2(C27 H46 O) FORMUL 6 OLC 6(C21 H40 O4) FORMUL 19 SIN C4 H6 O4 FORMUL 20 HOH *23(H2 O) HELIX 1 AA1 PHE A 25 TRP A 60 1 36 HELIX 2 AA2 CYS A 66 CYS A 84 1 19 HELIX 3 AA3 THR A 85 ASP A 95 1 11 HELIX 4 AA4 PRO A 103 VAL A 134 1 32 HELIX 5 AA5 PRO A 140 ILE A 158 1 19 HELIX 6 AA6 ALA A 159 MET A 164 1 6 HELIX 7 AA7 SER A 183 PHE A 197 1 15 HELIX 8 AA8 PHE A 197 ALA A 216 1 20 HELIX 9 AA9 HIS A 222 LEU A 256 1 35 HELIX 10 AB1 SER A 262 PHE A 281 1 20 HELIX 11 AB2 CYS A 282 TYR A 291 1 10 HELIX 12 AB3 GLY A 295 PHE A 309 1 15 HELIX 13 AB4 GLN B 31 GLY B 35 5 5 HELIX 14 AB5 GLU B 55 GLN B 68 1 14 HELIX 15 AB6 LYS C 86 THR C 90 5 5 SHEET 1 AA1 2 CYS A 23 VAL A 24 0 SHEET 2 AA1 2 ILE B 10 THR B 11 -1 O THR B 11 N CYS A 23 SHEET 1 AA2 2 VAL A 166 LYS A 169 0 SHEET 2 AA2 2 GLN A 172 THR A 175 -1 O GLN A 172 N LYS A 169 SHEET 1 AA3 3 LEU B 24 GLN B 29 0 SHEET 2 AA3 3 ILE B 39 THR B 43 -1 O ILE B 40 N GLN B 28 SHEET 3 AA3 3 LEU B 48 ALA B 51 -1 O ALA B 51 N ILE B 39 SHEET 1 AA4 4 LEU C 4 SER C 7 0 SHEET 2 AA4 4 SER C 17 ALA C 24 -1 O SER C 21 N SER C 7 SHEET 3 AA4 4 ALA C 77 ASN C 83 -1 O MET C 82 N LEU C 18 SHEET 4 AA4 4 PHE C 67 ASP C 72 -1 N ASP C 72 O ALA C 77 SHEET 1 AA5 6 GLY C 10 LEU C 11 0 SHEET 2 AA5 6 THR C 112 THR C 115 1 O THR C 115 N GLY C 10 SHEET 3 AA5 6 ALA C 91 GLU C 99 -1 N TYR C 93 O THR C 112 SHEET 4 AA5 6 ILE C 31 GLN C 39 -1 N TYR C 37 O TYR C 94 SHEET 5 AA5 6 ARG C 45 THR C 52 -1 O ALA C 49 N TRP C 36 SHEET 6 AA5 6 THR C 57 TYR C 59 -1 O ASN C 58 N ARG C 50 SHEET 1 AA6 4 GLY C 10 LEU C 11 0 SHEET 2 AA6 4 THR C 112 THR C 115 1 O THR C 115 N GLY C 10 SHEET 3 AA6 4 ALA C 91 GLU C 99 -1 N TYR C 93 O THR C 112 SHEET 4 AA6 4 TYR C 107 TRP C 108 -1 O TYR C 107 N ALA C 97 SSBOND 1 CYS A 23 CYS A 263 1555 1555 2.03 SSBOND 2 CYS A 104 CYS A 173 1555 1555 2.03 SSBOND 3 CYS B 8 CYS B 34 1555 1555 2.03 SSBOND 4 CYS B 12 CYS B 50 1555 1555 2.03 SSBOND 5 CYS C 22 CYS C 95 1555 1555 2.03 LINK C PCA B 1 N HIS B 2 1555 1555 1.33 SITE 1 AC1 3 PRO A 243 LEU A 246 CLR A 402 SITE 1 AC2 6 PHE A 249 LEU A 253 SER A 268 ARG A 271 SITE 2 AC2 6 LEU A 279 CLR A 401 SITE 1 AC3 2 PRO A 34 PHE A 38 SITE 1 AC4 6 GLY A 224 ARG A 228 ILE A 231 LEU A 235 SITE 2 AC4 6 OLC A 406 OLC A 407 SITE 1 AC5 6 PHE A 46 ILE A 49 LEU A 289 PHE A 293 SITE 2 AC5 6 ARG A 299 LEU A 302 SITE 1 AC6 5 TYR A 209 ARG A 213 ILE A 231 VAL A 234 SITE 2 AC6 5 OLC A 404 SITE 1 AC7 8 SER A 202 TYR A 209 ARG A 210 ARG A 213 SITE 2 AC7 8 ARG A 225 ARG A 228 OLC A 404 OLC A 408 SITE 1 AC8 3 LEU A 289 LEU A 290 OLC A 407 SITE 1 AC9 3 LEU A 119 THR A 123 GLY A 195 CRYST1 81.024 81.024 231.303 90.00 90.00 90.00 I 4 8 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.012342 0.000000 0.000000 0.00000 SCALE2 0.000000 0.012342 0.000000 0.00000 SCALE3 0.000000 0.000000 0.004323 0.00000 ATOM 1 N ASP A 15 101.309 36.475 192.154 1.00123.83 N ATOM 2 CA ASP A 15 101.691 35.103 191.846 1.00116.36 C ATOM 3 C ASP A 15 103.158 35.027 191.415 1.00106.09 C ATOM 4 O ASP A 15 103.521 34.268 190.513 1.00123.35 O ATOM 5 CB ASP A 15 100.780 34.530 190.762 1.00116.56 C ATOM 6 CG ASP A 15 100.813 33.015 190.710 1.00124.69 C ATOM 7 OD1 ASP A 15 100.183 32.444 189.794 1.00135.28 O ATOM 8 OD2 ASP A 15 101.467 32.396 191.578 1.00123.07 O ATOM 9 N TYR A 16 103.994 35.825 192.073 1.00206.21 N ANISOU 9 N TYR A 16 29187 27991 21172 1099 -1203 7881 N ATOM 10 CA TYR A 16 105.445 35.745 191.924 1.00176.07 C ANISOU 10 CA TYR A 16 25588 24036 17276 455 -804 7799 C ATOM 11 C TYR A 16 105.929 34.353 192.348 1.00143.42 C ANISOU 11 C TYR A 16 21026 20322 13144 105 -581 7003 C ATOM 12 O TYR A 16 105.163 33.590 192.938 1.00137.29 O ANISOU 12 O TYR A 16 19858 19766 12538 353 -714 6548 O ATOM 13 CB TYR A 16 106.114 36.835 192.767 1.00169.20 C ANISOU 13 CB TYR A 16 25133 22162 16992 422 -611 7955 C ATOM 14 CG TYR A 16 107.550 37.149 192.407 1.00166.78 C ANISOU 14 CG TYR A 16 25141 21656 16573 -222 -247 8111 C ATOM 15 CD1 TYR A 16 108.042 36.913 191.130 1.00170.14 C ANISOU 15 CD1 TYR A 16 25616 22615 16415 -586 -133 8184 C ATOM 16 CD2 TYR A 16 108.413 37.689 193.351 1.00158.65 C ANISOU 16 CD2 TYR A 16 24322 19863 16094 -438 13 7940 C ATOM 17 CE1 TYR A 16 109.355 37.205 190.805 1.00166.14 C ANISOU 17 CE1 TYR A 16 25326 21948 15851 -1134 249 8205 C ATOM 18 CE2 TYR A 16 109.727 37.983 193.038 1.00159.42 C ANISOU 18 CE2 TYR A 16 24653 19813 16106 -1057 352 8059 C ATOM 19 CZ TYR A 16 110.192 37.739 191.762 1.00163.06 C ANISOU 19 CZ TYR A 16 25113 20851 15991 -1372 493 8141 C ATOM 20 OH TYR A 16 111.495 38.026 191.435 1.00162.83 O ANISOU 20 OH TYR A 16 25217 20723 15929 -1916 880 8132 O ATOM 21 N ASP A 17 107.182 34.013 192.052 1.00126.48 N ANISOU 21 N ASP A 17 18948 18294 10816 -464 -243 6838 N ATOM 22 CA ASP A 17 107.721 32.723 192.481 1.00110.79 C ANISOU 22 CA ASP A 17 16592 16629 8874 -758 -34 6088 C ATOM 23 C ASP A 17 107.536 32.570 193.993 1.00122.45 C ANISOU 23 C ASP A 17 17920 17576 11029 -531 -3 5631 C ATOM 24 O ASP A 17 108.338 33.054 194.791 1.00130.23 O ANISOU 24 O ASP A 17 19086 17963 12433 -673 218 5542 O ATOM 25 CB ASP A 17 109.194 32.573 192.089 1.00110.76 C ANISOU 25 CB ASP A 17 16694 16715 8674 -1350 349 5988 C ATOM 26 CG ASP A 17 109.980 33.861 192.233 1.00131.14 C ANISOU 26 CG ASP A 17 19718 18619 11491 -1536 533 6458 C ATOM 27 OD1 ASP A 17 111.086 33.949 191.657 1.00134.83 O ANISOU 27 OD1 ASP A 17 20300 19238 11694 -2034 824 6550 O ATOM 28 OD2 ASP A 17 109.494 34.785 192.912 1.00134.76 O ANISOU 28 OD2 ASP A 17 20404 18401 12400 -1197 395 6717 O ATOM 29 N GLU A 18 106.457 31.885 194.363 1.00108.50 N ANISOU 29 N GLU A 18 15809 16080 9335 -199 -230 5341 N ATOM 30 CA GLU A 18 105.886 31.967 195.707 1.00111.25 C ANISOU 30 CA GLU A 18 16034 15978 10258 153 -283 5074 C ATOM 31 C GLU A 18 106.846 31.623 196.840 1.00104.03 C ANISOU 31 C GLU A 18 15097 14661 9767 -87 13 4580 C ATOM 32 O GLU A 18 107.682 30.728 196.727 1.00 90.12 O ANISOU 32 O GLU A 18 13203 13166 7872 -474 211 4205 O ATOM 33 CB GLU A 18 104.649 31.067 195.804 1.00106.81 C ANISOU 33 CB GLU A 18 15032 15931 9621 425 -531 4797 C ATOM 34 CG GLU A 18 103.348 31.724 195.340 1.00111.99 C ANISOU 34 CG GLU A 18 15656 16748 10148 923 -894 5251 C ATOM 35 CD GLU A 18 102.782 32.707 196.357 1.00121.50 C ANISOU 35 CD GLU A 18 16967 17317 11881 1417 -970 5389 C ATOM 36 OE1 GLU A 18 103.456 33.713 196.663 1.00123.30 O ANISOU 36 OE1 GLU A 18 17602 16874 12373 1411 -832 5632 O ATOM 37 OE2 GLU A 18 101.659 32.474 196.853 1.00123.88 O ANISOU 37 OE2 GLU A 18 16932 17801 12335 1802 -1160 5230 O ATOM 38 N ASP A 19 106.706 32.362 197.935 1.00111.52 N ANISOU 38 N ASP A 19 16175 14977 11222 178 24 4572 N ATOM 39 CA ASP A 19 107.428 32.087 199.166 1.00100.08 C ANISOU 39 CA ASP A 19 14680 13156 10189 41 246 4097 C ATOM 40 C ASP A 19 106.620 31.115 200.024 1.00 88.54 C ANISOU 40 C ASP A 19 12831 11923 8886 264 163 3644 C ATOM 41 O ASP A 19 106.946 30.867 201.185 1.00 96.28 O ANISOU 41 O ASP A 19 13746 12625 10211 257 294 3265 O ATOM 42 CB ASP A 19 107.707 33.391 199.924 1.00109.77 C ANISOU 42 CB ASP A 19 16256 13596 11856 189 302 4282 C ATOM 43 CG ASP A 19 106.455 34.239 200.116 1.00126.04 C ANISOU 43 CG ASP A 19 18393 15407 14089 771 42 4588 C ATOM 44 OD1 ASP A 19 105.463 33.727 200.675 1.00131.35 O ANISOU 44 OD1 ASP A 19 18744 16311 14852 1112 -92 4343 O ATOM 45 OD2 ASP A 19 106.459 35.419 199.705 1.00128.79 O ANISOU 45 OD2 ASP A 19 19119 15328 14488 891 -27 5080 O ATOM 46 N ALA A 20 105.561 30.562 199.436 1.00 92.12 N ANISOU 46 N ALA A 20 13024 12912 9066 438 -58 3695 N ATOM 47 CA ALA A 20 104.717 29.585 200.117 1.00 87.36 C ANISOU 47 CA ALA A 20 12030 12592 8571 585 -138 3304 C ATOM 48 C ALA A 20 105.439 28.250 200.270 1.00 92.88 C ANISOU 48 C ALA A 20 12553 13531 9205 183 32 2816 C ATOM 49 O ALA A 20 104.924 27.204 199.882 1.00 75.47 O ANISOU 49 O ALA A 20 10069 11821 6786 93 -66 2608 O ATOM 50 CB ALA A 20 103.405 29.396 199.362 1.00 84.07 C ANISOU 50 CB ALA A 20 11362 12713 7869 836 -436 3496 C ATOM 51 N THR A 21 106.638 28.296 200.838 1.00 92.51 N ANISOU 51 N THR A 21 12671 13120 9360 -50 272 2623 N ATOM 52 CA THR A 21 107.446 27.107 201.042 1.00 81.22 C ANISOU 52 CA THR A 21 11103 11848 7911 -378 432 2168 C ATOM 53 C THR A 21 107.263 26.621 202.476 1.00 86.96 C ANISOU 53 C THR A 21 11688 12343 9011 -254 480 1817 C ATOM 54 O THR A 21 107.379 27.403 203.414 1.00 94.97 O ANISOU 54 O THR A 21 12836 12913 10337 -82 537 1850 O ATOM 55 CB THR A 21 108.940 27.388 200.761 1.00 70.35 C ANISOU 55 CB THR A 21 9937 10297 6496 -717 664 2151 C ATOM 56 OG1 THR A 21 109.077 28.083 199.513 1.00 76.63 O ANISOU 56 OG1 THR A 21 10916 11255 6947 -822 641 2574 O ATOM 57 CG2 THR A 21 109.731 26.098 200.716 1.00 66.74 C ANISOU 57 CG2 THR A 21 9306 10102 5952 -1007 796 1689 C ATOM 58 N PRO A 22 106.963 25.327 202.652 1.00 83.58 N ANISOU 58 N PRO A 22 11006 12210 8542 -351 455 1482 N ATOM 59 CA PRO A 22 106.723 24.778 203.992 1.00 76.62 C ANISOU 59 CA PRO A 22 9993 11155 7965 -256 498 1195 C ATOM 60 C PRO A 22 107.940 24.882 204.908 1.00 71.82 C ANISOU 60 C PRO A 22 9538 10148 7601 -358 691 987 C ATOM 61 O PRO A 22 109.067 24.639 204.474 1.00 71.02 O ANISOU 61 O PRO A 22 9518 10053 7414 -617 808 870 O ATOM 62 CB PRO A 22 106.381 23.311 203.715 1.00 77.61 C ANISOU 62 CB PRO A 22 9879 11658 7950 -445 442 911 C ATOM 63 CG PRO A 22 106.951 23.041 202.367 1.00 77.53 C ANISOU 63 CG PRO A 22 9920 11938 7601 -690 441 917 C ATOM 64 CD PRO A 22 106.818 24.303 201.606 1.00 82.56 C ANISOU 64 CD PRO A 22 10717 12581 8071 -568 381 1351 C ATOM 65 N CYS A 23 107.707 25.256 206.161 1.00 64.06 N ANISOU 65 N CYS A 23 8568 8869 6901 -148 721 926 N ATOM 66 CA CYS A 23 108.767 25.299 207.159 1.00 67.68 C ANISOU 66 CA CYS A 23 9137 8999 7581 -225 868 695 C ATOM 67 C CYS A 23 108.815 23.961 207.890 1.00 61.91 C ANISOU 67 C CYS A 23 8238 8384 6901 -305 892 371 C ATOM 68 O CYS A 23 107.876 23.599 208.595 1.00 63.87 O ANISOU 68 O CYS A 23 8345 8704 7218 -152 843 335 O ATOM 69 CB CYS A 23 108.538 26.452 208.137 1.00 65.09 C ANISOU 69 CB CYS A 23 8940 8289 7501 45 883 772 C ATOM 70 SG CYS A 23 109.870 26.729 209.328 1.00 75.33 S ANISOU 70 SG CYS A 23 10383 9195 9044 -56 1032 489 S ATOM 71 N VAL A 24 109.909 23.227 207.711 1.00 66.55 N ANISOU 71 N VAL A 24 8837 8994 7454 -542 972 146 N ATOM 72 CA VAL A 24 110.011 21.869 208.237 1.00 67.45 C ANISOU 72 CA VAL A 24 8832 9187 7610 -619 972 -134 C ATOM 73 C VAL A 24 110.571 21.820 209.658 1.00 61.21 C ANISOU 73 C VAL A 24 8089 8130 7038 -535 1035 -306 C ATOM 74 O VAL A 24 111.450 22.599 210.024 1.00 60.20 O ANISOU 74 O VAL A 24 8076 7786 7010 -532 1107 -337 O ATOM 75 CB VAL A 24 110.886 20.980 207.328 1.00 65.39 C ANISOU 75 CB VAL A 24 8544 9096 7205 -858 1005 -334 C ATOM 76 CG1 VAL A 24 110.174 20.711 206.011 1.00 49.08 C ANISOU 76 CG1 VAL A 24 6400 7376 4874 -950 916 -232 C ATOM 77 CG2 VAL A 24 112.246 21.624 207.085 1.00 87.74 C ANISOU 77 CG2 VAL A 24 11480 11815 10041 -972 1132 -376 C ATOM 78 N PHE A 25 110.051 20.889 210.452 1.00 52.28 N ANISOU 78 N PHE A 25 6867 7032 5964 -492 1003 -411 N ATOM 79 CA PHE A 25 110.484 20.707 211.836 1.00 47.91 C ANISOU 79 CA PHE A 25 6356 6289 5559 -404 1044 -552 C ATOM 80 C PHE A 25 110.917 19.268 212.087 1.00 44.35 C ANISOU 80 C PHE A 25 5875 5852 5124 -515 1022 -748 C ATOM 81 O PHE A 25 111.000 18.830 213.234 1.00 46.34 O ANISOU 81 O PHE A 25 6150 6003 5455 -441 1024 -814 O ATOM 82 CB PHE A 25 109.363 21.082 212.809 1.00 44.63 C ANISOU 82 CB PHE A 25 5890 5878 5191 -201 1040 -440 C ATOM 83 CG PHE A 25 108.927 22.514 212.715 1.00 53.21 C ANISOU 83 CG PHE A 25 7026 6882 6308 -16 1047 -277 C ATOM 84 CD1 PHE A 25 109.411 23.455 213.604 1.00 50.84 C ANISOU 84 CD1 PHE A 25 6855 6334 6130 123 1100 -345 C ATOM 85 CD2 PHE A 25 108.022 22.917 211.746 1.00 49.10 C ANISOU 85 CD2 PHE A 25 6434 6522 5699 36 982 -65 C ATOM 86 CE1 PHE A 25 109.008 24.771 213.527 1.00 56.49 C ANISOU 86 CE1 PHE A 25 7654 6896 6912 311 1099 -213 C ATOM 87 CE2 PHE A 25 107.618 24.234 211.663 1.00 56.16 C ANISOU 87 CE2 PHE A 25 7404 7290 6646 255 968 106 C ATOM 88 CZ PHE A 25 108.113 25.162 212.556 1.00 66.20 C ANISOU 88 CZ PHE A 25 8832 8247 8074 395 1032 29 C ATOM 89 N THR A 26 111.190 18.540 211.008 1.00 48.43 N ANISOU 89 N THR A 26 6357 6490 5554 -678 997 -840 N ATOM 90 CA THR A 26 111.446 17.104 211.091 1.00 48.94 C ANISOU 90 CA THR A 26 6411 6528 5654 -766 955 -1033 C ATOM 91 C THR A 26 112.678 16.751 211.927 1.00 51.73 C ANISOU 91 C THR A 26 6836 6689 6131 -694 972 -1219 C ATOM 92 O THR A 26 112.682 15.740 212.632 1.00 53.43 O ANISOU 92 O THR A 26 7088 6786 6427 -667 922 -1287 O ATOM 93 CB THR A 26 111.601 16.488 209.684 1.00 50.51 C ANISOU 93 CB THR A 26 6566 6900 5726 -935 929 -1164 C ATOM 94 OG1 THR A 26 112.073 15.139 209.796 1.00 43.13 O ANISOU 94 OG1 THR A 26 5659 5855 4873 -984 890 -1407 O ATOM 95 CG2 THR A 26 112.580 17.297 208.842 1.00 74.01 C ANISOU 95 CG2 THR A 26 9555 9964 8601 -976 1009 -1199 C ATOM 96 N ASP A 27 113.716 17.578 211.856 1.00 52.11 N ANISOU 96 N ASP A 27 6898 6709 6193 -671 1033 -1287 N ATOM 97 CA ASP A 27 114.940 17.316 212.607 1.00 51.65 C ANISOU 97 CA ASP A 27 6854 6533 6240 -595 1028 -1485 C ATOM 98 C ASP A 27 114.797 17.740 214.066 1.00 48.79 C ANISOU 98 C ASP A 27 6550 6040 5947 -443 1007 -1415 C ATOM 99 O ASP A 27 115.349 17.100 214.959 1.00 55.68 O ANISOU 99 O ASP A 27 7447 6830 6879 -344 947 -1521 O ATOM 100 CB ASP A 27 116.129 18.033 211.965 1.00 52.81 C ANISOU 100 CB ASP A 27 6946 6752 6369 -679 1110 -1609 C ATOM 101 CG ASP A 27 115.935 19.533 211.901 1.00 73.04 C ANISOU 101 CG ASP A 27 9556 9283 8915 -720 1178 -1425 C ATOM 102 OD1 ASP A 27 116.880 20.274 212.245 1.00 67.82 O ANISOU 102 OD1 ASP A 27 8888 8557 8323 -750 1225 -1511 O ATOM 103 OD2 ASP A 27 114.836 19.974 211.506 1.00 96.65 O ANISOU 103 OD2 ASP A 27 12588 12302 11835 -719 1174 -1198 O ATOM 104 N VAL A 28 114.057 18.820 214.301 1.00 39.55 N ANISOU 104 N VAL A 28 5406 4864 4756 -402 1047 -1243 N ATOM 105 CA VAL A 28 113.835 19.312 215.657 1.00 41.86 C ANISOU 105 CA VAL A 28 5750 5073 5081 -247 1043 -1213 C ATOM 106 C VAL A 28 113.109 18.268 216.497 1.00 43.32 C ANISOU 106 C VAL A 28 5945 5281 5235 -186 1000 -1143 C ATOM 107 O VAL A 28 113.475 18.011 217.643 1.00 46.72 O ANISOU 107 O VAL A 28 6424 5665 5662 -81 966 -1195 O ATOM 108 CB VAL A 28 113.022 20.624 215.659 1.00 39.94 C ANISOU 108 CB VAL A 28 5534 4808 4832 -175 1096 -1061 C ATOM 109 CG1 VAL A 28 112.751 21.083 217.084 1.00 40.20 C ANISOU 109 CG1 VAL A 28 5612 4787 4875 4 1103 -1089 C ATOM 110 CG2 VAL A 28 113.753 21.702 214.877 1.00 40.69 C ANISOU 110 CG2 VAL A 28 5671 4819 4970 -269 1141 -1078 C ATOM 111 N LEU A 29 112.084 17.662 215.908 1.00 44.61 N ANISOU 111 N LEU A 29 6059 5533 5360 -275 997 -1016 N ATOM 112 CA LEU A 29 111.305 16.629 216.581 1.00 42.93 C ANISOU 112 CA LEU A 29 5850 5337 5125 -296 974 -917 C ATOM 113 C LEU A 29 112.141 15.378 216.837 1.00 44.50 C ANISOU 113 C LEU A 29 6138 5387 5382 -320 895 -1029 C ATOM 114 O LEU A 29 112.023 14.749 217.889 1.00 53.89 O ANISOU 114 O LEU A 29 7403 6514 6557 -272 869 -950 O ATOM 115 CB LEU A 29 110.064 16.270 215.757 1.00 45.02 C ANISOU 115 CB LEU A 29 6007 5747 5352 -440 976 -790 C ATOM 116 CG LEU A 29 108.776 17.061 216.008 1.00 41.46 C ANISOU 116 CG LEU A 29 5433 5482 4839 -367 1034 -616 C ATOM 117 CD1 LEU A 29 108.983 18.555 215.817 1.00 51.12 C ANISOU 117 CD1 LEU A 29 6665 6692 6065 -202 1069 -614 C ATOM 118 CD2 LEU A 29 107.666 16.557 215.099 1.00 42.63 C ANISOU 118 CD2 LEU A 29 5430 5819 4947 -534 1001 -525 C ATOM 119 N ASN A 30 112.986 15.023 215.874 1.00 56.74 N ANISOU 119 N ASN A 30 7681 6890 6986 -377 859 -1205 N ATOM 120 CA ASN A 30 113.839 13.846 216.002 1.00 53.96 C ANISOU 120 CA ASN A 30 7405 6378 6720 -342 771 -1351 C ATOM 121 C ASN A 30 114.931 14.034 217.050 1.00 54.92 C ANISOU 121 C ASN A 30 7565 6436 6864 -149 720 -1435 C ATOM 122 O ASN A 30 115.392 13.068 217.656 1.00 76.05 O ANISOU 122 O ASN A 30 10333 8970 9592 -47 620 -1458 O ATOM 123 CB ASN A 30 114.469 13.494 214.653 1.00 61.11 C ANISOU 123 CB ASN A 30 8255 7308 7657 -422 765 -1572 C ATOM 124 CG ASN A 30 113.465 12.923 213.671 1.00 62.84 C ANISOU 124 CG ASN A 30 8454 7580 7842 -616 764 -1540 C ATOM 125 OD1 ASN A 30 112.472 12.313 214.067 1.00 63.83 O ANISOU 125 OD1 ASN A 30 8624 7644 7985 -703 736 -1390 O ATOM 126 ND2 ASN A 30 113.720 13.118 212.382 1.00 57.43 N ANISOU 126 ND2 ASN A 30 7689 7044 7089 -708 796 -1686 N ATOM 127 N GLN A 31 115.340 15.281 217.257 1.00 49.00 N ANISOU 127 N GLN A 31 6754 5784 6078 -99 772 -1481 N ATOM 128 CA GLN A 31 116.375 15.595 218.234 1.00 46.98 C ANISOU 128 CA GLN A 31 6501 5523 5827 56 710 -1599 C ATOM 129 C GLN A 31 115.786 15.787 219.628 1.00 51.92 C ANISOU 129 C GLN A 31 7213 6167 6349 162 696 -1445 C ATOM 130 O GLN A 31 116.455 15.550 220.633 1.00 53.31 O ANISOU 130 O GLN A 31 7429 6342 6484 308 598 -1495 O ATOM 131 CB GLN A 31 117.144 16.848 217.812 1.00 40.25 C ANISOU 131 CB GLN A 31 5546 4750 4997 7 773 -1753 C ATOM 132 CG GLN A 31 117.986 16.667 216.558 1.00 49.16 C ANISOU 132 CG GLN A 31 6562 5935 6184 -97 804 -1931 C ATOM 133 CD GLN A 31 118.423 17.987 215.953 1.00 49.32 C ANISOU 133 CD GLN A 31 6506 6031 6205 -240 912 -1982 C ATOM 134 OE1 GLN A 31 118.129 19.056 216.488 1.00 56.64 O ANISOU 134 OE1 GLN A 31 7485 6910 7126 -243 944 -1906 O ATOM 135 NE2 GLN A 31 119.125 17.919 214.828 1.00 45.95 N ANISOU 135 NE2 GLN A 31 5966 5713 5781 -365 976 -2114 N ATOM 136 N SER A 32 114.528 16.212 219.681 1.00 40.51 N ANISOU 136 N SER A 32 5775 4781 4838 103 792 -1266 N ATOM 137 CA SER A 32 113.870 16.488 220.953 1.00 42.66 C ANISOU 137 CA SER A 32 6095 5137 4975 200 821 -1141 C ATOM 138 C SER A 32 113.272 15.228 221.572 1.00 51.83 C ANISOU 138 C SER A 32 7347 6278 6068 175 792 -936 C ATOM 139 O SER A 32 113.136 15.135 222.793 1.00 58.39 O ANISOU 139 O SER A 32 8246 7188 6750 270 784 -841 O ATOM 140 CB SER A 32 112.778 17.544 220.768 1.00 50.50 C ANISOU 140 CB SER A 32 7023 6233 5934 187 947 -1061 C ATOM 141 OG SER A 32 113.312 18.742 220.230 1.00 52.86 O ANISOU 141 OG SER A 32 7291 6483 6309 199 971 -1207 O ATOM 142 N LYS A 33 112.916 14.264 220.726 1.00 46.99 N ANISOU 142 N LYS A 33 6744 5560 5552 25 777 -868 N ATOM 143 CA LYS A 33 112.279 13.030 221.185 1.00 49.88 C ANISOU 143 CA LYS A 33 7217 5842 5894 -71 756 -653 C ATOM 144 C LYS A 33 113.104 12.239 222.215 1.00 45.97 C ANISOU 144 C LYS A 33 6893 5215 5360 76 627 -602 C ATOM 145 O LYS A 33 112.554 11.812 223.229 1.00 47.76 O ANISOU 145 O LYS A 33 7220 5481 5447 61 647 -364 O ATOM 146 CB LYS A 33 111.945 12.125 219.992 1.00 53.66 C ANISOU 146 CB LYS A 33 7693 6175 6520 -270 732 -670 C ATOM 147 CG LYS A 33 111.134 10.893 220.371 1.00 74.93 C ANISOU 147 CG LYS A 33 10503 8742 9227 -448 724 -441 C ATOM 148 CD LYS A 33 111.297 9.770 219.358 1.00 78.63 C ANISOU 148 CD LYS A 33 11048 8946 9882 -591 635 -551 C ATOM 149 CE LYS A 33 110.802 10.175 217.981 1.00 83.23 C ANISOU 149 CE LYS A 33 11454 9674 10497 -747 683 -701 C ATOM 150 NZ LYS A 33 110.943 9.060 217.003 1.00 83.02 N ANISOU 150 NZ LYS A 33 11504 9414 10624 -892 596 -864 N ATOM 151 N PRO A 34 114.416 12.031 221.967 1.00 48.20 N ANISOU 151 N PRO A 34 6729 5515 6071 508 606 -1203 N ATOM 152 CA PRO A 34 115.168 11.277 222.979 1.00 49.88 C ANISOU 152 CA PRO A 34 6944 5569 6439 572 663 -1194 C ATOM 153 C PRO A 34 115.265 12.006 224.317 1.00 43.98 C ANISOU 153 C PRO A 34 6008 4844 5861 568 605 -1072 C ATOM 154 O PRO A 34 115.260 11.362 225.367 1.00 44.91 O ANISOU 154 O PRO A 34 6131 4856 6077 568 583 -1068 O ATOM 155 CB PRO A 34 116.558 11.128 222.347 1.00 55.33 C ANISOU 155 CB PRO A 34 7661 6244 7119 747 828 -1183 C ATOM 156 CG PRO A 34 116.337 11.302 220.889 1.00 57.44 C ANISOU 156 CG PRO A 34 8032 6599 7192 742 863 -1245 C ATOM 157 CD PRO A 34 115.250 12.321 220.786 1.00 60.91 C ANISOU 157 CD PRO A 34 8383 7186 7572 628 732 -1196 C ATOM 158 N VAL A 35 115.352 13.331 224.275 1.00 43.76 N ANISOU 158 N VAL A 35 5832 4940 5854 568 595 -975 N ATOM 159 CA VAL A 35 115.422 14.130 225.493 1.00 48.97 C ANISOU 159 CA VAL A 35 6322 5626 6660 545 546 -881 C ATOM 160 C VAL A 35 114.101 14.070 226.254 1.00 47.58 C ANISOU 160 C VAL A 35 6141 5439 6496 421 407 -886 C ATOM 161 O VAL A 35 114.083 13.897 227.473 1.00 38.96 O ANISOU 161 O VAL A 35 4991 4299 5514 408 363 -858 O ATOM 162 CB VAL A 35 115.771 15.599 225.186 1.00 45.69 C ANISOU 162 CB VAL A 35 5784 5313 6261 554 599 -790 C ATOM 163 CG1 VAL A 35 115.797 16.421 226.467 1.00 33.45 C ANISOU 163 CG1 VAL A 35 4078 3776 4855 508 553 -723 C ATOM 164 CG2 VAL A 35 117.105 15.687 224.463 1.00 47.28 C ANISOU 164 CG2 VAL A 35 5969 5534 6462 661 757 -782 C ATOM 165 N THR A 36 112.999 14.208 225.524 1.00 50.39 N ANISOU 165 N THR A 36 6551 5867 6727 337 338 -920 N ATOM 166 CA THR A 36 111.668 14.168 226.120 1.00 30.38 C ANISOU 166 CA THR A 36 3990 3361 4192 213 212 -930 C ATOM 167 C THR A 36 111.378 12.809 226.752 1.00 43.94 C ANISOU 167 C THR A 36 5806 4938 5950 142 193 -1016 C ATOM 168 O THR A 36 110.874 12.731 227.874 1.00 40.23 O ANISOU 168 O THR A 36 5284 4431 5570 84 138 -983 O ATOM 169 CB THR A 36 110.577 14.482 225.077 1.00 42.29 C ANISOU 169 CB THR A 36 5518 5021 5528 152 139 -964 C ATOM 170 OG1 THR A 36 110.828 15.766 224.491 1.00 45.35 O ANISOU 170 OG1 THR A 36 5843 5517 5869 245 182 -857 O ATOM 171 CG2 THR A 36 109.201 14.487 225.725 1.00 39.39 C ANISOU 171 CG2 THR A 36 5081 4719 5165 26 12 -970 C ATOM 172 N LEU A 37 111.702 11.742 226.028 1.00 43.18 N ANISOU 172 N LEU A 37 5871 4751 5785 152 260 -1125 N ATOM 173 CA LEU A 37 111.483 10.383 226.513 1.00 41.59 C ANISOU 173 CA LEU A 37 5813 4370 5618 89 286 -1211 C ATOM 174 C LEU A 37 112.283 10.103 227.780 1.00 46.29 C ANISOU 174 C LEU A 37 6383 4844 6361 203 339 -1120 C ATOM 175 O LEU A 37 111.801 9.430 228.690 1.00 52.39 O ANISOU 175 O LEU A 37 7209 5503 7196 143 329 -1121 O ATOM 176 CB LEU A 37 111.847 9.363 225.433 1.00 41.72 C ANISOU 176 CB LEU A 37 6034 4289 5529 103 382 -1348 C ATOM 177 CG LEU A 37 110.879 9.236 224.255 1.00 50.55 C ANISOU 177 CG LEU A 37 7218 5518 6471 -46 319 -1490 C ATOM 178 CD1 LEU A 37 111.471 8.348 223.174 1.00 38.57 C ANISOU 178 CD1 LEU A 37 5909 3904 4842 -1 433 -1627 C ATOM 179 CD2 LEU A 37 109.540 8.691 224.723 1.00 48.44 C ANISOU 179 CD2 LEU A 37 6963 5233 6207 -271 231 -1580 C ATOM 180 N PHE A 38 113.505 10.625 227.833 1.00 50.63 N ANISOU 180 N PHE A 38 6844 5436 6958 367 399 -1042 N ATOM 181 CA PHE A 38 114.371 10.426 228.989 1.00 53.21 C ANISOU 181 CA PHE A 38 7109 5710 7397 500 435 -958 C ATOM 182 C PHE A 38 113.786 11.083 230.234 1.00 50.20 C ANISOU 182 C PHE A 38 6591 5388 7096 434 333 -880 C ATOM 183 O PHE A 38 113.651 10.443 231.278 1.00 62.17 O ANISOU 183 O PHE A 38 8146 6812 8664 454 329 -848 O ATOM 184 CB PHE A 38 115.773 10.977 228.712 1.00 52.07 C ANISOU 184 CB PHE A 38 6847 5658 7278 662 511 -909 C ATOM 185 CG PHE A 38 116.718 10.847 229.874 1.00 35.47 C ANISOU 185 CG PHE A 38 4636 3571 5270 808 530 -832 C ATOM 186 CD1 PHE A 38 117.406 9.666 230.096 1.00 39.10 C ANISOU 186 CD1 PHE A 38 5207 3918 5730 976 621 -829 C ATOM 187 CD2 PHE A 38 116.921 11.908 230.743 1.00 36.15 C ANISOU 187 CD2 PHE A 38 4513 3792 5429 789 460 -765 C ATOM 188 CE1 PHE A 38 118.277 9.544 231.165 1.00 43.63 C ANISOU 188 CE1 PHE A 38 5664 4551 6364 1143 627 -747 C ATOM 189 CE2 PHE A 38 117.790 11.793 231.812 1.00 30.86 C ANISOU 189 CE2 PHE A 38 3723 3182 4819 921 459 -710 C ATOM 190 CZ PHE A 38 118.469 10.609 232.023 1.00 41.03 C ANISOU 190 CZ PHE A 38 5102 4394 6095 1109 534 -694 C ATOM 191 N LEU A 39 113.441 12.361 230.116 1.00 36.45 N ANISOU 191 N LEU A 39 4706 3788 5355 369 268 -842 N ATOM 192 CA LEU A 39 112.908 13.116 231.244 1.00 41.76 C ANISOU 192 CA LEU A 39 5252 4519 6095 314 184 -774 C ATOM 193 C LEU A 39 111.579 12.547 231.725 1.00 45.69 C ANISOU 193 C LEU A 39 5820 4959 6582 185 120 -796 C ATOM 194 O LEU A 39 111.301 12.546 232.923 1.00 59.17 O ANISOU 194 O LEU A 39 7484 6650 8350 177 85 -744 O ATOM 195 CB LEU A 39 112.749 14.593 230.874 1.00 44.29 C ANISOU 195 CB LEU A 39 5448 4971 6410 277 159 -733 C ATOM 196 CG LEU A 39 114.056 15.350 230.630 1.00 34.85 C ANISOU 196 CG LEU A 39 4154 3834 5255 367 239 -706 C ATOM 197 CD1 LEU A 39 113.789 16.823 230.366 1.00 46.62 C ANISOU 197 CD1 LEU A 39 5559 5407 6749 317 244 -657 C ATOM 198 CD2 LEU A 39 115.005 15.176 231.806 1.00 40.17 C ANISOU 198 CD2 LEU A 39 4729 4514 6019 446 245 -684 C ATOM 199 N TYR A 40 110.765 12.060 230.792 1.00 42.00 N ANISOU 199 N TYR A 40 5452 4476 6027 78 109 -881 N ATOM 200 CA TYR A 40 109.493 11.434 231.145 1.00 39.03 C ANISOU 200 CA TYR A 40 5130 4059 5641 -79 62 -926 C ATOM 201 C TYR A 40 109.710 10.233 232.062 1.00 47.22 C ANISOU 201 C TYR A 40 6296 4903 6743 -58 132 -922 C ATOM 202 O TYR A 40 109.000 10.063 233.053 1.00 58.76 O ANISOU 202 O TYR A 40 7741 6332 8252 -129 108 -884 O ATOM 203 CB TYR A 40 108.727 11.001 229.892 1.00 39.85 C ANISOU 203 CB TYR A 40 5315 4200 5625 -210 43 -1053 C ATOM 204 CG TYR A 40 107.958 12.110 229.204 1.00 31.15 C ANISOU 204 CG TYR A 40 4080 3320 4435 -255 -51 -1039 C ATOM 205 CD1 TYR A 40 108.064 13.428 229.628 1.00 36.84 C ANISOU 205 CD1 TYR A 40 4652 4147 5198 -172 -83 -915 C ATOM 206 CD2 TYR A 40 107.112 11.832 228.137 1.00 41.81 C ANISOU 206 CD2 TYR A 40 5461 4777 5649 -374 -102 -1152 C ATOM 207 CE1 TYR A 40 107.358 14.440 229.001 1.00 50.94 C ANISOU 207 CE1 TYR A 40 6341 6117 6896 -175 -144 -880 C ATOM 208 CE2 TYR A 40 106.402 12.837 227.505 1.00 31.47 C ANISOU 208 CE2 TYR A 40 4026 3698 4235 -372 -188 -1119 C ATOM 209 CZ TYR A 40 106.528 14.138 227.941 1.00 51.30 C ANISOU 209 CZ TYR A 40 6408 6288 6794 -258 -201 -970 C ATOM 210 OH TYR A 40 105.823 15.139 227.314 1.00 55.32 O ANISOU 210 OH TYR A 40 6817 7008 7193 -221 -263 -916 O ATOM 211 N GLY A 41 110.696 9.406 231.726 1.00 46.21 N ANISOU 211 N GLY A 41 6303 4646 6610 60 234 -951 N ATOM 212 CA GLY A 41 111.028 8.245 232.531 1.00 36.52 C ANISOU 212 CA GLY A 41 5227 3219 5431 135 330 -925 C ATOM 213 C GLY A 41 111.579 8.630 233.890 1.00 40.98 C ANISOU 213 C GLY A 41 5677 3827 6066 280 309 -788 C ATOM 214 O GLY A 41 111.324 7.957 234.888 1.00 55.08 O ANISOU 214 O GLY A 41 7546 5497 7885 297 347 -734 O ATOM 215 N VAL A 42 112.337 9.721 233.928 1.00 37.33 N ANISOU 215 N VAL A 42 5030 3536 5618 377 257 -738 N ATOM 216 CA VAL A 42 112.907 10.217 235.175 1.00 45.42 C ANISOU 216 CA VAL A 42 5918 4649 6692 495 220 -638 C ATOM 217 C VAL A 42 111.818 10.767 236.093 1.00 42.68 C ANISOU 217 C VAL A 42 5498 4350 6368 370 136 -600 C ATOM 218 O VAL A 42 111.779 10.449 237.282 1.00 49.73 O ANISOU 218 O VAL A 42 6402 5214 7279 429 136 -530 O ATOM 219 CB VAL A 42 113.962 11.310 234.915 1.00 44.78 C ANISOU 219 CB VAL A 42 5648 4742 6625 579 197 -627 C ATOM 220 CG1 VAL A 42 114.416 11.939 236.224 1.00 45.52 C ANISOU 220 CG1 VAL A 42 5580 4959 6758 651 139 -559 C ATOM 221 CG2 VAL A 42 115.146 10.731 234.158 1.00 41.02 C ANISOU 221 CG2 VAL A 42 5219 4239 6129 734 294 -649 C ATOM 222 N VAL A 43 110.932 11.586 235.534 1.00 37.49 N ANISOU 222 N VAL A 43 4771 3777 5698 217 73 -638 N ATOM 223 CA VAL A 43 109.843 12.176 236.305 1.00 32.29 C ANISOU 223 CA VAL A 43 4033 3180 5056 109 4 -602 C ATOM 224 C VAL A 43 108.894 11.103 236.840 1.00 32.43 C ANISOU 224 C VAL A 43 4177 3068 5077 14 36 -603 C ATOM 225 O VAL A 43 108.441 11.181 237.981 1.00 42.72 O ANISOU 225 O VAL A 43 5450 4377 6405 7 21 -537 O ATOM 226 CB VAL A 43 109.047 13.200 235.464 1.00 35.37 C ANISOU 226 CB VAL A 43 4332 3694 5414 -1 -56 -631 C ATOM 227 CG1 VAL A 43 107.808 13.667 236.213 1.00 37.43 C ANISOU 227 CG1 VAL A 43 4519 4016 5685 -99 -112 -594 C ATOM 228 CG2 VAL A 43 109.925 14.389 235.108 1.00 29.04 C ANISOU 228 CG2 VAL A 43 3418 2993 4622 81 -58 -611 C ATOM 229 N PHE A 44 108.607 10.094 236.023 1.00 28.57 N ANISOU 229 N PHE A 44 3839 2455 4560 -68 95 -685 N ATOM 230 CA PHE A 44 107.726 9.009 236.446 1.00 50.47 C ANISOU 230 CA PHE A 44 6753 5077 7348 -196 158 -706 C ATOM 231 C PHE A 44 108.364 8.160 237.540 1.00 48.10 C ANISOU 231 C PHE A 44 6581 4616 7080 -44 254 -612 C ATOM 232 O PHE A 44 107.674 7.661 238.426 1.00 68.06 O ANISOU 232 O PHE A 44 9174 7055 9632 -108 301 -565 O ATOM 233 CB PHE A 44 107.346 8.120 235.259 1.00 49.19 C ANISOU 233 CB PHE A 44 6738 4809 7143 -340 212 -846 C ATOM 234 CG PHE A 44 106.606 6.871 235.653 1.00 48.64 C ANISOU 234 CG PHE A 44 6848 4534 7101 -489 318 -887 C ATOM 235 CD1 PHE A 44 105.281 6.932 236.055 1.00 36.03 C ANISOU 235 CD1 PHE A 44 5177 2992 5520 -700 287 -906 C ATOM 236 CD2 PHE A 44 107.235 5.637 235.622 1.00 64.75 C ANISOU 236 CD2 PHE A 44 9135 6316 9151 -415 471 -905 C ATOM 237 CE1 PHE A 44 104.597 5.785 236.420 1.00 45.21 C ANISOU 237 CE1 PHE A 44 6505 3954 6717 -868 410 -949 C ATOM 238 CE2 PHE A 44 106.556 4.486 235.986 1.00 54.42 C ANISOU 238 CE2 PHE A 44 8023 4778 7875 -566 604 -942 C ATOM 239 CZ PHE A 44 105.236 4.561 236.385 1.00 37.12 C ANISOU 239 CZ PHE A 44 5753 2642 5709 -808 575 -969 C ATOM 240 N LEU A 45 109.681 7.997 237.474 1.00 40.02 N ANISOU 240 N LEU A 45 5587 3570 6048 171 293 -577 N ATOM 241 CA LEU A 45 110.395 7.168 238.437 1.00 36.19 C ANISOU 241 CA LEU A 45 5220 2962 5567 372 385 -474 C ATOM 242 C LEU A 45 110.404 7.801 239.825 1.00 45.89 C ANISOU 242 C LEU A 45 6316 4322 6799 457 317 -359 C ATOM 243 O LEU A 45 109.912 7.213 240.788 1.00 57.27 O ANISOU 243 O LEU A 45 7858 5662 8241 462 376 -282 O ATOM 244 CB LEU A 45 111.829 6.916 237.967 1.00 47.31 C ANISOU 244 CB LEU A 45 6650 4371 6953 603 434 -465 C ATOM 245 CG LEU A 45 112.645 5.920 238.793 1.00 58.26 C ANISOU 245 CG LEU A 45 8178 5637 8322 862 546 -351 C ATOM 246 CD1 LEU A 45 111.983 4.550 238.781 1.00 40.94 C ANISOU 246 CD1 LEU A 45 6288 3132 6138 793 711 -360 C ATOM 247 CD2 LEU A 45 114.073 5.834 238.278 1.00 60.86 C ANISOU 247 CD2 LEU A 45 8468 6031 8626 1102 579 -344 C ATOM 248 N PHE A 46 110.962 9.003 239.922 1.00 39.46 N ANISOU 248 N PHE A 46 5285 3726 5981 515 206 -355 N ATOM 249 CA PHE A 46 111.082 9.689 241.203 1.00 34.24 C ANISOU 249 CA PHE A 46 4492 3211 5308 593 135 -276 C ATOM 250 C PHE A 46 109.750 10.278 241.659 1.00 41.43 C ANISOU 250 C PHE A 46 5350 4157 6236 408 87 -275 C ATOM 251 O PHE A 46 109.471 10.347 242.856 1.00 59.23 O ANISOU 251 O PHE A 46 7591 6443 8469 449 78 -200 O ATOM 252 CB PHE A 46 112.141 10.790 241.120 1.00 37.85 C ANISOU 252 CB PHE A 46 4742 3878 5762 682 51 -300 C ATOM 253 CG PHE A 46 113.513 10.286 240.772 1.00 58.63 C ANISOU 253 CG PHE A 46 7375 6526 8374 882 96 -293 C ATOM 254 CD1 PHE A 46 114.325 9.724 241.743 1.00 59.61 C ANISOU 254 CD1 PHE A 46 7504 6698 8447 1112 114 -205 C ATOM 255 CD2 PHE A 46 113.990 10.374 239.476 1.00 71.69 C ANISOU 255 CD2 PHE A 46 9022 8171 10046 861 126 -367 C ATOM 256 CE1 PHE A 46 115.585 9.259 241.427 1.00 71.02 C ANISOU 256 CE1 PHE A 46 8927 8189 9867 1324 159 -190 C ATOM 257 CE2 PHE A 46 115.250 9.910 239.153 1.00 79.46 C ANISOU 257 CE2 PHE A 46 9996 9184 11012 1057 181 -358 C ATOM 258 CZ PHE A 46 116.049 9.352 240.131 1.00 81.48 C ANISOU 258 CZ PHE A 46 10239 9497 11225 1291 197 -269 C ATOM 259 N GLY A 47 108.931 10.697 240.699 1.00 39.41 N ANISOU 259 N GLY A 47 5059 3914 6002 222 58 -355 N ATOM 260 CA GLY A 47 107.653 11.314 241.003 1.00 27.39 C ANISOU 260 CA GLY A 47 3459 2458 4490 64 13 -355 C ATOM 261 C GLY A 47 106.654 10.354 241.618 1.00 39.03 C ANISOU 261 C GLY A 47 5055 3803 5973 -35 90 -320 C ATOM 262 O GLY A 47 105.903 10.725 242.518 1.00 43.41 O ANISOU 262 O GLY A 47 5550 4416 6529 -77 76 -267 O ATOM 263 N SER A 48 106.642 9.116 241.134 1.00 32.12 N ANISOU 263 N SER A 48 4361 2740 5105 -78 190 -354 N ATOM 264 CA SER A 48 105.724 8.111 241.656 1.00 45.02 C ANISOU 264 CA SER A 48 6137 4212 6758 -202 300 -331 C ATOM 265 C SER A 48 106.185 7.608 243.019 1.00 54.31 C ANISOU 265 C SER A 48 7416 5304 7916 -18 378 -190 C ATOM 266 O SER A 48 105.369 7.372 243.909 1.00 62.17 O ANISOU 266 O SER A 48 8445 6259 8917 -87 437 -124 O ATOM 267 CB SER A 48 105.589 6.941 240.679 1.00 36.71 C ANISOU 267 CB SER A 48 5274 2957 5718 -325 406 -432 C ATOM 268 OG SER A 48 106.850 6.359 240.402 1.00 59.98 O ANISOU 268 OG SER A 48 8358 5785 8648 -123 469 -416 O ATOM 269 N ILE A 49 107.495 7.447 243.179 1.00 40.54 N ANISOU 269 N ILE A 49 5711 3554 6137 227 383 -138 N ATOM 270 CA ILE A 49 108.061 7.002 244.447 1.00 32.56 C ANISOU 270 CA ILE A 49 4783 2512 5076 453 441 6 C ATOM 271 C ILE A 49 107.900 8.067 245.525 1.00 40.37 C ANISOU 271 C ILE A 49 5593 3720 6027 497 333 62 C ATOM 272 O ILE A 49 107.421 7.784 246.624 1.00 36.58 O ANISOU 272 O ILE A 49 5177 3208 5512 528 391 162 O ATOM 273 CB ILE A 49 109.556 6.650 244.308 1.00 39.01 C ANISOU 273 CB ILE A 49 5638 3335 5850 729 453 43 C ATOM 274 CG1 ILE A 49 109.733 5.398 243.448 1.00 35.62 C ANISOU 274 CG1 ILE A 49 5449 2641 5445 731 607 11 C ATOM 275 CG2 ILE A 49 110.183 6.435 245.677 1.00 36.30 C ANISOU 275 CG2 ILE A 49 5315 3057 5419 997 469 196 C ATOM 276 CD1 ILE A 49 109.106 4.156 244.042 1.00 72.10 C ANISOU 276 CD1 ILE A 49 10341 6982 10070 710 798 94 C ATOM 277 N GLY A 50 108.299 9.292 245.199 1.00 39.04 N ANISOU 277 N GLY A 50 5216 3759 5860 495 193 -7 N ATOM 278 CA GLY A 50 108.250 10.395 246.141 1.00 47.04 C ANISOU 278 CA GLY A 50 6068 4971 6835 529 96 15 C ATOM 279 C GLY A 50 106.850 10.730 246.614 1.00 49.16 C ANISOU 279 C GLY A 50 6314 5243 7121 361 109 29 C ATOM 280 O GLY A 50 106.642 11.039 247.787 1.00 50.99 O ANISOU 280 O GLY A 50 6521 5554 7299 424 101 96 O ATOM 281 N ASN A 51 105.884 10.669 245.704 1.00 36.65 N ANISOU 281 N ASN A 51 4729 3596 5600 152 129 -37 N ATOM 282 CA ASN A 51 104.505 10.995 246.042 1.00 39.68 C ANISOU 282 CA ASN A 51 5055 4018 6003 -11 142 -29 C ATOM 283 C ASN A 51 103.781 9.830 246.707 1.00 49.46 C ANISOU 283 C ASN A 51 6453 5095 7246 -73 285 47 C ATOM 284 O ASN A 51 102.771 10.024 247.383 1.00 57.38 O ANISOU 284 O ASN A 51 7412 6140 8249 -161 319 88 O ATOM 285 CB ASN A 51 103.746 11.448 244.797 1.00 38.96 C ANISOU 285 CB ASN A 51 4864 3982 5958 -197 94 -131 C ATOM 286 CG ASN A 51 104.215 12.798 244.293 1.00 42.64 C ANISOU 286 CG ASN A 51 5176 4607 6418 -142 -18 -178 C ATOM 287 OD1 ASN A 51 103.747 13.839 244.751 1.00 54.65 O ANISOU 287 OD1 ASN A 51 6582 6253 7931 -141 -60 -163 O ATOM 288 ND2 ASN A 51 105.150 12.787 243.350 1.00 25.64 N ANISOU 288 ND2 ASN A 51 3036 2436 4269 -93 -46 -235 N ATOM 289 N PHE A 52 104.295 8.620 246.513 1.00 45.20 N ANISOU 289 N PHE A 52 6107 4356 6709 -23 389 69 N ATOM 290 CA PHE A 52 103.779 7.466 247.236 1.00 43.95 C ANISOU 290 CA PHE A 52 6145 4002 6553 -53 562 160 C ATOM 291 C PHE A 52 104.216 7.538 248.693 1.00 52.33 C ANISOU 291 C PHE A 52 7244 5115 7525 178 582 310 C ATOM 292 O PHE A 52 103.422 7.295 249.600 1.00 49.15 O ANISOU 292 O PHE A 52 6893 4676 7105 133 678 396 O ATOM 293 CB PHE A 52 104.254 6.156 246.605 1.00 34.76 C ANISOU 293 CB PHE A 52 5215 2577 5414 -43 695 145 C ATOM 294 CG PHE A 52 104.033 4.950 247.476 1.00 41.58 C ANISOU 294 CG PHE A 52 6330 3200 6267 0 905 272 C ATOM 295 CD1 PHE A 52 102.776 4.378 247.584 1.00 52.18 C ANISOU 295 CD1 PHE A 52 7748 4407 7671 -264 1045 256 C ATOM 296 CD2 PHE A 52 105.081 4.392 248.190 1.00 38.18 C ANISOU 296 CD2 PHE A 52 6057 2690 5759 309 974 413 C ATOM 297 CE1 PHE A 52 102.570 3.270 248.388 1.00 40.92 C ANISOU 297 CE1 PHE A 52 6576 2731 6240 -234 1272 382 C ATOM 298 CE2 PHE A 52 104.881 3.286 248.995 1.00 40.60 C ANISOU 298 CE2 PHE A 52 6623 2759 6043 378 1191 555 C ATOM 299 CZ PHE A 52 103.624 2.724 249.094 1.00 41.96 C ANISOU 299 CZ PHE A 52 6896 2758 6289 98 1352 541 C ATOM 300 N LEU A 53 105.485 7.878 248.903 1.00 45.84 N ANISOU 300 N LEU A 53 6383 4402 6634 422 492 335 N ATOM 301 CA LEU A 53 106.043 7.995 250.246 1.00 45.57 C ANISOU 301 CA LEU A 53 6360 4474 6481 664 480 458 C ATOM 302 C LEU A 53 105.339 9.083 251.051 1.00 51.61 C ANISOU 302 C LEU A 53 6969 5428 7212 602 405 455 C ATOM 303 O LEU A 53 105.220 8.981 252.271 1.00 52.21 O ANISOU 303 O LEU A 53 7099 5546 7192 723 450 565 O ATOM 304 CB LEU A 53 107.545 8.277 250.178 1.00 39.85 C ANISOU 304 CB LEU A 53 5560 3893 5689 905 370 447 C ATOM 305 CG LEU A 53 108.434 7.112 249.737 1.00 37.89 C ANISOU 305 CG LEU A 53 5485 3478 5432 1076 467 499 C ATOM 306 CD1 LEU A 53 109.884 7.552 249.629 1.00 34.63 C ANISOU 306 CD1 LEU A 53 4930 3272 4956 1299 342 473 C ATOM 307 CD2 LEU A 53 108.297 5.945 250.701 1.00 37.24 C ANISOU 307 CD2 LEU A 53 5649 3223 5276 1236 644 678 C ATOM 308 N VAL A 54 104.878 10.123 250.362 1.00 52.01 N ANISOU 308 N VAL A 54 6842 5591 7330 434 302 334 N ATOM 309 CA VAL A 54 104.107 11.181 251.003 1.00 43.29 C ANISOU 309 CA VAL A 54 5604 4640 6205 371 254 323 C ATOM 310 C VAL A 54 102.802 10.626 251.556 1.00 47.74 C ANISOU 310 C VAL A 54 6243 5111 6785 247 393 401 C ATOM 311 O VAL A 54 102.517 10.755 252.745 1.00 51.20 O ANISOU 311 O VAL A 54 6704 5608 7142 329 435 488 O ATOM 312 CB VAL A 54 103.793 12.330 250.026 1.00 34.35 C ANISOU 312 CB VAL A 54 4292 3613 5145 231 149 197 C ATOM 313 CG1 VAL A 54 102.701 13.227 250.590 1.00 27.87 C ANISOU 313 CG1 VAL A 54 3367 2902 4318 153 149 201 C ATOM 314 CG2 VAL A 54 105.047 13.130 249.729 1.00 42.35 C ANISOU 314 CG2 VAL A 54 5212 4742 6136 345 28 122 C ATOM 315 N ILE A 55 102.020 10.001 250.683 1.00 47.36 N ANISOU 315 N ILE A 55 6229 4930 6836 38 468 361 N ATOM 316 CA ILE A 55 100.740 9.422 251.069 1.00 44.79 C ANISOU 316 CA ILE A 55 5952 4520 6546 -132 614 412 C ATOM 317 C ILE A 55 100.934 8.315 252.100 1.00 34.88 C ANISOU 317 C ILE A 55 4926 3095 5231 -13 782 562 C ATOM 318 O ILE A 55 100.161 8.196 253.049 1.00 35.90 O ANISOU 318 O ILE A 55 5085 3226 5330 -38 892 655 O ATOM 319 CB ILE A 55 99.989 8.868 249.840 1.00 40.76 C ANISOU 319 CB ILE A 55 5430 3913 6146 -400 657 308 C ATOM 320 CG1 ILE A 55 99.765 9.981 248.814 1.00 31.68 C ANISOU 320 CG1 ILE A 55 4057 2952 5029 -483 494 182 C ATOM 321 CG2 ILE A 55 98.663 8.245 250.250 1.00 35.18 C ANISOU 321 CG2 ILE A 55 4747 3135 5484 -611 819 344 C ATOM 322 CD1 ILE A 55 99.056 9.525 247.557 1.00 40.59 C ANISOU 322 CD1 ILE A 55 5146 4048 6231 -732 504 64 C ATOM 323 N PHE A 56 101.983 7.520 251.916 1.00 35.61 N ANISOU 323 N PHE A 56 5185 3047 5299 140 815 598 N ATOM 324 CA PHE A 56 102.275 6.407 252.812 1.00 37.83 C ANISOU 324 CA PHE A 56 5716 3147 5510 301 991 761 C ATOM 325 C PHE A 56 102.608 6.881 254.227 1.00 38.02 C ANISOU 325 C PHE A 56 5726 3341 5380 548 958 887 C ATOM 326 O PHE A 56 102.268 6.221 255.205 1.00 43.87 O ANISOU 326 O PHE A 56 6632 3983 6054 622 1123 1039 O ATOM 327 CB PHE A 56 103.430 5.572 252.253 1.00 45.26 C ANISOU 327 CB PHE A 56 6821 3932 6444 464 1021 774 C ATOM 328 CG PHE A 56 103.739 4.343 253.059 1.00 53.87 C ANISOU 328 CG PHE A 56 8203 4803 7463 658 1230 959 C ATOM 329 CD1 PHE A 56 102.899 3.243 253.019 1.00 50.53 C ANISOU 329 CD1 PHE A 56 8003 4080 7117 477 1476 1004 C ATOM 330 CD2 PHE A 56 104.877 4.282 253.847 1.00 54.42 C ANISOU 330 CD2 PHE A 56 8325 4973 7380 1025 1190 1087 C ATOM 331 CE1 PHE A 56 103.182 2.109 253.756 1.00 56.56 C ANISOU 331 CE1 PHE A 56 9070 4607 7814 670 1702 1192 C ATOM 332 CE2 PHE A 56 105.167 3.150 254.586 1.00 55.39 C ANISOU 332 CE2 PHE A 56 8729 4900 7416 1248 1393 1283 C ATOM 333 CZ PHE A 56 104.318 2.062 254.541 1.00 62.68 C ANISOU 333 CZ PHE A 56 9907 5483 8424 1078 1662 1344 C ATOM 334 N THR A 57 103.265 8.031 254.329 1.00 36.30 N ANISOU 334 N THR A 57 5318 3377 5099 664 756 816 N ATOM 335 CA THR A 57 103.703 8.552 255.620 1.00 40.25 C ANISOU 335 CA THR A 57 5790 4073 5431 892 697 896 C ATOM 336 C THR A 57 102.540 9.094 256.455 1.00 51.62 C ANISOU 336 C THR A 57 7176 5593 6846 790 749 926 C ATOM 337 O THR A 57 102.509 8.926 257.675 1.00 56.11 O ANISOU 337 O THR A 57 7836 6212 7272 951 818 1053 O ATOM 338 CB THR A 57 104.759 9.664 255.437 1.00 43.88 C ANISOU 338 CB THR A 57 6055 4779 5840 1001 474 774 C ATOM 339 OG1 THR A 57 105.873 9.147 254.700 1.00 35.23 O ANISOU 339 OG1 THR A 57 4992 3631 4761 1113 436 755 O ATOM 340 CG2 THR A 57 105.248 10.177 256.781 1.00 58.92 C ANISOU 340 CG2 THR A 57 7926 6909 7553 1220 404 825 C ATOM 341 N ILE A 58 101.578 9.729 255.791 1.00 54.83 N ANISOU 341 N ILE A 58 7435 6024 7376 542 724 818 N ATOM 342 CA ILE A 58 100.477 10.394 256.484 1.00 42.11 C ANISOU 342 CA ILE A 58 5734 4519 5746 457 765 833 C ATOM 343 C ILE A 58 99.258 9.482 256.663 1.00 37.05 C ANISOU 343 C ILE A 58 5191 3713 5172 281 982 925 C ATOM 344 O ILE A 58 98.266 9.870 257.279 1.00 86.30 O ANISOU 344 O ILE A 58 11361 10032 11397 210 1053 958 O ATOM 345 CB ILE A 58 100.046 11.675 255.728 1.00 36.28 C ANISOU 345 CB ILE A 58 4766 3928 5091 316 629 682 C ATOM 346 CG1 ILE A 58 101.263 12.373 255.121 1.00 33.34 C ANISOU 346 CG1 ILE A 58 4312 3645 4709 412 448 569 C ATOM 347 CG2 ILE A 58 99.309 12.637 256.648 1.00 46.73 C ANISOU 347 CG2 ILE A 58 5997 5412 6347 337 638 693 C ATOM 348 CD1 ILE A 58 100.926 13.648 254.379 1.00 35.13 C ANISOU 348 CD1 ILE A 58 4350 3988 5008 302 340 439 C ATOM 349 N THR A 59 99.333 8.264 256.138 1.00 50.40 N ANISOU 349 N THR A 59 7046 5168 6936 205 1106 960 N ATOM 350 CA THR A 59 98.173 7.375 256.157 1.00 44.82 C ANISOU 350 CA THR A 59 6426 4285 6319 -24 1327 1012 C ATOM 351 C THR A 59 98.420 6.060 256.897 1.00 47.16 C ANISOU 351 C THR A 59 7026 4335 6557 90 1555 1189 C ATOM 352 O THR A 59 97.537 5.567 257.602 1.00 57.64 O ANISOU 352 O THR A 59 8442 5573 7885 -1 1762 1295 O ATOM 353 CB THR A 59 97.704 7.047 254.724 1.00 53.85 C ANISOU 353 CB THR A 59 7500 5333 7629 -315 1320 862 C ATOM 354 OG1 THR A 59 97.535 8.262 253.983 1.00 59.39 O ANISOU 354 OG1 THR A 59 7936 6262 8366 -380 1114 720 O ATOM 355 CG2 THR A 59 96.387 6.283 254.747 1.00 72.72 C ANISOU 355 CG2 THR A 59 9919 7595 10115 -607 1535 876 C ATOM 356 N TRP A 60 99.615 5.498 256.738 1.00 43.12 N ANISOU 356 N TRP A 60 6676 3714 5992 302 1534 1230 N ATOM 357 CA TRP A 60 99.905 4.158 257.246 1.00 52.40 C ANISOU 357 CA TRP A 60 8173 4615 7122 431 1771 1405 C ATOM 358 C TRP A 60 99.750 4.047 258.758 1.00 62.74 C ANISOU 358 C TRP A 60 9602 5969 8266 639 1898 1609 C ATOM 359 O TRP A 60 98.789 3.457 259.247 1.00 76.55 O ANISOU 359 O TRP A 60 11472 7564 10048 496 2137 1706 O ATOM 360 CB TRP A 60 101.318 3.734 256.846 1.00 55.72 C ANISOU 360 CB TRP A 60 8712 4972 7489 690 1701 1422 C ATOM 361 CG TRP A 60 101.677 2.341 257.266 1.00 56.86 C ANISOU 361 CG TRP A 60 9210 4811 7585 863 1958 1610 C ATOM 362 CD1 TRP A 60 102.441 1.977 258.337 1.00 50.66 C ANISOU 362 CD1 TRP A 60 8592 4051 6605 1246 2016 1818 C ATOM 363 CD2 TRP A 60 101.291 1.125 256.616 1.00 52.64 C ANISOU 363 CD2 TRP A 60 8918 3896 7186 669 2205 1608 C ATOM 364 NE1 TRP A 60 102.553 0.609 258.393 1.00 53.63 N ANISOU 364 NE1 TRP A 60 9315 4070 6992 1328 2298 1970 N ATOM 365 CE2 TRP A 60 101.856 0.063 257.348 1.00 53.91 C ANISOU 365 CE2 TRP A 60 9413 3832 7237 963 2427 1835 C ATOM 366 CE3 TRP A 60 100.520 0.832 255.488 1.00 57.04 C ANISOU 366 CE3 TRP A 60 9447 4288 7937 274 2263 1428 C ATOM 367 CZ2 TRP A 60 101.676 -1.271 256.988 1.00 69.76 C ANISOU 367 CZ2 TRP A 60 11717 5458 9330 861 2702 1861 C ATOM 368 CZ3 TRP A 60 100.343 -0.491 255.131 1.00 60.41 C ANISOU 368 CZ3 TRP A 60 10184 4317 8453 153 2543 1455 C ATOM 369 CH2 TRP A 60 100.918 -1.526 255.878 1.00 56.56 C ANISOU 369 CH2 TRP A 60 10006 3631 7855 441 2747 1652 C ATOM 370 N ARG A 61 100.700 4.613 259.493 1.00 76.83 N ANISOU 370 N ARG A 61 11349 7980 9864 968 1743 1667 N ATOM 371 CA ARG A 61 100.707 4.515 260.948 1.00 85.74 C ANISOU 371 CA ARG A 61 12600 9189 10789 1216 1840 1861 C ATOM 372 C ARG A 61 99.836 5.590 261.596 1.00 72.66 C ANISOU 372 C ARG A 61 10747 7767 9092 1115 1780 1813 C ATOM 373 O ARG A 61 98.888 5.281 262.316 1.00 70.81 O ANISOU 373 O ARG A 61 10601 7462 8842 1039 1987 1928 O ATOM 374 CB ARG A 61 102.144 4.606 261.471 1.00102.01 C ANISOU 374 CB ARG A 61 14694 11426 12638 1623 1692 1932 C ATOM 375 CG ARG A 61 102.282 4.438 262.973 1.00 95.67 C ANISOU 375 CG ARG A 61 14032 10738 11581 1928 1778 2140 C ATOM 376 CD ARG A 61 103.749 4.450 263.377 1.00 99.62 C ANISOU 376 CD ARG A 61 14537 11449 11864 2332 1615 2197 C ATOM 377 NE ARG A 61 103.926 4.309 264.819 1.00123.30 N ANISOU 377 NE ARG A 61 17661 14605 14582 2652 1676 2393 N ATOM 378 CZ ARG A 61 105.104 4.255 265.433 1.00128.47 C ANISOU 378 CZ ARG A 61 18326 15496 14989 3044 1554 2477 C ATOM 379 NH1 ARG A 61 106.227 4.328 264.733 1.00122.34 N ANISOU 379 NH1 ARG A 61 17432 14823 14230 3158 1372 2382 N ATOM 380 NH2 ARG A 61 105.157 4.125 266.751 1.00125.34 N ANISOU 380 NH2 ARG A 61 18046 15258 14318 3328 1614 2657 N ATOM 381 N ARG A 62 100.168 6.851 261.340 1.00 75.60 N ANISOU 381 N ARG A 62 10865 8409 9450 1118 1518 1645 N ATOM 382 CA ARG A 62 99.385 7.968 261.856 1.00 72.57 C ANISOU 382 CA ARG A 62 10299 8240 9035 1034 1458 1579 C ATOM 383 C ARG A 62 98.355 8.423 260.833 1.00 88.67 C ANISOU 383 C ARG A 62 12147 10252 11292 692 1445 1430 C ATOM 384 O ARG A 62 98.637 8.457 259.639 1.00113.55 O ANISOU 384 O ARG A 62 15216 13351 14579 567 1340 1303 O ATOM 385 CB ARG A 62 100.301 9.136 262.242 1.00 59.59 C ANISOU 385 CB ARG A 62 8508 6893 7239 1231 1206 1476 C ATOM 386 N ARG A 63 97.163 8.772 261.307 1.00 82.27 N ANISOU 386 N ARG A 63 11257 9501 10499 559 1552 1452 N ATOM 387 CA ARG A 63 96.096 9.232 260.426 1.00 78.00 C ANISOU 387 CA ARG A 63 10506 8991 10141 263 1542 1326 C ATOM 388 C ARG A 63 96.272 10.701 260.048 1.00 65.84 C ANISOU 388 C ARG A 63 8734 7683 8598 290 1310 1167 C ATOM 389 O ARG A 63 97.305 11.307 260.335 1.00 52.44 O ANISOU 389 O ARG A 63 7041 6099 6785 494 1152 1126 O ATOM 390 CB ARG A 63 94.732 9.019 261.085 1.00 72.26 C ANISOU 390 CB ARG A 63 9763 8258 9434 120 1764 1418 C ATOM 391 N ILE A 64 95.258 11.268 259.402 1.00 57.94 N ANISOU 391 N ILE A 64 7531 6759 7722 84 1300 1078 N ATOM 392 CA ILE A 64 95.279 12.678 259.032 1.00 47.78 C ANISOU 392 CA ILE A 64 6048 5665 6440 114 1123 948 C ATOM 393 C ILE A 64 94.992 13.538 260.259 1.00 60.91 C ANISOU 393 C ILE A 64 7697 7486 7961 267 1152 987 C ATOM 394 O ILE A 64 93.954 13.388 260.904 1.00 68.82 O ANISOU 394 O ILE A 64 8684 8516 8951 216 1317 1073 O ATOM 395 CB ILE A 64 94.257 12.997 257.917 1.00 48.49 C ANISOU 395 CB ILE A 64 5925 5809 6690 -118 1108 859 C ATOM 396 CG1 ILE A 64 94.758 12.497 256.558 1.00 54.66 C ANISOU 396 CG1 ILE A 64 6703 6482 7584 -240 1015 767 C ATOM 397 CG2 ILE A 64 93.997 14.494 257.842 1.00 62.80 C ANISOU 397 CG2 ILE A 64 7562 7817 8483 -47 998 777 C ATOM 398 CD1 ILE A 64 94.528 11.019 256.307 1.00 70.91 C ANISOU 398 CD1 ILE A 64 8895 8332 9716 -407 1167 816 C ATOM 399 N GLN A 65 95.919 14.436 260.579 1.00 57.45 N ANISOU 399 N GLN A 65 7262 7154 7413 443 1001 910 N ATOM 400 CA GLN A 65 95.810 15.251 261.783 1.00 59.86 C ANISOU 400 CA GLN A 65 7584 7603 7556 598 1020 919 C ATOM 401 C GLN A 65 95.200 16.622 261.506 1.00 60.96 C ANISOU 401 C GLN A 65 7557 7864 7742 564 974 808 C ATOM 402 O GLN A 65 94.142 16.957 262.037 1.00 71.72 O ANISOU 402 O GLN A 65 8867 9296 9086 555 1099 856 O ATOM 403 CB GLN A 65 97.184 15.418 262.435 1.00 65.41 C ANISOU 403 CB GLN A 65 8397 8373 8085 806 894 885 C ATOM 404 N CYS A 66 95.872 17.413 260.676 1.00 65.04 N ANISOU 404 N CYS A 66 7999 8398 8314 557 813 670 N ATOM 405 CA CYS A 66 95.431 18.776 260.402 1.00 49.98 C ANISOU 405 CA CYS A 66 5972 6577 6440 559 783 570 C ATOM 406 C CYS A 66 94.941 18.947 258.968 1.00 50.17 C ANISOU 406 C CYS A 66 5846 6576 6642 418 743 533 C ATOM 407 O CYS A 66 94.904 17.991 258.193 1.00 49.74 O ANISOU 407 O CYS A 66 5772 6443 6682 294 737 565 O ATOM 408 CB CYS A 66 96.563 19.766 260.682 1.00 52.95 C ANISOU 408 CB CYS A 66 6396 7001 6722 669 655 431 C ATOM 409 SG CYS A 66 98.023 19.545 259.638 1.00 42.32 S ANISOU 409 SG CYS A 66 5047 5589 5443 633 476 335 S ATOM 410 N SER A 67 94.568 20.177 258.626 1.00 46.52 N ANISOU 410 N SER A 67 5289 6179 6208 448 726 463 N ATOM 411 CA SER A 67 94.086 20.495 257.287 1.00 50.44 C ANISOU 411 CA SER A 67 5637 6688 6838 359 685 436 C ATOM 412 C SER A 67 95.213 20.422 256.264 1.00 60.92 C ANISOU 412 C SER A 67 6989 7932 8224 318 543 351 C ATOM 413 O SER A 67 94.975 20.179 255.081 1.00 50.52 O ANISOU 413 O SER A 67 5580 6608 7008 218 500 344 O ATOM 414 CB SER A 67 93.447 21.885 257.266 1.00 44.76 C ANISOU 414 CB SER A 67 4842 6050 6114 456 727 406 C ATOM 415 OG SER A 67 94.391 22.882 257.614 1.00 49.42 O ANISOU 415 OG SER A 67 5543 6597 6639 558 677 298 O ATOM 416 N GLY A 68 96.440 20.637 256.728 1.00 54.23 N ANISOU 416 N GLY A 68 6255 7046 7303 394 470 281 N ATOM 417 CA GLY A 68 97.604 20.571 255.866 1.00 28.33 C ANISOU 417 CA GLY A 68 2993 3702 4071 365 347 201 C ATOM 418 C GLY A 68 97.824 19.177 255.315 1.00 28.30 C ANISOU 418 C GLY A 68 3010 3622 4119 280 329 256 C ATOM 419 O GLY A 68 98.221 19.011 254.162 1.00 67.71 O ANISOU 419 O GLY A 68 7967 8566 9195 212 259 213 O ATOM 420 N ASP A 69 97.560 18.172 256.144 1.00 47.96 N ANISOU 420 N ASP A 69 5580 6089 6555 287 410 353 N ATOM 421 CA ASP A 69 97.707 16.779 255.738 1.00 43.78 C ANISOU 421 CA ASP A 69 5114 5447 6073 209 436 413 C ATOM 422 C ASP A 69 96.753 16.436 254.600 1.00 36.28 C ANISOU 422 C ASP A 69 4057 4476 5254 28 464 409 C ATOM 423 O ASP A 69 97.102 15.680 253.694 1.00 44.44 O ANISOU 423 O ASP A 69 5115 5416 6354 -60 433 384 O ATOM 424 CB ASP A 69 97.466 15.847 256.927 1.00 36.65 C ANISOU 424 CB ASP A 69 4338 4506 5082 259 560 538 C ATOM 425 CG ASP A 69 98.530 15.983 257.999 1.00 54.09 C ANISOU 425 CG ASP A 69 6658 6764 7132 454 513 544 C ATOM 426 OD1 ASP A 69 99.226 17.019 258.017 1.00 80.65 O ANISOU 426 OD1 ASP A 69 9972 10218 10452 524 398 432 O ATOM 427 OD2 ASP A 69 98.668 15.056 258.824 1.00 51.75 O ANISOU 427 OD2 ASP A 69 6496 6422 6744 536 597 658 O ATOM 428 N VAL A 70 95.551 17.000 254.655 1.00 37.39 N ANISOU 428 N VAL A 70 4070 4722 5416 -18 523 428 N ATOM 429 CA VAL A 70 94.553 16.792 253.613 1.00 30.55 C ANISOU 429 CA VAL A 70 3054 3907 4649 -182 535 414 C ATOM 430 C VAL A 70 95.050 17.314 252.270 1.00 36.88 C ANISOU 430 C VAL A 70 3790 4720 5501 -195 403 321 C ATOM 431 O VAL A 70 94.939 16.638 251.247 1.00 47.54 O ANISOU 431 O VAL A 70 5105 6042 6914 -332 373 283 O ATOM 432 CB VAL A 70 93.222 17.483 253.964 1.00 31.43 C ANISOU 432 CB VAL A 70 3007 4180 4754 -179 615 455 C ATOM 433 CG1 VAL A 70 92.229 17.344 252.819 1.00 38.00 C ANISOU 433 CG1 VAL A 70 3643 5127 5669 -335 599 428 C ATOM 434 CG2 VAL A 70 92.650 16.906 255.249 1.00 37.88 C ANISOU 434 CG2 VAL A 70 3884 4988 5521 -182 769 555 C ATOM 435 N TYR A 71 95.611 18.517 252.285 1.00 30.25 N ANISOU 435 N TYR A 71 2948 3916 4628 -58 338 277 N ATOM 436 CA TYR A 71 96.089 19.155 251.066 1.00 29.22 C ANISOU 436 CA TYR A 71 2771 3793 4539 -50 239 205 C ATOM 437 C TYR A 71 97.370 18.504 250.548 1.00 45.80 C ANISOU 437 C TYR A 71 4975 5771 6656 -71 165 152 C ATOM 438 O TYR A 71 97.613 18.478 249.342 1.00 54.62 O ANISOU 438 O TYR A 71 6057 6878 7818 -123 103 104 O ATOM 439 CB TYR A 71 96.313 20.648 251.308 1.00 26.63 C ANISOU 439 CB TYR A 71 2438 3504 4177 91 232 175 C ATOM 440 CG TYR A 71 95.060 21.398 251.703 1.00 40.18 C ANISOU 440 CG TYR A 71 4054 5338 5873 150 317 230 C ATOM 441 CD1 TYR A 71 93.825 21.059 251.164 1.00 38.32 C ANISOU 441 CD1 TYR A 71 3661 5228 5670 74 345 281 C ATOM 442 CD2 TYR A 71 95.111 22.439 252.619 1.00 28.68 C ANISOU 442 CD2 TYR A 71 2654 3884 4358 281 373 221 C ATOM 443 CE1 TYR A 71 92.677 21.741 251.522 1.00 40.49 C ANISOU 443 CE1 TYR A 71 3820 5641 5922 152 428 341 C ATOM 444 CE2 TYR A 71 93.969 23.126 252.985 1.00 32.68 C ANISOU 444 CE2 TYR A 71 3079 4495 4843 362 469 277 C ATOM 445 CZ TYR A 71 92.755 22.773 252.434 1.00 45.05 C ANISOU 445 CZ TYR A 71 4472 6199 6444 309 496 347 C ATOM 446 OH TYR A 71 91.616 23.456 252.796 1.00 38.90 O ANISOU 446 OH TYR A 71 3588 5553 5640 412 596 412 O ATOM 447 N PHE A 72 98.184 17.978 251.458 1.00 27.89 N ANISOU 447 N PHE A 72 2833 3427 4339 -11 176 168 N ATOM 448 CA PHE A 72 99.416 17.295 251.072 1.00 26.25 C ANISOU 448 CA PHE A 72 2716 3120 4136 4 119 134 C ATOM 449 C PHE A 72 99.112 16.025 250.285 1.00 31.65 C ANISOU 449 C PHE A 72 3432 3713 4880 -129 150 147 C ATOM 450 O PHE A 72 99.744 15.747 249.266 1.00 47.35 O ANISOU 450 O PHE A 72 5437 5647 6906 -159 95 91 O ATOM 451 CB PHE A 72 100.263 16.957 252.302 1.00 32.11 C ANISOU 451 CB PHE A 72 3571 3842 4786 129 128 168 C ATOM 452 CG PHE A 72 100.881 18.156 252.965 1.00 38.41 C ANISOU 452 CG PHE A 72 4348 4730 5515 238 76 105 C ATOM 453 CD1 PHE A 72 101.021 19.350 252.277 1.00 25.36 C ANISOU 453 CD1 PHE A 72 2618 3110 3906 222 30 19 C ATOM 454 CD2 PHE A 72 101.323 18.088 254.275 1.00 49.09 C ANISOU 454 CD2 PHE A 72 5771 6133 6749 353 83 128 C ATOM 455 CE1 PHE A 72 101.588 20.455 252.886 1.00 25.33 C ANISOU 455 CE1 PHE A 72 2613 3162 3847 289 5 -61 C ATOM 456 CE2 PHE A 72 101.892 19.190 254.889 1.00 40.00 C ANISOU 456 CE2 PHE A 72 4599 5075 5525 423 34 38 C ATOM 457 CZ PHE A 72 102.024 20.374 254.192 1.00 26.15 C ANISOU 457 CZ PHE A 72 2775 3327 3835 376 1 -66 C ATOM 458 N ILE A 73 98.139 15.258 250.768 1.00 37.57 N ANISOU 458 N ILE A 73 4198 4440 5637 -219 253 213 N ATOM 459 CA ILE A 73 97.727 14.026 250.105 1.00 37.79 C ANISOU 459 CA ILE A 73 4268 4365 5726 -387 311 206 C ATOM 460 C ILE A 73 97.131 14.322 248.734 1.00 44.98 C ANISOU 460 C ILE A 73 5034 5364 6691 -522 246 120 C ATOM 461 O ILE A 73 97.461 13.662 247.748 1.00 54.87 O ANISOU 461 O ILE A 73 6332 6538 7978 -611 221 55 O ATOM 462 CB ILE A 73 96.703 13.247 250.954 1.00 40.87 C ANISOU 462 CB ILE A 73 4690 4720 6120 -487 461 289 C ATOM 463 CG1 ILE A 73 97.338 12.803 252.272 1.00 45.38 C ANISOU 463 CG1 ILE A 73 5435 5197 6612 -331 537 392 C ATOM 464 CG2 ILE A 73 96.177 12.043 250.189 1.00 60.70 C ANISOU 464 CG2 ILE A 73 7237 7120 8707 -712 537 249 C ATOM 465 CD1 ILE A 73 96.394 12.050 253.180 1.00 72.10 C ANISOU 465 CD1 ILE A 73 8877 8527 9989 -412 714 494 C ATOM 466 N ASN A 74 96.260 15.324 248.676 1.00 50.18 N ANISOU 466 N ASN A 74 5525 6198 7344 -516 222 124 N ATOM 467 CA ASN A 74 95.645 15.731 247.419 1.00 44.61 C ANISOU 467 CA ASN A 74 4664 5628 6659 -598 151 61 C ATOM 468 C ASN A 74 96.675 16.253 246.423 1.00 41.12 C ANISOU 468 C ASN A 74 4253 5161 6211 -516 48 0 C ATOM 469 O ASN A 74 96.518 16.089 245.213 1.00 48.63 O ANISOU 469 O ASN A 74 5148 6162 7168 -600 -8 -64 O ATOM 470 CB ASN A 74 94.574 16.792 247.670 1.00 28.90 C ANISOU 470 CB ASN A 74 2496 3838 4646 -543 161 105 C ATOM 471 CG ASN A 74 93.324 16.218 248.306 1.00 30.60 C ANISOU 471 CG ASN A 74 2619 4132 4876 -671 265 150 C ATOM 472 OD1 ASN A 74 92.414 15.764 247.612 1.00 46.38 O ANISOU 472 OD1 ASN A 74 4475 6249 6898 -841 263 107 O ATOM 473 ND2 ASN A 74 93.273 16.234 249.632 1.00 37.97 N ANISOU 473 ND2 ASN A 74 3624 5016 5787 -598 360 228 N ATOM 474 N LEU A 75 97.729 16.880 246.937 1.00 46.80 N ANISOU 474 N LEU A 75 5055 5817 6909 -360 26 13 N ATOM 475 CA LEU A 75 98.815 17.358 246.090 1.00 35.30 C ANISOU 475 CA LEU A 75 3632 4326 5455 -290 -48 -43 C ATOM 476 C LEU A 75 99.629 16.182 245.563 1.00 51.70 C ANISOU 476 C LEU A 75 5824 6269 7552 -346 -56 -86 C ATOM 477 O LEU A 75 100.026 16.162 244.398 1.00 58.12 O ANISOU 477 O LEU A 75 6634 7077 8372 -370 -104 -145 O ATOM 478 CB LEU A 75 99.716 18.328 246.858 1.00 24.24 C ANISOU 478 CB LEU A 75 2272 2908 4031 -143 -58 -40 C ATOM 479 CG LEU A 75 100.899 18.902 246.078 1.00 36.94 C ANISOU 479 CG LEU A 75 3903 4482 5651 -87 -112 -101 C ATOM 480 CD1 LEU A 75 100.419 19.581 244.804 1.00 37.64 C ANISOU 480 CD1 LEU A 75 3912 4641 5749 -103 -134 -114 C ATOM 481 CD2 LEU A 75 101.696 19.871 246.938 1.00 22.97 C ANISOU 481 CD2 LEU A 75 2157 2712 3859 14 -110 -124 C ATOM 482 N ALA A 76 99.868 15.203 246.428 1.00 46.05 N ANISOU 482 N ALA A 76 5223 5440 6834 -348 7 -47 N ATOM 483 CA ALA A 76 100.608 14.006 246.047 1.00 40.48 C ANISOU 483 CA ALA A 76 4656 4581 6143 -373 33 -71 C ATOM 484 C ALA A 76 99.783 13.138 245.103 1.00 48.65 C ANISOU 484 C ALA A 76 5691 5581 7212 -571 64 -129 C ATOM 485 O ALA A 76 100.329 12.455 244.237 1.00 49.41 O ANISOU 485 O ALA A 76 5875 5578 7320 -609 62 -193 O ATOM 486 CB ALA A 76 101.012 13.215 247.280 1.00 27.13 C ANISOU 486 CB ALA A 76 3105 2779 4426 -290 113 11 C ATOM 487 N ALA A 77 98.466 13.171 245.278 1.00 53.17 N ANISOU 487 N ALA A 77 6157 6250 7795 -702 97 -119 N ATOM 488 CA ALA A 77 97.560 12.412 244.425 1.00 50.76 C ANISOU 488 CA ALA A 77 5811 5962 7515 -928 119 -200 C ATOM 489 C ALA A 77 97.489 13.025 243.031 1.00 52.01 C ANISOU 489 C ALA A 77 5849 6268 7644 -949 3 -288 C ATOM 490 O ALA A 77 97.410 12.312 242.031 1.00 33.84 O ANISOU 490 O ALA A 77 3578 3940 5339 -1089 -8 -390 O ATOM 491 CB ALA A 77 96.174 12.344 245.047 1.00 42.50 C ANISOU 491 CB ALA A 77 4642 5023 6483 -1061 186 -166 C ATOM 492 N ALA A 78 97.517 14.353 242.975 1.00 51.87 N ANISOU 492 N ALA A 78 5712 6400 7595 -804 -71 -247 N ATOM 493 CA ALA A 78 97.488 15.064 241.703 1.00 42.71 C ANISOU 493 CA ALA A 78 4454 5383 6390 -777 -166 -297 C ATOM 494 C ALA A 78 98.789 14.848 240.939 1.00 38.98 C ANISOU 494 C ALA A 78 4116 4782 5914 -716 -192 -348 C ATOM 495 O ALA A 78 98.786 14.717 239.715 1.00 55.95 O ANISOU 495 O ALA A 78 6248 6988 8023 -769 -242 -425 O ATOM 496 CB ALA A 78 97.240 16.548 241.927 1.00 40.83 C ANISOU 496 CB ALA A 78 4098 5290 6125 -614 -197 -221 C ATOM 497 N ASP A 79 99.900 14.807 241.668 1.00 26.16 N ANISOU 497 N ASP A 79 2613 3009 4319 -597 -159 -308 N ATOM 498 CA ASP A 79 101.203 14.566 241.059 1.00 27.69 C ANISOU 498 CA ASP A 79 2916 3092 4512 -524 -170 -349 C ATOM 499 C ASP A 79 101.307 13.130 240.553 1.00 44.71 C ANISOU 499 C ASP A 79 5205 5108 6677 -642 -122 -420 C ATOM 500 O ASP A 79 101.908 12.875 239.509 1.00 43.52 O ANISOU 500 O ASP A 79 5110 4921 6505 -640 -139 -490 O ATOM 501 CB ASP A 79 102.327 14.862 242.053 1.00 41.99 C ANISOU 501 CB ASP A 79 4787 4826 6340 -366 -152 -293 C ATOM 502 CG ASP A 79 102.420 16.335 242.408 1.00 66.88 C ANISOU 502 CG ASP A 79 7838 8087 9485 -265 -186 -259 C ATOM 503 OD1 ASP A 79 102.043 17.177 241.565 1.00 69.45 O ANISOU 503 OD1 ASP A 79 8082 8510 9794 -266 -218 -271 O ATOM 504 OD2 ASP A 79 102.872 16.652 243.529 1.00 49.62 O ANISOU 504 OD2 ASP A 79 5667 5887 7300 -179 -173 -222 O ATOM 505 N LEU A 80 100.719 12.197 241.296 1.00 37.29 N ANISOU 505 N LEU A 80 4330 4073 5765 -746 -42 -404 N ATOM 506 CA LEU A 80 100.698 10.796 240.891 1.00 37.60 C ANISOU 506 CA LEU A 80 4525 3939 5821 -884 40 -477 C ATOM 507 C LEU A 80 99.916 10.613 239.597 1.00 45.14 C ANISOU 507 C LEU A 80 5408 5000 6743 -1076 -8 -611 C ATOM 508 O LEU A 80 100.385 9.959 238.667 1.00 57.18 O ANISOU 508 O LEU A 80 7047 6432 8248 -1122 6 -709 O ATOM 509 CB LEU A 80 100.095 9.921 241.992 1.00 47.72 C ANISOU 509 CB LEU A 80 5895 5093 7144 -974 163 -422 C ATOM 510 CG LEU A 80 101.050 9.419 243.075 1.00 55.07 C ANISOU 510 CG LEU A 80 6999 5843 8084 -794 251 -312 C ATOM 511 CD1 LEU A 80 100.299 8.599 244.111 1.00 49.55 C ANISOU 511 CD1 LEU A 80 6392 5022 7412 -889 393 -243 C ATOM 512 CD2 LEU A 80 102.168 8.601 242.451 1.00 42.65 C ANISOU 512 CD2 LEU A 80 5610 4087 6507 -713 296 -353 C ATOM 513 N LEU A 81 98.724 11.198 239.546 1.00 46.24 N ANISOU 513 N LEU A 81 5353 5356 6862 -1176 -64 -616 N ATOM 514 CA LEU A 81 97.872 11.116 238.365 1.00 46.95 C ANISOU 514 CA LEU A 81 5325 5621 6891 -1350 -132 -743 C ATOM 515 C LEU A 81 98.553 11.733 237.147 1.00 43.53 C ANISOU 515 C LEU A 81 4881 5277 6383 -1232 -227 -783 C ATOM 516 O LEU A 81 98.345 11.294 236.017 1.00 51.15 O ANISOU 516 O LEU A 81 5851 6304 7281 -1353 -264 -914 O ATOM 517 CB LEU A 81 96.531 11.806 238.628 1.00 64.48 C ANISOU 517 CB LEU A 81 7299 8108 9091 -1414 -183 -710 C ATOM 518 CG LEU A 81 95.505 11.801 237.492 1.00 58.94 C ANISOU 518 CG LEU A 81 6417 7674 8304 -1581 -274 -834 C ATOM 519 CD1 LEU A 81 95.136 10.378 237.104 1.00 52.66 C ANISOU 519 CD1 LEU A 81 5713 6773 7525 -1879 -209 -1003 C ATOM 520 CD2 LEU A 81 94.268 12.591 237.887 1.00 67.36 C ANISOU 520 CD2 LEU A 81 7219 9026 9347 -1579 -317 -767 C ATOM 521 N PHE A 82 99.376 12.748 237.388 1.00 34.72 N ANISOU 521 N PHE A 82 3756 4165 5270 -1005 -254 -679 N ATOM 522 CA PHE A 82 100.082 13.430 236.311 1.00 37.15 C ANISOU 522 CA PHE A 82 4061 4540 5514 -881 -314 -694 C ATOM 523 C PHE A 82 101.210 12.577 235.737 1.00 37.69 C ANISOU 523 C PHE A 82 4318 4417 5585 -868 -266 -767 C ATOM 524 O PHE A 82 101.285 12.369 234.526 1.00 53.89 O ANISOU 524 O PHE A 82 6396 6521 7560 -911 -298 -863 O ATOM 525 CB PHE A 82 100.637 14.769 236.802 1.00 30.84 C ANISOU 525 CB PHE A 82 3207 3778 4735 -674 -327 -572 C ATOM 526 CG PHE A 82 101.453 15.499 235.774 1.00 34.89 C ANISOU 526 CG PHE A 82 3734 4326 5195 -550 -352 -572 C ATOM 527 CD1 PHE A 82 100.835 16.214 234.762 1.00 34.60 C ANISOU 527 CD1 PHE A 82 3595 4490 5061 -525 -412 -572 C ATOM 528 CD2 PHE A 82 102.838 15.472 235.822 1.00 32.08 C ANISOU 528 CD2 PHE A 82 3488 3821 4881 -446 -307 -565 C ATOM 529 CE1 PHE A 82 101.582 16.887 233.814 1.00 30.14 C ANISOU 529 CE1 PHE A 82 3063 3945 4442 -403 -411 -556 C ATOM 530 CE2 PHE A 82 103.590 16.142 234.877 1.00 33.59 C ANISOU 530 CE2 PHE A 82 3689 4042 5031 -347 -308 -562 C ATOM 531 CZ PHE A 82 102.960 16.851 233.872 1.00 41.42 C ANISOU 531 CZ PHE A 82 4606 5205 5928 -327 -351 -554 C ATOM 532 N VAL A 83 102.084 12.085 236.610 1.00 38.70 N ANISOU 532 N VAL A 83 4577 4339 5787 -790 -187 -717 N ATOM 533 CA VAL A 83 103.258 11.333 236.176 1.00 35.81 C ANISOU 533 CA VAL A 83 4384 3796 5425 -723 -127 -761 C ATOM 534 C VAL A 83 102.899 9.960 235.613 1.00 39.99 C ANISOU 534 C VAL A 83 5062 4192 5939 -901 -62 -890 C ATOM 535 O VAL A 83 103.675 9.375 234.859 1.00 46.48 O ANISOU 535 O VAL A 83 6025 4901 6736 -866 -17 -961 O ATOM 536 CB VAL A 83 104.268 11.146 237.329 1.00 33.31 C ANISOU 536 CB VAL A 83 4150 3331 5174 -562 -62 -662 C ATOM 537 CG1 VAL A 83 104.730 12.494 237.853 1.00 26.45 C ANISOU 537 CG1 VAL A 83 3146 2588 4318 -413 -120 -571 C ATOM 538 CG2 VAL A 83 103.659 10.314 238.448 1.00 39.43 C ANISOU 538 CG2 VAL A 83 5000 3987 5996 -640 14 -622 C ATOM 539 N CYS A 84 101.725 9.451 235.974 1.00 38.74 N ANISOU 539 N CYS A 84 4877 4045 5799 -1102 -42 -931 N ATOM 540 CA CYS A 84 101.290 8.139 235.504 1.00 48.88 C ANISOU 540 CA CYS A 84 6308 5186 7077 -1322 41 -1077 C ATOM 541 C CYS A 84 100.805 8.188 234.060 1.00 45.37 C ANISOU 541 C CYS A 84 5798 4916 6525 -1462 -46 -1241 C ATOM 542 O CYS A 84 100.598 7.150 233.433 1.00 49.21 O ANISOU 542 O CYS A 84 6420 5293 6986 -1648 15 -1402 O ATOM 543 CB CYS A 84 100.188 7.581 236.407 1.00 44.89 C ANISOU 543 CB CYS A 84 5785 4638 6634 -1520 111 -1073 C ATOM 544 SG CYS A 84 100.783 6.936 237.987 1.00 53.81 S ANISOU 544 SG CYS A 84 7103 5479 7863 -1389 271 -913 S ATOM 545 N THR A 85 100.623 9.395 233.535 1.00 50.34 N ANISOU 545 N THR A 85 6232 5815 7080 -1366 -178 -1200 N ATOM 546 CA THR A 85 100.229 9.568 232.143 1.00 43.70 C ANISOU 546 CA THR A 85 5319 5184 6102 -1444 -273 -1330 C ATOM 547 C THR A 85 101.454 9.563 231.235 1.00 49.88 C ANISOU 547 C THR A 85 6245 5878 6829 -1290 -252 -1356 C ATOM 548 O THR A 85 101.350 9.314 230.034 1.00 59.88 O ANISOU 548 O THR A 85 7541 7237 7973 -1363 -290 -1494 O ATOM 549 CB THR A 85 99.448 10.879 231.931 1.00 44.34 C ANISOU 549 CB THR A 85 5139 5601 6106 -1374 -407 -1253 C ATOM 550 OG1 THR A 85 100.267 11.992 232.312 1.00 40.15 O ANISOU 550 OG1 THR A 85 4586 5057 5612 -1114 -409 -1083 O ATOM 551 CG2 THR A 85 98.177 10.883 232.763 1.00 45.58 C ANISOU 551 CG2 THR A 85 5130 5881 6308 -1521 -423 -1233 C ATOM 552 N LEU A 86 102.614 9.836 231.823 1.00 43.34 N ANISOU 552 N LEU A 86 5494 4891 6081 -1078 -190 -1229 N ATOM 553 CA LEU A 86 103.868 9.906 231.078 1.00 45.32 C ANISOU 553 CA LEU A 86 5855 5070 6296 -912 -154 -1232 C ATOM 554 C LEU A 86 104.287 8.587 230.409 1.00 52.49 C ANISOU 554 C LEU A 86 6991 5779 7172 -991 -56 -1383 C ATOM 555 O LEU A 86 104.743 8.607 229.266 1.00 71.55 O ANISOU 555 O LEU A 86 9460 8240 9485 -946 -61 -1461 O ATOM 556 CB LEU A 86 104.992 10.400 231.993 1.00 42.92 C ANISOU 556 CB LEU A 86 5553 4661 6092 -693 -106 -1077 C ATOM 557 CG LEU A 86 104.759 11.775 232.622 1.00 37.46 C ANISOU 557 CG LEU A 86 4670 4133 5430 -604 -179 -943 C ATOM 558 CD1 LEU A 86 105.960 12.195 233.449 1.00 47.39 C ANISOU 558 CD1 LEU A 86 5933 5301 6772 -419 -133 -833 C ATOM 559 CD2 LEU A 86 104.452 12.810 231.551 1.00 34.34 C ANISOU 559 CD2 LEU A 86 4161 3958 4928 -570 -257 -942 C ATOM 560 N PRO A 87 104.152 7.439 231.107 1.00 49.75 N ANISOU 560 N PRO A 87 6801 5195 6907 -1097 53 -1422 N ATOM 561 CA PRO A 87 104.487 6.207 230.383 1.00 38.05 C ANISOU 561 CA PRO A 87 5563 3505 5388 -1177 167 -1581 C ATOM 562 C PRO A 87 103.538 5.932 229.219 1.00 53.06 C ANISOU 562 C PRO A 87 7445 5557 7159 -1425 100 -1795 C ATOM 563 O PRO A 87 103.915 5.243 228.271 1.00 54.65 O ANISOU 563 O PRO A 87 7822 5662 7281 -1462 161 -1945 O ATOM 564 CB PRO A 87 104.368 5.120 231.458 1.00 49.39 C ANISOU 564 CB PRO A 87 7173 4652 6940 -1249 314 -1560 C ATOM 565 CG PRO A 87 103.509 5.712 232.514 1.00 66.13 C ANISOU 565 CG PRO A 87 9103 6899 9126 -1311 246 -1449 C ATOM 566 CD PRO A 87 103.849 7.165 232.523 1.00 57.98 C ANISOU 566 CD PRO A 87 7848 6114 8069 -1118 110 -1319 C ATOM 567 N LEU A 88 102.325 6.471 229.290 1.00 45.64 N ANISOU 567 N LEU A 88 6286 4871 6185 -1584 -25 -1812 N ATOM 568 CA LEU A 88 101.377 6.352 228.189 1.00 54.76 C ANISOU 568 CA LEU A 88 7360 6258 7188 -1804 -123 -2011 C ATOM 569 C LEU A 88 101.813 7.226 227.016 1.00 47.09 C ANISOU 569 C LEU A 88 6315 5520 6059 -1632 -226 -2003 C ATOM 570 O LEU A 88 101.716 6.818 225.859 1.00 53.94 O ANISOU 570 O LEU A 88 7253 6467 6776 -1728 -250 -2185 O ATOM 571 CB LEU A 88 99.964 6.732 228.639 1.00 59.25 C ANISOU 571 CB LEU A 88 7676 7078 7759 -1989 -229 -2013 C ATOM 572 CG LEU A 88 99.138 5.680 229.388 1.00 48.48 C ANISOU 572 CG LEU A 88 6367 5554 6498 -2284 -129 -2112 C ATOM 573 CD1 LEU A 88 99.115 4.363 228.622 1.00 52.19 C ANISOU 573 CD1 LEU A 88 7067 5842 6919 -2516 -29 -2359 C ATOM 574 CD2 LEU A 88 99.641 5.474 230.809 1.00 54.97 C ANISOU 574 CD2 LEU A 88 7301 6085 7501 -2164 7 -1926 C ATOM 575 N TRP A 89 102.294 8.427 227.322 1.00 39.26 N ANISOU 575 N TRP A 89 5195 4629 5094 -1383 -275 -1795 N ATOM 576 CA TRP A 89 102.786 9.333 226.290 1.00 41.22 C ANISOU 576 CA TRP A 89 5392 5063 5206 -1199 -337 -1751 C ATOM 577 C TRP A 89 104.097 8.829 225.696 1.00 50.75 C ANISOU 577 C TRP A 89 6821 6063 6399 -1073 -219 -1791 C ATOM 578 O TRP A 89 104.393 9.079 224.528 1.00 61.20 O ANISOU 578 O TRP A 89 8173 7512 7568 -1003 -242 -1844 O ATOM 579 CB TRP A 89 102.976 10.745 226.848 1.00 38.41 C ANISOU 579 CB TRP A 89 4867 4823 4905 -987 -381 -1523 C ATOM 580 CG TRP A 89 101.694 11.456 227.156 1.00 47.20 C ANISOU 580 CG TRP A 89 5749 6199 5986 -1049 -499 -1472 C ATOM 581 CD1 TRP A 89 101.279 11.903 228.376 1.00 54.33 C ANISOU 581 CD1 TRP A 89 6537 7089 7018 -1037 -503 -1345 C ATOM 582 CD2 TRP A 89 100.657 11.802 226.228 1.00 42.65 C ANISOU 582 CD2 TRP A 89 5021 5962 5223 -1113 -629 -1544 C ATOM 583 NE1 TRP A 89 100.050 12.507 228.266 1.00 56.07 N ANISOU 583 NE1 TRP A 89 6544 7605 7154 -1084 -614 -1329 N ATOM 584 CE2 TRP A 89 99.646 12.458 226.958 1.00 42.44 C ANISOU 584 CE2 TRP A 89 4780 6112 5231 -1125 -699 -1445 C ATOM 585 CE3 TRP A 89 100.485 11.621 224.853 1.00 46.30 C ANISOU 585 CE3 TRP A 89 5502 6616 5474 -1147 -693 -1681 C ATOM 586 CZ2 TRP A 89 98.482 12.933 226.359 1.00 39.38 C ANISOU 586 CZ2 TRP A 89 4183 6099 4681 -1155 -832 -1470 C ATOM 587 CZ3 TRP A 89 99.329 12.093 224.260 1.00 41.75 C ANISOU 587 CZ3 TRP A 89 4718 6422 4722 -1184 -838 -1712 C ATOM 588 CH2 TRP A 89 98.342 12.741 225.013 1.00 41.40 C ANISOU 588 CH2 TRP A 89 4446 6560 4723 -1181 -907 -1602 C ATOM 589 N MET A 90 104.882 8.124 226.506 1.00 54.68 N ANISOU 589 N MET A 90 7474 6257 7046 -1023 -87 -1753 N ATOM 590 CA MET A 90 106.134 7.544 226.033 1.00 52.10 C ANISOU 590 CA MET A 90 7353 5727 6715 -885 43 -1785 C ATOM 591 C MET A 90 105.863 6.427 225.034 1.00 46.79 C ANISOU 591 C MET A 90 6875 4981 5921 -1058 92 -2027 C ATOM 592 O MET A 90 106.571 6.291 224.038 1.00 68.00 O ANISOU 592 O MET A 90 9678 7658 8501 -961 142 -2094 O ATOM 593 CB MET A 90 106.970 7.021 227.203 1.00 38.01 C ANISOU 593 CB MET A 90 5674 3664 5103 -765 170 -1676 C ATOM 594 CG MET A 90 107.740 8.104 227.939 1.00 54.56 C ANISOU 594 CG MET A 90 7616 5826 7290 -543 148 -1466 C ATOM 595 SD MET A 90 109.019 7.450 229.029 1.00 64.29 S ANISOU 595 SD MET A 90 8969 6795 8665 -340 292 -1354 S ATOM 596 CE MET A 90 108.038 6.823 230.386 1.00 60.06 C ANISOU 596 CE MET A 90 8460 6129 8230 -492 301 -1326 C ATOM 597 N GLN A 91 104.832 5.634 225.304 1.00 49.28 N ANISOU 597 N GLN A 91 7227 5246 6252 -1328 88 -2167 N ATOM 598 CA GLN A 91 104.423 4.579 224.386 1.00 58.95 C ANISOU 598 CA GLN A 91 8630 6411 7359 -1554 131 -2436 C ATOM 599 C GLN A 91 103.865 5.183 223.103 1.00 59.29 C ANISOU 599 C GLN A 91 8536 6819 7174 -1610 -27 -2551 C ATOM 600 O GLN A 91 103.926 4.573 222.036 1.00 72.39 O ANISOU 600 O GLN A 91 10347 8479 8681 -1698 0 -2759 O ATOM 601 CB GLN A 91 103.383 3.666 225.040 1.00 69.11 C ANISOU 601 CB GLN A 91 9961 7571 8728 -1868 172 -2563 C ATOM 602 N TYR A 92 103.325 6.392 223.219 1.00 51.51 N ANISOU 602 N TYR A 92 7274 6144 6152 -1539 -184 -2409 N ATOM 603 CA TYR A 92 102.763 7.106 222.080 1.00 46.77 C ANISOU 603 CA TYR A 92 6522 5928 5321 -1535 -339 -2467 C ATOM 604 C TYR A 92 103.861 7.649 221.170 1.00 55.29 C ANISOU 604 C TYR A 92 7684 7034 6290 -1269 -299 -2392 C ATOM 605 O TYR A 92 103.735 7.620 219.946 1.00 68.03 O ANISOU 605 O TYR A 92 9332 8838 7679 -1283 -351 -2526 O ATOM 606 CB TYR A 92 101.860 8.244 222.567 1.00 49.70 C ANISOU 606 CB TYR A 92 6589 6598 5696 -1501 -490 -2308 C ATOM 607 CG TYR A 92 101.296 9.117 221.468 1.00 50.11 C ANISOU 607 CG TYR A 92 6472 7067 5501 -1427 -645 -2311 C ATOM 608 CD1 TYR A 92 100.206 8.702 220.715 1.00 49.47 C ANISOU 608 CD1 TYR A 92 6297 7274 5225 -1652 -771 -2532 C ATOM 609 CD2 TYR A 92 101.845 10.363 221.194 1.00 66.54 C ANISOU 609 CD2 TYR A 92 8484 9263 7534 -1130 -658 -2092 C ATOM 610 CE1 TYR A 92 99.685 9.499 219.713 1.00 50.69 C ANISOU 610 CE1 TYR A 92 6289 7848 5125 -1548 -921 -2520 C ATOM 611 CE2 TYR A 92 101.330 11.167 220.195 1.00 64.20 C ANISOU 611 CE2 TYR A 92 8056 9339 6998 -1026 -781 -2067 C ATOM 612 CZ TYR A 92 100.250 10.731 219.458 1.00 48.93 C ANISOU 612 CZ TYR A 92 6024 7714 4853 -1218 -920 -2274 C ATOM 613 OH TYR A 92 99.736 11.530 218.463 1.00 66.08 O ANISOU 613 OH TYR A 92 8057 10292 6758 -1079 -1050 -2235 O ATOM 614 N LEU A 93 104.940 8.137 221.775 1.00 52.28 N ANISOU 614 N LEU A 93 7329 6476 6059 -1033 -203 -2184 N ATOM 615 CA LEU A 93 106.055 8.707 221.024 1.00 43.14 C ANISOU 615 CA LEU A 93 6230 5331 4829 -785 -138 -2093 C ATOM 616 C LEU A 93 106.876 7.643 220.303 1.00 53.54 C ANISOU 616 C LEU A 93 7812 6444 6087 -777 2 -2254 C ATOM 617 O LEU A 93 107.374 7.872 219.201 1.00 66.47 O ANISOU 617 O LEU A 93 9514 8183 7559 -659 28 -2283 O ATOM 618 CB LEU A 93 106.965 9.512 221.954 1.00 50.13 C ANISOU 618 CB LEU A 93 7040 6102 5905 -572 -71 -1848 C ATOM 619 CG LEU A 93 106.431 10.854 222.456 1.00 58.80 C ANISOU 619 CG LEU A 93 7903 7401 7036 -505 -175 -1662 C ATOM 620 CD1 LEU A 93 107.389 11.466 223.464 1.00 36.30 C ANISOU 620 CD1 LEU A 93 5007 4400 4385 -343 -94 -1471 C ATOM 621 CD2 LEU A 93 106.203 11.802 221.289 1.00 65.74 C ANISOU 621 CD2 LEU A 93 8710 8563 7706 -399 -240 -1621 C ATOM 622 N LEU A 94 107.015 6.480 220.931 1.00 59.01 N ANISOU 622 N LEU A 94 8674 6837 6909 -887 111 -2350 N ATOM 623 CA LEU A 94 107.856 5.415 220.393 1.00 62.34 C ANISOU 623 CA LEU A 94 9377 7009 7300 -849 279 -2486 C ATOM 624 C LEU A 94 107.273 4.789 219.128 1.00 83.83 C ANISOU 624 C LEU A 94 12228 9837 9788 -1034 249 -2765 C ATOM 625 O LEU A 94 108.002 4.195 218.333 1.00 92.64 O ANISOU 625 O LEU A 94 13562 10828 10810 -960 374 -2878 O ATOM 626 CB LEU A 94 108.083 4.338 221.454 1.00 67.05 C ANISOU 626 CB LEU A 94 10141 7242 8093 -900 421 -2497 C ATOM 627 CG LEU A 94 109.010 4.746 222.602 1.00 51.94 C ANISOU 627 CG LEU A 94 8155 5199 6379 -661 487 -2243 C ATOM 628 CD1 LEU A 94 109.005 3.699 223.703 1.00 57.00 C ANISOU 628 CD1 LEU A 94 8952 5521 7185 -715 609 -2239 C ATOM 629 CD2 LEU A 94 110.422 4.977 222.086 1.00 44.71 C ANISOU 629 CD2 LEU A 94 7294 4251 5443 -377 597 -2158 C ATOM 630 N ASP A 95 105.963 4.923 218.944 1.00 86.98 N ANISOU 630 N ASP A 95 12481 10485 10081 -1272 83 -2882 N ATOM 631 CA ASP A 95 105.307 4.414 217.744 1.00 83.85 C ANISOU 631 CA ASP A 95 12160 10265 9434 -1471 18 -3166 C ATOM 632 C ASP A 95 103.942 5.065 217.541 1.00 82.61 C ANISOU 632 C ASP A 95 11721 10528 9140 -1634 -213 -3206 C ATOM 633 O ASP A 95 102.906 4.418 217.687 1.00 89.50 O ANISOU 633 O ASP A 95 12557 11450 9998 -1948 -274 -3408 O ATOM 634 CB ASP A 95 105.157 2.892 217.815 1.00 90.54 C ANISOU 634 CB ASP A 95 13283 10791 10326 -1728 159 -3434 C ATOM 635 CG ASP A 95 104.731 2.286 216.491 1.00109.75 C ANISOU 635 CG ASP A 95 15795 13374 12532 -1848 103 -3649 C ATOM 636 OD1 ASP A 95 104.959 2.925 215.443 1.00113.27 O ANISOU 636 OD1 ASP A 95 16216 14088 12735 -1729 35 -3694 O ATOM 637 OD2 ASP A 95 104.170 1.170 216.499 1.00122.12 O ANISOU 637 OD2 ASP A 95 17451 14793 14154 -2057 138 -3772 O ATOM 638 N SER A 101 95.297 1.184 224.088 1.00123.31 N ANISOU 638 N SER A 101 15942 15576 15334 -3548 -224 -3301 N ATOM 639 CA SER A 101 94.215 1.815 223.341 1.00121.11 C ANISOU 639 CA SER A 101 15340 15797 14878 -3627 -433 -3379 C ATOM 640 C SER A 101 94.527 3.279 223.050 1.00129.02 C ANISOU 640 C SER A 101 16154 17105 15761 -3356 -611 -3241 C ATOM 641 O SER A 101 93.962 3.865 222.127 1.00127.21 O ANISOU 641 O SER A 101 15717 17289 15329 -3331 -785 -3298 O ATOM 642 CB SER A 101 92.896 1.703 224.110 1.00100.78 C ANISOU 642 CB SER A 101 12531 13373 12390 -3825 -439 -3356 C ATOM 643 OG SER A 101 92.569 0.349 224.370 1.00 94.95 O ANISOU 643 OG SER A 101 11967 12358 11753 -4091 -260 -3489 O ATOM 644 N VAL A 102 95.452 3.833 223.836 1.00133.69 N ANISOU 644 N VAL A 102 16831 17489 16474 -3149 -552 -3062 N ATOM 645 CA VAL A 102 95.836 5.253 223.828 1.00112.96 C ANISOU 645 CA VAL A 102 14044 15094 13781 -2890 -681 -2907 C ATOM 646 C VAL A 102 94.680 6.199 223.447 1.00105.62 C ANISOU 646 C VAL A 102 12749 14685 12698 -2863 -883 -2865 C ATOM 647 O VAL A 102 94.545 6.625 222.298 1.00115.64 O ANISOU 647 O VAL A 102 13929 16268 13739 -2787 -1016 -2931 O ATOM 648 CB VAL A 102 97.089 5.495 222.908 1.00 93.08 C ANISOU 648 CB VAL A 102 11721 12509 11137 -2702 -677 -2953 C ATOM 649 CG1 VAL A 102 96.896 4.950 221.486 1.00 86.34 C ANISOU 649 CG1 VAL A 102 10932 11807 10065 -2792 -731 -3162 C ATOM 650 CG2 VAL A 102 97.504 6.969 222.907 1.00 74.27 C ANISOU 650 CG2 VAL A 102 9177 10363 8681 -2440 -791 -2798 C ATOM 651 N PRO A 103 93.819 6.510 224.429 1.00 80.72 N ANISOU 651 N PRO A 103 9386 11626 9660 -2905 -895 -2745 N ATOM 652 CA PRO A 103 92.705 7.441 224.224 1.00 88.47 C ANISOU 652 CA PRO A 103 10015 13083 10515 -2836 -1062 -2669 C ATOM 653 C PRO A 103 93.158 8.898 224.302 1.00 86.72 C ANISOU 653 C PRO A 103 9669 13045 10235 -2517 -1156 -2468 C ATOM 654 O PRO A 103 93.491 9.382 225.382 1.00 63.98 O ANISOU 654 O PRO A 103 6780 10011 7518 -2420 -1099 -2309 O ATOM 655 CB PRO A 103 91.749 7.096 225.367 1.00 83.50 C ANISOU 655 CB PRO A 103 9262 12406 10058 -2999 -991 -2618 C ATOM 656 CG PRO A 103 92.636 6.582 226.448 1.00 69.49 C ANISOU 656 CG PRO A 103 7742 10152 8509 -3019 -812 -2553 C ATOM 657 CD PRO A 103 93.791 5.897 225.769 1.00 56.20 C ANISOU 657 CD PRO A 103 6376 8179 6797 -3019 -734 -2677 C ATOM 658 N CYS A 104 93.164 9.581 223.161 1.00 80.92 N ANISOU 658 N CYS A 104 10066 11589 9089 -1981 225 -2067 N ATOM 659 CA CYS A 104 93.667 10.949 223.075 1.00 67.96 C ANISOU 659 CA CYS A 104 8140 10218 7464 -1726 42 -1749 C ATOM 660 C CYS A 104 92.955 11.914 224.020 1.00 61.66 C ANISOU 660 C CYS A 104 7127 9453 6847 -1703 -81 -1523 C ATOM 661 O CYS A 104 93.598 12.598 224.815 1.00 55.10 O ANISOU 661 O CYS A 104 6288 8492 6156 -1462 -101 -1273 O ATOM 662 CB CYS A 104 93.552 11.462 221.639 1.00 81.05 C ANISOU 662 CB CYS A 104 9576 12348 8870 -1799 -117 -1776 C ATOM 663 SG CYS A 104 94.780 10.774 220.510 1.00 94.26 S ANISOU 663 SG CYS A 104 11423 14086 10306 -1701 -3 -1951 S ATOM 664 N THR A 105 91.630 11.964 223.929 1.00 49.66 N ANISOU 664 N THR A 105 5418 8148 5301 -1954 -162 -1638 N ATOM 665 CA THR A 105 90.841 12.896 224.727 1.00 53.75 C ANISOU 665 CA THR A 105 5694 8775 5955 -1900 -292 -1466 C ATOM 666 C THR A 105 90.959 12.612 226.223 1.00 58.82 C ANISOU 666 C THR A 105 6501 9013 6833 -1854 -142 -1399 C ATOM 667 O THR A 105 91.129 13.529 227.026 1.00 58.49 O ANISOU 667 O THR A 105 6367 8921 6935 -1635 -216 -1158 O ATOM 668 CB THR A 105 89.354 12.856 224.325 1.00 49.15 C ANISOU 668 CB THR A 105 4830 8592 5253 -2176 -394 -1666 C ATOM 669 OG1 THR A 105 89.229 13.096 222.918 1.00 61.83 O ANISOU 669 OG1 THR A 105 6283 10606 6606 -2206 -547 -1728 O ATOM 670 CG2 THR A 105 88.564 13.910 225.088 1.00 48.15 C ANISOU 670 CG2 THR A 105 4420 8640 5236 -2030 -548 -1499 C ATOM 671 N LEU A 106 90.876 11.337 226.590 1.00 62.39 N ANISOU 671 N LEU A 106 7238 9162 7304 -2069 74 -1612 N ATOM 672 CA LEU A 106 90.915 10.941 227.993 1.00 45.44 C ANISOU 672 CA LEU A 106 5298 6627 5340 -2061 230 -1554 C ATOM 673 C LEU A 106 92.294 11.147 228.613 1.00 56.15 C ANISOU 673 C LEU A 106 6842 7687 6804 -1675 277 -1326 C ATOM 674 O LEU A 106 92.410 11.622 229.742 1.00 55.15 O ANISOU 674 O LEU A 106 6692 7430 6833 -1531 279 -1142 O ATOM 675 CB LEU A 106 90.490 9.479 228.144 1.00 63.42 C ANISOU 675 CB LEU A 106 7927 8609 7563 -2416 458 -1833 C ATOM 676 CG LEU A 106 90.475 8.930 229.572 1.00 65.33 C ANISOU 676 CG LEU A 106 8461 8416 7944 -2455 640 -1774 C ATOM 677 CD1 LEU A 106 89.509 9.721 230.442 1.00 47.28 C ANISOU 677 CD1 LEU A 106 5832 6369 5764 -2550 562 -1680 C ATOM 678 CD2 LEU A 106 90.121 7.451 229.578 1.00 52.18 C ANISOU 678 CD2 LEU A 106 7255 6393 6178 -2837 876 -2046 C ATOM 679 N LEU A 107 93.336 10.784 227.872 1.00 53.23 N ANISOU 679 N LEU A 107 6632 7268 6327 -1511 315 -1360 N ATOM 680 CA LEU A 107 94.703 10.905 228.367 1.00 41.66 C ANISOU 680 CA LEU A 107 5295 5625 4909 -1143 361 -1189 C ATOM 681 C LEU A 107 95.113 12.368 228.489 1.00 45.54 C ANISOU 681 C LEU A 107 5480 6374 5449 -959 187 -915 C ATOM 682 O LEU A 107 95.848 12.743 229.402 1.00 63.79 O ANISOU 682 O LEU A 107 7813 8567 7859 -738 206 -738 O ATOM 683 CB LEU A 107 95.676 10.160 227.451 1.00 53.44 C ANISOU 683 CB LEU A 107 6979 7094 6230 -1003 444 -1337 C ATOM 684 CG LEU A 107 97.119 10.024 227.938 1.00 53.00 C ANISOU 684 CG LEU A 107 7057 6909 6172 -597 519 -1231 C ATOM 685 CD1 LEU A 107 97.170 9.254 229.247 1.00 68.23 C ANISOU 685 CD1 LEU A 107 9317 8387 8222 -480 666 -1208 C ATOM 686 CD2 LEU A 107 97.976 9.350 226.880 1.00 48.52 C ANISOU 686 CD2 LEU A 107 6614 6424 5399 -445 587 -1420 C ATOM 687 N THR A 108 94.633 13.191 227.561 1.00 54.89 N ANISOU 687 N THR A 108 6411 7905 6539 -1058 15 -883 N ATOM 688 CA THR A 108 94.895 14.624 227.601 1.00 37.19 C ANISOU 688 CA THR A 108 3960 5854 4315 -924 -155 -622 C ATOM 689 C THR A 108 94.159 15.251 228.781 1.00 35.74 C ANISOU 689 C THR A 108 3687 5571 4323 -906 -205 -501 C ATOM 690 O THR A 108 94.652 16.187 229.411 1.00 33.94 O ANISOU 690 O THR A 108 3417 5305 4174 -748 -263 -290 O ATOM 691 CB THR A 108 94.464 15.315 226.292 1.00 40.26 C ANISOU 691 CB THR A 108 4169 6607 4521 -1011 -335 -604 C ATOM 692 OG1 THR A 108 95.069 14.649 225.176 1.00 40.03 O ANISOU 692 OG1 THR A 108 4214 6701 4294 -1057 -274 -754 O ATOM 693 CG2 THR A 108 94.881 16.778 226.291 1.00 37.04 C ANISOU 693 CG2 THR A 108 3666 6312 4097 -875 -493 -315 C ATOM 694 N ALA A 109 92.978 14.716 229.077 1.00 42.04 N ANISOU 694 N ALA A 109 4452 6351 5172 -1096 -170 -661 N ATOM 695 CA ALA A 109 92.171 15.190 230.194 1.00 36.07 C ANISOU 695 CA ALA A 109 3581 5554 4570 -1097 -197 -598 C ATOM 696 C ALA A 109 92.887 14.967 231.521 1.00 37.90 C ANISOU 696 C ALA A 109 3995 5453 4951 -967 -57 -493 C ATOM 697 O ALA A 109 93.024 15.889 232.322 1.00 47.04 O ANISOU 697 O ALA A 109 5070 6588 6214 -814 -123 -319 O ATOM 698 CB ALA A 109 90.815 14.500 230.201 1.00 38.32 C ANISOU 698 CB ALA A 109 3776 5957 4829 -1392 -151 -834 C ATOM 699 N CYS A 110 93.349 13.740 231.744 1.00 43.83 N ANISOU 699 N CYS A 110 5022 5941 5689 -1009 130 -605 N ATOM 700 CA CYS A 110 94.072 13.401 232.966 1.00 51.95 C ANISOU 700 CA CYS A 110 6256 6666 6815 -844 259 -505 C ATOM 701 C CYS A 110 95.384 14.171 233.069 1.00 65.45 C ANISOU 701 C CYS A 110 7914 8434 8519 -553 196 -311 C ATOM 702 O CYS A 110 95.884 14.420 234.166 1.00 80.91 O ANISOU 702 O CYS A 110 9907 10275 10561 -398 230 -181 O ATOM 703 CB CYS A 110 94.346 11.897 233.029 1.00 36.26 C ANISOU 703 CB CYS A 110 4648 4360 4768 -891 460 -660 C ATOM 704 SG CYS A 110 92.863 10.872 233.149 1.00 56.98 S ANISOU 704 SG CYS A 110 7420 6856 7374 -1346 592 -899 S ATOM 705 N PHE A 111 95.937 14.547 231.921 1.00 58.07 N ANISOU 705 N PHE A 111 6886 7720 7457 -513 110 -304 N ATOM 706 CA PHE A 111 97.188 15.292 231.877 1.00 54.03 C ANISOU 706 CA PHE A 111 6302 7339 6888 -323 62 -147 C ATOM 707 C PHE A 111 97.020 16.701 232.435 1.00 52.95 C ANISOU 707 C PHE A 111 6003 7276 6839 -316 -71 49 C ATOM 708 O PHE A 111 97.830 17.158 233.242 1.00 70.23 O ANISOU 708 O PHE A 111 8185 9440 9060 -194 -53 171 O ATOM 709 CB PHE A 111 97.718 15.354 230.443 1.00 69.33 C ANISOU 709 CB PHE A 111 8182 9529 8631 -349 15 -199 C ATOM 710 CG PHE A 111 98.977 16.160 230.294 1.00 56.15 C ANISOU 710 CG PHE A 111 6410 8069 6854 -242 -22 -55 C ATOM 711 CD1 PHE A 111 100.214 15.595 230.558 1.00 46.98 C ANISOU 711 CD1 PHE A 111 5294 6947 5611 -39 93 -94 C ATOM 712 CD2 PHE A 111 98.924 17.482 229.879 1.00 52.58 C ANISOU 712 CD2 PHE A 111 5832 7793 6352 -347 -170 112 C ATOM 713 CE1 PHE A 111 101.372 16.334 230.418 1.00 58.04 C ANISOU 713 CE1 PHE A 111 6547 8631 6875 3 71 7 C ATOM 714 CE2 PHE A 111 100.078 18.225 229.739 1.00 53.12 C ANISOU 714 CE2 PHE A 111 5832 8060 6289 -340 -182 233 C ATOM 715 CZ PHE A 111 101.303 17.651 230.008 1.00 59.15 C ANISOU 715 CZ PHE A 111 6573 8934 6965 -192 -57 169 C ATOM 716 N TYR A 112 95.967 17.386 232.002 1.00 35.19 N ANISOU 716 N TYR A 112 3634 5131 4606 -430 -207 64 N ATOM 717 CA TYR A 112 95.745 18.771 232.400 1.00 44.59 C ANISOU 717 CA TYR A 112 4733 6354 5855 -383 -346 239 C ATOM 718 C TYR A 112 95.021 18.890 233.738 1.00 48.24 C ANISOU 718 C TYR A 112 5170 6664 6495 -347 -319 241 C ATOM 719 O TYR A 112 95.324 19.782 234.531 1.00 54.20 O ANISOU 719 O TYR A 112 5923 7353 7318 -260 -358 372 O ATOM 720 CB TYR A 112 94.964 19.516 231.317 1.00 30.17 C ANISOU 720 CB TYR A 112 2814 4720 3928 -432 -527 267 C ATOM 721 CG TYR A 112 95.812 19.927 230.135 1.00 52.04 C ANISOU 721 CG TYR A 112 5620 7654 6499 -466 -586 354 C ATOM 722 CD1 TYR A 112 96.594 21.074 230.184 1.00 38.34 C ANISOU 722 CD1 TYR A 112 3949 5914 4704 -448 -651 556 C ATOM 723 CD2 TYR A 112 95.832 19.170 228.971 1.00 43.49 C ANISOU 723 CD2 TYR A 112 4523 6739 5261 -557 -565 222 C ATOM 724 CE1 TYR A 112 97.371 21.456 229.108 1.00 52.29 C ANISOU 724 CE1 TYR A 112 5758 7857 6252 -540 -686 638 C ATOM 725 CE2 TYR A 112 96.607 19.544 227.888 1.00 41.87 C ANISOU 725 CE2 TYR A 112 4340 6725 4845 -607 -608 296 C ATOM 726 CZ TYR A 112 97.374 20.688 227.963 1.00 50.30 C ANISOU 726 CZ TYR A 112 5463 7803 5847 -608 -665 511 C ATOM 727 OH TYR A 112 98.146 21.065 226.889 1.00 44.71 O ANISOU 727 OH TYR A 112 4784 7310 4894 -716 -689 588 O ATOM 728 N VAL A 113 94.066 17.999 233.986 1.00 41.92 N ANISOU 728 N VAL A 113 4357 5822 5747 -451 -242 81 N ATOM 729 CA VAL A 113 93.336 18.000 235.251 1.00 42.75 C ANISOU 729 CA VAL A 113 4425 5829 5990 -459 -190 61 C ATOM 730 C VAL A 113 94.296 17.833 236.425 1.00 34.30 C ANISOU 730 C VAL A 113 3491 4554 4986 -347 -73 156 C ATOM 731 O VAL A 113 94.228 18.577 237.402 1.00 35.46 O ANISOU 731 O VAL A 113 3588 4665 5221 -268 -100 242 O ATOM 732 CB VAL A 113 92.265 16.888 235.293 1.00 30.26 C ANISOU 732 CB VAL A 113 2838 4254 4403 -681 -81 -145 C ATOM 733 CG1 VAL A 113 91.843 16.594 236.726 1.00 30.04 C ANISOU 733 CG1 VAL A 113 2847 4086 4483 -726 43 -159 C ATOM 734 CG2 VAL A 113 91.062 17.279 234.447 1.00 31.89 C ANISOU 734 CG2 VAL A 113 2804 4769 4542 -776 -224 -253 C ATOM 735 N ALA A 114 95.203 16.869 236.312 1.00 38.77 N ANISOU 735 N ALA A 114 4231 5012 5490 -309 49 130 N ATOM 736 CA ALA A 114 96.187 16.620 237.359 1.00 26.69 C ANISOU 736 CA ALA A 114 2820 3346 3976 -148 146 215 C ATOM 737 C ALA A 114 97.182 17.773 237.476 1.00 41.45 C ANISOU 737 C ALA A 114 4580 5352 5817 -30 52 362 C ATOM 738 O ALA A 114 97.683 18.060 238.562 1.00 43.46 O ANISOU 738 O ALA A 114 4838 5569 6106 67 81 442 O ATOM 739 CB ALA A 114 96.920 15.316 237.096 1.00 37.13 C ANISOU 739 CB ALA A 114 4367 4543 5200 -60 280 138 C ATOM 740 N MET A 115 97.465 18.430 236.355 1.00 44.50 N ANISOU 740 N MET A 115 4885 5910 6115 -74 -55 393 N ATOM 741 CA MET A 115 98.405 19.545 236.345 1.00 40.96 C ANISOU 741 CA MET A 115 4373 5592 5599 -55 -130 524 C ATOM 742 C MET A 115 97.817 20.767 237.040 1.00 44.57 C ANISOU 742 C MET A 115 4798 5977 6160 -82 -228 615 C ATOM 743 O MET A 115 98.458 21.373 237.897 1.00 41.51 O ANISOU 743 O MET A 115 4410 5582 5780 -56 -219 688 O ATOM 744 CB MET A 115 98.807 19.907 234.914 1.00 47.40 C ANISOU 744 CB MET A 115 5157 6597 6255 -142 -205 542 C ATOM 745 CG MET A 115 99.887 20.977 234.835 1.00 58.56 C ANISOU 745 CG MET A 115 6539 8164 7547 -207 -249 668 C ATOM 746 SD MET A 115 100.191 21.572 233.160 1.00 53.55 S ANISOU 746 SD MET A 115 5908 7745 6695 -375 -340 724 S ATOM 747 CE MET A 115 98.638 22.392 232.810 1.00 61.89 C ANISOU 747 CE MET A 115 7037 8636 7843 -395 -514 793 C ATOM 748 N PHE A 116 96.595 21.126 236.662 1.00 56.46 N ANISOU 748 N PHE A 116 6271 7457 7723 -115 -325 589 N ATOM 749 CA PHE A 116 95.928 22.282 237.247 1.00 57.18 C ANISOU 749 CA PHE A 116 6349 7477 7898 -69 -429 650 C ATOM 750 C PHE A 116 95.599 22.049 238.720 1.00 46.90 C ANISOU 750 C PHE A 116 5021 6071 6728 -14 -338 605 C ATOM 751 O PHE A 116 95.727 22.959 239.539 1.00 57.05 O ANISOU 751 O PHE A 116 6332 7288 8058 34 -371 663 O ATOM 752 CB PHE A 116 94.657 22.623 236.464 1.00 44.57 C ANISOU 752 CB PHE A 116 4686 5952 6297 -44 -566 610 C ATOM 753 CG PHE A 116 94.917 23.364 235.180 1.00 40.43 C ANISOU 753 CG PHE A 116 4235 5504 5623 -63 -703 715 C ATOM 754 CD1 PHE A 116 95.310 24.692 235.201 1.00 51.32 C ANISOU 754 CD1 PHE A 116 5768 6780 6953 -35 -805 870 C ATOM 755 CD2 PHE A 116 94.760 22.736 233.956 1.00 36.55 C ANISOU 755 CD2 PHE A 116 3697 5174 5017 -134 -724 657 C ATOM 756 CE1 PHE A 116 95.549 25.378 234.025 1.00 53.98 C ANISOU 756 CE1 PHE A 116 6233 7159 7120 -81 -922 992 C ATOM 757 CE2 PHE A 116 94.997 23.417 232.777 1.00 45.37 C ANISOU 757 CE2 PHE A 116 4893 6378 5965 -161 -849 768 C ATOM 758 CZ PHE A 116 95.391 24.739 232.812 1.00 53.95 C ANISOU 758 CZ PHE A 116 6157 7348 6995 -137 -947 950 C ATOM 759 N ALA A 117 95.182 20.830 239.052 1.00 41.48 N ANISOU 759 N ALA A 117 4319 5361 6081 -46 -215 498 N ATOM 760 CA ALA A 117 94.879 20.479 240.436 1.00 41.80 C ANISOU 760 CA ALA A 117 4363 5311 6209 -26 -108 466 C ATOM 761 C ALA A 117 96.129 20.581 241.300 1.00 32.61 C ANISOU 761 C ALA A 117 3271 4104 5016 54 -47 558 C ATOM 762 O ALA A 117 96.065 21.020 242.448 1.00 42.02 O ANISOU 762 O ALA A 117 4447 5259 6260 94 -27 579 O ATOM 763 CB ALA A 117 94.290 19.081 240.518 1.00 24.53 C ANISOU 763 CB ALA A 117 2228 3071 4023 -132 31 350 C ATOM 764 N SER A 118 97.263 20.174 240.739 1.00 31.09 N ANISOU 764 N SER A 118 3129 3968 4715 85 -19 593 N ATOM 765 CA SER A 118 98.541 20.274 241.431 1.00 32.56 C ANISOU 765 CA SER A 118 3321 4227 4822 174 23 660 C ATOM 766 C SER A 118 98.849 21.727 241.765 1.00 42.46 C ANISOU 766 C SER A 118 4521 5537 6075 113 -72 728 C ATOM 767 O SER A 118 99.357 22.033 242.841 1.00 56.00 O ANISOU 767 O SER A 118 6218 7284 7776 144 -41 752 O ATOM 768 CB SER A 118 99.664 19.674 240.581 1.00 35.09 C ANISOU 768 CB SER A 118 3648 4692 4991 236 54 653 C ATOM 769 OG SER A 118 100.912 19.754 241.246 1.00 52.98 O ANISOU 769 OG SER A 118 5859 7128 7144 342 88 693 O ATOM 770 N LEU A 119 98.527 22.619 240.836 1.00 43.01 N ANISOU 770 N LEU A 119 4600 5605 6138 20 -187 757 N ATOM 771 CA LEU A 119 98.745 24.046 241.029 1.00 36.43 C ANISOU 771 CA LEU A 119 3818 4739 5285 -61 -278 824 C ATOM 772 C LEU A 119 97.682 24.648 241.942 1.00 45.49 C ANISOU 772 C LEU A 119 4988 5727 6571 12 -315 791 C ATOM 773 O LEU A 119 97.937 25.622 242.649 1.00 57.16 O ANISOU 773 O LEU A 119 6532 7140 8047 -18 -342 811 O ATOM 774 CB LEU A 119 98.754 24.767 239.681 1.00 24.11 C ANISOU 774 CB LEU A 119 2339 3190 3634 -164 -389 891 C ATOM 775 CG LEU A 119 99.855 24.319 238.720 1.00 41.68 C ANISOU 775 CG LEU A 119 4522 5630 5685 -263 -349 911 C ATOM 776 CD1 LEU A 119 99.490 24.668 237.291 1.00 25.27 C ANISOU 776 CD1 LEU A 119 2516 3561 3524 -338 -450 962 C ATOM 777 CD2 LEU A 119 101.185 24.948 239.105 1.00 30.22 C ANISOU 777 CD2 LEU A 119 3059 4336 4087 -416 -313 951 C ATOM 778 N CYS A 120 96.489 24.062 241.920 1.00 40.33 N ANISOU 778 N CYS A 120 4269 5040 6016 91 -308 716 N ATOM 779 CA CYS A 120 95.394 24.531 242.759 1.00 38.24 C ANISOU 779 CA CYS A 120 3964 4706 5858 181 -333 649 C ATOM 780 C CYS A 120 95.664 24.262 244.235 1.00 37.77 C ANISOU 780 C CYS A 120 3880 4639 5831 193 -216 620 C ATOM 781 O CYS A 120 95.483 25.142 245.077 1.00 42.62 O ANISOU 781 O CYS A 120 4516 5198 6479 239 -242 597 O ATOM 782 CB CYS A 120 94.077 23.873 242.340 1.00 43.01 C ANISOU 782 CB CYS A 120 4445 5384 6514 209 -337 546 C ATOM 783 SG CYS A 120 93.302 24.615 240.888 1.00 43.02 S ANISOU 783 SG CYS A 120 4437 5441 6469 286 -531 557 S ATOM 784 N PHE A 121 96.098 23.045 244.546 1.00 31.08 N ANISOU 784 N PHE A 121 3020 3836 4953 171 -89 620 N ATOM 785 CA PHE A 121 96.358 22.672 245.931 1.00 33.09 C ANISOU 785 CA PHE A 121 3276 4096 5201 203 20 616 C ATOM 786 C PHE A 121 97.609 23.354 246.468 1.00 33.29 C ANISOU 786 C PHE A 121 3319 4191 5138 202 2 673 C ATOM 787 O PHE A 121 97.663 23.709 247.643 1.00 54.02 O ANISOU 787 O PHE A 121 5931 6833 7761 219 34 653 O ATOM 788 CB PHE A 121 96.476 21.154 246.070 1.00 21.81 C ANISOU 788 CB PHE A 121 1909 2648 3731 213 153 620 C ATOM 789 CG PHE A 121 95.154 20.445 246.012 1.00 34.10 C ANISOU 789 CG PHE A 121 3456 4150 5349 126 218 532 C ATOM 790 CD1 PHE A 121 94.240 20.577 247.044 1.00 28.34 C ANISOU 790 CD1 PHE A 121 2663 3442 4665 88 273 468 C ATOM 791 CD2 PHE A 121 94.821 19.654 244.927 1.00 29.34 C ANISOU 791 CD2 PHE A 121 2894 3520 4735 50 233 488 C ATOM 792 CE1 PHE A 121 93.019 19.933 246.995 1.00 32.32 C ANISOU 792 CE1 PHE A 121 3118 3973 5188 -53 347 363 C ATOM 793 CE2 PHE A 121 93.601 19.006 244.871 1.00 34.51 C ANISOU 793 CE2 PHE A 121 3523 4175 5415 -101 302 378 C ATOM 794 CZ PHE A 121 92.699 19.147 245.907 1.00 44.65 C ANISOU 794 CZ PHE A 121 4719 5514 6731 -166 362 315 C ATOM 795 N ILE A 122 98.607 23.537 245.607 1.00 30.43 N ANISOU 795 N ILE A 122 2968 3914 4679 152 -41 727 N ATOM 796 CA ILE A 122 99.800 24.302 245.963 1.00 36.85 C ANISOU 796 CA ILE A 122 3767 4864 5371 72 -61 755 C ATOM 797 C ILE A 122 99.401 25.705 246.411 1.00 39.94 C ANISOU 797 C ILE A 122 4239 5126 5811 -15 -133 727 C ATOM 798 O ILE A 122 99.898 26.216 247.416 1.00 29.65 O ANISOU 798 O ILE A 122 2929 3885 4453 -66 -111 697 O ATOM 799 CB ILE A 122 100.792 24.388 244.782 1.00 33.45 C ANISOU 799 CB ILE A 122 3319 4587 4804 -28 -94 797 C ATOM 800 CG1 ILE A 122 101.623 23.108 244.690 1.00 39.00 C ANISOU 800 CG1 ILE A 122 3933 5491 5395 111 -11 796 C ATOM 801 CG2 ILE A 122 101.717 25.586 244.933 1.00 34.51 C ANISOU 801 CG2 ILE A 122 3466 4836 4809 -237 -133 806 C ATOM 802 CD1 ILE A 122 102.553 23.071 243.498 1.00 60.43 C ANISOU 802 CD1 ILE A 122 6585 8420 7956 39 -28 806 C ATOM 803 N THR A 123 98.490 26.315 245.660 1.00 41.94 N ANISOU 803 N THR A 123 4583 5203 6149 -6 -225 727 N ATOM 804 CA THR A 123 97.931 27.609 246.024 1.00 36.30 C ANISOU 804 CA THR A 123 4006 4303 5483 0 -303 692 C ATOM 805 C THR A 123 97.156 27.496 247.334 1.00 40.17 C ANISOU 805 C THR A 123 4420 4777 6065 127 -247 591 C ATOM 806 O THR A 123 97.195 28.396 248.173 1.00 48.25 O ANISOU 806 O THR A 123 5529 5724 7081 114 -257 532 O ATOM 807 CB THR A 123 97.004 28.151 244.917 1.00 39.42 C ANISOU 807 CB THR A 123 4512 4540 5926 84 -429 718 C ATOM 808 OG1 THR A 123 97.742 28.285 243.697 1.00 41.30 O ANISOU 808 OG1 THR A 123 4839 4805 6049 -63 -475 821 O ATOM 809 CG2 THR A 123 96.428 29.504 245.307 1.00 32.34 C ANISOU 809 CG2 THR A 123 3816 3412 5059 173 -519 678 C ATOM 810 N GLU A 124 96.464 26.373 247.505 1.00 38.88 N ANISOU 810 N GLU A 124 4115 4691 5965 218 -175 561 N ATOM 811 CA GLU A 124 95.658 26.136 248.698 1.00 36.23 C ANISOU 811 CA GLU A 124 3692 4387 5688 297 -99 467 C ATOM 812 C GLU A 124 96.527 25.938 249.939 1.00 37.43 C ANISOU 812 C GLU A 124 3831 4637 5755 252 -6 475 C ATOM 813 O GLU A 124 96.110 26.261 251.052 1.00 23.40 O ANISOU 813 O GLU A 124 2025 2878 3988 288 34 392 O ATOM 814 CB GLU A 124 94.746 24.924 248.491 1.00 36.13 C ANISOU 814 CB GLU A 124 3566 4440 5723 316 -24 437 C ATOM 815 CG GLU A 124 93.786 24.669 249.639 1.00 45.01 C ANISOU 815 CG GLU A 124 4586 5639 6876 342 69 331 C ATOM 816 CD GLU A 124 92.950 25.888 249.978 1.00 55.65 C ANISOU 816 CD GLU A 124 5890 6979 8276 472 -14 209 C ATOM 817 OE1 GLU A 124 93.030 26.360 251.131 1.00 55.39 O ANISOU 817 OE1 GLU A 124 5861 6963 8221 500 29 148 O ATOM 818 OE2 GLU A 124 92.214 26.373 249.095 1.00 74.82 O ANISOU 818 OE2 GLU A 124 8288 9394 10745 576 -127 166 O ATOM 819 N ILE A 125 97.731 25.404 249.745 1.00 25.78 N ANISOU 819 N ILE A 125 2355 3271 4171 196 24 561 N ATOM 820 CA ILE A 125 98.688 25.259 250.839 1.00 26.85 C ANISOU 820 CA ILE A 125 2451 3572 4178 184 85 571 C ATOM 821 C ILE A 125 98.977 26.614 251.471 1.00 23.37 C ANISOU 821 C ILE A 125 2056 3125 3701 80 36 494 C ATOM 822 O ILE A 125 98.891 26.778 252.688 1.00 23.83 O ANISOU 822 O ILE A 125 2084 3248 3723 97 84 429 O ATOM 823 CB ILE A 125 100.027 24.645 250.371 1.00 44.08 C ANISOU 823 CB ILE A 125 4589 5948 6212 182 95 652 C ATOM 824 CG1 ILE A 125 99.817 23.264 249.750 1.00 37.22 C ANISOU 824 CG1 ILE A 125 3742 5040 5361 305 151 712 C ATOM 825 CG2 ILE A 125 100.996 24.544 251.536 1.00 26.65 C ANISOU 825 CG2 ILE A 125 2300 3990 3834 210 137 650 C ATOM 826 CD1 ILE A 125 99.431 22.203 250.738 1.00 35.65 C ANISOU 826 CD1 ILE A 125 3588 4814 5143 426 260 736 C ATOM 827 N ALA A 126 99.317 27.582 250.626 1.00 31.55 N ANISOU 827 N ALA A 126 3200 4065 4724 -48 -52 498 N ATOM 828 CA ALA A 126 99.664 28.922 251.079 1.00 34.46 C ANISOU 828 CA ALA A 126 3702 4358 5034 -203 -92 420 C ATOM 829 C ALA A 126 98.485 29.606 251.758 1.00 31.42 C ANISOU 829 C ALA A 126 3409 3763 4766 -74 -108 306 C ATOM 830 O ALA A 126 98.636 30.188 252.831 1.00 27.03 O ANISOU 830 O ALA A 126 2887 3228 4156 -123 -79 200 O ATOM 831 CB ALA A 126 100.160 29.760 249.910 1.00 33.11 C ANISOU 831 CB ALA A 126 3707 4067 4808 -392 -172 472 C ATOM 832 N LEU A 127 97.317 29.529 251.128 1.00 32.58 N ANISOU 832 N LEU A 127 3574 3755 5050 102 -156 307 N ATOM 833 CA LEU A 127 96.108 30.156 251.655 1.00 27.01 C ANISOU 833 CA LEU A 127 2910 2916 4437 290 -181 175 C ATOM 834 C LEU A 127 95.734 29.607 253.028 1.00 40.31 C ANISOU 834 C LEU A 127 4417 4784 6116 347 -66 80 C ATOM 835 O LEU A 127 95.463 30.370 253.956 1.00 28.09 O ANISOU 835 O LEU A 127 2924 3195 4553 394 -55 -58 O ATOM 836 CB LEU A 127 94.941 29.963 250.685 1.00 27.13 C ANISOU 836 CB LEU A 127 2882 2866 4558 483 -254 185 C ATOM 837 CG LEU A 127 95.035 30.698 249.349 1.00 42.30 C ANISOU 837 CG LEU A 127 5023 4580 6471 489 -390 274 C ATOM 838 CD1 LEU A 127 93.867 30.323 248.451 1.00 36.39 C ANISOU 838 CD1 LEU A 127 4158 3872 5795 696 -463 274 C ATOM 839 CD2 LEU A 127 95.079 32.200 249.575 1.00 39.43 C ANISOU 839 CD2 LEU A 127 4987 3924 6070 525 -469 215 C ATOM 840 N ASP A 128 95.722 28.283 253.149 1.00 39.63 N ANISOU 840 N ASP A 128 4156 4880 6022 338 25 152 N ATOM 841 CA ASP A 128 95.382 27.628 254.407 1.00 40.35 C ANISOU 841 CA ASP A 128 4118 5141 6072 361 147 100 C ATOM 842 C ASP A 128 96.335 28.045 255.519 1.00 31.86 C ANISOU 842 C ASP A 128 3072 4171 4862 273 180 67 C ATOM 843 O ASP A 128 95.927 28.224 256.667 1.00 40.54 O ANISOU 843 O ASP A 128 4123 5359 5922 305 244 -43 O ATOM 844 CB ASP A 128 95.404 26.108 254.246 1.00 53.65 C ANISOU 844 CB ASP A 128 5723 6928 7732 337 241 219 C ATOM 845 CG ASP A 128 95.000 25.383 255.515 1.00 57.61 C ANISOU 845 CG ASP A 128 6157 7574 8160 332 379 195 C ATOM 846 OD1 ASP A 128 94.054 25.843 256.187 1.00 66.86 O ANISOU 846 OD1 ASP A 128 7251 8797 9357 367 411 52 O ATOM 847 OD2 ASP A 128 95.633 24.357 255.842 1.00 59.83 O ANISOU 847 OD2 ASP A 128 6476 7923 8334 311 456 319 O ATOM 848 N ARG A 129 97.607 28.200 255.171 1.00 37.32 N ANISOU 848 N ARG A 129 3815 4906 5457 147 140 145 N ATOM 849 CA ARG A 129 98.613 28.607 256.140 1.00 39.54 C ANISOU 849 CA ARG A 129 4086 5365 5572 26 161 96 C ATOM 850 C ARG A 129 98.647 30.126 256.279 1.00 58.03 C ANISOU 850 C ARG A 129 6604 7533 7911 -90 99 -53 C ATOM 851 O ARG A 129 99.191 30.656 257.244 1.00 47.98 O ANISOU 851 O ARG A 129 5341 6382 6508 -211 124 -160 O ATOM 852 CB ARG A 129 99.987 28.061 255.744 1.00 26.35 C ANISOU 852 CB ARG A 129 2340 3918 3752 -63 151 213 C ATOM 853 CG ARG A 129 100.018 26.541 255.675 1.00 44.04 C ANISOU 853 CG ARG A 129 4487 6278 5969 103 214 354 C ATOM 854 CD ARG A 129 101.429 25.978 255.691 1.00 55.80 C ANISOU 854 CD ARG A 129 5869 8080 7250 115 211 434 C ATOM 855 NE ARG A 129 102.136 26.178 254.430 1.00 33.70 N ANISOU 855 NE ARG A 129 3061 5307 4438 19 149 469 N ATOM 856 CZ ARG A 129 103.205 25.478 254.060 1.00 52.80 C ANISOU 856 CZ ARG A 129 5361 8002 6698 92 146 538 C ATOM 857 NH1 ARG A 129 103.683 24.525 254.850 1.00 43.47 N ANISOU 857 NH1 ARG A 129 4096 7059 5360 309 188 595 N ATOM 858 NH2 ARG A 129 103.792 25.723 252.896 1.00 59.58 N ANISOU 858 NH2 ARG A 129 6193 8914 7528 -25 102 550 N ATOM 859 N TYR A 130 98.053 30.826 255.319 1.00 55.66 N ANISOU 859 N TYR A 130 6477 6935 7735 -48 18 -64 N ATOM 860 CA TYR A 130 97.936 32.276 255.410 1.00 38.17 C ANISOU 860 CA TYR A 130 4535 4451 5516 -107 -41 -199 C ATOM 861 C TYR A 130 96.891 32.652 256.454 1.00 42.74 C ANISOU 861 C TYR A 130 5107 4984 6146 94 -6 -382 C ATOM 862 O TYR A 130 97.196 33.337 257.428 1.00 43.77 O ANISOU 862 O TYR A 130 5326 5126 6180 -2 26 -533 O ATOM 863 CB TYR A 130 97.575 32.882 254.052 1.00 40.35 C ANISOU 863 CB TYR A 130 5045 4405 5879 -60 -151 -130 C ATOM 864 CG TYR A 130 97.428 34.388 254.067 1.00 38.36 C ANISOU 864 CG TYR A 130 5188 3782 5607 -85 -217 -246 C ATOM 865 CD1 TYR A 130 98.543 35.215 254.123 1.00 37.42 C ANISOU 865 CD1 TYR A 130 5314 3574 5332 -445 -213 -273 C ATOM 866 CD2 TYR A 130 96.174 34.983 254.014 1.00 43.86 C ANISOU 866 CD2 TYR A 130 6030 4224 6412 253 -282 -342 C ATOM 867 CE1 TYR A 130 98.412 36.592 254.133 1.00 39.16 C ANISOU 867 CE1 TYR A 130 5990 3375 5513 -498 -261 -380 C ATOM 868 CE2 TYR A 130 96.034 36.358 254.023 1.00 43.97 C ANISOU 868 CE2 TYR A 130 6482 3834 6390 291 -348 -447 C ATOM 869 CZ TYR A 130 97.155 37.157 254.083 1.00 40.64 C ANISOU 869 CZ TYR A 130 6377 3244 5821 -100 -332 -459 C ATOM 870 OH TYR A 130 97.020 38.526 254.092 1.00 46.67 O ANISOU 870 OH TYR A 130 7670 3531 6531 -92 -385 -564 O ATOM 871 N TYR A 131 95.663 32.182 256.254 1.00 40.72 N ANISOU 871 N TYR A 131 4724 4728 6019 355 -5 -391 N ATOM 872 CA TYR A 131 94.560 32.484 257.162 1.00 36.00 C ANISOU 872 CA TYR A 131 4060 4165 5453 571 35 -585 C ATOM 873 C TYR A 131 94.813 31.978 258.581 1.00 38.49 C ANISOU 873 C TYR A 131 4196 4775 5651 479 164 -652 C ATOM 874 O TYR A 131 94.253 32.504 259.542 1.00 53.48 O ANISOU 874 O TYR A 131 6090 6714 7517 581 206 -850 O ATOM 875 CB TYR A 131 93.253 31.889 256.629 1.00 43.79 C ANISOU 875 CB TYR A 131 4853 5229 6555 810 27 -585 C ATOM 876 CG TYR A 131 92.698 32.596 255.412 1.00 51.29 C ANISOU 876 CG TYR A 131 5972 5921 7593 1009 -119 -573 C ATOM 877 CD1 TYR A 131 92.035 33.811 255.533 1.00 61.74 C ANISOU 877 CD1 TYR A 131 7497 7032 8929 1276 -201 -745 C ATOM 878 CD2 TYR A 131 92.827 32.045 254.143 1.00 61.79 C ANISOU 878 CD2 TYR A 131 7283 7224 8972 963 -180 -394 C ATOM 879 CE1 TYR A 131 91.523 34.460 254.425 1.00 72.54 C ANISOU 879 CE1 TYR A 131 9059 8159 10344 1516 -351 -713 C ATOM 880 CE2 TYR A 131 92.318 32.687 253.029 1.00 83.68 C ANISOU 880 CE2 TYR A 131 10216 9788 11792 1158 -324 -369 C ATOM 881 CZ TYR A 131 91.667 33.894 253.175 1.00 86.32 C ANISOU 881 CZ TYR A 131 10764 9907 12126 1446 -415 -516 C ATOM 882 OH TYR A 131 91.158 34.537 252.070 1.00101.31 O ANISOU 882 OH TYR A 131 12861 11593 14040 1696 -574 -469 O ATOM 883 N ALA A 132 95.658 30.960 258.709 1.00 49.15 N ANISOU 883 N ALA A 132 5415 6342 6917 318 221 -491 N ATOM 884 CA ALA A 132 95.933 30.356 260.009 1.00 36.63 C ANISOU 884 CA ALA A 132 3681 5051 5185 260 332 -508 C ATOM 885 C ALA A 132 96.932 31.169 260.828 1.00 36.95 C ANISOU 885 C ALA A 132 3810 5167 5062 89 324 -617 C ATOM 886 O ALA A 132 96.787 31.293 262.044 1.00 47.42 O ANISOU 886 O ALA A 132 5074 6667 6277 89 395 -748 O ATOM 887 CB ALA A 132 96.439 28.933 259.830 1.00 32.00 C ANISOU 887 CB ALA A 132 2973 4646 4541 222 384 -286 C ATOM 888 N ILE A 133 97.944 31.721 260.165 1.00 32.68 N ANISOU 888 N ILE A 133 3405 4530 4482 -92 247 -578 N ATOM 889 CA ILE A 133 99.009 32.434 260.866 1.00 34.35 C ANISOU 889 CA ILE A 133 3677 4874 4500 -339 246 -693 C ATOM 890 C ILE A 133 98.647 33.884 261.195 1.00 52.98 C ANISOU 890 C ILE A 133 6316 6943 6873 -392 223 -937 C ATOM 891 O ILE A 133 98.659 34.279 262.361 1.00 66.00 O ANISOU 891 O ILE A 133 7957 8720 8402 -438 276 -1121 O ATOM 892 CB ILE A 133 100.320 32.430 260.054 1.00 40.81 C ANISOU 892 CB ILE A 133 4502 5787 5216 -584 192 -578 C ATOM 893 CG1 ILE A 133 100.811 30.998 259.831 1.00 38.70 C ANISOU 893 CG1 ILE A 133 3979 5829 4894 -481 214 -364 C ATOM 894 CG2 ILE A 133 101.387 33.249 260.763 1.00 40.14 C ANISOU 894 CG2 ILE A 133 4459 5893 4901 -907 196 -737 C ATOM 895 CD1 ILE A 133 101.010 30.210 261.100 1.00 48.55 C ANISOU 895 CD1 ILE A 133 5029 7441 5974 -387 283 -352 C ATOM 896 N VAL A 134 98.327 34.675 260.175 1.00 37.56 N ANISOU 896 N VAL A 134 4643 4583 5046 -367 144 -940 N ATOM 897 CA VAL A 134 98.100 36.104 260.377 1.00 62.16 C ANISOU 897 CA VAL A 134 8136 7331 8149 -405 114 -1158 C ATOM 898 C VAL A 134 96.677 36.415 260.850 1.00 67.95 C ANISOU 898 C VAL A 134 8902 7916 9000 -14 124 -1327 C ATOM 899 O VAL A 134 96.480 37.266 261.719 1.00 95.83 O ANISOU 899 O VAL A 134 12607 11344 12461 5 153 -1572 O ATOM 900 CB VAL A 134 98.410 36.915 259.086 1.00 58.16 C ANISOU 900 CB VAL A 134 8010 6407 7680 -540 20 -1076 C ATOM 901 CG1 VAL A 134 97.634 36.380 257.894 1.00 60.15 C ANISOU 901 CG1 VAL A 134 8207 6531 8117 -255 -51 -886 C ATOM 902 CG2 VAL A 134 98.126 38.396 259.296 1.00 71.76 C ANISOU 902 CG2 VAL A 134 10233 7657 9375 -549 -9 -1292 C ATOM 903 N TYR A 135 95.689 35.715 260.301 1.00 45.72 N ANISOU 903 N TYR A 135 5897 5135 6339 289 106 -1223 N ATOM 904 CA TYR A 135 94.294 35.995 260.631 1.00 50.44 C ANISOU 904 CA TYR A 135 6460 5682 7025 676 110 -1400 C ATOM 905 C TYR A 135 93.736 35.017 261.663 1.00 54.21 C ANISOU 905 C TYR A 135 6535 6603 7461 747 236 -1448 C ATOM 906 O TYR A 135 92.580 35.132 262.071 1.00 64.01 O ANISOU 906 O TYR A 135 7656 7930 8735 1031 267 -1620 O ATOM 907 CB TYR A 135 93.436 35.975 259.364 1.00 43.96 C ANISOU 907 CB TYR A 135 5676 4667 6359 961 5 -1300 C ATOM 908 CG TYR A 135 93.629 37.191 258.483 1.00 55.72 C ANISOU 908 CG TYR A 135 7654 5650 7866 1003 -123 -1298 C ATOM 909 CD1 TYR A 135 93.897 38.436 259.036 1.00 64.05 C ANISOU 909 CD1 TYR A 135 9119 6383 8832 962 -130 -1496 C ATOM 910 CD2 TYR A 135 93.551 37.092 257.100 1.00 55.18 C ANISOU 910 CD2 TYR A 135 7683 5407 7878 1065 -232 -1097 C ATOM 911 CE1 TYR A 135 94.077 39.550 258.239 1.00 67.26 C ANISOU 911 CE1 TYR A 135 10069 6260 9227 974 -237 -1477 C ATOM 912 CE2 TYR A 135 93.730 38.202 256.293 1.00 55.68 C ANISOU 912 CE2 TYR A 135 8249 4984 7921 1093 -346 -1066 C ATOM 913 CZ TYR A 135 93.993 39.428 256.868 1.00 69.05 C ANISOU 913 CZ TYR A 135 10395 6319 9523 1043 -345 -1248 C ATOM 914 OH TYR A 135 94.172 40.536 256.072 1.00 91.51 O ANISOU 914 OH TYR A 135 13833 8615 12322 1046 -448 -1201 O ATOM 915 N MET A 136 94.568 34.064 262.078 1.00 46.79 N ANISOU 915 N MET A 136 5398 5961 6420 498 308 -1298 N ATOM 916 CA MET A 136 94.208 33.083 263.103 1.00 41.64 C ANISOU 916 CA MET A 136 4440 5702 5677 507 437 -1297 C ATOM 917 C MET A 136 92.922 32.325 262.779 1.00 43.72 C ANISOU 917 C MET A 136 4482 6080 6049 712 480 -1269 C ATOM 918 O MET A 136 92.125 32.031 263.670 1.00 38.96 O ANISOU 918 O MET A 136 3687 5736 5378 785 589 -1395 O ATOM 919 CB MET A 136 94.077 33.763 264.469 1.00 44.05 C ANISOU 919 CB MET A 136 4763 6133 5841 511 507 -1562 C ATOM 920 CG MET A 136 95.374 34.362 264.993 1.00 61.74 C ANISOU 920 CG MET A 136 7165 8378 7917 232 490 -1618 C ATOM 921 SD MET A 136 95.212 35.044 266.656 1.00 84.75 S ANISOU 921 SD MET A 136 10078 11491 10631 213 584 -1947 S ATOM 922 CE MET A 136 93.994 36.330 266.383 1.00 84.12 C ANISOU 922 CE MET A 136 10256 11006 10702 553 540 -2242 C ATOM 923 N ARG A 137 92.727 32.011 261.503 1.00 67.33 N ANISOU 923 N ARG A 137 7485 8916 9179 769 402 -1118 N ATOM 924 CA ARG A 137 91.568 31.237 261.073 1.00 35.91 C ANISOU 924 CA ARG A 137 3279 5084 5281 899 440 -1097 C ATOM 925 C ARG A 137 91.981 29.808 260.741 1.00 33.60 C ANISOU 925 C ARG A 137 2883 4912 4971 705 505 -843 C ATOM 926 O ARG A 137 92.672 29.567 259.751 1.00 66.29 O ANISOU 926 O ARG A 137 7127 8890 9170 637 428 -666 O ATOM 927 CB ARG A 137 90.897 31.891 259.864 1.00 36.65 C ANISOU 927 CB ARG A 137 3457 4950 5520 1137 301 -1137 C ATOM 928 CG ARG A 137 89.667 31.152 259.363 1.00 50.55 C ANISOU 928 CG ARG A 137 4935 6936 7335 1255 327 -1154 C ATOM 929 N TYR A 138 91.557 28.863 261.573 1.00 42.48 N ANISOU 929 N TYR A 138 3837 6311 5993 617 654 -829 N ATOM 930 CA TYR A 138 91.951 27.469 261.404 1.00 32.35 C ANISOU 930 CA TYR A 138 2544 5089 4657 450 732 -590 C ATOM 931 C TYR A 138 90.821 26.626 260.821 1.00 37.85 C ANISOU 931 C TYR A 138 3099 5868 5414 416 799 -582 C ATOM 932 O TYR A 138 89.651 26.815 261.154 1.00 41.42 O ANISOU 932 O TYR A 138 3362 6520 5856 466 859 -773 O ATOM 933 CB TYR A 138 92.414 26.884 262.740 1.00 32.93 C ANISOU 933 CB TYR A 138 2617 5371 4523 333 859 -532 C ATOM 934 CG TYR A 138 93.556 27.649 263.370 1.00 42.45 C ANISOU 934 CG TYR A 138 3918 6583 5627 326 796 -562 C ATOM 935 CD1 TYR A 138 94.875 27.361 263.044 1.00 31.86 C ANISOU 935 CD1 TYR A 138 2677 5201 4228 271 730 -381 C ATOM 936 CD2 TYR A 138 93.314 28.663 264.287 1.00 34.84 C ANISOU 936 CD2 TYR A 138 2928 5708 4600 368 807 -800 C ATOM 937 CE1 TYR A 138 95.921 28.060 263.617 1.00 58.49 C ANISOU 937 CE1 TYR A 138 6090 8662 7471 215 677 -437 C ATOM 938 CE2 TYR A 138 94.353 29.368 264.865 1.00 44.68 C ANISOU 938 CE2 TYR A 138 4266 6980 5729 303 758 -856 C ATOM 939 CZ TYR A 138 95.655 29.062 264.526 1.00 59.49 C ANISOU 939 CZ TYR A 138 6210 8856 7538 205 693 -675 C ATOM 940 OH TYR A 138 96.692 29.761 265.100 1.00 67.92 O ANISOU 940 OH TYR A 138 7323 10029 8453 92 648 -759 O ATOM 941 N ARG A 139 91.186 25.695 259.946 1.00 41.17 N ANISOU 941 N ARG A 139 3600 6169 5874 323 792 -384 N ATOM 942 CA ARG A 139 90.218 24.825 259.289 1.00 46.88 C ANISOU 942 CA ARG A 139 4222 6955 6636 224 858 -380 C ATOM 943 C ARG A 139 90.342 23.388 259.782 1.00 44.08 C ANISOU 943 C ARG A 139 3973 6637 6140 -2 1028 -216 C ATOM 944 O ARG A 139 91.428 22.809 259.751 1.00 50.34 O ANISOU 944 O ARG A 139 4973 7277 6879 -9 1022 -13 O ATOM 945 CB ARG A 139 90.404 24.872 257.771 1.00 42.92 C ANISOU 945 CB ARG A 139 3773 6256 6280 283 720 -307 C ATOM 946 CG ARG A 139 90.184 26.240 257.149 1.00 58.37 C ANISOU 946 CG ARG A 139 5698 8126 8353 512 548 -437 C ATOM 947 CD ARG A 139 88.758 26.400 256.651 1.00 88.52 C ANISOU 947 CD ARG A 139 9285 12130 12218 613 524 -615 C ATOM 948 NE ARG A 139 87.990 27.342 257.459 1.00113.97 N ANISOU 948 NE ARG A 139 12366 15527 15410 810 523 -852 N ATOM 949 CZ ARG A 139 87.858 28.634 257.177 1.00113.16 C ANISOU 949 CZ ARG A 139 12331 15296 15369 1111 370 -969 C ATOM 950 NH1 ARG A 139 88.444 29.143 256.101 1.00102.17 N ANISOU 950 NH1 ARG A 139 11152 13602 14064 1202 211 -850 N ATOM 951 NH2 ARG A 139 87.139 29.417 257.968 1.00111.44 N ANISOU 951 NH2 ARG A 139 11998 15239 15104 1326 383 -1209 N ATOM 952 N PRO A 140 89.225 22.805 260.241 1.00 42.62 N ANISOU 952 N PRO A 140 3660 6666 5865 -183 1185 -309 N ATOM 953 CA PRO A 140 89.217 21.399 260.654 1.00 47.09 C ANISOU 953 CA PRO A 140 4411 7208 6273 -447 1366 -147 C ATOM 954 C PRO A 140 89.359 20.461 259.459 1.00 51.05 C ANISOU 954 C PRO A 140 5079 7475 6841 -549 1357 -15 C ATOM 955 O PRO A 140 89.178 20.893 258.319 1.00 55.36 O ANISOU 955 O PRO A 140 5511 7976 7548 -456 1226 -88 O ATOM 956 CB PRO A 140 87.851 21.237 261.324 1.00 45.94 C ANISOU 956 CB PRO A 140 4041 7404 6011 -666 1534 -337 C ATOM 957 CG PRO A 140 87.001 22.279 260.694 1.00 37.87 C ANISOU 957 CG PRO A 140 2683 6572 5133 -491 1414 -595 C ATOM 958 CD PRO A 140 87.910 23.443 260.422 1.00 48.83 C ANISOU 958 CD PRO A 140 4136 7755 6664 -152 1208 -583 C ATOM 959 N VAL A 141 89.682 19.199 259.723 1.00 40.43 N ANISOU 959 N VAL A 141 4037 5969 5354 -722 1492 175 N ATOM 960 CA VAL A 141 89.878 18.209 258.669 1.00 43.78 C ANISOU 960 CA VAL A 141 4692 6129 5814 -815 1504 290 C ATOM 961 C VAL A 141 88.624 18.048 257.812 1.00 54.61 C ANISOU 961 C VAL A 141 5862 7633 7255 -1055 1542 104 C ATOM 962 O VAL A 141 88.708 17.886 256.594 1.00 51.39 O ANISOU 962 O VAL A 141 5472 7093 6961 -1033 1454 101 O ATOM 963 CB VAL A 141 90.271 16.839 259.259 1.00 54.53 C ANISOU 963 CB VAL A 141 6487 7266 6967 -960 1672 509 C ATOM 964 CG1 VAL A 141 90.493 15.817 258.153 1.00 45.07 C ANISOU 964 CG1 VAL A 141 5578 5748 5797 -1029 1687 602 C ATOM 965 CG2 VAL A 141 91.515 16.974 260.120 1.00 54.14 C ANISOU 965 CG2 VAL A 141 6598 7168 6807 -677 1615 689 C ATOM 966 N LYS A 142 87.465 18.113 258.460 1.00 55.26 N ANISOU 966 N LYS A 142 5719 8036 7241 -1285 1672 -69 N ATOM 967 CA LYS A 142 86.185 17.938 257.782 1.00 48.18 C ANISOU 967 CA LYS A 142 4558 7397 6352 -1544 1722 -283 C ATOM 968 C LYS A 142 85.960 18.992 256.698 1.00 51.63 C ANISOU 968 C LYS A 142 4677 7955 6987 -1257 1496 -434 C ATOM 969 O LYS A 142 85.429 18.687 255.631 1.00 53.06 O ANISOU 969 O LYS A 142 4759 8193 7207 -1379 1464 -519 O ATOM 970 CB LYS A 142 85.042 17.978 258.798 1.00 46.28 C ANISOU 970 CB LYS A 142 4057 7590 5939 -1804 1897 -472 C ATOM 971 CG LYS A 142 83.707 17.494 258.259 1.00 59.09 C ANISOU 971 CG LYS A 142 5535 9435 7481 -2065 1894 -652 C ATOM 972 CD LYS A 142 82.661 17.441 259.361 1.00 72.20 C ANISOU 972 CD LYS A 142 7059 11438 8934 -2245 1986 -796 C ATOM 973 CE LYS A 142 81.343 16.884 258.851 1.00 70.42 C ANISOU 973 CE LYS A 142 6691 11485 8580 -2553 2001 -997 C ATOM 974 NZ LYS A 142 80.335 16.769 259.940 1.00 67.97 N ANISOU 974 NZ LYS A 142 6251 11539 8037 -2774 2107 -1152 N ATOM 975 N GLN A 143 86.371 20.226 256.972 1.00 60.09 N ANISOU 975 N GLN A 143 5624 9053 8157 -887 1341 -464 N ATOM 976 CA GLN A 143 86.202 21.316 256.016 1.00 35.99 C ANISOU 976 CA GLN A 143 2358 6054 5264 -580 1121 -578 C ATOM 977 C GLN A 143 87.232 21.252 254.894 1.00 33.47 C ANISOU 977 C GLN A 143 2273 5379 5067 -457 978 -397 C ATOM 978 O GLN A 143 86.933 21.592 253.749 1.00 44.91 O ANISOU 978 O GLN A 143 3607 6855 6603 -357 841 -457 O ATOM 979 CB GLN A 143 86.291 22.670 256.721 1.00 51.84 C ANISOU 979 CB GLN A 143 4240 8145 7310 -252 1021 -681 C ATOM 980 CG GLN A 143 85.150 22.951 257.679 1.00 62.12 C ANISOU 980 CG GLN A 143 5232 9878 8494 -290 1133 -924 C ATOM 981 CD GLN A 143 85.180 24.368 258.216 1.00 63.38 C ANISOU 981 CD GLN A 143 5301 10083 8699 90 1013 -1064 C ATOM 982 OE1 GLN A 143 85.948 25.207 257.745 1.00 40.69 O ANISOU 982 OE1 GLN A 143 2593 6917 5952 355 839 -992 O ATOM 983 NE2 GLN A 143 84.340 24.643 259.207 1.00 76.93 N ANISOU 983 NE2 GLN A 143 6892 12065 10274 94 1076 -1220 N ATOM 984 N ALA A 144 88.443 20.819 255.228 1.00 31.91 N ANISOU 984 N ALA A 144 2383 4894 4846 -448 1008 -184 N ATOM 985 CA ALA A 144 89.525 20.735 254.252 1.00 29.83 C ANISOU 985 CA ALA A 144 2318 4353 4663 -328 889 -25 C ATOM 986 C ALA A 144 89.210 19.713 253.163 1.00 44.04 C ANISOU 986 C ALA A 144 4194 6075 6463 -521 928 -13 C ATOM 987 O ALA A 144 89.571 19.902 252.000 1.00 52.89 O ANISOU 987 O ALA A 144 5330 7097 7668 -422 798 17 O ATOM 988 CB ALA A 144 90.837 20.389 254.942 1.00 30.76 C ANISOU 988 CB ALA A 144 2697 4285 4704 -258 925 170 C ATOM 989 N CYS A 145 88.538 18.632 253.546 1.00 37.90 N ANISOU 989 N CYS A 145 3489 5342 5570 -831 1119 -43 N ATOM 990 CA CYS A 145 88.117 17.617 252.588 1.00 51.61 C ANISOU 990 CA CYS A 145 5323 7008 7279 -1088 1184 -74 C ATOM 991 C CYS A 145 87.083 18.186 251.624 1.00 52.74 C ANISOU 991 C CYS A 145 5100 7451 7486 -1104 1072 -283 C ATOM 992 O CYS A 145 87.083 17.864 250.437 1.00 54.02 O ANISOU 992 O CYS A 145 5289 7554 7681 -1152 1007 -299 O ATOM 993 CB CYS A 145 87.550 16.392 253.311 1.00 57.65 C ANISOU 993 CB CYS A 145 6288 7747 7869 -1488 1435 -76 C ATOM 994 SG CYS A 145 88.750 15.489 254.317 1.00 69.46 S ANISOU 994 SG CYS A 145 8312 8846 9235 -1432 1562 204 S ATOM 995 N LEU A 146 86.205 19.037 252.145 1.00 54.36 N ANISOU 995 N LEU A 146 4961 8008 7687 -1031 1042 -452 N ATOM 996 CA LEU A 146 85.175 19.672 251.331 1.00 43.09 C ANISOU 996 CA LEU A 146 3154 6935 6286 -951 914 -660 C ATOM 997 C LEU A 146 85.795 20.619 250.310 1.00 41.44 C ANISOU 997 C LEU A 146 2963 6571 6212 -580 666 -582 C ATOM 998 O LEU A 146 85.383 20.651 249.151 1.00 49.93 O ANISOU 998 O LEU A 146 3912 7765 7297 -564 555 -650 O ATOM 999 CB LEU A 146 84.181 20.428 252.215 1.00 45.05 C ANISOU 999 CB LEU A 146 3039 7601 6475 -860 932 -866 C ATOM 1000 CG LEU A 146 83.034 21.139 251.495 1.00 40.79 C ANISOU 1000 CG LEU A 146 2206 7401 5894 -651 751 -1047 C ATOM 1001 CD1 LEU A 146 82.126 20.135 250.801 1.00 54.26 C ANISOU 1001 CD1 LEU A 146 3848 9313 7456 -1007 812 -1152 C ATOM 1002 CD2 LEU A 146 82.245 22.002 252.466 1.00 42.86 C ANISOU 1002 CD2 LEU A 146 2289 7923 6073 -433 726 -1190 C ATOM 1003 N PHE A 147 86.789 21.387 250.747 1.00 36.22 N ANISOU 1003 N PHE A 147 2469 5666 5627 -316 586 -444 N ATOM 1004 CA PHE A 147 87.480 22.316 249.862 1.00 48.48 C ANISOU 1004 CA PHE A 147 4103 7040 7277 -29 375 -352 C ATOM 1005 C PHE A 147 88.282 21.569 248.803 1.00 55.72 C ANISOU 1005 C PHE A 147 5233 7733 8207 -138 360 -209 C ATOM 1006 O PHE A 147 88.398 22.024 247.665 1.00 55.12 O ANISOU 1006 O PHE A 147 5145 7631 8165 -14 203 -185 O ATOM 1007 CB PHE A 147 88.399 23.243 250.660 1.00 41.62 C ANISOU 1007 CB PHE A 147 3384 5980 6451 178 327 -259 C ATOM 1008 CG PHE A 147 87.666 24.242 251.507 1.00 48.55 C ANISOU 1008 CG PHE A 147 4081 7042 7324 370 298 -423 C ATOM 1009 CD1 PHE A 147 86.331 24.527 251.268 1.00 62.57 C ANISOU 1009 CD1 PHE A 147 5552 9150 9071 467 255 -629 C ATOM 1010 CD2 PHE A 147 88.312 24.901 252.540 1.00 43.68 C ANISOU 1010 CD2 PHE A 147 3583 6304 6708 472 313 -394 C ATOM 1011 CE1 PHE A 147 85.653 25.448 252.046 1.00 64.70 C ANISOU 1011 CE1 PHE A 147 5652 9613 9320 706 228 -805 C ATOM 1012 CE2 PHE A 147 87.639 25.823 253.321 1.00 52.13 C ANISOU 1012 CE2 PHE A 147 4514 7529 7765 668 293 -571 C ATOM 1013 CZ PHE A 147 86.309 26.097 253.073 1.00 52.09 C ANISOU 1013 CZ PHE A 147 4218 7838 7737 808 251 -777 C ATOM 1014 N SER A 148 88.834 20.421 249.186 1.00 45.86 N ANISOU 1014 N SER A 148 4199 6318 6906 -346 523 -114 N ATOM 1015 CA SER A 148 89.588 19.586 248.258 1.00 40.09 C ANISOU 1015 CA SER A 148 3690 5378 6165 -422 532 -7 C ATOM 1016 C SER A 148 88.700 19.128 247.107 1.00 54.42 C ANISOU 1016 C SER A 148 5378 7341 7957 -590 509 -139 C ATOM 1017 O SER A 148 89.139 19.068 245.960 1.00 49.23 O ANISOU 1017 O SER A 148 4786 6606 7313 -544 415 -96 O ATOM 1018 CB SER A 148 90.185 18.376 248.981 1.00 36.55 C ANISOU 1018 CB SER A 148 3536 4717 5634 -564 719 99 C ATOM 1019 OG SER A 148 91.110 18.781 249.976 1.00 41.15 O ANISOU 1019 OG SER A 148 4214 5215 6207 -386 719 223 O ATOM 1020 N ILE A 149 87.448 18.810 247.424 1.00 56.21 N ANISOU 1020 N ILE A 149 5400 7836 8122 -807 600 -315 N ATOM 1021 CA ILE A 149 86.473 18.439 246.407 1.00 41.66 C ANISOU 1021 CA ILE A 149 3361 6245 6221 -998 575 -485 C ATOM 1022 C ILE A 149 86.239 19.607 245.455 1.00 38.88 C ANISOU 1022 C ILE A 149 2775 6080 5918 -687 326 -519 C ATOM 1023 O ILE A 149 86.200 19.429 244.239 1.00 45.84 O ANISOU 1023 O ILE A 149 3640 7004 6773 -715 234 -539 O ATOM 1024 CB ILE A 149 85.131 18.007 247.033 1.00 51.14 C ANISOU 1024 CB ILE A 149 4310 7811 7309 -1311 723 -701 C ATOM 1025 CG1 ILE A 149 85.322 16.769 247.909 1.00 45.37 C ANISOU 1025 CG1 ILE A 149 3900 6849 6490 -1676 986 -646 C ATOM 1026 CG2 ILE A 149 84.099 17.729 245.952 1.00 41.51 C ANISOU 1026 CG2 ILE A 149 2815 6958 5999 -1512 676 -912 C ATOM 1027 CD1 ILE A 149 85.815 15.555 247.153 1.00 38.22 C ANISOU 1027 CD1 ILE A 149 3365 5617 5541 -1915 1077 -590 C ATOM 1028 N PHE A 150 86.100 20.804 246.020 1.00 47.03 N ANISOU 1028 N PHE A 150 3670 7200 7001 -381 216 -521 N ATOM 1029 CA PHE A 150 85.865 22.010 245.232 1.00 44.62 C ANISOU 1029 CA PHE A 150 3227 7007 6719 -32 -25 -532 C ATOM 1030 C PHE A 150 87.018 22.304 244.276 1.00 40.37 C ANISOU 1030 C PHE A 150 2957 6156 6226 85 -147 -332 C ATOM 1031 O PHE A 150 86.797 22.709 243.135 1.00 34.17 O ANISOU 1031 O PHE A 150 2113 5466 5403 210 -312 -331 O ATOM 1032 CB PHE A 150 85.637 23.213 246.150 1.00 47.38 C ANISOU 1032 CB PHE A 150 3493 7403 7107 286 -95 -567 C ATOM 1033 CG PHE A 150 84.304 23.205 246.842 1.00 52.00 C ANISOU 1033 CG PHE A 150 3710 8433 7613 268 -30 -811 C ATOM 1034 CD1 PHE A 150 83.273 22.405 246.380 1.00 62.64 C ANISOU 1034 CD1 PHE A 150 4860 10115 8826 8 29 -957 C ATOM 1035 CD2 PHE A 150 84.080 24.003 247.952 1.00 56.42 C ANISOU 1035 CD2 PHE A 150 4228 9028 8180 482 -19 -868 C ATOM 1036 CE1 PHE A 150 82.045 22.397 247.014 1.00 70.66 C ANISOU 1036 CE1 PHE A 150 5680 11471 9696 -40 93 -1132 C ATOM 1037 CE2 PHE A 150 82.854 24.001 248.590 1.00 53.36 C ANISOU 1037 CE2 PHE A 150 3643 8979 7654 449 49 -1041 C ATOM 1038 CZ PHE A 150 81.836 23.197 248.120 1.00 63.69 C ANISOU 1038 CZ PHE A 150 4766 10619 8816 189 102 -1174 C ATOM 1039 N TRP A 151 88.245 22.100 244.744 1.00 29.74 N ANISOU 1039 N TRP A 151 1886 4484 4928 44 -66 -169 N ATOM 1040 CA TRP A 151 89.419 22.364 243.921 1.00 43.93 C ANISOU 1040 CA TRP A 151 3905 6051 6737 118 -156 2 C ATOM 1041 C TRP A 151 89.525 21.387 242.753 1.00 37.72 C ANISOU 1041 C TRP A 151 3159 5281 5893 -60 -135 -6 C ATOM 1042 O TRP A 151 89.863 21.785 241.639 1.00 50.93 O ANISOU 1042 O TRP A 151 4874 6943 7533 19 -269 60 O ATOM 1043 CB TRP A 151 90.692 22.312 244.767 1.00 39.77 C ANISOU 1043 CB TRP A 151 3594 5281 6237 116 -67 141 C ATOM 1044 CG TRP A 151 90.911 23.548 245.585 1.00 39.96 C ANISOU 1044 CG TRP A 151 3640 5243 6299 299 -135 169 C ATOM 1045 CD1 TRP A 151 90.889 23.647 246.945 1.00 32.21 C ANISOU 1045 CD1 TRP A 151 2644 4260 5333 307 -38 135 C ATOM 1046 CD2 TRP A 151 91.176 24.868 245.090 1.00 60.24 C ANISOU 1046 CD2 TRP A 151 6297 7719 8873 480 -307 230 C ATOM 1047 NE1 TRP A 151 91.129 24.944 247.328 1.00 36.28 N ANISOU 1047 NE1 TRP A 151 3220 4693 5872 481 -139 147 N ATOM 1048 CE2 TRP A 151 91.308 25.713 246.209 1.00 41.24 C ANISOU 1048 CE2 TRP A 151 3939 5235 6494 583 -302 210 C ATOM 1049 CE3 TRP A 151 91.316 25.415 243.811 1.00 66.67 C ANISOU 1049 CE3 TRP A 151 7191 8492 9649 548 -461 304 C ATOM 1050 CZ2 TRP A 151 91.574 27.077 246.087 1.00 41.76 C ANISOU 1050 CZ2 TRP A 151 4173 5139 6556 739 -437 251 C ATOM 1051 CZ3 TRP A 151 91.580 26.768 243.692 1.00 57.82 C ANISOU 1051 CZ3 TRP A 151 6244 7210 8513 705 -597 373 C ATOM 1052 CH2 TRP A 151 91.706 27.584 244.823 1.00 54.64 C ANISOU 1052 CH2 TRP A 151 5928 6688 8145 792 -581 341 C ATOM 1053 N TRP A 152 89.239 20.114 243.010 1.00 35.64 N ANISOU 1053 N TRP A 152 2919 5026 5596 -317 40 -89 N ATOM 1054 CA TRP A 152 89.253 19.109 241.951 1.00 46.67 C ANISOU 1054 CA TRP A 152 4388 6418 6924 -512 81 -140 C ATOM 1055 C TRP A 152 88.206 19.428 240.888 1.00 53.76 C ANISOU 1055 C TRP A 152 5028 7638 7761 -524 -61 -276 C ATOM 1056 O TRP A 152 88.465 19.291 239.693 1.00 56.69 O ANISOU 1056 O TRP A 152 5439 8026 8075 -536 -141 -263 O ATOM 1057 CB TRP A 152 89.015 17.708 242.521 1.00 30.49 C ANISOU 1057 CB TRP A 152 2485 4271 4830 -815 310 -220 C ATOM 1058 CG TRP A 152 90.248 17.065 243.086 1.00 35.97 C ANISOU 1058 CG TRP A 152 3516 4624 5528 -767 431 -71 C ATOM 1059 CD1 TRP A 152 90.555 16.896 244.405 1.00 40.19 C ANISOU 1059 CD1 TRP A 152 4175 5026 6071 -741 547 8 C ATOM 1060 CD2 TRP A 152 91.341 16.505 242.346 1.00 36.70 C ANISOU 1060 CD2 TRP A 152 3845 4517 5584 -696 438 8 C ATOM 1061 NE1 TRP A 152 91.769 16.266 244.533 1.00 37.04 N ANISOU 1061 NE1 TRP A 152 4074 4363 5636 -630 612 138 N ATOM 1062 CE2 TRP A 152 92.272 16.016 243.284 1.00 39.62 C ANISOU 1062 CE2 TRP A 152 4464 4652 5936 -590 551 130 C ATOM 1063 CE3 TRP A 152 91.622 16.371 240.983 1.00 41.68 C ANISOU 1063 CE3 TRP A 152 4486 5180 6170 -692 359 -24 C ATOM 1064 CZ2 TRP A 152 93.463 15.402 242.902 1.00 36.46 C ANISOU 1064 CZ2 TRP A 152 4303 4074 5477 -442 581 208 C ATOM 1065 CZ3 TRP A 152 92.805 15.761 240.606 1.00 36.09 C ANISOU 1065 CZ3 TRP A 152 4019 4283 5411 -582 405 47 C ATOM 1066 CH2 TRP A 152 93.710 15.284 241.562 1.00 34.98 C ANISOU 1066 CH2 TRP A 152 4105 3932 5253 -440 513 155 C ATOM 1067 N ILE A 153 87.027 19.856 241.330 1.00 32.91 N ANISOU 1067 N ILE A 153 2101 5298 5104 -500 -94 -416 N ATOM 1068 CA ILE A 153 85.968 20.267 240.416 1.00 45.30 C ANISOU 1068 CA ILE A 153 3367 7262 6582 -433 -256 -557 C ATOM 1069 C ILE A 153 86.404 21.494 239.623 1.00 56.64 C ANISOU 1069 C ILE A 153 4857 8639 8024 -66 -496 -404 C ATOM 1070 O ILE A 153 86.201 21.572 238.410 1.00 61.77 O ANISOU 1070 O ILE A 153 5445 9448 8577 -32 -631 -417 O ATOM 1071 CB ILE A 153 84.658 20.575 241.168 1.00 42.03 C ANISOU 1071 CB ILE A 153 2594 7248 6126 -407 -249 -753 C ATOM 1072 CG1 ILE A 153 84.130 19.316 241.857 1.00 47.98 C ANISOU 1072 CG1 ILE A 153 3306 8099 6824 -867 7 -913 C ATOM 1073 CG2 ILE A 153 83.609 21.129 240.217 1.00 40.40 C ANISOU 1073 CG2 ILE A 153 2047 7507 5795 -230 -454 -892 C ATOM 1074 CD1 ILE A 153 82.895 19.553 242.698 1.00 53.55 C ANISOU 1074 CD1 ILE A 153 3727 9176 7442 -874 50 -1084 C ATOM 1075 N PHE A 154 87.017 22.446 240.318 1.00 48.16 N ANISOU 1075 N PHE A 154 3933 7327 7041 179 -541 -259 N ATOM 1076 CA PHE A 154 87.504 23.668 239.689 1.00 47.20 C ANISOU 1076 CA PHE A 154 3960 7067 6907 477 -744 -96 C ATOM 1077 C PHE A 154 88.646 23.373 238.719 1.00 53.22 C ANISOU 1077 C PHE A 154 4958 7629 7633 356 -750 58 C ATOM 1078 O PHE A 154 88.822 24.074 237.723 1.00 57.09 O ANISOU 1078 O PHE A 154 5535 8114 8041 496 -917 162 O ATOM 1079 CB PHE A 154 87.958 24.668 240.755 1.00 39.81 C ANISOU 1079 CB PHE A 154 3175 5889 6060 679 -753 -6 C ATOM 1080 CG PHE A 154 88.442 25.974 240.195 1.00 38.95 C ANISOU 1080 CG PHE A 154 3304 5577 5920 935 -942 159 C ATOM 1081 CD1 PHE A 154 87.542 26.928 239.751 1.00 49.99 C ANISOU 1081 CD1 PHE A 154 4642 7107 7244 1274 -1144 128 C ATOM 1082 CD2 PHE A 154 89.797 26.252 240.121 1.00 39.43 C ANISOU 1082 CD2 PHE A 154 3663 5326 5992 835 -914 342 C ATOM 1083 CE1 PHE A 154 87.983 28.131 239.237 1.00 55.63 C ANISOU 1083 CE1 PHE A 154 5673 7562 7902 1498 -1310 302 C ATOM 1084 CE2 PHE A 154 90.245 27.455 239.608 1.00 39.10 C ANISOU 1084 CE2 PHE A 154 3890 5076 5888 988 -1065 495 C ATOM 1085 CZ PHE A 154 89.337 28.395 239.167 1.00 44.08 C ANISOU 1085 CZ PHE A 154 4543 5755 6451 1315 -1261 488 C ATOM 1086 N ALA A 155 89.415 22.330 239.014 1.00 35.24 N ANISOU 1086 N ALA A 155 2798 5200 5392 117 -565 69 N ATOM 1087 CA ALA A 155 90.531 21.939 238.162 1.00 35.34 C ANISOU 1087 CA ALA A 155 2999 5076 5352 23 -547 177 C ATOM 1088 C ALA A 155 90.039 21.286 236.875 1.00 50.33 C ANISOU 1088 C ALA A 155 4805 7180 7137 -102 -588 75 C ATOM 1089 O ALA A 155 90.711 21.341 235.846 1.00 62.71 O ANISOU 1089 O ALA A 155 6479 8731 8619 -111 -648 158 O ATOM 1090 CB ALA A 155 91.467 21.000 238.909 1.00 27.14 C ANISOU 1090 CB ALA A 155 2114 3838 4360 -108 -348 201 C ATOM 1091 N VAL A 156 88.866 20.666 236.938 1.00 51.49 N ANISOU 1091 N VAL A 156 4742 7561 7261 -233 -548 -120 N ATOM 1092 CA VAL A 156 88.291 20.008 235.771 1.00 54.95 C ANISOU 1092 CA VAL A 156 5064 8247 7568 -400 -581 -261 C ATOM 1093 C VAL A 156 87.681 21.027 234.815 1.00 56.72 C ANISOU 1093 C VAL A 156 5124 8747 7679 -171 -833 -233 C ATOM 1094 O VAL A 156 87.921 20.978 233.608 1.00 67.96 O ANISOU 1094 O VAL A 156 6588 10255 8979 -193 -923 -203 O ATOM 1095 CB VAL A 156 87.215 18.976 236.171 1.00 42.91 C ANISOU 1095 CB VAL A 156 3362 6926 6016 -697 -438 -508 C ATOM 1096 CG1 VAL A 156 86.465 18.480 234.944 1.00 38.11 C ANISOU 1096 CG1 VAL A 156 2577 6662 5241 -880 -502 -689 C ATOM 1097 CG2 VAL A 156 87.847 17.811 236.916 1.00 46.79 C ANISOU 1097 CG2 VAL A 156 4121 7088 6570 -936 -187 -518 C ATOM 1098 N ILE A 157 86.902 21.957 235.360 1.00 51.69 N ANISOU 1098 N ILE A 157 4324 8253 7065 81 -950 -242 N ATOM 1099 CA ILE A 157 86.215 22.953 234.544 1.00 62.09 C ANISOU 1099 CA ILE A 157 5509 9832 8248 387 -1206 -215 C ATOM 1100 C ILE A 157 87.194 23.931 233.897 1.00 63.56 C ANISOU 1100 C ILE A 157 6017 9736 8397 586 -1344 55 C ATOM 1101 O ILE A 157 86.869 24.577 232.901 1.00 84.65 O ANISOU 1101 O ILE A 157 8689 12566 10911 789 -1551 126 O ATOM 1102 CB ILE A 157 85.175 23.745 235.371 1.00 61.01 C ANISOU 1102 CB ILE A 157 5147 9902 8133 687 -1296 -304 C ATOM 1103 CG1 ILE A 157 85.862 24.654 236.393 1.00 73.12 C ANISOU 1103 CG1 ILE A 157 6941 11028 9813 895 -1279 -139 C ATOM 1104 CG2 ILE A 157 84.203 22.796 236.059 1.00 41.94 C ANISOU 1104 CG2 ILE A 157 2391 7822 5720 426 -1136 -581 C ATOM 1105 CD1 ILE A 157 85.748 26.132 236.072 1.00 78.98 C ANISOU 1105 CD1 ILE A 157 7839 11680 10488 1350 -1521 8 C ATOM 1106 N ILE A 158 88.392 24.035 234.462 1.00 38.04 N ANISOU 1106 N ILE A 158 3060 6115 5279 510 -1228 204 N ATOM 1107 CA ILE A 158 89.404 24.935 233.927 1.00 37.07 C ANISOU 1107 CA ILE A 158 3249 5741 5097 597 -1321 445 C ATOM 1108 C ILE A 158 90.289 24.196 232.926 1.00 56.66 C ANISOU 1108 C ILE A 158 5817 8230 7480 349 -1253 484 C ATOM 1109 O ILE A 158 91.039 24.811 232.167 1.00 62.77 O ANISOU 1109 O ILE A 158 6801 8910 8137 356 -1331 661 O ATOM 1110 CB ILE A 158 90.271 25.546 235.053 1.00 40.14 C ANISOU 1110 CB ILE A 158 3857 5779 5617 622 -1237 563 C ATOM 1111 CG1 ILE A 158 90.923 26.849 234.586 1.00 66.39 C ANISOU 1111 CG1 ILE A 158 7509 8871 8843 742 -1375 791 C ATOM 1112 CG2 ILE A 158 91.314 24.549 235.539 1.00 39.94 C ANISOU 1112 CG2 ILE A 158 3870 5635 5670 353 -1017 545 C ATOM 1113 CD1 ILE A 158 89.933 27.894 234.119 1.00 78.68 C ANISOU 1113 CD1 ILE A 158 9118 10482 10294 1093 -1611 838 C ATOM 1114 N ALA A 159 90.186 22.870 232.922 1.00 58.86 N ANISOU 1114 N ALA A 159 5956 8621 7786 118 -1098 306 N ATOM 1115 CA ALA A 159 90.946 22.046 231.991 1.00 42.28 C ANISOU 1115 CA ALA A 159 3932 6545 5586 -85 -1020 290 C ATOM 1116 C ALA A 159 90.130 21.744 230.741 1.00 52.38 C ANISOU 1116 C ALA A 159 5054 8158 6690 -133 -1135 176 C ATOM 1117 O ALA A 159 90.673 21.293 229.733 1.00 49.62 O ANISOU 1117 O ALA A 159 4769 7875 6209 -262 -1118 169 O ATOM 1118 CB ALA A 159 91.384 20.755 232.660 1.00 36.44 C ANISOU 1118 CB ALA A 159 3223 5673 4949 -279 -783 161 C ATOM 1119 N ILE A 160 88.826 22.002 230.820 1.00 60.21 N ANISOU 1119 N ILE A 160 5810 9409 7657 -19 -1253 68 N ATOM 1120 CA ILE A 160 87.893 21.740 229.722 1.00 40.40 C ANISOU 1120 CA ILE A 160 3080 7316 4954 -53 -1381 -74 C ATOM 1121 C ILE A 160 88.363 22.248 228.349 1.00 62.76 C ANISOU 1121 C ILE A 160 6044 10229 7573 18 -1539 83 C ATOM 1122 O ILE A 160 88.342 21.487 227.381 1.00 67.12 O ANISOU 1122 O ILE A 160 6531 10993 7979 -182 -1519 -41 O ATOM 1123 CB ILE A 160 86.498 22.346 230.025 1.00 59.79 C ANISOU 1123 CB ILE A 160 5242 10104 7372 188 -1544 -168 C ATOM 1124 CG1 ILE A 160 85.841 21.620 231.199 1.00 68.17 C ANISOU 1124 CG1 ILE A 160 6098 11229 8576 14 -1367 -388 C ATOM 1125 CG2 ILE A 160 85.599 22.275 228.801 1.00 46.29 C ANISOU 1125 CG2 ILE A 160 3283 8896 5408 217 -1724 -287 C ATOM 1126 CD1 ILE A 160 85.531 20.166 230.924 1.00 77.45 C ANISOU 1126 CD1 ILE A 160 7156 12575 9699 -425 -1192 -648 C ATOM 1127 N PRO A 161 88.807 23.518 228.248 1.00 58.04 N ANISOU 1127 N PRO A 161 5669 9449 6935 271 -1683 352 N ATOM 1128 CA PRO A 161 89.175 23.952 226.895 1.00 67.29 C ANISOU 1128 CA PRO A 161 6982 10725 7859 294 -1825 505 C ATOM 1129 C PRO A 161 90.508 23.385 226.401 1.00 67.81 C ANISOU 1129 C PRO A 161 7225 10655 7884 15 -1664 550 C ATOM 1130 O PRO A 161 90.958 23.760 225.318 1.00 71.22 O ANISOU 1130 O PRO A 161 7793 11172 8096 -10 -1753 687 O ATOM 1131 CB PRO A 161 89.258 25.473 227.034 1.00 54.06 C ANISOU 1131 CB PRO A 161 5573 8828 6140 612 -2004 784 C ATOM 1132 CG PRO A 161 89.661 25.686 228.443 1.00 44.42 C ANISOU 1132 CG PRO A 161 4444 7260 5175 623 -1867 802 C ATOM 1133 CD PRO A 161 88.967 24.610 229.230 1.00 43.85 C ANISOU 1133 CD PRO A 161 4042 7351 5269 513 -1726 521 C ATOM 1134 N HIS A 162 91.123 22.495 227.174 1.00 61.85 N ANISOU 1134 N HIS A 162 6469 9721 7311 -170 -1433 432 N ATOM 1135 CA HIS A 162 92.419 21.936 226.802 1.00 57.30 C ANISOU 1135 CA HIS A 162 6030 9054 6686 -361 -1277 447 C ATOM 1136 C HIS A 162 92.331 20.517 226.241 1.00 63.98 C ANISOU 1136 C HIS A 162 6769 10063 7479 -566 -1148 184 C ATOM 1137 O HIS A 162 93.190 20.107 225.461 1.00 84.68 O ANISOU 1137 O HIS A 162 9471 12741 9963 -677 -1077 167 O ATOM 1138 CB HIS A 162 93.367 21.952 228.003 1.00 49.10 C ANISOU 1138 CB HIS A 162 5111 7705 5840 -368 -1116 512 C ATOM 1139 CG HIS A 162 93.975 23.296 228.276 1.00 49.73 C ANISOU 1139 CG HIS A 162 5384 7610 5900 -279 -1198 771 C ATOM 1140 ND1 HIS A 162 95.156 23.705 227.698 1.00 46.39 N ANISOU 1140 ND1 HIS A 162 5122 7187 5317 -402 -1172 917 N ATOM 1141 CD2 HIS A 162 93.564 24.314 229.063 1.00 60.22 C ANISOU 1141 CD2 HIS A 162 6794 8759 7328 -108 -1293 889 C ATOM 1142 CE1 HIS A 162 95.448 24.925 228.120 1.00 51.67 C ANISOU 1142 CE1 HIS A 162 5989 7659 5984 -357 -1242 1121 C ATOM 1143 NE2 HIS A 162 94.499 25.317 228.948 1.00 47.46 N ANISOU 1143 NE2 HIS A 162 5432 6988 5615 -157 -1320 1107 N ATOM 1144 N PHE A 163 91.305 19.765 226.633 1.00 56.77 N ANISOU 1144 N PHE A 163 5689 9231 6651 -637 -1105 -38 N ATOM 1145 CA PHE A 163 91.184 18.385 226.166 1.00 58.45 C ANISOU 1145 CA PHE A 163 5872 9530 6805 -879 -963 -310 C ATOM 1146 C PHE A 163 89.910 18.122 225.364 1.00 53.78 C ANISOU 1146 C PHE A 163 5047 9334 6051 -994 -1081 -506 C ATOM 1147 O PHE A 163 89.841 17.152 224.610 1.00 60.18 O ANISOU 1147 O PHE A 163 5855 10276 6733 -1219 -1003 -727 O ATOM 1148 CB PHE A 163 91.262 17.405 227.347 1.00 58.10 C ANISOU 1148 CB PHE A 163 5912 9197 6966 -983 -739 -446 C ATOM 1149 CG PHE A 163 90.143 17.548 228.346 1.00 51.34 C ANISOU 1149 CG PHE A 163 4895 8366 6244 -986 -753 -505 C ATOM 1150 CD1 PHE A 163 88.928 16.910 228.150 1.00 52.57 C ANISOU 1150 CD1 PHE A 163 4858 8784 6330 -1205 -747 -757 C ATOM 1151 CD2 PHE A 163 90.320 18.295 229.497 1.00 60.33 C ANISOU 1151 CD2 PHE A 163 6061 9307 7556 -801 -760 -335 C ATOM 1152 CE1 PHE A 163 87.905 17.036 229.070 1.00 52.78 C ANISOU 1152 CE1 PHE A 163 4693 8912 6448 -1230 -746 -833 C ATOM 1153 CE2 PHE A 163 89.300 18.424 230.422 1.00 61.68 C ANISOU 1153 CE2 PHE A 163 6065 9541 7830 -796 -762 -408 C ATOM 1154 CZ PHE A 163 88.092 17.792 230.208 1.00 49.22 C ANISOU 1154 CZ PHE A 163 4268 8261 6172 -1008 -753 -657 C ATOM 1155 N MET A 164 88.905 18.978 225.524 1.00 49.68 N ANISOU 1155 N MET A 164 4328 9033 5514 -825 -1270 -448 N ATOM 1156 CA MET A 164 87.631 18.781 224.834 1.00 54.77 C ANISOU 1156 CA MET A 164 4676 10159 5974 -904 -1401 -652 C ATOM 1157 C MET A 164 87.756 18.971 223.325 1.00 53.71 C ANISOU 1157 C MET A 164 4533 10325 5549 -898 -1554 -620 C ATOM 1158 O MET A 164 86.927 18.480 222.561 1.00 76.06 O ANISOU 1158 O MET A 164 7139 13576 8183 -1054 -1619 -847 O ATOM 1159 CB MET A 164 86.565 19.725 225.390 1.00 76.06 C ANISOU 1159 CB MET A 164 7136 13068 8694 -629 -1585 -598 C ATOM 1160 CG MET A 164 85.942 19.247 226.691 1.00104.09 C ANISOU 1160 CG MET A 164 10548 16558 12442 -745 -1434 -767 C ATOM 1161 SD MET A 164 85.147 17.636 226.520 1.00112.78 S ANISOU 1161 SD MET A 164 11491 17895 13465 -1263 -1230 -1180 S ATOM 1162 CE MET A 164 83.936 17.987 225.247 1.00110.65 C ANISOU 1162 CE MET A 164 10996 18137 12909 -1135 -1400 -1258 C ATOM 1163 N VAL A 165 88.794 19.682 222.901 1.00 59.28 N ANISOU 1163 N VAL A 165 5478 10847 6200 -753 -1603 -349 N ATOM 1164 CA VAL A 165 89.045 19.887 221.480 1.00 52.79 C ANISOU 1164 CA VAL A 165 4690 10290 5077 -768 -1729 -287 C ATOM 1165 C VAL A 165 89.963 18.800 220.930 1.00 63.30 C ANISOU 1165 C VAL A 165 6145 11551 6354 -1046 -1521 -451 C ATOM 1166 O VAL A 165 90.107 18.648 219.716 1.00 65.96 O ANISOU 1166 O VAL A 165 6475 12162 6426 -1136 -1579 -496 O ATOM 1167 CB VAL A 165 89.671 21.267 221.211 1.00 54.18 C ANISOU 1167 CB VAL A 165 5094 10332 5158 -514 -1885 96 C ATOM 1168 CG1 VAL A 165 88.675 22.370 221.529 1.00 51.71 C ANISOU 1168 CG1 VAL A 165 4705 10111 4830 -167 -2127 243 C ATOM 1169 CG2 VAL A 165 90.947 21.439 222.023 1.00 46.91 C ANISOU 1169 CG2 VAL A 165 4428 8957 4440 -543 -1707 252 C ATOM 1170 N VAL A 166 90.577 18.043 221.833 1.00 61.81 N ANISOU 1170 N VAL A 166 6083 11005 6399 -1148 -1284 -544 N ATOM 1171 CA VAL A 166 91.506 16.988 221.447 1.00 60.53 C ANISOU 1171 CA VAL A 166 6076 10728 6197 -1323 -1077 -709 C ATOM 1172 C VAL A 166 90.778 15.691 221.109 1.00 62.62 C ANISOU 1172 C VAL A 166 6274 11121 6399 -1603 -973 -1087 C ATOM 1173 O VAL A 166 90.059 15.135 221.940 1.00 74.45 O ANISOU 1173 O VAL A 166 7729 12506 8051 -1725 -885 -1245 O ATOM 1174 CB VAL A 166 92.534 16.711 222.563 1.00 55.51 C ANISOU 1174 CB VAL A 166 5635 9657 5800 -1251 -877 -642 C ATOM 1175 CG1 VAL A 166 93.436 15.547 222.180 1.00 55.59 C ANISOU 1175 CG1 VAL A 166 5810 9564 5748 -1350 -670 -844 C ATOM 1176 CG2 VAL A 166 93.354 17.960 222.849 1.00 42.61 C ANISOU 1176 CG2 VAL A 166 4076 7921 4192 -1055 -958 -303 C ATOM 1177 N THR A 167 90.966 15.217 219.881 1.00 62.62 N ANISOU 1177 N THR A 167 6283 11364 6147 -1741 -973 -1242 N ATOM 1178 CA THR A 167 90.383 13.953 219.443 1.00 78.92 C ANISOU 1178 CA THR A 167 8341 13531 8113 -2055 -857 -1632 C ATOM 1179 C THR A 167 91.432 13.084 218.755 1.00 82.67 C ANISOU 1179 C THR A 167 9053 13886 8470 -2122 -684 -1794 C ATOM 1180 O THR A 167 92.584 13.491 218.604 1.00 70.56 O ANISOU 1180 O THR A 167 7623 12269 6916 -1925 -661 -1605 O ATOM 1181 CB THR A 167 89.198 14.171 218.482 1.00 78.74 C ANISOU 1181 CB THR A 167 8019 14073 7826 -2190 -1063 -1761 C ATOM 1182 OG1 THR A 167 89.602 15.029 217.408 1.00 68.76 O ANISOU 1182 OG1 THR A 167 6709 13102 6316 -2024 -1248 -1553 O ATOM 1183 CG2 THR A 167 88.022 14.799 219.214 1.00 83.31 C ANISOU 1183 CG2 THR A 167 8345 14796 8515 -2100 -1196 -1685 C ATOM 1184 N LYS A 168 91.027 11.889 218.339 1.00 87.15 N ANISOU 1184 N LYS A 168 9705 14467 8939 -2412 -554 -2167 N ATOM 1185 CA LYS A 168 91.940 10.956 217.688 1.00 69.28 C ANISOU 1185 CA LYS A 168 7699 12074 6551 -2450 -379 -2380 C ATOM 1186 C LYS A 168 91.662 10.857 216.191 1.00 61.84 C ANISOU 1186 C LYS A 168 6623 11616 5259 -2625 -478 -2567 C ATOM 1187 O LYS A 168 90.621 10.349 215.775 1.00 84.89 O ANISOU 1187 O LYS A 168 9438 14770 8046 -2939 -504 -2844 O ATOM 1188 CB LYS A 168 91.841 9.573 218.333 1.00 72.71 C ANISOU 1188 CB LYS A 168 8461 12053 7112 -2635 -125 -2683 C ATOM 1189 CG LYS A 168 92.767 8.533 217.723 1.00 63.61 C ANISOU 1189 CG LYS A 168 7637 10705 5829 -2607 67 -2937 C ATOM 1190 CD LYS A 168 92.623 7.191 218.423 1.00 83.57 C ANISOU 1190 CD LYS A 168 10591 12690 8471 -2767 314 -3209 C ATOM 1191 CE LYS A 168 93.541 6.145 217.811 1.00 99.23 C ANISOU 1191 CE LYS A 168 12952 14443 10309 -2663 500 -3481 C ATOM 1192 NZ LYS A 168 93.411 4.826 218.490 1.00101.32 N ANISOU 1192 NZ LYS A 168 13744 14092 10661 -2794 743 -3731 N ATOM 1193 N LYS A 169 92.600 11.348 215.389 1.00 69.68 N ANISOU 1193 N LYS A 169 7604 12799 6073 -2451 -526 -2425 N ATOM 1194 CA LYS A 169 92.476 11.296 213.937 1.00 78.48 C ANISOU 1194 CA LYS A 169 8606 14392 6822 -2595 -616 -2577 C ATOM 1195 C LYS A 169 93.724 10.681 213.314 1.00 75.70 C ANISOU 1195 C LYS A 169 8458 13980 6326 -2519 -438 -2727 C ATOM 1196 O LYS A 169 94.837 11.158 213.542 1.00 71.60 O ANISOU 1196 O LYS A 169 7986 13366 5852 -2268 -395 -2497 O ATOM 1197 CB LYS A 169 92.235 12.696 213.367 1.00 74.61 C ANISOU 1197 CB LYS A 169 7873 14281 6194 -2444 -874 -2200 C ATOM 1198 CG LYS A 169 92.111 12.744 211.852 1.00 70.39 C ANISOU 1198 CG LYS A 169 7250 14116 5377 -2492 -918 -2221 C ATOM 1199 CD LYS A 169 90.869 12.011 211.373 1.00 90.14 C ANISOU 1199 CD LYS A 169 9634 16775 7839 -2717 -900 -2499 C ATOM 1200 CE LYS A 169 90.700 12.143 209.868 1.00 99.61 C ANISOU 1200 CE LYS A 169 10719 18381 8746 -2751 -967 -2504 C ATOM 1201 NZ LYS A 169 89.454 11.483 209.389 1.00100.92 N ANISOU 1201 NZ LYS A 169 10733 18766 8846 -2979 -953 -2769 N ATOM 1202 N ASP A 170 93.524 9.621 212.534 1.00 77.19 N ANISOU 1202 N ASP A 170 10030 11673 7626 -1453 -557 -4493 N ATOM 1203 CA ASP A 170 94.615 8.896 211.885 1.00 81.17 C ANISOU 1203 CA ASP A 170 10980 12320 7539 -1179 -561 -4302 C ATOM 1204 C ASP A 170 95.635 8.417 212.917 1.00 73.22 C ANISOU 1204 C ASP A 170 10398 11051 6373 -1281 -9 -3881 C ATOM 1205 O ASP A 170 96.844 8.553 212.724 1.00 79.60 O ANISOU 1205 O ASP A 170 11488 12120 6637 -990 11 -3440 O ATOM 1206 CB ASP A 170 95.288 9.772 210.822 1.00 92.47 C ANISOU 1206 CB ASP A 170 12521 14278 8337 -707 -976 -3926 C ATOM 1207 CG ASP A 170 96.113 8.967 209.835 1.00100.02 C ANISOU 1207 CG ASP A 170 13823 15452 8729 -394 -1080 -3947 C ATOM 1208 OD1 ASP A 170 95.522 8.371 208.911 1.00109.95 O ANISOU 1208 OD1 ASP A 170 15011 16780 9986 -260 -1436 -4475 O ATOM 1209 OD2 ASP A 170 97.354 8.937 209.979 1.00 99.51 O ANISOU 1209 OD2 ASP A 170 14066 15513 8229 -263 -819 -3488 O ATOM 1210 N ASN A 171 95.126 7.864 214.017 1.00 73.64 N ANISOU 1210 N ASN A 171 10502 10586 6894 -1675 446 -4060 N ATOM 1211 CA ASN A 171 95.949 7.358 215.114 1.00 83.08 C ANISOU 1211 CA ASN A 171 12189 11447 7931 -1714 953 -3718 C ATOM 1212 C ASN A 171 96.899 8.407 215.689 1.00 78.20 C ANISOU 1212 C ASN A 171 11618 11098 6998 -1519 981 -3096 C ATOM 1213 O ASN A 171 97.974 8.077 216.191 1.00 64.88 O ANISOU 1213 O ASN A 171 10317 9388 4947 -1314 1185 -2796 O ATOM 1214 CB ASN A 171 96.743 6.130 214.660 1.00 84.97 C ANISOU 1214 CB ASN A 171 12909 11613 7764 -1470 1008 -3791 C ATOM 1215 CG ASN A 171 95.850 4.955 214.316 1.00 94.91 C ANISOU 1215 CG ASN A 171 14220 12460 9379 -1739 1104 -4434 C ATOM 1216 OD1 ASN A 171 94.789 4.772 214.913 1.00 98.70 O ANISOU 1216 OD1 ASN A 171 14543 12510 10450 -2206 1400 -4786 O ATOM 1217 ND2 ASN A 171 96.275 4.151 213.348 1.00 80.45 N ANISOU 1217 ND2 ASN A 171 12595 10756 7215 -1472 888 -4634 N ATOM 1218 N GLN A 172 96.493 9.670 215.615 1.00 77.90 N ANISOU 1218 N GLN A 172 11180 11308 7112 -1561 756 -2957 N ATOM 1219 CA GLN A 172 97.287 10.767 216.154 1.00 67.61 C ANISOU 1219 CA GLN A 172 9873 10222 5592 -1452 795 -2428 C ATOM 1220 C GLN A 172 96.413 11.751 216.922 1.00 60.22 C ANISOU 1220 C GLN A 172 8626 9136 5117 -1714 854 -2407 C ATOM 1221 O GLN A 172 95.352 12.154 216.446 1.00 62.32 O ANISOU 1221 O GLN A 172 8527 9441 5710 -1801 596 -2705 O ATOM 1222 CB GLN A 172 98.033 11.499 215.035 1.00 76.60 C ANISOU 1222 CB GLN A 172 10949 11894 6259 -1139 446 -2166 C ATOM 1223 CG GLN A 172 99.153 10.698 214.393 1.00 72.39 C ANISOU 1223 CG GLN A 172 10706 11589 5209 -846 451 -2116 C ATOM 1224 CD GLN A 172 99.909 11.493 213.347 1.00 61.42 C ANISOU 1224 CD GLN A 172 9282 10705 3351 -599 237 -1844 C ATOM 1225 OE1 GLN A 172 99.508 12.598 212.980 1.00 61.52 O ANISOU 1225 OE1 GLN A 172 9133 10847 3393 -621 46 -1698 O ATOM 1226 NE2 GLN A 172 101.013 10.936 212.863 1.00 70.49 N ANISOU 1226 NE2 GLN A 172 10615 11913 4255 -306 287 -1694 N ATOM 1227 N CYS A 173 96.863 12.133 218.113 1.00 57.50 N ANISOU 1227 N CYS A 173 8424 8640 4785 -1787 1161 -2099 N ATOM 1228 CA CYS A 173 96.157 13.122 218.917 1.00 63.72 C ANISOU 1228 CA CYS A 173 8954 9296 5962 -2003 1243 -2044 C ATOM 1229 C CYS A 173 96.308 14.504 218.295 1.00 64.93 C ANISOU 1229 C CYS A 173 8849 9831 5989 -1849 869 -1785 C ATOM 1230 O CYS A 173 97.414 15.036 218.210 1.00 85.21 O ANISOU 1230 O CYS A 173 11546 12655 8174 -1682 842 -1402 O ATOM 1231 CB CYS A 173 96.681 13.123 220.354 1.00 75.95 C ANISOU 1231 CB CYS A 173 10801 10581 7474 -2064 1654 -1793 C ATOM 1232 SG CYS A 173 96.534 11.532 221.200 1.00111.70 S ANISOU 1232 SG CYS A 173 15872 14526 12042 -2193 2179 -2021 S ATOM 1233 N MET A 174 95.194 15.084 217.859 1.00 63.46 N ANISOU 1233 N MET A 174 8313 9667 6130 -1894 596 -2032 N ATOM 1234 CA MET A 174 95.240 16.350 217.139 1.00 71.30 C ANISOU 1234 CA MET A 174 9196 10949 6946 -1678 215 -1801 C ATOM 1235 C MET A 174 94.127 17.307 217.546 1.00 66.69 C ANISOU 1235 C MET A 174 8279 10245 6817 -1756 87 -1951 C ATOM 1236 O MET A 174 93.081 16.893 218.044 1.00 70.12 O ANISOU 1236 O MET A 174 8430 10456 7758 -1971 203 -2391 O ATOM 1237 CB MET A 174 95.176 16.094 215.632 1.00 79.39 C ANISOU 1237 CB MET A 174 10256 12255 7654 -1388 -207 -1958 C ATOM 1238 CG MET A 174 93.943 15.328 215.176 1.00 81.61 C ANISOU 1238 CG MET A 174 10248 12456 8306 -1421 -432 -2608 C ATOM 1239 SD MET A 174 92.559 16.388 214.712 1.00 90.19 S ANISOU 1239 SD MET A 174 10907 13635 9725 -1231 -967 -2953 S ATOM 1240 CE MET A 174 93.199 17.154 213.225 1.00 94.13 C ANISOU 1240 CE MET A 174 11790 14506 9468 -687 -1463 -2588 C ATOM 1241 N THR A 175 94.369 18.595 217.325 1.00 64.90 N ANISOU 1241 N THR A 175 8100 10150 6411 -1587 -117 -1607 N ATOM 1242 CA THR A 175 93.372 19.626 217.571 1.00 69.05 C ANISOU 1242 CA THR A 175 8358 10585 7291 -1548 -322 -1731 C ATOM 1243 C THR A 175 93.000 20.303 216.258 1.00 79.04 C ANISOU 1243 C THR A 175 9673 12062 8294 -1131 -887 -1762 C ATOM 1244 O THR A 175 93.829 20.969 215.640 1.00 83.76 O ANISOU 1244 O THR A 175 10649 12784 8391 -939 -968 -1315 O ATOM 1245 CB THR A 175 93.877 20.682 218.571 1.00 58.73 C ANISOU 1245 CB THR A 175 7155 9149 6009 -1668 -77 -1311 C ATOM 1246 OG1 THR A 175 94.196 20.052 219.817 1.00 56.72 O ANISOU 1246 OG1 THR A 175 6925 8695 5929 -1966 405 -1303 O ATOM 1247 CG2 THR A 175 92.817 21.748 218.803 1.00 57.77 C ANISOU 1247 CG2 THR A 175 6781 8919 6249 -1579 -306 -1462 C ATOM 1248 N ASP A 176 91.754 20.125 215.832 1.00 75.92 N ANISOU 1248 N ASP A 176 8918 11702 8226 -979 -1262 -2330 N ATOM 1249 CA ASP A 176 91.290 20.698 214.575 1.00 72.38 C ANISOU 1249 CA ASP A 176 8556 11457 7488 -462 -1893 -2448 C ATOM 1250 C ASP A 176 91.149 22.213 214.692 1.00 71.75 C ANISOU 1250 C ASP A 176 8647 11288 7328 -216 -2081 -2125 C ATOM 1251 O ASP A 176 90.118 22.716 215.137 1.00 88.96 O ANISOU 1251 O ASP A 176 10453 13383 9966 -142 -2269 -2469 O ATOM 1252 CB ASP A 176 89.959 20.068 214.160 1.00 76.15 C ANISOU 1252 CB ASP A 176 8503 12031 8398 -337 -2295 -3276 C ATOM 1253 CG ASP A 176 89.698 20.179 212.670 1.00101.79 C ANISOU 1253 CG ASP A 176 11932 15553 11190 261 -2982 -3471 C ATOM 1254 OD1 ASP A 176 90.170 21.154 212.049 1.00109.01 O ANISOU 1254 OD1 ASP A 176 13373 16514 11533 661 -3213 -2979 O ATOM 1255 OD2 ASP A 176 89.021 19.286 212.118 1.00108.18 O ANISOU 1255 OD2 ASP A 176 12400 16508 12195 334 -3271 -4134 O ATOM 1256 N TYR A 177 92.190 22.933 214.287 1.00 70.61 N ANISOU 1256 N TYR A 177 9074 11143 6611 -102 -1994 -1494 N ATOM 1257 CA TYR A 177 92.205 24.388 214.397 1.00 79.16 C ANISOU 1257 CA TYR A 177 10457 12053 7569 85 -2083 -1121 C ATOM 1258 C TYR A 177 91.358 25.052 213.314 1.00 92.85 C ANISOU 1258 C TYR A 177 12400 13836 9041 743 -2761 -1306 C ATOM 1259 O TYR A 177 90.964 26.210 213.449 1.00106.73 O ANISOU 1259 O TYR A 177 14335 15406 10813 1000 -2956 -1176 O ATOM 1260 CB TYR A 177 93.641 24.917 214.332 1.00 69.13 C ANISOU 1260 CB TYR A 177 9731 10726 5809 -96 -1667 -435 C ATOM 1261 CG TYR A 177 94.507 24.493 215.499 1.00 64.35 C ANISOU 1261 CG TYR A 177 8933 10078 5439 -637 -1082 -272 C ATOM 1262 CD1 TYR A 177 94.319 25.041 216.762 1.00 61.19 C ANISOU 1262 CD1 TYR A 177 8311 9462 5476 -889 -861 -247 C ATOM 1263 CD2 TYR A 177 95.518 23.556 215.336 1.00 61.56 C ANISOU 1263 CD2 TYR A 177 8647 9910 4832 -824 -787 -171 C ATOM 1264 CE1 TYR A 177 95.108 24.660 217.832 1.00 71.88 C ANISOU 1264 CE1 TYR A 177 9550 10785 6975 -1287 -390 -129 C ATOM 1265 CE2 TYR A 177 96.312 23.168 216.400 1.00 68.33 C ANISOU 1265 CE2 TYR A 177 9365 10744 5852 -1199 -334 -68 C ATOM 1266 CZ TYR A 177 96.103 23.724 217.646 1.00 75.66 C ANISOU 1266 CZ TYR A 177 10110 11456 7181 -1416 -151 -47 C ATOM 1267 OH TYR A 177 96.890 23.344 218.708 1.00 69.93 O ANISOU 1267 OH TYR A 177 9304 10714 6551 -1699 241 27 O ATOM 1268 N ASP A 178 91.080 24.315 212.243 1.00 93.13 N ANISOU 1268 N ASP A 178 12458 14115 8811 1070 -3152 -1633 N ATOM 1269 CA ASP A 178 90.287 24.848 211.140 1.00 98.48 C ANISOU 1269 CA ASP A 178 13385 14881 9152 1812 -3885 -1871 C ATOM 1270 C ASP A 178 88.811 24.954 211.513 1.00 96.34 C ANISOU 1270 C ASP A 178 12427 14652 9527 2045 -4363 -2615 C ATOM 1271 O ASP A 178 88.116 25.868 211.069 1.00 96.89 O ANISOU 1271 O ASP A 178 12683 14689 9444 2671 -4929 -2738 O ATOM 1272 CB ASP A 178 90.453 23.980 209.892 1.00107.01 C ANISOU 1272 CB ASP A 178 14686 16240 9732 2117 -4183 -2059 C ATOM 1273 CG ASP A 178 91.858 24.039 209.325 1.00109.96 C ANISOU 1273 CG ASP A 178 15797 16602 9379 2013 -3757 -1354 C ATOM 1274 OD1 ASP A 178 92.528 25.078 209.501 1.00111.72 O ANISOU 1274 OD1 ASP A 178 16537 16587 9323 1939 -3438 -735 O ATOM 1275 OD2 ASP A 178 92.292 23.047 208.702 1.00106.92 O ANISOU 1275 OD2 ASP A 178 15460 16441 8725 1985 -3715 -1460 O ATOM 1276 N TYR A 179 88.338 24.019 212.331 1.00 95.70 N ANISOU 1276 N TYR A 179 11577 14627 10157 1554 -4109 -3134 N ATOM 1277 CA TYR A 179 86.955 24.040 212.794 1.00 97.68 C ANISOU 1277 CA TYR A 179 11050 14933 11131 1641 -4417 -3923 C ATOM 1278 C TYR A 179 86.804 24.913 214.036 1.00 94.51 C ANISOU 1278 C TYR A 179 10494 14266 11150 1383 -4066 -3716 C ATOM 1279 O TYR A 179 85.714 25.033 214.595 1.00106.82 O ANISOU 1279 O TYR A 179 11390 15847 13348 1393 -4198 -4332 O ATOM 1280 CB TYR A 179 86.459 22.620 213.082 1.00 93.22 C ANISOU 1280 CB TYR A 179 9768 14493 11159 1173 -4209 -4629 C ATOM 1281 CG TYR A 179 86.175 21.805 211.839 1.00117.88 C ANISOU 1281 CG TYR A 179 12835 17913 14039 1529 -4742 -5139 C ATOM 1282 CD1 TYR A 179 86.016 22.418 210.603 1.00128.78 C ANISOU 1282 CD1 TYR A 179 14649 19483 14798 2352 -5505 -5140 C ATOM 1283 CD2 TYR A 179 86.060 20.422 211.904 1.00120.65 C ANISOU 1283 CD2 TYR A 179 12772 18322 14750 1069 -4480 -5633 C ATOM 1284 CE1 TYR A 179 85.755 21.678 209.466 1.00123.89 C ANISOU 1284 CE1 TYR A 179 14063 19001 14008 2666 -5774 -5440 C ATOM 1285 CE2 TYR A 179 85.799 19.672 210.770 1.00115.85 C ANISOU 1285 CE2 TYR A 179 12164 17884 13969 1380 -4829 -5990 C ATOM 1286 CZ TYR A 179 85.647 20.306 209.555 1.00116.89 C ANISOU 1286 CZ TYR A 179 12717 18157 13541 2176 -5459 -5878 C ATOM 1287 OH TYR A 179 85.387 19.567 208.424 1.00117.32 O ANISOU 1287 OH TYR A 179 12795 18341 13439 2495 -5742 -6197 O ATOM 1288 N LEU A 180 87.908 25.519 214.463 1.00 85.17 N ANISOU 1288 N LEU A 180 9890 12849 9622 1145 -3606 -2902 N ATOM 1289 CA LEU A 180 87.895 26.435 215.598 1.00 82.61 C ANISOU 1289 CA LEU A 180 9527 12256 9607 933 -3291 -2651 C ATOM 1290 C LEU A 180 88.262 27.846 215.154 1.00 84.54 C ANISOU 1290 C LEU A 180 10500 12298 9324 1383 -3529 -2089 C ATOM 1291 O LEU A 180 88.789 28.045 214.060 1.00 86.84 O ANISOU 1291 O LEU A 180 11434 12619 8942 1734 -3755 -1748 O ATOM 1292 CB LEU A 180 88.860 25.962 216.687 1.00 77.97 C ANISOU 1292 CB LEU A 180 8952 11522 9152 216 -2504 -2259 C ATOM 1293 CG LEU A 180 88.507 24.660 217.408 1.00 81.61 C ANISOU 1293 CG LEU A 180 8833 12028 10148 -282 -2116 -2738 C ATOM 1294 CD1 LEU A 180 89.599 24.286 218.397 1.00 67.89 C ANISOU 1294 CD1 LEU A 180 7313 10127 8354 -820 -1422 -2269 C ATOM 1295 CD2 LEU A 180 87.164 24.786 218.109 1.00 87.75 C ANISOU 1295 CD2 LEU A 180 8927 12770 11646 -315 -2170 -3404 C ATOM 1296 N GLU A 181 87.981 28.823 216.008 1.00 84.13 N ANISOU 1296 N GLU A 181 10404 12002 9560 1366 -3434 -1996 N ATOM 1297 CA GLU A 181 88.330 30.207 215.717 1.00 86.26 C ANISOU 1297 CA GLU A 181 11423 11974 9378 1729 -3573 -1457 C ATOM 1298 C GLU A 181 89.827 30.431 215.897 1.00 98.92 C ANISOU 1298 C GLU A 181 13610 13386 10588 1244 -2955 -689 C ATOM 1299 O GLU A 181 90.496 29.681 216.607 1.00 95.91 O ANISOU 1299 O GLU A 181 12945 13086 10413 642 -2428 -609 O ATOM 1300 CB GLU A 181 87.534 31.162 216.607 1.00 87.62 C ANISOU 1300 CB GLU A 181 11341 11934 10019 1867 -3669 -1660 C ATOM 1301 CG GLU A 181 86.044 31.185 216.302 1.00 93.94 C ANISOU 1301 CG GLU A 181 11590 12937 11165 2482 -4363 -2465 C ATOM 1302 CD GLU A 181 85.278 32.138 217.198 1.00120.54 C ANISOU 1302 CD GLU A 181 14685 16115 15001 2642 -4435 -2694 C ATOM 1303 OE1 GLU A 181 84.201 32.612 216.779 1.00122.52 O ANISOU 1303 OE1 GLU A 181 14745 16457 15352 3360 -5113 -3219 O ATOM 1304 OE2 GLU A 181 85.749 32.410 218.322 1.00115.98 O ANISOU 1304 OE2 GLU A 181 14076 15313 14679 2097 -3844 -2390 O ATOM 1305 N VAL A 182 90.346 31.468 215.248 1.00 92.60 N ANISOU 1305 N VAL A 182 13645 12319 9219 1527 -3012 -162 N ATOM 1306 CA VAL A 182 91.774 31.765 215.278 1.00 86.73 C ANISOU 1306 CA VAL A 182 13442 11403 8107 1063 -2412 495 C ATOM 1307 C VAL A 182 92.212 32.256 216.658 1.00 77.35 C ANISOU 1307 C VAL A 182 12030 9999 7361 514 -1913 655 C ATOM 1308 O VAL A 182 93.391 32.193 217.008 1.00 73.92 O ANISOU 1308 O VAL A 182 11711 9541 6834 -8 -1372 1002 O ATOM 1309 CB VAL A 182 92.142 32.821 214.216 1.00 94.32 C ANISOU 1309 CB VAL A 182 15435 12049 8353 1477 -2519 993 C ATOM 1310 CG1 VAL A 182 93.643 32.830 213.963 1.00 91.44 C ANISOU 1310 CG1 VAL A 182 15541 11621 7581 961 -1859 1550 C ATOM 1311 CG2 VAL A 182 91.392 32.547 212.922 1.00 93.57 C ANISOU 1311 CG2 VAL A 182 15614 12127 7810 2243 -3194 742 C ATOM 1312 N SER A 183 91.254 32.737 217.443 1.00 78.48 N ANISOU 1312 N SER A 183 11820 10014 7986 662 -2117 341 N ATOM 1313 CA SER A 183 91.546 33.272 218.768 1.00 74.39 C ANISOU 1313 CA SER A 183 11121 9277 7866 226 -1706 443 C ATOM 1314 C SER A 183 91.775 32.169 219.798 1.00 89.71 C ANISOU 1314 C SER A 183 12401 11461 10222 -308 -1313 207 C ATOM 1315 O SER A 183 92.319 32.421 220.873 1.00 65.30 O ANISOU 1315 O SER A 183 9224 8245 7341 -714 -910 337 O ATOM 1316 CB SER A 183 90.409 34.184 219.234 1.00 77.60 C ANISOU 1316 CB SER A 183 11411 9459 8614 622 -2055 166 C ATOM 1317 OG SER A 183 90.200 35.245 218.319 1.00118.83 O ANISOU 1317 OG SER A 183 17369 14385 13395 1199 -2438 402 O ATOM 1318 N TYR A 184 91.364 30.950 219.463 1.00 68.17 N ANISOU 1318 N TYR A 184 7299 11237 7367 42 -743 135 N ATOM 1319 CA TYR A 184 91.415 29.835 220.407 1.00 68.40 C ANISOU 1319 CA TYR A 184 7247 11224 7520 -241 -686 70 C ATOM 1320 C TYR A 184 92.831 29.480 220.892 1.00 62.83 C ANISOU 1320 C TYR A 184 6772 10059 7041 -372 -600 76 C ATOM 1321 O TYR A 184 93.037 29.330 222.096 1.00 63.87 O ANISOU 1321 O TYR A 184 6912 10069 7287 -403 -556 84 O ATOM 1322 CB TYR A 184 90.748 28.595 219.800 1.00 63.01 C ANISOU 1322 CB TYR A 184 6393 10807 6742 -553 -704 -31 C ATOM 1323 CG TYR A 184 90.317 27.577 220.830 1.00 66.93 C ANISOU 1323 CG TYR A 184 6765 11387 7279 -820 -666 -91 C ATOM 1324 CD1 TYR A 184 89.055 27.639 221.409 1.00 63.78 C ANISOU 1324 CD1 TYR A 184 6091 11410 6733 -800 -704 -102 C ATOM 1325 CD2 TYR A 184 91.170 26.557 221.230 1.00 66.04 C ANISOU 1325 CD2 TYR A 184 6816 10945 7329 -1082 -591 -132 C ATOM 1326 CE1 TYR A 184 88.655 26.714 222.353 1.00 59.09 C ANISOU 1326 CE1 TYR A 184 5393 10900 6159 -1074 -665 -150 C ATOM 1327 CE2 TYR A 184 90.779 25.626 222.175 1.00 69.90 C ANISOU 1327 CE2 TYR A 184 7234 11486 7840 -1331 -555 -177 C ATOM 1328 CZ TYR A 184 89.520 25.710 222.733 1.00 70.28 C ANISOU 1328 CZ TYR A 184 7012 11946 7743 -1346 -591 -184 C ATOM 1329 OH TYR A 184 89.126 24.787 223.673 1.00 46.58 O ANISOU 1329 OH TYR A 184 3948 9003 4746 -1624 -550 -223 O ATOM 1330 N PRO A 185 93.811 29.338 219.975 1.00 62.75 N ANISOU 1330 N PRO A 185 6936 9824 7082 -439 -575 73 N ATOM 1331 CA PRO A 185 95.144 29.015 220.502 1.00 64.90 C ANISOU 1331 CA PRO A 185 7391 9723 7546 -535 -494 78 C ATOM 1332 C PRO A 185 95.760 30.158 221.308 1.00 49.78 C ANISOU 1332 C PRO A 185 5605 7601 5710 -329 -475 167 C ATOM 1333 O PRO A 185 96.645 29.920 222.129 1.00 45.75 O ANISOU 1333 O PRO A 185 5184 6854 5346 -398 -414 171 O ATOM 1334 CB PRO A 185 95.964 28.735 219.237 1.00 51.23 C ANISOU 1334 CB PRO A 185 5787 7871 5807 -616 -478 56 C ATOM 1335 CG PRO A 185 95.264 29.480 218.162 1.00 40.26 C ANISOU 1335 CG PRO A 185 4349 6705 4242 -467 -552 86 C ATOM 1336 CD PRO A 185 93.809 29.383 218.501 1.00 58.79 C ANISOU 1336 CD PRO A 185 6462 9409 6465 -440 -613 61 C ATOM 1337 N ILE A 186 95.292 31.379 221.074 1.00 48.28 N ANISOU 1337 N ILE A 186 5441 7499 5406 -76 -529 235 N ATOM 1338 CA ILE A 186 95.761 32.536 221.827 1.00 50.62 C ANISOU 1338 CA ILE A 186 5899 7592 5743 117 -517 315 C ATOM 1339 C ILE A 186 95.160 32.542 223.229 1.00 52.76 C ANISOU 1339 C ILE A 186 6058 7938 6050 178 -513 309 C ATOM 1340 O ILE A 186 95.875 32.685 224.221 1.00 37.00 O ANISOU 1340 O ILE A 186 4160 5719 4180 158 -465 328 O ATOM 1341 CB ILE A 186 95.409 33.854 221.118 1.00 56.82 C ANISOU 1341 CB ILE A 186 6808 8418 6365 392 -577 392 C ATOM 1342 CG1 ILE A 186 95.965 33.857 219.693 1.00 56.26 C ANISOU 1342 CG1 ILE A 186 6844 8293 6241 324 -581 403 C ATOM 1343 CG2 ILE A 186 95.942 35.040 221.906 1.00 59.27 C ANISOU 1343 CG2 ILE A 186 7346 8471 6701 562 -562 469 C ATOM 1344 CD1 ILE A 186 95.567 35.071 218.886 1.00 57.94 C ANISOU 1344 CD1 ILE A 186 7196 8551 6268 588 -644 484 C ATOM 1345 N ILE A 187 93.841 32.386 223.297 1.00 47.77 N ANISOU 1345 N ILE A 187 5207 7653 5290 249 -564 282 N ATOM 1346 CA ILE A 187 93.129 32.315 224.569 1.00 40.00 C ANISOU 1346 CA ILE A 187 4074 6814 4309 297 -559 270 C ATOM 1347 C ILE A 187 93.649 31.154 225.409 1.00 48.43 C ANISOU 1347 C ILE A 187 5110 7747 5544 10 -490 221 C ATOM 1348 O ILE A 187 93.812 31.274 226.625 1.00 50.84 O ANISOU 1348 O ILE A 187 5431 7955 5932 38 -457 236 O ATOM 1349 CB ILE A 187 91.607 32.157 224.352 1.00 43.72 C ANISOU 1349 CB ILE A 187 4262 7764 4585 368 -623 235 C ATOM 1350 CG1 ILE A 187 91.040 33.388 223.643 1.00 50.13 C ANISOU 1350 CG1 ILE A 187 5114 8726 5207 727 -697 292 C ATOM 1351 CG2 ILE A 187 90.888 31.936 225.673 1.00 42.57 C ANISOU 1351 CG2 ILE A 187 3934 7807 4435 371 -608 216 C ATOM 1352 CD1 ILE A 187 89.552 33.312 223.387 1.00 64.01 C ANISOU 1352 CD1 ILE A 187 6566 11016 6740 841 -766 260 C ATOM 1353 N LEU A 188 93.922 30.036 224.745 1.00 49.40 N ANISOU 1353 N LEU A 188 5215 7851 5702 -252 -469 163 N ATOM 1354 CA LEU A 188 94.423 28.841 225.411 1.00 54.66 C ANISOU 1354 CA LEU A 188 5897 8369 6501 -512 -405 116 C ATOM 1355 C LEU A 188 95.786 29.093 226.049 1.00 57.30 C ANISOU 1355 C LEU A 188 6430 8341 7002 -482 -347 155 C ATOM 1356 O LEU A 188 96.093 28.553 227.111 1.00 66.27 O ANISOU 1356 O LEU A 188 7574 9367 8239 -575 -301 147 O ATOM 1357 CB LEU A 188 94.511 27.680 224.419 1.00 51.57 C ANISOU 1357 CB LEU A 188 5513 7995 6088 -762 -398 44 C ATOM 1358 CG LEU A 188 94.418 26.279 225.017 1.00 49.99 C ANISOU 1358 CG LEU A 188 5297 7763 5934 -1047 -353 -20 C ATOM 1359 CD1 LEU A 188 93.124 26.136 225.797 1.00 52.05 C ANISOU 1359 CD1 LEU A 188 5339 8340 6096 -1104 -376 -32 C ATOM 1360 CD2 LEU A 188 94.508 25.227 223.925 1.00 55.12 C ANISOU 1360 CD2 LEU A 188 6008 8402 6535 -1272 -351 -97 C ATOM 1361 N ASN A 189 96.599 29.916 225.396 1.00 51.15 N ANISOU 1361 N ASN A 189 5804 7396 6232 -365 -349 199 N ATOM 1362 CA ASN A 189 97.905 30.278 225.931 1.00 52.83 C ANISOU 1362 CA ASN A 189 6186 7317 6571 -350 -298 237 C ATOM 1363 C ASN A 189 97.791 31.283 227.071 1.00 46.45 C ANISOU 1363 C ASN A 189 5415 6459 5777 -179 -304 290 C ATOM 1364 O ASN A 189 98.466 31.153 228.091 1.00 44.56 O ANISOU 1364 O ASN A 189 5221 6064 5646 -224 -260 296 O ATOM 1365 CB ASN A 189 98.801 30.846 224.830 1.00 57.75 C ANISOU 1365 CB ASN A 189 6961 7810 7172 -321 -296 267 C ATOM 1366 CG ASN A 189 99.280 29.784 223.862 1.00 57.13 C ANISOU 1366 CG ASN A 189 6882 7719 7106 -492 -270 209 C ATOM 1367 OD1 ASN A 189 99.310 28.597 224.189 1.00 74.83 O ANISOU 1367 OD1 ASN A 189 9075 9951 9404 -641 -238 149 O ATOM 1368 ND2 ASN A 189 99.667 30.207 222.665 1.00 52.90 N ANISOU 1368 ND2 ASN A 189 6427 7171 6501 -467 -281 226 N ATOM 1369 N VAL A 190 96.935 32.284 226.889 1.00 43.55 N ANISOU 1369 N VAL A 190 5037 6228 5283 33 -361 325 N ATOM 1370 CA VAL A 190 96.738 33.317 227.901 1.00 39.19 C ANISOU 1370 CA VAL A 190 4552 5626 4711 233 -371 369 C ATOM 1371 C VAL A 190 96.201 32.713 229.195 1.00 34.49 C ANISOU 1371 C VAL A 190 3797 5141 4166 187 -350 338 C ATOM 1372 O VAL A 190 96.683 33.029 230.283 1.00 46.40 O ANISOU 1372 O VAL A 190 5383 6496 5751 215 -319 355 O ATOM 1373 CB VAL A 190 95.776 34.417 227.407 1.00 40.44 C ANISOU 1373 CB VAL A 190 4736 5943 4688 517 -440 406 C ATOM 1374 CG1 VAL A 190 95.455 35.393 228.528 1.00 37.01 C ANISOU 1374 CG1 VAL A 190 4381 5469 4214 748 -450 438 C ATOM 1375 CG2 VAL A 190 96.377 35.151 226.219 1.00 36.85 C ANISOU 1375 CG2 VAL A 190 4494 5337 4172 570 -458 454 C ATOM 1376 N GLU A 191 95.211 31.835 229.067 1.00 46.07 N ANISOU 1376 N GLU A 191 5045 6884 5577 93 -364 290 N ATOM 1377 CA GLU A 191 94.623 31.161 230.220 1.00 53.76 C ANISOU 1377 CA GLU A 191 5858 7995 6574 5 -341 262 C ATOM 1378 C GLU A 191 95.665 30.317 230.947 1.00 49.64 C ANISOU 1378 C GLU A 191 5421 7219 6221 -199 -273 251 C ATOM 1379 O GLU A 191 95.683 30.257 232.177 1.00 40.85 O ANISOU 1379 O GLU A 191 4288 6073 5161 -197 -245 259 O ATOM 1380 CB GLU A 191 93.440 30.290 229.783 1.00 57.63 C ANISOU 1380 CB GLU A 191 6110 8837 6949 -131 -366 210 C ATOM 1381 CG GLU A 191 92.688 29.613 230.925 1.00 84.47 C ANISOU 1381 CG GLU A 191 9331 12432 10333 -251 -342 184 C ATOM 1382 CD GLU A 191 93.297 28.281 231.329 1.00103.12 C ANISOU 1382 CD GLU A 191 11753 14610 12819 -563 -280 154 C ATOM 1383 OE1 GLU A 191 93.932 27.630 230.473 1.00113.81 O ANISOU 1383 OE1 GLU A 191 13215 15805 14221 -715 -268 128 O ATOM 1384 OE2 GLU A 191 93.147 27.890 232.505 1.00112.54 O ANISOU 1384 OE2 GLU A 191 12900 15814 14048 -639 -244 156 O ATOM 1385 N LEU A 192 96.532 29.668 230.178 1.00 42.46 N ANISOU 1385 N LEU A 192 4607 6147 5380 -353 -249 232 N ATOM 1386 CA LEU A 192 97.566 28.814 230.745 1.00 36.96 C ANISOU 1386 CA LEU A 192 3997 5227 4817 -509 -188 219 C ATOM 1387 C LEU A 192 98.654 29.643 231.420 1.00 43.39 C ANISOU 1387 C LEU A 192 4950 5818 5717 -401 -164 266 C ATOM 1388 O LEU A 192 99.228 29.227 232.423 1.00 41.99 O ANISOU 1388 O LEU A 192 4800 5526 5629 -457 -123 268 O ATOM 1389 CB LEU A 192 98.177 27.923 229.661 1.00 39.50 C ANISOU 1389 CB LEU A 192 4389 5462 5159 -660 -170 180 C ATOM 1390 CG LEU A 192 99.116 26.814 230.139 1.00 50.45 C ANISOU 1390 CG LEU A 192 5867 6653 6648 -799 -109 156 C ATOM 1391 CD1 LEU A 192 98.382 25.865 231.072 1.00 54.96 C ANISOU 1391 CD1 LEU A 192 6372 7295 7216 -935 -92 133 C ATOM 1392 CD2 LEU A 192 99.704 26.060 228.958 1.00 43.85 C ANISOU 1392 CD2 LEU A 192 5118 5740 5803 -895 -94 111 C ATOM 1393 N MET A 193 98.931 30.819 230.868 1.00 43.57 N ANISOU 1393 N MET A 193 5073 5785 5695 -259 -192 303 N ATOM 1394 CA MET A 193 99.982 31.678 231.402 1.00 43.25 C ANISOU 1394 CA MET A 193 5187 5540 5707 -201 -172 343 C ATOM 1395 C MET A 193 99.591 32.315 232.732 1.00 53.00 C ANISOU 1395 C MET A 193 6421 6776 6940 -82 -177 363 C ATOM 1396 O MET A 193 100.374 32.307 233.680 1.00 45.71 O ANISOU 1396 O MET A 193 5549 5722 6096 -125 -142 370 O ATOM 1397 CB MET A 193 100.346 32.766 230.392 1.00 40.51 C ANISOU 1397 CB MET A 193 4991 5118 5285 -116 -198 381 C ATOM 1398 CG MET A 193 101.230 32.286 229.255 1.00 39.13 C ANISOU 1398 CG MET A 193 4856 4885 5128 -247 -175 369 C ATOM 1399 SD MET A 193 101.679 33.630 228.144 1.00 54.02 S ANISOU 1399 SD MET A 193 6941 6679 6906 -175 -200 427 S ATOM 1400 CE MET A 193 102.295 34.830 229.323 1.00 86.66 C ANISOU 1400 CE MET A 193 11252 10626 11048 -123 -190 473 C ATOM 1401 N LEU A 194 98.385 32.869 232.802 1.00 48.46 N ANISOU 1401 N LEU A 194 5781 6373 6259 82 -220 368 N ATOM 1402 CA LEU A 194 97.939 33.528 234.024 1.00 46.81 C ANISOU 1402 CA LEU A 194 5577 6186 6024 231 -225 380 C ATOM 1403 C LEU A 194 97.396 32.519 235.030 1.00 49.73 C ANISOU 1403 C LEU A 194 5759 6700 6438 133 -197 351 C ATOM 1404 O LEU A 194 97.537 32.697 236.239 1.00 60.52 O ANISOU 1404 O LEU A 194 7139 8014 7840 166 -176 357 O ATOM 1405 CB LEU A 194 96.887 34.602 233.712 1.00 50.22 C ANISOU 1405 CB LEU A 194 6029 6759 6295 500 -282 398 C ATOM 1406 CG LEU A 194 95.555 34.243 233.045 1.00 59.97 C ANISOU 1406 CG LEU A 194 7050 8328 7407 568 -323 376 C ATOM 1407 CD1 LEU A 194 94.496 33.824 234.059 1.00 85.02 C ANISOU 1407 CD1 LEU A 194 9997 11773 10534 600 -319 348 C ATOM 1408 CD2 LEU A 194 95.056 35.414 232.212 1.00 52.96 C ANISOU 1408 CD2 LEU A 194 6277 7487 6360 839 -383 408 C ATOM 1409 N GLY A 195 96.784 31.454 234.526 1.00 43.01 N ANISOU 1409 N GLY A 195 4749 6024 5569 -8 -196 318 N ATOM 1410 CA GLY A 195 96.164 30.461 235.382 1.00 54.18 C ANISOU 1410 CA GLY A 195 6005 7588 6993 -140 -170 294 C ATOM 1411 C GLY A 195 97.147 29.527 236.060 1.00 59.39 C ANISOU 1411 C GLY A 195 6736 8044 7787 -320 -113 292 C ATOM 1412 O GLY A 195 96.951 29.143 237.213 1.00 73.99 O ANISOU 1412 O GLY A 195 8532 9922 9657 -364 -85 295 O ATOM 1413 N ALA A 196 98.209 29.163 235.349 1.00 53.40 N ANISOU 1413 N ALA A 196 6096 7092 7101 -407 -96 288 N ATOM 1414 CA ALA A 196 99.159 28.180 235.858 1.00 42.75 C ANISOU 1414 CA ALA A 196 4817 5571 5852 -544 -46 283 C ATOM 1415 C ALA A 196 100.419 28.818 236.437 1.00 47.04 C ANISOU 1415 C ALA A 196 5477 5925 6473 -467 -27 312 C ATOM 1416 O ALA A 196 101.168 28.166 237.164 1.00 53.87 O ANISOU 1416 O ALA A 196 6379 6683 7404 -527 11 316 O ATOM 1417 CB ALA A 196 99.532 27.197 234.760 1.00 49.39 C ANISOU 1417 CB ALA A 196 5707 6356 6702 -681 -33 249 C ATOM 1418 N PHE A 197 100.657 30.086 236.118 1.00 42.96 N ANISOU 1418 N PHE A 197 5028 5369 5925 -342 -55 334 N ATOM 1419 CA PHE A 197 101.862 30.753 236.598 1.00 40.77 C ANISOU 1419 CA PHE A 197 4867 4931 5693 -316 -39 357 C ATOM 1420 C PHE A 197 101.569 32.035 237.376 1.00 49.43 C ANISOU 1420 C PHE A 197 6027 6011 6745 -177 -63 379 C ATOM 1421 O PHE A 197 101.852 32.112 238.569 1.00 40.69 O ANISOU 1421 O PHE A 197 4927 4863 5671 -169 -45 384 O ATOM 1422 CB PHE A 197 102.802 31.064 235.432 1.00 32.61 C ANISOU 1422 CB PHE A 197 3927 3812 4653 -353 -38 362 C ATOM 1423 CG PHE A 197 104.143 31.587 235.862 1.00 36.99 C ANISOU 1423 CG PHE A 197 4572 4246 5234 -386 -16 379 C ATOM 1424 CD1 PHE A 197 105.142 30.716 236.265 1.00 38.81 C ANISOU 1424 CD1 PHE A 197 4769 4452 5527 -463 24 368 C ATOM 1425 CD2 PHE A 197 104.405 32.949 235.869 1.00 36.84 C ANISOU 1425 CD2 PHE A 197 4687 4153 5158 -341 -37 406 C ATOM 1426 CE1 PHE A 197 106.377 31.190 236.665 1.00 38.82 C ANISOU 1426 CE1 PHE A 197 4816 4405 5530 -503 42 380 C ATOM 1427 CE2 PHE A 197 105.639 33.430 236.269 1.00 47.05 C ANISOU 1427 CE2 PHE A 197 6059 5365 6454 -421 -17 417 C ATOM 1428 CZ PHE A 197 106.626 32.549 236.667 1.00 44.00 C ANISOU 1428 CZ PHE A 197 5586 5005 6128 -506 22 403 C ATOM 1429 N VAL A 198 101.009 33.034 236.698 1.00 50.39 N ANISOU 1429 N VAL A 198 6215 6156 6775 -53 -103 391 N ATOM 1430 CA VAL A 198 100.818 34.358 237.291 1.00 29.18 C ANISOU 1430 CA VAL A 198 3662 3407 4018 106 -128 410 C ATOM 1431 C VAL A 198 100.018 34.325 238.591 1.00 42.19 C ANISOU 1431 C VAL A 198 5219 5160 5653 203 -125 398 C ATOM 1432 O VAL A 198 100.512 34.748 239.634 1.00 68.05 O ANISOU 1432 O VAL A 198 8574 8333 8948 214 -111 401 O ATOM 1433 CB VAL A 198 100.116 35.318 236.311 1.00 44.76 C ANISOU 1433 CB VAL A 198 5732 5410 5866 272 -176 427 C ATOM 1434 CG1 VAL A 198 99.868 36.664 236.975 1.00 31.41 C ANISOU 1434 CG1 VAL A 198 4229 3626 4080 469 -201 442 C ATOM 1435 CG2 VAL A 198 100.946 35.486 235.047 1.00 30.28 C ANISOU 1435 CG2 VAL A 198 4013 3465 4029 174 -177 445 C ATOM 1436 N ILE A 199 98.789 33.821 238.527 1.00 48.46 N ANISOU 1436 N ILE A 199 5836 6180 6398 257 -137 383 N ATOM 1437 CA ILE A 199 97.924 33.767 239.705 1.00 50.77 C ANISOU 1437 CA ILE A 199 6012 6627 6653 344 -131 372 C ATOM 1438 C ILE A 199 98.488 32.896 240.843 1.00 52.36 C ANISOU 1438 C ILE A 199 6161 6776 6959 188 -83 369 C ATOM 1439 O ILE A 199 98.501 33.338 241.992 1.00 56.99 O ANISOU 1439 O ILE A 199 6778 7341 7536 266 -74 370 O ATOM 1440 CB ILE A 199 96.502 33.273 239.337 1.00 48.42 C ANISOU 1440 CB ILE A 199 5493 6645 6259 383 -149 354 C ATOM 1441 CG1 ILE A 199 95.817 34.269 238.399 1.00 59.02 C ANISOU 1441 CG1 ILE A 199 6880 8082 7465 610 -204 360 C ATOM 1442 CG2 ILE A 199 95.663 33.068 240.589 1.00 50.63 C ANISOU 1442 CG2 ILE A 199 5620 7124 6492 430 -131 343 C ATOM 1443 CD1 ILE A 199 94.446 33.827 237.933 1.00 34.55 C ANISOU 1443 CD1 ILE A 199 3534 5350 4245 650 -230 339 C ATOM 1444 N PRO A 200 98.957 31.664 240.543 1.00 48.86 N ANISOU 1444 N PRO A 200 5660 6304 6600 -14 -53 366 N ATOM 1445 CA PRO A 200 99.504 30.880 241.659 1.00 30.69 C ANISOU 1445 CA PRO A 200 3342 3942 4377 -124 -10 372 C ATOM 1446 C PRO A 200 100.753 31.500 242.287 1.00 37.46 C ANISOU 1446 C PRO A 200 4338 4609 5287 -103 -2 384 C ATOM 1447 O PRO A 200 100.879 31.509 243.511 1.00 37.62 O ANISOU 1447 O PRO A 200 4351 4621 5320 -89 15 390 O ATOM 1448 CB PRO A 200 99.847 29.534 241.008 1.00 27.82 C ANISOU 1448 CB PRO A 200 2954 3546 4069 -307 15 364 C ATOM 1449 CG PRO A 200 98.981 29.462 239.807 1.00 49.28 C ANISOU 1449 CG PRO A 200 5605 6400 6720 -317 -14 345 C ATOM 1450 CD PRO A 200 98.909 30.867 239.303 1.00 63.60 C ANISOU 1450 CD PRO A 200 7484 8204 8476 -136 -55 353 C ATOM 1451 N LEU A 201 101.659 32.009 241.458 1.00 27.13 N ANISOU 1451 N LEU A 201 3145 3170 3992 -119 -13 388 N ATOM 1452 CA LEU A 201 102.899 32.596 241.954 1.00 38.05 C ANISOU 1452 CA LEU A 201 4646 4411 5401 -147 -5 396 C ATOM 1453 C LEU A 201 102.622 33.880 242.731 1.00 41.93 C ANISOU 1453 C LEU A 201 5248 4862 5823 -21 -28 394 C ATOM 1454 O LEU A 201 103.323 34.192 243.689 1.00 41.21 O ANISOU 1454 O LEU A 201 5216 4702 5742 -49 -18 392 O ATOM 1455 CB LEU A 201 103.867 32.866 240.796 1.00 26.56 C ANISOU 1455 CB LEU A 201 3279 2867 3947 -221 -8 400 C ATOM 1456 CG LEU A 201 105.337 33.172 241.101 1.00 26.30 C ANISOU 1456 CG LEU A 201 3318 2747 3928 -317 8 404 C ATOM 1457 CD1 LEU A 201 105.573 34.663 241.302 1.00 55.39 C ANISOU 1457 CD1 LEU A 201 7184 6330 7534 -296 -17 409 C ATOM 1458 CD2 LEU A 201 105.812 32.385 242.315 1.00 49.39 C ANISOU 1458 CD2 LEU A 201 6157 5703 6907 -348 35 403 C ATOM 1459 N SER A 202 101.595 34.617 242.318 1.00 39.47 N ANISOU 1459 N SER A 202 4972 4600 5423 130 -60 391 N ATOM 1460 CA SER A 202 101.234 35.862 242.990 1.00 35.74 C ANISOU 1460 CA SER A 202 4646 4074 4858 297 -83 384 C ATOM 1461 C SER A 202 100.655 35.597 244.374 1.00 38.19 C ANISOU 1461 C SER A 202 4851 4496 5165 363 -66 370 C ATOM 1462 O SER A 202 100.943 36.322 245.326 1.00 53.55 O ANISOU 1462 O SER A 202 6917 6354 7076 416 -67 359 O ATOM 1463 CB SER A 202 100.233 36.658 242.150 1.00 38.66 C ANISOU 1463 CB SER A 202 5085 4492 5110 495 -123 387 C ATOM 1464 OG SER A 202 100.796 37.035 240.905 1.00 39.29 O ANISOU 1464 OG SER A 202 5299 4452 5177 437 -139 406 O ATOM 1465 N VAL A 203 99.840 34.553 244.479 1.00 41.31 N ANISOU 1465 N VAL A 203 5029 5086 5582 338 -49 370 N ATOM 1466 CA VAL A 203 99.193 34.209 245.739 1.00 43.18 C ANISOU 1466 CA VAL A 203 5143 5463 5799 379 -27 363 C ATOM 1467 C VAL A 203 100.190 33.665 246.759 1.00 42.96 C ANISOU 1467 C VAL A 203 5126 5338 5858 241 6 372 C ATOM 1468 O VAL A 203 100.251 34.148 247.889 1.00 58.16 O ANISOU 1468 O VAL A 203 7097 7249 7753 308 11 362 O ATOM 1469 CB VAL A 203 98.068 33.175 245.533 1.00 40.39 C ANISOU 1469 CB VAL A 203 4561 5361 5425 331 -13 364 C ATOM 1470 CG1 VAL A 203 97.580 32.644 246.871 1.00 30.16 C ANISOU 1470 CG1 VAL A 203 3140 4205 4112 308 21 365 C ATOM 1471 CG2 VAL A 203 96.918 33.792 244.749 1.00 31.22 C ANISOU 1471 CG2 VAL A 203 3345 4378 4139 511 -51 350 C ATOM 1472 N ILE A 204 100.975 32.669 246.358 1.00 35.64 N ANISOU 1472 N ILE A 204 4165 4353 5024 69 27 388 N ATOM 1473 CA ILE A 204 101.917 32.034 247.275 1.00 44.32 C ANISOU 1473 CA ILE A 204 5262 5389 6188 -33 55 401 C ATOM 1474 C ILE A 204 103.050 32.976 247.681 1.00 49.70 C ANISOU 1474 C ILE A 204 6085 5934 6864 -30 42 392 C ATOM 1475 O ILE A 204 103.665 32.794 248.730 1.00 58.27 O ANISOU 1475 O ILE A 204 7168 7007 7966 -65 56 396 O ATOM 1476 CB ILE A 204 102.526 30.747 246.673 1.00 42.62 C ANISOU 1476 CB ILE A 204 5005 5141 6048 -174 79 418 C ATOM 1477 CG1 ILE A 204 103.432 31.075 245.483 1.00 63.29 C ANISOU 1477 CG1 ILE A 204 7702 7658 8688 -210 64 412 C ATOM 1478 CG2 ILE A 204 101.429 29.773 246.269 1.00 39.43 C ANISOU 1478 CG2 ILE A 204 4493 4856 5630 -228 93 421 C ATOM 1479 CD1 ILE A 204 104.126 29.866 244.894 1.00 56.19 C ANISOU 1479 CD1 ILE A 204 6779 6727 7843 -309 89 419 C ATOM 1480 N SER A 205 103.323 33.983 246.856 1.00 32.17 N ANISOU 1480 N SER A 205 3998 3619 4606 -5 14 381 N ATOM 1481 CA SER A 205 104.361 34.956 247.178 1.00 34.33 C ANISOU 1481 CA SER A 205 4432 3765 4846 -50 1 369 C ATOM 1482 C SER A 205 103.858 35.945 248.220 1.00 40.41 C ANISOU 1482 C SER A 205 5313 4508 5533 74 -14 345 C ATOM 1483 O SER A 205 104.545 36.227 249.200 1.00 40.56 O ANISOU 1483 O SER A 205 5386 4489 5537 20 -11 331 O ATOM 1484 CB SER A 205 104.822 35.702 245.925 1.00 29.13 C ANISOU 1484 CB SER A 205 3915 3001 4153 -96 -20 371 C ATOM 1485 OG SER A 205 105.354 34.805 244.964 1.00 30.51 O ANISOU 1485 OG SER A 205 3989 3211 4393 -202 -3 386 O ATOM 1486 N TYR A 206 102.655 36.468 247.999 1.00 35.81 N ANISOU 1486 N TYR A 206 4761 3964 4879 253 -31 336 N ATOM 1487 CA TYR A 206 102.041 37.404 248.934 1.00 40.32 C ANISOU 1487 CA TYR A 206 5448 4524 5349 426 -44 306 C ATOM 1488 C TYR A 206 101.801 36.746 250.284 1.00 47.92 C ANISOU 1488 C TYR A 206 6258 5616 6335 429 -15 302 C ATOM 1489 O TYR A 206 102.097 37.324 251.329 1.00 56.04 O ANISOU 1489 O TYR A 206 7390 6589 7315 455 -17 276 O ATOM 1490 CB TYR A 206 100.722 37.945 248.375 1.00 36.33 C ANISOU 1490 CB TYR A 206 4964 4097 4745 663 -66 299 C ATOM 1491 CG TYR A 206 99.944 38.798 249.357 1.00 40.03 C ANISOU 1491 CG TYR A 206 5526 4597 5088 898 -75 264 C ATOM 1492 CD1 TYR A 206 100.276 40.130 249.565 1.00 48.88 C ANISOU 1492 CD1 TYR A 206 6971 5500 6100 992 -101 235 C ATOM 1493 CD2 TYR A 206 98.874 38.271 250.073 1.00 42.50 C ANISOU 1493 CD2 TYR A 206 5619 5159 5369 1019 -55 257 C ATOM 1494 CE1 TYR A 206 99.569 40.913 250.460 1.00 58.90 C ANISOU 1494 CE1 TYR A 206 8357 6786 7238 1236 -108 195 C ATOM 1495 CE2 TYR A 206 98.162 39.046 250.970 1.00 55.80 C ANISOU 1495 CE2 TYR A 206 7378 6902 6923 1258 -59 219 C ATOM 1496 CZ TYR A 206 98.514 40.367 251.158 1.00 62.94 C ANISOU 1496 CZ TYR A 206 8618 7572 7724 1384 -86 186 C ATOM 1497 OH TYR A 206 97.808 41.143 252.049 1.00 60.26 O ANISOU 1497 OH TYR A 206 8382 7277 7238 1651 -90 141 O ATOM 1498 N CYS A 207 101.261 35.532 250.252 1.00 47.51 N ANISOU 1498 N CYS A 207 5977 5731 6343 387 11 327 N ATOM 1499 CA CYS A 207 100.961 34.800 251.474 1.00 36.40 C ANISOU 1499 CA CYS A 207 4430 4454 4947 371 43 335 C ATOM 1500 C CYS A 207 102.221 34.518 252.286 1.00 36.61 C ANISOU 1500 C CYS A 207 4493 4389 5029 237 54 343 C ATOM 1501 O CYS A 207 102.276 34.821 253.476 1.00 39.06 O ANISOU 1501 O CYS A 207 4829 4716 5295 278 60 327 O ATOM 1502 CB CYS A 207 100.236 33.490 251.150 1.00 40.15 C ANISOU 1502 CB CYS A 207 4696 5095 5463 294 71 366 C ATOM 1503 SG CYS A 207 98.561 33.704 250.491 1.00 41.75 S ANISOU 1503 SG CYS A 207 4776 5527 5562 447 60 351 S ATOM 1504 N TYR A 208 103.235 33.953 251.638 1.00 35.10 N ANISOU 1504 N TYR A 208 4295 4124 4916 92 57 364 N ATOM 1505 CA TYR A 208 104.451 33.551 252.337 1.00 27.12 C ANISOU 1505 CA TYR A 208 3281 3084 3941 -17 66 375 C ATOM 1506 C TYR A 208 105.315 34.739 252.734 1.00 32.24 C ANISOU 1506 C TYR A 208 4086 3635 4528 -46 39 339 C ATOM 1507 O TYR A 208 106.115 34.635 253.659 1.00 36.54 O ANISOU 1507 O TYR A 208 4618 4202 5062 -108 41 336 O ATOM 1508 CB TYR A 208 105.261 32.572 251.481 1.00 32.54 C ANISOU 1508 CB TYR A 208 3905 3755 4702 -128 78 403 C ATOM 1509 CG TYR A 208 104.610 31.217 251.339 1.00 42.07 C ANISOU 1509 CG TYR A 208 4998 5032 5957 -141 108 437 C ATOM 1510 CD1 TYR A 208 103.657 30.787 252.249 1.00 37.05 C ANISOU 1510 CD1 TYR A 208 4293 4489 5295 -105 130 452 C ATOM 1511 CD2 TYR A 208 104.950 30.370 250.297 1.00 31.38 C ANISOU 1511 CD2 TYR A 208 3621 3649 4653 -205 118 453 C ATOM 1512 CE1 TYR A 208 103.056 29.547 252.128 1.00 32.72 C ANISOU 1512 CE1 TYR A 208 3670 3995 4765 -166 160 484 C ATOM 1513 CE2 TYR A 208 104.358 29.125 250.160 1.00 39.46 C ANISOU 1513 CE2 TYR A 208 4588 4705 5699 -244 146 479 C ATOM 1514 CZ TYR A 208 103.411 28.720 251.079 1.00 32.00 C ANISOU 1514 CZ TYR A 208 3591 3844 4724 -241 167 496 C ATOM 1515 OH TYR A 208 102.820 27.488 250.951 1.00 26.63 O ANISOU 1515 OH TYR A 208 2885 3190 4045 -326 197 523 O ATOM 1516 N TYR A 209 105.162 35.863 252.039 1.00 33.87 N ANISOU 1516 N TYR A 209 4457 3735 4678 -12 13 312 N ATOM 1517 CA TYR A 209 105.843 37.087 252.458 1.00 38.83 C ANISOU 1517 CA TYR A 209 5292 4244 5217 -61 -12 273 C ATOM 1518 C TYR A 209 105.252 37.594 253.765 1.00 38.03 C ANISOU 1518 C TYR A 209 5251 4157 5041 62 -14 239 C ATOM 1519 O TYR A 209 105.982 37.938 254.697 1.00 35.82 O ANISOU 1519 O TYR A 209 5035 3859 4716 -19 -21 213 O ATOM 1520 CB TYR A 209 105.752 38.183 251.389 1.00 42.08 C ANISOU 1520 CB TYR A 209 5924 4503 5564 -48 -38 258 C ATOM 1521 CG TYR A 209 106.263 39.538 251.847 1.00 41.34 C ANISOU 1521 CG TYR A 209 6115 4246 5345 -102 -63 214 C ATOM 1522 CD1 TYR A 209 107.616 39.862 251.783 1.00 35.25 C ANISOU 1522 CD1 TYR A 209 5422 3430 4542 -348 -71 204 C ATOM 1523 CD2 TYR A 209 105.388 40.488 252.339 1.00 42.09 C ANISOU 1523 CD2 TYR A 209 6410 4248 5333 89 -79 177 C ATOM 1524 CE1 TYR A 209 108.075 41.102 252.199 1.00 33.41 C ANISOU 1524 CE1 TYR A 209 5478 3041 4174 -446 -94 158 C ATOM 1525 CE2 TYR A 209 105.831 41.717 252.759 1.00 58.12 C ANISOU 1525 CE2 TYR A 209 8755 6095 7233 35 -102 131 C ATOM 1526 CZ TYR A 209 107.172 42.020 252.684 1.00 65.10 C ANISOU 1526 CZ TYR A 209 9732 6916 8088 -254 -110 121 C ATOM 1527 OH TYR A 209 107.605 43.247 253.101 1.00114.82 O ANISOU 1527 OH TYR A 209 16369 13022 14235 -352 -132 71 O ATOM 1528 N ARG A 210 103.925 37.647 253.816 1.00 30.18 N ANISOU 1528 N ARG A 210 4226 3223 4018 260 -8 236 N ATOM 1529 CA ARG A 210 103.208 38.061 255.014 1.00 33.61 C ANISOU 1529 CA ARG A 210 4690 3711 4368 414 -3 203 C ATOM 1530 C ARG A 210 103.523 37.147 256.194 1.00 41.70 C ANISOU 1530 C ARG A 210 5544 4863 5436 338 24 222 C ATOM 1531 O ARG A 210 103.750 37.614 257.310 1.00 43.83 O ANISOU 1531 O ARG A 210 5892 5124 5639 355 20 187 O ATOM 1532 CB ARG A 210 101.699 38.074 254.752 1.00 36.70 C ANISOU 1532 CB ARG A 210 5004 4229 4711 641 4 203 C ATOM 1533 CG ARG A 210 101.219 39.156 253.796 1.00 45.80 C ANISOU 1533 CG ARG A 210 6362 5267 5775 798 -28 181 C ATOM 1534 CD ARG A 210 101.366 40.539 254.404 1.00 38.71 C ANISOU 1534 CD ARG A 210 5781 4190 4738 911 -52 123 C ATOM 1535 NE ARG A 210 100.759 40.619 255.729 1.00 44.12 N ANISOU 1535 NE ARG A 210 6420 4995 5348 1061 -35 88 N ATOM 1536 CZ ARG A 210 99.468 40.842 255.950 1.00 44.95 C ANISOU 1536 CZ ARG A 210 6468 5259 5350 1343 -28 69 C ATOM 1537 NH1 ARG A 210 98.635 41.002 254.931 1.00 56.68 N ANISOU 1537 NH1 ARG A 210 7931 6811 6794 1512 -42 82 N ATOM 1538 NH2 ARG A 210 99.009 40.900 257.193 1.00 58.53 N ANISOU 1538 NH2 ARG A 210 8140 7103 6994 1464 -8 36 N ATOM 1539 N ILE A 211 103.529 35.842 255.936 1.00 29.43 N ANISOU 1539 N ILE A 211 3783 3416 3982 259 50 275 N ATOM 1540 CA ILE A 211 103.813 34.853 256.969 1.00 39.70 C ANISOU 1540 CA ILE A 211 4946 4824 5316 196 77 308 C ATOM 1541 C ILE A 211 105.244 34.973 257.475 1.00 40.18 C ANISOU 1541 C ILE A 211 5060 4831 5377 68 61 300 C ATOM 1542 O ILE A 211 105.481 35.032 258.681 1.00 49.92 O ANISOU 1542 O ILE A 211 6291 6114 6562 72 63 289 O ATOM 1543 CB ILE A 211 103.580 33.418 256.456 1.00 43.46 C ANISOU 1543 CB ILE A 211 5254 5378 5880 129 107 369 C ATOM 1544 CG1 ILE A 211 102.093 33.186 256.188 1.00 28.68 C ANISOU 1544 CG1 ILE A 211 3286 3631 3981 219 127 375 C ATOM 1545 CG2 ILE A 211 104.103 32.398 257.458 1.00 39.54 C ANISOU 1545 CG2 ILE A 211 4675 4943 5405 63 132 411 C ATOM 1546 CD1 ILE A 211 101.785 31.829 255.608 1.00 49.68 C ANISOU 1546 CD1 ILE A 211 5821 6352 6705 115 156 426 C ATOM 1547 N SER A 212 106.195 35.017 256.547 1.00 37.82 N ANISOU 1547 N SER A 212 4794 4461 5116 -48 44 303 N ATOM 1548 CA SER A 212 107.607 35.108 256.902 1.00 33.45 C ANISOU 1548 CA SER A 212 4252 3918 4540 -185 28 294 C ATOM 1549 C SER A 212 107.909 36.379 257.686 1.00 48.71 C ANISOU 1549 C SER A 212 6357 5791 6361 -218 0 231 C ATOM 1550 O SER A 212 108.773 36.388 258.560 1.00 55.16 O ANISOU 1550 O SER A 212 7151 6678 7129 -305 -11 218 O ATOM 1551 CB SER A 212 108.481 35.055 255.647 1.00 38.46 C ANISOU 1551 CB SER A 212 4886 4518 5209 -304 18 303 C ATOM 1552 OG SER A 212 108.236 33.876 254.901 1.00 62.13 O ANISOU 1552 OG SER A 212 7753 7555 8298 -271 43 352 O ATOM 1553 N ARG A 213 107.188 37.449 257.374 1.00 33.76 N ANISOU 1553 N ARG A 213 4652 3768 4408 -140 -14 190 N ATOM 1554 CA ARG A 213 107.442 38.740 257.999 1.00 31.73 C ANISOU 1554 CA ARG A 213 4633 3400 4023 -172 -41 123 C ATOM 1555 C ARG A 213 106.917 38.788 259.431 1.00 33.96 C ANISOU 1555 C ARG A 213 4905 3751 4246 -54 -33 96 C ATOM 1556 O ARG A 213 107.322 39.640 260.221 1.00 43.47 O ANISOU 1556 O ARG A 213 6279 4897 5342 -107 -54 37 O ATOM 1557 CB ARG A 213 106.818 39.862 257.166 1.00 32.62 C ANISOU 1557 CB ARG A 213 5001 3323 4069 -86 -58 91 C ATOM 1558 CG ARG A 213 107.448 41.228 257.385 1.00 54.85 C ANISOU 1558 CG ARG A 213 8141 5957 6741 -206 -90 26 C ATOM 1559 CD ARG A 213 108.721 41.428 256.559 1.00 42.51 C ANISOU 1559 CD ARG A 213 6628 4352 5170 -489 -105 34 C ATOM 1560 NE ARG A 213 109.807 40.528 256.941 1.00 70.52 N ANISOU 1560 NE ARG A 213 9917 8107 8771 -663 -98 57 N ATOM 1561 CZ ARG A 213 110.554 40.672 258.032 1.00 94.11 C ANISOU 1561 CZ ARG A 213 12894 11182 11684 -789 -111 20 C ATOM 1562 NH1 ARG A 213 110.335 41.681 258.863 1.00 89.04 N ANISOU 1562 NH1 ARG A 213 12501 10415 10914 -782 -130 -47 N ATOM 1563 NH2 ARG A 213 111.518 39.801 258.296 1.00104.79 N ANISOU 1563 NH2 ARG A 213 13992 12752 13071 -905 -108 47 N ATOM 1564 N ILE A 214 106.017 37.867 259.758 1.00 40.99 N ANISOU 1564 N ILE A 214 5605 4774 5197 85 0 138 N ATOM 1565 CA ILE A 214 105.454 37.780 261.100 1.00 32.03 C ANISOU 1565 CA ILE A 214 4426 3740 4003 196 17 123 C ATOM 1566 C ILE A 214 106.285 36.851 261.978 1.00 45.78 C ANISOU 1566 C ILE A 214 6006 5612 5775 86 25 161 C ATOM 1567 O ILE A 214 106.590 37.167 263.129 1.00 50.79 O ANISOU 1567 O ILE A 214 6682 6288 6328 75 16 127 O ATOM 1568 CB ILE A 214 103.994 37.284 261.063 1.00 31.93 C ANISOU 1568 CB ILE A 214 4285 3842 4007 384 52 152 C ATOM 1569 CG1 ILE A 214 103.090 38.354 260.449 1.00 32.92 C ANISOU 1569 CG1 ILE A 214 4577 3877 4053 562 38 104 C ATOM 1570 CG2 ILE A 214 103.508 36.915 262.457 1.00 36.23 C ANISOU 1570 CG2 ILE A 214 4730 4540 4497 460 80 154 C ATOM 1571 CD1 ILE A 214 101.624 38.019 260.521 1.00 36.93 C ANISOU 1571 CD1 ILE A 214 4937 4565 4531 761 70 117 C ATOM 1572 N VAL A 215 106.658 35.708 261.412 1.00 36.96 N ANISOU 1572 N VAL A 215 4724 4557 4763 19 40 230 N ATOM 1573 CA VAL A 215 107.414 34.689 262.130 1.00 36.28 C ANISOU 1573 CA VAL A 215 4496 4593 4696 -40 48 280 C ATOM 1574 C VAL A 215 108.837 35.152 262.437 1.00 30.71 C ANISOU 1574 C VAL A 215 3827 3912 3929 -181 10 245 C ATOM 1575 O VAL A 215 109.389 34.827 263.488 1.00 46.95 O ANISOU 1575 O VAL A 215 5817 6085 5934 -198 4 254 O ATOM 1576 CB VAL A 215 107.467 33.371 261.328 1.00 33.03 C ANISOU 1576 CB VAL A 215 3949 4210 4390 -53 73 357 C ATOM 1577 CG1 VAL A 215 108.126 32.272 262.139 1.00 43.18 C ANISOU 1577 CG1 VAL A 215 5129 5606 5673 -60 84 415 C ATOM 1578 CG2 VAL A 215 106.068 32.950 260.925 1.00 28.99 C ANISOU 1578 CG2 VAL A 215 3397 3697 3920 34 108 383 C ATOM 1579 N ALA A 216 109.419 35.923 261.522 1.00 57.73 N ANISOU 1579 N ALA A 216 7352 7243 7338 -294 -16 207 N ATOM 1580 CA ALA A 216 110.798 36.388 261.665 1.00 44.55 C ANISOU 1580 CA ALA A 216 5702 5635 5589 -478 -51 171 C ATOM 1581 C ALA A 216 110.986 37.283 262.888 1.00 32.93 C ANISOU 1581 C ALA A 216 4353 4173 3986 -529 -76 102 C ATOM 1582 O ALA A 216 112.093 37.404 263.411 1.00 47.14 O ANISOU 1582 O ALA A 216 6108 6103 5701 -676 -104 79 O ATOM 1583 CB ALA A 216 111.238 37.123 260.406 1.00 31.93 C ANISOU 1583 CB ALA A 216 4219 3930 3984 -615 -67 144 C ATOM 1584 N VAL A 217 109.904 37.906 263.342 1.00 43.43 N ANISOU 1584 N VAL A 217 5832 5388 5282 -400 -67 65 N ATOM 1585 CA VAL A 217 109.966 38.800 264.492 1.00 40.81 C ANISOU 1585 CA VAL A 217 5655 5038 4813 -424 -89 -11 C ATOM 1586 C VAL A 217 109.327 38.144 265.720 1.00 34.59 C ANISOU 1586 C VAL A 217 4743 4377 4021 -265 -64 15 C ATOM 1587 O VAL A 217 109.344 38.700 266.818 1.00 49.58 O ANISOU 1587 O VAL A 217 6735 6297 5807 -261 -77 -43 O ATOM 1588 CB VAL A 217 109.272 40.146 264.186 1.00 42.23 C ANISOU 1588 CB VAL A 217 6150 4986 4912 -372 -99 -86 C ATOM 1589 CG1 VAL A 217 107.763 40.011 264.331 1.00 43.07 C ANISOU 1589 CG1 VAL A 217 6249 5068 5047 -92 -65 -73 C ATOM 1590 CG2 VAL A 217 109.812 41.255 265.082 1.00 55.43 C ANISOU 1590 CG2 VAL A 217 8056 6592 6412 -500 -134 -182 C ATOM 1591 N SER A 218 108.772 36.951 265.529 1.00 33.28 N ANISOU 1591 N SER A 218 4383 4294 3966 -151 -26 101 N ATOM 1592 CA SER A 218 108.159 36.211 266.627 1.00 37.66 C ANISOU 1592 CA SER A 218 4821 4978 4512 -29 5 142 C ATOM 1593 C SER A 218 109.223 35.547 267.494 1.00 49.51 C ANISOU 1593 C SER A 218 6197 6638 5975 -106 -11 175 C ATOM 1594 O SER A 218 110.414 35.617 267.190 1.00 54.36 O ANISOU 1594 O SER A 218 6785 7298 6573 -244 -46 165 O ATOM 1595 CB SER A 218 107.188 35.156 266.096 1.00 34.94 C ANISOU 1595 CB SER A 218 4343 4658 4274 76 52 224 C ATOM 1596 OG SER A 218 107.885 34.098 265.463 1.00 48.89 O ANISOU 1596 OG SER A 218 5987 6458 6130 7 55 296 O ATOM 1597 N GLN A 219 108.789 34.898 268.570 1.00 53.15 N ANISOU 1597 N GLN A 219 6575 7212 6408 -12 14 217 N ATOM 1598 CA GLN A 219 109.712 34.233 269.482 1.00 52.94 C ANISOU 1598 CA GLN A 219 6440 7349 6328 -45 -2 258 C ATOM 1599 C GLN A 219 109.737 32.724 269.253 1.00 43.31 C ANISOU 1599 C GLN A 219 5081 6185 5188 17 28 376 C ATOM 1600 O GLN A 219 110.130 31.962 270.137 1.00 45.26 O ANISOU 1600 O GLN A 219 5255 6557 5384 58 29 434 O ATOM 1601 CB GLN A 219 109.344 34.535 270.937 1.00 64.52 C ANISOU 1601 CB GLN A 219 7937 8900 7678 13 2 227 C ATOM 1602 CG GLN A 219 109.318 36.017 271.277 1.00 77.03 C ANISOU 1602 CG GLN A 219 9707 10406 9154 -34 -29 101 C ATOM 1603 CD GLN A 219 109.091 36.273 272.755 1.00 94.54 C ANISOU 1603 CD GLN A 219 11954 12725 11241 22 -28 65 C ATOM 1604 OE1 GLN A 219 109.637 35.574 273.609 1.00104.77 O ANISOU 1604 OE1 GLN A 219 13130 14186 12493 14 -35 115 O ATOM 1605 NE2 GLN A 219 108.280 37.279 273.064 1.00100.63 N ANISOU 1605 NE2 GLN A 219 12894 13403 11936 100 -19 -23 N ATOM 1606 N SER A 220 109.314 32.298 268.067 1.00 51.72 N ANISOU 1606 N SER A 220 6136 7148 6366 27 52 411 N ATOM 1607 CA SER A 220 109.362 30.887 267.702 1.00 31.84 C ANISOU 1607 CA SER A 220 3541 4640 3916 71 81 514 C ATOM 1608 C SER A 220 110.806 30.404 267.632 1.00 36.36 C ANISOU 1608 C SER A 220 4045 5312 4459 57 46 540 C ATOM 1609 O SER A 220 111.684 31.118 267.147 1.00 44.89 O ANISOU 1609 O SER A 220 5113 6424 5518 -31 6 480 O ATOM 1610 CB SER A 220 108.660 30.649 266.365 1.00 57.71 C ANISOU 1610 CB SER A 220 6834 7789 7305 63 108 528 C ATOM 1611 OG SER A 220 108.783 29.297 265.960 1.00 64.25 O ANISOU 1611 OG SER A 220 7628 8599 8183 91 133 618 O ATOM 1612 N ARG A 221 111.050 29.192 268.118 1.00 32.49 N ANISOU 1612 N ARG A 221 3515 4883 3946 147 61 632 N ATOM 1613 CA ARG A 221 112.403 28.647 268.152 1.00 33.14 C ANISOU 1613 CA ARG A 221 3521 5101 3969 195 28 662 C ATOM 1614 C ARG A 221 112.762 27.975 266.830 1.00 36.26 C ANISOU 1614 C ARG A 221 3906 5428 4442 224 37 693 C ATOM 1615 O ARG A 221 113.837 27.391 266.690 1.00 33.34 O ANISOU 1615 O ARG A 221 3469 5178 4019 305 16 723 O ATOM 1616 CB ARG A 221 112.553 27.661 269.311 1.00 34.03 C ANISOU 1616 CB ARG A 221 3631 5305 3994 320 36 751 C ATOM 1617 CG ARG A 221 111.731 26.396 269.168 1.00 42.29 C ANISOU 1617 CG ARG A 221 4772 6207 5089 395 92 854 C ATOM 1618 CD ARG A 221 111.433 25.784 270.526 1.00 66.37 C ANISOU 1618 CD ARG A 221 7867 9311 8042 466 111 929 C ATOM 1619 NE ARG A 221 112.634 25.619 271.338 1.00 77.00 N ANISOU 1619 NE ARG A 221 9149 10847 9259 572 63 949 N ATOM 1620 CZ ARG A 221 112.628 25.212 272.602 1.00 86.77 C ANISOU 1620 CZ ARG A 221 10413 12172 10385 647 65 1009 C ATOM 1621 NH1 ARG A 221 111.480 24.929 273.203 1.00 76.71 N ANISOU 1621 NH1 ARG A 221 9227 10810 9111 611 118 1056 N ATOM 1622 NH2 ARG A 221 113.768 25.089 273.268 1.00 96.50 N ANISOU 1622 NH2 ARG A 221 11570 13609 11488 756 15 1023 N ATOM 1623 N HIS A 222 111.857 28.067 265.861 1.00 45.45 N ANISOU 1623 N HIS A 222 5130 6421 5717 173 68 682 N ATOM 1624 CA HIS A 222 112.107 27.540 264.526 1.00 38.58 C ANISOU 1624 CA HIS A 222 4263 5474 4922 185 78 697 C ATOM 1625 C HIS A 222 111.781 28.587 263.469 1.00 33.10 C ANISOU 1625 C HIS A 222 3582 4694 4299 66 71 621 C ATOM 1626 O HIS A 222 111.556 28.259 262.305 1.00 33.60 O ANISOU 1626 O HIS A 222 3667 4657 4442 58 88 629 O ATOM 1627 CB HIS A 222 111.290 26.271 264.283 1.00 37.50 C ANISOU 1627 CB HIS A 222 4216 5196 4836 249 127 781 C ATOM 1628 CG HIS A 222 111.609 25.158 265.231 1.00 32.42 C ANISOU 1628 CG HIS A 222 3617 4593 4107 375 138 869 C ATOM 1629 ND1 HIS A 222 112.797 24.460 265.186 1.00 42.72 N ANISOU 1629 ND1 HIS A 222 4903 5985 5342 515 116 905 N ATOM 1630 CD2 HIS A 222 110.896 24.621 266.249 1.00 32.64 C ANISOU 1630 CD2 HIS A 222 3716 4594 4090 392 168 932 C ATOM 1631 CE1 HIS A 222 112.802 23.542 266.136 1.00 38.15 C ANISOU 1631 CE1 HIS A 222 4407 5409 4681 630 129 990 C ATOM 1632 NE2 HIS A 222 111.660 23.618 266.795 1.00 44.60 N ANISOU 1632 NE2 HIS A 222 5284 6150 5513 540 162 1010 N ATOM 1633 N LYS A 223 111.766 29.850 263.887 1.00 38.12 N ANISOU 1633 N LYS A 223 4230 5359 4892 -23 44 547 N ATOM 1634 CA LYS A 223 111.424 30.959 263.001 1.00 33.00 C ANISOU 1634 CA LYS A 223 3647 4606 4284 -122 35 476 C ATOM 1635 C LYS A 223 112.380 31.071 261.818 1.00 30.11 C ANISOU 1635 C LYS A 223 3242 4264 3934 -196 17 458 C ATOM 1636 O LYS A 223 111.991 31.510 260.736 1.00 29.58 O ANISOU 1636 O LYS A 223 3232 4079 3927 -246 23 434 O ATOM 1637 CB LYS A 223 111.406 32.278 263.782 1.00 30.79 C ANISOU 1637 CB LYS A 223 3440 4340 3920 -197 6 398 C ATOM 1638 CG LYS A 223 112.725 32.633 264.454 1.00 38.67 C ANISOU 1638 CG LYS A 223 4379 5512 4800 -284 -37 365 C ATOM 1639 CD LYS A 223 112.622 33.938 265.230 1.00 41.32 C ANISOU 1639 CD LYS A 223 4834 5827 5039 -378 -64 278 C ATOM 1640 CE LYS A 223 113.932 34.274 265.928 1.00 54.28 C ANISOU 1640 CE LYS A 223 6407 7673 6543 -502 -109 240 C ATOM 1641 NZ LYS A 223 113.840 35.543 266.703 1.00 72.08 N ANISOU 1641 NZ LYS A 223 8817 9885 8686 -615 -137 146 N ATOM 1642 N GLY A 224 113.629 30.669 262.027 1.00 37.13 N ANISOU 1642 N GLY A 224 4023 5333 4752 -190 -4 472 N ATOM 1643 CA GLY A 224 114.640 30.761 260.992 1.00 31.10 C ANISOU 1643 CA GLY A 224 3187 4657 3971 -259 -18 452 C ATOM 1644 C GLY A 224 114.393 29.813 259.835 1.00 39.28 C ANISOU 1644 C GLY A 224 4222 5599 5102 -169 14 498 C ATOM 1645 O GLY A 224 114.401 30.224 258.675 1.00 30.02 O ANISOU 1645 O GLY A 224 3072 4362 3972 -250 17 470 O ATOM 1646 N ARG A 225 114.166 28.542 260.151 1.00 38.08 N ANISOU 1646 N ARG A 225 4071 5427 4971 -7 39 568 N ATOM 1647 CA ARG A 225 113.993 27.521 259.125 1.00 32.25 C ANISOU 1647 CA ARG A 225 3364 4590 4299 82 69 609 C ATOM 1648 C ARG A 225 112.653 27.654 258.410 1.00 36.59 C ANISOU 1648 C ARG A 225 4015 4926 4960 22 96 604 C ATOM 1649 O ARG A 225 112.546 27.343 257.225 1.00 36.50 O ANISOU 1649 O ARG A 225 4027 4838 5005 17 111 602 O ATOM 1650 CB ARG A 225 114.127 26.123 259.733 1.00 30.70 C ANISOU 1650 CB ARG A 225 3199 4400 4064 265 88 687 C ATOM 1651 CG ARG A 225 114.303 25.024 258.701 1.00 30.85 C ANISOU 1651 CG ARG A 225 3274 4340 4109 376 113 719 C ATOM 1652 CD ARG A 225 114.931 23.785 259.311 1.00 43.68 C ANISOU 1652 CD ARG A 225 4940 6019 5639 593 118 788 C ATOM 1653 NE ARG A 225 113.955 22.952 260.004 1.00 56.90 N ANISOU 1653 NE ARG A 225 6781 7513 7328 627 149 856 N ATOM 1654 CZ ARG A 225 113.260 21.982 259.419 1.00 51.33 C ANISOU 1654 CZ ARG A 225 6247 6594 6664 644 188 894 C ATOM 1655 NH1 ARG A 225 113.433 21.726 258.130 1.00 37.65 N ANISOU 1655 NH1 ARG A 225 4539 4795 4970 655 197 866 N ATOM 1656 NH2 ARG A 225 112.392 21.267 260.122 1.00 57.75 N ANISOU 1656 NH2 ARG A 225 7213 7264 7464 629 218 958 N ATOM 1657 N ILE A 226 111.639 28.116 259.136 1.00 28.68 N ANISOU 1657 N ILE A 226 3064 3860 3974 -13 102 598 N ATOM 1658 CA ILE A 226 110.309 28.315 258.568 1.00 39.15 C ANISOU 1658 CA ILE A 226 4454 5046 5375 -54 124 589 C ATOM 1659 C ILE A 226 110.352 29.247 257.359 1.00 42.28 C ANISOU 1659 C ILE A 226 4866 5393 5807 -135 107 534 C ATOM 1660 O ILE A 226 109.769 28.950 256.314 1.00 31.14 O ANISOU 1660 O ILE A 226 3479 3893 4458 -143 123 539 O ATOM 1661 CB ILE A 226 109.328 28.883 259.615 1.00 28.06 C ANISOU 1661 CB ILE A 226 3074 3641 3945 -58 129 578 C ATOM 1662 CG1 ILE A 226 108.912 27.789 260.598 1.00 33.75 C ANISOU 1662 CG1 ILE A 226 3801 4382 4640 2 160 647 C ATOM 1663 CG2 ILE A 226 108.097 29.469 258.943 1.00 27.62 C ANISOU 1663 CG2 ILE A 226 3056 3505 3935 -84 139 547 C ATOM 1664 CD1 ILE A 226 107.953 28.262 261.669 1.00 40.18 C ANISOU 1664 CD1 ILE A 226 4618 5235 5414 4 172 639 C ATOM 1665 N VAL A 227 111.056 30.365 257.502 1.00 32.71 N ANISOU 1665 N VAL A 227 3653 4236 4540 -212 75 482 N ATOM 1666 CA VAL A 227 111.171 31.336 256.421 1.00 38.01 C ANISOU 1666 CA VAL A 227 4377 4847 5219 -308 59 436 C ATOM 1667 C VAL A 227 111.930 30.747 255.233 1.00 44.85 C ANISOU 1667 C VAL A 227 5184 5747 6110 -323 66 450 C ATOM 1668 O VAL A 227 111.528 30.927 254.085 1.00 48.17 O ANISOU 1668 O VAL A 227 5648 6076 6578 -351 72 441 O ATOM 1669 CB VAL A 227 111.873 32.624 256.893 1.00 45.23 C ANISOU 1669 CB VAL A 227 5341 5807 6039 -429 24 378 C ATOM 1670 CG1 VAL A 227 111.992 33.618 255.748 1.00 28.66 C ANISOU 1670 CG1 VAL A 227 3343 3619 3930 -547 10 340 C ATOM 1671 CG2 VAL A 227 111.113 33.241 258.056 1.00 28.80 C ANISOU 1671 CG2 VAL A 227 3342 3682 3919 -394 17 354 C ATOM 1672 N ARG A 228 113.015 30.031 255.516 1.00 34.40 N ANISOU 1672 N ARG A 228 3759 4571 4739 -281 65 471 N ATOM 1673 CA ARG A 228 113.829 29.422 254.466 1.00 41.77 C ANISOU 1673 CA ARG A 228 4626 5575 5670 -258 75 479 C ATOM 1674 C ARG A 228 113.046 28.386 253.666 1.00 46.19 C ANISOU 1674 C ARG A 228 5240 5993 6317 -166 107 513 C ATOM 1675 O ARG A 228 113.246 28.237 252.460 1.00 41.62 O ANISOU 1675 O ARG A 228 4658 5395 5760 -180 116 502 O ATOM 1676 CB ARG A 228 115.079 28.774 255.064 1.00 29.40 C ANISOU 1676 CB ARG A 228 2934 4227 4008 -171 67 497 C ATOM 1677 CG ARG A 228 115.964 29.737 255.824 1.00 36.88 C ANISOU 1677 CG ARG A 228 3803 5365 4844 -293 32 458 C ATOM 1678 CD ARG A 228 117.344 29.150 256.061 1.00 31.59 C ANISOU 1678 CD ARG A 228 2962 4987 4054 -210 21 467 C ATOM 1679 NE ARG A 228 117.303 27.929 256.860 1.00 45.13 N ANISOU 1679 NE ARG A 228 4671 6718 5757 18 30 527 N ATOM 1680 CZ ARG A 228 117.349 27.906 258.188 1.00 41.97 C ANISOU 1680 CZ ARG A 228 4255 6393 5300 61 12 543 C ATOM 1681 NH1 ARG A 228 117.427 29.041 258.869 1.00 48.88 N ANISOU 1681 NH1 ARG A 228 5114 7331 6125 -113 -17 496 N ATOM 1682 NH2 ARG A 228 117.310 26.749 258.834 1.00 51.70 N ANISOU 1682 NH2 ARG A 228 5513 7620 6510 274 23 608 N ATOM 1683 N VAL A 229 112.157 27.668 254.345 1.00 43.22 N ANISOU 1683 N VAL A 229 4920 5527 5975 -92 125 552 N ATOM 1684 CA VAL A 229 111.309 26.685 253.686 1.00 27.23 C ANISOU 1684 CA VAL A 229 2968 3366 4012 -53 156 580 C ATOM 1685 C VAL A 229 110.349 27.373 252.720 1.00 36.00 C ANISOU 1685 C VAL A 229 4112 4383 5183 -145 154 548 C ATOM 1686 O VAL A 229 110.183 26.940 251.579 1.00 44.51 O ANISOU 1686 O VAL A 229 5216 5401 6297 -153 166 544 O ATOM 1687 CB VAL A 229 110.512 25.850 254.713 1.00 27.45 C ANISOU 1687 CB VAL A 229 3057 3335 4037 -6 178 631 C ATOM 1688 CG1 VAL A 229 109.410 25.058 254.027 1.00 48.49 C ANISOU 1688 CG1 VAL A 229 5808 5864 6750 -42 208 649 C ATOM 1689 CG2 VAL A 229 111.442 24.922 255.480 1.00 28.35 C ANISOU 1689 CG2 VAL A 229 3178 3513 4080 124 182 676 C ATOM 1690 N LEU A 230 109.733 28.457 253.181 1.00 35.48 N ANISOU 1690 N LEU A 230 4055 4311 5114 -195 137 523 N ATOM 1691 CA LEU A 230 108.759 29.192 252.380 1.00 31.49 C ANISOU 1691 CA LEU A 230 3590 3733 4640 -238 131 496 C ATOM 1692 C LEU A 230 109.404 29.900 251.192 1.00 33.79 C ANISOU 1692 C LEU A 230 3898 4012 4929 -299 113 465 C ATOM 1693 O LEU A 230 108.796 30.018 250.128 1.00 42.56 O ANISOU 1693 O LEU A 230 5039 5063 6070 -313 114 456 O ATOM 1694 CB LEU A 230 108.016 30.205 253.251 1.00 43.43 C ANISOU 1694 CB LEU A 230 5134 5248 6121 -228 117 475 C ATOM 1695 CG LEU A 230 107.196 29.610 254.398 1.00 38.95 C ANISOU 1695 CG LEU A 230 4539 4716 5542 -179 139 504 C ATOM 1696 CD1 LEU A 230 106.472 30.706 255.162 1.00 55.11 C ANISOU 1696 CD1 LEU A 230 6616 6782 7541 -142 126 472 C ATOM 1697 CD2 LEU A 230 106.214 28.573 253.874 1.00 26.21 C ANISOU 1697 CD2 LEU A 230 2909 3083 3965 -189 169 535 C ATOM 1698 N ILE A 231 110.631 30.375 251.378 1.00 30.81 N ANISOU 1698 N ILE A 231 3495 3714 4498 -349 98 449 N ATOM 1699 CA ILE A 231 111.375 31.011 250.296 1.00 36.06 C ANISOU 1699 CA ILE A 231 4170 4397 5136 -442 88 424 C ATOM 1700 C ILE A 231 111.702 29.991 249.209 1.00 53.25 C ANISOU 1700 C ILE A 231 6295 6593 7345 -402 110 438 C ATOM 1701 O ILE A 231 111.593 30.280 248.016 1.00 43.92 O ANISOU 1701 O ILE A 231 5145 5368 6175 -449 110 426 O ATOM 1702 CB ILE A 231 112.680 31.662 250.807 1.00 43.97 C ANISOU 1702 CB ILE A 231 5130 5533 6044 -542 70 402 C ATOM 1703 CG1 ILE A 231 112.362 32.834 251.734 1.00 42.84 C ANISOU 1703 CG1 ILE A 231 5089 5336 5851 -606 45 374 C ATOM 1704 CG2 ILE A 231 113.535 32.142 249.647 1.00 27.78 C ANISOU 1704 CG2 ILE A 231 3068 3541 3946 -665 68 383 C ATOM 1705 CD1 ILE A 231 113.578 33.609 252.183 1.00 34.87 C ANISOU 1705 CD1 ILE A 231 4065 4454 4728 -762 23 342 C ATOM 1706 N ALA A 232 112.087 28.791 249.637 1.00 47.54 N ANISOU 1706 N ALA A 232 5516 5925 6622 -302 129 465 N ATOM 1707 CA ALA A 232 112.437 27.713 248.719 1.00 26.70 C ANISOU 1707 CA ALA A 232 2862 3289 3992 -230 152 473 C ATOM 1708 C ALA A 232 111.265 27.344 247.815 1.00 38.75 C ANISOU 1708 C ALA A 232 4468 4669 5588 -240 164 473 C ATOM 1709 O ALA A 232 111.450 27.083 246.627 1.00 35.58 O ANISOU 1709 O ALA A 232 4074 4255 5191 -246 173 459 O ATOM 1710 CB ALA A 232 112.911 26.495 249.493 1.00 27.28 C ANISOU 1710 CB ALA A 232 2922 3408 4034 -88 168 506 C ATOM 1711 N VAL A 233 110.064 27.325 248.387 1.00 35.48 N ANISOU 1711 N VAL A 233 4098 4173 5210 -249 164 487 N ATOM 1712 CA VAL A 233 108.851 27.029 247.631 1.00 38.19 C ANISOU 1712 CA VAL A 233 4486 4429 5595 -280 171 484 C ATOM 1713 C VAL A 233 108.686 27.992 246.458 1.00 37.44 C ANISOU 1713 C VAL A 233 4396 4325 5504 -335 152 454 C ATOM 1714 O VAL A 233 108.381 27.578 245.339 1.00 43.63 O ANISOU 1714 O VAL A 233 5199 5075 6304 -352 158 444 O ATOM 1715 CB VAL A 233 107.595 27.098 248.528 1.00 32.26 C ANISOU 1715 CB VAL A 233 3740 3664 4852 -291 172 499 C ATOM 1716 CG1 VAL A 233 106.329 26.964 247.693 1.00 31.43 C ANISOU 1716 CG1 VAL A 233 3642 3536 4763 -338 174 488 C ATOM 1717 CG2 VAL A 233 107.647 26.023 249.602 1.00 25.90 C ANISOU 1717 CG2 VAL A 233 2958 2850 4032 -255 197 538 C ATOM 1718 N VAL A 234 108.905 29.276 246.719 1.00 26.40 N ANISOU 1718 N VAL A 234 3006 2947 4079 -367 127 441 N ATOM 1719 CA VAL A 234 108.773 30.300 245.690 1.00 29.12 C ANISOU 1719 CA VAL A 234 3400 3258 4405 -417 107 422 C ATOM 1720 C VAL A 234 109.891 30.199 244.654 1.00 42.44 C ANISOU 1720 C VAL A 234 5068 4988 6071 -469 116 413 C ATOM 1721 O VAL A 234 109.639 30.270 243.451 1.00 41.41 O ANISOU 1721 O VAL A 234 4964 4827 5943 -490 114 406 O ATOM 1722 CB VAL A 234 108.776 31.715 246.300 1.00 29.78 C ANISOU 1722 CB VAL A 234 3560 3317 4439 -444 81 410 C ATOM 1723 CG1 VAL A 234 108.534 32.758 245.221 1.00 25.88 C ANISOU 1723 CG1 VAL A 234 3173 2754 3908 -480 60 399 C ATOM 1724 CG2 VAL A 234 107.726 31.822 247.394 1.00 25.58 C ANISOU 1724 CG2 VAL A 234 3035 2774 3911 -366 76 413 C ATOM 1725 N LEU A 235 111.122 30.029 245.128 1.00 40.90 N ANISOU 1725 N LEU A 235 4811 4892 5837 -484 125 413 N ATOM 1726 CA LEU A 235 112.286 29.963 244.247 1.00 37.11 C ANISOU 1726 CA LEU A 235 4276 4516 5307 -529 137 402 C ATOM 1727 C LEU A 235 112.236 28.766 243.304 1.00 38.69 C ANISOU 1727 C LEU A 235 4459 4707 5535 -447 162 399 C ATOM 1728 O LEU A 235 112.487 28.902 242.107 1.00 42.99 O ANISOU 1728 O LEU A 235 5006 5272 6059 -488 169 386 O ATOM 1729 CB LEU A 235 113.575 29.916 245.070 1.00 34.84 C ANISOU 1729 CB LEU A 235 3888 4399 4948 -538 140 400 C ATOM 1730 CG LEU A 235 113.963 31.199 245.804 1.00 44.81 C ANISOU 1730 CG LEU A 235 5176 5703 6147 -676 115 388 C ATOM 1731 CD1 LEU A 235 115.254 30.997 246.577 1.00 54.10 C ANISOU 1731 CD1 LEU A 235 6215 7104 7236 -688 117 383 C ATOM 1732 CD2 LEU A 235 114.097 32.355 244.825 1.00 44.43 C ANISOU 1732 CD2 LEU A 235 5216 5617 6047 -838 106 376 C ATOM 1733 N VAL A 236 111.919 27.596 243.850 1.00 36.55 N ANISOU 1733 N VAL A 236 4195 4397 5297 -340 178 412 N ATOM 1734 CA VAL A 236 111.843 26.375 243.054 1.00 44.66 C ANISOU 1734 CA VAL A 236 5258 5378 6333 -263 202 404 C ATOM 1735 C VAL A 236 110.750 26.486 241.993 1.00 44.28 C ANISOU 1735 C VAL A 236 5271 5228 6325 -327 195 390 C ATOM 1736 O VAL A 236 110.939 26.069 240.849 1.00 51.55 O ANISOU 1736 O VAL A 236 6209 6147 7230 -320 208 368 O ATOM 1737 CB VAL A 236 111.586 25.139 243.944 1.00 36.07 C ANISOU 1737 CB VAL A 236 4229 4222 5255 -159 219 426 C ATOM 1738 CG1 VAL A 236 111.240 23.924 243.097 1.00 36.73 C ANISOU 1738 CG1 VAL A 236 4419 4197 5339 -113 243 413 C ATOM 1739 CG2 VAL A 236 112.800 24.853 244.815 1.00 27.42 C ANISOU 1739 CG2 VAL A 236 3070 3254 4095 -48 225 440 C ATOM 1740 N PHE A 237 109.617 27.068 242.374 1.00 30.22 N ANISOU 1740 N PHE A 237 3513 3389 4580 -377 174 400 N ATOM 1741 CA PHE A 237 108.497 27.249 241.455 1.00 38.03 C ANISOU 1741 CA PHE A 237 4534 4329 5586 -423 161 388 C ATOM 1742 C PHE A 237 108.894 28.111 240.260 1.00 38.67 C ANISOU 1742 C PHE A 237 4620 4437 5637 -466 148 375 C ATOM 1743 O PHE A 237 108.517 27.824 239.125 1.00 40.85 O ANISOU 1743 O PHE A 237 4916 4697 5908 -483 148 358 O ATOM 1744 CB PHE A 237 107.304 27.876 242.181 1.00 26.72 C ANISOU 1744 CB PHE A 237 3099 2887 4166 -431 138 400 C ATOM 1745 CG PHE A 237 106.076 28.020 241.324 1.00 40.04 C ANISOU 1745 CG PHE A 237 4789 4579 5846 -454 120 388 C ATOM 1746 CD1 PHE A 237 105.822 29.199 240.642 1.00 45.01 C ANISOU 1746 CD1 PHE A 237 5440 5217 6445 -444 90 385 C ATOM 1747 CD2 PHE A 237 105.174 26.976 241.204 1.00 33.38 C ANISOU 1747 CD2 PHE A 237 3936 3740 5006 -492 131 381 C ATOM 1748 CE1 PHE A 237 104.695 29.333 239.855 1.00 38.62 C ANISOU 1748 CE1 PHE A 237 4619 4447 5609 -436 68 376 C ATOM 1749 CE2 PHE A 237 104.044 27.105 240.418 1.00 40.12 C ANISOU 1749 CE2 PHE A 237 4761 4651 5832 -524 111 366 C ATOM 1750 CZ PHE A 237 103.805 28.285 239.744 1.00 42.69 C ANISOU 1750 CZ PHE A 237 5083 5011 6128 -477 77 364 C ATOM 1751 N ILE A 238 109.657 29.165 240.524 1.00 34.64 N ANISOU 1751 N ILE A 238 4104 3966 5091 -504 138 382 N ATOM 1752 CA ILE A 238 110.095 30.076 239.474 1.00 28.97 C ANISOU 1752 CA ILE A 238 3419 3265 4323 -577 129 378 C ATOM 1753 C ILE A 238 111.098 29.415 238.532 1.00 37.33 C ANISOU 1753 C ILE A 238 4425 4410 5350 -584 159 362 C ATOM 1754 O ILE A 238 110.909 29.414 237.318 1.00 41.45 O ANISOU 1754 O ILE A 238 4972 4922 5854 -605 160 352 O ATOM 1755 CB ILE A 238 110.723 31.353 240.066 1.00 30.60 C ANISOU 1755 CB ILE A 238 3665 3486 4474 -660 115 389 C ATOM 1756 CG1 ILE A 238 109.673 32.146 240.847 1.00 26.28 C ANISOU 1756 CG1 ILE A 238 3206 2842 3938 -625 85 398 C ATOM 1757 CG2 ILE A 238 111.326 32.212 238.966 1.00 27.97 C ANISOU 1757 CG2 ILE A 238 3390 3172 4066 -774 114 391 C ATOM 1758 CD1 ILE A 238 110.216 33.392 241.510 1.00 27.80 C ANISOU 1758 CD1 ILE A 238 3492 3009 4063 -710 69 400 C ATOM 1759 N ILE A 239 112.154 28.833 239.095 1.00 34.47 N ANISOU 1759 N ILE A 239 3985 4150 4964 -544 182 357 N ATOM 1760 CA ILE A 239 113.238 28.272 238.290 1.00 45.14 C ANISOU 1760 CA ILE A 239 5268 5631 6254 -517 213 337 C ATOM 1761 C ILE A 239 112.827 27.042 237.477 1.00 46.22 C ANISOU 1761 C ILE A 239 5446 5703 6413 -418 231 312 C ATOM 1762 O ILE A 239 113.614 26.535 236.678 1.00 62.41 O ANISOU 1762 O ILE A 239 7460 7849 8404 -367 258 288 O ATOM 1763 CB ILE A 239 114.448 27.890 239.170 1.00 48.33 C ANISOU 1763 CB ILE A 239 5562 6201 6602 -452 230 336 C ATOM 1764 CG1 ILE A 239 114.079 26.763 240.134 1.00 70.65 C ANISOU 1764 CG1 ILE A 239 8420 8949 9477 -303 235 344 C ATOM 1765 CG2 ILE A 239 114.962 29.104 239.931 1.00 44.17 C ANISOU 1765 CG2 ILE A 239 4995 5759 6027 -589 211 350 C ATOM 1766 CD1 ILE A 239 115.221 26.325 241.024 1.00 98.48 C ANISOU 1766 CD1 ILE A 239 11844 12643 12931 -197 247 348 C ATOM 1767 N PHE A 240 111.602 26.566 237.672 1.00 40.54 N ANISOU 1767 N PHE A 240 4806 4837 5761 -401 219 314 N ATOM 1768 CA PHE A 240 111.125 25.391 236.947 1.00 34.66 C ANISOU 1768 CA PHE A 240 4134 4013 5023 -351 234 286 C ATOM 1769 C PHE A 240 109.957 25.703 236.013 1.00 45.86 C ANISOU 1769 C PHE A 240 5596 5367 6461 -436 210 276 C ATOM 1770 O PHE A 240 109.751 25.004 235.022 1.00 52.87 O ANISOU 1770 O PHE A 240 6534 6226 7327 -433 220 242 O ATOM 1771 CB PHE A 240 110.721 24.286 237.927 1.00 35.60 C ANISOU 1771 CB PHE A 240 4323 4034 5168 -283 245 293 C ATOM 1772 CG PHE A 240 111.868 23.426 238.376 1.00 39.62 C ANISOU 1772 CG PHE A 240 4840 4589 5625 -133 274 290 C ATOM 1773 CD1 PHE A 240 112.310 22.375 237.589 1.00 46.87 C ANISOU 1773 CD1 PHE A 240 5842 5480 6486 -26 302 254 C ATOM 1774 CD2 PHE A 240 112.503 23.664 239.584 1.00 36.96 C ANISOU 1774 CD2 PHE A 240 4434 4332 5279 -78 272 320 C ATOM 1775 CE1 PHE A 240 113.365 21.580 237.995 1.00 36.81 C ANISOU 1775 CE1 PHE A 240 4585 4262 5138 165 328 251 C ATOM 1776 CE2 PHE A 240 113.560 22.873 239.997 1.00 42.78 C ANISOU 1776 CE2 PHE A 240 5165 5144 5944 94 295 320 C ATOM 1777 CZ PHE A 240 113.991 21.829 239.201 1.00 38.37 C ANISOU 1777 CZ PHE A 240 4694 4563 5323 231 323 287 C ATOM 1778 N TRP A 241 109.199 26.750 236.323 1.00 41.17 N ANISOU 1778 N TRP A 241 4988 4763 5890 -496 177 301 N ATOM 1779 CA TRP A 241 108.015 27.081 235.535 1.00 33.50 C ANISOU 1779 CA TRP A 241 4041 3769 4918 -543 148 295 C ATOM 1780 C TRP A 241 108.195 28.317 234.656 1.00 30.26 C ANISOU 1780 C TRP A 241 3642 3393 4464 -579 128 309 C ATOM 1781 O TRP A 241 107.637 28.386 233.560 1.00 55.03 O ANISOU 1781 O TRP A 241 6800 6538 7572 -597 112 297 O ATOM 1782 CB TRP A 241 106.805 27.278 236.451 1.00 36.90 C ANISOU 1782 CB TRP A 241 4460 4182 5379 -545 124 312 C ATOM 1783 CG TRP A 241 106.139 25.997 236.848 1.00 38.12 C ANISOU 1783 CG TRP A 241 4631 4303 5550 -567 139 297 C ATOM 1784 CD1 TRP A 241 106.252 25.348 238.042 1.00 43.43 C ANISOU 1784 CD1 TRP A 241 5317 4937 6247 -550 160 311 C ATOM 1785 CD2 TRP A 241 105.257 25.206 236.043 1.00 50.24 C ANISOU 1785 CD2 TRP A 241 6191 5838 7060 -636 135 265 C ATOM 1786 NE1 TRP A 241 105.492 24.202 238.032 1.00 48.20 N ANISOU 1786 NE1 TRP A 241 5976 5499 6839 -615 172 295 N ATOM 1787 CE2 TRP A 241 104.871 24.092 236.815 1.00 46.93 C ANISOU 1787 CE2 TRP A 241 5820 5365 6645 -680 157 262 C ATOM 1788 CE3 TRP A 241 104.754 25.332 234.744 1.00 56.98 C ANISOU 1788 CE3 TRP A 241 7040 6737 7873 -677 114 238 C ATOM 1789 CZ2 TRP A 241 104.008 23.111 236.333 1.00 45.57 C ANISOU 1789 CZ2 TRP A 241 5703 5178 6433 -795 160 229 C ATOM 1790 CZ3 TRP A 241 103.896 24.357 234.266 1.00 59.82 C ANISOU 1790 CZ3 TRP A 241 7428 7102 8197 -774 113 201 C ATOM 1791 CH2 TRP A 241 103.532 23.261 235.059 1.00 51.53 C ANISOU 1791 CH2 TRP A 241 6437 5994 7147 -846 137 195 C ATOM 1792 N LEU A 242 108.965 29.290 235.135 1.00 35.17 N ANISOU 1792 N LEU A 242 4267 4032 5065 -603 127 335 N ATOM 1793 CA LEU A 242 109.167 30.542 234.401 1.00 40.29 C ANISOU 1793 CA LEU A 242 4979 4681 5650 -663 110 356 C ATOM 1794 C LEU A 242 109.735 30.362 232.983 1.00 41.86 C ANISOU 1794 C LEU A 242 5174 4937 5794 -705 128 343 C ATOM 1795 O LEU A 242 109.272 31.032 232.061 1.00 60.37 O ANISOU 1795 O LEU A 242 7587 7258 8092 -728 105 358 O ATOM 1796 CB LEU A 242 110.070 31.490 235.200 1.00 26.86 C ANISOU 1796 CB LEU A 242 3302 2990 3913 -730 113 379 C ATOM 1797 CG LEU A 242 110.378 32.850 234.567 1.00 41.11 C ANISOU 1797 CG LEU A 242 5228 4764 5628 -833 99 407 C ATOM 1798 CD1 LEU A 242 109.100 33.632 234.311 1.00 35.85 C ANISOU 1798 CD1 LEU A 242 4691 3983 4946 -763 55 428 C ATOM 1799 CD2 LEU A 242 111.329 33.650 235.444 1.00 36.19 C ANISOU 1799 CD2 LEU A 242 4637 4160 4954 -945 105 418 C ATOM 1800 N PRO A 243 110.734 29.473 232.795 1.00 40.30 N ANISOU 1800 N PRO A 243 4903 4824 5586 -694 169 315 N ATOM 1801 CA PRO A 243 111.221 29.303 231.419 1.00 43.86 C ANISOU 1801 CA PRO A 243 5348 5346 5971 -720 189 297 C ATOM 1802 C PRO A 243 110.152 28.828 230.435 1.00 49.24 C ANISOU 1802 C PRO A 243 6074 5974 6663 -692 169 274 C ATOM 1803 O PRO A 243 110.213 29.177 229.257 1.00 53.41 O ANISOU 1803 O PRO A 243 6628 6537 7127 -732 167 275 O ATOM 1804 CB PRO A 243 112.319 28.246 231.566 1.00 28.79 C ANISOU 1804 CB PRO A 243 3352 3544 4043 -651 235 262 C ATOM 1805 CG PRO A 243 112.805 28.411 232.953 1.00 28.11 C ANISOU 1805 CG PRO A 243 3217 3485 3979 -641 237 281 C ATOM 1806 CD PRO A 243 111.586 28.747 233.758 1.00 47.42 C ANISOU 1806 CD PRO A 243 5728 5784 6503 -642 198 303 C ATOM 1807 N TYR A 244 109.188 28.048 230.912 1.00 45.44 N ANISOU 1807 N TYR A 244 5598 5424 6242 -643 155 255 N ATOM 1808 CA TYR A 244 108.134 27.536 230.043 1.00 46.81 C ANISOU 1808 CA TYR A 244 5799 5580 6407 -648 133 225 C ATOM 1809 C TYR A 244 107.116 28.617 229.693 1.00 52.81 C ANISOU 1809 C TYR A 244 6582 6345 7140 -660 83 259 C ATOM 1810 O TYR A 244 106.731 28.764 228.533 1.00 54.25 O ANISOU 1810 O TYR A 244 6783 6562 7266 -674 64 251 O ATOM 1811 CB TYR A 244 107.430 26.345 230.696 1.00 30.86 C ANISOU 1811 CB TYR A 244 3788 3505 4434 -635 137 194 C ATOM 1812 CG TYR A 244 106.230 25.849 229.922 1.00 36.32 C ANISOU 1812 CG TYR A 244 4496 4206 5098 -686 110 160 C ATOM 1813 CD1 TYR A 244 106.369 25.343 228.636 1.00 59.14 C ANISOU 1813 CD1 TYR A 244 7425 7115 7932 -709 117 115 C ATOM 1814 CD2 TYR A 244 104.958 25.881 230.479 1.00 44.60 C ANISOU 1814 CD2 TYR A 244 5510 5276 6159 -719 77 168 C ATOM 1815 CE1 TYR A 244 105.275 24.889 227.924 1.00 67.40 C ANISOU 1815 CE1 TYR A 244 8481 8192 8936 -779 88 78 C ATOM 1816 CE2 TYR A 244 103.858 25.427 229.775 1.00 65.11 C ANISOU 1816 CE2 TYR A 244 8096 7937 8708 -791 50 133 C ATOM 1817 CZ TYR A 244 104.023 24.932 228.498 1.00 74.02 C ANISOU 1817 CZ TYR A 244 9270 9074 9782 -829 54 87 C ATOM 1818 OH TYR A 244 102.931 24.479 227.792 1.00 74.50 O ANISOU 1818 OH TYR A 244 9314 9215 9777 -923 23 45 O ATOM 1819 N HIS A 245 106.685 29.375 230.697 1.00 43.33 N ANISOU 1819 N HIS A 245 5386 5114 5965 -633 60 295 N ATOM 1820 CA HIS A 245 105.671 30.405 230.493 1.00 44.12 C ANISOU 1820 CA HIS A 245 5524 5219 6019 -589 11 327 C ATOM 1821 C HIS A 245 106.225 31.621 229.761 1.00 49.95 C ANISOU 1821 C HIS A 245 6369 5929 6681 -606 2 368 C ATOM 1822 O HIS A 245 105.492 32.321 229.062 1.00 56.02 O ANISOU 1822 O HIS A 245 7201 6706 7379 -554 -38 391 O ATOM 1823 CB HIS A 245 105.066 30.828 231.831 1.00 31.45 C ANISOU 1823 CB HIS A 245 3910 3592 4447 -530 -7 347 C ATOM 1824 CG HIS A 245 104.152 29.802 232.426 1.00 27.33 C ANISOU 1824 CG HIS A 245 3293 3123 3966 -527 -7 317 C ATOM 1825 ND1 HIS A 245 102.810 29.739 232.120 1.00 36.13 N ANISOU 1825 ND1 HIS A 245 4350 4344 5036 -497 -44 306 N ATOM 1826 CD2 HIS A 245 104.389 28.796 233.298 1.00 36.60 C ANISOU 1826 CD2 HIS A 245 4428 4274 5203 -565 25 298 C ATOM 1827 CE1 HIS A 245 102.257 28.738 232.783 1.00 58.12 C ANISOU 1827 CE1 HIS A 245 7059 7171 7851 -550 -31 280 C ATOM 1828 NE2 HIS A 245 103.194 28.149 233.506 1.00 57.21 N ANISOU 1828 NE2 HIS A 245 6974 6957 7804 -588 12 278 N ATOM 1829 N LEU A 246 107.519 31.872 229.923 1.00 45.15 N ANISOU 1829 N LEU A 246 5786 5303 6067 -683 38 380 N ATOM 1830 CA LEU A 246 108.164 32.971 229.218 1.00 37.61 C ANISOU 1830 CA LEU A 246 4946 4324 5018 -755 39 420 C ATOM 1831 C LEU A 246 108.340 32.607 227.748 1.00 38.16 C ANISOU 1831 C LEU A 246 5003 4464 5033 -787 50 407 C ATOM 1832 O LEU A 246 108.441 33.480 226.887 1.00 58.91 O ANISOU 1832 O LEU A 246 7743 7073 7565 -828 39 446 O ATOM 1833 CB LEU A 246 109.510 33.314 229.858 1.00 41.15 C ANISOU 1833 CB LEU A 246 5397 4786 5454 -868 77 431 C ATOM 1834 CG LEU A 246 109.730 34.793 230.188 1.00 56.32 C ANISOU 1834 CG LEU A 246 7498 6608 7295 -945 60 482 C ATOM 1835 CD1 LEU A 246 108.572 35.335 231.010 1.00 63.27 C ANISOU 1835 CD1 LEU A 246 8469 7372 8199 -815 13 495 C ATOM 1836 CD2 LEU A 246 111.043 34.990 230.926 1.00 48.60 C ANISOU 1836 CD2 LEU A 246 6484 5687 6295 -1091 96 480 C ATOM 1837 N THR A 247 108.372 31.307 227.470 1.00 39.48 N ANISOU 1837 N THR A 247 5057 4697 5245 -767 72 351 N ATOM 1838 CA THR A 247 108.430 30.814 226.100 1.00 37.15 C ANISOU 1838 CA THR A 247 4751 4470 4896 -783 82 323 C ATOM 1839 C THR A 247 107.029 30.823 225.495 1.00 45.31 C ANISOU 1839 C THR A 247 5803 5507 5907 -723 28 319 C ATOM 1840 O THR A 247 106.858 31.023 224.294 1.00 47.87 O ANISOU 1840 O THR A 247 6163 5875 6152 -732 14 323 O ATOM 1841 CB THR A 247 109.021 29.393 226.029 1.00 39.03 C ANISOU 1841 CB THR A 247 4902 4760 5167 -769 127 256 C ATOM 1842 OG1 THR A 247 110.244 29.345 226.774 1.00 40.41 O ANISOU 1842 OG1 THR A 247 5028 4973 5353 -785 171 260 O ATOM 1843 CG2 THR A 247 109.300 28.997 224.587 1.00 39.80 C ANISOU 1843 CG2 THR A 247 5004 4932 5187 -786 145 223 C ATOM 1844 N LEU A 248 106.026 30.607 226.341 1.00 50.10 N ANISOU 1844 N LEU A 248 6371 6097 6568 -665 -2 311 N ATOM 1845 CA LEU A 248 104.634 30.702 225.917 1.00 50.16 C ANISOU 1845 CA LEU A 248 6359 6167 6532 -604 -58 308 C ATOM 1846 C LEU A 248 104.273 32.140 225.566 1.00 51.46 C ANISOU 1846 C LEU A 248 6635 6312 6606 -525 -101 375 C ATOM 1847 O LEU A 248 103.439 32.386 224.694 1.00 50.30 O ANISOU 1847 O LEU A 248 6495 6244 6375 -463 -145 382 O ATOM 1848 CB LEU A 248 103.698 30.183 227.010 1.00 52.04 C ANISOU 1848 CB LEU A 248 6512 6432 6829 -573 -73 287 C ATOM 1849 CG LEU A 248 103.386 28.688 227.012 1.00 53.55 C ANISOU 1849 CG LEU A 248 6628 6662 7057 -652 -55 218 C ATOM 1850 CD1 LEU A 248 102.523 28.336 228.210 1.00 56.32 C ANISOU 1850 CD1 LEU A 248 6907 7042 7449 -650 -65 213 C ATOM 1851 CD2 LEU A 248 102.693 28.292 225.719 1.00 53.89 C ANISOU 1851 CD2 LEU A 248 6647 6812 7017 -689 -84 180 C ATOM 1852 N PHE A 249 104.908 33.085 226.252 1.00 44.87 N ANISOU 1852 N PHE A 249 5906 5369 5773 -526 -89 423 N ATOM 1853 CA PHE A 249 104.634 34.499 226.039 1.00 39.22 C ANISOU 1853 CA PHE A 249 5367 4579 4955 -448 -126 489 C ATOM 1854 C PHE A 249 105.083 34.947 224.651 1.00 47.25 C ANISOU 1854 C PHE A 249 6492 5595 5866 -501 -125 522 C ATOM 1855 O PHE A 249 104.373 35.691 223.975 1.00 54.58 O ANISOU 1855 O PHE A 249 7532 6521 6686 -394 -172 563 O ATOM 1856 CB PHE A 249 105.317 35.344 227.117 1.00 49.26 C ANISOU 1856 CB PHE A 249 6763 5714 6240 -482 -109 523 C ATOM 1857 CG PHE A 249 105.018 36.814 227.018 1.00 41.91 C ANISOU 1857 CG PHE A 249 6080 4657 5188 -396 -147 589 C ATOM 1858 CD1 PHE A 249 103.786 37.312 227.411 1.00 32.98 C ANISOU 1858 CD1 PHE A 249 4994 3526 4011 -183 -200 601 C ATOM 1859 CD2 PHE A 249 105.969 37.698 226.539 1.00 34.02 C ANISOU 1859 CD2 PHE A 249 5285 3545 4097 -526 -127 638 C ATOM 1860 CE1 PHE A 249 103.506 38.661 227.324 1.00 40.52 C ANISOU 1860 CE1 PHE A 249 6223 4341 4832 -62 -236 660 C ATOM 1861 CE2 PHE A 249 105.695 39.051 226.449 1.00 47.89 C ANISOU 1861 CE2 PHE A 249 7334 5141 5721 -451 -161 701 C ATOM 1862 CZ PHE A 249 104.462 39.532 226.842 1.00 38.25 C ANISOU 1862 CZ PHE A 249 6185 3891 4456 -199 -217 712 C ATOM 1863 N VAL A 250 106.257 34.489 224.226 1.00 49.06 N ANISOU 1863 N VAL A 250 6685 5844 6111 -652 -70 504 N ATOM 1864 CA VAL A 250 106.779 34.855 222.913 1.00 46.36 C ANISOU 1864 CA VAL A 250 6429 5526 5661 -726 -58 533 C ATOM 1865 C VAL A 250 106.104 34.035 221.818 1.00 50.91 C ANISOU 1865 C VAL A 250 6904 6225 6213 -676 -79 490 C ATOM 1866 O VAL A 250 106.097 34.427 220.651 1.00 67.57 O ANISOU 1866 O VAL A 250 9094 8365 8214 -685 -90 519 O ATOM 1867 CB VAL A 250 108.310 34.669 222.828 1.00 43.99 C ANISOU 1867 CB VAL A 250 6098 5259 5357 -902 12 525 C ATOM 1868 CG1 VAL A 250 108.994 35.387 223.981 1.00 37.23 C ANISOU 1868 CG1 VAL A 250 5316 4314 4515 -983 31 556 C ATOM 1869 CG2 VAL A 250 108.680 33.197 222.824 1.00 57.72 C ANISOU 1869 CG2 VAL A 250 7637 7113 7182 -907 52 442 C ATOM 1870 N ASP A 251 105.534 32.896 222.201 1.00 50.91 N ANISOU 1870 N ASP A 251 6746 6296 6304 -642 -83 420 N ATOM 1871 CA ASP A 251 104.761 32.081 221.272 1.00 49.15 C ANISOU 1871 CA ASP A 251 6436 6191 6048 -621 -109 367 C ATOM 1872 C ASP A 251 103.395 32.712 221.056 1.00 51.67 C ANISOU 1872 C ASP A 251 6772 6574 6287 -486 -185 399 C ATOM 1873 O ASP A 251 102.869 32.721 219.943 1.00 53.04 O ANISOU 1873 O ASP A 251 6943 6850 6361 -456 -220 396 O ATOM 1874 CB ASP A 251 104.615 30.650 221.792 1.00 53.30 C ANISOU 1874 CB ASP A 251 6828 6752 6672 -662 -86 282 C ATOM 1875 CG ASP A 251 103.589 29.849 221.012 1.00 74.26 C ANISOU 1875 CG ASP A 251 9409 9528 9279 -669 -123 222 C ATOM 1876 OD1 ASP A 251 103.921 29.361 219.912 1.00 70.24 O ANISOU 1876 OD1 ASP A 251 8910 9063 8713 -721 -108 183 O ATOM 1877 OD2 ASP A 251 102.449 29.706 221.502 1.00 89.25 O ANISOU 1877 OD2 ASP A 251 11233 11499 11180 -633 -166 210 O ATOM 1878 N THR A 252 102.826 33.241 222.134 1.00 54.09 N ANISOU 1878 N THR A 252 7089 6842 6622 -389 -210 427 N ATOM 1879 CA THR A 252 101.555 33.946 222.063 1.00 57.42 C ANISOU 1879 CA THR A 252 7524 7349 6945 -210 -282 460 C ATOM 1880 C THR A 252 101.730 35.243 221.280 1.00 58.54 C ANISOU 1880 C THR A 252 7885 7408 6951 -122 -307 544 C ATOM 1881 O THR A 252 100.838 35.659 220.541 1.00 49.57 O ANISOU 1881 O THR A 252 6769 6379 5686 23 -366 569 O ATOM 1882 CB THR A 252 100.999 34.255 223.465 1.00 46.23 C ANISOU 1882 CB THR A 252 6079 5910 5576 -106 -295 468 C ATOM 1883 OG1 THR A 252 101.049 33.071 224.271 1.00 36.18 O ANISOU 1883 OG1 THR A 252 4645 4674 4430 -220 -260 402 O ATOM 1884 CG2 THR A 252 99.562 34.747 223.378 1.00 45.52 C ANISOU 1884 CG2 THR A 252 5942 5987 5366 107 -368 483 C ATOM 1885 N LEU A 253 102.891 35.869 221.444 1.00 51.23 N ANISOU 1885 N LEU A 253 7128 6302 6034 -220 -262 588 N ATOM 1886 CA LEU A 253 103.227 37.084 220.709 1.00 50.04 C ANISOU 1886 CA LEU A 253 7234 6035 5742 -196 -274 674 C ATOM 1887 C LEU A 253 103.300 36.818 219.209 1.00 51.03 C ANISOU 1887 C LEU A 253 7347 6265 5777 -242 -279 675 C ATOM 1888 O LEU A 253 102.959 37.681 218.399 1.00 54.33 O ANISOU 1888 O LEU A 253 7941 6658 6043 -141 -318 743 O ATOM 1889 CB LEU A 253 104.553 37.660 221.207 1.00 53.01 C ANISOU 1889 CB LEU A 253 7770 6233 6139 -370 -216 709 C ATOM 1890 CG LEU A 253 104.482 38.924 222.066 1.00 55.11 C ANISOU 1890 CG LEU A 253 8291 6301 6347 -292 -235 771 C ATOM 1891 CD1 LEU A 253 103.491 38.755 223.206 1.00 67.24 C ANISOU 1891 CD1 LEU A 253 9722 7871 7954 -107 -271 737 C ATOM 1892 CD2 LEU A 253 105.861 39.277 222.601 1.00 51.71 C ANISOU 1892 CD2 LEU A 253 7965 5743 5939 -531 -173 787 C ATOM 1893 N LYS A 254 103.751 35.621 218.845 1.00 41.95 N ANISOU 1893 N LYS A 254 6009 5222 4707 -381 -238 600 N ATOM 1894 CA LYS A 254 103.817 35.218 217.446 1.00 40.31 C ANISOU 1894 CA LYS A 254 5769 5129 4416 -428 -238 583 C ATOM 1895 C LYS A 254 102.415 35.052 216.870 1.00 47.61 C ANISOU 1895 C LYS A 254 6611 6219 5260 -272 -316 566 C ATOM 1896 O LYS A 254 102.117 35.544 215.781 1.00 50.32 O ANISOU 1896 O LYS A 254 7042 6618 5459 -206 -352 609 O ATOM 1897 CB LYS A 254 104.607 33.916 217.295 1.00 43.77 C ANISOU 1897 CB LYS A 254 6047 5634 4950 -583 -175 494 C ATOM 1898 CG LYS A 254 104.748 33.440 215.856 1.00 36.48 C ANISOU 1898 CG LYS A 254 5097 4829 3936 -634 -169 463 C ATOM 1899 CD LYS A 254 105.428 32.080 215.773 1.00 46.00 C ANISOU 1899 CD LYS A 254 6167 6090 5222 -740 -109 362 C ATOM 1900 CE LYS A 254 104.422 30.935 215.794 1.00 40.43 C ANISOU 1900 CE LYS A 254 5330 5475 4556 -716 -144 268 C ATOM 1901 NZ LYS A 254 103.689 30.821 217.085 1.00 53.67 N ANISOU 1901 NZ LYS A 254 6943 7117 6331 -666 -170 262 N ATOM 1902 N LEU A 255 101.561 34.354 217.612 1.00 50.10 N ANISOU 1902 N LEU A 255 6748 6635 5650 -223 -341 505 N ATOM 1903 CA LEU A 255 100.175 34.144 217.210 1.00 54.53 C ANISOU 1903 CA LEU A 255 7182 7416 6121 -97 -415 479 C ATOM 1904 C LEU A 255 99.410 35.460 217.163 1.00 43.51 C ANISOU 1904 C LEU A 255 5922 6030 4581 152 -482 569 C ATOM 1905 O LEU A 255 98.504 35.638 216.350 1.00 51.03 O ANISOU 1905 O LEU A 255 6833 7170 5387 287 -548 579 O ATOM 1906 CB LEU A 255 99.480 33.175 218.169 1.00 45.58 C ANISOU 1906 CB LEU A 255 5838 6393 5086 -135 -419 400 C ATOM 1907 CG LEU A 255 100.044 31.757 218.266 1.00 40.20 C ANISOU 1907 CG LEU A 255 5055 5696 4525 -350 -360 306 C ATOM 1908 CD1 LEU A 255 99.322 30.973 219.349 1.00 49.97 C ANISOU 1908 CD1 LEU A 255 6138 7010 5840 -390 -364 249 C ATOM 1909 CD2 LEU A 255 99.936 31.048 216.926 1.00 37.07 C ANISOU 1909 CD2 LEU A 255 4613 5426 4044 -440 -371 248 C ATOM 1910 N LEU A 256 99.789 36.383 218.041 1.00 44.12 N ANISOU 1910 N LEU A 256 6176 5906 4683 222 -467 631 N ATOM 1911 CA LEU A 256 99.112 37.668 218.157 1.00 50.62 C ANISOU 1911 CA LEU A 256 7187 6686 5360 489 -526 714 C ATOM 1912 C LEU A 256 99.567 38.634 217.067 1.00 51.87 C ANISOU 1912 C LEU A 256 7629 6716 5365 524 -535 805 C ATOM 1913 O LEU A 256 99.073 39.759 216.979 1.00 64.36 O ANISOU 1913 O LEU A 256 9436 8226 6790 761 -585 885 O ATOM 1914 CB LEU A 256 99.362 38.270 219.540 1.00 49.23 C ANISOU 1914 CB LEU A 256 7132 6317 5257 538 -504 738 C ATOM 1915 CG LEU A 256 98.222 39.048 220.195 1.00 60.79 C ANISOU 1915 CG LEU A 256 8643 7840 6615 856 -567 767 C ATOM 1916 CD1 LEU A 256 96.928 38.256 220.125 1.00 46.61 C ANISOU 1916 CD1 LEU A 256 6516 6405 4786 964 -618 702 C ATOM 1917 CD2 LEU A 256 98.575 39.362 221.640 1.00 54.90 C ANISOU 1917 CD2 LEU A 256 7973 6913 5971 847 -532 764 C ATOM 1918 N LYS A 257 100.514 38.181 216.248 1.00 51.92 N ANISOU 1918 N LYS A 257 7635 6693 5399 296 -485 793 N ATOM 1919 CA LYS A 257 101.069 38.965 215.144 1.00 45.02 C ANISOU 1919 CA LYS A 257 7013 5716 4378 267 -481 878 C ATOM 1920 C LYS A 257 101.726 40.260 215.619 1.00 48.40 C ANISOU 1920 C LYS A 257 7799 5847 4745 264 -459 975 C ATOM 1921 O LYS A 257 101.837 41.221 214.857 1.00 57.26 O ANISOU 1921 O LYS A 257 9211 6853 5692 317 -477 1069 O ATOM 1922 CB LYS A 257 99.985 39.284 214.108 1.00 49.82 C ANISOU 1922 CB LYS A 257 7637 6498 4796 498 -564 913 C ATOM 1923 CG LYS A 257 99.237 38.066 213.588 1.00 59.83 C ANISOU 1923 CG LYS A 257 8565 8081 6088 481 -595 813 C ATOM 1924 CD LYS A 257 100.171 37.091 212.890 1.00 62.75 C ANISOU 1924 CD LYS A 257 8831 8474 6538 201 -530 749 C ATOM 1925 CE LYS A 257 99.413 35.875 212.379 1.00 69.23 C ANISOU 1925 CE LYS A 257 9364 9576 7364 162 -561 641 C ATOM 1926 NZ LYS A 257 100.312 34.895 211.707 1.00 62.18 N ANISOU 1926 NZ LYS A 257 8402 8690 6534 -78 -497 569 N ATOM 1927 N TRP A 258 102.160 40.285 216.876 1.00 47.81 N ANISOU 1927 N TRP A 258 7725 5643 4798 188 -421 953 N ATOM 1928 CA TRP A 258 102.856 41.449 217.415 1.00 54.82 C ANISOU 1928 CA TRP A 258 8957 6244 5626 131 -397 1030 C ATOM 1929 C TRP A 258 104.309 41.457 216.959 1.00 62.29 C ANISOU 1929 C TRP A 258 9982 7111 6576 -204 -318 1050 C ATOM 1930 O TRP A 258 104.912 42.516 216.790 1.00 64.56 O ANISOU 1930 O TRP A 258 10607 7192 6732 -304 -300 1136 O ATOM 1931 CB TRP A 258 102.783 41.476 218.944 1.00 48.84 C ANISOU 1931 CB TRP A 258 8163 5403 4992 166 -388 993 C ATOM 1932 CG TRP A 258 101.440 41.875 219.481 1.00 43.34 C ANISOU 1932 CG TRP A 258 7485 4747 4235 512 -462 997 C ATOM 1933 CD1 TRP A 258 100.257 41.887 218.804 1.00 44.51 C ANISOU 1933 CD1 TRP A 258 7563 5083 4264 783 -534 1006 C ATOM 1934 CD2 TRP A 258 101.147 42.331 220.808 1.00 43.32 C ANISOU 1934 CD2 TRP A 258 7561 4632 4266 639 -470 989 C ATOM 1935 NE1 TRP A 258 99.243 42.315 219.627 1.00 45.29 N ANISOU 1935 NE1 TRP A 258 7677 5217 4315 1082 -585 1004 N ATOM 1936 CE2 TRP A 258 99.764 42.595 220.862 1.00 44.55 C ANISOU 1936 CE2 TRP A 258 7683 4927 4316 1003 -546 993 C ATOM 1937 CE3 TRP A 258 101.919 42.539 221.956 1.00 42.52 C ANISOU 1937 CE3 TRP A 258 7545 4349 4261 485 -423 975 C ATOM 1938 CZ2 TRP A 258 99.136 43.056 222.018 1.00 45.00 C ANISOU 1938 CZ2 TRP A 258 7794 4943 4360 1227 -570 982 C ATOM 1939 CZ3 TRP A 258 101.293 42.996 223.102 1.00 42.87 C ANISOU 1939 CZ3 TRP A 258 7658 4330 4301 692 -449 964 C ATOM 1940 CH2 TRP A 258 99.917 43.250 223.124 1.00 57.29 C ANISOU 1940 CH2 TRP A 258 9454 6292 6020 1066 -520 967 C ATOM 1941 N ILE A 259 104.865 40.266 216.765 1.00 56.22 N ANISOU 1941 N ILE A 259 8909 6516 5935 -377 -268 969 N ATOM 1942 CA ILE A 259 106.228 40.129 216.269 1.00 57.67 C ANISOU 1942 CA ILE A 259 9099 6707 6107 -668 -190 975 C ATOM 1943 C ILE A 259 106.246 39.314 214.981 1.00 55.23 C ANISOU 1943 C ILE A 259 8619 6600 5767 -700 -181 938 C ATOM 1944 O ILE A 259 105.323 38.545 214.709 1.00 45.49 O ANISOU 1944 O ILE A 259 7193 5515 4576 -548 -225 878 O ATOM 1945 CB ILE A 259 107.152 39.461 217.310 1.00 52.53 C ANISOU 1945 CB ILE A 259 8258 6082 5618 -846 -125 906 C ATOM 1946 CG1 ILE A 259 106.713 38.020 217.575 1.00 48.22 C ANISOU 1946 CG1 ILE A 259 7369 5715 5236 -768 -127 796 C ATOM 1947 CG2 ILE A 259 107.169 40.264 218.603 1.00 57.61 C ANISOU 1947 CG2 ILE A 259 9071 6533 6285 -832 -134 935 C ATOM 1948 CD1 ILE A 259 107.612 37.277 218.540 1.00 51.31 C ANISOU 1948 CD1 ILE A 259 7583 6140 5772 -903 -65 731 C ATOM 1949 N SER A 260 107.293 39.496 214.184 1.00 64.02 N ANISOU 1949 N SER A 260 9805 7733 6788 -912 -123 971 N ATOM 1950 CA SER A 260 107.454 38.728 212.957 1.00 68.62 C ANISOU 1950 CA SER A 260 10234 8510 7330 -956 -103 931 C ATOM 1951 C SER A 260 108.049 37.362 213.270 1.00 62.25 C ANISOU 1951 C SER A 260 9115 7861 6678 -1043 -47 812 C ATOM 1952 O SER A 260 108.652 37.169 214.324 1.00 65.57 O ANISOU 1952 O SER A 260 9461 8244 7207 -1122 -7 782 O ATOM 1953 CB SER A 260 108.339 39.481 211.961 1.00 88.21 C ANISOU 1953 CB SER A 260 12918 10972 9627 -1145 -58 1017 C ATOM 1954 OG SER A 260 109.605 39.775 212.527 1.00103.13 O ANISOU 1954 OG SER A 260 14840 12824 11519 -1400 18 1032 O ATOM 1955 N SER A 261 107.878 36.412 212.356 1.00 63.77 N ANISOU 1955 N SER A 261 9143 8222 6863 -1016 -44 742 N ATOM 1956 CA SER A 261 108.402 35.068 212.565 1.00 72.02 C ANISOU 1956 CA SER A 261 9942 9393 8028 -1064 8 624 C ATOM 1957 C SER A 261 108.834 34.414 211.258 1.00 72.10 C ANISOU 1957 C SER A 261 9876 9571 7947 -1117 44 576 C ATOM 1958 O SER A 261 108.004 34.089 210.410 1.00 80.63 O ANISOU 1958 O SER A 261 10940 10722 8974 -1028 -5 549 O ATOM 1959 CB SER A 261 107.361 34.191 213.264 1.00 61.72 C ANISOU 1959 CB SER A 261 8494 8093 6863 -922 -42 543 C ATOM 1960 OG SER A 261 106.256 33.933 212.415 1.00 66.84 O ANISOU 1960 OG SER A 261 9119 8831 7446 -814 -107 521 O ATOM 1961 N SER A 262 110.140 34.227 211.102 1.00 68.55 N ANISOU 1961 N SER A 262 9369 9213 7466 -1261 129 561 N ATOM 1962 CA SER A 262 110.676 33.506 209.956 1.00 63.68 C ANISOU 1962 CA SER A 262 8659 8776 6759 -1295 177 500 C ATOM 1963 C SER A 262 110.552 32.008 210.200 1.00 62.18 C ANISOU 1963 C SER A 262 8293 8647 6686 -1198 188 360 C ATOM 1964 O SER A 262 110.053 31.585 211.242 1.00 56.70 O ANISOU 1964 O SER A 262 7551 7857 6136 -1126 160 323 O ATOM 1965 CB SER A 262 112.136 33.889 209.707 1.00 71.51 C ANISOU 1965 CB SER A 262 9639 9890 7643 -1477 268 535 C ATOM 1966 OG SER A 262 112.941 33.580 210.832 1.00 74.78 O ANISOU 1966 OG SER A 262 9933 10325 8154 -1518 316 501 O ATOM 1967 N CYS A 263 111.001 31.208 209.240 1.00 71.87 N ANISOU 1967 N CYS A 263 9448 10024 7836 -1196 231 282 N ATOM 1968 CA CYS A 263 110.988 29.759 209.400 1.00 58.34 C ANISOU 1968 CA CYS A 263 7625 8340 6200 -1103 249 145 C ATOM 1969 C CYS A 263 111.929 29.346 210.527 1.00 48.99 C ANISOU 1969 C CYS A 263 6348 7155 5110 -1093 309 115 C ATOM 1970 O CYS A 263 111.568 28.536 211.378 1.00 50.87 O ANISOU 1970 O CYS A 263 6555 7300 5475 -1011 294 51 O ATOM 1971 CB CYS A 263 111.377 29.066 208.093 1.00 59.08 C ANISOU 1971 CB CYS A 263 7693 8592 6162 -1090 288 67 C ATOM 1972 SG CYS A 263 111.463 27.257 208.180 1.00 81.77 S ANISOU 1972 SG CYS A 263 10511 11469 9089 -966 318 -111 S ATOM 1973 N GLU A 264 113.128 29.923 210.535 1.00 60.43 N ANISOU 1973 N GLU A 264 7755 8726 6479 -1188 375 166 N ATOM 1974 CA GLU A 264 114.135 29.601 211.543 1.00 63.88 C ANISOU 1974 CA GLU A 264 8076 9225 6969 -1178 433 141 C ATOM 1975 C GLU A 264 113.658 29.940 212.953 1.00 64.08 C ANISOU 1975 C GLU A 264 8128 9069 7149 -1175 389 182 C ATOM 1976 O GLU A 264 113.945 29.212 213.904 1.00 80.26 O ANISOU 1976 O GLU A 264 10098 11103 9295 -1091 408 128 O ATOM 1977 CB GLU A 264 115.447 30.337 211.252 1.00 70.04 C ANISOU 1977 CB GLU A 264 8791 10219 7602 -1330 507 200 C ATOM 1978 CG GLU A 264 116.082 29.996 209.911 1.00103.55 C ANISOU 1978 CG GLU A 264 12978 14694 11673 -1334 565 157 C ATOM 1979 CD GLU A 264 115.535 30.837 208.772 1.00121.75 C ANISOU 1979 CD GLU A 264 15424 16970 13865 -1442 534 234 C ATOM 1980 OE1 GLU A 264 114.707 31.733 209.039 1.00112.51 O ANISOU 1980 OE1 GLU A 264 14404 15603 12741 -1499 467 325 O ATOM 1981 OE2 GLU A 264 115.936 30.605 207.612 1.00132.97 O ANISOU 1981 OE2 GLU A 264 16813 18571 15138 -1451 576 205 O ATOM 1982 N PHE A 265 112.928 31.043 213.080 1.00 59.09 N ANISOU 1982 N PHE A 265 7623 8302 6526 -1246 332 278 N ATOM 1983 CA PHE A 265 112.436 31.490 214.379 1.00 53.41 C ANISOU 1983 CA PHE A 265 6945 7415 5933 -1235 289 320 C ATOM 1984 C PHE A 265 111.399 30.526 214.949 1.00 54.42 C ANISOU 1984 C PHE A 265 7041 7435 6201 -1092 242 247 C ATOM 1985 O PHE A 265 111.405 30.231 216.144 1.00 53.61 O ANISOU 1985 O PHE A 265 6894 7261 6214 -1053 241 232 O ATOM 1986 CB PHE A 265 111.841 32.896 214.273 1.00 59.56 C ANISOU 1986 CB PHE A 265 7906 8067 6656 -1304 238 435 C ATOM 1987 CG PHE A 265 111.258 33.407 215.561 1.00 55.38 C ANISOU 1987 CG PHE A 265 7439 7365 6237 -1267 192 473 C ATOM 1988 CD1 PHE A 265 112.082 33.827 216.593 1.00 47.61 C ANISOU 1988 CD1 PHE A 265 6444 6364 5283 -1364 226 500 C ATOM 1989 CD2 PHE A 265 109.885 33.474 215.738 1.00 52.54 C ANISOU 1989 CD2 PHE A 265 7138 6891 5935 -1135 114 479 C ATOM 1990 CE1 PHE A 265 111.547 34.297 217.779 1.00 41.05 C ANISOU 1990 CE1 PHE A 265 5680 5372 4544 -1324 185 529 C ATOM 1991 CE2 PHE A 265 109.345 33.944 216.921 1.00 43.45 C ANISOU 1991 CE2 PHE A 265 6037 5602 4869 -1082 76 510 C ATOM 1992 CZ PHE A 265 110.177 34.357 217.942 1.00 41.93 C ANISOU 1992 CZ PHE A 265 5854 5363 4713 -1174 112 534 C ATOM 1993 N GLU A 266 110.512 30.039 214.087 1.00 36.70 N ANISOU 1993 N GLU A 266 4821 5193 3929 -1034 202 204 N ATOM 1994 CA GLU A 266 109.476 29.102 214.502 1.00 36.01 C ANISOU 1994 CA GLU A 266 4710 5031 3941 -949 158 131 C ATOM 1995 C GLU A 266 110.082 27.773 214.938 1.00 59.86 C ANISOU 1995 C GLU A 266 7666 8059 7020 -896 210 30 C ATOM 1996 O GLU A 266 109.507 27.060 215.758 1.00 58.04 O ANISOU 1996 O GLU A 266 7431 7731 6889 -854 190 -14 O ATOM 1997 CB GLU A 266 108.470 28.877 213.371 1.00 60.99 C ANISOU 1997 CB GLU A 266 7907 8240 7028 -933 105 100 C ATOM 1998 CG GLU A 266 107.725 30.130 212.948 1.00 79.47 C ANISOU 1998 CG GLU A 266 10326 10575 9293 -931 42 200 C ATOM 1999 CD GLU A 266 106.781 29.884 211.788 1.00106.25 C ANISOU 1999 CD GLU A 266 13726 14058 12586 -906 -13 167 C ATOM 2000 OE1 GLU A 266 106.481 28.705 211.502 1.00112.01 O ANISOU 2000 OE1 GLU A 266 14403 14831 13327 -911 -13 58 O ATOM 2001 OE2 GLU A 266 106.343 30.870 211.161 1.00117.69 O ANISOU 2001 OE2 GLU A 266 15252 15533 13930 -881 -58 250 O ATOM 2002 N ARG A 267 111.248 27.445 214.390 1.00 62.02 N ANISOU 2002 N ARG A 267 7899 8454 7210 -889 280 -4 N ATOM 2003 CA ARG A 267 111.933 26.206 214.740 1.00 36.78 C ANISOU 2003 CA ARG A 267 4666 5275 4033 -787 333 -98 C ATOM 2004 C ARG A 267 112.605 26.314 216.101 1.00 54.37 C ANISOU 2004 C ARG A 267 6829 7484 6346 -761 360 -67 C ATOM 2005 O ARG A 267 112.583 25.369 216.888 1.00 53.36 O ANISOU 2005 O ARG A 267 6711 7273 6291 -665 368 -123 O ATOM 2006 CB ARG A 267 112.958 25.846 213.666 1.00 38.11 C ANISOU 2006 CB ARG A 267 4799 5625 4057 -749 399 -149 C ATOM 2007 CG ARG A 267 112.338 25.688 212.294 1.00 61.19 C ANISOU 2007 CG ARG A 267 7789 8575 6885 -774 374 -187 C ATOM 2008 CD ARG A 267 113.382 25.562 211.199 1.00 56.15 C ANISOU 2008 CD ARG A 267 7106 8144 6085 -749 443 -221 C ATOM 2009 NE ARG A 267 113.736 24.173 210.919 1.00 56.77 N ANISOU 2009 NE ARG A 267 7218 8234 6116 -595 484 -353 N ATOM 2010 CZ ARG A 267 114.891 23.612 211.261 1.00 63.23 C ANISOU 2010 CZ ARG A 267 7968 9167 6888 -459 556 -399 C ATOM 2011 NH1 ARG A 267 115.814 24.321 211.897 1.00 64.74 N ANISOU 2011 NH1 ARG A 267 8020 9503 7076 -492 594 -325 N ATOM 2012 NH2 ARG A 267 115.125 22.343 210.960 1.00 78.15 N ANISOU 2012 NH2 ARG A 267 9941 11037 8717 -286 589 -522 N ATOM 2013 N SER A 268 113.200 27.470 216.373 1.00 53.72 N ANISOU 2013 N SER A 268 6699 7476 6238 -858 372 22 N ATOM 2014 CA SER A 268 113.815 27.720 217.668 1.00 42.67 C ANISOU 2014 CA SER A 268 5232 6077 4903 -863 390 56 C ATOM 2015 C SER A 268 112.748 27.775 218.756 1.00 39.93 C ANISOU 2015 C SER A 268 4941 5528 4701 -846 331 78 C ATOM 2016 O SER A 268 112.936 27.250 219.853 1.00 48.70 O ANISOU 2016 O SER A 268 6016 6592 5894 -779 340 58 O ATOM 2017 CB SER A 268 114.618 29.020 217.638 1.00 42.99 C ANISOU 2017 CB SER A 268 5240 6237 4858 -1023 413 145 C ATOM 2018 OG SER A 268 115.628 28.967 216.644 1.00 71.14 O ANISOU 2018 OG SER A 268 8729 10033 8270 -1058 475 127 O ATOM 2019 N LEU A 269 111.623 28.406 218.436 1.00 45.02 N ANISOU 2019 N LEU A 269 5670 6075 5362 -894 269 119 N ATOM 2020 CA LEU A 269 110.512 28.537 219.373 1.00 35.19 C ANISOU 2020 CA LEU A 269 4460 4682 4228 -871 211 140 C ATOM 2021 C LEU A 269 109.848 27.185 219.624 1.00 38.13 C ANISOU 2021 C LEU A 269 4831 4989 4666 -798 201 55 C ATOM 2022 O LEU A 269 109.371 26.911 220.725 1.00 46.86 O ANISOU 2022 O LEU A 269 5932 6004 5868 -774 183 54 O ATOM 2023 CB LEU A 269 109.494 29.552 218.843 1.00 37.41 C ANISOU 2023 CB LEU A 269 4823 4923 4469 -903 148 203 C ATOM 2024 CG LEU A 269 108.333 29.972 219.746 1.00 57.65 C ANISOU 2024 CG LEU A 269 7413 7384 7109 -860 86 237 C ATOM 2025 CD1 LEU A 269 108.038 31.450 219.560 1.00 70.55 C ANISOU 2025 CD1 LEU A 269 9158 8976 8672 -873 48 333 C ATOM 2026 CD2 LEU A 269 107.096 29.149 219.440 1.00 83.08 C ANISOU 2026 CD2 LEU A 269 10605 10617 10344 -818 41 178 C ATOM 2027 N LYS A 270 109.822 26.347 218.592 1.00 43.06 N ANISOU 2027 N LYS A 270 5481 5657 5225 -778 214 -19 N ATOM 2028 CA LYS A 270 109.270 25.002 218.701 1.00 33.71 C ANISOU 2028 CA LYS A 270 4347 4391 4069 -741 210 -109 C ATOM 2029 C LYS A 270 110.095 24.162 219.667 1.00 49.73 C ANISOU 2029 C LYS A 270 6381 6368 6146 -651 261 -143 C ATOM 2030 O LYS A 270 109.556 23.532 220.578 1.00 52.33 O ANISOU 2030 O LYS A 270 6754 6578 6551 -642 247 -161 O ATOM 2031 CB LYS A 270 109.229 24.325 217.331 1.00 49.07 C ANISOU 2031 CB LYS A 270 6349 6390 5908 -741 219 -187 C ATOM 2032 CG LYS A 270 108.490 22.997 217.300 1.00 55.43 C ANISOU 2032 CG LYS A 270 7257 7090 6714 -752 206 -286 C ATOM 2033 CD LYS A 270 107.027 23.190 216.938 1.00 68.62 C ANISOU 2033 CD LYS A 270 8925 8776 8372 -865 132 -285 C ATOM 2034 CE LYS A 270 106.374 21.871 216.556 1.00 71.37 C ANISOU 2034 CE LYS A 270 9390 9057 8669 -934 122 -397 C ATOM 2035 NZ LYS A 270 105.009 22.070 215.995 1.00 65.55 N ANISOU 2035 NZ LYS A 270 8615 8414 7879 -1060 48 -406 N ATOM 2036 N ARG A 271 111.408 24.163 219.457 1.00 57.17 N ANISOU 2036 N ARG A 271 7273 7424 7026 -580 319 -149 N ATOM 2037 CA ARG A 271 112.327 23.399 220.290 1.00 49.82 C ANISOU 2037 CA ARG A 271 6332 6492 6107 -450 368 -179 C ATOM 2038 C ARG A 271 112.308 23.900 221.729 1.00 52.45 C ANISOU 2038 C ARG A 271 6609 6775 6545 -468 352 -112 C ATOM 2039 O ARG A 271 112.332 23.108 222.670 1.00 45.90 O ANISOU 2039 O ARG A 271 5823 5850 5766 -383 361 -134 O ATOM 2040 CB ARG A 271 113.747 23.474 219.728 1.00 47.02 C ANISOU 2040 CB ARG A 271 5883 6350 5634 -370 432 -193 C ATOM 2041 CG ARG A 271 114.727 22.521 220.391 1.00 52.26 C ANISOU 2041 CG ARG A 271 6535 7056 6264 -174 482 -240 C ATOM 2042 CD ARG A 271 116.153 22.806 219.952 1.00 55.00 C ANISOU 2042 CD ARG A 271 6726 7697 6476 -105 543 -241 C ATOM 2043 NE ARG A 271 116.299 22.787 218.499 1.00 38.41 N ANISOU 2043 NE ARG A 271 4632 5707 4255 -119 566 -283 N ATOM 2044 CZ ARG A 271 116.670 21.719 217.800 1.00 50.84 C ANISOU 2044 CZ ARG A 271 6279 7315 5723 62 605 -379 C ATOM 2045 NH1 ARG A 271 116.933 20.577 218.419 1.00 55.33 N ANISOU 2045 NH1 ARG A 271 6945 7794 6284 281 625 -440 N ATOM 2046 NH2 ARG A 271 116.779 21.794 216.480 1.00 40.68 N ANISOU 2046 NH2 ARG A 271 4992 6142 4323 36 625 -414 N ATOM 2047 N ALA A 272 112.261 25.219 221.889 1.00 50.87 N ANISOU 2047 N ALA A 272 6340 6626 6363 -578 329 -30 N ATOM 2048 CA ALA A 272 112.243 25.834 223.211 1.00 38.13 C ANISOU 2048 CA ALA A 272 4685 4968 4834 -606 313 31 C ATOM 2049 C ALA A 272 110.988 25.444 223.982 1.00 43.03 C ANISOU 2049 C ALA A 272 5371 5420 5558 -607 268 27 C ATOM 2050 O ALA A 272 111.045 25.187 225.183 1.00 57.88 O ANISOU 2050 O ALA A 272 7242 7243 7508 -567 270 38 O ATOM 2051 CB ALA A 272 112.343 27.346 223.094 1.00 31.76 C ANISOU 2051 CB ALA A 272 3854 4214 4001 -734 294 112 C ATOM 2052 N LEU A 273 109.857 25.399 223.286 1.00 40.67 N ANISOU 2052 N LEU A 273 5126 5072 5254 -659 226 12 N ATOM 2053 CA LEU A 273 108.594 25.012 223.905 1.00 37.47 C ANISOU 2053 CA LEU A 273 4756 4565 4916 -688 185 3 C ATOM 2054 C LEU A 273 108.625 23.564 224.381 1.00 33.42 C ANISOU 2054 C LEU A 273 4322 3953 4421 -644 212 -62 C ATOM 2055 O LEU A 273 108.130 23.251 225.460 1.00 42.33 O ANISOU 2055 O LEU A 273 5467 5000 5616 -655 202 -50 O ATOM 2056 CB LEU A 273 107.431 25.220 222.933 1.00 39.03 C ANISOU 2056 CB LEU A 273 4969 4794 5068 -756 134 -8 C ATOM 2057 CG LEU A 273 106.836 26.627 222.880 1.00 45.56 C ANISOU 2057 CG LEU A 273 5758 5667 5884 -774 85 69 C ATOM 2058 CD1 LEU A 273 105.776 26.719 221.798 1.00 50.82 C ANISOU 2058 CD1 LEU A 273 6427 6406 6475 -807 35 52 C ATOM 2059 CD2 LEU A 273 106.252 27.004 224.232 1.00 56.11 C ANISOU 2059 CD2 LEU A 273 7064 6954 7300 -759 61 110 C ATOM 2060 N ILE A 274 109.211 22.687 223.573 1.00 36.16 N ANISOU 2060 N ILE A 274 4741 4301 4695 -588 248 -130 N ATOM 2061 CA ILE A 274 109.282 21.269 223.907 1.00 39.28 C ANISOU 2061 CA ILE A 274 5280 4566 5078 -527 275 -196 C ATOM 2062 C ILE A 274 110.199 21.014 225.100 1.00 38.90 C ANISOU 2062 C ILE A 274 5223 4493 5066 -396 311 -170 C ATOM 2063 O ILE A 274 109.833 20.299 226.032 1.00 41.27 O ANISOU 2063 O ILE A 274 5618 4657 5404 -388 311 -173 O ATOM 2064 CB ILE A 274 109.770 20.434 222.705 1.00 40.93 C ANISOU 2064 CB ILE A 274 5597 4779 5176 -460 308 -282 C ATOM 2065 CG1 ILE A 274 108.762 20.517 221.557 1.00 34.56 C ANISOU 2065 CG1 ILE A 274 4816 3993 4321 -600 267 -318 C ATOM 2066 CG2 ILE A 274 109.991 18.985 223.111 1.00 35.35 C ANISOU 2066 CG2 ILE A 274 5096 3903 4432 -359 341 -348 C ATOM 2067 CD1 ILE A 274 109.138 19.682 220.352 1.00 35.96 C ANISOU 2067 CD1 ILE A 274 5118 4164 4380 -549 295 -412 C ATOM 2068 N LEU A 275 111.387 21.610 225.069 1.00 35.89 N ANISOU 2068 N LEU A 275 4722 4261 4656 -307 342 -143 N ATOM 2069 CA LEU A 275 112.379 21.406 226.120 1.00 32.84 C ANISOU 2069 CA LEU A 275 4292 3911 4274 -169 374 -122 C ATOM 2070 C LEU A 275 111.941 21.988 227.462 1.00 40.05 C ANISOU 2070 C LEU A 275 5150 4777 5292 -236 345 -53 C ATOM 2071 O LEU A 275 111.971 21.301 228.483 1.00 37.43 O ANISOU 2071 O LEU A 275 4883 4351 4989 -159 353 -50 O ATOM 2072 CB LEU A 275 113.720 22.015 225.706 1.00 33.32 C ANISOU 2072 CB LEU A 275 4198 4209 4252 -103 410 -110 C ATOM 2073 CG LEU A 275 114.404 21.376 224.495 1.00 46.04 C ANISOU 2073 CG LEU A 275 5841 5917 5735 13 452 -182 C ATOM 2074 CD1 LEU A 275 115.707 22.091 224.177 1.00 35.33 C ANISOU 2074 CD1 LEU A 275 4290 4853 4282 43 491 -161 C ATOM 2075 CD2 LEU A 275 114.645 19.893 224.734 1.00 35.95 C ANISOU 2075 CD2 LEU A 275 4736 4518 4405 225 481 -250 C ATOM 2076 N THR A 276 111.534 23.254 227.454 1.00 39.31 N ANISOU 2076 N THR A 276 4956 4738 5240 -366 311 2 N ATOM 2077 CA THR A 276 111.154 23.946 228.683 1.00 36.69 C ANISOU 2077 CA THR A 276 4574 4373 4991 -417 284 62 C ATOM 2078 C THR A 276 109.907 23.344 229.325 1.00 44.88 C ANISOU 2078 C THR A 276 5697 5261 6093 -458 258 57 C ATOM 2079 O THR A 276 109.717 23.443 230.538 1.00 55.65 O ANISOU 2079 O THR A 276 7044 6584 7515 -454 250 92 O ATOM 2080 CB THR A 276 110.908 25.444 228.433 1.00 32.75 C ANISOU 2080 CB THR A 276 4008 3937 4498 -530 253 117 C ATOM 2081 OG1 THR A 276 109.977 25.605 227.356 1.00 37.67 O ANISOU 2081 OG1 THR A 276 4675 4537 5100 -594 223 103 O ATOM 2082 CG2 THR A 276 112.211 26.146 228.082 1.00 29.71 C ANISOU 2082 CG2 THR A 276 3539 3711 4038 -543 283 135 C ATOM 2083 N GLU A 277 109.061 22.723 228.510 1.00 34.58 N ANISOU 2083 N GLU A 277 4479 3896 4764 -516 245 11 N ATOM 2084 CA GLU A 277 107.858 22.071 229.013 1.00 38.11 C ANISOU 2084 CA GLU A 277 5003 4238 5241 -600 223 -1 C ATOM 2085 C GLU A 277 108.217 20.853 229.856 1.00 46.46 C ANISOU 2085 C GLU A 277 6192 5164 6295 -529 258 -19 C ATOM 2086 O GLU A 277 107.619 20.612 230.906 1.00 44.35 O ANISOU 2086 O GLU A 277 5951 4831 6070 -578 251 7 O ATOM 2087 CB GLU A 277 106.947 21.660 227.857 1.00 38.54 C ANISOU 2087 CB GLU A 277 5115 4289 5238 -708 201 -55 C ATOM 2088 CG GLU A 277 105.650 21.001 228.284 1.00 45.50 C ANISOU 2088 CG GLU A 277 6055 5112 6119 -848 179 -72 C ATOM 2089 CD GLU A 277 104.819 20.546 227.103 1.00 60.05 C ANISOU 2089 CD GLU A 277 7950 6984 7882 -977 155 -136 C ATOM 2090 OE1 GLU A 277 105.075 19.437 226.586 1.00 43.22 O ANISOU 2090 OE1 GLU A 277 5993 4741 5687 -991 181 -203 O ATOM 2091 OE2 GLU A 277 103.913 21.298 226.687 1.00 77.13 O ANISOU 2091 OE2 GLU A 277 9990 9287 10031 -1052 108 -121 O ATOM 2092 N SER A 278 109.200 20.090 229.387 1.00 38.77 N ANISOU 2092 N SER A 278 5313 4162 5256 -399 297 -63 N ATOM 2093 CA SER A 278 109.653 18.896 230.091 1.00 47.26 C ANISOU 2093 CA SER A 278 6560 5098 6299 -278 331 -80 C ATOM 2094 C SER A 278 110.358 19.267 231.390 1.00 42.35 C ANISOU 2094 C SER A 278 5841 4528 5721 -168 340 -18 C ATOM 2095 O SER A 278 110.358 18.497 232.350 1.00 45.15 O ANISOU 2095 O SER A 278 6320 4762 6073 -109 353 -4 O ATOM 2096 CB SER A 278 110.585 18.071 229.201 1.00 54.27 C ANISOU 2096 CB SER A 278 7572 5969 7080 -111 370 -147 C ATOM 2097 OG SER A 278 109.931 17.666 228.011 1.00 68.26 O ANISOU 2097 OG SER A 278 9453 7682 8800 -220 361 -212 O ATOM 2098 N LEU A 279 110.961 20.450 231.408 1.00 36.13 N ANISOU 2098 N LEU A 279 4849 3919 4959 -157 333 19 N ATOM 2099 CA LEU A 279 111.626 20.959 232.601 1.00 47.95 C ANISOU 2099 CA LEU A 279 6233 5497 6487 -89 335 73 C ATOM 2100 C LEU A 279 110.622 21.225 233.719 1.00 49.14 C ANISOU 2100 C LEU A 279 6384 5563 6722 -198 307 119 C ATOM 2101 O LEU A 279 110.889 20.947 234.889 1.00 42.39 O ANISOU 2101 O LEU A 279 5544 4682 5881 -127 315 150 O ATOM 2102 CB LEU A 279 112.397 22.238 232.278 1.00 45.33 C ANISOU 2102 CB LEU A 279 5710 5369 6144 -118 331 97 C ATOM 2103 CG LEU A 279 113.008 22.965 233.476 1.00 36.74 C ANISOU 2103 CG LEU A 279 4498 4385 5078 -105 326 147 C ATOM 2104 CD1 LEU A 279 114.125 22.137 234.089 1.00 35.80 C ANISOU 2104 CD1 LEU A 279 4372 4342 4890 95 358 139 C ATOM 2105 CD2 LEU A 279 113.505 24.345 233.076 1.00 42.43 C ANISOU 2105 CD2 LEU A 279 5079 5267 5777 -217 317 171 C ATOM 2106 N ALA A 280 109.466 21.764 233.345 1.00 41.05 N ANISOU 2106 N ALA A 280 5336 4523 5738 -354 274 122 N ATOM 2107 CA ALA A 280 108.429 22.110 234.309 1.00 28.59 C ANISOU 2107 CA ALA A 280 3730 2913 4219 -450 248 160 C ATOM 2108 C ALA A 280 107.789 20.868 234.919 1.00 44.14 C ANISOU 2108 C ALA A 280 5851 4742 6179 -486 262 151 C ATOM 2109 O ALA A 280 107.184 20.935 235.988 1.00 59.45 O ANISOU 2109 O ALA A 280 7773 6663 8151 -538 254 188 O ATOM 2110 CB ALA A 280 107.371 22.981 233.652 1.00 29.53 C ANISOU 2110 CB ALA A 280 3776 3094 4351 -569 208 162 C ATOM 2111 N PHE A 281 107.926 19.737 234.234 1.00 42.24 N ANISOU 2111 N PHE A 281 5780 4394 5875 -468 284 102 N ATOM 2112 CA PHE A 281 107.351 18.481 234.707 1.00 39.09 C ANISOU 2112 CA PHE A 281 5592 3823 5438 -531 301 91 C ATOM 2113 C PHE A 281 108.136 17.922 235.887 1.00 50.43 C ANISOU 2113 C PHE A 281 7121 5177 6864 -376 329 129 C ATOM 2114 O PHE A 281 107.657 17.044 236.603 1.00 59.59 O ANISOU 2114 O PHE A 281 8457 6189 7994 -433 342 144 O ATOM 2115 CB PHE A 281 107.305 17.447 233.581 1.00 37.91 C ANISOU 2115 CB PHE A 281 5648 3553 5202 -556 317 18 C ATOM 2116 CG PHE A 281 106.353 17.792 232.472 1.00 46.54 C ANISOU 2116 CG PHE A 281 6675 4723 6284 -736 286 -22 C ATOM 2117 CD1 PHE A 281 105.438 18.823 232.616 1.00 48.10 C ANISOU 2117 CD1 PHE A 281 6667 5075 6534 -858 247 10 C ATOM 2118 CD2 PHE A 281 106.367 17.076 231.287 1.00 48.22 C ANISOU 2118 CD2 PHE A 281 7041 4865 6416 -763 295 -96 C ATOM 2119 CE1 PHE A 281 104.562 19.137 231.597 1.00 44.75 C ANISOU 2119 CE1 PHE A 281 6174 4751 6078 -994 214 -24 C ATOM 2120 CE2 PHE A 281 105.493 17.385 230.264 1.00 44.85 C ANISOU 2120 CE2 PHE A 281 6544 4532 5965 -928 262 -134 C ATOM 2121 CZ PHE A 281 104.590 18.417 230.419 1.00 34.65 C ANISOU 2121 CZ PHE A 281 5029 3413 4721 -1039 220 -95 C ATOM 2122 N CYS A 282 109.347 18.431 236.080 1.00 34.26 N ANISOU 2122 N CYS A 282 4955 3240 4822 -190 336 146 N ATOM 2123 CA CYS A 282 110.206 17.968 237.161 1.00 48.31 C ANISOU 2123 CA CYS A 282 6789 4993 6573 -8 357 182 C ATOM 2124 C CYS A 282 109.782 18.560 238.501 1.00 55.85 C ANISOU 2124 C CYS A 282 7637 5988 7595 -77 340 245 C ATOM 2125 O CYS A 282 110.186 18.077 239.558 1.00 65.25 O ANISOU 2125 O CYS A 282 8899 7133 8761 34 353 283 O ATOM 2126 CB CYS A 282 111.666 18.319 236.869 1.00 46.05 C ANISOU 2126 CB CYS A 282 6374 4879 6243 202 369 172 C ATOM 2127 SG CYS A 282 112.315 17.599 235.343 1.00 47.49 S ANISOU 2127 SG CYS A 282 6670 5051 6322 335 397 94 S ATOM 2128 N HIS A 283 108.962 19.604 238.448 1.00 52.24 N ANISOU 2128 N HIS A 283 7021 5620 7208 -239 311 256 N ATOM 2129 CA HIS A 283 108.549 20.315 239.653 1.00 51.74 C ANISOU 2129 CA HIS A 283 6846 5615 7199 -289 294 306 C ATOM 2130 C HIS A 283 107.666 19.463 240.562 1.00 60.42 C ANISOU 2130 C HIS A 283 8080 6591 8284 -377 306 334 C ATOM 2131 O HIS A 283 107.703 19.608 241.783 1.00 75.04 O ANISOU 2131 O HIS A 283 9901 8461 10150 -348 307 380 O ATOM 2132 CB HIS A 283 107.817 21.606 239.283 1.00 49.81 C ANISOU 2132 CB HIS A 283 6437 5484 7006 -407 260 305 C ATOM 2133 CG HIS A 283 107.366 22.401 240.468 1.00 47.81 C ANISOU 2133 CG HIS A 283 6084 5291 6792 -437 243 346 C ATOM 2134 ND1 HIS A 283 106.038 22.531 240.816 1.00 55.54 N ANISOU 2134 ND1 HIS A 283 7036 6285 7780 -554 230 356 N ATOM 2135 CD2 HIS A 283 108.066 23.100 241.392 1.00 37.76 C ANISOU 2135 CD2 HIS A 283 4728 4084 5535 -363 238 375 C ATOM 2136 CE1 HIS A 283 105.941 23.280 241.899 1.00 54.03 C ANISOU 2136 CE1 HIS A 283 6761 6156 7613 -529 220 388 C ATOM 2137 NE2 HIS A 283 107.157 23.638 242.269 1.00 46.05 N ANISOU 2137 NE2 HIS A 283 5726 5162 6609 -423 223 400 N ATOM 2138 N CYS A 284 106.877 18.574 239.967 1.00 54.62 N ANISOU 2138 N CYS A 284 7506 5741 7508 -504 316 304 N ATOM 2139 CA CYS A 284 105.981 17.723 240.744 1.00 59.56 C ANISOU 2139 CA CYS A 284 8281 6256 8094 -645 332 330 C ATOM 2140 C CYS A 284 106.759 16.633 241.478 1.00 51.00 C ANISOU 2140 C CYS A 284 7433 4999 6948 -502 365 360 C ATOM 2141 O CYS A 284 106.228 15.975 242.372 1.00 57.20 O ANISOU 2141 O CYS A 284 8360 5682 7693 -593 382 400 O ATOM 2142 CB CYS A 284 104.913 17.097 239.846 1.00 74.17 C ANISOU 2142 CB CYS A 284 10241 8049 9891 -868 332 284 C ATOM 2143 SG CYS A 284 105.543 15.903 238.651 1.00 84.97 S ANISOU 2143 SG CYS A 284 11898 9215 11173 -806 355 219 S ATOM 2144 N CYS A 285 108.018 16.447 241.093 1.00 38.01 N ANISOU 2144 N CYS A 285 5830 3337 5277 -268 373 343 N ATOM 2145 CA CYS A 285 108.902 15.516 241.786 1.00 50.96 C ANISOU 2145 CA CYS A 285 7673 4850 6837 -54 398 373 C ATOM 2146 C CYS A 285 109.516 16.178 243.013 1.00 48.97 C ANISOU 2146 C CYS A 285 7245 4742 6620 74 388 431 C ATOM 2147 O CYS A 285 109.961 15.503 243.941 1.00 48.72 O ANISOU 2147 O CYS A 285 7359 4627 6524 215 402 477 O ATOM 2148 CB CYS A 285 110.006 15.017 240.851 1.00 45.05 C ANISOU 2148 CB CYS A 285 7026 4075 6018 180 412 324 C ATOM 2149 SG CYS A 285 109.420 14.084 239.423 1.00 57.71 S ANISOU 2149 SG CYS A 285 8896 5479 7551 58 427 245 S ATOM 2150 N LEU A 286 109.535 17.507 243.006 1.00 40.30 N ANISOU 2150 N LEU A 286 5854 3850 5607 24 360 428 N ATOM 2151 CA LEU A 286 110.134 18.278 244.089 1.00 47.04 C ANISOU 2151 CA LEU A 286 6530 4856 6486 115 346 470 C ATOM 2152 C LEU A 286 109.113 18.626 245.169 1.00 50.02 C ANISOU 2152 C LEU A 286 6866 5233 6908 -41 339 513 C ATOM 2153 O LEU A 286 109.482 18.981 246.288 1.00 54.15 O ANISOU 2153 O LEU A 286 7309 5834 7431 28 332 553 O ATOM 2154 CB LEU A 286 110.775 19.557 243.542 1.00 51.31 C ANISOU 2154 CB LEU A 286 6821 5605 7070 130 323 441 C ATOM 2155 CG LEU A 286 112.237 19.484 243.087 1.00 54.25 C ANISOU 2155 CG LEU A 286 7134 6105 7374 335 330 419 C ATOM 2156 CD1 LEU A 286 113.134 19.055 244.240 1.00 71.55 C ANISOU 2156 CD1 LEU A 286 9334 8358 9493 534 334 460 C ATOM 2157 CD2 LEU A 286 112.410 18.554 241.895 1.00 35.90 C ANISOU 2157 CD2 LEU A 286 4971 3677 4991 414 353 373 C ATOM 2158 N ASN A 287 107.832 18.525 244.826 1.00 45.37 N ANISOU 2158 N ASN A 287 6315 4584 6338 -252 340 501 N ATOM 2159 CA ASN A 287 106.755 18.794 245.777 1.00 44.46 C ANISOU 2159 CA ASN A 287 6146 4506 6240 -404 339 537 C ATOM 2160 C ASN A 287 106.824 17.976 247.077 1.00 36.69 C ANISOU 2160 C ASN A 287 5314 3428 5199 -368 363 599 C ATOM 2161 O ASN A 287 106.532 18.512 248.146 1.00 40.18 O ANISOU 2161 O ASN A 287 5644 3963 5657 -390 358 635 O ATOM 2162 CB ASN A 287 105.394 18.576 245.107 1.00 42.68 C ANISOU 2162 CB ASN A 287 5944 4267 6004 -637 341 510 C ATOM 2163 CG ASN A 287 104.990 19.736 244.219 1.00 40.63 C ANISOU 2163 CG ASN A 287 5477 4161 5801 -680 308 467 C ATOM 2164 OD1 ASN A 287 105.343 20.885 244.483 1.00 29.57 O ANISOU 2164 OD1 ASN A 287 3909 2877 4449 -594 285 471 O ATOM 2165 ND2 ASN A 287 104.242 19.442 243.163 1.00 54.94 N ANISOU 2165 ND2 ASN A 287 7320 5966 7589 -820 304 426 N ATOM 2166 N PRO A 288 107.193 16.680 247.000 1.00 47.38 N ANISOU 2166 N PRO A 288 6944 4587 6470 -303 390 614 N ATOM 2167 CA PRO A 288 107.376 15.966 248.271 1.00 40.59 C ANISOU 2167 CA PRO A 288 6248 3633 5542 -235 410 684 C ATOM 2168 C PRO A 288 108.477 16.558 249.151 1.00 33.39 C ANISOU 2168 C PRO A 288 5186 2860 4641 -4 392 714 C ATOM 2169 O PRO A 288 108.387 16.484 250.376 1.00 39.27 O ANISOU 2169 O PRO A 288 5947 3618 5358 8 397 772 O ATOM 2170 CB PRO A 288 107.750 14.551 247.822 1.00 35.91 C ANISOU 2170 CB PRO A 288 6014 2787 4842 -152 438 685 C ATOM 2171 CG PRO A 288 107.103 14.403 246.501 1.00 42.98 C ANISOU 2171 CG PRO A 288 6952 3628 5749 -328 439 618 C ATOM 2172 CD PRO A 288 107.220 15.751 245.854 1.00 41.89 C ANISOU 2172 CD PRO A 288 6470 3725 5722 -319 405 570 C ATOM 2173 N LEU A 289 109.500 17.139 248.533 1.00 40.85 N ANISOU 2173 N LEU A 289 5981 3928 5611 157 371 673 N ATOM 2174 CA LEU A 289 110.621 17.707 249.274 1.00 46.55 C ANISOU 2174 CA LEU A 289 6543 4824 6318 349 351 692 C ATOM 2175 C LEU A 289 110.338 19.131 249.746 1.00 30.93 C ANISOU 2175 C LEU A 289 4299 3031 4422 233 323 682 C ATOM 2176 O LEU A 289 111.076 19.682 250.562 1.00 40.06 O ANISOU 2176 O LEU A 289 5326 4334 5560 330 305 697 O ATOM 2177 CB LEU A 289 111.888 17.692 248.415 1.00 46.25 C ANISOU 2177 CB LEU A 289 6451 4882 6241 553 345 650 C ATOM 2178 CG LEU A 289 112.389 16.332 247.925 1.00 44.32 C ANISOU 2178 CG LEU A 289 6477 4472 5888 748 370 649 C ATOM 2179 CD1 LEU A 289 113.609 16.504 247.035 1.00 35.03 C ANISOU 2179 CD1 LEU A 289 5181 3464 4665 949 365 599 C ATOM 2180 CD2 LEU A 289 112.707 15.424 249.099 1.00 45.96 C ANISOU 2180 CD2 LEU A 289 6883 4587 5992 925 381 720 C ATOM 2181 N LEU A 290 109.264 19.719 249.231 1.00 31.04 N ANISOU 2181 N LEU A 290 4246 3040 4506 35 319 653 N ATOM 2182 CA LEU A 290 108.965 21.123 249.487 1.00 28.77 C ANISOU 2182 CA LEU A 290 3749 2901 4280 -47 292 635 C ATOM 2183 C LEU A 290 107.980 21.334 250.636 1.00 29.39 C ANISOU 2183 C LEU A 290 3808 2998 4362 -144 296 669 C ATOM 2184 O LEU A 290 107.966 22.397 251.257 1.00 41.72 O ANISOU 2184 O LEU A 290 5233 4676 5945 -148 275 662 O ATOM 2185 CB LEU A 290 108.418 21.777 248.216 1.00 38.47 C ANISOU 2185 CB LEU A 290 4908 4146 5562 -157 279 583 C ATOM 2186 CG LEU A 290 109.399 22.571 247.348 1.00 42.73 C ANISOU 2186 CG LEU A 290 5340 4780 6114 -100 259 543 C ATOM 2187 CD1 LEU A 290 110.702 21.821 247.149 1.00 56.78 C ANISOU 2187 CD1 LEU A 290 7165 6576 7833 66 272 543 C ATOM 2188 CD2 LEU A 290 108.768 22.894 246.005 1.00 43.91 C ANISOU 2188 CD2 LEU A 290 5480 4906 6298 -199 252 502 C ATOM 2189 N TYR A 291 107.162 20.326 250.921 1.00 34.92 N ANISOU 2189 N TYR A 291 2523 4428 6317 544 -67 -518 N ATOM 2190 CA TYR A 291 106.102 20.478 251.912 1.00 33.77 C ANISOU 2190 CA TYR A 291 2577 4109 6146 487 -153 -800 C ATOM 2191 C TYR A 291 106.132 19.416 253.009 1.00 44.57 C ANISOU 2191 C TYR A 291 4088 5463 7382 455 -187 -1007 C ATOM 2192 O TYR A 291 106.162 19.744 254.195 1.00 69.69 O ANISOU 2192 O TYR A 291 7364 8509 10606 377 -314 -1131 O ATOM 2193 CB TYR A 291 104.737 20.455 251.223 1.00 33.17 C ANISOU 2193 CB TYR A 291 2539 4144 5919 564 -59 -864 C ATOM 2194 CG TYR A 291 104.559 21.531 250.178 1.00 39.72 C ANISOU 2194 CG TYR A 291 3220 4999 6871 597 -40 -628 C ATOM 2195 CD1 TYR A 291 104.175 22.817 250.535 1.00 54.07 C ANISOU 2195 CD1 TYR A 291 5041 6579 8923 587 -146 -601 C ATOM 2196 CD2 TYR A 291 104.769 21.260 248.832 1.00 49.77 C ANISOU 2196 CD2 TYR A 291 4377 6530 8005 671 71 -429 C ATOM 2197 CE1 TYR A 291 104.009 23.804 249.582 1.00 37.34 C ANISOU 2197 CE1 TYR A 291 2778 4447 6963 607 -159 -328 C ATOM 2198 CE2 TYR A 291 104.604 22.239 247.872 1.00 51.60 C ANISOU 2198 CE2 TYR A 291 4442 6833 8330 687 83 -145 C ATOM 2199 CZ TYR A 291 104.224 23.509 248.252 1.00 37.72 C ANISOU 2199 CZ TYR A 291 2655 4806 6873 634 -41 -67 C ATOM 2200 OH TYR A 291 104.060 24.486 247.299 1.00 56.46 O ANISOU 2200 OH TYR A 291 4853 7215 9385 640 -59 271 O ATOM 2201 N VAL A 292 106.117 18.148 252.612 1.00 35.26 N ANISOU 2201 N VAL A 292 2957 4410 6029 526 -101 -1045 N ATOM 2202 CA VAL A 292 105.984 17.055 253.571 1.00 37.51 C ANISOU 2202 CA VAL A 292 3376 4664 6213 478 -157 -1183 C ATOM 2203 C VAL A 292 107.303 16.678 254.243 1.00 44.53 C ANISOU 2203 C VAL A 292 4212 5506 7199 463 -224 -1097 C ATOM 2204 O VAL A 292 107.457 16.838 255.453 1.00 50.89 O ANISOU 2204 O VAL A 292 5054 6249 8034 344 -350 -1143 O ATOM 2205 CB VAL A 292 105.392 15.801 252.902 1.00 34.49 C ANISOU 2205 CB VAL A 292 3125 4328 5652 531 -128 -1255 C ATOM 2206 CG1 VAL A 292 105.334 14.645 253.890 1.00 31.47 C ANISOU 2206 CG1 VAL A 292 2863 3865 5230 447 -232 -1314 C ATOM 2207 CG2 VAL A 292 104.009 16.105 252.355 1.00 44.92 C ANISOU 2207 CG2 VAL A 292 4459 5731 6877 484 -121 -1285 C ATOM 2208 N PHE A 293 108.256 16.183 253.458 1.00 33.17 N ANISOU 2208 N PHE A 293 2679 4144 5781 617 -135 -954 N ATOM 2209 CA PHE A 293 109.499 15.657 254.016 1.00 49.51 C ANISOU 2209 CA PHE A 293 4645 6218 7950 653 -179 -810 C ATOM 2210 C PHE A 293 110.483 16.751 254.419 1.00 49.89 C ANISOU 2210 C PHE A 293 4455 6275 8225 506 -299 -567 C ATOM 2211 O PHE A 293 111.654 16.475 254.683 1.00 37.31 O ANISOU 2211 O PHE A 293 2672 4756 6750 528 -339 -333 O ATOM 2212 CB PHE A 293 110.163 14.703 253.022 1.00 44.43 C ANISOU 2212 CB PHE A 293 3975 5684 7220 968 -10 -734 C ATOM 2213 CG PHE A 293 109.334 13.492 252.706 1.00 56.87 C ANISOU 2213 CG PHE A 293 5864 7140 8602 1080 -7 -991 C ATOM 2214 CD1 PHE A 293 108.970 12.607 253.707 1.00 35.36 C ANISOU 2214 CD1 PHE A 293 3307 4235 5893 954 -162 -1091 C ATOM 2215 CD2 PHE A 293 108.922 13.236 251.409 1.00 58.18 C ANISOU 2215 CD2 PHE A 293 6168 7372 8566 1282 103 -1102 C ATOM 2216 CE1 PHE A 293 108.206 11.492 253.421 1.00 35.98 C ANISOU 2216 CE1 PHE A 293 3675 4141 5854 985 -244 -1267 C ATOM 2217 CE2 PHE A 293 108.161 12.122 251.116 1.00 37.40 C ANISOU 2217 CE2 PHE A 293 3876 4560 5774 1329 3 -1345 C ATOM 2218 CZ PHE A 293 107.802 11.249 252.124 1.00 44.15 C ANISOU 2218 CZ PHE A 293 4887 5176 6712 1159 -189 -1413 C ATOM 2219 N VAL A 294 110.007 17.990 254.467 1.00 46.60 N ANISOU 2219 N VAL A 294 4051 5761 7895 351 -393 -597 N ATOM 2220 CA VAL A 294 110.817 19.097 254.953 1.00 37.44 C ANISOU 2220 CA VAL A 294 2753 4490 6983 137 -627 -401 C ATOM 2221 C VAL A 294 110.527 19.298 256.439 1.00 52.50 C ANISOU 2221 C VAL A 294 4898 6213 8838 -36 -871 -654 C ATOM 2222 O VAL A 294 111.267 19.985 257.145 1.00 45.14 O ANISOU 2222 O VAL A 294 3943 5145 8063 -248 -1162 -560 O ATOM 2223 CB VAL A 294 110.541 20.397 254.169 1.00 38.36 C ANISOU 2223 CB VAL A 294 2796 4519 7258 78 -657 -278 C ATOM 2224 CG1 VAL A 294 109.213 21.005 254.589 1.00 40.60 C ANISOU 2224 CG1 VAL A 294 3370 4596 7461 72 -707 -624 C ATOM 2225 CG2 VAL A 294 111.675 21.392 254.363 1.00 57.14 C ANISOU 2225 CG2 VAL A 294 4958 6784 9968 -174 -941 77 C ATOM 2226 N GLY A 295 109.446 18.679 256.905 1.00 42.99 N ANISOU 2226 N GLY A 295 3915 5034 7387 48 -772 -946 N ATOM 2227 CA GLY A 295 109.083 18.718 258.310 1.00 51.98 C ANISOU 2227 CA GLY A 295 5266 6121 8365 -40 -931 -1169 C ATOM 2228 C GLY A 295 109.680 17.546 259.064 1.00 58.45 C ANISOU 2228 C GLY A 295 6049 7058 9101 -82 -980 -1080 C ATOM 2229 O GLY A 295 109.683 16.419 258.568 1.00 54.06 O ANISOU 2229 O GLY A 295 5424 6595 8524 33 -820 -991 O ATOM 2230 N THR A 296 110.181 17.812 260.267 1.00 67.10 N ANISOU 2230 N THR A 296 7225 8125 10144 -238 -1238 -1110 N ATOM 2231 CA THR A 296 110.883 16.801 261.053 1.00 76.87 C ANISOU 2231 CA THR A 296 8392 9484 11331 -305 -1336 -954 C ATOM 2232 C THR A 296 109.993 15.623 261.438 1.00 67.92 C ANISOU 2232 C THR A 296 7350 8489 9967 -215 -1180 -1023 C ATOM 2233 O THR A 296 110.457 14.485 261.499 1.00 63.61 O ANISOU 2233 O THR A 296 6707 7988 9473 -187 -1166 -830 O ATOM 2234 CB THR A 296 111.478 17.409 262.336 1.00 42.03 C ANISOU 2234 CB THR A 296 4090 5040 6837 -521 -1698 -992 C ATOM 2235 OG1 THR A 296 110.449 18.087 263.067 1.00 62.12 O ANISOU 2235 OG1 THR A 296 6955 7562 9084 -480 -1734 -1359 O ATOM 2236 CG2 THR A 296 112.581 18.393 261.989 1.00 44.24 C ANISOU 2236 CG2 THR A 296 4223 5156 7432 -709 -1962 -791 C ATOM 2237 N LYS A 297 108.718 15.898 261.695 1.00 52.31 N ANISOU 2237 N LYS A 297 5538 6576 7762 -162 -1078 -1248 N ATOM 2238 CA LYS A 297 107.774 14.853 262.079 1.00 44.17 C ANISOU 2238 CA LYS A 297 4536 5716 6532 -137 -963 -1217 C ATOM 2239 C LYS A 297 107.612 13.819 260.970 1.00 53.16 C ANISOU 2239 C LYS A 297 5598 6765 7834 -73 -833 -1094 C ATOM 2240 O LYS A 297 107.548 12.619 261.234 1.00 66.13 O ANISOU 2240 O LYS A 297 7238 8416 9471 -111 -868 -945 O ATOM 2241 CB LYS A 297 106.415 15.459 262.434 1.00 48.19 C ANISOU 2241 CB LYS A 297 5150 6384 6776 -52 -842 -1408 C ATOM 2242 N PHE A 298 107.551 14.289 259.728 1.00 39.44 N ANISOU 2242 N PHE A 298 3832 4922 6232 28 -716 -1156 N ATOM 2243 CA PHE A 298 107.442 13.395 258.582 1.00 43.41 C ANISOU 2243 CA PHE A 298 4339 5333 6822 132 -620 -1109 C ATOM 2244 C PHE A 298 108.783 12.735 258.280 1.00 39.77 C ANISOU 2244 C PHE A 298 3803 4784 6526 251 -643 -958 C ATOM 2245 O PHE A 298 108.834 11.643 257.715 1.00 48.60 O ANISOU 2245 O PHE A 298 5005 5788 7675 383 -617 -938 O ATOM 2246 CB PHE A 298 106.932 14.149 257.353 1.00 32.42 C ANISOU 2246 CB PHE A 298 2937 3931 5450 223 -487 -1203 C ATOM 2247 CG PHE A 298 105.521 14.645 257.490 1.00 42.96 C ANISOU 2247 CG PHE A 298 4308 5368 6647 171 -439 -1302 C ATOM 2248 CD1 PHE A 298 104.456 13.759 257.464 1.00 32.42 C ANISOU 2248 CD1 PHE A 298 3014 4095 5210 97 -449 -1263 C ATOM 2249 CD2 PHE A 298 105.257 15.998 257.637 1.00 46.64 C ANISOU 2249 CD2 PHE A 298 4754 5857 7109 204 -409 -1396 C ATOM 2250 CE1 PHE A 298 103.155 14.211 257.588 1.00 41.16 C ANISOU 2250 CE1 PHE A 298 4065 5378 6198 70 -386 -1263 C ATOM 2251 CE2 PHE A 298 103.957 16.456 257.760 1.00 54.07 C ANISOU 2251 CE2 PHE A 298 5698 6924 7921 245 -327 -1461 C ATOM 2252 CZ PHE A 298 102.905 15.561 257.735 1.00 52.88 C ANISOU 2252 CZ PHE A 298 5511 6929 7653 184 -293 -1369 C ATOM 2253 N ARG A 299 109.866 13.405 258.657 1.00 45.94 N ANISOU 2253 N ARG A 299 4431 5609 7416 218 -715 -839 N ATOM 2254 CA ARG A 299 111.204 12.849 258.498 1.00 36.91 C ANISOU 2254 CA ARG A 299 3119 4469 6438 350 -726 -603 C ATOM 2255 C ARG A 299 111.428 11.703 259.476 1.00 50.46 C ANISOU 2255 C ARG A 299 4877 6149 8145 317 -856 -491 C ATOM 2256 O ARG A 299 111.953 10.653 259.108 1.00 56.99 O ANISOU 2256 O ARG A 299 5696 6885 9072 537 -810 -379 O ATOM 2257 CB ARG A 299 112.267 13.929 258.702 1.00 46.19 C ANISOU 2257 CB ARG A 299 4057 5727 7765 238 -840 -410 C ATOM 2258 CG ARG A 299 112.358 14.933 257.568 1.00 54.78 C ANISOU 2258 CG ARG A 299 5022 6846 8946 293 -722 -368 C ATOM 2259 CD ARG A 299 113.310 16.063 257.917 1.00 57.82 C ANISOU 2259 CD ARG A 299 5186 7251 9532 69 -943 -127 C ATOM 2260 NE ARG A 299 113.505 16.976 256.797 1.00 65.48 N ANISOU 2260 NE ARG A 299 5975 8265 10640 100 -850 37 N ATOM 2261 CZ ARG A 299 114.231 18.088 256.860 1.00 59.44 C ANISOU 2261 CZ ARG A 299 5006 7469 10110 -139 -1077 305 C ATOM 2262 NH1 ARG A 299 114.830 18.427 257.994 1.00 70.64 N ANISOU 2262 NH1 ARG A 299 6420 8794 11626 -429 -1439 382 N ATOM 2263 NH2 ARG A 299 114.357 18.862 255.790 1.00 63.07 N ANISOU 2263 NH2 ARG A 299 5271 7989 10705 -119 -987 527 N ATOM 2264 N GLN A 300 111.023 11.916 260.725 1.00 58.48 N ANISOU 2264 N GLN A 300 5953 7244 9022 79 -1017 -516 N ATOM 2265 CA GLN A 300 111.157 10.901 261.763 1.00 47.06 C ANISOU 2265 CA GLN A 300 4522 5819 7538 2 -1162 -347 C ATOM 2266 C GLN A 300 110.221 9.725 261.506 1.00 47.71 C ANISOU 2266 C GLN A 300 4768 5761 7599 43 -1121 -367 C ATOM 2267 O GLN A 300 110.588 8.571 261.728 1.00 64.40 O ANISOU 2267 O GLN A 300 6899 7739 9832 101 -1213 -180 O ATOM 2268 CB GLN A 300 110.877 11.503 263.142 1.00 43.83 C ANISOU 2268 CB GLN A 300 4155 5613 6887 -238 -1330 -378 C ATOM 2269 CG GLN A 300 111.900 12.536 263.591 1.00 61.97 C ANISOU 2269 CG GLN A 300 6354 7973 9220 -353 -1518 -339 C ATOM 2270 CD GLN A 300 111.497 13.234 264.876 1.00 62.14 C ANISOU 2270 CD GLN A 300 6541 8161 8909 -534 -1702 -496 C ATOM 2271 OE1 GLN A 300 110.424 12.981 265.422 1.00 55.95 O ANISOU 2271 OE1 GLN A 300 5892 7527 7841 -526 -1618 -602 O ATOM 2272 NE2 GLN A 300 112.358 14.121 265.364 1.00 66.62 N ANISOU 2272 NE2 GLN A 300 7100 8724 9489 -689 -1972 -492 N ATOM 2273 N GLU A 301 109.014 10.026 261.035 1.00 39.34 N ANISOU 2273 N GLU A 301 3822 4708 6416 -4 -1024 -558 N ATOM 2274 CA GLU A 301 108.017 8.998 260.753 1.00 43.53 C ANISOU 2274 CA GLU A 301 4495 5100 6944 -55 -1062 -536 C ATOM 2275 C GLU A 301 108.477 8.070 259.637 1.00 50.42 C ANISOU 2275 C GLU A 301 5510 5642 8005 180 -1064 -578 C ATOM 2276 O GLU A 301 108.346 6.851 259.739 1.00 58.73 O ANISOU 2276 O GLU A 301 6706 6444 9163 167 -1225 -470 O ATOM 2277 CB GLU A 301 106.677 9.636 260.383 1.00 37.01 C ANISOU 2277 CB GLU A 301 3697 4402 5961 -149 -966 -683 C ATOM 2278 CG GLU A 301 105.575 8.635 260.063 1.00 49.23 C ANISOU 2278 CG GLU A 301 5348 5828 7528 -287 -1074 -593 C ATOM 2279 CD GLU A 301 105.114 7.853 261.279 1.00 74.96 C ANISOU 2279 CD GLU A 301 8536 9209 10736 -521 -1229 -281 C ATOM 2280 OE1 GLU A 301 105.392 8.289 262.416 1.00 93.92 O ANISOU 2280 OE1 GLU A 301 10812 11898 12975 -558 -1198 -189 O ATOM 2281 OE2 GLU A 301 104.470 6.800 261.096 1.00 69.99 O ANISOU 2281 OE2 GLU A 301 7986 8391 10217 -687 -1416 -105 O ATOM 2282 N LEU A 302 109.016 8.655 258.572 1.00 46.93 N ANISOU 2282 N LEU A 302 5047 5196 7590 417 -897 -727 N ATOM 2283 CA LEU A 302 109.532 7.879 257.452 1.00 54.61 C ANISOU 2283 CA LEU A 302 6176 5930 8643 755 -844 -812 C ATOM 2284 C LEU A 302 110.735 7.047 257.882 1.00 53.70 C ANISOU 2284 C LEU A 302 6003 5699 8701 975 -894 -614 C ATOM 2285 O LEU A 302 110.937 5.933 257.399 1.00 48.66 O ANISOU 2285 O LEU A 302 5596 4749 8145 1241 -950 -666 O ATOM 2286 CB LEU A 302 109.911 8.797 256.289 1.00 48.77 C ANISOU 2286 CB LEU A 302 5346 5350 7836 981 -612 -929 C ATOM 2287 CG LEU A 302 110.450 8.102 255.037 1.00 61.94 C ANISOU 2287 CG LEU A 302 7183 6881 9469 1429 -493 -1048 C ATOM 2288 CD1 LEU A 302 109.430 7.117 254.486 1.00 58.03 C ANISOU 2288 CD1 LEU A 302 7111 6052 8888 1415 -668 -1290 C ATOM 2289 CD2 LEU A 302 110.837 9.124 253.982 1.00 56.81 C ANISOU 2289 CD2 LEU A 302 6356 6516 8712 1623 -241 -1057 C ATOM 2290 N HIS A 303 111.527 7.594 258.798 1.00 47.41 N ANISOU 2290 N HIS A 303 4919 5133 7961 875 -907 -388 N ATOM 2291 CA HIS A 303 112.692 6.891 259.319 1.00 45.54 C ANISOU 2291 CA HIS A 303 4545 4855 7903 1054 -973 -115 C ATOM 2292 C HIS A 303 112.264 5.669 260.127 1.00 58.68 C ANISOU 2292 C HIS A 303 6387 6263 9646 927 -1210 8 C ATOM 2293 O HIS A 303 112.957 4.652 260.147 1.00 72.27 O ANISOU 2293 O HIS A 303 8151 7753 11554 1194 -1275 159 O ATOM 2294 CB HIS A 303 113.545 7.826 260.178 1.00 63.95 C ANISOU 2294 CB HIS A 303 6528 7509 10261 872 -1023 127 C ATOM 2295 CG HIS A 303 114.885 7.263 260.536 1.00 61.67 C ANISOU 2295 CG HIS A 303 5995 7261 10175 1083 -1071 480 C ATOM 2296 ND1 HIS A 303 115.098 6.515 261.674 1.00 63.90 N ANISOU 2296 ND1 HIS A 303 6248 7502 10528 953 -1294 729 N ATOM 2297 CD2 HIS A 303 116.081 7.339 259.906 1.00 53.28 C ANISOU 2297 CD2 HIS A 303 4654 6331 9258 1433 -915 690 C ATOM 2298 CE1 HIS A 303 116.368 6.154 261.729 1.00 53.34 C ANISOU 2298 CE1 HIS A 303 4637 6236 9395 1214 -1290 1061 C ATOM 2299 NE2 HIS A 303 116.986 6.641 260.669 1.00 62.05 N ANISOU 2299 NE2 HIS A 303 5568 7463 10546 1521 -1048 1053 N ATOM 2300 N CYS A 304 111.116 5.776 260.790 1.00 56.05 N ANISOU 2300 N CYS A 304 6131 5988 9177 540 -1336 -11 N ATOM 2301 CA CYS A 304 110.562 4.661 261.548 1.00 66.28 C ANISOU 2301 CA CYS A 304 7549 7090 10545 343 -1580 197 C ATOM 2302 C CYS A 304 109.959 3.614 260.618 1.00 64.59 C ANISOU 2302 C CYS A 304 7689 6395 10458 456 -1694 49 C ATOM 2303 O CYS A 304 110.121 2.413 260.834 1.00 53.90 O ANISOU 2303 O CYS A 304 6496 4665 9317 511 -1917 217 O ATOM 2304 CB CYS A 304 109.503 5.152 262.538 1.00 68.92 C ANISOU 2304 CB CYS A 304 7790 7752 10645 -73 -1640 291 C ATOM 2305 SG CYS A 304 110.142 6.183 263.877 1.00 79.30 S ANISOU 2305 SG CYS A 304 8829 9559 11741 -223 -1633 431 S ATOM 2306 N LEU A 305 109.263 4.078 259.585 1.00 62.07 N ANISOU 2306 N LEU A 305 7514 6057 10011 480 -1587 -261 N ATOM 2307 CA LEU A 305 108.621 3.185 258.626 1.00 55.82 C ANISOU 2307 CA LEU A 305 7114 4810 9285 546 -1758 -456 C ATOM 2308 C LEU A 305 109.648 2.377 257.841 1.00 61.67 C ANISOU 2308 C LEU A 305 8112 5160 10158 1084 -1742 -612 C ATOM 2309 O LEU A 305 109.477 1.177 257.633 1.00 64.30 O ANISOU 2309 O LEU A 305 8815 4960 10657 1161 -2024 -649 O ATOM 2310 CB LEU A 305 107.732 3.980 257.668 1.00 59.45 C ANISOU 2310 CB LEU A 305 7635 5417 9535 469 -1643 -735 C ATOM 2311 CG LEU A 305 106.500 4.651 258.281 1.00 59.16 C ANISOU 2311 CG LEU A 305 7391 5721 9366 15 -1663 -596 C ATOM 2312 CD1 LEU A 305 105.738 5.446 257.232 1.00 44.00 C ANISOU 2312 CD1 LEU A 305 5508 3935 7274 9 -1542 -844 C ATOM 2313 CD2 LEU A 305 105.596 3.620 258.941 1.00 56.89 C ANISOU 2313 CD2 LEU A 305 7173 5241 9200 -364 -2006 -299 C ATOM 2314 N LEU A 306 110.717 3.038 257.412 1.00 61.25 N ANISOU 2314 N LEU A 306 7860 5375 10038 1474 -1425 -676 N ATOM 2315 CA LEU A 306 111.776 2.369 256.664 1.00 61.53 C ANISOU 2315 CA LEU A 306 8058 5178 10143 2100 -1314 -783 C ATOM 2316 C LEU A 306 112.556 1.401 257.549 1.00 60.35 C ANISOU 2316 C LEU A 306 7864 4787 10278 2241 -1471 -474 C ATOM 2317 O LEU A 306 113.221 0.492 257.052 1.00 64.96 O ANISOU 2317 O LEU A 306 8695 5012 10975 2779 -1474 -560 O ATOM 2318 CB LEU A 306 112.725 3.396 256.042 1.00 72.29 C ANISOU 2318 CB LEU A 306 9087 7015 11366 2444 -915 -785 C ATOM 2319 CG LEU A 306 112.154 4.247 254.906 1.00 78.84 C ANISOU 2319 CG LEU A 306 9986 8051 11919 2457 -733 -1075 C ATOM 2320 CD1 LEU A 306 113.193 5.234 254.396 1.00 58.27 C ANISOU 2320 CD1 LEU A 306 6972 5936 9231 2757 -369 -932 C ATOM 2321 CD2 LEU A 306 111.650 3.361 253.776 1.00 57.24 C ANISOU 2321 CD2 LEU A 306 7812 4901 9037 2761 -835 -1472 C ATOM 2322 N ALA A 307 112.470 1.599 258.860 1.00 65.12 N ANISOU 2322 N ALA A 307 8169 5601 10972 1798 -1603 -114 N ATOM 2323 CA ALA A 307 113.154 0.732 259.812 1.00 61.79 C ANISOU 2323 CA ALA A 307 7654 5009 10814 1857 -1785 261 C ATOM 2324 C ALA A 307 112.285 -0.463 260.191 1.00 81.40 C ANISOU 2324 C ALA A 307 10491 6952 13484 1593 -2192 352 C ATOM 2325 O ALA A 307 112.792 -1.557 260.439 1.00 95.68 O ANISOU 2325 O ALA A 307 12451 8329 15575 1831 -2390 534 O ATOM 2326 CB ALA A 307 113.548 1.515 261.053 1.00 70.53 C ANISOU 2326 CB ALA A 307 8280 6644 11874 1512 -1766 628 C ATOM 2327 N GLU A 308 110.974 -0.247 260.235 1.00 83.07 N ANISOU 2327 N GLU A 308 10805 7189 13568 1099 -2335 279 N ATOM 2328 CA GLU A 308 110.034 -1.307 260.585 1.00 94.93 C ANISOU 2328 CA GLU A 308 12574 8231 15265 736 -2767 464 C ATOM 2329 C GLU A 308 109.808 -2.260 259.415 1.00 92.90 C ANISOU 2329 C GLU A 308 12914 7239 15146 1020 -3000 102 C ATOM 2330 O GLU A 308 109.455 -3.423 259.612 1.00100.60 O ANISOU 2330 O GLU A 308 14204 7608 16412 876 -3439 263 O ATOM 2331 CB GLU A 308 108.700 -0.712 261.044 1.00104.77 C ANISOU 2331 CB GLU A 308 13638 9855 16314 122 -2822 596 C ATOM 2332 CG GLU A 308 108.765 -0.014 262.395 1.00109.66 C ANISOU 2332 CG GLU A 308 13781 11119 16768 -171 -2696 968 C ATOM 2333 CD GLU A 308 107.445 0.619 262.790 1.00105.34 C ANISOU 2333 CD GLU A 308 13052 11006 15967 -639 -2675 1070 C ATOM 2334 OE1 GLU A 308 106.510 0.614 261.962 1.00 90.49 O ANISOU 2334 OE1 GLU A 308 11352 8963 14066 -761 -2743 877 O ATOM 2335 OE2 GLU A 308 107.343 1.122 263.929 1.00109.01 O ANISOU 2335 OE2 GLU A 308 13191 12002 16225 -855 -2592 1351 O ATOM 2336 N PHE A 309 110.012 -1.764 258.199 1.00 88.69 N ANISOU 2336 N PHE A 309 12560 6749 14390 1420 -2742 -379 N ATOM 2337 CA PHE A 309 109.869 -2.591 257.007 1.00 73.59 C ANISOU 2337 CA PHE A 309 11272 4209 12479 1770 -2933 -815 C ATOM 2338 C PHE A 309 111.188 -3.266 256.642 1.00114.54 C ANISOU 2338 C PHE A 309 16582 9285 17655 2466 -2690 -909 C ATOM 2339 O PHE A 309 111.257 -4.038 255.685 1.00117.31 O ANISOU 2339 O PHE A 309 17381 9342 17849 2771 -2691 -1241 O ATOM 2340 CB PHE A 309 109.356 -1.757 255.831 1.00 71.04 C ANISOU 2340 CB PHE A 309 11059 4148 11784 1822 -2727 -1249 C ATOM 2341 CG PHE A 309 107.862 -1.584 255.816 1.00 81.20 C ANISOU 2341 CG PHE A 309 12408 5412 13031 1155 -3037 -1216 C ATOM 2342 CD1 PHE A 309 107.256 -0.581 256.554 1.00 75.35 C ANISOU 2342 CD1 PHE A 309 11142 5300 12190 665 -2870 -920 C ATOM 2343 CD2 PHE A 309 107.063 -2.426 255.060 1.00 87.27 C ANISOU 2343 CD2 PHE A 309 13617 5841 13701 981 -3363 -1393 C ATOM 2344 CE1 PHE A 309 105.884 -0.421 256.540 1.00 63.48 C ANISOU 2344 CE1 PHE A 309 9612 3875 10634 104 -3100 -818 C ATOM 2345 CE2 PHE A 309 105.690 -2.271 255.042 1.00 90.08 C ANISOU 2345 CE2 PHE A 309 13939 6253 14033 363 -3655 -1265 C ATOM 2346 CZ PHE A 309 105.100 -1.267 255.783 1.00 72.06 C ANISOU 2346 CZ PHE A 309 11190 4393 11796 -67 -3566 -983 C ATOM 2347 N ARG A 310 112.232 -2.972 257.412 1.00111.01 N ANISOU 2347 N ARG A 310 15704 9098 17376 2710 -2490 -583 N ATOM 2348 CA ARG A 310 113.529 -3.614 257.228 1.00112.38 C ANISOU 2348 CA ARG A 310 15886 9225 17589 3356 -2238 -535 C ATOM 2349 C ARG A 310 114.001 -4.273 258.521 1.00102.04 C ANISOU 2349 C ARG A 310 14358 7756 16656 3242 -2467 -8 C ATOM 2350 O ARG A 310 113.321 -5.139 259.072 1.00 93.95 O ANISOU 2350 O ARG A 310 13561 6296 15841 2834 -2889 162 O ATOM 2351 CB ARG A 310 114.574 -2.605 256.745 1.00104.17 C ANISOU 2351 CB ARG A 310 14431 8801 16347 3848 -1706 -557 C ATOM 2352 CG ARG A 310 114.356 -2.104 255.326 1.00102.93 C ANISOU 2352 CG ARG A 310 14476 8850 15781 4075 -1406 -1018 C ATOM 2353 CD ARG A 310 115.599 -1.405 254.797 1.00100.20 C ANISOU 2353 CD ARG A 310 13689 9097 15287 4604 -864 -911 C ATOM 2354 NE ARG A 310 115.422 -0.919 253.432 1.00107.89 N ANISOU 2354 NE ARG A 310 14804 10329 15861 4780 -587 -1278 N ATOM 2355 CZ ARG A 310 115.126 0.338 253.119 1.00109.15 C ANISOU 2355 CZ ARG A 310 14690 10963 15820 4586 -422 -1303 C ATOM 2356 NH1 ARG A 310 114.978 1.244 254.076 1.00113.09 N ANISOU 2356 NH1 ARG A 310 14771 11706 16493 4230 -518 -1041 N ATOM 2357 NH2 ARG A 310 114.983 0.692 251.849 1.00103.48 N ANISOU 2357 NH2 ARG A 310 14111 10478 14727 4750 -197 -1585 N TER 2358 ARG A 310 HETATM 2359 N PCA B 1 96.775 18.253 222.953 1.00 67.61 N HETATM 2360 CA PCA B 1 97.749 17.757 223.919 1.00 56.88 C HETATM 2361 CB PCA B 1 98.441 16.506 223.394 1.00 63.55 C HETATM 2362 CG PCA B 1 98.137 16.436 221.911 1.00 73.62 C HETATM 2363 CD PCA B 1 97.039 17.452 221.757 1.00 64.77 C HETATM 2364 OE PCA B 1 96.417 17.570 220.702 1.00 55.55 O HETATM 2365 C PCA B 1 98.808 18.809 224.197 1.00 43.80 C HETATM 2366 O PCA B 1 98.579 19.998 223.981 1.00 58.54 O ATOM 2367 N HIS B 2 99.969 18.371 224.676 1.00 66.24 N ANISOU 2367 N HIS B 2 7404 8147 9617 -1499 2951 -996 N ATOM 2368 CA HIS B 2 101.064 19.290 224.962 1.00 53.64 C ANISOU 2368 CA HIS B 2 6231 6783 7367 -1798 2992 -787 C ATOM 2369 C HIS B 2 102.130 19.240 223.869 1.00 49.92 C ANISOU 2369 C HIS B 2 5703 6770 6494 -1661 2536 -635 C ATOM 2370 O HIS B 2 102.064 18.414 222.959 1.00 48.68 O ANISOU 2370 O HIS B 2 5235 6729 6533 -1332 2221 -700 O ATOM 2371 CB HIS B 2 101.684 18.983 226.327 1.00 58.81 C ANISOU 2371 CB HIS B 2 7184 7530 7633 -2136 3099 -614 C ATOM 2372 CG HIS B 2 102.060 17.546 226.517 1.00 68.35 C ANISOU 2372 CG HIS B 2 8168 8939 8864 -2060 2963 -498 C ATOM 2373 ND1 HIS B 2 101.152 16.585 226.910 1.00 48.28 N ANISOU 2373 ND1 HIS B 2 5453 6090 6803 -1962 3126 -644 N ATOM 2374 CD2 HIS B 2 103.246 16.909 226.382 1.00 46.44 C ANISOU 2374 CD2 HIS B 2 5328 6613 5702 -2051 2725 -227 C ATOM 2375 CE1 HIS B 2 101.763 15.417 227.003 1.00 47.88 C ANISOU 2375 CE1 HIS B 2 5300 6239 6654 -1916 3029 -477 C ATOM 2376 NE2 HIS B 2 103.034 15.586 226.687 1.00 46.85 N ANISOU 2376 NE2 HIS B 2 5208 6580 6013 -1943 2809 -212 N ATOM 2377 N HIS B 3 103.110 20.134 223.968 1.00 46.09 N ANISOU 2377 N HIS B 3 5549 6541 5423 -1960 2538 -449 N ATOM 2378 CA HIS B 3 104.120 20.296 222.928 1.00 45.11 C ANISOU 2378 CA HIS B 3 5390 6860 4891 -1873 2174 -297 C ATOM 2379 C HIS B 3 105.094 19.123 222.866 1.00 51.65 C ANISOU 2379 C HIS B 3 5967 8159 5498 -1807 1978 -115 C ATOM 2380 O HIS B 3 105.751 18.908 221.847 1.00 57.01 O ANISOU 2380 O HIS B 3 6501 9170 5992 -1588 1695 -42 O ATOM 2381 CB HIS B 3 104.891 21.601 223.145 1.00 51.74 C ANISOU 2381 CB HIS B 3 6664 7841 5153 -2309 2282 -146 C ATOM 2382 CG HIS B 3 104.021 22.820 223.157 1.00 55.39 C ANISOU 2382 CG HIS B 3 7466 7773 5806 -2318 2539 -293 C ATOM 2383 ND1 HIS B 3 103.173 23.119 224.201 1.00 60.49 N ANISOU 2383 ND1 HIS B 3 8320 7944 6721 -2461 2981 -432 N ATOM 2384 CD2 HIS B 3 103.868 23.814 222.251 1.00 48.92 C ANISOU 2384 CD2 HIS B 3 6838 6797 4954 -2157 2452 -295 C ATOM 2385 CE1 HIS B 3 102.535 24.245 223.938 1.00 65.58 C ANISOU 2385 CE1 HIS B 3 9251 8145 7520 -2350 3188 -515 C ATOM 2386 NE2 HIS B 3 102.939 24.688 222.761 1.00 51.40 N ANISOU 2386 NE2 HIS B 3 7459 6526 5546 -2158 2852 -416 N ATOM 2387 N GLY B 4 105.188 18.371 223.957 1.00 55.84 N ANISOU 2387 N GLY B 4 6470 8704 6043 -1973 2164 -19 N ATOM 2388 CA GLY B 4 106.074 17.223 224.012 1.00 51.22 C ANISOU 2388 CA GLY B 4 5657 8510 5293 -1839 2034 215 C ATOM 2389 C GLY B 4 105.678 16.144 223.023 1.00 48.72 C ANISOU 2389 C GLY B 4 5067 8049 5397 -1320 1862 41 C ATOM 2390 O GLY B 4 106.529 15.572 222.342 1.00 43.87 O ANISOU 2390 O GLY B 4 4299 7778 4591 -1071 1687 180 O ATOM 2391 N VAL B 5 104.380 15.871 222.940 1.00 65.91 N ANISOU 2391 N VAL B 5 7185 9723 8135 -1184 1939 -272 N ATOM 2392 CA VAL B 5 103.866 14.850 222.033 1.00 52.65 C ANISOU 2392 CA VAL B 5 5296 7866 6844 -810 1779 -497 C ATOM 2393 C VAL B 5 103.254 15.471 220.777 1.00 56.96 C ANISOU 2393 C VAL B 5 5766 8338 7536 -626 1510 -735 C ATOM 2394 O VAL B 5 102.056 15.747 220.717 1.00 96.19 O ANISOU 2394 O VAL B 5 10636 12975 12938 -610 1525 -960 O ATOM 2395 CB VAL B 5 102.822 13.953 222.733 1.00 54.48 C ANISOU 2395 CB VAL B 5 5454 7646 7598 -837 2008 -677 C ATOM 2396 CG1 VAL B 5 103.516 12.883 223.559 1.00 51.11 C ANISOU 2396 CG1 VAL B 5 5091 7291 7038 -849 2181 -424 C ATOM 2397 CG2 VAL B 5 101.889 14.783 223.607 1.00 45.85 C ANISOU 2397 CG2 VAL B 5 4431 6258 6734 -1110 2277 -774 C ATOM 2398 N THR B 6 104.092 15.690 219.771 1.00 58.88 N ANISOU 2398 N THR B 6 6035 8931 7406 -480 1265 -651 N ATOM 2399 CA THR B 6 103.638 16.274 218.516 1.00 44.42 C ANISOU 2399 CA THR B 6 4181 7089 5607 -312 971 -819 C ATOM 2400 C THR B 6 104.343 15.613 217.340 1.00 58.24 C ANISOU 2400 C THR B 6 5910 9113 7105 -64 746 -849 C ATOM 2401 O THR B 6 105.563 15.453 217.347 1.00 69.64 O ANISOU 2401 O THR B 6 7398 10921 8140 -49 807 -619 O ATOM 2402 CB THR B 6 103.887 17.792 218.478 1.00 53.34 C ANISOU 2402 CB THR B 6 5520 8320 6428 -480 964 -666 C ATOM 2403 OG1 THR B 6 103.246 18.410 219.601 1.00100.48 O ANISOU 2403 OG1 THR B 6 11589 13977 12613 -708 1261 -665 O ATOM 2404 CG2 THR B 6 103.337 18.395 217.195 1.00 45.27 C ANISOU 2404 CG2 THR B 6 4493 7257 5452 -265 649 -784 C ATOM 2405 N LYS B 7 103.569 15.222 216.333 1.00 56.90 N ANISOU 2405 N LYS B 7 5660 8794 7164 113 501 -1130 N ATOM 2406 CA LYS B 7 104.128 14.568 215.158 1.00 66.35 C ANISOU 2406 CA LYS B 7 6919 10189 8104 320 329 -1228 C ATOM 2407 C LYS B 7 103.947 15.434 213.917 1.00 66.23 C ANISOU 2407 C LYS B 7 6980 10330 7853 377 -16 -1285 C ATOM 2408 O LYS B 7 104.078 14.958 212.789 1.00 74.07 O ANISOU 2408 O LYS B 7 8053 11430 8660 512 -210 -1449 O ATOM 2409 CB LYS B 7 103.485 13.195 214.957 1.00 70.76 C ANISOU 2409 CB LYS B 7 7423 10446 9016 407 339 -1536 C ATOM 2410 CG LYS B 7 103.670 12.261 216.144 1.00 60.55 C ANISOU 2410 CG LYS B 7 6115 8949 7942 380 698 -1447 C ATOM 2411 CD LYS B 7 103.133 10.870 215.858 1.00 72.52 C ANISOU 2411 CD LYS B 7 7682 10113 9758 441 757 -1756 C ATOM 2412 CE LYS B 7 103.376 9.938 217.035 1.00 78.09 C ANISOU 2412 CE LYS B 7 8436 10582 10654 447 1139 -1606 C ATOM 2413 NZ LYS B 7 102.921 8.550 216.750 1.00 89.07 N ANISOU 2413 NZ LYS B 7 9977 11553 12312 488 1260 -1904 N ATOM 2414 N CYS B 8 103.648 16.710 214.136 1.00 57.57 N ANISOU 2414 N CYS B 8 5919 9215 6741 271 -63 -1139 N ATOM 2415 CA CYS B 8 103.513 17.667 213.046 1.00 52.74 C ANISOU 2415 CA CYS B 8 5430 8728 5881 340 -369 -1102 C ATOM 2416 C CYS B 8 104.853 18.321 212.735 1.00 54.95 C ANISOU 2416 C CYS B 8 5951 9379 5549 264 -300 -848 C ATOM 2417 O CYS B 8 105.401 19.052 213.558 1.00 53.02 O ANISOU 2417 O CYS B 8 5808 9193 5145 51 -71 -620 O ATOM 2418 CB CYS B 8 102.475 18.736 213.390 1.00 51.36 C ANISOU 2418 CB CYS B 8 5207 8280 6027 327 -406 -1044 C ATOM 2419 SG CYS B 8 102.325 20.043 212.149 1.00 73.21 S ANISOU 2419 SG CYS B 8 8184 11149 8483 461 -756 -886 S ATOM 2420 N ALA B 9 105.375 18.057 211.541 1.00 56.38 N ANISOU 2420 N ALA B 9 6238 9824 5361 385 -482 -900 N ATOM 2421 CA ALA B 9 106.682 18.574 211.151 1.00 49.88 C ANISOU 2421 CA ALA B 9 5594 9407 3952 304 -389 -667 C ATOM 2422 C ALA B 9 106.573 19.587 210.013 1.00 69.48 C ANISOU 2422 C ALA B 9 8331 11975 6092 308 -660 -603 C ATOM 2423 O ALA B 9 107.574 20.166 209.592 1.00 62.89 O ANISOU 2423 O ALA B 9 7683 11464 4750 191 -588 -408 O ATOM 2424 CB ALA B 9 107.604 17.429 210.753 1.00 50.62 C ANISOU 2424 CB ALA B 9 5629 9771 3833 461 -250 -727 C ATOM 2425 N ILE B 10 105.357 19.801 209.519 1.00 69.62 N ANISOU 2425 N ILE B 10 8337 11733 6382 433 -977 -735 N ATOM 2426 CA ILE B 10 105.137 20.733 208.417 1.00 56.12 C ANISOU 2426 CA ILE B 10 6875 10086 4361 486 -1284 -625 C ATOM 2427 C ILE B 10 104.149 21.832 208.793 1.00 62.72 C ANISOU 2427 C ILE B 10 7729 10582 5521 533 -1369 -470 C ATOM 2428 O ILE B 10 103.047 21.554 209.264 1.00 76.25 O ANISOU 2428 O ILE B 10 9154 12025 7792 647 -1438 -593 O ATOM 2429 CB ILE B 10 104.612 20.010 207.162 1.00 64.61 C ANISOU 2429 CB ILE B 10 7943 11258 5348 639 -1675 -870 C ATOM 2430 CG1 ILE B 10 105.465 18.778 206.850 1.00 59.08 C ANISOU 2430 CG1 ILE B 10 7262 10774 4412 647 -1495 -1083 C ATOM 2431 CG2 ILE B 10 104.576 20.966 205.977 1.00 74.33 C ANISOU 2431 CG2 ILE B 10 9483 12633 6127 676 -1996 -694 C ATOM 2432 CD1 ILE B 10 106.896 19.102 206.495 1.00 71.83 C ANISOU 2432 CD1 ILE B 10 9099 12757 5435 580 -1248 -890 C ATOM 2433 N THR B 11 104.550 23.082 208.582 1.00 68.34 N ANISOU 2433 N THR B 11 8790 11287 5889 451 -1319 -192 N ATOM 2434 CA THR B 11 103.663 24.220 208.805 1.00 73.66 C ANISOU 2434 CA THR B 11 9578 11578 6832 571 -1347 -4 C ATOM 2435 C THR B 11 103.632 25.129 207.580 1.00 63.64 C ANISOU 2435 C THR B 11 8656 10366 5160 697 -1647 229 C ATOM 2436 O THR B 11 104.669 25.422 206.985 1.00 63.84 O ANISOU 2436 O THR B 11 9015 10658 4585 510 -1601 341 O ATOM 2437 CB THR B 11 104.086 25.048 210.036 1.00 67.65 C ANISOU 2437 CB THR B 11 9043 10569 6092 308 -866 144 C ATOM 2438 OG1 THR B 11 105.417 25.545 209.848 1.00 91.64 O ANISOU 2438 OG1 THR B 11 12442 13886 8493 -23 -695 307 O ATOM 2439 CG2 THR B 11 104.032 24.201 211.298 1.00 55.07 C ANISOU 2439 CG2 THR B 11 7135 8911 4876 180 -587 -43 C ATOM 2440 N CYS B 12 102.435 25.572 207.209 1.00 67.18 N ANISOU 2440 N CYS B 12 9001 10586 5939 1021 -1947 335 N ATOM 2441 CA CYS B 12 102.262 26.429 206.043 1.00 71.66 C ANISOU 2441 CA CYS B 12 9887 11189 6151 1202 -2285 619 C ATOM 2442 C CYS B 12 101.755 27.813 206.432 1.00 77.04 C ANISOU 2442 C CYS B 12 10844 11384 7044 1394 -2097 962 C ATOM 2443 O CYS B 12 100.869 27.946 207.276 1.00102.54 O ANISOU 2443 O CYS B 12 13802 14265 10893 1592 -1933 952 O ATOM 2444 CB CYS B 12 101.299 25.785 205.045 1.00102.34 C ANISOU 2444 CB CYS B 12 13431 15300 10152 1457 -2892 530 C ATOM 2445 SG CYS B 12 101.913 24.272 204.270 1.00103.22 S ANISOU 2445 SG CYS B 12 13446 15908 9864 1228 -3100 122 S ATOM 2446 N SER B 13 102.320 28.841 205.807 1.00 76.86 N ANISOU 2446 N SER B 13 11396 11306 6500 1339 -2069 1267 N ATOM 2447 CA SER B 13 101.907 30.216 206.061 1.00 85.29 C ANISOU 2447 CA SER B 13 12869 11832 7704 1540 -1843 1621 C ATOM 2448 C SER B 13 101.077 30.757 204.902 1.00 91.72 C ANISOU 2448 C SER B 13 13740 12625 8484 2017 -2348 1973 C ATOM 2449 O SER B 13 100.157 31.551 205.101 1.00110.67 O ANISOU 2449 O SER B 13 16150 14587 11312 2447 -2302 2257 O ATOM 2450 CB SER B 13 103.127 31.109 206.298 1.00 91.01 C ANISOU 2450 CB SER B 13 14293 12420 7868 1085 -1384 1756 C ATOM 2451 OG SER B 13 103.973 31.127 205.161 1.00108.46 O ANISOU 2451 OG SER B 13 16803 15035 9371 895 -1612 1855 O ATOM 2452 N LYS B 14 101.408 30.321 203.691 1.00 88.04 N ANISOU 2452 N LYS B 14 13316 12643 7491 1955 -2813 1974 N ATOM 2453 CA LYS B 14 100.688 30.749 202.498 1.00101.88 C ANISOU 2453 CA LYS B 14 15132 14490 9090 2348 -3379 2328 C ATOM 2454 C LYS B 14 100.458 29.581 201.545 1.00100.10 C ANISOU 2454 C LYS B 14 14511 14869 8653 2305 -3988 2086 C ATOM 2455 O LYS B 14 100.985 28.487 201.747 1.00 90.74 O ANISOU 2455 O LYS B 14 13111 13972 7394 1980 -3898 1648 O ATOM 2456 CB LYS B 14 101.449 31.867 201.783 1.00103.01 C ANISOU 2456 CB LYS B 14 16087 14503 8549 2246 -3278 2712 C ATOM 2457 N MET B 15 99.666 29.822 200.506 1.00101.70 N ANISOU 2457 N MET B 15 14655 15252 8736 2628 -4600 2388 N ATOM 2458 CA MET B 15 99.364 28.795 199.518 1.00103.86 C ANISOU 2458 CA MET B 15 14635 16099 8729 2526 -5224 2167 C ATOM 2459 C MET B 15 99.800 29.236 198.126 1.00116.63 C ANISOU 2459 C MET B 15 16730 17954 9631 2338 -5443 2433 C ATOM 2460 O MET B 15 99.719 30.416 197.785 1.00125.61 O ANISOU 2460 O MET B 15 18259 18854 10615 2579 -5452 2940 O ATOM 2461 CB MET B 15 97.869 28.469 199.523 1.00114.94 C ANISOU 2461 CB MET B 15 15295 17615 10762 2880 -5742 2232 C ATOM 2462 CG MET B 15 97.343 27.977 200.862 1.00119.48 C ANISOU 2462 CG MET B 15 15273 17931 12191 2925 -5375 1947 C ATOM 2463 SD MET B 15 98.114 26.437 201.394 1.00131.51 S ANISOU 2463 SD MET B 15 16649 19648 13672 2374 -5073 1231 S ATOM 2464 CE MET B 15 97.273 26.156 202.950 1.00120.58 C ANISOU 2464 CE MET B 15 14612 17895 13309 2513 -4678 1065 C ATOM 2465 N THR B 16 100.262 28.281 197.324 1.00118.14 N ANISOU 2465 N THR B 16 16869 18555 9465 1849 -5487 2090 N ATOM 2466 CA THR B 16 100.699 28.572 195.964 1.00119.81 C ANISOU 2466 CA THR B 16 17416 19059 9049 1576 -5563 2277 C ATOM 2467 C THR B 16 99.511 28.823 195.043 1.00121.72 C ANISOU 2467 C THR B 16 17404 19545 9298 1799 -6209 2641 C ATOM 2468 O THR B 16 98.417 28.307 195.269 1.00135.07 O ANISOU 2468 O THR B 16 18533 21332 11455 1964 -6624 2588 O ATOM 2469 CB THR B 16 101.549 27.427 195.387 1.00119.88 C ANISOU 2469 CB THR B 16 17453 19424 8671 1035 -5350 1796 C ATOM 2470 OG1 THR B 16 100.817 26.197 195.467 1.00111.25 O ANISOU 2470 OG1 THR B 16 15932 18462 7874 941 -5665 1421 O ATOM 2471 CG2 THR B 16 102.846 27.290 196.163 1.00130.26 C ANISOU 2471 CG2 THR B 16 18978 20571 9942 800 -4689 1552 C ATOM 2472 N SER B 17 99.736 29.618 194.002 1.00108.09 N ANISOU 2472 N SER B 17 14963 17578 8527 2946 -1873 36 N ATOM 2473 CA SER B 17 98.684 29.942 193.048 1.00122.37 C ANISOU 2473 CA SER B 17 15728 20558 10210 2818 -1810 -97 C ATOM 2474 C SER B 17 98.969 29.328 191.681 1.00129.88 C ANISOU 2474 C SER B 17 16239 21816 11293 2248 -1881 -201 C ATOM 2475 O SER B 17 98.140 28.596 191.140 1.00137.69 O ANISOU 2475 O SER B 17 16654 23548 12114 1600 -1475 -491 O ATOM 2476 CB SER B 17 98.522 31.457 192.925 1.00128.75 C ANISOU 2476 CB SER B 17 16183 21686 11051 3692 -2282 137 C ATOM 2477 OG SER B 17 98.151 32.027 194.168 1.00133.24 O ANISOU 2477 OG SER B 17 17090 22059 11479 4202 -2191 215 O ATOM 2478 N LYS B 18 100.139 29.629 191.124 1.00136.03 N ANISOU 2478 N LYS B 18 17278 22034 12374 2475 -2383 12 N ATOM 2479 CA LYS B 18 100.531 29.059 189.840 1.00136.08 C ANISOU 2479 CA LYS B 18 16937 22236 12530 1956 -2481 -66 C ATOM 2480 C LYS B 18 100.766 27.562 189.981 1.00132.98 C ANISOU 2480 C LYS B 18 16951 21467 12107 1132 -2043 -283 C ATOM 2481 O LYS B 18 101.281 27.098 191.001 1.00123.51 O ANISOU 2481 O LYS B 18 16591 19437 10902 1136 -1903 -260 O ATOM 2482 CB LYS B 18 101.787 29.742 189.291 1.00126.35 C ANISOU 2482 CB LYS B 18 15956 20420 11631 2391 -3100 194 C ATOM 2483 CG LYS B 18 103.034 29.557 190.141 1.00106.68 C ANISOU 2483 CG LYS B 18 14450 16743 9341 2582 -3275 312 C ATOM 2484 CD LYS B 18 104.291 29.687 189.296 1.00100.67 C ANISOU 2484 CD LYS B 18 13835 15500 8915 2615 -3743 418 C ATOM 2485 CE LYS B 18 104.311 28.644 188.188 1.00 96.31 C ANISOU 2485 CE LYS B 18 12918 15274 8402 1825 -3578 237 C ATOM 2486 NZ LYS B 18 105.523 28.753 187.331 1.00 89.26 N ANISOU 2486 NZ LYS B 18 12143 13938 7836 1828 -4019 320 N ATOM 2487 N ILE B 19 100.381 26.806 188.958 1.00128.39 N ANISOU 2487 N ILE B 19 15800 21495 11486 443 -1823 -500 N ATOM 2488 CA ILE B 19 100.518 25.357 189.003 1.00136.11 C ANISOU 2488 CA ILE B 19 17127 22182 12405 -389 -1361 -725 C ATOM 2489 C ILE B 19 100.421 24.717 187.616 1.00140.66 C ANISOU 2489 C ILE B 19 17064 23340 13041 -1046 -1309 -898 C ATOM 2490 O ILE B 19 99.336 24.586 187.046 1.00148.35 O ANISOU 2490 O ILE B 19 17219 25317 13828 -1397 -1025 -1134 O ATOM 2491 CB ILE B 19 99.457 24.733 189.950 1.00150.80 C ANISOU 2491 CB ILE B 19 19083 24288 13925 -765 -673 -978 C ATOM 2492 CG1 ILE B 19 99.449 23.205 189.832 1.00162.30 C ANISOU 2492 CG1 ILE B 19 20819 25572 15275 -1713 -120 -1250 C ATOM 2493 CG2 ILE B 19 98.076 25.340 189.702 1.00156.08 C ANISOU 2493 CG2 ILE B 19 18786 26142 14374 -676 -508 -1141 C ATOM 2494 CD1 ILE B 19 100.730 22.547 190.302 1.00158.96 C ANISOU 2494 CD1 ILE B 19 21460 23944 14992 -1745 -225 -1123 C ATOM 2495 N PRO B 20 101.577 24.343 187.051 1.00139.21 N ANISOU 2495 N PRO B 20 17230 22544 13120 -1192 -1605 -799 N ATOM 2496 CA PRO B 20 101.600 23.487 185.862 1.00123.31 C ANISOU 2496 CA PRO B 20 14782 20912 11160 -1922 -1484 -979 C ATOM 2497 C PRO B 20 101.350 22.033 186.255 1.00113.69 C ANISOU 2497 C PRO B 20 13946 19498 9755 -2749 -837 -1254 C ATOM 2498 O PRO B 20 102.080 21.483 187.080 1.00113.88 O ANISOU 2498 O PRO B 20 14897 18576 9795 -2764 -751 -1203 O ATOM 2499 CB PRO B 20 103.010 23.689 185.304 1.00120.76 C ANISOU 2499 CB PRO B 20 14814 19882 11187 -1694 -2047 -762 C ATOM 2500 CG PRO B 20 103.827 24.099 186.479 1.00131.80 C ANISOU 2500 CG PRO B 20 17104 20299 12675 -1094 -2270 -565 C ATOM 2501 CD PRO B 20 102.914 24.857 187.397 1.00140.63 C ANISOU 2501 CD PRO B 20 18121 21735 13576 -619 -2127 -523 C ATOM 2502 N VAL B 21 100.320 21.428 185.672 1.00121.57 N ANISOU 2502 N VAL B 21 14249 21385 10556 -3417 -377 -1562 N ATOM 2503 CA VAL B 21 99.871 20.099 186.076 1.00124.17 C ANISOU 2503 CA VAL B 21 14886 21640 10654 -4244 341 -1868 C ATOM 2504 C VAL B 21 100.925 19.019 185.822 1.00118.49 C ANISOU 2504 C VAL B 21 14845 20108 10068 -4723 370 -1864 C ATOM 2505 O VAL B 21 100.923 17.975 186.475 1.00114.47 O ANISOU 2505 O VAL B 21 15008 19108 9378 -5214 887 -2018 O ATOM 2506 CB VAL B 21 98.570 19.712 185.342 1.00138.36 C ANISOU 2506 CB VAL B 21 15680 24652 12236 -4894 803 -2248 C ATOM 2507 CG1 VAL B 21 97.842 18.604 186.091 1.00151.26 C ANISOU 2507 CG1 VAL B 21 17640 26273 13561 -5631 1637 -2589 C ATOM 2508 CG2 VAL B 21 97.668 20.927 185.193 1.00134.24 C ANISOU 2508 CG2 VAL B 21 14301 25070 11635 -4317 579 -2239 C ATOM 2509 N ALA B 22 101.830 19.278 184.884 1.00116.44 N ANISOU 2509 N ALA B 22 14443 19691 10108 -4565 -178 -1695 N ATOM 2510 CA ALA B 22 102.827 18.285 184.495 1.00106.41 C ANISOU 2510 CA ALA B 22 13706 17748 8978 -5013 -195 -1713 C ATOM 2511 C ALA B 22 104.203 18.567 185.093 1.00104.29 C ANISOU 2511 C ALA B 22 14348 16349 8929 -4413 -679 -1447 C ATOM 2512 O ALA B 22 105.218 18.109 184.566 1.00 89.66 O ANISOU 2512 O ALA B 22 12793 13995 7280 -4562 -929 -1412 O ATOM 2513 CB ALA B 22 102.922 18.210 182.979 1.00 93.84 C ANISOU 2513 CB ALA B 22 11338 16754 7564 -5361 -421 -1766 C ATOM 2514 N LEU B 23 104.239 19.314 186.191 1.00112.84 N ANISOU 2514 N LEU B 23 15854 17055 9966 -3733 -810 -1288 N ATOM 2515 CA LEU B 23 105.502 19.624 186.854 1.00104.08 C ANISOU 2515 CA LEU B 23 15593 14908 9044 -3123 -1261 -1080 C ATOM 2516 C LEU B 23 105.645 18.859 188.164 1.00110.07 C ANISOU 2516 C LEU B 23 17379 14876 9565 -3160 -875 -1145 C ATOM 2517 O LEU B 23 106.703 18.879 188.793 1.00104.10 O ANISOU 2517 O LEU B 23 17429 13212 8911 -2719 -1181 -1036 O ATOM 2518 CB LEU B 23 105.620 21.126 187.112 1.00 88.36 C ANISOU 2518 CB LEU B 23 13393 12975 7204 -2239 -1778 -834 C ATOM 2519 N LEU B 24 104.574 18.184 188.568 1.00133.83 N ANISOU 2519 N LEU B 24 17803 22061 10984 -4360 -479 -4401 N ATOM 2520 CA LEU B 24 104.576 17.417 189.807 1.00128.46 C ANISOU 2520 CA LEU B 24 17678 20606 10526 -4427 -729 -4438 C ATOM 2521 C LEU B 24 104.984 15.969 189.558 1.00130.15 C ANISOU 2521 C LEU B 24 18285 20178 10990 -4969 -788 -4991 C ATOM 2522 O LEU B 24 104.714 15.412 188.494 1.00145.37 O ANISOU 2522 O LEU B 24 19951 22471 12812 -5408 -604 -5116 O ATOM 2523 CB LEU B 24 103.197 17.466 190.467 1.00126.81 C ANISOU 2523 CB LEU B 24 17372 21083 9729 -4634 -729 -3900 C ATOM 2524 CG LEU B 24 102.623 18.858 190.741 1.00123.82 C ANISOU 2524 CG LEU B 24 16608 21390 9047 -4081 -628 -3255 C ATOM 2525 CD1 LEU B 24 101.254 18.755 191.396 1.00129.80 C ANISOU 2525 CD1 LEU B 24 17290 22819 9210 -4336 -639 -2759 C ATOM 2526 CD2 LEU B 24 103.575 19.672 191.604 1.00126.10 C ANISOU 2526 CD2 LEU B 24 17144 20842 9926 -3280 -750 -3190 C ATOM 2527 N ILE B 25 105.639 15.365 190.544 1.00117.64 N ANISOU 2527 N ILE B 25 17290 17553 9854 -4783 -999 -5192 N ATOM 2528 CA ILE B 25 106.047 13.968 190.451 1.00115.11 C ANISOU 2528 CA ILE B 25 17361 16458 9919 -5055 -1001 -5514 C ATOM 2529 C ILE B 25 105.417 13.162 191.586 1.00117.24 C ANISOU 2529 C ILE B 25 18119 16388 10040 -5306 -1084 -5382 C ATOM 2530 O ILE B 25 105.134 11.973 191.438 1.00125.78 O ANISOU 2530 O ILE B 25 19425 17223 11143 -5787 -961 -5520 O ATOM 2531 CB ILE B 25 107.591 13.825 190.478 1.00113.42 C ANISOU 2531 CB ILE B 25 17410 15231 10455 -4485 -1138 -5868 C ATOM 2532 CG1 ILE B 25 108.008 12.363 190.301 1.00127.57 C ANISOU 2532 CG1 ILE B 25 19561 16318 12592 -4685 -1115 -6129 C ATOM 2533 CG2 ILE B 25 108.174 14.412 191.759 1.00110.03 C ANISOU 2533 CG2 ILE B 25 17290 14225 10291 -3848 -1388 -5826 C ATOM 2534 CD1 ILE B 25 107.556 11.751 188.991 1.00127.87 C ANISOU 2534 CD1 ILE B 25 19311 16857 12417 -5290 -857 -6237 C ATOM 2535 N HIS B 26 105.179 13.829 192.712 1.00122.93 N ANISOU 2535 N HIS B 26 19000 17101 10608 -4954 -1257 -5076 N ATOM 2536 CA HIS B 26 104.563 13.199 193.873 1.00123.71 C ANISOU 2536 CA HIS B 26 19541 16880 10583 -5056 -1327 -4826 C ATOM 2537 C HIS B 26 104.057 14.260 194.843 1.00132.27 C ANISOU 2537 C HIS B 26 20461 18291 11504 -4500 -1450 -4220 C ATOM 2538 O HIS B 26 104.559 15.383 194.862 1.00109.30 O ANISOU 2538 O HIS B 26 17280 15466 8781 -3885 -1524 -4094 O ATOM 2539 CB HIS B 26 105.555 12.270 194.576 1.00117.35 C ANISOU 2539 CB HIS B 26 19441 14847 10299 -4804 -1456 -5173 C ATOM 2540 N TYR B 27 103.059 13.902 195.644 1.00136.57 N ANISOU 2540 N TYR B 27 21181 19004 11704 -4731 -1440 -3855 N ATOM 2541 CA TYR B 27 102.519 14.820 196.640 1.00139.12 C ANISOU 2541 CA TYR B 27 21399 19613 11846 -4217 -1552 -3266 C ATOM 2542 C TYR B 27 102.379 14.126 197.990 1.00143.59 C ANISOU 2542 C TYR B 27 22570 19490 12498 -4073 -1676 -3105 C ATOM 2543 O TYR B 27 102.157 12.917 198.057 1.00149.26 O ANISOU 2543 O TYR B 27 23688 19840 13184 -4603 -1571 -3302 O ATOM 2544 CB TYR B 27 101.169 15.381 196.185 1.00138.55 C ANISOU 2544 CB TYR B 27 20756 20792 11097 -4589 -1376 -2817 C ATOM 2545 CG TYR B 27 100.014 14.412 196.311 1.00138.16 C ANISOU 2545 CG TYR B 27 20802 21102 10589 -5368 -1240 -2718 C ATOM 2546 CD1 TYR B 27 99.814 13.411 195.369 1.00138.70 C ANISOU 2546 CD1 TYR B 27 20847 21330 10521 -6206 -1053 -3159 C ATOM 2547 CD2 TYR B 27 99.116 14.507 197.366 1.00135.33 C ANISOU 2547 CD2 TYR B 27 20550 20934 9935 -5289 -1274 -2204 C ATOM 2548 CE1 TYR B 27 98.757 12.526 195.480 1.00140.30 C ANISOU 2548 CE1 TYR B 27 21125 21859 10322 -6981 -887 -3122 C ATOM 2549 CE2 TYR B 27 98.057 13.628 197.485 1.00139.13 C ANISOU 2549 CE2 TYR B 27 21104 21745 10012 -6034 -1115 -2129 C ATOM 2550 CZ TYR B 27 97.882 12.640 196.540 1.00140.67 C ANISOU 2550 CZ TYR B 27 21268 22084 10095 -6898 -912 -2603 C ATOM 2551 OH TYR B 27 96.827 11.764 196.656 1.00145.78 O ANISOU 2551 OH TYR B 27 21977 23056 10357 -7701 -714 -2581 O ATOM 2552 N GLN B 28 102.511 14.898 199.064 1.00139.97 N ANISOU 2552 N GLN B 28 22192 18847 12143 -3347 -1868 -2752 N ATOM 2553 CA GLN B 28 102.433 14.346 200.411 1.00136.52 C ANISOU 2553 CA GLN B 28 22318 17775 11778 -3077 -2000 -2564 C ATOM 2554 C GLN B 28 101.280 14.950 201.203 1.00123.84 C ANISOU 2554 C GLN B 28 20554 16782 9716 -2966 -2002 -1911 C ATOM 2555 O GLN B 28 101.065 16.163 201.183 1.00112.98 O ANISOU 2555 O GLN B 28 18748 15981 8198 -2593 -2033 -1598 O ATOM 2556 CB GLN B 28 103.751 14.570 201.155 1.00137.63 C ANISOU 2556 CB GLN B 28 22783 17034 12477 -2236 -2267 -2792 C ATOM 2557 CG GLN B 28 104.950 13.882 200.521 1.00142.46 C ANISOU 2557 CG GLN B 28 23615 16961 13552 -2269 -2279 -3429 C ATOM 2558 CD GLN B 28 104.867 12.369 200.599 1.00147.21 C ANISOU 2558 CD GLN B 28 24791 16981 14161 -2747 -2144 -3643 C ATOM 2559 OE1 GLN B 28 104.160 11.816 201.441 1.00141.90 O ANISOU 2559 OE1 GLN B 28 24478 16174 13265 -2855 -2094 -3334 O ATOM 2560 NE2 GLN B 28 105.592 11.692 199.716 1.00151.58 N ANISOU 2560 NE2 GLN B 28 25456 17164 14976 -3032 -2049 -4173 N ATOM 2561 N GLN B 29 100.540 14.094 201.899 1.00117.91 N ANISOU 2561 N GLN B 29 20176 15887 8739 -3285 -1933 -1703 N ATOM 2562 CA GLN B 29 99.455 14.543 202.760 1.00114.00 C ANISOU 2562 CA GLN B 29 19595 15899 7820 -3170 -1936 -1081 C ATOM 2563 C GLN B 29 100.025 15.043 204.082 1.00119.74 C ANISOU 2563 C GLN B 29 20650 16033 8813 -2244 -2206 -875 C ATOM 2564 O GLN B 29 100.884 14.393 204.678 1.00121.36 O ANISOU 2564 O GLN B 29 21385 15321 9404 -1909 -2335 -1144 O ATOM 2565 CB GLN B 29 98.453 13.413 203.002 1.00119.01 C ANISOU 2565 CB GLN B 29 20506 16589 8126 -3895 -1722 -956 C ATOM 2566 CG GLN B 29 97.097 13.876 203.510 1.00124.84 C ANISOU 2566 CG GLN B 29 20968 18165 8301 -4015 -1650 -328 C ATOM 2567 CD GLN B 29 96.232 14.460 202.410 1.00130.08 C ANISOU 2567 CD GLN B 29 20886 20067 8472 -4519 -1486 -204 C ATOM 2568 OE1 GLN B 29 96.528 14.308 201.225 1.00142.23 O ANISOU 2568 OE1 GLN B 29 22150 21839 10051 -4932 -1386 -616 O ATOM 2569 NE2 GLN B 29 95.155 15.133 202.799 1.00128.57 N ANISOU 2569 NE2 GLN B 29 20356 20712 7783 -4452 -1450 375 N ATOM 2570 N ASN B 30 99.551 16.199 204.534 1.00104.79 N ANISOU 2570 N ASN B 30 11823 21073 6918 -502 -951 -507 N ATOM 2571 CA ASN B 30 100.037 16.790 205.776 1.00 96.65 C ANISOU 2571 CA ASN B 30 10471 20227 6026 -343 -938 -399 C ATOM 2572 C ASN B 30 99.687 15.928 206.985 1.00 93.93 C ANISOU 2572 C ASN B 30 9988 19895 5808 -305 -883 -341 C ATOM 2573 O ASN B 30 98.681 15.217 206.980 1.00 97.91 O ANISOU 2573 O ASN B 30 10575 20304 6323 -430 -943 -399 O ATOM 2574 CB ASN B 30 99.471 18.200 205.953 1.00 97.96 C ANISOU 2574 CB ASN B 30 10457 20349 6412 -384 -1123 -394 C ATOM 2575 CG ASN B 30 100.138 18.959 207.084 1.00 97.48 C ANISOU 2575 CG ASN B 30 10128 20400 6508 -263 -1061 -304 C ATOM 2576 OD1 ASN B 30 101.247 18.626 207.501 1.00 93.67 O ANISOU 2576 OD1 ASN B 30 9590 20030 5973 -144 -905 -225 O ATOM 2577 ND2 ASN B 30 99.464 19.988 207.584 1.00 89.18 N ANISOU 2577 ND2 ASN B 30 8916 19332 5636 -303 -1170 -308 N ATOM 2578 N GLN B 31 100.525 15.991 208.015 1.00 87.80 N ANISOU 2578 N GLN B 31 9003 19242 5115 -152 -772 -216 N ATOM 2579 CA GLN B 31 100.317 15.210 209.228 1.00102.56 C ANISOU 2579 CA GLN B 31 10738 21135 7094 -113 -715 -132 C ATOM 2580 C GLN B 31 99.017 15.596 209.927 1.00 98.24 C ANISOU 2580 C GLN B 31 10040 20678 6608 -248 -916 -188 C ATOM 2581 O GLN B 31 98.618 16.760 209.918 1.00 96.03 O ANISOU 2581 O GLN B 31 9646 20447 6394 -301 -1055 -230 O ATOM 2582 CB GLN B 31 101.498 15.383 210.185 1.00107.83 C ANISOU 2582 CB GLN B 31 11186 21970 7814 47 -600 40 C ATOM 2583 CG GLN B 31 102.827 14.900 209.626 1.00113.20 C ANISOU 2583 CG GLN B 31 11960 22571 8481 212 -370 135 C ATOM 2584 CD GLN B 31 102.860 13.398 209.409 1.00120.16 C ANISOU 2584 CD GLN B 31 13042 23201 9411 279 -159 164 C ATOM 2585 OE1 GLN B 31 102.129 12.648 210.057 1.00116.32 O ANISOU 2585 OE1 GLN B 31 12559 22655 8984 232 -173 173 O ATOM 2586 NE2 GLN B 31 103.710 12.952 208.491 1.00120.74 N ANISOU 2586 NE2 GLN B 31 13301 23111 9462 384 62 175 N ATOM 2587 N ALA B 32 98.362 14.609 210.529 1.00 87.55 N ANISOU 2587 N ALA B 32 8698 19251 5317 -295 -885 -182 N ATOM 2588 CA ALA B 32 97.099 14.835 211.220 1.00 87.04 C ANISOU 2588 CA ALA B 32 8488 19258 5326 -426 -1041 -234 C ATOM 2589 C ALA B 32 97.293 15.712 212.451 1.00100.76 C ANISOU 2589 C ALA B 32 9948 21209 7125 -389 -1070 -166 C ATOM 2590 O ALA B 32 96.432 16.523 212.786 1.00 97.47 O ANISOU 2590 O ALA B 32 9403 20786 6845 -473 -1169 -223 O ATOM 2591 CB ALA B 32 96.463 13.509 211.609 1.00 88.18 C ANISOU 2591 CB ALA B 32 8724 19269 5512 -494 -971 -239 C ATOM 2592 N SER B 33 98.438 15.552 213.109 1.00102.36 N ANISOU 2592 N SER B 33 10076 21497 7319 -268 -938 -32 N ATOM 2593 CA SER B 33 98.741 16.282 214.337 1.00 84.69 C ANISOU 2593 CA SER B 33 7612 19401 5165 -273 -929 44 C ATOM 2594 C SER B 33 98.810 17.792 214.123 1.00 83.62 C ANISOU 2594 C SER B 33 7411 19204 5158 -303 -961 -19 C ATOM 2595 O SER B 33 98.705 18.565 215.076 1.00 82.99 O ANISOU 2595 O SER B 33 7187 19176 5171 -364 -943 -13 O ATOM 2596 CB SER B 33 100.060 15.785 214.933 1.00 85.22 C ANISOU 2596 CB SER B 33 7608 19622 5152 -149 -809 236 C ATOM 2597 OG SER B 33 100.393 16.505 216.107 1.00105.62 O ANISOU 2597 OG SER B 33 9995 22302 7836 -203 -794 309 O ATOM 2598 N CYS B 34 98.990 18.207 212.874 1.00 95.24 N ANISOU 2598 N CYS B 34 9015 20568 6605 -272 -992 -80 N ATOM 2599 CA CYS B 34 99.063 19.626 212.541 1.00 92.55 C ANISOU 2599 CA CYS B 34 8646 20163 6358 -293 -1019 -129 C ATOM 2600 C CYS B 34 97.730 20.326 212.782 1.00 82.54 C ANISOU 2600 C CYS B 34 7309 18848 5205 -388 -1114 -215 C ATOM 2601 O CYS B 34 97.693 21.485 213.195 1.00 94.90 O ANISOU 2601 O CYS B 34 8783 20431 6844 -414 -1096 -233 O ATOM 2602 CB CYS B 34 99.495 19.812 211.085 1.00 83.17 C ANISOU 2602 CB CYS B 34 7638 18870 5095 -251 -1040 -165 C ATOM 2603 SG CYS B 34 101.161 19.216 210.703 1.00 93.85 S ANISOU 2603 SG CYS B 34 9053 20309 6298 -117 -893 -62 S ATOM 2604 N GLY B 35 96.637 19.617 212.520 1.00 83.20 N ANISOU 2604 N GLY B 35 7433 18894 5286 -447 -1210 -265 N ATOM 2605 CA GLY B 35 95.308 20.168 212.713 1.00 83.33 C ANISOU 2605 CA GLY B 35 7347 18901 5413 -528 -1309 -326 C ATOM 2606 C GLY B 35 94.954 21.222 211.682 1.00 83.48 C ANISOU 2606 C GLY B 35 7410 18829 5480 -524 -1410 -355 C ATOM 2607 O GLY B 35 93.999 21.978 211.857 1.00 92.29 O ANISOU 2607 O GLY B 35 8404 19967 6697 -556 -1481 -377 O ATOM 2608 N LYS B 36 95.727 21.270 210.602 1.00 83.58 N ANISOU 2608 N LYS B 36 7592 18753 5410 -481 -1414 -345 N ATOM 2609 CA LYS B 36 95.494 22.235 209.534 1.00 83.90 C ANISOU 2609 CA LYS B 36 7705 18704 5470 -484 -1517 -354 C ATOM 2610 C LYS B 36 95.506 21.552 208.171 1.00 91.23 C ANISOU 2610 C LYS B 36 8858 19527 6278 -531 -1605 -369 C ATOM 2611 O LYS B 36 96.516 20.979 207.762 1.00 98.48 O ANISOU 2611 O LYS B 36 9925 20425 7067 -496 -1512 -371 O ATOM 2612 CB LYS B 36 96.544 23.347 209.577 1.00 83.05 C ANISOU 2612 CB LYS B 36 7596 18600 5361 -415 -1419 -336 C ATOM 2613 N ARG B 37 94.376 21.617 207.474 1.00 91.93 N ANISOU 2613 N ARG B 37 8969 19567 6394 -624 -1782 -373 N ATOM 2614 CA ARG B 37 94.241 20.985 206.167 1.00 91.55 C ANISOU 2614 CA ARG B 37 9156 19425 6205 -728 -1884 -392 C ATOM 2615 C ARG B 37 95.094 21.685 205.114 1.00 95.71 C ANISOU 2615 C ARG B 37 9860 19863 6645 -696 -1874 -383 C ATOM 2616 O ARG B 37 94.813 22.819 204.727 1.00107.66 O ANISOU 2616 O ARG B 37 11331 21347 8229 -682 -1969 -340 O ATOM 2617 CB ARG B 37 92.775 20.973 205.729 1.00 89.03 C ANISOU 2617 CB ARG B 37 8783 19098 5948 -861 -2101 -370 C ATOM 2618 N ALA B 38 96.138 21.001 204.657 1.00 93.27 N ANISOU 2618 N ALA B 38 9747 19522 6169 -683 -1749 -419 N ATOM 2619 CA ALA B 38 97.024 21.538 203.631 1.00 96.04 C ANISOU 2619 CA ALA B 38 10286 19793 6413 -667 -1713 -422 C ATOM 2620 C ALA B 38 97.675 20.410 202.836 1.00 91.58 C ANISOU 2620 C ALA B 38 9997 19185 5614 -723 -1610 -483 C ATOM 2621 O ALA B 38 97.883 19.314 203.355 1.00 98.16 O ANISOU 2621 O ALA B 38 10840 20079 6375 -703 -1493 -508 O ATOM 2622 CB ALA B 38 98.085 22.428 204.257 1.00 98.42 C ANISOU 2622 CB ALA B 38 10460 20144 6791 -523 -1571 -390 C ATOM 2623 N ILE B 39 97.992 20.683 201.575 1.00 90.11 N ANISOU 2623 N ILE B 39 10052 18895 5289 -799 -1637 -506 N ATOM 2624 CA ILE B 39 98.605 19.683 200.708 1.00105.31 C ANISOU 2624 CA ILE B 39 12289 20766 6960 -875 -1504 -583 C ATOM 2625 C ILE B 39 100.042 20.060 200.362 1.00 99.51 C ANISOU 2625 C ILE B 39 11637 20026 6145 -758 -1306 -584 C ATOM 2626 O ILE B 39 100.323 21.201 199.996 1.00101.64 O ANISOU 2626 O ILE B 39 11885 20256 6477 -734 -1362 -549 O ATOM 2627 CB ILE B 39 97.802 19.498 199.403 1.00107.94 C ANISOU 2627 CB ILE B 39 12896 20974 7140 -1115 -1671 -625 C ATOM 2628 CG1 ILE B 39 96.335 19.196 199.714 1.00109.47 C ANISOU 2628 CG1 ILE B 39 12970 21196 7428 -1246 -1887 -602 C ATOM 2629 CG2 ILE B 39 98.407 18.390 198.553 1.00106.76 C ANISOU 2629 CG2 ILE B 39 13114 20751 6697 -1229 -1483 -733 C ATOM 2630 CD1 ILE B 39 96.127 17.924 200.506 1.00103.08 C ANISOU 2630 CD1 ILE B 39 12133 20456 6576 -1263 -1783 -656 C ATOM 2631 N ILE B 40 100.948 19.096 200.487 1.00 91.73 N ANISOU 2631 N ILE B 40 10744 19091 5018 -681 -1060 -615 N ATOM 2632 CA ILE B 40 102.349 19.313 200.151 1.00 99.30 C ANISOU 2632 CA ILE B 40 11768 20069 5893 -565 -838 -606 C ATOM 2633 C ILE B 40 102.660 18.767 198.762 1.00107.56 C ANISOU 2633 C ILE B 40 13217 20978 6671 -700 -709 -709 C ATOM 2634 O ILE B 40 102.503 17.573 198.506 1.00109.87 O ANISOU 2634 O ILE B 40 13726 21232 6788 -778 -571 -785 O ATOM 2635 CB ILE B 40 103.283 18.650 201.177 1.00 95.64 C ANISOU 2635 CB ILE B 40 11123 19772 5444 -359 -601 -538 C ATOM 2636 CG1 ILE B 40 102.862 19.026 202.599 1.00 91.75 C ANISOU 2636 CG1 ILE B 40 10272 19402 5187 -278 -727 -449 C ATOM 2637 CG2 ILE B 40 104.729 19.042 200.912 1.00 91.50 C ANISOU 2637 CG2 ILE B 40 10588 19302 4875 -228 -387 -495 C ATOM 2638 CD1 ILE B 40 103.619 18.280 203.674 1.00108.75 C ANISOU 2638 CD1 ILE B 40 12241 21734 7345 -103 -538 -349 C ATOM 2639 N LEU B 41 103.100 19.645 197.868 1.00 98.65 N ANISOU 2639 N LEU B 41 12216 19765 5502 -746 -730 -719 N ATOM 2640 CA LEU B 41 103.394 19.253 196.494 1.00106.64 C ANISOU 2640 CA LEU B 41 13637 20626 6256 -905 -606 -822 C ATOM 2641 C LEU B 41 104.893 19.240 196.218 1.00110.09 C ANISOU 2641 C LEU B 41 14141 21087 6602 -769 -274 -832 C ATOM 2642 O LEU B 41 105.572 20.254 196.382 1.00 95.87 O ANISOU 2642 O LEU B 41 12166 19345 4915 -661 -285 -763 O ATOM 2643 CB LEU B 41 102.695 20.192 195.509 1.00 97.13 C ANISOU 2643 CB LEU B 41 12576 19291 5036 -1091 -878 -819 C ATOM 2644 CG LEU B 41 101.173 20.306 195.619 1.00113.33 C ANISOU 2644 CG LEU B 41 14548 21325 7185 -1229 -1210 -781 C ATOM 2645 CD1 LEU B 41 100.630 21.250 194.557 1.00 98.20 C ANISOU 2645 CD1 LEU B 41 12774 19301 5236 -1383 -1450 -743 C ATOM 2646 CD2 LEU B 41 100.522 18.938 195.507 1.00120.67 C ANISOU 2646 CD2 LEU B 41 15665 22222 7964 -1393 -1176 -867 C ATOM 2647 N GLU B 42 105.404 18.088 195.797 1.00113.67 N ANISOU 2647 N GLU B 42 14848 21486 6853 -780 51 -918 N ATOM 2648 CA GLU B 42 106.804 17.972 195.406 1.00104.21 C ANISOU 2648 CA GLU B 42 13735 20242 5620 -646 423 -922 C ATOM 2649 C GLU B 42 106.930 18.001 193.889 1.00105.28 C ANISOU 2649 C GLU B 42 14323 20203 5476 -880 521 -1062 C ATOM 2650 O GLU B 42 106.551 17.049 193.206 1.00113.65 O ANISOU 2650 O GLU B 42 15746 21039 6398 -1058 653 -1181 O ATOM 2651 CB GLU B 42 107.426 16.689 195.962 1.00105.10 C ANISOU 2651 CB GLU B 42 13817 20200 5915 -442 794 -880 C ATOM 2652 CG GLU B 42 108.921 16.572 195.704 1.00109.54 C ANISOU 2652 CG GLU B 42 14376 20700 6543 -248 1197 -834 C ATOM 2653 CD GLU B 42 109.504 15.268 196.211 1.00122.04 C ANISOU 2653 CD GLU B 42 15929 22107 8335 -25 1579 -760 C ATOM 2654 OE1 GLU B 42 110.716 15.235 196.513 1.00120.51 O ANISOU 2654 OE1 GLU B 42 15528 21956 8304 221 1851 -629 O ATOM 2655 OE2 GLU B 42 108.753 14.274 196.302 1.00135.29 O ANISOU 2655 OE2 GLU B 42 17783 23604 10019 -99 1612 -818 O ATOM 2656 N THR B 43 107.463 19.100 193.366 1.00112.20 N ANISOU 2656 N THR B 43 15197 21059 6376 -886 459 -1035 N ATOM 2657 CA THR B 43 107.624 19.264 191.928 1.00120.35 C ANISOU 2657 CA THR B 43 16653 21879 7196 -1103 530 -1144 C ATOM 2658 C THR B 43 108.736 18.370 191.388 1.00123.35 C ANISOU 2658 C THR B 43 17286 22165 7415 -1061 1055 -1244 C ATOM 2659 O THR B 43 109.434 17.702 192.150 1.00125.25 O ANISOU 2659 O THR B 43 17325 22426 7838 -807 1347 -1182 O ATOM 2660 CB THR B 43 107.934 20.727 191.560 1.00112.75 C ANISOU 2660 CB THR B 43 15609 20923 6306 -1105 340 -1077 C ATOM 2661 OG1 THR B 43 109.199 21.105 192.118 1.00102.20 O ANISOU 2661 OG1 THR B 43 14010 19736 5084 -873 568 -1007 O ATOM 2662 CG2 THR B 43 106.852 21.653 192.096 1.00101.03 C ANISOU 2662 CG2 THR B 43 13875 19500 5013 -1122 -109 -973 C ATOM 2663 N ARG B 44 108.898 18.367 190.068 1.00119.91 N ANISOU 2663 N ARG B 44 17285 21502 6774 -1280 1174 -1365 N ATOM 2664 CA ARG B 44 109.972 17.614 189.430 1.00124.11 C ANISOU 2664 CA ARG B 44 18098 21883 7175 -1259 1720 -1475 C ATOM 2665 C ARG B 44 111.322 18.261 189.724 1.00129.48 C ANISOU 2665 C ARG B 44 18490 22714 7992 -998 1942 -1378 C ATOM 2666 O ARG B 44 112.375 17.664 189.502 1.00130.07 O ANISOU 2666 O ARG B 44 18637 22625 8158 -851 2415 -1394 O ATOM 2667 CB ARG B 44 109.744 17.523 187.919 1.00114.63 C ANISOU 2667 CB ARG B 44 17447 20373 5733 -1583 1762 -1626 C ATOM 2668 N GLN B 45 111.273 19.490 190.228 1.00135.02 N ANISOU 2668 N GLN B 45 18858 23601 8844 -920 1586 -1248 N ATOM 2669 CA GLN B 45 112.469 20.234 190.597 1.00128.74 C ANISOU 2669 CA GLN B 45 17756 22971 8188 -712 1724 -1141 C ATOM 2670 C GLN B 45 112.879 19.916 192.032 1.00127.67 C ANISOU 2670 C GLN B 45 17128 23095 8284 -407 1796 -983 C ATOM 2671 O GLN B 45 113.767 20.563 192.588 1.00140.68 O ANISOU 2671 O GLN B 45 18437 24942 10073 -238 1838 -858 O ATOM 2672 CB GLN B 45 112.225 21.735 190.438 1.00123.74 C ANISOU 2672 CB GLN B 45 17038 22364 7614 -806 1330 -1083 C ATOM 2673 CG GLN B 45 111.440 22.100 189.187 1.00106.87 C ANISOU 2673 CG GLN B 45 15328 19990 5289 -1095 1115 -1180 C ATOM 2674 CD GLN B 45 110.763 23.452 189.297 1.00104.87 C ANISOU 2674 CD GLN B 45 14930 19771 5146 -1151 663 -1086 C ATOM 2675 OE1 GLN B 45 111.130 24.277 190.133 1.00128.35 O ANISOU 2675 OE1 GLN B 45 17546 22908 8313 -1002 575 -981 O ATOM 2676 NE2 GLN B 45 109.761 23.682 188.457 1.00105.79 N ANISOU 2676 NE2 GLN B 45 15319 19731 5146 -1368 391 -1115 N ATOM 2677 N HIS B 46 112.221 18.917 192.616 1.00124.43 N ANISOU 2677 N HIS B 46 16693 22588 7995 -350 1785 -970 N ATOM 2678 CA HIS B 46 112.427 18.530 194.011 1.00125.15 C ANISOU 2678 CA HIS B 46 16347 22816 8387 -77 1791 -794 C ATOM 2679 C HIS B 46 112.229 19.706 194.963 1.00121.75 C ANISOU 2679 C HIS B 46 15516 22722 8021 -40 1416 -677 C ATOM 2680 O HIS B 46 113.000 19.893 195.904 1.00136.27 O ANISOU 2680 O HIS B 46 16966 24756 10052 165 1476 -514 O ATOM 2681 CB HIS B 46 113.820 17.924 194.209 1.00136.88 C ANISOU 2681 CB HIS B 46 17676 24250 10083 196 2253 -678 C ATOM 2682 CG HIS B 46 113.896 16.465 193.876 1.00154.43 C ANISOU 2682 CG HIS B 46 20166 26133 12378 265 2649 -729 C ATOM 2683 ND1 HIS B 46 113.723 15.983 192.598 1.00167.10 N ANISOU 2683 ND1 HIS B 46 22296 27429 13765 56 2875 -936 N ATOM 2684 CD2 HIS B 46 114.125 15.385 194.660 1.00156.94 C ANISOU 2684 CD2 HIS B 46 20319 26357 12954 507 2873 -598 C ATOM 2685 CE1 HIS B 46 113.843 14.666 192.607 1.00171.65 C ANISOU 2685 CE1 HIS B 46 23033 27718 14468 166 3246 -946 C ATOM 2686 NE2 HIS B 46 114.087 14.279 193.844 1.00168.11 N ANISOU 2686 NE2 HIS B 46 22166 27389 14319 454 3251 -734 N ATOM 2687 N ARG B 47 111.189 20.493 194.710 1.00128.49 N ANISOU 2687 N ARG B 47 16469 23582 8767 -248 1030 -746 N ATOM 2688 CA ARG B 47 110.851 21.619 195.573 1.00 97.54 C ANISOU 2688 CA ARG B 47 12223 19792 5048 -230 683 -646 C ATOM 2689 C ARG B 47 109.469 21.425 196.187 1.00 96.21 C ANISOU 2689 C ARG B 47 11989 19608 4959 -292 377 -647 C ATOM 2690 O ARG B 47 108.516 21.074 195.492 1.00 97.05 O ANISOU 2690 O ARG B 47 12378 19547 4949 -467 257 -744 O ATOM 2691 CB ARG B 47 110.906 22.933 194.792 1.00 97.21 C ANISOU 2691 CB ARG B 47 12303 19641 4989 -376 517 -679 C ATOM 2692 N LEU B 48 109.368 21.652 197.492 1.00 94.37 N ANISOU 2692 N LEU B 48 11380 19552 4923 -167 256 -534 N ATOM 2693 CA LEU B 48 108.106 21.480 198.202 1.00 93.14 C ANISOU 2693 CA LEU B 48 11122 19393 4874 -210 0 -527 C ATOM 2694 C LEU B 48 107.311 22.781 198.252 1.00100.08 C ANISOU 2694 C LEU B 48 11928 20201 5897 -316 -315 -521 C ATOM 2695 O LEU B 48 107.880 23.862 198.405 1.00107.27 O ANISOU 2695 O LEU B 48 12707 21154 6897 -291 -334 -476 O ATOM 2696 CB LEU B 48 108.357 20.965 199.621 1.00 94.83 C ANISOU 2696 CB LEU B 48 10994 19821 5216 -31 62 -408 C ATOM 2697 CG LEU B 48 109.027 19.595 199.736 1.00 98.41 C ANISOU 2697 CG LEU B 48 11481 20319 5592 123 395 -367 C ATOM 2698 CD1 LEU B 48 109.258 19.231 201.195 1.00 93.08 C ANISOU 2698 CD1 LEU B 48 10440 19803 5125 294 407 -201 C ATOM 2699 CD2 LEU B 48 108.191 18.532 199.042 1.00 95.41 C ANISOU 2699 CD2 LEU B 48 11445 19668 5139 8 441 -490 C ATOM 2700 N PHE B 49 105.993 22.669 198.121 1.00 99.00 N ANISOU 2700 N PHE B 49 11876 19961 5781 -434 -538 -557 N ATOM 2701 CA PHE B 49 105.116 23.834 198.157 1.00105.01 C ANISOU 2701 CA PHE B 49 12561 20655 6683 -507 -804 -529 C ATOM 2702 C PHE B 49 103.778 23.515 198.815 1.00107.55 C ANISOU 2702 C PHE B 49 12758 20983 7124 -539 -997 -515 C ATOM 2703 O PHE B 49 103.244 22.417 198.661 1.00108.74 O ANISOU 2703 O PHE B 49 13027 21111 7178 -602 -998 -560 O ATOM 2704 CB PHE B 49 104.884 24.375 196.746 1.00 91.88 C ANISOU 2704 CB PHE B 49 11209 18822 4881 -662 -902 -572 C ATOM 2705 CG PHE B 49 106.073 25.084 196.164 1.00 99.83 C ANISOU 2705 CG PHE B 49 12305 19813 5814 -643 -753 -576 C ATOM 2706 CD1 PHE B 49 106.361 26.390 196.526 1.00 97.68 C ANISOU 2706 CD1 PHE B 49 11866 19573 5675 -599 -810 -519 C ATOM 2707 CD2 PHE B 49 106.899 24.449 195.253 1.00111.83 C ANISOU 2707 CD2 PHE B 49 14090 21279 7120 -682 -531 -647 C ATOM 2708 CE1 PHE B 49 107.453 27.048 195.993 1.00103.97 C ANISOU 2708 CE1 PHE B 49 12746 20360 6399 -600 -675 -525 C ATOM 2709 CE2 PHE B 49 107.993 25.101 194.715 1.00114.05 C ANISOU 2709 CE2 PHE B 49 14446 21551 7339 -671 -382 -651 C ATOM 2710 CZ PHE B 49 108.271 26.403 195.086 1.00110.09 C ANISOU 2710 CZ PHE B 49 13763 21092 6975 -634 -468 -588 C ATOM 2711 N CYS B 50 103.241 24.487 199.548 1.00 99.62 N ANISOU 2711 N CYS B 50 11526 20009 6317 -506 -1137 -458 N ATOM 2712 CA CYS B 50 101.953 24.329 200.213 1.00 94.49 C ANISOU 2712 CA CYS B 50 10730 19374 5797 -530 -1304 -438 C ATOM 2713 C CYS B 50 100.800 24.597 199.253 1.00 96.78 C ANISOU 2713 C CYS B 50 11180 19546 6047 -674 -1534 -435 C ATOM 2714 O CYS B 50 100.817 25.575 198.506 1.00 98.42 O ANISOU 2714 O CYS B 50 11486 19680 6228 -714 -1618 -408 O ATOM 2715 CB CYS B 50 101.852 25.264 201.419 1.00103.95 C ANISOU 2715 CB CYS B 50 11633 20661 7204 -442 -1317 -384 C ATOM 2716 SG CYS B 50 103.053 24.951 202.732 1.00111.44 S ANISOU 2716 SG CYS B 50 12347 21783 8214 -312 -1096 -352 S ATOM 2717 N ALA B 51 99.796 23.727 199.283 1.00 99.07 N ANISOU 2717 N ALA B 51 11487 19831 6324 -761 -1643 -451 N ATOM 2718 CA ALA B 51 98.627 23.876 198.424 1.00 91.81 C ANISOU 2718 CA ALA B 51 10684 18832 5369 -918 -1886 -423 C ATOM 2719 C ALA B 51 97.337 23.654 199.208 1.00 98.77 C ANISOU 2719 C ALA B 51 11338 19780 6409 -934 -2037 -383 C ATOM 2720 O ALA B 51 97.215 22.685 199.957 1.00105.52 O ANISOU 2720 O ALA B 51 12113 20698 7283 -920 -1959 -424 O ATOM 2721 CB ALA B 51 98.705 22.914 197.250 1.00 93.87 C ANISOU 2721 CB ALA B 51 11293 18999 5375 -1095 -1873 -497 C ATOM 2722 N ASP B 52 96.379 24.557 199.031 1.00100.32 N ANISOU 2722 N ASP B 52 11427 19975 6716 -959 -2248 -293 N ATOM 2723 CA ASP B 52 95.095 24.456 199.715 1.00101.50 C ANISOU 2723 CA ASP B 52 11339 20201 7027 -973 -2393 -240 C ATOM 2724 C ASP B 52 94.261 23.313 199.144 1.00103.58 C ANISOU 2724 C ASP B 52 11733 20441 7182 -1172 -2523 -262 C ATOM 2725 O ASP B 52 93.975 23.287 197.949 1.00 96.36 O ANISOU 2725 O ASP B 52 11034 19453 6126 -1333 -2669 -237 O ATOM 2726 CB ASP B 52 94.328 25.776 199.611 1.00106.45 C ANISOU 2726 CB ASP B 52 11805 20854 7789 -931 -2573 -117 C ATOM 2727 CG ASP B 52 92.976 25.720 200.293 1.00121.22 C ANISOU 2727 CG ASP B 52 13401 22820 9837 -936 -2715 -49 C ATOM 2728 OD1 ASP B 52 92.922 25.906 201.527 1.00126.77 O ANISOU 2728 OD1 ASP B 52 13867 23613 10687 -815 -2602 -68 O ATOM 2729 OD2 ASP B 52 91.967 25.495 199.593 1.00125.65 O ANISOU 2729 OD2 ASP B 52 13980 23375 10386 -1075 -2938 27 O ATOM 2730 N PRO B 53 93.865 22.364 200.005 1.00111.04 N ANISOU 2730 N PRO B 53 12559 21454 8175 -1183 -2471 -308 N ATOM 2731 CA PRO B 53 93.115 21.172 199.589 1.00110.22 C ANISOU 2731 CA PRO B 53 12587 21340 7951 -1395 -2564 -348 C ATOM 2732 C PRO B 53 91.710 21.492 199.082 1.00110.33 C ANISOU 2732 C PRO B 53 12508 21373 8038 -1542 -2855 -240 C ATOM 2733 O PRO B 53 91.119 20.681 198.369 1.00109.51 O ANISOU 2733 O PRO B 53 12572 21244 7792 -1774 -2971 -259 O ATOM 2734 CB PRO B 53 93.050 20.337 200.871 1.00110.34 C ANISOU 2734 CB PRO B 53 12434 21447 8045 -1328 -2429 -403 C ATOM 2735 CG PRO B 53 93.160 21.333 201.971 1.00109.42 C ANISOU 2735 CG PRO B 53 12012 21404 8157 -1117 -2372 -348 C ATOM 2736 CD PRO B 53 94.094 22.390 201.460 1.00105.03 C ANISOU 2736 CD PRO B 53 11540 20790 7576 -1015 -2318 -324 C ATOM 2737 N LYS B 54 91.188 22.659 199.444 1.00110.34 N ANISOU 2737 N LYS B 54 12244 21430 8250 -1416 -2964 -121 N ATOM 2738 CA LYS B 54 89.844 23.053 199.037 1.00 99.71 C ANISOU 2738 CA LYS B 54 10747 20131 7008 -1517 -3241 21 C ATOM 2739 C LYS B 54 89.854 23.834 197.726 1.00121.86 C ANISOU 2739 C LYS B 54 13718 22869 9715 -1588 -3416 122 C ATOM 2740 O LYS B 54 89.083 24.777 197.549 1.00129.43 O ANISOU 2740 O LYS B 54 14485 23878 10814 -1546 -3609 285 O ATOM 2741 CB LYS B 54 89.175 23.883 200.135 1.00 98.87 C ANISOU 2741 CB LYS B 54 10248 20138 7181 -1340 -3260 110 C ATOM 2742 N GLU B 55 90.733 23.439 196.810 1.00120.26 N ANISOU 2742 N GLU B 55 13872 22557 9266 -1692 -3340 33 N ATOM 2743 CA GLU B 55 90.801 24.066 195.495 1.00118.54 C ANISOU 2743 CA GLU B 55 13861 22266 8912 -1792 -3495 114 C ATOM 2744 C GLU B 55 90.371 23.085 194.411 1.00116.40 C ANISOU 2744 C GLU B 55 13869 21949 8408 -2102 -3619 83 C ATOM 2745 O GLU B 55 90.522 21.872 194.562 1.00119.55 O ANISOU 2745 O GLU B 55 14414 22329 8681 -2225 -3493 -56 O ATOM 2746 CB GLU B 55 92.214 24.582 195.212 1.00116.66 C ANISOU 2746 CB GLU B 55 13827 21937 8561 -1677 -3296 39 C ATOM 2747 CG GLU B 55 92.690 25.685 196.149 1.00118.81 C ANISOU 2747 CG GLU B 55 13857 22257 9028 -1411 -3179 74 C ATOM 2748 CD GLU B 55 92.137 27.054 195.789 1.00116.40 C ANISOU 2748 CD GLU B 55 13419 21981 8826 -1347 -3380 252 C ATOM 2749 OE1 GLU B 55 91.282 27.141 194.883 1.00127.86 O ANISOU 2749 OE1 GLU B 55 14916 23432 10234 -1494 -3636 376 O ATOM 2750 OE2 GLU B 55 92.565 28.048 196.413 1.00103.41 O ANISOU 2750 OE2 GLU B 55 11625 20370 7295 -1157 -3280 276 O ATOM 2751 N GLN B 56 89.837 23.617 193.317 1.00120.51 N ANISOU 2751 N GLN B 56 14472 22459 8859 -2238 -3860 216 N ATOM 2752 CA GLN B 56 89.343 22.788 192.224 1.00112.60 C ANISOU 2752 CA GLN B 56 13730 21430 7624 -2569 -3998 203 C ATOM 2753 C GLN B 56 90.483 22.160 191.428 1.00130.38 C ANISOU 2753 C GLN B 56 16430 23542 9565 -2697 -3788 24 C ATOM 2754 O GLN B 56 90.343 21.063 190.888 1.00142.55 O ANISOU 2754 O GLN B 56 18229 25043 10889 -2968 -3759 -80 O ATOM 2755 CB GLN B 56 88.449 23.611 191.295 1.00115.71 C ANISOU 2755 CB GLN B 56 14056 21875 8035 -2673 -4324 423 C ATOM 2756 N TRP B 57 91.611 22.859 191.359 1.00124.02 N ANISOU 2756 N TRP B 57 15721 22664 8739 -2514 -3625 -15 N ATOM 2757 CA TRP B 57 92.750 22.390 190.577 1.00128.62 C ANISOU 2757 CA TRP B 57 16712 23115 9043 -2612 -3404 -172 C ATOM 2758 C TRP B 57 93.587 21.365 191.337 1.00124.50 C ANISOU 2758 C TRP B 57 16269 22563 8473 -2539 -3080 -360 C ATOM 2759 O TRP B 57 94.242 20.518 190.729 1.00128.55 O ANISOU 2759 O TRP B 57 17135 22974 8732 -2690 -2884 -508 O ATOM 2760 CB TRP B 57 93.626 23.570 190.150 1.00129.58 C ANISOU 2760 CB TRP B 57 16901 23179 9155 -2458 -3358 -128 C ATOM 2761 CG TRP B 57 94.112 24.413 191.289 1.00126.62 C ANISOU 2761 CG TRP B 57 16225 22855 9028 -2137 -3248 -95 C ATOM 2762 CD1 TRP B 57 93.485 25.495 191.834 1.00123.05 C ANISOU 2762 CD1 TRP B 57 15445 22489 8819 -1976 -3415 66 C ATOM 2763 CD2 TRP B 57 95.334 24.249 192.018 1.00123.54 C ANISOU 2763 CD2 TRP B 57 15836 22445 8657 -1952 -2933 -223 C ATOM 2764 NE1 TRP B 57 94.238 26.013 192.859 1.00119.50 N ANISOU 2764 NE1 TRP B 57 14815 22066 8524 -1725 -3215 29 N ATOM 2765 CE2 TRP B 57 95.379 25.265 192.993 1.00124.24 C ANISOU 2765 CE2 TRP B 57 15597 22610 8998 -1707 -2931 -140 C ATOM 2766 CE3 TRP B 57 96.393 23.338 191.944 1.00120.16 C ANISOU 2766 CE3 TRP B 57 15647 21954 8055 -1974 -2643 -391 C ATOM 2767 CZ2 TRP B 57 96.441 25.398 193.885 1.00132.58 C ANISOU 2767 CZ2 TRP B 57 16552 23688 10135 -1505 -2668 -217 C ATOM 2768 CZ3 TRP B 57 97.447 23.473 192.829 1.00128.69 C ANISOU 2768 CZ3 TRP B 57 16599 23067 9230 -1745 -2388 -447 C ATOM 2769 CH2 TRP B 57 97.463 24.494 193.787 1.00135.69 C ANISOU 2769 CH2 TRP B 57 17150 24036 10368 -1524 -2413 -359 C ATOM 2770 N VAL B 58 93.564 21.443 192.664 1.00110.51 N ANISOU 2770 N VAL B 58 10739 21902 9348 -4746 -331 4224 N ATOM 2771 CA VAL B 58 94.306 20.502 193.497 1.00104.30 C ANISOU 2771 CA VAL B 58 10535 20046 9049 -4983 -65 3966 C ATOM 2772 C VAL B 58 93.723 19.099 193.379 1.00112.31 C ANISOU 2772 C VAL B 58 11221 21272 10182 -5979 57 3523 C ATOM 2773 O VAL B 58 94.458 18.117 193.265 1.00116.15 O ANISOU 2773 O VAL B 58 12001 21334 10796 -6394 167 3073 O ATOM 2774 CB VAL B 58 94.307 20.936 194.976 1.00102.64 C ANISOU 2774 CB VAL B 58 10753 18728 9517 -4401 146 4189 C ATOM 2775 CG1 VAL B 58 94.955 19.871 195.848 1.00105.27 C ANISOU 2775 CG1 VAL B 58 11633 18077 10289 -4557 474 3935 C ATOM 2776 CG2 VAL B 58 95.026 22.262 195.132 1.00 87.46 C ANISOU 2776 CG2 VAL B 58 9085 16404 7743 -3570 85 4344 C ATOM 2777 N LYS B 59 92.396 19.013 193.397 1.00105.40 N ANISOU 2777 N LYS B 59 9677 20908 9462 -6310 -4 3505 N ATOM 2778 CA LYS B 59 91.708 17.736 193.249 1.00117.48 C ANISOU 2778 CA LYS B 59 10740 22385 11514 -7145 -19 2808 C ATOM 2779 C LYS B 59 91.987 17.127 191.878 1.00124.85 C ANISOU 2779 C LYS B 59 11475 23884 12078 -7343 -486 1897 C ATOM 2780 O LYS B 59 92.026 15.906 191.727 1.00141.80 O ANISOU 2780 O LYS B 59 13615 25566 14697 -7905 -521 1129 O ATOM 2781 CB LYS B 59 90.202 17.909 193.455 1.00119.93 C ANISOU 2781 CB LYS B 59 10368 23100 12101 -7223 -78 2881 C ATOM 2782 N ASP B 60 92.183 17.987 190.884 1.00119.85 N ANISOU 2782 N ASP B 60 10699 24246 10595 -6818 -825 1999 N ATOM 2783 CA ASP B 60 92.509 17.540 189.536 1.00127.02 C ANISOU 2783 CA ASP B 60 11452 25844 10964 -6788 -1275 1204 C ATOM 2784 C ASP B 60 93.990 17.195 189.424 1.00125.97 C ANISOU 2784 C ASP B 60 12092 25091 10681 -6623 -1128 1101 C ATOM 2785 O ASP B 60 94.387 16.382 188.589 1.00133.43 O ANISOU 2785 O ASP B 60 13064 26201 11431 -6752 -1404 292 O ATOM 2786 CB ASP B 60 92.137 18.611 188.508 1.00128.33 C ANISOU 2786 CB ASP B 60 11180 27382 10199 -6153 -1620 1448 C ATOM 2787 CG ASP B 60 90.649 18.904 188.483 1.00135.33 C ANISOU 2787 CG ASP B 60 11228 29047 11142 -6263 -1845 1425 C ATOM 2788 OD1 ASP B 60 89.858 17.995 188.812 1.00137.19 O ANISOU 2788 OD1 ASP B 60 11028 29000 12100 -6952 -1905 838 O ATOM 2789 OD2 ASP B 60 90.270 20.042 188.133 1.00131.87 O ANISOU 2789 OD2 ASP B 60 10549 29491 10064 -5651 -1935 2007 O ATOM 2790 N ALA B 61 94.804 17.819 190.269 1.00114.05 N ANISOU 2790 N ALA B 61 11178 22894 9262 -6300 -720 1875 N ATOM 2791 CA ALA B 61 96.239 17.564 190.279 1.00116.86 C ANISOU 2791 CA ALA B 61 12227 22645 9529 -6114 -551 1827 C ATOM 2792 C ALA B 61 96.553 16.274 191.027 1.00119.33 C ANISOU 2792 C ALA B 61 12953 21843 10544 -6620 -331 1338 C ATOM 2793 O ALA B 61 97.470 15.540 190.660 1.00116.35 O ANISOU 2793 O ALA B 61 12971 21157 10080 -6652 -362 831 O ATOM 2794 CB ALA B 61 96.984 18.734 190.900 1.00111.05 C ANISOU 2794 CB ALA B 61 11889 21600 8706 -5572 -245 2743 C ATOM 2795 N MET B 62 95.785 16.003 192.077 1.00120.69 N ANISOU 2795 N MET B 62 13042 21421 11393 -6959 -67 1537 N ATOM 2796 CA MET B 62 95.976 14.799 192.878 1.00117.80 C ANISOU 2796 CA MET B 62 13073 19939 11745 -7387 255 1212 C ATOM 2797 C MET B 62 95.465 13.563 192.145 1.00123.17 C ANISOU 2797 C MET B 62 13398 20666 12734 -8028 -8 211 C ATOM 2798 O MET B 62 95.825 12.436 192.483 1.00117.43 O ANISOU 2798 O MET B 62 13058 19031 12530 -8371 204 -227 O ATOM 2799 CB MET B 62 95.273 14.937 194.230 1.00115.32 C ANISOU 2799 CB MET B 62 12756 19025 12037 -7456 697 1841 C ATOM 2800 N GLN B 63 94.624 13.783 191.139 1.00127.79 N ANISOU 2800 N GLN B 63 13243 22308 13005 -8142 -484 -185 N ATOM 2801 CA GLN B 63 94.067 12.689 190.354 1.00142.84 C ANISOU 2801 CA GLN B 63 14686 24378 15209 -8718 -857 -1275 C ATOM 2802 C GLN B 63 95.056 12.208 189.296 1.00148.24 C ANISOU 2802 C GLN B 63 15692 25315 15319 -8503 -1210 -2006 C ATOM 2803 O GLN B 63 95.125 11.016 188.994 1.00164.89 O ANISOU 2803 O GLN B 63 17846 26969 17836 -8945 -1354 -2918 O ATOM 2804 CB GLN B 63 92.757 13.119 189.690 1.00148.66 C ANISOU 2804 CB GLN B 63 14440 26256 15789 -8834 -1296 -1508 C ATOM 2805 N HIS B 64 95.821 13.141 188.739 1.00140.41 N ANISOU 2805 N HIS B 64 14914 25023 13411 -7800 -1318 -1584 N ATOM 2806 CA HIS B 64 96.788 12.816 187.697 1.00145.82 C ANISOU 2806 CA HIS B 64 15877 26098 13430 -7460 -1606 -2146 C ATOM 2807 C HIS B 64 98.027 12.134 188.271 1.00145.98 C ANISOU 2807 C HIS B 64 16743 25008 13716 -7466 -1247 -2179 C ATOM 2808 O HIS B 64 98.652 11.306 187.609 1.00157.68 O ANISOU 2808 O HIS B 64 18468 26445 15000 -7454 -1459 -2942 O ATOM 2809 CB HIS B 64 97.193 14.078 186.932 1.00137.44 C ANISOU 2809 CB HIS B 64 14735 26130 11357 -6675 -1721 -1548 C ATOM 2810 N LEU B 65 98.377 12.487 189.504 1.00137.18 N ANISOU 2810 N LEU B 65 16071 23044 13006 -7409 -729 -1384 N ATOM 2811 CA LEU B 65 99.555 11.927 190.156 1.00126.20 C ANISOU 2811 CA LEU B 65 15478 20644 11828 -7304 -375 -1358 C ATOM 2812 C LEU B 65 99.313 10.501 190.638 1.00147.16 C ANISOU 2812 C LEU B 65 18356 22272 15285 -7894 -216 -1996 C ATOM 2813 O LEU B 65 100.175 9.634 190.498 1.00154.19 O ANISOU 2813 O LEU B 65 19767 22641 16178 -7868 -185 -2507 O ATOM 2814 CB LEU B 65 99.985 12.807 191.331 1.00104.48 C ANISOU 2814 CB LEU B 65 13090 17393 9215 -6945 71 -369 C ATOM 2815 CG LEU B 65 100.470 14.213 190.978 1.00105.39 C ANISOU 2815 CG LEU B 65 13107 18243 8694 -6345 14 308 C ATOM 2816 CD1 LEU B 65 100.861 14.976 192.233 1.00104.29 C ANISOU 2816 CD1 LEU B 65 13310 17473 8842 -6030 398 1115 C ATOM 2817 CD2 LEU B 65 101.634 14.144 190.003 1.00105.84 C ANISOU 2817 CD2 LEU B 65 13389 18694 8129 -5983 -135 8 C ATOM 2818 N ASP B 66 98.136 10.266 191.209 1.00150.38 N ANISOU 2818 N ASP B 66 18361 22373 16405 -8409 -76 -1931 N ATOM 2819 CA ASP B 66 97.790 8.954 191.744 1.00157.80 C ANISOU 2819 CA ASP B 66 19453 22230 18274 -9015 195 -2407 C ATOM 2820 C ASP B 66 97.622 7.922 190.633 1.00165.32 C ANISOU 2820 C ASP B 66 20142 23350 19321 -9432 -290 -3626 C ATOM 2821 O ASP B 66 97.891 6.737 190.830 1.00174.06 O ANISOU 2821 O ASP B 66 21638 23484 21013 -9765 -116 -4176 O ATOM 2822 CB ASP B 66 96.511 9.039 192.579 1.00161.46 C ANISOU 2822 CB ASP B 66 19429 22409 19511 -9456 511 -1964 C ATOM 2823 N ARG B 67 97.177 8.379 189.467 1.00172.04 N ANISOU 2823 N ARG B 67 20346 25442 19578 -9344 -906 -4066 N ATOM 2824 CA ARG B 67 96.960 7.492 188.330 1.00165.02 C ANISOU 2824 CA ARG B 67 19123 24901 18675 -9624 -1490 -5330 C ATOM 2825 C ARG B 67 98.272 7.162 187.625 1.00149.30 C ANISOU 2825 C ARG B 67 17750 23028 15948 -9112 -1685 -5768 C ATOM 2826 O ARG B 67 98.558 6.000 187.339 1.00155.35 O ANISOU 2826 O ARG B 67 18788 23151 17087 -9228 -1788 -6574 O ATOM 2827 CB ARG B 67 95.976 8.119 187.342 1.00156.36 C ANISOU 2827 CB ARG B 67 17108 25174 17127 -9486 -2085 -5617 C ATOM 2828 N GLN B 68 99.064 8.193 187.346 1.00146.28 N ANISOU 2828 N GLN B 68 17585 23386 14607 -8378 -1675 -5107 N ATOM 2829 CA GLN B 68 100.342 8.016 186.665 1.00149.98 C ANISOU 2829 CA GLN B 68 18575 24093 14319 -7816 -1801 -5386 C ATOM 2830 C GLN B 68 101.355 7.311 187.561 1.00145.89 C ANISOU 2830 C GLN B 68 18924 22288 14218 -7828 -1306 -5258 C ATOM 2831 O GLN B 68 101.629 6.123 187.390 1.00157.75 O ANISOU 2831 O GLN B 68 20748 23161 16029 -8054 -1391 -6096 O ATOM 2832 CB GLN B 68 100.896 9.366 186.207 1.00134.24 C ANISOU 2832 CB GLN B 68 16521 23148 11338 -7062 -1801 -4579 C TER 2833 GLN B 68 ATOM 2834 N GLN C 1 112.656 33.131 274.237 1.00 97.04 N ANISOU 2834 N GLN C 1 9044 11829 15999 -877 -890 630 N ATOM 2835 CA GLN C 1 112.215 31.754 274.052 1.00 96.44 C ANISOU 2835 CA GLN C 1 9168 11886 15591 -617 -607 705 C ATOM 2836 C GLN C 1 110.807 31.547 274.598 1.00 90.25 C ANISOU 2836 C GLN C 1 8906 11233 14153 -726 -511 162 C ATOM 2837 O GLN C 1 110.423 32.152 275.599 1.00 97.92 O ANISOU 2837 O GLN C 1 10117 12253 14835 -1058 -789 -191 O ATOM 2838 CB GLN C 1 113.188 30.784 274.726 1.00103.00 C ANISOU 2838 CB GLN C 1 9821 12817 16495 -674 -924 1173 C ATOM 2839 N VAL C 2 110.040 30.688 273.934 1.00 77.32 N ANISOU 2839 N VAL C 2 7460 9631 12285 -450 -108 113 N ATOM 2840 CA VAL C 2 108.674 30.400 274.354 1.00 83.52 C ANISOU 2840 CA VAL C 2 8667 10545 12522 -534 20 -314 C ATOM 2841 C VAL C 2 108.625 29.167 275.251 1.00101.47 C ANISOU 2841 C VAL C 2 11156 12985 14412 -633 -136 -215 C ATOM 2842 O VAL C 2 109.060 28.085 274.859 1.00109.37 O ANISOU 2842 O VAL C 2 12101 13966 15490 -424 -33 131 O ATOM 2843 CB VAL C 2 107.745 30.183 273.144 1.00 83.73 C ANISOU 2843 CB VAL C 2 8798 10514 12501 -248 481 -422 C ATOM 2844 CG1 VAL C 2 106.350 29.790 273.608 1.00 81.52 C ANISOU 2844 CG1 VAL C 2 8876 10380 11719 -355 588 -770 C ATOM 2845 CG2 VAL C 2 107.694 31.435 272.283 1.00 76.40 C ANISOU 2845 CG2 VAL C 2 7679 9434 11917 -152 639 -515 C ATOM 2846 N GLN C 3 108.094 29.341 276.457 1.00100.76 N ANISOU 2846 N GLN C 3 11344 13038 13900 -936 -356 -511 N ATOM 2847 CA GLN C 3 107.977 28.243 277.409 1.00 87.29 C ANISOU 2847 CA GLN C 3 9873 11507 11787 -1059 -512 -423 C ATOM 2848 C GLN C 3 106.515 27.921 277.699 1.00 71.77 C ANISOU 2848 C GLN C 3 8274 9662 9333 -1096 -249 -776 C ATOM 2849 O GLN C 3 105.674 28.817 277.761 1.00 83.63 O ANISOU 2849 O GLN C 3 9897 11159 10720 -1161 -99 -1154 O ATOM 2850 CB GLN C 3 108.709 28.581 278.710 1.00 98.60 C ANISOU 2850 CB GLN C 3 11351 13028 13085 -1409 -1037 -382 C ATOM 2851 CG GLN C 3 110.200 28.827 278.544 1.00104.26 C ANISOU 2851 CG GLN C 3 11636 13647 14331 -1428 -1379 61 C ATOM 2852 CD GLN C 3 110.964 27.573 278.166 1.00108.48 C ANISOU 2852 CD GLN C 3 11925 14183 15109 -1180 -1336 615 C ATOM 2853 OE1 GLN C 3 110.493 26.456 278.376 1.00113.00 O ANISOU 2853 OE1 GLN C 3 12725 14846 15363 -1095 -1198 662 O ATOM 2854 NE2 GLN C 3 112.154 27.753 277.603 1.00114.76 N ANISOU 2854 NE2 GLN C 3 12248 14855 16501 -1049 -1426 1064 N ATOM 2855 N LEU C 4 106.219 26.638 277.875 1.00 57.15 N ANISOU 2855 N LEU C 4 6578 7901 7236 -1048 -177 -615 N ATOM 2856 CA LEU C 4 104.864 26.205 278.197 1.00 55.27 C ANISOU 2856 CA LEU C 4 6640 7786 6574 -1109 55 -861 C ATOM 2857 C LEU C 4 104.657 26.141 279.707 1.00 57.67 C ANISOU 2857 C LEU C 4 7228 8284 6398 -1397 -161 -982 C ATOM 2858 O LEU C 4 105.196 25.263 280.381 1.00 63.31 O ANISOU 2858 O LEU C 4 8016 9086 6951 -1482 -396 -713 O ATOM 2859 CB LEU C 4 104.568 24.843 277.564 1.00 58.39 C ANISOU 2859 CB LEU C 4 7098 8139 6949 -936 251 -629 C ATOM 2860 CG LEU C 4 104.552 24.794 276.035 1.00 57.14 C ANISOU 2860 CG LEU C 4 6805 7778 7127 -652 516 -554 C ATOM 2861 CD1 LEU C 4 104.247 23.388 275.543 1.00 57.22 C ANISOU 2861 CD1 LEU C 4 7005 7704 7034 -533 669 -362 C ATOM 2862 CD2 LEU C 4 103.548 25.790 275.476 1.00 56.86 C ANISOU 2862 CD2 LEU C 4 6746 7737 7123 -646 729 -885 C ATOM 2863 N VAL C 5 103.873 27.078 280.231 1.00 57.16 N ANISOU 2863 N VAL C 5 7348 8273 6097 -1527 -57 -1372 N ATOM 2864 CA VAL C 5 103.603 27.138 281.663 1.00 70.17 C ANISOU 2864 CA VAL C 5 9360 10086 7218 -1783 -194 -1538 C ATOM 2865 C VAL C 5 102.400 26.275 282.031 1.00 79.04 C ANISOU 2865 C VAL C 5 10701 11368 7962 -1780 114 -1565 C ATOM 2866 O VAL C 5 101.301 26.472 281.514 1.00 83.65 O ANISOU 2866 O VAL C 5 11246 11941 8595 -1667 497 -1732 O ATOM 2867 CB VAL C 5 103.351 28.583 282.129 1.00 67.74 C ANISOU 2867 CB VAL C 5 9228 9711 6800 -1906 -176 -1958 C ATOM 2868 CG1 VAL C 5 103.040 28.615 283.618 1.00 68.52 C ANISOU 2868 CG1 VAL C 5 9812 9958 6263 -2154 -271 -2149 C ATOM 2869 CG2 VAL C 5 104.553 29.459 281.811 1.00 66.02 C ANISOU 2869 CG2 VAL C 5 8787 9313 6983 -1964 -526 -1907 C ATOM 2870 N GLU C 6 102.617 25.320 282.930 1.00 87.09 N ANISOU 2870 N GLU C 6 11920 12536 8635 -1916 -71 -1354 N ATOM 2871 CA GLU C 6 101.567 24.396 283.345 1.00 88.04 C ANISOU 2871 CA GLU C 6 12231 12805 8414 -1940 195 -1305 C ATOM 2872 C GLU C 6 101.068 24.704 284.753 1.00 92.06 C ANISOU 2872 C GLU C 6 13155 13495 8331 -2143 232 -1512 C ATOM 2873 O GLU C 6 101.832 25.159 285.605 1.00103.32 O ANISOU 2873 O GLU C 6 14797 14953 9508 -2322 -115 -1571 O ATOM 2874 CB GLU C 6 102.073 22.955 283.278 1.00 89.56 C ANISOU 2874 CB GLU C 6 12377 13008 8643 -1914 33 -874 C ATOM 2875 CG GLU C 6 102.489 22.504 281.891 1.00 89.50 C ANISOU 2875 CG GLU C 6 12066 12789 9150 -1678 84 -667 C ATOM 2876 CD GLU C 6 103.479 21.358 281.932 1.00101.57 C ANISOU 2876 CD GLU C 6 13548 14261 10781 -1624 -154 -226 C ATOM 2877 OE1 GLU C 6 104.457 21.449 282.702 1.00109.95 O ANISOU 2877 OE1 GLU C 6 14606 15395 11777 -1736 -521 -58 O ATOM 2878 OE2 GLU C 6 103.279 20.365 281.202 1.00110.07 O ANISOU 2878 OE2 GLU C 6 14608 15204 12010 -1476 13 -34 O ATOM 2879 N SER C 7 99.785 24.445 284.989 1.00 80.35 N ANISOU 2879 N SER C 7 11793 12119 6616 -2121 651 -1597 N ATOM 2880 CA SER C 7 99.180 24.657 286.300 1.00 81.95 C ANISOU 2880 CA SER C 7 12421 12491 6224 -2262 814 -1768 C ATOM 2881 C SER C 7 97.834 23.947 286.403 1.00 75.16 C ANISOU 2881 C SER C 7 11563 11762 5232 -2215 1280 -1665 C ATOM 2882 O SER C 7 97.081 23.885 285.431 1.00 79.17 O ANISOU 2882 O SER C 7 11754 12202 6125 -2076 1553 -1639 O ATOM 2883 CB SER C 7 99.005 26.152 286.578 1.00 97.48 C ANISOU 2883 CB SER C 7 14578 14368 8091 -2260 951 -2211 C ATOM 2884 OG SER C 7 98.471 26.369 287.873 1.00124.21 O ANISOU 2884 OG SER C 7 18470 17885 10841 -2371 1148 -2394 O ATOM 2885 N GLY C 8 97.535 23.411 287.582 1.00 76.40 N ANISOU 2885 N GLY C 8 12073 12108 4849 -2349 1349 -1572 N ATOM 2886 CA GLY C 8 96.259 22.760 287.813 1.00 93.47 C ANISOU 2886 CA GLY C 8 14229 14404 6880 -2328 1808 -1429 C ATOM 2887 C GLY C 8 96.372 21.366 288.400 1.00105.70 C ANISOU 2887 C GLY C 8 15905 16087 8171 -2461 1668 -1032 C ATOM 2888 O GLY C 8 95.366 20.678 288.577 1.00120.60 O ANISOU 2888 O GLY C 8 17756 18075 9991 -2477 2009 -838 O ATOM 2889 N GLY C 9 97.596 20.946 288.702 1.00 76.91 N ANISOU 2889 N GLY C 9 12375 12431 4417 -2562 1162 -869 N ATOM 2890 CA GLY C 9 97.825 19.635 289.282 1.00 78.76 C ANISOU 2890 CA GLY C 9 12735 12768 4422 -2676 992 -459 C ATOM 2891 C GLY C 9 97.491 19.597 290.760 1.00 92.07 C ANISOU 2891 C GLY C 9 14908 14690 5386 -2826 1109 -454 C ATOM 2892 O GLY C 9 97.062 20.599 291.333 1.00 96.26 O ANISOU 2892 O GLY C 9 15665 15238 5671 -2778 1338 -785 O ATOM 2893 N GLY C 10 97.687 18.439 291.382 1.00 86.66 N ANISOU 2893 N GLY C 10 14364 14112 4452 -2938 956 -57 N ATOM 2894 CA GLY C 10 97.435 18.292 292.803 1.00 96.85 C ANISOU 2894 CA GLY C 10 16039 15539 5220 -2976 1015 10 C ATOM 2895 C GLY C 10 97.016 16.893 293.209 1.00102.42 C ANISOU 2895 C GLY C 10 16742 16321 5854 -3014 1115 471 C ATOM 2896 O GLY C 10 97.154 15.941 292.440 1.00 91.01 O ANISOU 2896 O GLY C 10 15054 14805 4720 -3057 1027 777 O ATOM 2897 N LEU C 11 96.501 16.771 294.429 1.00111.32 N ANISOU 2897 N LEU C 11 18166 17567 6562 -2988 1311 528 N ATOM 2898 CA LEU C 11 96.052 15.488 294.955 1.00108.73 C ANISOU 2898 CA LEU C 11 17861 17315 6138 -3020 1434 971 C ATOM 2899 C LEU C 11 94.532 15.470 295.079 1.00112.28 C ANISOU 2899 C LEU C 11 18203 17807 6651 -2894 2085 974 C ATOM 2900 O LEU C 11 93.925 16.464 295.478 1.00129.17 O ANISOU 2900 O LEU C 11 20464 19991 8625 -2753 2427 669 O ATOM 2901 CB LEU C 11 96.697 15.199 296.315 1.00110.56 C ANISOU 2901 CB LEU C 11 18504 17678 5825 -3092 1129 1140 C ATOM 2902 CG LEU C 11 98.227 15.172 296.403 1.00113.81 C ANISOU 2902 CG LEU C 11 19005 18077 6162 -3235 426 1240 C ATOM 2903 CD1 LEU C 11 98.801 16.564 296.650 1.00110.82 C ANISOU 2903 CD1 LEU C 11 18844 17686 5577 -3267 191 793 C ATOM 2904 CD2 LEU C 11 98.686 14.201 297.480 1.00118.34 C ANISOU 2904 CD2 LEU C 11 19812 18763 6390 -3318 149 1664 C ATOM 2905 N VAL C 12 93.921 14.340 294.739 1.00113.12 N ANISOU 2905 N VAL C 12 18072 17883 7026 -2943 2250 1352 N ATOM 2906 CA VAL C 12 92.467 14.227 294.765 1.00119.97 C ANISOU 2906 CA VAL C 12 18744 18790 8048 -2858 2830 1453 C ATOM 2907 C VAL C 12 92.026 12.777 294.979 1.00105.66 C ANISOU 2907 C VAL C 12 16846 16970 6328 -2966 2895 1971 C ATOM 2908 O VAL C 12 92.670 11.842 294.501 1.00103.40 O ANISOU 2908 O VAL C 12 16497 16554 6236 -3102 2535 2214 O ATOM 2909 CB VAL C 12 91.847 14.786 293.459 1.00105.81 C ANISOU 2909 CB VAL C 12 16530 16879 6793 -2821 3036 1253 C ATOM 2910 CG1 VAL C 12 92.326 13.993 292.253 1.00 93.91 C ANISOU 2910 CG1 VAL C 12 14773 15195 5712 -2979 2702 1416 C ATOM 2911 CG2 VAL C 12 90.325 14.802 293.535 1.00107.24 C ANISOU 2911 CG2 VAL C 12 16456 17120 7169 -2727 3623 1397 C ATOM 2912 N ARG C 13 90.936 12.599 295.721 1.00119.47 N ANISOU 2912 N ARG C 13 18604 18841 7950 -2886 3373 2161 N ATOM 2913 CA ARG C 13 90.376 11.276 295.975 1.00118.25 C ANISOU 2913 CA ARG C 13 18352 18666 7912 -2990 3494 2668 C ATOM 2914 C ARG C 13 89.837 10.653 294.688 1.00119.66 C ANISOU 2914 C ARG C 13 18087 18637 8741 -3144 3489 2835 C ATOM 2915 O ARG C 13 89.408 11.372 293.785 1.00110.43 O ANISOU 2915 O ARG C 13 16635 17417 7908 -3119 3610 2596 O ATOM 2916 CB ARG C 13 89.267 11.363 297.027 1.00119.00 C ANISOU 2916 CB ARG C 13 18517 18951 7748 -2840 4072 2847 C ATOM 2917 N PRO C 14 89.868 9.312 294.600 1.00119.48 N ANISOU 2917 N PRO C 14 18024 18473 8900 -3311 3325 3249 N ATOM 2918 CA PRO C 14 89.350 8.582 293.436 1.00109.09 C ANISOU 2918 CA PRO C 14 16362 16911 8177 -3499 3265 3434 C ATOM 2919 C PRO C 14 87.901 8.936 293.111 1.00108.71 C ANISOU 2919 C PRO C 14 15930 16901 8474 -3511 3720 3486 C ATOM 2920 O PRO C 14 87.025 8.810 293.967 1.00112.38 O ANISOU 2920 O PRO C 14 16365 17498 8837 -3449 4141 3731 O ATOM 2921 CB PRO C 14 89.467 7.118 293.865 1.00114.52 C ANISOU 2921 CB PRO C 14 17169 17462 8883 -3631 3125 3902 C ATOM 2922 CG PRO C 14 90.597 7.108 294.830 1.00111.09 C ANISOU 2922 CG PRO C 14 17126 17152 7932 -3522 2882 3894 C ATOM 2923 CD PRO C 14 90.497 8.407 295.578 1.00112.87 C ANISOU 2923 CD PRO C 14 17505 17665 7717 -3336 3127 3558 C ATOM 2924 N GLY C 15 87.661 9.377 291.881 1.00111.44 N ANISOU 2924 N GLY C 15 15974 17128 9239 -3579 3641 3291 N ATOM 2925 CA GLY C 15 86.334 9.789 291.462 1.00109.15 C ANISOU 2925 CA GLY C 15 15256 16867 9348 -3593 4011 3360 C ATOM 2926 C GLY C 15 86.198 11.298 291.435 1.00104.77 C ANISOU 2926 C GLY C 15 14625 16481 8702 -3341 4276 2962 C ATOM 2927 O GLY C 15 85.169 11.832 291.022 1.00103.67 O ANISOU 2927 O GLY C 15 14097 16366 8927 -3296 4587 2994 O ATOM 2928 N GLY C 16 87.246 11.987 291.876 1.00102.96 N ANISOU 2928 N GLY C 16 14759 16341 8019 -3179 4132 2604 N ATOM 2929 CA GLY C 16 87.254 13.438 291.901 1.00100.99 C ANISOU 2929 CA GLY C 16 14519 16198 7655 -2935 4336 2182 C ATOM 2930 C GLY C 16 87.522 14.042 290.536 1.00115.95 C ANISOU 2930 C GLY C 16 16169 17956 9929 -2976 4108 1887 C ATOM 2931 O GLY C 16 87.410 13.363 289.514 1.00 99.41 O ANISOU 2931 O GLY C 16 13840 15701 8232 -3192 3874 2045 O ATOM 2932 N SER C 17 87.881 15.321 290.516 1.00112.94 N ANISOU 2932 N SER C 17 15877 17616 9421 -2770 4168 1458 N ATOM 2933 CA SER C 17 88.129 16.018 289.260 1.00 94.43 C ANISOU 2933 CA SER C 17 13300 15150 7427 -2768 3999 1169 C ATOM 2934 C SER C 17 89.228 17.070 289.386 1.00 87.42 C ANISOU 2934 C SER C 17 12708 14250 6258 -2619 3812 703 C ATOM 2935 O SER C 17 89.385 17.701 290.431 1.00 91.49 O ANISOU 2935 O SER C 17 13533 14857 6371 -2458 3958 531 O ATOM 2936 CB SER C 17 86.843 16.672 288.753 1.00101.22 C ANISOU 2936 CB SER C 17 13698 16028 8734 -2657 4394 1214 C ATOM 2937 OG SER C 17 86.367 17.641 289.670 1.00123.82 O ANISOU 2937 OG SER C 17 16651 19015 11381 -2358 4836 1084 O ATOM 2938 N LEU C 18 89.986 17.247 288.309 1.00 83.01 N ANISOU 2938 N LEU C 18 12066 13561 5913 -2684 3479 516 N ATOM 2939 CA LEU C 18 91.028 18.265 288.246 1.00 80.18 C ANISOU 2939 CA LEU C 18 11906 13164 5396 -2569 3274 105 C ATOM 2940 C LEU C 18 91.002 18.970 286.897 1.00 75.78 C ANISOU 2940 C LEU C 18 11011 12456 5327 -2489 3217 -110 C ATOM 2941 O LEU C 18 90.479 18.437 285.919 1.00 96.65 O ANISOU 2941 O LEU C 18 13330 14985 8409 -2549 3160 79 O ATOM 2942 CB LEU C 18 92.408 17.651 288.489 1.00 79.32 C ANISOU 2942 CB LEU C 18 12101 13024 5012 -2682 2787 160 C ATOM 2943 CG LEU C 18 92.741 17.188 289.907 1.00 93.18 C ANISOU 2943 CG LEU C 18 14250 14915 6240 -2727 2720 314 C ATOM 2944 CD1 LEU C 18 94.119 16.546 289.945 1.00 82.92 C ANISOU 2944 CD1 LEU C 18 13152 13581 4771 -2850 2196 451 C ATOM 2945 CD2 LEU C 18 92.664 18.353 290.880 1.00105.23 C ANISOU 2945 CD2 LEU C 18 16045 16517 7422 -2566 2903 -5 C ATOM 2946 N ARG C 19 91.569 20.171 286.847 1.00 74.82 N ANISOU 2946 N ARG C 19 10979 12291 5160 -2341 3180 -493 N ATOM 2947 CA ARG C 19 91.631 20.930 285.605 1.00 73.53 C ANISOU 2947 CA ARG C 19 10501 11953 5485 -2212 3093 -691 C ATOM 2948 C ARG C 19 93.044 21.436 285.341 1.00 76.75 C ANISOU 2948 C ARG C 19 11053 12222 5887 -2152 2673 -933 C ATOM 2949 O ARG C 19 93.503 22.385 285.977 1.00 77.91 O ANISOU 2949 O ARG C 19 11438 12394 5769 -2102 2688 -1220 O ATOM 2950 CB ARG C 19 90.652 22.105 285.642 1.00 78.31 C ANISOU 2950 CB ARG C 19 10942 12605 6208 -2049 3574 -883 C ATOM 2951 CG ARG C 19 90.564 22.876 284.334 1.00 73.41 C ANISOU 2951 CG ARG C 19 9960 11821 6111 -1922 3516 -1027 C ATOM 2952 CD ARG C 19 89.737 24.142 284.490 1.00 95.91 C ANISOU 2952 CD ARG C 19 12674 14644 9125 -1677 3920 -1190 C ATOM 2953 NE ARG C 19 88.394 23.863 284.992 1.00121.56 N ANISOU 2953 NE ARG C 19 15738 18006 12442 -1615 4313 -890 N ATOM 2954 CZ ARG C 19 87.479 24.796 285.232 1.00129.50 C ANISOU 2954 CZ ARG C 19 16587 18997 13619 -1350 4698 -898 C ATOM 2955 NH1 ARG C 19 87.759 26.074 285.016 1.00133.78 N ANISOU 2955 NH1 ARG C 19 17172 19385 14272 -1139 4724 -1213 N ATOM 2956 NH2 ARG C 19 86.282 24.452 285.688 1.00127.14 N ANISOU 2956 NH2 ARG C 19 16072 18838 13398 -1289 5059 -555 N ATOM 2957 N LEU C 20 93.730 20.796 284.401 1.00 76.01 N ANISOU 2957 N LEU C 20 10828 11960 6090 -2162 2309 -799 N ATOM 2958 CA LEU C 20 95.076 21.209 284.025 1.00 76.24 C ANISOU 2958 CA LEU C 20 10900 11849 6217 -2086 1937 -939 C ATOM 2959 C LEU C 20 95.021 22.379 283.051 1.00 69.26 C ANISOU 2959 C LEU C 20 9772 10834 5709 -1927 2006 -1200 C ATOM 2960 O LEU C 20 94.151 22.434 282.185 1.00 73.48 O ANISOU 2960 O LEU C 20 10043 11319 6557 -1877 2189 -1164 O ATOM 2961 CB LEU C 20 95.848 20.042 283.407 1.00 69.83 C ANISOU 2961 CB LEU C 20 10064 10884 5584 -2103 1607 -658 C ATOM 2962 CG LEU C 20 96.008 18.791 284.273 1.00 72.92 C ANISOU 2962 CG LEU C 20 10682 11358 5668 -2246 1501 -344 C ATOM 2963 CD1 LEU C 20 96.853 17.749 283.555 1.00 62.67 C ANISOU 2963 CD1 LEU C 20 9366 9836 4610 -2199 1215 -85 C ATOM 2964 CD2 LEU C 20 96.614 19.141 285.623 1.00 88.20 C ANISOU 2964 CD2 LEU C 20 12909 13476 7127 -2322 1383 -404 C ATOM 2965 N SER C 21 95.953 23.315 283.200 1.00 60.31 N ANISOU 2965 N SER C 21 8722 9640 4553 -1871 1830 -1432 N ATOM 2966 CA SER C 21 96.008 24.482 282.328 1.00 58.20 C ANISOU 2966 CA SER C 21 8239 9228 4645 -1721 1884 -1667 C ATOM 2967 C SER C 21 97.414 24.687 281.776 1.00 60.71 C ANISOU 2967 C SER C 21 8496 9385 5186 -1670 1498 -1662 C ATOM 2968 O SER C 21 98.400 24.574 282.504 1.00 61.04 O ANISOU 2968 O SER C 21 8721 9454 5018 -1765 1203 -1624 O ATOM 2969 CB SER C 21 95.546 25.734 283.077 1.00 69.85 C ANISOU 2969 CB SER C 21 9863 10749 5927 -1690 2164 -1995 C ATOM 2970 OG SER C 21 96.368 25.987 284.203 1.00110.42 O ANISOU 2970 OG SER C 21 15378 15930 10646 -1812 1951 -2127 O ATOM 2971 N CYS C 22 97.498 24.989 280.485 1.00 54.15 N ANISOU 2971 N CYS C 22 7395 8391 4790 -1523 1501 -1659 N ATOM 2972 CA CYS C 22 98.781 25.195 279.826 1.00 53.41 C ANISOU 2972 CA CYS C 22 7188 8132 4974 -1433 1216 -1601 C ATOM 2973 C CYS C 22 98.695 26.342 278.829 1.00 55.86 C ANISOU 2973 C CYS C 22 7266 8298 5661 -1278 1329 -1775 C ATOM 2974 O CYS C 22 97.700 26.480 278.123 1.00 64.65 O ANISOU 2974 O CYS C 22 8240 9398 6926 -1204 1568 -1803 O ATOM 2975 CB CYS C 22 99.231 23.915 279.122 1.00 59.15 C ANISOU 2975 CB CYS C 22 7879 8764 5832 -1375 1085 -1280 C ATOM 2976 SG CYS C 22 100.778 24.063 278.207 1.00 80.46 S ANISOU 2976 SG CYS C 22 10399 11245 8926 -1191 850 -1121 S ATOM 2977 N ALA C 23 99.739 27.163 278.776 1.00 59.41 N ANISOU 2977 N ALA C 23 7655 8637 6283 -1248 1133 -1852 N ATOM 2978 CA ALA C 23 99.762 28.306 277.869 1.00 48.30 C ANISOU 2978 CA ALA C 23 6030 7073 5248 -1105 1231 -1993 C ATOM 2979 C ALA C 23 101.188 28.683 277.481 1.00 74.25 C ANISOU 2979 C ALA C 23 9173 10209 8831 -1058 954 -1882 C ATOM 2980 O ALA C 23 102.145 28.311 278.159 1.00 92.21 O ANISOU 2980 O ALA C 23 11519 12514 11001 -1171 659 -1748 O ATOM 2981 CB ALA C 23 99.054 29.494 278.500 1.00 50.35 C ANISOU 2981 CB ALA C 23 6382 7344 5406 -1142 1437 -2327 C ATOM 2982 N ALA C 24 101.319 29.423 276.385 1.00 65.94 N ANISOU 2982 N ALA C 24 7889 8997 8168 -892 1048 -1893 N ATOM 2983 CA ALA C 24 102.622 29.880 275.917 1.00 60.82 C ANISOU 2983 CA ALA C 24 7041 8193 7874 -827 845 -1747 C ATOM 2984 C ALA C 24 102.956 31.248 276.501 1.00 72.62 C ANISOU 2984 C ALA C 24 8539 9599 9455 -957 722 -1992 C ATOM 2985 O ALA C 24 102.149 32.174 276.435 1.00 69.48 O ANISOU 2985 O ALA C 24 8170 9147 9084 -929 941 -2262 O ATOM 2986 CB ALA C 24 102.654 29.927 274.397 1.00 54.26 C ANISOU 2986 CB ALA C 24 5996 7221 7400 -575 1025 -1593 C ATOM 2987 N SER C 25 104.150 31.368 277.071 1.00 88.46 N ANISOU 2987 N SER C 25 10518 11570 11524 -1106 358 -1875 N ATOM 2988 CA SER C 25 104.574 32.610 277.706 1.00105.75 C ANISOU 2988 CA SER C 25 12775 13637 13768 -1301 148 -2103 C ATOM 2989 C SER C 25 104.969 33.665 276.676 1.00113.96 C ANISOU 2989 C SER C 25 13509 14446 15343 -1169 217 -2077 C ATOM 2990 O SER C 25 104.659 34.845 276.834 1.00131.16 O ANISOU 2990 O SER C 25 15772 16475 17590 -1231 278 -2373 O ATOM 2991 CB SER C 25 105.740 32.350 278.662 1.00114.49 C ANISOU 2991 CB SER C 25 13940 14787 14776 -1563 -355 -1930 C ATOM 2992 OG SER C 25 106.851 31.799 277.975 1.00123.03 O ANISOU 2992 OG SER C 25 14647 15832 16266 -1447 -516 -1470 O ATOM 2993 N GLY C 26 105.653 33.232 275.621 1.00 94.72 N ANISOU 2993 N GLY C 26 10745 11961 13282 -968 243 -1710 N ATOM 2994 CA GLY C 26 106.107 34.140 274.584 1.00 80.48 C ANISOU 2994 CA GLY C 26 8634 9951 11993 -822 331 -1608 C ATOM 2995 C GLY C 26 105.076 34.361 273.494 1.00 77.73 C ANISOU 2995 C GLY C 26 8248 9567 11719 -565 751 -1701 C ATOM 2996 O GLY C 26 103.969 33.825 273.553 1.00 86.01 O ANISOU 2996 O GLY C 26 9484 10751 12447 -520 954 -1843 O ATOM 2997 N SER C 27 105.443 35.156 272.493 1.00 71.87 N ANISOU 2997 N SER C 27 7244 8644 11418 -412 859 -1581 N ATOM 2998 CA SER C 27 104.551 35.443 271.376 1.00 71.04 C ANISOU 2998 CA SER C 27 7086 8498 11407 -175 1207 -1615 C ATOM 2999 C SER C 27 104.906 34.597 270.157 1.00 56.47 C ANISOU 2999 C SER C 27 5131 6656 9668 87 1360 -1259 C ATOM 3000 O SER C 27 105.881 34.873 269.459 1.00 43.32 O ANISOU 3000 O SER C 27 3229 4856 8373 219 1375 -978 O ATOM 3001 CB SER C 27 104.599 36.930 271.017 1.00 68.92 C ANISOU 3001 CB SER C 27 6657 8009 11522 -157 1270 -1719 C ATOM 3002 OG SER C 27 105.900 37.316 270.613 1.00 52.55 O ANISOU 3002 OG SER C 27 4306 5780 9881 -144 1125 -1429 O ATOM 3003 N ILE C 28 104.107 33.564 269.912 1.00 48.53 N ANISOU 3003 N ILE C 28 4325 5784 8331 158 1488 -1264 N ATOM 3004 CA ILE C 28 104.311 32.685 268.767 1.00 39.51 C ANISOU 3004 CA ILE C 28 3220 4605 7186 396 1649 -986 C ATOM 3005 C ILE C 28 102.995 32.511 268.008 1.00 57.57 C ANISOU 3005 C ILE C 28 5664 6941 9270 466 1830 -1091 C ATOM 3006 O ILE C 28 101.932 32.369 268.614 1.00 62.24 O ANISOU 3006 O ILE C 28 6369 7666 9614 313 1810 -1305 O ATOM 3007 CB ILE C 28 104.871 31.312 269.206 1.00 39.91 C ANISOU 3007 CB ILE C 28 3413 4722 7031 386 1550 -806 C ATOM 3008 CG1 ILE C 28 105.035 30.379 268.004 1.00 51.34 C ANISOU 3008 CG1 ILE C 28 5005 6070 8433 656 1769 -555 C ATOM 3009 CG2 ILE C 28 103.987 30.681 270.273 1.00 57.86 C ANISOU 3009 CG2 ILE C 28 5918 7177 8891 161 1439 -1030 C ATOM 3010 CD1 ILE C 28 105.733 29.078 268.334 1.00 60.60 C ANISOU 3010 CD1 ILE C 28 6304 7234 9488 709 1727 -328 C ATOM 3011 N PHE C 29 103.066 32.539 266.680 1.00 43.23 N ANISOU 3011 N PHE C 29 3915 5029 7481 658 1920 -872 N ATOM 3012 CA PHE C 29 101.862 32.523 265.856 1.00 46.53 C ANISOU 3012 CA PHE C 29 4506 5495 7679 667 1940 -889 C ATOM 3013 C PHE C 29 101.781 31.290 264.962 1.00 35.75 C ANISOU 3013 C PHE C 29 3408 4083 6092 792 2048 -759 C ATOM 3014 O PHE C 29 100.856 31.158 264.160 1.00 45.07 O ANISOU 3014 O PHE C 29 4722 5269 7132 801 2086 -768 O ATOM 3015 CB PHE C 29 101.800 33.788 264.997 1.00 48.76 C ANISOU 3015 CB PHE C 29 4718 5709 8099 729 1897 -779 C ATOM 3016 CG PHE C 29 102.091 35.052 265.757 1.00 51.93 C ANISOU 3016 CG PHE C 29 4917 6054 8761 634 1838 -891 C ATOM 3017 CD1 PHE C 29 101.084 35.712 266.440 1.00 37.58 C ANISOU 3017 CD1 PHE C 29 3060 4282 6938 513 1833 -1116 C ATOM 3018 CD2 PHE C 29 103.371 35.580 265.787 1.00 55.22 C ANISOU 3018 CD2 PHE C 29 5180 6339 9464 668 1815 -767 C ATOM 3019 CE1 PHE C 29 101.348 36.874 267.140 1.00 39.09 C ANISOU 3019 CE1 PHE C 29 3111 4355 7384 436 1831 -1278 C ATOM 3020 CE2 PHE C 29 103.641 36.741 266.485 1.00 45.74 C ANISOU 3020 CE2 PHE C 29 3784 5026 8571 560 1774 -914 C ATOM 3021 CZ PHE C 29 102.628 37.389 267.162 1.00 40.23 C ANISOU 3021 CZ PHE C 29 3096 4342 7846 447 1794 -1205 C ATOM 3022 N THR C 30 102.744 30.386 265.107 1.00 36.29 N ANISOU 3022 N THR C 30 3565 4071 6154 897 2124 -632 N ATOM 3023 CA THR C 30 102.844 29.231 264.221 1.00 36.67 C ANISOU 3023 CA THR C 30 3973 3987 5971 1060 2267 -489 C ATOM 3024 C THR C 30 102.430 27.922 264.887 1.00 41.82 C ANISOU 3024 C THR C 30 4902 4691 6298 901 2159 -557 C ATOM 3025 O THR C 30 102.639 26.844 264.332 1.00 40.18 O ANISOU 3025 O THR C 30 5059 4332 5875 1014 2244 -440 O ATOM 3026 CB THR C 30 104.275 29.076 263.677 1.00 38.03 C ANISOU 3026 CB THR C 30 4164 4017 6269 1280 2339 -178 C ATOM 3027 OG1 THR C 30 105.210 29.200 264.755 1.00 47.91 O ANISOU 3027 OG1 THR C 30 5105 5301 7800 1256 2286 -109 O ATOM 3028 CG2 THR C 30 104.567 30.146 262.646 1.00 38.42 C ANISOU 3028 CG2 THR C 30 4132 4032 6433 1343 2321 -43 C ATOM 3029 N ILE C 31 101.847 28.016 266.076 1.00 36.21 N ANISOU 3029 N ILE C 31 4056 4169 5532 644 1986 -738 N ATOM 3030 CA ILE C 31 101.328 26.834 266.753 1.00 45.74 C ANISOU 3030 CA ILE C 31 5502 5446 6431 460 1873 -782 C ATOM 3031 C ILE C 31 99.928 26.519 266.239 1.00 43.75 C ANISOU 3031 C ILE C 31 5439 5235 5950 302 1817 -869 C ATOM 3032 O ILE C 31 99.057 27.387 266.226 1.00 39.59 O ANISOU 3032 O ILE C 31 4700 4831 5513 207 1795 -979 O ATOM 3033 CB ILE C 31 101.297 27.021 268.281 1.00 43.01 C ANISOU 3033 CB ILE C 31 4970 5293 6079 252 1733 -907 C ATOM 3034 CG1 ILE C 31 102.723 27.090 268.829 1.00 50.08 C ANISOU 3034 CG1 ILE C 31 5714 6144 7170 347 1687 -759 C ATOM 3035 CG2 ILE C 31 100.527 25.890 268.944 1.00 36.99 C ANISOU 3035 CG2 ILE C 31 4437 4626 4993 42 1641 -940 C ATOM 3036 CD1 ILE C 31 102.797 27.217 270.332 1.00 48.95 C ANISOU 3036 CD1 ILE C 31 5476 6176 6948 119 1496 -869 C ATOM 3037 N TYR C 32 99.719 25.281 265.804 1.00 43.19 N ANISOU 3037 N TYR C 32 5764 5037 5609 269 1785 -794 N ATOM 3038 CA TYR C 32 98.432 24.886 265.244 1.00 37.45 C ANISOU 3038 CA TYR C 32 5237 4319 4672 68 1658 -829 C ATOM 3039 C TYR C 32 97.739 23.829 266.096 1.00 38.16 C ANISOU 3039 C TYR C 32 5460 4485 4553 -209 1515 -846 C ATOM 3040 O TYR C 32 96.554 23.553 265.909 1.00 56.88 O ANISOU 3040 O TYR C 32 7884 6914 6812 -451 1368 -849 O ATOM 3041 CB TYR C 32 98.606 24.370 263.812 1.00 38.60 C ANISOU 3041 CB TYR C 32 5832 4200 4633 208 1700 -735 C ATOM 3042 CG TYR C 32 99.204 22.984 263.719 1.00 40.00 C ANISOU 3042 CG TYR C 32 6491 4131 4577 279 1752 -657 C ATOM 3043 CD1 TYR C 32 100.572 22.786 263.844 1.00 56.29 C ANISOU 3043 CD1 TYR C 32 8569 6055 6762 582 1977 -537 C ATOM 3044 CD2 TYR C 32 98.399 21.873 263.497 1.00 41.57 C ANISOU 3044 CD2 TYR C 32 7118 4208 4468 40 1577 -673 C ATOM 3045 CE1 TYR C 32 101.122 21.520 263.757 1.00 59.21 C ANISOU 3045 CE1 TYR C 32 9374 6167 6957 693 2075 -436 C ATOM 3046 CE2 TYR C 32 98.939 20.603 263.409 1.00 43.28 C ANISOU 3046 CE2 TYR C 32 7822 4142 4480 118 1650 -611 C ATOM 3047 CZ TYR C 32 100.301 20.433 263.539 1.00 64.28 C ANISOU 3047 CZ TYR C 32 10495 6662 7268 469 1924 -493 C ATOM 3048 OH TYR C 32 100.844 19.171 263.452 1.00 75.80 O ANISOU 3048 OH TYR C 32 12431 7809 8559 592 2046 -402 O ATOM 3049 N ALA C 33 98.477 23.241 267.032 1.00 48.22 N ANISOU 3049 N ALA C 33 6763 5762 5799 -185 1543 -814 N ATOM 3050 CA ALA C 33 97.924 22.191 267.881 1.00 46.24 C ANISOU 3050 CA ALA C 33 6651 5568 5349 -430 1431 -793 C ATOM 3051 C ALA C 33 98.691 22.043 269.190 1.00 50.77 C ANISOU 3051 C ALA C 33 7090 6256 5946 -415 1446 -767 C ATOM 3052 O ALA C 33 99.900 22.270 269.247 1.00 54.74 O ANISOU 3052 O ALA C 33 7521 6688 6591 -193 1514 -695 O ATOM 3053 CB ALA C 33 97.908 20.866 267.134 1.00 40.73 C ANISOU 3053 CB ALA C 33 6471 4581 4423 -451 1384 -695 C ATOM 3054 N MET C 34 97.972 21.662 270.241 1.00 45.00 N ANISOU 3054 N MET C 34 6313 5706 5078 -662 1371 -788 N ATOM 3055 CA MET C 34 98.578 21.376 271.535 1.00 44.28 C ANISOU 3055 CA MET C 34 6172 5732 4919 -697 1341 -743 C ATOM 3056 C MET C 34 97.948 20.132 272.151 1.00 50.24 C ANISOU 3056 C MET C 34 7144 6503 5441 -924 1271 -637 C ATOM 3057 O MET C 34 96.849 19.731 271.771 1.00 63.87 O ANISOU 3057 O MET C 34 8959 8212 7095 -1112 1237 -631 O ATOM 3058 CB MET C 34 98.429 22.562 272.485 1.00 40.52 C ANISOU 3058 CB MET C 34 5384 5515 4498 -759 1362 -908 C ATOM 3059 CG MET C 34 99.223 23.795 272.098 1.00 55.97 C ANISOU 3059 CG MET C 34 7120 7435 6712 -564 1400 -993 C ATOM 3060 SD MET C 34 98.954 25.152 273.255 1.00 50.22 S ANISOU 3060 SD MET C 34 6149 6933 6000 -670 1423 -1234 S ATOM 3061 CE MET C 34 100.177 26.326 272.682 1.00 78.28 C ANISOU 3061 CE MET C 34 9493 10347 9904 -460 1402 -1254 C ATOM 3062 N GLY C 35 98.643 19.524 273.106 1.00 43.28 N ANISOU 3062 N GLY C 35 6329 5652 4465 -925 1224 -516 N ATOM 3063 CA GLY C 35 98.148 18.317 273.739 1.00 44.99 C ANISOU 3063 CA GLY C 35 6755 5866 4473 -1127 1169 -377 C ATOM 3064 C GLY C 35 98.772 18.028 275.089 1.00 53.92 C ANISOU 3064 C GLY C 35 7861 7150 5477 -1164 1105 -262 C ATOM 3065 O GLY C 35 99.645 18.761 275.554 1.00 55.78 O ANISOU 3065 O GLY C 35 7925 7489 5781 -1053 1060 -292 O ATOM 3066 N TRP C 36 98.317 16.950 275.719 1.00 69.48 N ANISOU 3066 N TRP C 36 10013 9128 7259 -1346 1069 -107 N ATOM 3067 CA TRP C 36 98.833 16.542 277.020 1.00 57.55 C ANISOU 3067 CA TRP C 36 8526 7765 5575 -1405 988 49 C ATOM 3068 C TRP C 36 99.438 15.143 276.969 1.00 51.72 C ANISOU 3068 C TRP C 36 8055 6767 4830 -1339 933 341 C ATOM 3069 O TRP C 36 98.896 14.243 276.328 1.00 52.19 O ANISOU 3069 O TRP C 36 8358 6583 4889 -1404 970 405 O ATOM 3070 CB TRP C 36 97.727 16.593 278.076 1.00 56.67 C ANISOU 3070 CB TRP C 36 8376 7940 5216 -1675 1043 11 C ATOM 3071 CG TRP C 36 97.341 17.982 278.482 1.00 53.92 C ANISOU 3071 CG TRP C 36 7802 7848 4836 -1693 1137 -251 C ATOM 3072 CD1 TRP C 36 96.328 18.737 277.966 1.00 57.36 C ANISOU 3072 CD1 TRP C 36 8065 8344 5384 -1729 1289 -428 C ATOM 3073 CD2 TRP C 36 97.964 18.783 279.493 1.00 52.05 C ANISOU 3073 CD2 TRP C 36 7519 7809 4448 -1679 1079 -354 C ATOM 3074 NE1 TRP C 36 96.282 19.958 278.594 1.00 66.34 N ANISOU 3074 NE1 TRP C 36 9062 9681 6463 -1701 1386 -646 N ATOM 3075 CE2 TRP C 36 97.276 20.012 279.535 1.00 61.60 C ANISOU 3075 CE2 TRP C 36 8572 9157 5676 -1688 1246 -629 C ATOM 3076 CE3 TRP C 36 99.037 18.581 280.366 1.00 53.81 C ANISOU 3076 CE3 TRP C 36 7833 8091 4523 -1675 875 -222 C ATOM 3077 CZ2 TRP C 36 97.626 21.033 280.415 1.00 59.10 C ANISOU 3077 CZ2 TRP C 36 8260 8995 5199 -1697 1233 -825 C ATOM 3078 CZ3 TRP C 36 99.383 19.596 281.239 1.00 59.36 C ANISOU 3078 CZ3 TRP C 36 8518 8979 5056 -1723 799 -398 C ATOM 3079 CH2 TRP C 36 98.679 20.806 281.257 1.00 66.39 C ANISOU 3079 CH2 TRP C 36 9325 9967 5935 -1736 986 -721 C ATOM 3080 N TYR C 37 100.567 14.972 277.648 1.00 60.28 N ANISOU 3080 N TYR C 37 9100 7881 5922 -1220 827 536 N ATOM 3081 CA TYR C 37 101.229 13.676 277.745 1.00 55.18 C ANISOU 3081 CA TYR C 37 8668 6994 5304 -1119 794 868 C ATOM 3082 C TYR C 37 101.503 13.340 279.206 1.00 63.11 C ANISOU 3082 C TYR C 37 9648 8239 6093 -1259 633 1086 C ATOM 3083 O TYR C 37 101.606 14.236 280.042 1.00 65.48 O ANISOU 3083 O TYR C 37 9772 8855 6253 -1360 519 980 O ATOM 3084 CB TYR C 37 102.534 13.671 276.947 1.00 66.20 C ANISOU 3084 CB TYR C 37 10018 8126 7008 -755 840 1015 C ATOM 3085 CG TYR C 37 102.351 13.768 275.448 1.00 81.55 C ANISOU 3085 CG TYR C 37 12109 9772 9105 -583 1031 854 C ATOM 3086 CD1 TYR C 37 102.091 14.989 274.837 1.00 77.27 C ANISOU 3086 CD1 TYR C 37 11369 9345 8645 -564 1072 578 C ATOM 3087 CD2 TYR C 37 102.450 12.641 274.642 1.00 78.43 C ANISOU 3087 CD2 TYR C 37 12100 8954 8745 -437 1171 982 C ATOM 3088 CE1 TYR C 37 101.925 15.081 273.468 1.00 87.29 C ANISOU 3088 CE1 TYR C 37 12806 10356 10007 -415 1227 455 C ATOM 3089 CE2 TYR C 37 102.287 12.725 273.272 1.00 66.36 C ANISOU 3089 CE2 TYR C 37 10800 7141 7275 -293 1334 823 C ATOM 3090 CZ TYR C 37 102.026 13.947 272.691 1.00 85.74 C ANISOU 3090 CZ TYR C 37 13035 9755 9788 -287 1349 571 C ATOM 3091 OH TYR C 37 101.863 14.036 271.327 1.00100.87 O ANISOU 3091 OH TYR C 37 15207 11401 11717 -151 1491 436 O ATOM 3092 N ARG C 38 101.618 12.052 279.512 1.00 71.80 N ANISOU 3092 N ARG C 38 10969 9167 7143 -1271 617 1391 N ATOM 3093 CA ARG C 38 101.903 11.621 280.877 1.00 79.35 C ANISOU 3093 CA ARG C 38 11934 10338 7876 -1399 450 1659 C ATOM 3094 C ARG C 38 102.863 10.437 280.896 1.00 69.37 C ANISOU 3094 C ARG C 38 10789 8789 6778 -1199 405 2092 C ATOM 3095 O ARG C 38 103.039 9.753 279.889 1.00 71.88 O ANISOU 3095 O ARG C 38 11283 8702 7326 -996 567 2157 O ATOM 3096 CB ARG C 38 100.610 11.256 281.611 1.00 83.80 C ANISOU 3096 CB ARG C 38 12641 11085 8116 -1723 512 1622 C ATOM 3097 CG ARG C 38 99.945 9.986 281.109 1.00 75.87 C ANISOU 3097 CG ARG C 38 11905 9754 7167 -1801 625 1767 C ATOM 3098 CD ARG C 38 98.681 9.677 281.896 1.00 83.34 C ANISOU 3098 CD ARG C 38 12913 10909 7845 -2138 689 1797 C ATOM 3099 NE ARG C 38 98.009 8.479 281.399 1.00 89.31 N ANISOU 3099 NE ARG C 38 13917 11327 8690 -2272 749 1948 N ATOM 3100 CZ ARG C 38 96.797 8.088 281.782 1.00 82.12 C ANISOU 3100 CZ ARG C 38 13036 10508 7659 -2583 821 2014 C ATOM 3101 NH1 ARG C 38 96.116 8.802 282.667 1.00 71.41 N ANISOU 3101 NH1 ARG C 38 11481 9576 6074 -2741 911 1942 N ATOM 3102 NH2 ARG C 38 96.265 6.984 281.277 1.00 88.52 N ANISOU 3102 NH2 ARG C 38 14089 10959 8587 -2735 818 2164 N ATOM 3103 N GLN C 39 103.480 10.201 282.048 1.00 68.51 N ANISOU 3103 N GLN C 39 10614 8877 6538 -1249 189 2398 N ATOM 3104 CA GLN C 39 104.411 9.090 282.198 1.00 74.33 C ANISOU 3104 CA GLN C 39 11413 9369 7461 -1049 134 2882 C ATOM 3105 C GLN C 39 104.355 8.504 283.604 1.00 75.17 C ANISOU 3105 C GLN C 39 11598 9713 7252 -1265 -72 3198 C ATOM 3106 O GLN C 39 104.804 9.125 284.567 1.00 76.71 O ANISOU 3106 O GLN C 39 11636 10260 7252 -1382 -348 3269 O ATOM 3107 CB GLN C 39 105.837 9.538 281.871 1.00 85.30 C ANISOU 3107 CB GLN C 39 12494 10696 9221 -736 33 3087 C ATOM 3108 CG GLN C 39 106.849 8.403 281.839 1.00 96.65 C ANISOU 3108 CG GLN C 39 13942 11821 10960 -440 55 3632 C ATOM 3109 CD GLN C 39 108.242 8.873 281.471 1.00104.15 C ANISOU 3109 CD GLN C 39 14506 12714 12354 -114 -7 3898 C ATOM 3110 OE1 GLN C 39 108.580 10.044 281.644 1.00116.66 O ANISOU 3110 OE1 GLN C 39 15783 14583 13960 -201 -213 3753 O ATOM 3111 NE2 GLN C 39 109.057 7.960 280.956 1.00103.06 N ANISOU 3111 NE2 GLN C 39 14380 12180 12598 271 194 4313 N ATOM 3112 N ALA C 40 103.795 7.304 283.714 1.00 84.60 N ANISOU 3112 N ALA C 40 13073 10696 8377 -1338 48 3393 N ATOM 3113 CA ALA C 40 103.709 6.608 284.991 1.00 97.42 C ANISOU 3113 CA ALA C 40 14804 12505 9708 -1527 -109 3748 C ATOM 3114 C ALA C 40 105.033 5.923 285.316 1.00112.23 C ANISOU 3114 C ALA C 40 16583 14239 11820 -1280 -291 4297 C ATOM 3115 O ALA C 40 105.757 5.513 284.408 1.00111.08 O ANISOU 3115 O ALA C 40 16401 13699 12104 -940 -156 4445 O ATOM 3116 CB ALA C 40 102.571 5.595 284.968 1.00 85.97 C ANISOU 3116 CB ALA C 40 13662 10861 8141 -1720 90 3782 C ATOM 3117 N PRO C 41 105.360 5.810 286.615 1.00120.93 N ANISOU 3117 N PRO C 41 17650 15661 12636 -1437 -586 4625 N ATOM 3118 CA PRO C 41 106.590 5.144 287.060 1.00129.00 C ANISOU 3118 CA PRO C 41 18535 16597 13884 -1236 -819 5235 C ATOM 3119 C PRO C 41 106.708 3.713 286.540 1.00137.21 C ANISOU 3119 C PRO C 41 19768 17112 15255 -989 -569 5594 C ATOM 3120 O PRO C 41 105.847 2.880 286.822 1.00126.30 O ANISOU 3120 O PRO C 41 18694 15622 13672 -1166 -438 5643 O ATOM 3121 CB PRO C 41 106.460 5.159 288.585 1.00123.56 C ANISOU 3121 CB PRO C 41 17925 16351 12670 -1556 -1149 5456 C ATOM 3122 CG PRO C 41 105.603 6.339 288.872 1.00117.59 C ANISOU 3122 CG PRO C 41 17232 15967 11478 -1844 -1138 4895 C ATOM 3123 CD PRO C 41 104.616 6.400 287.742 1.00111.04 C ANISOU 3123 CD PRO C 41 16491 14885 10813 -1804 -719 4446 C ATOM 3124 N GLY C 42 107.768 3.441 285.786 1.00138.32 N ANISOU 3124 N GLY C 42 19737 16904 15914 -578 -479 5856 N ATOM 3125 CA GLY C 42 107.987 2.121 285.226 1.00144.55 C ANISOU 3125 CA GLY C 42 20758 17121 17043 -278 -190 6186 C ATOM 3126 C GLY C 42 107.306 1.942 283.883 1.00142.74 C ANISOU 3126 C GLY C 42 20856 16442 16938 -175 222 5736 C ATOM 3127 O GLY C 42 107.271 0.839 283.338 1.00149.76 O ANISOU 3127 O GLY C 42 22083 16789 18029 18 494 5893 O ATOM 3128 N LYS C 43 106.760 3.031 283.351 1.00134.68 N ANISOU 3128 N LYS C 43 19768 15624 15781 -315 253 5181 N ATOM 3129 CA LYS C 43 106.080 2.996 282.061 1.00123.90 C ANISOU 3129 CA LYS C 43 18707 13884 14484 -263 574 4741 C ATOM 3130 C LYS C 43 106.595 4.099 281.140 1.00115.27 C ANISOU 3130 C LYS C 43 17369 12829 13600 -33 662 4453 C ATOM 3131 O LYS C 43 107.324 4.991 281.573 1.00120.45 O ANISOU 3131 O LYS C 43 17597 13843 14325 9 448 4541 O ATOM 3132 CB LYS C 43 104.566 3.125 282.248 1.00120.10 C ANISOU 3132 CB LYS C 43 18435 13584 13612 -726 553 4351 C ATOM 3133 CG LYS C 43 103.952 2.021 283.097 1.00119.38 C ANISOU 3133 CG LYS C 43 18593 13436 13329 -979 507 4644 C ATOM 3134 CD LYS C 43 102.443 2.172 283.206 1.00114.00 C ANISOU 3134 CD LYS C 43 18051 12925 12340 -1423 527 4311 C ATOM 3135 CE LYS C 43 101.773 2.028 281.849 1.00115.36 C ANISOU 3135 CE LYS C 43 18510 12674 12647 -1440 719 3946 C ATOM 3136 NZ LYS C 43 100.291 2.128 281.950 1.00112.76 N ANISOU 3136 NZ LYS C 43 18243 12507 12095 -1891 706 3710 N ATOM 3137 N GLN C 44 106.210 4.032 279.870 1.00120.52 N ANISOU 3137 N GLN C 44 18330 13111 14353 91 956 4124 N ATOM 3138 CA GLN C 44 106.673 4.996 278.877 1.00120.71 C ANISOU 3138 CA GLN C 44 18175 13116 14574 338 1097 3875 C ATOM 3139 C GLN C 44 105.749 6.207 278.787 1.00110.70 C ANISOU 3139 C GLN C 44 16774 12243 13045 8 972 3357 C ATOM 3140 O GLN C 44 104.648 6.204 279.338 1.00107.78 O ANISOU 3140 O GLN C 44 16503 12094 12354 -387 846 3169 O ATOM 3141 CB GLN C 44 106.793 4.332 277.504 1.00129.71 C ANISOU 3141 CB GLN C 44 19764 13621 15898 675 1498 3796 C ATOM 3142 CG GLN C 44 107.662 3.085 277.487 1.00137.65 C ANISOU 3142 CG GLN C 44 20973 14140 17188 1062 1721 4294 C ATOM 3143 CD GLN C 44 107.807 2.496 276.097 1.00142.29 C ANISOU 3143 CD GLN C 44 22099 14060 17904 1427 2173 4171 C ATOM 3144 OE1 GLN C 44 107.638 3.191 275.095 1.00138.89 O ANISOU 3144 OE1 GLN C 44 21762 13580 17430 1497 2322 3800 O ATOM 3145 NE2 GLN C 44 108.117 1.206 276.030 1.00145.74 N ANISOU 3145 NE2 GLN C 44 22774 14118 18481 1597 2302 4327 N ATOM 3146 N ARG C 45 106.208 7.241 278.088 1.00108.80 N ANISOU 3146 N ARG C 45 16290 12075 12976 192 1039 3166 N ATOM 3147 CA ARG C 45 105.413 8.446 277.881 1.00 96.42 C ANISOU 3147 CA ARG C 45 14585 10826 11224 -56 961 2694 C ATOM 3148 C ARG C 45 104.314 8.189 276.855 1.00 82.09 C ANISOU 3148 C ARG C 45 13179 8738 9275 -170 1141 2339 C ATOM 3149 O ARG C 45 104.581 7.697 275.759 1.00 77.00 O ANISOU 3149 O ARG C 45 12850 7639 8769 98 1389 2331 O ATOM 3150 CB ARG C 45 106.305 9.605 277.430 1.00105.40 C ANISOU 3150 CB ARG C 45 15333 12089 12628 181 971 2649 C ATOM 3151 CG ARG C 45 105.570 10.917 277.217 1.00109.87 C ANISOU 3151 CG ARG C 45 15739 12957 13048 -40 904 2186 C ATOM 3152 CD ARG C 45 106.535 12.037 276.857 1.00112.81 C ANISOU 3152 CD ARG C 45 15712 13432 13720 177 891 2197 C ATOM 3153 NE ARG C 45 107.524 12.264 277.907 1.00121.42 N ANISOU 3153 NE ARG C 45 16436 14767 14932 167 604 2537 N ATOM 3154 CZ ARG C 45 108.476 13.190 277.852 1.00113.94 C ANISOU 3154 CZ ARG C 45 15077 13935 14279 287 491 2645 C ATOM 3155 NH1 ARG C 45 108.572 13.983 276.794 1.00107.70 N ANISOU 3155 NH1 ARG C 45 14185 13042 13695 459 694 2439 N ATOM 3156 NH2 ARG C 45 109.332 13.325 278.856 1.00105.76 N ANISOU 3156 NH2 ARG C 45 13732 13116 13335 212 148 2986 N ATOM 3157 N GLU C 46 103.079 8.525 277.214 1.00 76.04 N ANISOU 3157 N GLU C 46 12419 8240 8234 -569 1017 2067 N ATOM 3158 CA GLU C 46 101.935 8.249 276.352 1.00 74.35 C ANISOU 3158 CA GLU C 46 12543 7803 7903 -762 1096 1793 C ATOM 3159 C GLU C 46 101.032 9.468 276.178 1.00 78.49 C ANISOU 3159 C GLU C 46 12823 8676 8324 -988 1031 1426 C ATOM 3160 O GLU C 46 100.923 10.309 277.071 1.00 98.31 O ANISOU 3160 O GLU C 46 14983 11623 10746 -1116 923 1370 O ATOM 3161 CB GLU C 46 101.126 7.076 276.912 1.00 84.66 C ANISOU 3161 CB GLU C 46 14140 8984 9045 -1060 1032 1948 C ATOM 3162 CG GLU C 46 100.549 7.322 278.299 1.00102.45 C ANISOU 3162 CG GLU C 46 16119 11719 11086 -1377 872 2024 C ATOM 3163 CD GLU C 46 99.901 6.084 278.891 1.00124.61 C ANISOU 3163 CD GLU C 46 19191 14382 13774 -1635 838 2268 C ATOM 3164 OE1 GLU C 46 100.472 4.983 278.744 1.00131.06 O ANISOU 3164 OE1 GLU C 46 20309 14785 14703 -1471 894 2533 O ATOM 3165 OE2 GLU C 46 98.819 6.213 279.502 1.00131.28 O ANISOU 3165 OE2 GLU C 46 19936 15508 14435 -1988 786 2221 O ATOM 3166 N LEU C 47 100.389 9.556 275.017 1.00 73.23 N ANISOU 3166 N LEU C 47 12378 7789 7657 -1031 1097 1185 N ATOM 3167 CA LEU C 47 99.447 10.633 274.729 1.00 62.77 C ANISOU 3167 CA LEU C 47 10825 6746 6279 -1235 1043 883 C ATOM 3168 C LEU C 47 98.091 10.337 275.358 1.00 68.64 C ANISOU 3168 C LEU C 47 11544 7675 6860 -1665 935 881 C ATOM 3169 O LEU C 47 97.622 9.200 275.327 1.00 94.14 O ANISOU 3169 O LEU C 47 15097 10642 10032 -1848 892 1021 O ATOM 3170 CB LEU C 47 99.301 10.827 273.217 1.00 62.39 C ANISOU 3170 CB LEU C 47 11025 6395 6284 -1124 1117 680 C ATOM 3171 CG LEU C 47 98.279 11.856 272.727 1.00 70.58 C ANISOU 3171 CG LEU C 47 11853 7664 7302 -1324 1046 415 C ATOM 3172 CD1 LEU C 47 98.622 13.246 273.234 1.00 83.32 C ANISOU 3172 CD1 LEU C 47 12960 9687 9011 -1214 1075 305 C ATOM 3173 CD2 LEU C 47 98.192 11.844 271.208 1.00 75.67 C ANISOU 3173 CD2 LEU C 47 12849 7962 7942 -1226 1081 268 C ATOM 3174 N VAL C 48 97.462 11.359 275.931 1.00 63.55 N ANISOU 3174 N VAL C 48 10522 7461 6165 -1818 918 743 N ATOM 3175 CA VAL C 48 96.165 11.177 276.574 1.00 74.63 C ANISOU 3175 CA VAL C 48 11826 9076 7453 -2187 888 788 C ATOM 3176 C VAL C 48 95.090 12.082 275.977 1.00 77.80 C ANISOU 3176 C VAL C 48 11996 9634 7930 -2336 896 579 C ATOM 3177 O VAL C 48 93.912 11.724 275.960 1.00 79.34 O ANISOU 3177 O VAL C 48 12164 9851 8131 -2648 851 658 O ATOM 3178 CB VAL C 48 96.252 11.429 278.095 1.00 73.15 C ANISOU 3178 CB VAL C 48 11422 9280 7092 -2245 925 896 C ATOM 3179 CG1 VAL C 48 97.074 10.341 278.759 1.00 95.53 C ANISOU 3179 CG1 VAL C 48 14479 11968 9849 -2177 870 1194 C ATOM 3180 CG2 VAL C 48 96.841 12.800 278.388 1.00 56.82 C ANISOU 3180 CG2 VAL C 48 9066 7499 5022 -2057 959 689 C ATOM 3181 N ALA C 49 95.498 13.246 275.481 1.00 53.94 N ANISOU 3181 N ALA C 49 8778 6713 5005 -2119 946 359 N ATOM 3182 CA ALA C 49 94.560 14.202 274.905 1.00 67.44 C ANISOU 3182 CA ALA C 49 10234 8572 6820 -2214 962 188 C ATOM 3183 C ALA C 49 95.276 15.221 274.026 1.00 61.24 C ANISOU 3183 C ALA C 49 9367 7736 6166 -1923 998 -18 C ATOM 3184 O ALA C 49 96.166 15.934 274.487 1.00 58.54 O ANISOU 3184 O ALA C 49 8868 7530 5847 -1707 1066 -91 O ATOM 3185 CB ALA C 49 93.779 14.909 276.005 1.00 72.07 C ANISOU 3185 CB ALA C 49 10458 9570 7354 -2349 1090 175 C ATOM 3186 N ARG C 50 94.880 15.283 272.759 1.00 61.64 N ANISOU 3186 N ARG C 50 9538 7585 6296 -1942 926 -89 N ATOM 3187 CA ARG C 50 95.448 16.242 271.819 1.00 67.64 C ANISOU 3187 CA ARG C 50 10233 8289 7177 -1677 978 -252 C ATOM 3188 C ARG C 50 94.346 16.982 271.070 1.00 47.36 C ANISOU 3188 C ARG C 50 7471 5817 4708 -1822 914 -336 C ATOM 3189 O ARG C 50 93.387 16.372 270.598 1.00 50.55 O ANISOU 3189 O ARG C 50 8013 6115 5079 -2100 750 -249 O ATOM 3190 CB ARG C 50 96.378 15.540 270.825 1.00 78.87 C ANISOU 3190 CB ARG C 50 12103 9299 8566 -1455 987 -220 C ATOM 3191 CG ARG C 50 96.886 16.439 269.707 1.00 53.80 C ANISOU 3191 CG ARG C 50 8909 6036 5496 -1187 1068 -348 C ATOM 3192 CD ARG C 50 97.673 15.649 268.674 1.00 56.98 C ANISOU 3192 CD ARG C 50 9834 5998 5820 -958 1145 -300 C ATOM 3193 NE ARG C 50 98.067 16.477 267.537 1.00 55.51 N ANISOU 3193 NE ARG C 50 9668 5725 5699 -710 1250 -394 N ATOM 3194 CZ ARG C 50 97.306 16.688 266.468 1.00 56.02 C ANISOU 3194 CZ ARG C 50 9924 5697 5664 -831 1139 -485 C ATOM 3195 NH1 ARG C 50 96.104 16.134 266.387 1.00 69.66 N ANISOU 3195 NH1 ARG C 50 11804 7405 7259 -1222 887 -483 N ATOM 3196 NH2 ARG C 50 97.745 17.454 265.479 1.00 55.02 N ANISOU 3196 NH2 ARG C 50 9823 5502 5580 -580 1259 -540 N ATOM 3197 N ILE C 51 94.483 18.300 270.968 1.00 45.51 N ANISOU 3197 N ILE C 51 6906 5768 4619 -1652 1017 -476 N ATOM 3198 CA ILE C 51 93.514 19.101 270.233 1.00 62.29 C ANISOU 3198 CA ILE C 51 8803 7982 6882 -1740 969 -517 C ATOM 3199 C ILE C 51 94.217 20.104 269.320 1.00 60.56 C ANISOU 3199 C ILE C 51 8538 7690 6784 -1447 1036 -645 C ATOM 3200 O ILE C 51 95.211 20.726 269.698 1.00 60.23 O ANISOU 3200 O ILE C 51 8380 7694 6813 -1203 1176 -731 O ATOM 3201 CB ILE C 51 92.547 19.842 271.192 1.00 62.31 C ANISOU 3201 CB ILE C 51 8345 8334 6996 -1868 1088 -513 C ATOM 3202 CG1 ILE C 51 91.434 20.541 270.407 1.00 53.91 C ANISOU 3202 CG1 ILE C 51 7003 7347 6132 -1969 1026 -467 C ATOM 3203 CG2 ILE C 51 93.294 20.832 272.079 1.00 44.56 C ANISOU 3203 CG2 ILE C 51 5890 6262 4777 -1640 1294 -676 C ATOM 3204 CD1 ILE C 51 90.356 21.140 271.282 1.00 48.01 C ANISOU 3204 CD1 ILE C 51 5802 6904 5535 -2074 1201 -397 C ATOM 3205 N THR C 52 93.710 20.235 268.099 1.00 46.82 N ANISOU 3205 N THR C 52 6902 5824 5063 -1496 909 -627 N ATOM 3206 CA THR C 52 94.236 21.219 267.167 1.00 48.64 C ANISOU 3206 CA THR C 52 7081 5996 5405 -1233 982 -709 C ATOM 3207 C THR C 52 93.429 22.503 267.285 1.00 52.47 C ANISOU 3207 C THR C 52 7063 6742 6130 -1256 1028 -739 C ATOM 3208 O THR C 52 92.357 22.517 267.890 1.00 60.13 O ANISOU 3208 O THR C 52 7768 7908 7169 -1480 999 -669 O ATOM 3209 CB THR C 52 94.200 20.710 265.714 1.00 43.80 C ANISOU 3209 CB THR C 52 6929 5087 4626 -1243 830 -668 C ATOM 3210 OG1 THR C 52 94.788 21.689 264.849 1.00103.10 O ANISOU 3210 OG1 THR C 52 14390 12552 12233 -957 948 -719 O ATOM 3211 CG2 THR C 52 92.770 20.448 265.276 1.00 46.02 C ANISOU 3211 CG2 THR C 52 7200 5408 4876 -1617 537 -562 C ATOM 3212 N PHE C 53 93.944 23.583 266.709 1.00 49.60 N ANISOU 3212 N PHE C 53 6558 6365 5923 -1006 1135 -812 N ATOM 3213 CA PHE C 53 93.247 24.862 266.759 1.00 45.80 C ANISOU 3213 CA PHE C 53 5621 6078 5702 -981 1212 -833 C ATOM 3214 C PHE C 53 92.086 24.872 265.769 1.00 51.97 C ANISOU 3214 C PHE C 53 6359 6864 6524 -1164 999 -674 C ATOM 3215 O PHE C 53 91.272 25.795 265.760 1.00 48.95 O ANISOU 3215 O PHE C 53 5566 6642 6390 -1174 1040 -614 O ATOM 3216 CB PHE C 53 94.208 26.020 266.474 1.00 46.98 C ANISOU 3216 CB PHE C 53 5635 6181 6036 -670 1381 -939 C ATOM 3217 CG PHE C 53 95.170 26.307 267.598 1.00 37.89 C ANISOU 3217 CG PHE C 53 4395 5079 4925 -552 1534 -1072 C ATOM 3218 CD1 PHE C 53 95.143 25.562 268.766 1.00 43.14 C ANISOU 3218 CD1 PHE C 53 5126 5841 5426 -698 1527 -1093 C ATOM 3219 CD2 PHE C 53 96.094 27.333 267.488 1.00 41.08 C ANISOU 3219 CD2 PHE C 53 4651 5427 5531 -322 1652 -1149 C ATOM 3220 CE1 PHE C 53 96.025 25.827 269.796 1.00 42.68 C ANISOU 3220 CE1 PHE C 53 5019 5833 5365 -626 1600 -1195 C ATOM 3221 CE2 PHE C 53 96.976 27.605 268.517 1.00 36.64 C ANISOU 3221 CE2 PHE C 53 4016 4899 5006 -272 1709 -1249 C ATOM 3222 CZ PHE C 53 96.942 26.850 269.671 1.00 37.34 C ANISOU 3222 CZ PHE C 53 4201 5095 4890 -428 1666 -1276 C ATOM 3223 N GLY C 54 92.015 23.835 264.940 1.00 63.89 N ANISOU 3223 N GLY C 54 8313 8175 7789 -1314 761 -591 N ATOM 3224 CA GLY C 54 90.923 23.679 263.999 1.00 67.93 C ANISOU 3224 CA GLY C 54 8860 8668 8281 -1569 452 -416 C ATOM 3225 C GLY C 54 89.697 23.077 264.658 1.00 60.06 C ANISOU 3225 C GLY C 54 7642 7824 7354 -1940 288 -248 C ATOM 3226 O GLY C 54 88.574 23.264 264.189 1.00 62.68 O ANISOU 3226 O GLY C 54 7733 8250 7832 -2169 53 -36 O ATOM 3227 N GLY C 55 89.913 22.347 265.748 1.00 47.93 N ANISOU 3227 N GLY C 55 6161 6316 5735 -2003 406 -295 N ATOM 3228 CA GLY C 55 88.816 21.771 266.505 1.00 50.28 C ANISOU 3228 CA GLY C 55 6221 6767 6115 -2332 321 -108 C ATOM 3229 C GLY C 55 88.889 20.264 266.672 1.00 52.65 C ANISOU 3229 C GLY C 55 6979 6868 6159 -2590 135 -58 C ATOM 3230 O GLY C 55 88.294 19.711 267.597 1.00 80.47 O ANISOU 3230 O GLY C 55 10332 10513 9729 -2805 162 76 O ATOM 3231 N ASP C 56 89.614 19.599 265.778 1.00 53.29 N ANISOU 3231 N ASP C 56 7662 6619 5967 -2552 -19 -152 N ATOM 3232 CA ASP C 56 89.724 18.143 265.809 1.00 53.63 C ANISOU 3232 CA ASP C 56 8231 6385 5762 -2777 -191 -117 C ATOM 3233 C ASP C 56 90.429 17.661 267.074 1.00 52.28 C ANISOU 3233 C ASP C 56 8061 6257 5547 -2645 79 -170 C ATOM 3234 O ASP C 56 91.557 18.061 267.358 1.00 49.75 O ANISOU 3234 O ASP C 56 7763 5937 5201 -2285 340 -322 O ATOM 3235 CB ASP C 56 90.466 17.634 264.572 1.00 62.10 C ANISOU 3235 CB ASP C 56 10014 7053 6530 -2673 -313 -235 C ATOM 3236 CG ASP C 56 89.836 18.112 263.279 1.00 68.68 C ANISOU 3236 CG ASP C 56 10930 7837 7327 -2807 -612 -180 C ATOM 3237 OD1 ASP C 56 88.874 17.469 262.808 1.00 67.33 O ANISOU 3237 OD1 ASP C 56 10944 7558 7081 -3242 -1028 -30 O ATOM 3238 OD2 ASP C 56 90.307 19.130 262.731 1.00 74.42 O ANISOU 3238 OD2 ASP C 56 11541 8632 8105 -2497 -459 -263 O ATOM 3239 N THR C 57 89.754 16.797 267.825 1.00 66.45 N ANISOU 3239 N THR C 57 9815 8088 7344 -2959 -9 -6 N ATOM 3240 CA THR C 57 90.289 16.287 269.082 1.00 58.85 C ANISOU 3240 CA THR C 57 8851 7191 6319 -2880 212 -3 C ATOM 3241 C THR C 57 90.703 14.824 268.971 1.00 64.72 C ANISOU 3241 C THR C 57 10192 7557 6843 -3002 81 45 C ATOM 3242 O THR C 57 90.191 14.083 268.132 1.00 60.41 O ANISOU 3242 O THR C 57 10018 6727 6209 -3283 -219 110 O ATOM 3243 CB THR C 57 89.267 16.428 270.224 1.00 67.72 C ANISOU 3243 CB THR C 57 9465 8659 7607 -3095 312 180 C ATOM 3244 OG1 THR C 57 88.099 15.656 269.920 1.00 78.85 O ANISOU 3244 OG1 THR C 57 10876 9991 9091 -3540 16 433 O ATOM 3245 CG2 THR C 57 88.874 17.884 270.409 1.00 66.95 C ANISOU 3245 CG2 THR C 57 8811 8891 7735 -2925 516 127 C ATOM 3246 N ASN C 58 91.633 14.415 269.829 1.00 66.71 N ANISOU 3246 N ASN C 58 10553 7786 7006 -2799 288 23 N ATOM 3247 CA ASN C 58 92.111 13.039 269.852 1.00 71.77 C ANISOU 3247 CA ASN C 58 11735 8057 7477 -2854 227 96 C ATOM 3248 C ASN C 58 92.399 12.580 271.278 1.00 67.15 C ANISOU 3248 C ASN C 58 11006 7633 6876 -2842 385 227 C ATOM 3249 O ASN C 58 93.204 13.187 271.983 1.00 70.31 O ANISOU 3249 O ASN C 58 11181 8247 7287 -2556 594 165 O ATOM 3250 CB ASN C 58 93.363 12.894 268.986 1.00 80.67 C ANISOU 3250 CB ASN C 58 13336 8831 8482 -2483 329 -47 C ATOM 3251 CG ASN C 58 93.851 11.461 268.899 1.00112.44 C ANISOU 3251 CG ASN C 58 17977 12399 12348 -2494 312 31 C ATOM 3252 OD1 ASN C 58 93.080 10.517 269.072 1.00128.16 O ANISOU 3252 OD1 ASN C 58 20167 14237 14291 -2867 112 159 O ATOM 3253 ND2 ASN C 58 95.141 11.292 268.628 1.00119.74 N ANISOU 3253 ND2 ASN C 58 19190 13081 13226 -2076 539 -14 N ATOM 3254 N TYR C 59 91.737 11.507 271.698 1.00 61.56 N ANISOU 3254 N TYR C 59 10440 6814 6134 -3180 257 429 N ATOM 3255 CA TYR C 59 91.901 10.993 273.052 1.00 60.51 C ANISOU 3255 CA TYR C 59 10198 6835 5957 -3206 393 601 C ATOM 3256 C TYR C 59 92.518 9.600 273.061 1.00 75.02 C ANISOU 3256 C TYR C 59 12581 8242 7682 -3207 345 721 C ATOM 3257 O TYR C 59 92.500 8.893 272.053 1.00 88.20 O ANISOU 3257 O TYR C 59 14741 9467 9303 -3294 184 684 O ATOM 3258 CB TYR C 59 90.556 10.962 273.780 1.00 62.66 C ANISOU 3258 CB TYR C 59 10083 7397 6327 -3585 367 813 C ATOM 3259 CG TYR C 59 89.913 12.319 273.954 1.00 61.23 C ANISOU 3259 CG TYR C 59 9338 7640 6286 -3542 500 739 C ATOM 3260 CD1 TYR C 59 90.187 13.100 275.069 1.00 59.96 C ANISOU 3260 CD1 TYR C 59 8860 7849 6074 -3337 787 688 C ATOM 3261 CD2 TYR C 59 89.029 12.816 273.006 1.00 61.70 C ANISOU 3261 CD2 TYR C 59 9213 7707 6521 -3709 331 734 C ATOM 3262 CE1 TYR C 59 89.599 14.340 275.235 1.00 59.19 C ANISOU 3262 CE1 TYR C 59 8305 8081 6105 -3269 958 607 C ATOM 3263 CE2 TYR C 59 88.437 14.055 273.163 1.00 72.33 C ANISOU 3263 CE2 TYR C 59 10030 9412 8041 -3634 489 701 C ATOM 3264 CZ TYR C 59 88.725 14.812 274.279 1.00 59.55 C ANISOU 3264 CZ TYR C 59 8130 8120 6377 -3398 831 625 C ATOM 3265 OH TYR C 59 88.137 16.045 274.438 1.00 59.17 O ANISOU 3265 OH TYR C 59 7611 8372 6500 -3295 1035 578 O ATOM 3266 N ALA C 60 93.063 9.212 274.209 1.00 77.82 N ANISOU 3266 N ALA C 60 12881 8710 7976 -3106 485 871 N ATOM 3267 CA ALA C 60 93.585 7.865 274.390 1.00 75.14 C ANISOU 3267 CA ALA C 60 13000 7982 7570 -3104 464 1052 C ATOM 3268 C ALA C 60 92.436 6.895 274.650 1.00 83.49 C ANISOU 3268 C ALA C 60 14155 8921 8648 -3584 299 1280 C ATOM 3269 O ALA C 60 91.331 7.311 274.993 1.00 94.75 O ANISOU 3269 O ALA C 60 15181 10669 10151 -3877 256 1358 O ATOM 3270 CB ALA C 60 94.588 7.829 275.532 1.00 68.97 C ANISOU 3270 CB ALA C 60 12091 7385 6728 -2836 630 1186 C ATOM 3271 N ASP C 61 92.703 5.604 274.482 1.00 80.59 N ANISOU 3271 N ASP C 61 14307 8070 8245 -3653 227 1415 N ATOM 3272 CA ASP C 61 91.685 4.574 274.667 1.00 79.52 C ANISOU 3272 CA ASP C 61 14322 7734 8158 -4137 39 1655 C ATOM 3273 C ASP C 61 91.202 4.489 276.115 1.00 85.82 C ANISOU 3273 C ASP C 61 14689 8948 8972 -4302 155 1954 C ATOM 3274 O ASP C 61 90.004 4.377 276.375 1.00 94.86 O ANISOU 3274 O ASP C 61 15574 10244 10224 -4714 59 2141 O ATOM 3275 CB ASP C 61 92.224 3.214 274.221 1.00 91.27 C ANISOU 3275 CB ASP C 61 16527 8554 9598 -4121 -22 1720 C ATOM 3276 N SER C 62 92.138 4.551 277.055 1.00 79.91 N ANISOU 3276 N SER C 62 13860 8387 8115 -3983 362 2030 N ATOM 3277 CA SER C 62 91.811 4.377 278.466 1.00 91.51 C ANISOU 3277 CA SER C 62 15042 10215 9512 -4110 487 2324 C ATOM 3278 C SER C 62 91.115 5.597 279.054 1.00 93.50 C ANISOU 3278 C SER C 62 14727 11062 9736 -4154 633 2257 C ATOM 3279 O SER C 62 90.363 5.485 280.021 1.00104.51 O ANISOU 3279 O SER C 62 15872 12744 11093 -4369 752 2507 O ATOM 3280 CB SER C 62 93.077 4.077 279.267 1.00 97.56 C ANISOU 3280 CB SER C 62 15936 10992 10140 -3767 605 2445 C ATOM 3281 OG SER C 62 94.045 5.095 279.074 1.00 90.98 O ANISOU 3281 OG SER C 62 14964 10339 9264 -3371 677 2190 O ATOM 3282 N VAL C 63 91.353 6.755 278.446 1.00 93.44 N ANISOU 3282 N VAL C 63 14540 11210 9755 -3933 659 1935 N ATOM 3283 CA VAL C 63 90.938 8.039 279.006 1.00 89.30 C ANISOU 3283 CA VAL C 63 13533 11205 9193 -3866 848 1819 C ATOM 3284 C VAL C 63 89.584 8.503 278.449 1.00 80.80 C ANISOU 3284 C VAL C 63 12130 10238 8330 -4145 812 1824 C ATOM 3285 O VAL C 63 88.759 9.067 279.180 1.00 78.71 O ANISOU 3285 O VAL C 63 11461 10358 8086 -4236 1021 1931 O ATOM 3286 CB VAL C 63 92.034 9.113 278.744 1.00 89.25 C ANISOU 3286 CB VAL C 63 13481 11303 9126 -3455 902 1494 C ATOM 3287 CG1 VAL C 63 91.436 10.481 278.506 1.00 91.01 C ANISOU 3287 CG1 VAL C 63 13306 11839 9435 -3417 1008 1271 C ATOM 3288 CG2 VAL C 63 93.036 9.156 279.900 1.00 83.78 C ANISOU 3288 CG2 VAL C 63 12821 10805 8207 -3237 998 1561 C ATOM 3289 N LYS C 64 89.372 8.239 277.160 1.00 80.76 N ANISOU 3289 N LYS C 64 12324 9881 8478 -4273 552 1735 N ATOM 3290 CA LYS C 64 88.167 8.632 276.425 1.00 79.65 C ANISOU 3290 CA LYS C 64 11899 9793 8571 -4559 409 1769 C ATOM 3291 C LYS C 64 86.866 8.422 277.195 1.00 76.42 C ANISOU 3291 C LYS C 64 11074 9641 8322 -4915 498 2138 C ATOM 3292 O LYS C 64 86.588 7.324 277.674 1.00 80.51 O ANISOU 3292 O LYS C 64 11743 10006 8842 -5180 443 2432 O ATOM 3293 CB LYS C 64 88.096 7.861 275.105 1.00 84.02 C ANISOU 3293 CB LYS C 64 12912 9828 9184 -4776 32 1725 C ATOM 3294 N GLY C 65 86.072 9.483 277.301 1.00 76.26 N ANISOU 3294 N GLY C 65 10516 9994 8464 -4902 666 2153 N ATOM 3295 CA GLY C 65 84.792 9.410 277.977 1.00 80.21 C ANISOU 3295 CA GLY C 65 10540 10760 9175 -5188 825 2544 C ATOM 3296 C GLY C 65 84.841 10.015 279.365 1.00 98.82 C ANISOU 3296 C GLY C 65 12646 13549 11354 -4936 1327 2579 C ATOM 3297 O GLY C 65 83.806 10.234 279.992 1.00102.35 O ANISOU 3297 O GLY C 65 12647 14281 11962 -5058 1603 2878 O ATOM 3298 N ARG C 66 86.050 10.292 279.843 1.00 92.09 N ANISOU 3298 N ARG C 66 12093 12734 10163 -4584 1449 2291 N ATOM 3299 CA ARG C 66 86.230 10.847 281.180 1.00 99.32 C ANISOU 3299 CA ARG C 66 12911 14022 10806 -4361 1868 2278 C ATOM 3300 C ARG C 66 86.880 12.231 281.152 1.00 99.85 C ANISOU 3300 C ARG C 66 12922 14267 10748 -3978 2020 1861 C ATOM 3301 O ARG C 66 86.427 13.150 281.835 1.00 87.12 O ANISOU 3301 O ARG C 66 11049 12972 9081 -3841 2393 1820 O ATOM 3302 CB ARG C 66 87.058 9.886 282.040 1.00 83.09 C ANISOU 3302 CB ARG C 66 11263 11883 8425 -4347 1847 2392 C ATOM 3303 CG ARG C 66 86.405 8.524 282.237 1.00 86.95 C ANISOU 3303 CG ARG C 66 11815 12193 9031 -4725 1747 2835 C ATOM 3304 CD ARG C 66 87.149 7.666 283.255 1.00 90.66 C ANISOU 3304 CD ARG C 66 12639 12635 9173 -4684 1792 3003 C ATOM 3305 NE ARG C 66 88.509 7.352 282.828 1.00 88.56 N ANISOU 3305 NE ARG C 66 12793 12073 8780 -4470 1529 2780 N ATOM 3306 CZ ARG C 66 89.602 7.900 283.349 1.00 87.04 C ANISOU 3306 CZ ARG C 66 12737 12033 8300 -4146 1586 2570 C ATOM 3307 NH1 ARG C 66 89.497 8.789 284.327 1.00 89.41 N ANISOU 3307 NH1 ARG C 66 12875 12754 8342 -4018 1872 2499 N ATOM 3308 NH2 ARG C 66 90.800 7.556 282.897 1.00 92.99 N ANISOU 3308 NH2 ARG C 66 13802 12501 9028 -3953 1359 2450 N ATOM 3309 N PHE C 67 87.939 12.380 280.363 1.00 94.12 N ANISOU 3309 N PHE C 67 10039 14777 10945 -3528 1781 506 N ATOM 3310 CA PHE C 67 88.613 13.671 280.254 1.00 82.88 C ANISOU 3310 CA PHE C 67 9116 13380 8996 -3201 1989 262 C ATOM 3311 C PHE C 67 88.090 14.449 279.051 1.00 78.60 C ANISOU 3311 C PHE C 67 8226 13141 8499 -2958 2004 141 C ATOM 3312 O PHE C 67 87.718 13.863 278.035 1.00 79.42 O ANISOU 3312 O PHE C 67 7874 13330 8971 -2942 1531 46 O ATOM 3313 CB PHE C 67 90.133 13.513 280.127 1.00 67.23 C ANISOU 3313 CB PHE C 67 7656 11202 6687 -3346 1647 -54 C ATOM 3314 CG PHE C 67 90.798 12.857 281.308 1.00 69.58 C ANISOU 3314 CG PHE C 67 8349 11252 6836 -3524 1610 -10 C ATOM 3315 CD1 PHE C 67 90.070 12.435 282.408 1.00 81.87 C ANISOU 3315 CD1 PHE C 67 9817 12786 8505 -3520 1913 364 C ATOM 3316 CD2 PHE C 67 92.169 12.672 281.310 1.00 60.67 C ANISOU 3316 CD2 PHE C 67 7664 9952 5435 -3672 1298 -333 C ATOM 3317 CE1 PHE C 67 90.698 11.834 283.476 1.00 83.16 C ANISOU 3317 CE1 PHE C 67 10354 12785 8458 -3638 1898 434 C ATOM 3318 CE2 PHE C 67 92.799 12.075 282.375 1.00 62.57 C ANISOU 3318 CE2 PHE C 67 8267 10009 5498 -3826 1242 -329 C ATOM 3319 CZ PHE C 67 92.068 11.656 283.457 1.00 62.93 C ANISOU 3319 CZ PHE C 67 8252 10056 5601 -3794 1537 64 C ATOM 3320 N THR C 68 88.076 15.772 279.172 1.00 80.76 N ANISOU 3320 N THR C 68 8820 13367 8500 -2532 2357 103 N ATOM 3321 CA THR C 68 87.630 16.643 278.093 1.00 79.65 C ANISOU 3321 CA THR C 68 8468 13456 8338 -2177 2399 28 C ATOM 3322 C THR C 68 88.661 17.741 277.865 1.00 69.37 C ANISOU 3322 C THR C 68 7759 11893 6706 -1920 2465 -118 C ATOM 3323 O THR C 68 88.971 18.507 278.776 1.00 75.12 O ANISOU 3323 O THR C 68 8905 12286 7349 -1746 2700 -109 O ATOM 3324 CB THR C 68 86.255 17.271 278.403 1.00 81.27 C ANISOU 3324 CB THR C 68 8304 13881 8695 -1891 2829 206 C ATOM 3325 OG1 THR C 68 85.303 16.234 278.669 1.00100.05 O ANISOU 3325 OG1 THR C 68 10073 16403 11537 -2142 2772 392 O ATOM 3326 CG2 THR C 68 85.764 18.109 277.231 1.00 77.47 C ANISOU 3326 CG2 THR C 68 7659 13526 8249 -1392 2723 122 C ATOM 3327 N ILE C 69 89.202 17.808 276.653 1.00 55.72 N ANISOU 3327 N ILE C 69 6034 10250 4887 -1810 2174 -232 N ATOM 3328 CA ILE C 69 90.220 18.802 276.343 1.00 63.00 C ANISOU 3328 CA ILE C 69 7434 10890 5614 -1613 2262 -281 C ATOM 3329 C ILE C 69 89.602 19.982 275.599 1.00 71.15 C ANISOU 3329 C ILE C 69 8400 12055 6579 -1139 2530 -143 C ATOM 3330 O ILE C 69 88.719 19.815 274.757 1.00 74.44 O ANISOU 3330 O ILE C 69 8428 12758 7099 -845 2339 -85 O ATOM 3331 CB ILE C 69 91.382 18.189 275.518 1.00 65.60 C ANISOU 3331 CB ILE C 69 7861 11249 5814 -1764 1861 -435 C ATOM 3332 CG1 ILE C 69 92.547 19.176 275.397 1.00 54.52 C ANISOU 3332 CG1 ILE C 69 6896 9408 4411 -1601 1960 -420 C ATOM 3333 CG2 ILE C 69 90.903 17.723 274.147 1.00 49.78 C ANISOU 3333 CG2 ILE C 69 5458 9629 3825 -1477 1469 -444 C ATOM 3334 CD1 ILE C 69 93.812 18.555 274.842 1.00 44.60 C ANISOU 3334 CD1 ILE C 69 5726 8117 3102 -1761 1605 -576 C ATOM 3335 N SER C 70 90.048 21.182 275.944 1.00 54.57 N ANISOU 3335 N SER C 70 6702 9563 4470 -955 2824 -91 N ATOM 3336 CA SER C 70 89.574 22.387 275.286 1.00 57.41 C ANISOU 3336 CA SER C 70 7073 9967 4772 -515 3103 68 C ATOM 3337 C SER C 70 90.736 23.341 275.105 1.00 61.56 C ANISOU 3337 C SER C 70 8031 10075 5285 -499 3276 126 C ATOM 3338 O SER C 70 91.775 23.193 275.746 1.00 60.55 O ANISOU 3338 O SER C 70 8128 9619 5260 -779 3146 -15 O ATOM 3339 CB SER C 70 88.452 23.047 276.090 1.00 64.28 C ANISOU 3339 CB SER C 70 7842 10850 5730 -289 3431 78 C ATOM 3340 OG SER C 70 88.873 23.347 277.410 1.00 60.46 O ANISOU 3340 OG SER C 70 7658 10063 5252 -447 3610 -58 O ATOM 3341 N ARG C 71 90.567 24.322 274.231 1.00 62.96 N ANISOU 3341 N ARG C 71 8264 10174 5483 -75 3415 383 N ATOM 3342 CA ARG C 71 91.651 25.247 273.964 1.00 73.04 C ANISOU 3342 CA ARG C 71 9880 11001 6869 -78 3614 538 C ATOM 3343 C ARG C 71 91.154 26.666 273.764 1.00 86.97 C ANISOU 3343 C ARG C 71 11778 12455 8811 363 3909 786 C ATOM 3344 O ARG C 71 89.946 26.917 273.694 1.00 71.70 O ANISOU 3344 O ARG C 71 9672 10731 6841 736 3930 825 O ATOM 3345 CB ARG C 71 92.450 24.790 272.740 1.00 77.69 C ANISOU 3345 CB ARG C 71 10430 11808 7280 -57 3446 733 C ATOM 3346 CG ARG C 71 91.616 24.488 271.498 1.00 73.70 C ANISOU 3346 CG ARG C 71 9656 11834 6514 441 3242 932 C ATOM 3347 CD ARG C 71 91.432 25.715 270.621 1.00 91.65 C ANISOU 3347 CD ARG C 71 12075 13979 8767 979 3520 1388 C ATOM 3348 NE ARG C 71 90.820 25.405 269.331 1.00110.15 N ANISOU 3348 NE ARG C 71 14214 16877 10762 1548 3280 1561 N ATOM 3349 CZ ARG C 71 89.509 25.368 269.115 1.00110.67 C ANISOU 3349 CZ ARG C 71 14035 17236 10780 1963 3103 1484 C ATOM 3350 NH1 ARG C 71 88.665 25.617 270.107 1.00109.43 N ANISOU 3350 NH1 ARG C 71 13785 16901 10893 1847 3201 1287 N ATOM 3351 NH2 ARG C 71 89.041 25.078 267.908 1.00106.48 N ANISOU 3351 NH2 ARG C 71 13328 17210 9921 2544 2813 1574 N ATOM 3352 N ASP C 72 92.107 27.589 273.688 1.00110.70 N ANISOU 3352 N ASP C 72 15065 14918 12076 310 4119 945 N ATOM 3353 CA ASP C 72 91.823 28.984 273.390 1.00121.60 C ANISOU 3353 CA ASP C 72 16605 15873 13725 708 4376 1249 C ATOM 3354 C ASP C 72 92.875 29.539 272.430 1.00130.74 C ANISOU 3354 C ASP C 72 17905 16720 15051 712 4558 1716 C ATOM 3355 O ASP C 72 94.055 29.663 272.767 1.00128.57 O ANISOU 3355 O ASP C 72 17746 16023 15083 310 4633 1643 O ATOM 3356 CB ASP C 72 91.766 29.821 274.673 1.00119.69 C ANISOU 3356 CB ASP C 72 16550 15083 13845 655 4492 917 C ATOM 3357 CG ASP C 72 91.251 31.231 274.429 1.00116.62 C ANISOU 3357 CG ASP C 72 16295 14245 13772 1127 4678 1168 C ATOM 3358 OD1 ASP C 72 91.338 32.072 275.351 1.00117.23 O ANISOU 3358 OD1 ASP C 72 16542 13774 14225 1151 4730 888 O ATOM 3359 OD2 ASP C 72 90.760 31.499 273.312 1.00120.86 O ANISOU 3359 OD2 ASP C 72 16776 14970 14174 1525 4731 1621 O ATOM 3360 N ASN C 73 92.427 29.854 271.222 1.00122.93 N ANISOU 3360 N ASN C 73 14930 18016 13762 324 2625 1741 N ATOM 3361 CA ASN C 73 93.278 30.468 270.224 1.00113.02 C ANISOU 3361 CA ASN C 73 13616 16675 12652 464 2575 1711 C ATOM 3362 C ASN C 73 93.608 31.892 270.640 1.00117.78 C ANISOU 3362 C ASN C 73 14349 16886 13515 822 2927 1672 C ATOM 3363 O ASN C 73 92.995 32.435 271.563 1.00127.08 O ANISOU 3363 O ASN C 73 15607 17911 14765 982 3217 1716 O ATOM 3364 CB ASN C 73 92.605 30.468 268.848 1.00107.83 C ANISOU 3364 CB ASN C 73 12479 16448 12042 488 2382 2061 C ATOM 3365 CG ASN C 73 92.220 29.078 268.368 1.00 91.22 C ANISOU 3365 CG ASN C 73 10244 14749 9668 77 2028 2072 C ATOM 3366 OD1 ASN C 73 92.857 28.086 268.709 1.00 82.94 O ANISOU 3366 OD1 ASN C 73 9501 13582 8431 -214 1881 1782 O ATOM 3367 ND2 ASN C 73 91.158 29.008 267.567 1.00 85.64 N ANISOU 3367 ND2 ASN C 73 9076 14539 8923 41 1879 2426 N ATOM 3368 N ALA C 74 94.600 32.468 269.961 1.00119.19 N ANISOU 3368 N ALA C 74 14579 16875 13832 932 2914 1577 N ATOM 3369 CA ALA C 74 95.124 33.816 270.219 1.00130.95 C ANISOU 3369 CA ALA C 74 16256 17910 15591 1221 3234 1502 C ATOM 3370 C ALA C 74 95.886 33.891 271.543 1.00130.73 C ANISOU 3370 C ALA C 74 16727 17482 15463 1117 3384 1080 C ATOM 3371 O ALA C 74 96.811 34.692 271.676 1.00150.85 O ANISOU 3371 O ALA C 74 19538 19627 18150 1183 3533 862 O ATOM 3372 CB ALA C 74 94.009 34.866 270.188 1.00138.54 C ANISOU 3372 CB ALA C 74 17007 18826 16807 1576 3547 1887 C ATOM 3373 N LYS C 75 95.506 33.065 272.514 1.00 95.38 N ANISOU 3373 N LYS C 75 12394 13119 10729 920 3329 969 N ATOM 3374 CA LYS C 75 96.222 32.993 273.783 1.00 85.38 C ANISOU 3374 CA LYS C 75 11609 11549 9285 767 3385 577 C ATOM 3375 C LYS C 75 97.103 31.747 273.863 1.00 79.56 C ANISOU 3375 C LYS C 75 11059 10918 8251 467 3005 364 C ATOM 3376 O LYS C 75 97.886 31.600 274.803 1.00 77.81 O ANISOU 3376 O LYS C 75 11232 10475 7856 293 2937 44 O ATOM 3377 CB LYS C 75 95.242 33.014 274.956 1.00 82.23 C ANISOU 3377 CB LYS C 75 11300 11157 8786 775 3604 606 C ATOM 3378 CG LYS C 75 94.528 34.339 275.138 1.00 89.02 C ANISOU 3378 CG LYS C 75 12132 11756 9936 1094 4057 757 C ATOM 3379 CD LYS C 75 94.260 34.622 276.608 1.00 99.22 C ANISOU 3379 CD LYS C 75 13792 12810 11097 1046 4339 538 C ATOM 3380 CE LYS C 75 93.669 36.009 276.791 1.00 97.03 C ANISOU 3380 CE LYS C 75 13586 12150 11130 1367 4861 664 C ATOM 3381 NZ LYS C 75 93.571 36.404 278.224 1.00 90.67 N ANISOU 3381 NZ LYS C 75 13228 11038 10185 1274 5183 374 N ATOM 3382 N ASN C 76 96.971 30.863 272.874 1.00 67.59 N ANISOU 3382 N ASN C 76 9279 9730 6671 378 2744 549 N ATOM 3383 CA ASN C 76 97.723 29.608 272.830 1.00 42.79 C ANISOU 3383 CA ASN C 76 6339 6636 3284 117 2396 392 C ATOM 3384 C ASN C 76 97.599 28.809 274.123 1.00 63.61 C ANISOU 3384 C ASN C 76 9265 9233 5669 -103 2289 260 C ATOM 3385 O ASN C 76 98.592 28.323 274.664 1.00 57.34 O ANISOU 3385 O ASN C 76 8750 8252 4783 -272 2016 14 O ATOM 3386 CB ASN C 76 99.199 29.877 272.525 1.00 40.82 C ANISOU 3386 CB ASN C 76 6266 6089 3157 99 2196 111 C ATOM 3387 CG ASN C 76 99.414 30.424 271.130 1.00 39.99 C ANISOU 3387 CG ASN C 76 5864 6058 3273 275 2228 256 C ATOM 3388 OD1 ASN C 76 98.585 30.229 270.242 1.00 51.54 O ANISOU 3388 OD1 ASN C 76 6974 7877 4733 322 2247 555 O ATOM 3389 ND2 ASN C 76 100.532 31.111 270.927 1.00 39.21 N ANISOU 3389 ND2 ASN C 76 5885 5675 3339 338 2225 67 N ATOM 3390 N ALA C 77 96.371 28.678 274.614 1.00 69.94 N ANISOU 3390 N ALA C 77 9910 10254 6410 -94 2443 470 N ATOM 3391 CA ALA C 77 96.123 27.987 275.871 1.00 58.07 C ANISOU 3391 CA ALA C 77 8632 8748 4682 -264 2376 403 C ATOM 3392 C ALA C 77 95.310 26.715 275.664 1.00 53.68 C ANISOU 3392 C ALA C 77 7908 8494 3994 -463 2202 637 C ATOM 3393 O ALA C 77 94.445 26.655 274.792 1.00 64.31 O ANISOU 3393 O ALA C 77 8946 10051 5437 -452 2266 884 O ATOM 3394 CB ALA C 77 95.417 28.912 276.851 1.00 63.51 C ANISOU 3394 CB ALA C 77 9343 9376 5412 -109 2724 404 C ATOM 3395 N VAL C 78 95.597 25.699 276.472 1.00 54.94 N ANISOU 3395 N VAL C 78 8319 8562 3995 -684 1972 536 N ATOM 3396 CA VAL C 78 94.866 24.439 276.419 1.00 54.27 C ANISOU 3396 CA VAL C 78 8133 8645 3842 -916 1810 710 C ATOM 3397 C VAL C 78 94.543 23.947 277.826 1.00 66.12 C ANISOU 3397 C VAL C 78 9824 10113 5185 -987 1833 734 C ATOM 3398 O VAL C 78 95.422 23.862 278.684 1.00 59.65 O ANISOU 3398 O VAL C 78 9299 9103 4260 -1022 1723 558 O ATOM 3399 CB VAL C 78 95.657 23.357 275.655 1.00 45.58 C ANISOU 3399 CB VAL C 78 7127 7443 2745 -1169 1478 601 C ATOM 3400 CG1 VAL C 78 95.174 21.963 276.026 1.00 50.96 C ANISOU 3400 CG1 VAL C 78 7882 8142 3340 -1462 1345 695 C ATOM 3401 CG2 VAL C 78 95.537 23.583 274.161 1.00 73.10 C ANISOU 3401 CG2 VAL C 78 10325 11103 6346 -1173 1449 648 C ATOM 3402 N TYR C 79 93.273 23.631 278.054 1.00 74.80 N ANISOU 3402 N TYR C 79 10732 11421 6269 -1013 1971 977 N ATOM 3403 CA TYR C 79 92.813 23.189 279.363 1.00 59.95 C ANISOU 3403 CA TYR C 79 8990 9553 4235 -1062 2038 1045 C ATOM 3404 C TYR C 79 92.291 21.759 279.299 1.00 55.82 C ANISOU 3404 C TYR C 79 8420 9103 3687 -1379 1850 1188 C ATOM 3405 O TYR C 79 91.678 21.357 278.311 1.00 55.68 O ANISOU 3405 O TYR C 79 8147 9246 3765 -1540 1786 1299 O ATOM 3406 CB TYR C 79 91.732 24.134 279.889 1.00 56.51 C ANISOU 3406 CB TYR C 79 8410 9257 3805 -787 2458 1221 C ATOM 3407 CG TYR C 79 92.102 25.594 279.761 1.00 71.67 C ANISOU 3407 CG TYR C 79 10235 11213 5782 -541 2659 1099 C ATOM 3408 CD1 TYR C 79 92.869 26.224 280.733 1.00 94.13 C ANISOU 3408 CD1 TYR C 79 13416 13818 8530 -538 2711 774 C ATOM 3409 CD2 TYR C 79 91.692 26.342 278.664 1.00 76.70 C ANISOU 3409 CD2 TYR C 79 10628 11889 6627 -644 2771 1084 C ATOM 3410 CE1 TYR C 79 93.214 27.557 280.618 1.00103.87 C ANISOU 3410 CE1 TYR C 79 14714 14850 9901 -371 2946 571 C ATOM 3411 CE2 TYR C 79 92.032 27.677 278.541 1.00 82.07 C ANISOU 3411 CE2 TYR C 79 11289 12422 7472 -333 3006 982 C ATOM 3412 CZ TYR C 79 92.793 28.279 279.521 1.00 93.51 C ANISOU 3412 CZ TYR C 79 13096 13583 8853 -210 3110 703 C ATOM 3413 OH TYR C 79 93.135 29.607 279.404 1.00 85.96 O ANISOU 3413 OH TYR C 79 12234 12325 8102 19 3381 542 O ATOM 3414 N LEU C 80 92.540 20.990 280.354 1.00 61.94 N ANISOU 3414 N LEU C 80 9435 9776 4324 -1502 1761 1187 N ATOM 3415 CA LEU C 80 92.120 19.595 280.392 1.00 57.11 C ANISOU 3415 CA LEU C 80 8836 9168 3696 -1819 1631 1328 C ATOM 3416 C LEU C 80 91.318 19.278 281.649 1.00 70.95 C ANISOU 3416 C LEU C 80 10617 11020 5321 -1821 1778 1508 C ATOM 3417 O LEU C 80 91.872 19.191 282.745 1.00 82.61 O ANISOU 3417 O LEU C 80 12335 12405 6650 -1763 1756 1479 O ATOM 3418 CB LEU C 80 93.336 18.671 280.304 1.00 55.92 C ANISOU 3418 CB LEU C 80 8985 8726 3536 -1988 1386 1227 C ATOM 3419 CG LEU C 80 93.049 17.169 280.358 1.00 64.31 C ANISOU 3419 CG LEU C 80 10161 9676 4598 -2330 1319 1374 C ATOM 3420 CD1 LEU C 80 92.196 16.742 279.174 1.00 81.98 C ANISOU 3420 CD1 LEU C 80 12173 12049 6925 -2626 1321 1387 C ATOM 3421 CD2 LEU C 80 94.345 16.374 280.406 1.00 70.86 C ANISOU 3421 CD2 LEU C 80 11341 10148 5436 -2388 1171 1350 C ATOM 3422 N GLN C 81 90.010 19.108 281.483 1.00 63.49 N ANISOU 3422 N GLN C 81 9404 10298 4422 -1902 1918 1709 N ATOM 3423 CA GLN C 81 89.145 18.714 282.588 1.00 72.66 C ANISOU 3423 CA GLN C 81 10570 11559 5477 -1927 2076 1906 C ATOM 3424 C GLN C 81 89.215 17.206 282.794 1.00 85.17 C ANISOU 3424 C GLN C 81 12288 13036 7037 -2291 1895 1998 C ATOM 3425 O GLN C 81 88.896 16.435 281.890 1.00 90.00 O ANISOU 3425 O GLN C 81 12786 13665 7746 -2615 1779 2025 O ATOM 3426 CB GLN C 81 87.701 19.149 282.329 1.00 74.39 C ANISOU 3426 CB GLN C 81 10437 12052 5777 -1875 2315 2110 C ATOM 3427 CG GLN C 81 86.721 18.704 283.403 1.00 76.50 C ANISOU 3427 CG GLN C 81 10692 12428 5947 -1923 2501 2325 C ATOM 3428 CD GLN C 81 87.004 19.338 284.751 1.00 78.18 C ANISOU 3428 CD GLN C 81 11193 12538 5976 -1630 2740 2275 C ATOM 3429 OE1 GLN C 81 87.502 20.461 284.829 1.00 88.29 O ANISOU 3429 OE1 GLN C 81 12584 13734 7227 -1340 2893 2118 O ATOM 3430 NE2 GLN C 81 86.691 18.618 285.821 1.00 79.81 N ANISOU 3430 NE2 GLN C 81 11519 12768 6035 -1725 2782 2411 N ATOM 3431 N MET C 82 89.634 16.788 283.984 1.00 84.57 N ANISOU 3431 N MET C 82 12468 12848 6818 -2256 1893 2053 N ATOM 3432 CA MET C 82 89.814 15.369 284.268 1.00 77.55 C ANISOU 3432 CA MET C 82 11754 11782 5928 -2548 1778 2193 C ATOM 3433 C MET C 82 88.798 14.847 285.277 1.00 76.09 C ANISOU 3433 C MET C 82 11519 11738 5654 -2618 1942 2448 C ATOM 3434 O MET C 82 89.066 14.810 286.476 1.00 77.56 O ANISOU 3434 O MET C 82 11873 11924 5671 -2477 1992 2538 O ATOM 3435 CB MET C 82 91.233 15.105 284.777 1.00 84.11 C ANISOU 3435 CB MET C 82 12906 12367 6685 -2459 1618 2148 C ATOM 3436 CG MET C 82 92.323 15.439 283.771 1.00 84.97 C ANISOU 3436 CG MET C 82 13096 12292 6896 -2416 1454 1926 C ATOM 3437 SD MET C 82 93.963 14.931 284.325 1.00 86.25 S ANISOU 3437 SD MET C 82 13588 12186 6997 -2327 1261 1988 S ATOM 3438 CE MET C 82 94.140 15.907 285.814 1.00 81.73 C ANISOU 3438 CE MET C 82 13018 11901 6134 -2074 1286 1967 C ATOM 3439 N ASN C 83 87.635 14.433 284.782 1.00 91.96 N ANISOU 3439 N ASN C 83 13280 13902 7758 -2861 2012 2569 N ATOM 3440 CA ASN C 83 86.581 13.901 285.638 1.00 79.62 C ANISOU 3440 CA ASN C 83 11636 12482 6135 -2961 2177 2824 C ATOM 3441 C ASN C 83 86.703 12.394 285.834 1.00 89.47 C ANISOU 3441 C ASN C 83 13075 13493 7429 -3318 2103 2976 C ATOM 3442 O ASN C 83 87.251 11.694 284.981 1.00100.37 O ANISOU 3442 O ASN C 83 14588 14616 8934 -3582 1963 2878 O ATOM 3443 CB ASN C 83 85.206 14.239 285.060 1.00 81.42 C ANISOU 3443 CB ASN C 83 11457 13040 6441 -3055 2295 2921 C ATOM 3444 CG ASN C 83 84.964 15.732 284.967 1.00 80.13 C ANISOU 3444 CG ASN C 83 11125 13048 6272 -2654 2474 2851 C ATOM 3445 OD1 ASN C 83 85.505 16.510 285.752 1.00 85.64 O ANISOU 3445 OD1 ASN C 83 12038 13649 6851 -2314 2611 2760 O ATOM 3446 ND2 ASN C 83 84.146 16.140 284.004 1.00 98.53 N ANISOU 3446 ND2 ASN C 83 13077 15638 8723 -2713 2488 2905 N ATOM 3447 N SER C 84 86.182 11.909 286.960 1.00 89.83 N ANISOU 3447 N SER C 84 13163 13588 7379 -3316 2246 3220 N ATOM 3448 CA SER C 84 86.204 10.487 287.301 1.00 93.14 C ANISOU 3448 CA SER C 84 13768 13757 7864 -3613 2250 3432 C ATOM 3449 C SER C 84 87.616 9.914 287.250 1.00 94.95 C ANISOU 3449 C SER C 84 14344 13581 8153 -3580 2117 3410 C ATOM 3450 O SER C 84 87.901 9.005 286.470 1.00 95.89 O ANISOU 3450 O SER C 84 14611 13361 8463 -3880 2077 3380 O ATOM 3451 CB SER C 84 85.282 9.696 286.369 1.00100.81 C ANISOU 3451 CB SER C 84 14572 14735 8995 -4106 2247 3445 C ATOM 3452 OG SER C 84 83.944 10.152 286.466 1.00 99.71 O ANISOU 3452 OG SER C 84 14064 15015 8807 -4133 2362 3548 O ATOM 3453 N LEU C 85 88.496 10.451 288.088 1.00102.81 N ANISOU 3453 N LEU C 85 15476 14607 8980 -3223 2070 3427 N ATOM 3454 CA LEU C 85 89.897 10.048 288.090 1.00103.53 C ANISOU 3454 CA LEU C 85 15835 14389 9114 -3122 1930 3465 C ATOM 3455 C LEU C 85 90.113 8.693 288.756 1.00 93.85 C ANISOU 3455 C LEU C 85 14806 12878 7973 -3211 2015 3849 C ATOM 3456 O LEU C 85 89.463 8.361 289.748 1.00 92.80 O ANISOU 3456 O LEU C 85 14637 12895 7728 -3206 2149 4098 O ATOM 3457 CB LEU C 85 90.750 11.114 288.781 1.00 97.83 C ANISOU 3457 CB LEU C 85 15146 13878 8148 -2758 1821 3361 C ATOM 3458 CG LEU C 85 91.077 12.338 287.923 1.00 87.36 C ANISOU 3458 CG LEU C 85 13722 12641 6829 -2636 1725 2986 C ATOM 3459 CD1 LEU C 85 91.487 13.514 288.787 1.00 85.17 C ANISOU 3459 CD1 LEU C 85 13453 12625 6282 -2346 1709 2848 C ATOM 3460 CD2 LEU C 85 92.177 12.001 286.932 1.00 76.68 C ANISOU 3460 CD2 LEU C 85 12516 10959 5659 -2686 1561 2894 C ATOM 3461 N LYS C 86 91.033 7.917 288.193 1.00100.19 N ANISOU 3461 N LYS C 86 15827 13237 9002 -3263 1978 3917 N ATOM 3462 CA LYS C 86 91.375 6.603 288.720 1.00 94.05 C ANISOU 3462 CA LYS C 86 15247 12090 8399 -3281 2113 4333 C ATOM 3463 C LYS C 86 92.813 6.599 289.233 1.00100.25 C ANISOU 3463 C LYS C 86 16155 12794 9142 -2912 1999 4575 C ATOM 3464 O LYS C 86 93.636 7.392 288.775 1.00 90.53 O ANISOU 3464 O LYS C 86 14917 11633 7846 -2753 1812 4348 O ATOM 3465 CB LYS C 86 91.188 5.530 287.644 1.00 95.84 C ANISOU 3465 CB LYS C 86 15643 11771 9002 -3646 2260 4262 C ATOM 3466 CG LYS C 86 89.766 5.418 287.120 1.00101.48 C ANISOU 3466 CG LYS C 86 16202 12624 9731 -4084 2343 4057 C ATOM 3467 CD LYS C 86 89.656 4.346 286.050 1.00105.05 C ANISOU 3467 CD LYS C 86 16872 12535 10509 -4506 2485 3902 C ATOM 3468 CE LYS C 86 88.236 4.237 285.520 1.00101.13 C ANISOU 3468 CE LYS C 86 16175 12281 9969 -5001 2517 3709 C ATOM 3469 NZ LYS C 86 88.120 3.198 284.461 1.00113.32 N ANISOU 3469 NZ LYS C 86 17962 13326 11768 -5483 2651 3472 N ATOM 3470 N PRO C 87 93.119 5.711 290.194 1.00109.92 N ANISOU 3470 N PRO C 87 17463 13902 10400 -2766 2116 5074 N ATOM 3471 CA PRO C 87 94.478 5.588 290.738 1.00114.53 C ANISOU 3471 CA PRO C 87 18118 14458 10940 -2395 2020 5414 C ATOM 3472 C PRO C 87 95.529 5.268 289.674 1.00111.95 C ANISOU 3472 C PRO C 87 17902 13662 10971 -2321 1993 5406 C ATOM 3473 O PRO C 87 96.710 5.551 289.877 1.00115.69 O ANISOU 3473 O PRO C 87 18365 14219 11371 -2003 1841 5572 O ATOM 3474 CB PRO C 87 94.350 4.433 291.735 1.00106.26 C ANISOU 3474 CB PRO C 87 17171 13241 9962 -2305 2263 5980 C ATOM 3475 CG PRO C 87 92.923 4.456 292.149 1.00107.24 C ANISOU 3475 CG PRO C 87 17211 13589 9947 -2569 2383 5875 C ATOM 3476 CD PRO C 87 92.160 4.861 290.922 1.00114.18 C ANISOU 3476 CD PRO C 87 18002 14409 10972 -2913 2350 5379 C ATOM 3477 N GLU C 88 95.101 4.688 288.557 1.00106.97 N ANISOU 3477 N GLU C 88 17404 12539 10700 -2625 2149 5176 N ATOM 3478 CA GLU C 88 96.018 4.332 287.480 1.00102.32 C ANISOU 3478 CA GLU C 88 16999 11408 10471 -2569 2192 5071 C ATOM 3479 C GLU C 88 96.422 5.554 286.659 1.00100.87 C ANISOU 3479 C GLU C 88 16777 11436 10114 -2530 1963 4586 C ATOM 3480 O GLU C 88 97.355 5.493 285.859 1.00100.29 O ANISOU 3480 O GLU C 88 16832 11005 10267 -2387 1971 4500 O ATOM 3481 CB GLU C 88 95.386 3.276 286.571 1.00114.10 C ANISOU 3481 CB GLU C 88 18718 12273 12361 -2939 2488 4868 C ATOM 3482 CG GLU C 88 94.160 3.759 285.818 1.00124.56 C ANISOU 3482 CG GLU C 88 19996 13800 13533 -3396 2467 4325 C ATOM 3483 CD GLU C 88 93.512 2.662 284.996 1.00137.60 C ANISOU 3483 CD GLU C 88 21862 14912 15506 -3834 2743 4114 C ATOM 3484 OE1 GLU C 88 93.593 1.485 285.406 1.00138.55 O ANISOU 3484 OE1 GLU C 88 22135 14583 15923 -3827 2985 4451 O ATOM 3485 OE2 GLU C 88 92.928 2.977 283.938 1.00144.08 O ANISOU 3485 OE2 GLU C 88 22687 15790 16268 -4201 2713 3616 O ATOM 3486 N ASP C 89 95.717 6.662 286.863 1.00 93.11 N ANISOU 3486 N ASP C 89 15601 11015 8761 -2628 1792 4284 N ATOM 3487 CA ASP C 89 96.008 7.900 286.147 1.00 83.52 C ANISOU 3487 CA ASP C 89 14303 10040 7390 -2590 1588 3848 C ATOM 3488 C ASP C 89 97.103 8.705 286.841 1.00 97.63 C ANISOU 3488 C ASP C 89 15984 12179 8930 -2237 1339 3973 C ATOM 3489 O ASP C 89 97.423 9.820 286.428 1.00101.11 O ANISOU 3489 O ASP C 89 16338 12855 9225 -2178 1165 3634 O ATOM 3490 CB ASP C 89 94.743 8.751 286.010 1.00 81.15 C ANISOU 3490 CB ASP C 89 13797 10158 6878 -2808 1566 3493 C ATOM 3491 CG ASP C 89 93.679 8.083 285.162 1.00 95.32 C ANISOU 3491 CG ASP C 89 15626 11724 8869 -3221 1745 3331 C ATOM 3492 OD1 ASP C 89 94.040 7.408 284.174 1.00 96.71 O ANISOU 3492 OD1 ASP C 89 16016 11413 9317 -3378 1847 3213 O ATOM 3493 OD2 ASP C 89 92.481 8.231 285.483 1.00103.99 O ANISOU 3493 OD2 ASP C 89 16530 13137 9844 -3395 1798 3310 O ATOM 3494 N THR C 90 97.676 8.133 287.896 1.00103.12 N ANISOU 3494 N THR C 90 16668 12936 9577 -2019 1331 4469 N ATOM 3495 CA THR C 90 98.728 8.799 288.654 1.00 97.70 C ANISOU 3495 CA THR C 90 15857 12658 8609 -1737 1076 4611 C ATOM 3496 C THR C 90 100.032 8.857 287.866 1.00104.53 C ANISOU 3496 C THR C 90 16749 13288 9679 -1544 957 4664 C ATOM 3497 O THR C 90 100.722 7.847 287.715 1.00116.12 O ANISOU 3497 O THR C 90 18304 14341 11474 -1357 1090 5099 O ATOM 3498 CB THR C 90 98.984 8.093 289.998 1.00 91.94 C ANISOU 3498 CB THR C 90 15122 12076 7735 -1557 1110 5146 C ATOM 3499 OG1 THR C 90 97.768 8.045 290.754 1.00 93.39 O ANISOU 3499 OG1 THR C 90 15294 12468 7721 -1727 1238 5104 O ATOM 3500 CG2 THR C 90 100.044 8.836 290.798 1.00 92.81 C ANISOU 3500 CG2 THR C 90 15100 12675 7489 -1371 791 5196 C ATOM 3501 N ALA C 91 100.364 10.044 287.367 1.00 80.94 N ANISOU 3501 N ALA C 91 13679 10538 6536 -1559 748 4241 N ATOM 3502 CA ALA C 91 101.584 10.239 286.590 1.00 79.47 C ANISOU 3502 CA ALA C 91 13497 10178 6520 -1382 617 4258 C ATOM 3503 C ALA C 91 101.967 11.713 286.524 1.00 90.69 C ANISOU 3503 C ALA C 91 14757 12052 7648 -1394 347 3842 C ATOM 3504 O ALA C 91 101.308 12.564 287.121 1.00 99.55 O ANISOU 3504 O ALA C 91 15795 13565 8465 -1514 306 3538 O ATOM 3505 CB ALA C 91 101.414 9.675 285.186 1.00 77.86 C ANISOU 3505 CB ALA C 91 13479 9322 6784 -1423 859 4016 C ATOM 3506 N VAL C 92 103.041 12.006 285.797 1.00 78.50 N ANISOU 3506 N VAL C 92 13135 10401 6291 -1218 217 3788 N ATOM 3507 CA VAL C 92 103.471 13.381 285.579 1.00 74.78 C ANISOU 3507 CA VAL C 92 12529 10269 5616 -1248 -2 3376 C ATOM 3508 C VAL C 92 102.975 13.876 284.226 1.00 66.61 C ANISOU 3508 C VAL C 92 11531 8929 4847 -1291 131 2833 C ATOM 3509 O VAL C 92 103.386 13.370 283.183 1.00 72.67 O ANISOU 3509 O VAL C 92 12314 9274 6024 -1149 228 2795 O ATOM 3510 CB VAL C 92 105.003 13.518 285.641 1.00 77.13 C ANISOU 3510 CB VAL C 92 12609 10736 5961 -1024 -251 3642 C ATOM 3511 CG1 VAL C 92 105.417 14.955 285.365 1.00 69.67 C ANISOU 3511 CG1 VAL C 92 11555 10092 4825 -1119 -448 3176 C ATOM 3512 CG2 VAL C 92 105.522 13.057 286.993 1.00 78.00 C ANISOU 3512 CG2 VAL C 92 12576 11243 5816 -956 -400 4181 C ATOM 3513 N TYR C 93 102.090 14.867 284.248 1.00 67.85 N ANISOU 3513 N TYR C 93 11701 9320 4761 -1477 167 2441 N ATOM 3514 CA TYR C 93 101.466 15.360 283.026 1.00 72.24 C ANISOU 3514 CA TYR C 93 12237 9689 5522 -1527 299 2013 C ATOM 3515 C TYR C 93 102.286 16.460 282.357 1.00 57.63 C ANISOU 3515 C TYR C 93 10257 7903 3735 -1405 166 1710 C ATOM 3516 O TYR C 93 102.533 17.512 282.946 1.00 67.26 O ANISOU 3516 O TYR C 93 11439 9445 4672 -1441 64 1569 O ATOM 3517 CB TYR C 93 100.053 15.863 283.322 1.00 70.28 C ANISOU 3517 CB TYR C 93 12008 9659 5038 -1729 465 1840 C ATOM 3518 CG TYR C 93 99.058 14.753 283.580 1.00 62.18 C ANISOU 3518 CG TYR C 93 11065 8506 4054 -1894 638 2071 C ATOM 3519 CD1 TYR C 93 99.032 14.086 284.798 1.00 77.00 C ANISOU 3519 CD1 TYR C 93 12965 10486 5807 -1878 627 2412 C ATOM 3520 CD2 TYR C 93 98.147 14.372 282.605 1.00 61.26 C ANISOU 3520 CD2 TYR C 93 10945 8201 4129 -2073 805 1936 C ATOM 3521 CE1 TYR C 93 98.126 13.070 285.036 1.00 80.38 C ANISOU 3521 CE1 TYR C 93 13451 10773 6316 -2027 803 2622 C ATOM 3522 CE2 TYR C 93 97.236 13.358 282.835 1.00 68.41 C ANISOU 3522 CE2 TYR C 93 11917 8997 5078 -2290 962 2127 C ATOM 3523 CZ TYR C 93 97.230 12.711 284.052 1.00 71.45 C ANISOU 3523 CZ TYR C 93 12347 9427 5375 -2248 970 2464 C ATOM 3524 OH TYR C 93 96.326 11.701 284.286 1.00 78.53 O ANISOU 3524 OH TYR C 93 13291 10192 6356 -2456 1141 2651 O ATOM 3525 N TYR C 94 102.703 16.205 281.120 1.00 75.77 N ANISOU 3525 N TYR C 94 12516 9877 6394 -1291 200 1595 N ATOM 3526 CA TYR C 94 103.480 17.171 280.353 1.00 62.00 C ANISOU 3526 CA TYR C 94 10637 8161 4758 -1167 99 1336 C ATOM 3527 C TYR C 94 102.627 17.836 279.278 1.00 50.18 C ANISOU 3527 C TYR C 94 9089 6631 3348 -1239 244 975 C ATOM 3528 O TYR C 94 101.742 17.208 278.697 1.00 60.77 O ANISOU 3528 O TYR C 94 10477 7828 4786 -1367 398 945 O ATOM 3529 CB TYR C 94 104.695 16.500 279.708 1.00 53.95 C ANISOU 3529 CB TYR C 94 9571 6855 4071 -943 48 1504 C ATOM 3530 CG TYR C 94 105.646 15.851 280.689 1.00 57.66 C ANISOU 3530 CG TYR C 94 9999 7411 4497 -807 -91 1978 C ATOM 3531 CD1 TYR C 94 106.634 16.594 281.323 1.00 58.59 C ANISOU 3531 CD1 TYR C 94 9938 7910 4412 -772 -354 2079 C ATOM 3532 CD2 TYR C 94 105.563 14.494 280.973 1.00 65.60 C ANISOU 3532 CD2 TYR C 94 11127 8139 5660 -737 53 2361 C ATOM 3533 CE1 TYR C 94 107.508 16.003 282.219 1.00 62.68 C ANISOU 3533 CE1 TYR C 94 10340 8627 4849 -665 -513 2596 C ATOM 3534 CE2 TYR C 94 106.432 13.896 281.866 1.00 79.95 C ANISOU 3534 CE2 TYR C 94 12850 10074 7452 -564 -55 2901 C ATOM 3535 CZ TYR C 94 107.403 14.655 282.485 1.00 65.81 C ANISOU 3535 CZ TYR C 94 10820 8760 5423 -525 -361 3041 C ATOM 3536 OH TYR C 94 108.270 14.062 283.375 1.00 70.47 O ANISOU 3536 OH TYR C 94 11243 9586 5947 -371 -500 3657 O ATOM 3537 N CYS C 95 102.902 19.109 279.016 1.00 57.88 N ANISOU 3537 N CYS C 95 9953 7762 4276 -1183 201 732 N ATOM 3538 CA CYS C 95 102.193 19.850 277.980 1.00 45.69 C ANISOU 3538 CA CYS C 95 8301 6232 2825 -1193 344 475 C ATOM 3539 C CYS C 95 103.045 19.957 276.722 1.00 49.90 C ANISOU 3539 C CYS C 95 8736 6584 3638 -1054 294 357 C ATOM 3540 O CYS C 95 104.243 20.224 276.795 1.00 43.86 O ANISOU 3540 O CYS C 95 7932 5789 2945 -922 151 376 O ATOM 3541 CB CYS C 95 101.811 21.242 278.481 1.00 60.77 C ANISOU 3541 CB CYS C 95 10177 8376 4537 -1194 436 306 C ATOM 3542 SG CYS C 95 100.950 22.267 277.272 1.00 80.59 S ANISOU 3542 SG CYS C 95 12490 10943 7189 -1123 659 123 S ATOM 3543 N ASN C 96 102.420 19.750 275.568 1.00 48.09 N ANISOU 3543 N ASN C 96 8447 6289 3535 -1113 411 250 N ATOM 3544 CA ASN C 96 103.137 19.772 274.300 1.00 41.45 C ANISOU 3544 CA ASN C 96 7535 5293 2922 -1007 401 129 C ATOM 3545 C ASN C 96 102.452 20.657 273.264 1.00 47.88 C ANISOU 3545 C ASN C 96 8157 6298 3736 -1033 497 -32 C ATOM 3546 O ASN C 96 101.227 20.755 273.233 1.00 63.74 O ANISOU 3546 O ASN C 96 10088 8518 5614 -1185 601 -6 O ATOM 3547 CB ASN C 96 103.288 18.348 273.759 1.00 50.09 C ANISOU 3547 CB ASN C 96 8793 6073 4166 -1083 472 180 C ATOM 3548 CG ASN C 96 103.900 18.310 272.374 1.00 49.15 C ANISOU 3548 CG ASN C 96 8640 5797 4239 -1008 527 16 C ATOM 3549 OD1 ASN C 96 105.102 18.519 272.206 1.00 51.98 O ANISOU 3549 OD1 ASN C 96 8950 6038 4760 -769 465 44 O ATOM 3550 ND2 ASN C 96 103.075 18.034 271.370 1.00 42.47 N ANISOU 3550 ND2 ASN C 96 7799 4995 3342 -1243 643 -141 N ATOM 3551 N ALA C 97 103.253 21.306 272.424 1.00 49.59 N ANISOU 3551 N ALA C 97 8260 6480 4102 -873 469 -139 N ATOM 3552 CA ALA C 97 102.730 22.157 271.363 1.00 41.91 C ANISOU 3552 CA ALA C 97 7073 5705 3145 -858 564 -222 C ATOM 3553 C ALA C 97 103.405 21.837 270.034 1.00 39.68 C ANISOU 3553 C ALA C 97 6757 5311 3010 -823 557 -321 C ATOM 3554 O ALA C 97 104.612 21.600 269.981 1.00 49.73 O ANISOU 3554 O ALA C 97 8104 6352 4440 -674 492 -339 O ATOM 3555 CB ALA C 97 102.917 23.624 271.716 1.00 43.83 C ANISOU 3555 CB ALA C 97 7201 6048 3405 -684 611 -250 C ATOM 3556 N GLU C 98 102.619 21.831 268.962 1.00 45.10 N ANISOU 3556 N GLU C 98 7309 6210 3618 -973 635 -358 N ATOM 3557 CA GLU C 98 103.135 21.529 267.631 1.00 44.38 C ANISOU 3557 CA GLU C 98 7206 6068 3588 -998 662 -481 C ATOM 3558 C GLU C 98 103.145 22.777 266.753 1.00 39.88 C ANISOU 3558 C GLU C 98 6341 5769 3042 -850 692 -454 C ATOM 3559 O GLU C 98 102.317 23.671 266.923 1.00 35.15 O ANISOU 3559 O GLU C 98 5524 5454 2377 -810 745 -317 O ATOM 3560 CB GLU C 98 102.306 20.420 266.981 1.00 49.05 C ANISOU 3560 CB GLU C 98 7907 6726 4005 -1383 727 -565 C ATOM 3561 CG GLU C 98 102.344 19.103 267.740 1.00 55.41 C ANISOU 3561 CG GLU C 98 9045 7172 4836 -1532 764 -581 C ATOM 3562 CD GLU C 98 101.424 18.058 267.143 1.00 79.21 C ANISOU 3562 CD GLU C 98 12199 10235 7661 -2006 862 -699 C ATOM 3563 OE1 GLU C 98 100.505 18.436 266.386 1.00 80.19 O ANISOU 3563 OE1 GLU C 98 12086 10820 7560 -2261 840 -706 O ATOM 3564 OE2 GLU C 98 101.620 16.857 267.429 1.00 96.62 O ANISOU 3564 OE2 GLU C 98 14744 12031 9937 -2144 975 -760 O ATOM 3565 N GLU C 99 104.083 22.830 265.812 1.00 34.96 N ANISOU 3565 N GLU C 99 5706 5045 2534 -739 702 -549 N ATOM 3566 CA GLU C 99 104.272 24.022 264.992 1.00 36.25 C ANISOU 3566 CA GLU C 99 5595 5422 2756 -563 743 -489 C ATOM 3567 C GLU C 99 104.089 23.727 263.503 1.00 41.29 C ANISOU 3567 C GLU C 99 6139 6298 3250 -726 793 -550 C ATOM 3568 O GLU C 99 104.434 22.645 263.030 1.00 46.32 O ANISOU 3568 O GLU C 99 7007 6758 3834 -896 823 -732 O ATOM 3569 CB GLU C 99 105.658 24.618 265.252 1.00 43.56 C ANISOU 3569 CB GLU C 99 6537 6079 3936 -277 707 -513 C ATOM 3570 CG GLU C 99 105.854 26.011 264.686 1.00 46.70 C ANISOU 3570 CG GLU C 99 6675 6625 4443 -83 782 -425 C ATOM 3571 CD GLU C 99 107.098 26.691 265.222 1.00 44.31 C ANISOU 3571 CD GLU C 99 6392 6076 4368 109 738 -449 C ATOM 3572 OE1 GLU C 99 107.863 26.040 265.964 1.00 41.39 O ANISOU 3572 OE1 GLU C 99 6187 5489 4049 105 618 -496 O ATOM 3573 OE2 GLU C 99 107.309 27.879 264.904 1.00 64.86 O ANISOU 3573 OE2 GLU C 99 8827 8722 7095 246 832 -388 O ATOM 3574 N THR C 100 103.548 24.698 262.772 1.00 44.38 N ANISOU 3574 N THR C 100 6203 7092 3567 -678 837 -383 N ATOM 3575 CA THR C 100 103.240 24.526 261.355 1.00 36.84 C ANISOU 3575 CA THR C 100 5098 6515 2384 -883 862 -388 C ATOM 3576 C THR C 100 104.493 24.643 260.484 1.00 40.13 C ANISOU 3576 C THR C 100 5565 6755 2928 -713 910 -513 C ATOM 3577 O THR C 100 105.533 25.109 260.949 1.00 37.52 O ANISOU 3577 O THR C 100 5282 6081 2892 -403 914 -521 O ATOM 3578 CB THR C 100 102.194 25.562 260.888 1.00 37.73 C ANISOU 3578 CB THR C 100 4763 7202 2370 -850 900 -44 C ATOM 3579 OG1 THR C 100 101.308 25.872 261.971 1.00 68.24 O ANISOU 3579 OG1 THR C 100 8549 11111 6268 -800 927 137 O ATOM 3580 CG2 THR C 100 101.383 25.028 259.713 1.00 40.80 C ANISOU 3580 CG2 THR C 100 4983 8108 2410 -1244 838 -10 C ATOM 3581 N ILE C 101 104.381 24.199 259.232 1.00 51.08 N ANISOU 3581 N ILE C 101 6937 8414 4058 -958 950 -612 N ATOM 3582 CA ILE C 101 105.443 24.304 258.227 1.00 43.99 C ANISOU 3582 CA ILE C 101 6061 7436 3216 -824 1038 -715 C ATOM 3583 C ILE C 101 106.718 23.552 258.609 1.00 38.18 C ANISOU 3583 C ILE C 101 5676 6085 2744 -657 1114 -940 C ATOM 3584 O ILE C 101 107.132 22.625 257.911 1.00 40.34 O ANISOU 3584 O ILE C 101 6209 6203 2916 -809 1255 -1181 O ATOM 3585 CB ILE C 101 105.803 25.777 257.943 1.00 37.07 C ANISOU 3585 CB ILE C 101 4826 6726 2535 -459 1057 -435 C ATOM 3586 CG1 ILE C 101 104.556 26.555 257.516 1.00 38.31 C ANISOU 3586 CG1 ILE C 101 4581 7502 2472 -541 1043 -102 C ATOM 3587 CG2 ILE C 101 106.885 25.864 256.879 1.00 40.43 C ANISOU 3587 CG2 ILE C 101 5254 7104 3005 -334 1157 -519 C ATOM 3588 CD1 ILE C 101 104.800 28.031 257.304 1.00 37.40 C ANISOU 3588 CD1 ILE C 101 4130 7483 2596 -157 1138 227 C ATOM 3589 N VAL C 102 107.341 23.956 259.711 1.00 60.65 N ANISOU 3589 N VAL C 102 8524 8606 5916 -354 1047 -842 N ATOM 3590 CA VAL C 102 108.558 23.307 260.184 1.00 48.85 C ANISOU 3590 CA VAL C 102 7260 6617 4684 -158 1093 -930 C ATOM 3591 C VAL C 102 108.227 21.933 260.773 1.00 48.40 C ANISOU 3591 C VAL C 102 7554 6271 4566 -364 1141 -1067 C ATOM 3592 O VAL C 102 109.085 21.052 260.843 1.00 39.24 O ANISOU 3592 O VAL C 102 6633 4703 3574 -249 1278 -1139 O ATOM 3593 CB VAL C 102 109.288 24.185 261.231 1.00 44.30 C ANISOU 3593 CB VAL C 102 6539 5890 4401 140 967 -756 C ATOM 3594 CG1 VAL C 102 108.559 24.161 262.569 1.00 50.65 C ANISOU 3594 CG1 VAL C 102 7410 6668 5166 49 843 -697 C ATOM 3595 CG2 VAL C 102 110.740 23.761 261.381 1.00 56.19 C ANISOU 3595 CG2 VAL C 102 8120 7054 6176 382 1006 -739 C ATOM 3596 N GLU C 103 106.968 21.767 261.175 1.00 52.16 N ANISOU 3596 N GLU C 103 8040 6957 4821 -652 1063 -1061 N ATOM 3597 CA GLU C 103 106.451 20.512 261.721 1.00 54.56 C ANISOU 3597 CA GLU C 103 8665 7023 5042 -916 1117 -1174 C ATOM 3598 C GLU C 103 107.283 20.000 262.898 1.00 50.50 C ANISOU 3598 C GLU C 103 8329 6039 4821 -656 1113 -1076 C ATOM 3599 O GLU C 103 107.657 18.828 262.943 1.00 60.06 O ANISOU 3599 O GLU C 103 9857 6843 6122 -687 1293 -1162 O ATOM 3600 CB GLU C 103 106.378 19.446 260.625 1.00 75.06 C ANISOU 3600 CB GLU C 103 11554 9519 7448 -1240 1341 -1459 C ATOM 3601 CG GLU C 103 105.246 18.450 260.808 1.00 91.59 C ANISOU 3601 CG GLU C 103 13886 11626 9290 -1737 1384 -1597 C ATOM 3602 CD GLU C 103 103.878 19.099 260.711 1.00 99.67 C ANISOU 3602 CD GLU C 103 14576 13299 9994 -2038 1189 -1470 C ATOM 3603 OE1 GLU C 103 103.665 19.904 259.780 1.00113.06 O ANISOU 3603 OE1 GLU C 103 15968 15483 11506 -2070 1131 -1409 O ATOM 3604 OE2 GLU C 103 103.017 18.807 261.568 1.00 86.44 O ANISOU 3604 OE2 GLU C 103 12914 11670 8260 -2220 1111 -1378 O ATOM 3605 N GLU C 104 107.563 20.886 263.848 1.00 41.44 N ANISOU 3605 N GLU C 104 6978 4958 3808 -417 934 -879 N ATOM 3606 CA GLU C 104 108.327 20.526 265.039 1.00 53.99 C ANISOU 3606 CA GLU C 104 8659 6254 5602 -210 869 -724 C ATOM 3607 C GLU C 104 107.429 20.469 266.271 1.00 56.84 C ANISOU 3607 C GLU C 104 9064 6699 5835 -356 748 -631 C ATOM 3608 O GLU C 104 106.468 21.230 266.386 1.00 54.98 O ANISOU 3608 O GLU C 104 8681 6777 5432 -483 683 -632 O ATOM 3609 CB GLU C 104 109.466 21.523 265.267 1.00 46.62 C ANISOU 3609 CB GLU C 104 7485 5362 4866 93 751 -588 C ATOM 3610 CG GLU C 104 110.532 21.519 264.184 1.00 49.42 C ANISOU 3610 CG GLU C 104 7776 5610 5391 291 884 -618 C ATOM 3611 CD GLU C 104 111.789 20.780 264.599 1.00 74.44 C ANISOU 3611 CD GLU C 104 10996 8466 8822 557 942 -437 C ATOM 3612 OE1 GLU C 104 112.831 20.959 263.933 1.00 80.79 O ANISOU 3612 OE1 GLU C 104 11671 9217 9809 784 1032 -383 O ATOM 3613 OE2 GLU C 104 111.738 20.023 265.591 1.00 76.96 O ANISOU 3613 OE2 GLU C 104 11452 8620 9170 560 911 -295 O ATOM 3614 N ALA C 105 107.747 19.565 267.192 1.00 50.01 N ANISOU 3614 N ALA C 105 8385 5560 5056 -310 752 -505 N ATOM 3615 CA ALA C 105 106.979 19.430 268.424 1.00 47.17 C ANISOU 3615 CA ALA C 105 8082 5277 4562 -440 651 -392 C ATOM 3616 C ALA C 105 107.898 19.377 269.640 1.00 62.52 C ANISOU 3616 C ALA C 105 10007 7135 6613 -229 516 -145 C ATOM 3617 O ALA C 105 107.653 18.622 270.582 1.00 56.88 O ANISOU 3617 O ALA C 105 9436 6320 5857 -282 507 14 O ATOM 3618 CB ALA C 105 106.101 18.191 268.368 1.00 41.49 C ANISOU 3618 CB ALA C 105 7629 4384 3751 -722 803 -453 C ATOM 3619 N ASP C 106 108.952 20.186 269.617 1.00 50.63 N ANISOU 3619 N ASP C 106 8299 5715 5223 -20 403 -84 N ATOM 3620 CA ASP C 106 109.908 20.230 270.718 1.00 55.90 C ANISOU 3620 CA ASP C 106 8876 6428 5937 119 228 179 C ATOM 3621 C ASP C 106 109.523 21.283 271.755 1.00 46.81 C ANISOU 3621 C ASP C 106 7651 5584 4551 -31 44 149 C ATOM 3622 O ASP C 106 110.375 21.792 272.483 1.00 49.41 O ANISOU 3622 O ASP C 106 7850 6076 4848 -4 -136 276 O ATOM 3623 CB ASP C 106 111.320 20.500 270.192 1.00 49.73 C ANISOU 3623 CB ASP C 106 7892 5618 5387 367 202 287 C ATOM 3624 CG ASP C 106 111.388 21.731 269.312 1.00 73.60 C ANISOU 3624 CG ASP C 106 10749 8792 8424 354 197 67 C ATOM 3625 OD1 ASP C 106 110.387 22.028 268.626 1.00 81.40 O ANISOU 3625 OD1 ASP C 106 11797 9819 9311 224 305 -156 O ATOM 3626 OD2 ASP C 106 112.443 22.401 269.303 1.00 77.70 O ANISOU 3626 OD2 ASP C 106 11050 9418 9055 465 88 158 O ATOM 3627 N TYR C 107 108.235 21.608 271.811 1.00 44.71 N ANISOU 3627 N TYR C 107 7466 5415 4106 -212 117 -14 N ATOM 3628 CA TYR C 107 107.715 22.511 272.830 1.00 41.47 C ANISOU 3628 CA TYR C 107 7058 5230 3470 -345 51 -61 C ATOM 3629 C TYR C 107 107.118 21.710 273.980 1.00 48.25 C ANISOU 3629 C TYR C 107 8078 6116 4137 -468 21 86 C ATOM 3630 O TYR C 107 106.045 21.125 273.844 1.00 55.52 O ANISOU 3630 O TYR C 107 9102 6994 5001 -574 145 69 O ATOM 3631 CB TYR C 107 106.659 23.449 272.243 1.00 47.81 C ANISOU 3631 CB TYR C 107 7803 6141 4220 -403 211 -249 C ATOM 3632 CG TYR C 107 107.182 24.404 271.196 1.00 42.00 C ANISOU 3632 CG TYR C 107 6895 5410 3655 -280 260 -354 C ATOM 3633 CD1 TYR C 107 107.570 25.694 271.537 1.00 37.04 C ANISOU 3633 CD1 TYR C 107 6206 4840 3029 -272 268 -436 C ATOM 3634 CD2 TYR C 107 107.279 24.021 269.866 1.00 45.29 C ANISOU 3634 CD2 TYR C 107 7235 5762 4211 -205 331 -382 C ATOM 3635 CE1 TYR C 107 108.044 26.573 270.582 1.00 38.89 C ANISOU 3635 CE1 TYR C 107 6283 5051 3444 -161 341 -500 C ATOM 3636 CE2 TYR C 107 107.753 24.892 268.904 1.00 46.09 C ANISOU 3636 CE2 TYR C 107 7164 5895 4453 -86 384 -440 C ATOM 3637 CZ TYR C 107 108.134 26.166 269.267 1.00 41.78 C ANISOU 3637 CZ TYR C 107 6534 5390 3949 -48 388 -477 C ATOM 3638 OH TYR C 107 108.606 27.035 268.311 1.00 38.43 O ANISOU 3638 OH TYR C 107 5940 4973 3690 69 467 -503 O ATOM 3639 N TRP C 108 107.815 21.681 275.111 1.00 50.56 N ANISOU 3639 N TRP C 108 8373 6530 4306 -486 -152 257 N ATOM 3640 CA TRP C 108 107.357 20.910 276.260 1.00 43.91 C ANISOU 3640 CA TRP C 108 7668 5753 3262 -589 -189 456 C ATOM 3641 C TRP C 108 107.281 21.749 277.530 1.00 60.70 C ANISOU 3641 C TRP C 108 9831 8187 5044 -771 -294 415 C ATOM 3642 O TRP C 108 107.979 22.754 277.669 1.00 64.82 O ANISOU 3642 O TRP C 108 10272 8855 5501 -829 -391 290 O ATOM 3643 CB TRP C 108 108.271 19.704 276.490 1.00 46.52 C ANISOU 3643 CB TRP C 108 7979 5956 3740 -434 -268 822 C ATOM 3644 CG TRP C 108 108.111 18.620 275.467 1.00 46.49 C ANISOU 3644 CG TRP C 108 8074 5562 4027 -312 -57 844 C ATOM 3645 CD1 TRP C 108 108.832 18.462 274.320 1.00 47.31 C ANISOU 3645 CD1 TRP C 108 8115 5443 4418 -127 37 793 C ATOM 3646 CD2 TRP C 108 107.169 17.541 275.502 1.00 50.85 C ANISOU 3646 CD2 TRP C 108 8845 5889 4589 -416 125 892 C ATOM 3647 NE1 TRP C 108 108.398 17.350 273.638 1.00 46.94 N ANISOU 3647 NE1 TRP C 108 8272 5028 4534 -129 286 767 N ATOM 3648 CE2 TRP C 108 107.377 16.767 274.342 1.00 48.02 C ANISOU 3648 CE2 TRP C 108 8583 5150 4512 -326 337 824 C ATOM 3649 CE3 TRP C 108 106.170 17.152 276.400 1.00 61.08 C ANISOU 3649 CE3 TRP C 108 10274 7265 5670 -605 151 978 C ATOM 3650 CZ2 TRP C 108 106.624 15.630 274.057 1.00 49.75 C ANISOU 3650 CZ2 TRP C 108 9057 5048 4798 -472 575 804 C ATOM 3651 CZ3 TRP C 108 105.423 16.023 276.116 1.00 58.15 C ANISOU 3651 CZ3 TRP C 108 10108 6595 5392 -722 364 1006 C ATOM 3652 CH2 TRP C 108 105.654 15.275 274.954 1.00 62.06 C ANISOU 3652 CH2 TRP C 108 10724 6693 6163 -680 574 903 C ATOM 3653 N GLY C 109 106.424 21.328 278.454 1.00 69.05 N ANISOU 3653 N GLY C 109 11034 9338 5864 -900 -247 503 N ATOM 3654 CA GLY C 109 106.302 21.983 279.741 1.00 59.41 C ANISOU 3654 CA GLY C 109 9905 8415 4254 -1104 -306 457 C ATOM 3655 C GLY C 109 107.174 21.305 280.779 1.00 62.83 C ANISOU 3655 C GLY C 109 10299 9078 4496 -1154 -558 815 C ATOM 3656 O GLY C 109 107.759 20.253 280.517 1.00 53.35 O ANISOU 3656 O GLY C 109 9001 7750 3520 -970 -634 1148 O ATOM 3657 N GLN C 110 107.262 21.907 281.961 1.00 62.90 N ANISOU 3657 N GLN C 110 10386 9437 4077 -1406 -656 767 N ATOM 3658 CA GLN C 110 108.089 21.371 283.036 1.00 58.98 C ANISOU 3658 CA GLN C 110 9802 9305 3300 -1508 -934 1152 C ATOM 3659 C GLN C 110 107.517 20.068 283.586 1.00 63.69 C ANISOU 3659 C GLN C 110 10463 9869 3868 -1419 -890 1548 C ATOM 3660 O GLN C 110 108.255 19.211 284.071 1.00 63.90 O ANISOU 3660 O GLN C 110 10344 10056 3877 -1331 -1072 2038 O ATOM 3661 CB GLN C 110 108.231 22.398 284.161 1.00 63.71 C ANISOU 3661 CB GLN C 110 10455 10277 3474 -1841 -1001 909 C ATOM 3662 N GLY C 111 106.198 19.923 283.506 1.00 67.69 N ANISOU 3662 N GLY C 111 11159 10177 4383 -1436 -628 1384 N ATOM 3663 CA GLY C 111 105.532 18.730 283.994 1.00 60.77 C ANISOU 3663 CA GLY C 111 10368 9230 3492 -1400 -543 1725 C ATOM 3664 C GLY C 111 104.916 18.930 285.364 1.00 63.67 C ANISOU 3664 C GLY C 111 10791 9915 3485 -1570 -507 1709 C ATOM 3665 O GLY C 111 105.598 19.323 286.310 1.00 78.41 O ANISOU 3665 O GLY C 111 12559 12133 5102 -1671 -687 1741 O ATOM 3666 N THR C 112 103.619 18.660 285.469 1.00 63.05 N ANISOU 3666 N THR C 112 10819 9706 3430 -1588 -259 1636 N ATOM 3667 CA THR C 112 102.913 18.784 286.739 1.00 76.15 C ANISOU 3667 CA THR C 112 12505 11604 4823 -1683 -167 1617 C ATOM 3668 C THR C 112 102.515 17.411 287.274 1.00 81.50 C ANISOU 3668 C THR C 112 13212 12254 5499 -1644 -137 2077 C ATOM 3669 O THR C 112 102.189 16.503 286.507 1.00 79.90 O ANISOU 3669 O THR C 112 13069 11731 5558 -1588 -40 2268 O ATOM 3670 CB THR C 112 101.659 19.672 286.606 1.00 81.34 C ANISOU 3670 CB THR C 112 13217 12187 5502 -1712 134 1221 C ATOM 3671 OG1 THR C 112 100.932 19.666 287.842 1.00101.93 O ANISOU 3671 OG1 THR C 112 15876 14999 7853 -1780 253 1256 O ATOM 3672 CG2 THR C 112 100.757 19.169 285.489 1.00 78.23 C ANISOU 3672 CG2 THR C 112 12819 11501 5405 -1647 312 1237 C ATOM 3673 N GLN C 113 102.550 17.265 288.595 1.00 82.17 N ANISOU 3673 N GLN C 113 13280 12651 5289 -1701 -197 2248 N ATOM 3674 CA GLN C 113 102.250 15.989 289.235 1.00 77.61 C ANISOU 3674 CA GLN C 113 12722 12066 4700 -1648 -158 2729 C ATOM 3675 C GLN C 113 100.770 15.854 289.575 1.00 80.75 C ANISOU 3675 C GLN C 113 13210 12409 5062 -1715 121 2632 C ATOM 3676 O GLN C 113 100.166 16.767 290.138 1.00 79.25 O ANISOU 3676 O GLN C 113 13048 12405 4657 -1796 233 2311 O ATOM 3677 CB GLN C 113 103.091 15.821 290.504 1.00 81.04 C ANISOU 3677 CB GLN C 113 13062 12907 4822 -1668 -379 3028 C ATOM 3678 CG GLN C 113 102.804 14.543 291.277 1.00 85.10 C ANISOU 3678 CG GLN C 113 13593 13424 5318 -1587 -317 3559 C ATOM 3679 CD GLN C 113 103.261 13.300 290.540 1.00 85.26 C ANISOU 3679 CD GLN C 113 13598 13058 5739 -1372 -286 4046 C ATOM 3680 OE1 GLN C 113 104.392 13.231 290.058 1.00 98.55 O ANISOU 3680 OE1 GLN C 113 15152 14713 7581 -1236 -457 4227 O ATOM 3681 NE2 GLN C 113 102.381 12.310 290.445 1.00 85.83 N ANISOU 3681 NE2 GLN C 113 13806 12798 6008 -1344 -30 4267 N ATOM 3682 N VAL C 114 100.192 14.710 289.227 1.00 76.88 N ANISOU 3682 N VAL C 114 12770 11639 4803 -1688 262 2928 N ATOM 3683 CA VAL C 114 98.806 14.414 289.569 1.00 77.38 C ANISOU 3683 CA VAL C 114 12872 11679 4852 -1772 510 2923 C ATOM 3684 C VAL C 114 98.710 13.062 290.270 1.00 86.57 C ANISOU 3684 C VAL C 114 14083 12778 6032 -1748 563 3450 C ATOM 3685 O VAL C 114 98.962 12.019 289.666 1.00 81.42 O ANISOU 3685 O VAL C 114 13489 11766 5682 -1712 608 3753 O ATOM 3686 CB VAL C 114 97.897 14.413 288.324 1.00 73.83 C ANISOU 3686 CB VAL C 114 12420 10932 4701 -1853 690 2699 C ATOM 3687 CG1 VAL C 114 96.501 13.928 288.683 1.00 80.31 C ANISOU 3687 CG1 VAL C 114 13224 11762 5528 -1961 924 2793 C ATOM 3688 CG2 VAL C 114 97.841 15.802 287.704 1.00 75.49 C ANISOU 3688 CG2 VAL C 114 12563 11215 4906 -1829 698 2223 C ATOM 3689 N THR C 115 98.351 13.089 291.550 1.00105.71 N ANISOU 3689 N THR C 115 16512 15510 8143 -1766 595 3559 N ATOM 3690 CA THR C 115 98.232 11.868 292.339 1.00 89.22 C ANISOU 3690 CA THR C 115 14473 13384 6042 -1729 665 4074 C ATOM 3691 C THR C 115 96.789 11.631 292.772 1.00 90.41 C ANISOU 3691 C THR C 115 14656 13546 6149 -1841 930 4063 C ATOM 3692 O THR C 115 96.162 12.501 293.376 1.00 90.63 O ANISOU 3692 O THR C 115 14670 13862 5905 -1890 1000 3787 O ATOM 3693 CB THR C 115 99.131 11.912 293.588 1.00 93.81 C ANISOU 3693 CB THR C 115 15022 14359 6263 -1672 453 4316 C ATOM 3694 OG1 THR C 115 100.496 12.100 293.193 1.00 93.30 O ANISOU 3694 OG1 THR C 115 14861 14331 6257 -1576 190 4379 O ATOM 3695 CG2 THR C 115 99.011 10.617 294.377 1.00100.94 C ANISOU 3695 CG2 THR C 115 15978 15195 7180 -1612 543 4887 C ATOM 3696 N VAL C 116 96.271 10.448 292.460 1.00 91.69 N ANISOU 3696 N VAL C 116 14870 13368 6599 -1887 1109 4376 N ATOM 3697 CA VAL C 116 94.901 10.095 292.812 1.00 97.48 C ANISOU 3697 CA VAL C 116 15602 14106 7331 -2022 1358 4418 C ATOM 3698 C VAL C 116 94.865 8.931 293.797 1.00 98.79 C ANISOU 3698 C VAL C 116 15865 14218 7454 -1987 1463 4943 C ATOM 3699 O VAL C 116 95.903 8.365 294.142 1.00101.46 O ANISOU 3699 O VAL C 116 16270 14488 7792 -1842 1351 5292 O ATOM 3700 CB VAL C 116 94.076 9.726 291.566 1.00105.51 C ANISOU 3700 CB VAL C 116 16585 14777 8726 -2216 1511 4279 C ATOM 3701 CG1 VAL C 116 92.676 9.293 291.967 1.00100.03 C ANISOU 3701 CG1 VAL C 116 15844 14128 8034 -2382 1750 4378 C ATOM 3702 CG2 VAL C 116 94.023 10.899 290.598 1.00 85.73 C ANISOU 3702 CG2 VAL C 116 13985 12341 6248 -2239 1427 3779 C TER 3703 VAL C 116 HETATM 3704 C1 CLR A 401 114.690 30.275 223.322 1.00100.48 C HETATM 3705 C2 CLR A 401 114.791 30.719 221.867 1.00104.64 C HETATM 3706 C3 CLR A 401 113.470 31.375 221.454 1.00 89.34 C HETATM 3707 C4 CLR A 401 113.264 32.626 222.316 1.00 78.82 C HETATM 3708 C5 CLR A 401 113.283 32.251 223.760 1.00 88.50 C HETATM 3709 C6 CLR A 401 112.322 32.713 224.540 1.00 97.67 C HETATM 3710 C7 CLR A 401 112.245 32.409 225.986 1.00102.59 C HETATM 3711 C8 CLR A 401 113.643 32.121 226.518 1.00104.87 C HETATM 3712 C9 CLR A 401 114.315 31.014 225.694 1.00 99.29 C HETATM 3713 C10 CLR A 401 114.493 31.495 224.234 1.00 98.33 C HETATM 3714 C11 CLR A 401 115.668 30.607 226.292 1.00104.26 C HETATM 3715 C12 CLR A 401 115.587 30.263 227.776 1.00 93.67 C HETATM 3716 C13 CLR A 401 114.968 31.433 228.541 1.00 99.32 C HETATM 3717 C14 CLR A 401 113.555 31.657 227.962 1.00111.83 C HETATM 3718 C15 CLR A 401 112.944 32.622 228.963 1.00120.49 C HETATM 3719 C16 CLR A 401 113.391 32.035 230.307 1.00115.86 C HETATM 3720 C17 CLR A 401 114.654 31.179 230.036 1.00 99.50 C HETATM 3721 C18 CLR A 401 115.808 32.721 228.392 1.00101.47 C HETATM 3722 C19 CLR A 401 115.709 32.424 224.126 1.00104.99 C HETATM 3723 C20 CLR A 401 115.806 31.549 230.990 1.00101.86 C HETATM 3724 C21 CLR A 401 116.829 30.413 231.073 1.00112.48 C HETATM 3725 C22 CLR A 401 115.255 31.892 232.383 1.00102.74 C HETATM 3726 C23 CLR A 401 116.310 31.617 233.450 1.00106.84 C HETATM 3727 C24 CLR A 401 115.654 31.068 234.707 1.00 95.44 C HETATM 3728 C25 CLR A 401 114.990 32.201 235.489 1.00 93.51 C HETATM 3729 C26 CLR A 401 114.260 31.622 236.690 1.00 84.57 C HETATM 3730 C27 CLR A 401 116.043 33.205 235.944 1.00103.85 C HETATM 3731 O1 CLR A 401 113.590 31.728 220.113 1.00 93.70 O HETATM 3732 C1 CLR A 402 117.401 28.046 222.173 1.00 78.72 C HETATM 3733 C2 CLR A 402 117.114 28.080 220.681 1.00 77.38 C HETATM 3734 C3 CLR A 402 118.205 27.295 219.957 1.00 75.39 C HETATM 3735 C4 CLR A 402 118.110 25.835 220.404 1.00 83.00 C HETATM 3736 C5 CLR A 402 118.259 25.748 221.887 1.00 83.84 C HETATM 3737 C6 CLR A 402 119.006 24.776 222.378 1.00 84.99 C HETATM 3738 C7 CLR A 402 119.306 24.643 223.821 1.00 81.90 C HETATM 3739 C8 CLR A 402 118.149 25.190 224.651 1.00 78.45 C HETATM 3740 C9 CLR A 402 117.754 26.602 224.194 1.00 75.34 C HETATM 3741 C10 CLR A 402 117.335 26.604 222.704 1.00 77.30 C HETATM 3742 C11 CLR A 402 116.640 27.167 225.071 1.00 73.59 C HETATM 3743 C12 CLR A 402 117.043 27.203 226.535 1.00 74.43 C HETATM 3744 C13 CLR A 402 117.426 25.794 227.001 1.00 75.25 C HETATM 3745 C14 CLR A 402 118.584 25.292 226.106 1.00 77.77 C HETATM 3746 C15 CLR A 402 119.001 24.009 226.814 1.00 78.66 C HETATM 3747 C16 CLR A 402 118.981 24.428 228.294 1.00 80.89 C HETATM 3748 C17 CLR A 402 118.081 25.690 228.401 1.00 82.97 C HETATM 3749 C18 CLR A 402 116.230 24.827 226.903 1.00 69.70 C HETATM 3750 C19 CLR A 402 115.911 26.060 222.543 1.00 75.35 C HETATM 3751 C20 CLR A 402 117.078 25.582 229.568 1.00 92.60 C HETATM 3752 C21 CLR A 402 116.541 26.961 229.958 1.00 94.88 C HETATM 3753 C22 CLR A 402 117.739 24.909 230.776 1.00 92.99 C HETATM 3754 C23 CLR A 402 116.891 25.138 232.023 1.00 91.77 C HETATM 3755 C24 CLR A 402 117.736 25.752 233.130 1.00 90.30 C HETATM 3756 C25 CLR A 402 117.872 24.772 234.295 1.00 90.87 C HETATM 3757 C26 CLR A 402 119.047 25.189 235.165 1.00101.14 C HETATM 3758 C27 CLR A 402 116.590 24.758 235.118 1.00 77.91 C HETATM 3759 O1 CLR A 402 117.953 27.403 218.592 1.00 63.89 O HETATM 3760 C10 OLC A 403 118.496 17.783 229.832 1.00 84.93 C HETATM 3761 C9 OLC A 403 118.156 16.502 229.710 1.00 78.57 C HETATM 3762 C11 OLC A 403 119.499 18.400 228.885 1.00 84.98 C HETATM 3763 C8 OLC A 403 118.773 15.647 228.628 1.00 72.98 C HETATM 3764 C24 OLC A 403 123.629 6.600 223.249 1.00117.32 C HETATM 3765 C12 OLC A 403 118.824 19.507 228.084 1.00 70.12 C HETATM 3766 C7 OLC A 403 119.016 14.246 229.176 1.00 65.33 C HETATM 3767 C13 OLC A 403 119.746 20.022 226.985 1.00 66.50 C HETATM 3768 C6 OLC A 403 119.953 13.435 228.288 1.00 49.62 C HETATM 3769 C5 OLC A 403 119.230 12.775 227.119 1.00 43.79 C HETATM 3770 C4 OLC A 403 119.880 11.429 226.821 1.00 51.76 C HETATM 3771 C3 OLC A 403 119.441 10.835 225.487 1.00 60.44 C HETATM 3772 C2 OLC A 403 119.945 9.401 225.379 1.00 73.87 C HETATM 3773 C21 OLC A 403 121.683 7.838 222.289 1.00126.46 C HETATM 3774 C1 OLC A 403 120.234 9.043 223.941 1.00 94.72 C HETATM 3775 C22 OLC A 403 123.166 7.519 222.124 1.00125.52 C HETATM 3776 O19 OLC A 403 119.470 9.368 223.046 1.00 92.21 O HETATM 3777 O25 OLC A 403 125.055 6.468 223.199 1.00102.84 O HETATM 3778 O23 OLC A 403 123.380 6.874 220.864 1.00120.73 O HETATM 3779 O20 OLC A 403 121.445 8.305 223.616 1.00123.33 O HETATM 3780 C10 OLC A 404 116.511 26.978 246.133 1.00 72.65 C HETATM 3781 C9 OLC A 404 116.319 26.901 247.451 1.00 72.49 C HETATM 3782 C11 OLC A 404 117.903 27.125 245.562 1.00 81.82 C HETATM 3783 C8 OLC A 404 117.476 26.966 248.423 1.00 74.67 C HETATM 3784 C24 OLC A 404 115.227 33.568 258.385 1.00 83.17 C HETATM 3785 C12 OLC A 404 118.014 26.257 244.314 1.00 83.87 C HETATM 3786 C7 OLC A 404 117.072 27.714 249.688 1.00 82.61 C HETATM 3787 C13 OLC A 404 119.204 26.655 243.448 1.00 80.67 C HETATM 3788 C6 OLC A 404 116.681 29.150 249.377 1.00 84.27 C HETATM 3789 C5 OLC A 404 116.339 29.931 250.642 1.00 73.42 C HETATM 3790 C4 OLC A 404 117.583 30.573 251.253 1.00 69.42 C HETATM 3791 C3 OLC A 404 117.224 31.941 251.829 1.00 80.65 C HETATM 3792 C2 OLC A 404 118.012 32.246 253.097 1.00 91.14 C HETATM 3793 C21 OLC A 404 116.271 33.805 256.123 1.00105.19 C HETATM 3794 C1 OLC A 404 117.271 33.300 253.886 1.00102.41 C HETATM 3795 C22 OLC A 404 116.528 33.484 257.593 1.00 95.75 C HETATM 3796 O19 OLC A 404 116.574 34.128 253.322 1.00107.26 O HETATM 3797 O25 OLC A 404 114.757 34.921 258.399 1.00 73.34 O HETATM 3798 O23 OLC A 404 117.078 32.166 257.708 1.00 80.58 O HETATM 3799 O20 OLC A 404 117.358 33.312 255.338 1.00106.76 O HETATM 3800 C9 OLC A 405 113.230 8.058 244.692 1.00109.85 C HETATM 3801 C8 OLC A 405 112.999 9.519 245.000 1.00100.39 C HETATM 3802 C24 OLC A 405 114.645 11.440 256.653 1.00100.60 C HETATM 3803 C7 OLC A 405 112.567 9.698 246.451 1.00 82.30 C HETATM 3804 C6 OLC A 405 112.377 11.178 246.756 1.00 72.25 C HETATM 3805 C5 OLC A 405 111.515 11.387 247.995 1.00 62.68 C HETATM 3806 C4 OLC A 405 112.253 10.981 249.266 1.00 59.57 C HETATM 3807 C3 OLC A 405 112.133 12.088 250.310 1.00 58.12 C HETATM 3808 C2 OLC A 405 112.330 11.532 251.715 1.00 59.10 C HETATM 3809 C21 OLC A 405 114.898 12.510 254.416 1.00 98.27 C HETATM 3810 C1 OLC A 405 113.422 12.300 252.417 1.00 79.89 C HETATM 3811 C22 OLC A 405 115.437 11.437 255.350 1.00104.89 C HETATM 3812 O19 OLC A 405 114.057 13.165 251.831 1.00 90.95 O HETATM 3813 O25 OLC A 405 115.250 10.523 257.573 1.00100.85 O HETATM 3814 O23 OLC A 405 115.267 10.171 254.702 1.00106.80 O HETATM 3815 O20 OLC A 405 113.724 11.989 253.803 1.00101.21 O HETATM 3816 C10 OLC A 406 108.065 37.932 242.874 1.00 86.06 C HETATM 3817 C9 OLC A 406 108.233 37.517 244.127 1.00 87.29 C HETATM 3818 C11 OLC A 406 109.189 37.733 241.890 1.00 94.29 C HETATM 3819 C8 OLC A 406 109.544 36.885 244.548 1.00 93.65 C HETATM 3820 C24 OLC A 406 112.867 37.391 254.962 1.00 68.16 C HETATM 3821 C12 OLC A 406 108.610 37.125 240.621 1.00 95.83 C HETATM 3822 C7 OLC A 406 109.397 36.229 245.915 1.00 95.86 C HETATM 3823 C13 OLC A 406 109.679 36.916 239.551 1.00 80.59 C HETATM 3824 C6 OLC A 406 108.914 37.231 246.954 1.00 87.08 C HETATM 3825 C14 OLC A 406 109.096 36.410 238.230 1.00 59.44 C HETATM 3826 C5 OLC A 406 108.229 36.512 248.111 1.00 77.95 C HETATM 3827 C4 OLC A 406 109.148 35.482 248.759 1.00 61.50 C HETATM 3828 C3 OLC A 406 108.518 34.965 250.048 1.00 52.09 C HETATM 3829 C2 OLC A 406 109.518 34.884 251.197 1.00 60.09 C HETATM 3830 C21 OLC A 406 110.925 37.730 253.427 1.00 58.31 C HETATM 3831 C1 OLC A 406 109.812 36.260 251.760 1.00 74.54 C HETATM 3832 C22 OLC A 406 111.375 37.697 254.885 1.00 64.46 C HETATM 3833 O19 OLC A 406 109.326 37.264 251.264 1.00 91.99 O HETATM 3834 O25 OLC A 406 113.283 37.397 256.332 1.00 74.78 O HETATM 3835 O23 OLC A 406 111.124 38.973 255.488 1.00 71.68 O HETATM 3836 O20 OLC A 406 110.676 36.417 252.922 1.00 58.63 O HETATM 3837 C18 OLC A 407 104.361 37.725 237.286 1.00 57.59 C HETATM 3838 C10 OLC A 407 104.461 40.220 246.249 1.00 71.71 C HETATM 3839 C9 OLC A 407 104.729 40.891 247.368 1.00 73.98 C HETATM 3840 C17 OLC A 407 104.678 37.389 238.731 1.00 62.76 C HETATM 3841 C11 OLC A 407 103.374 40.722 245.326 1.00 56.77 C HETATM 3842 C8 OLC A 407 103.926 42.127 247.711 1.00 84.93 C HETATM 3843 C24 OLC A 407 103.364 44.996 256.698 1.00 96.76 C HETATM 3844 C16 OLC A 407 104.306 38.550 239.653 1.00 58.87 C HETATM 3845 C12 OLC A 407 103.076 39.713 244.219 1.00 58.25 C HETATM 3846 C7 OLC A 407 103.760 42.232 249.225 1.00 73.13 C HETATM 3847 C15 OLC A 407 104.851 38.347 241.066 1.00 55.24 C HETATM 3848 C13 OLC A 407 104.250 39.474 243.273 1.00 49.49 C HETATM 3849 C6 OLC A 407 104.781 43.200 249.811 1.00 66.63 C HETATM 3850 C14 OLC A 407 103.758 38.642 242.090 1.00 60.76 C HETATM 3851 C5 OLC A 407 104.134 44.533 250.182 1.00 73.63 C HETATM 3852 C4 OLC A 407 104.494 45.001 251.596 1.00 81.81 C HETATM 3853 C3 OLC A 407 105.837 45.725 251.596 1.00 88.03 C HETATM 3854 C2 OLC A 407 106.239 46.210 252.981 1.00 97.86 C HETATM 3855 C21 OLC A 407 105.627 44.133 256.204 1.00 93.00 C HETATM 3856 C1 OLC A 407 106.296 45.068 253.973 1.00114.59 C HETATM 3857 C22 OLC A 407 104.271 43.783 256.816 1.00101.79 C HETATM 3858 O19 OLC A 407 107.054 44.124 253.820 1.00122.81 O HETATM 3859 O25 OLC A 407 102.004 44.577 256.699 1.00 68.87 O HETATM 3860 O23 OLC A 407 103.677 42.666 256.138 1.00116.19 O HETATM 3861 O20 OLC A 407 105.430 45.070 255.142 1.00110.77 O HETATM 3862 C24 OLC A 408 116.155 17.678 251.850 1.00123.44 C HETATM 3863 C7 OLC A 408 117.094 22.681 242.654 1.00 56.68 C HETATM 3864 C6 OLC A 408 116.287 23.002 243.912 1.00 58.82 C HETATM 3865 C5 OLC A 408 116.184 21.765 244.810 1.00 64.60 C HETATM 3866 C4 OLC A 408 115.312 22.020 246.042 1.00 68.34 C HETATM 3867 C3 OLC A 408 115.342 20.818 246.985 1.00 72.10 C HETATM 3868 C2 OLC A 408 114.100 20.792 247.874 1.00 73.72 C HETATM 3869 C21 OLC A 408 115.319 19.094 249.982 1.00110.23 C HETATM 3870 C1 OLC A 408 114.408 21.310 249.261 1.00 91.12 C HETATM 3871 C22 OLC A 408 114.914 18.137 251.089 1.00116.97 C HETATM 3872 O19 OLC A 408 114.263 22.494 249.521 1.00 89.61 O HETATM 3873 O25 OLC A 408 115.758 16.727 252.854 1.00113.97 O HETATM 3874 O23 OLC A 408 114.031 18.825 251.981 1.00111.47 O HETATM 3875 O20 OLC A 408 114.861 20.402 250.305 1.00103.43 O HETATM 3876 C33 UNL A 409 97.693 39.107 244.097 1.00 66.46 C HETATM 3877 C32 UNL A 409 97.400 37.935 244.993 1.00 61.52 C HETATM 3878 C31 UNL A 409 96.448 38.440 246.044 1.00 55.56 C HETATM 3879 C30 UNL A 409 96.290 37.324 247.047 1.00 61.57 C HETATM 3880 C29 UNL A 409 95.374 37.839 248.133 1.00 64.12 C HETATM 3881 C28 UNL A 409 95.268 36.776 249.208 1.00 47.52 C HETATM 3882 C27 UNL A 409 94.299 37.233 250.275 1.00 48.99 C HETATM 3883 C38 UNL A 410 122.141 15.071 215.657 1.00 67.44 C HETATM 3884 C37 UNL A 410 121.692 14.024 216.642 1.00 72.99 C HETATM 3885 C36 UNL A 410 121.025 14.758 217.774 1.00 82.67 C HETATM 3886 C35 UNL A 410 120.571 13.706 218.749 1.00 83.48 C HETATM 3887 C34 UNL A 410 120.237 14.427 220.027 1.00 68.76 C HETATM 3888 C33 UNL A 410 119.989 13.362 221.059 1.00 61.77 C HETATM 3889 C32 UNL A 410 119.759 14.073 222.365 1.00 64.39 C HETATM 3890 C31 UNL A 410 121.120 14.434 222.900 1.00 40.26 C HETATM 3891 C30 UNL A 410 120.881 15.384 224.047 1.00 43.13 C HETATM 3892 C29 UNL A 410 122.155 15.432 224.857 1.00 42.25 C HETATM 3893 C28 UNL A 410 121.973 16.460 225.955 1.00 51.75 C HETATM 3894 C27 UNL A 410 123.058 16.290 226.993 1.00 68.72 C HETATM 3895 C36 UNL A 411 91.575 37.986 226.655 1.00 54.71 C HETATM 3896 C35 UNL A 411 92.144 38.183 225.276 1.00 62.89 C HETATM 3897 C34 UNL A 411 92.261 36.813 224.665 1.00 70.89 C HETATM 3898 C33 UNL A 411 93.058 36.976 223.399 1.00 75.96 C HETATM 3899 C32 UNL A 411 92.129 37.557 222.367 1.00 64.32 C HETATM 3900 C31 UNL A 411 92.931 37.653 221.095 1.00 57.44 C HETATM 3901 C30 UNL A 411 91.964 38.033 220.003 1.00 60.03 C HETATM 3902 C29 UNL A 411 92.748 38.044 218.710 1.00 70.36 C HETATM 3903 C28 UNL A 411 91.766 38.062 217.556 1.00 78.90 C HETATM 3904 C27 UNL A 411 91.016 39.374 217.548 1.00 85.26 C HETATM 3905 C42 UNL A 412 87.907 27.949 243.983 1.00 52.12 C HETATM 3906 C41 UNL A 412 87.683 26.950 245.098 1.00 50.13 C HETATM 3907 C40 UNL A 412 87.828 27.646 246.437 1.00 55.71 C HETATM 3908 C39 UNL A 412 87.470 26.666 247.531 1.00 61.58 C HETATM 3909 C38 UNL A 412 87.386 27.447 248.822 1.00 55.11 C HETATM 3910 C37 UNL A 412 88.774 27.464 249.411 1.00 59.02 C HETATM 3911 C36 UNL A 412 89.050 28.890 249.802 1.00 57.59 C HETATM 3912 C35 UNL A 412 90.383 28.896 250.504 1.00 62.46 C HETATM 3913 C34 UNL A 412 90.149 28.306 251.869 1.00 75.15 C HETATM 3914 C33 UNL A 412 91.242 28.844 252.753 1.00 68.14 C HETATM 3915 C32 UNL A 412 91.075 28.186 254.097 1.00 56.56 C HETATM 3916 C31 UNL A 412 91.590 26.780 253.941 1.00 39.50 C HETATM 3917 C42 UNL A 413 89.917 13.022 237.792 1.00 44.01 C HETATM 3918 C41 UNL A 413 89.476 12.877 239.232 1.00 50.56 C HETATM 3919 C40 UNL A 413 90.666 12.489 240.089 1.00 62.65 C HETATM 3920 C39 UNL A 413 90.208 12.383 241.525 1.00 65.33 C HETATM 3921 C38 UNL A 413 91.439 12.174 242.374 1.00 61.55 C HETATM 3922 C37 UNL A 413 90.954 12.069 243.797 1.00 62.79 C HETATM 3923 C36 UNL A 413 92.173 12.142 244.676 1.00 52.51 C HETATM 3924 C35 UNL A 413 91.676 12.013 246.091 1.00 52.12 C HETATM 3925 C34 UNL A 413 92.866 12.238 246.984 1.00 48.85 C HETATM 3926 C33 UNL A 413 92.371 12.067 248.394 1.00 42.42 C HETATM 3927 C38 UNL A 414 111.563 4.062 234.702 1.00 61.81 C HETATM 3928 C37 UNL A 414 111.245 3.781 233.257 1.00 60.48 C HETATM 3929 C36 UNL A 414 109.765 4.001 233.093 1.00 61.11 C HETATM 3930 C35 UNL A 414 109.401 3.430 231.750 1.00 61.41 C HETATM 3931 C34 UNL A 414 107.898 3.347 231.717 1.00 60.77 C HETATM 3932 C33 UNL A 414 107.549 2.501 230.523 1.00 59.17 C HETATM 3933 C32 UNL A 414 107.878 3.318 229.304 1.00 62.32 C HETATM 3934 C31 UNL A 414 108.206 2.333 228.216 1.00 56.62 C HETATM 3935 C30 UNL A 414 107.080 2.403 227.217 1.00 61.70 C HETATM 3936 C29 UNL A 414 107.405 1.403 226.133 1.00 70.61 C HETATM 3937 C28 UNL A 414 106.306 1.453 225.093 1.00 66.54 C HETATM 3938 C27 UNL A 414 106.584 0.432 224.016 1.00 59.55 C HETATM 3939 C27 UNL A 415 121.465 29.133 225.227 1.00 95.11 C HETATM 3940 C28 UNL A 415 122.728 29.367 224.433 1.00 77.71 C HETATM 3941 C29 UNL A 415 122.448 29.183 222.954 1.00 67.52 C HETATM 3942 C30 UNL A 415 123.492 29.979 222.194 1.00 57.72 C HETATM 3943 C31 UNL A 415 123.158 29.849 220.720 1.00 65.23 C HETATM 3944 C32 UNL A 415 124.074 30.797 219.981 1.00 61.65 C HETATM 3945 C33 UNL A 415 123.669 30.734 218.528 1.00 60.02 C HETATM 3946 C34 UNL A 415 124.435 31.845 217.861 1.00 71.17 C HETATM 3947 C35 UNL A 415 124.005 31.905 216.425 1.00 73.91 C HETATM 3948 C36 UNL A 415 124.517 30.650 215.734 1.00 64.61 C HETATM 3949 C37 UNL A 415 124.875 31.084 214.330 1.00 69.50 C HETATM 3950 C38 UNL A 415 123.643 31.775 213.773 1.00 71.27 C HETATM 3951 C1 SIN A 416 94.962 28.415 240.325 1.00 89.35 C HETATM 3952 O1 SIN A 416 95.198 27.957 239.175 1.00 73.87 O HETATM 3953 O2 SIN A 416 95.557 28.001 241.353 1.00107.20 O HETATM 3954 C2 SIN A 416 93.899 29.516 240.438 1.00 84.34 C HETATM 3955 C3 SIN A 416 93.563 29.909 241.868 1.00 79.28 C HETATM 3956 C4 SIN A 416 92.565 31.067 241.989 1.00 89.13 C HETATM 3957 O3 SIN A 416 92.152 31.664 240.964 1.00 86.31 O HETATM 3958 O4 SIN A 416 92.188 31.378 243.152 1.00 98.57 O HETATM 3959 O HOH A 501 117.905 27.738 261.908 1.00 45.01 O HETATM 3960 O HOH A 502 105.620 23.776 245.236 1.00 31.46 O HETATM 3961 O HOH A 503 102.360 26.521 248.523 1.00 33.42 O HETATM 3962 O HOH A 504 107.159 17.907 227.119 1.00 32.71 O HETATM 3963 O HOH A 505 107.392 25.425 244.519 1.00 27.05 O HETATM 3964 O HOH A 506 106.337 24.458 252.857 1.00 37.83 O HETATM 3965 O HOH A 507 103.513 16.109 246.279 1.00 44.45 O HETATM 3966 O HOH A 508 102.491 6.818 259.111 1.00 28.14 O HETATM 3967 O HOH A 509 115.606 28.399 263.700 1.00 31.21 O HETATM 3968 O HOH A 510 93.816 27.862 257.919 1.00 41.32 O HETATM 3969 O HOH A 511 104.639 17.496 249.496 1.00 38.68 O HETATM 3970 O HOH A 512 90.096 10.229 221.754 1.00 60.46 O HETATM 3971 O HOH A 513 110.499 25.551 232.077 1.00 51.39 O HETATM 3972 O HOH A 514 96.328 22.388 225.472 1.00 44.94 O HETATM 3973 O HOH A 515 89.436 9.304 224.107 1.00 50.73 O HETATM 3974 O HOH A 516 93.505 25.696 258.915 1.00 38.95 O HETATM 3975 O HOH A 517 93.367 21.829 260.859 1.00 45.30 O HETATM 3976 O HOH A 518 103.835 21.048 239.745 1.00 69.30 O HETATM 3977 O HOH B 101 98.652 16.492 226.868 1.00 47.47 O HETATM 3978 O HOH C 201 106.421 22.540 255.359 1.00 25.65 O HETATM 3979 O HOH C 202 105.661 32.087 265.174 1.00 32.06 O HETATM 3980 O HOH C 203 100.058 29.968 267.293 1.00 32.66 O HETATM 3981 O HOH C 204 109.729 17.944 266.927 1.00 40.20 O CONECT 70 1972 CONECT 663 1232 CONECT 1232 663 CONECT 1972 70 CONECT 2359 2360 2363 CONECT 2360 2359 2361 2365 CONECT 2361 2360 2362 CONECT 2362 2361 2363 CONECT 2363 2359 2362 2364 CONECT 2364 2363 CONECT 2365 2360 2366 2367 CONECT 2366 2365 CONECT 2367 2365 CONECT 2419 2603 CONECT 2445 2716 CONECT 2603 2419 CONECT 2716 2445 CONECT 2976 3542 CONECT 3542 2976 CONECT 3704 3705 3713 CONECT 3705 3704 3706 CONECT 3706 3705 3707 3731 CONECT 3707 3706 3708 CONECT 3708 3707 3709 3713 CONECT 3709 3708 3710 CONECT 3710 3709 3711 CONECT 3711 3710 3712 3717 CONECT 3712 3711 3713 3714 CONECT 3713 3704 3708 3712 3722 CONECT 3714 3712 3715 CONECT 3715 3714 3716 CONECT 3716 3715 3717 3720 3721 CONECT 3717 3711 3716 3718 CONECT 3718 3717 3719 CONECT 3719 3718 3720 CONECT 3720 3716 3719 3723 CONECT 3721 3716 CONECT 3722 3713 CONECT 3723 3720 3724 3725 CONECT 3724 3723 CONECT 3725 3723 3726 CONECT 3726 3725 3727 CONECT 3727 3726 3728 CONECT 3728 3727 3729 3730 CONECT 3729 3728 CONECT 3730 3728 CONECT 3731 3706 CONECT 3732 3733 3741 CONECT 3733 3732 3734 CONECT 3734 3733 3735 3759 CONECT 3735 3734 3736 CONECT 3736 3735 3737 3741 CONECT 3737 3736 3738 CONECT 3738 3737 3739 CONECT 3739 3738 3740 3745 CONECT 3740 3739 3741 3742 CONECT 3741 3732 3736 3740 3750 CONECT 3742 3740 3743 CONECT 3743 3742 3744 CONECT 3744 3743 3745 3748 3749 CONECT 3745 3739 3744 3746 CONECT 3746 3745 3747 CONECT 3747 3746 3748 CONECT 3748 3744 3747 3751 CONECT 3749 3744 CONECT 3750 3741 CONECT 3751 3748 3752 3753 CONECT 3752 3751 CONECT 3753 3751 3754 CONECT 3754 3753 3755 CONECT 3755 3754 3756 CONECT 3756 3755 3757 3758 CONECT 3757 3756 CONECT 3758 3756 CONECT 3759 3734 CONECT 3760 3761 3762 CONECT 3761 3760 3763 CONECT 3762 3760 3765 CONECT 3763 3761 3766 CONECT 3764 3775 3777 CONECT 3765 3762 3767 CONECT 3766 3763 3768 CONECT 3767 3765 CONECT 3768 3766 3769 CONECT 3769 3768 3770 CONECT 3770 3769 3771 CONECT 3771 3770 3772 CONECT 3772 3771 3774 CONECT 3773 3775 3779 CONECT 3774 3772 3776 3779 CONECT 3775 3764 3773 3778 CONECT 3776 3774 CONECT 3777 3764 CONECT 3778 3775 CONECT 3779 3773 3774 CONECT 3780 3781 3782 CONECT 3781 3780 3783 CONECT 3782 3780 3785 CONECT 3783 3781 3786 CONECT 3784 3795 3797 CONECT 3785 3782 3787 CONECT 3786 3783 3788 CONECT 3787 3785 CONECT 3788 3786 3789 CONECT 3789 3788 3790 CONECT 3790 3789 3791 CONECT 3791 3790 3792 CONECT 3792 3791 3794 CONECT 3793 3795 3799 CONECT 3794 3792 3796 3799 CONECT 3795 3784 3793 3798 CONECT 3796 3794 CONECT 3797 3784 CONECT 3798 3795 CONECT 3799 3793 3794 CONECT 3800 3801 CONECT 3801 3800 3803 CONECT 3802 3811 3813 CONECT 3803 3801 3804 CONECT 3804 3803 3805 CONECT 3805 3804 3806 CONECT 3806 3805 3807 CONECT 3807 3806 3808 CONECT 3808 3807 3810 CONECT 3809 3811 3815 CONECT 3810 3808 3812 3815 CONECT 3811 3802 3809 3814 CONECT 3812 3810 CONECT 3813 3802 CONECT 3814 3811 CONECT 3815 3809 3810 CONECT 3816 3817 3818 CONECT 3817 3816 3819 CONECT 3818 3816 3821 CONECT 3819 3817 3822 CONECT 3820 3832 3834 CONECT 3821 3818 3823 CONECT 3822 3819 3824 CONECT 3823 3821 3825 CONECT 3824 3822 3826 CONECT 3825 3823 CONECT 3826 3824 3827 CONECT 3827 3826 3828 CONECT 3828 3827 3829 CONECT 3829 3828 3831 CONECT 3830 3832 3836 CONECT 3831 3829 3833 3836 CONECT 3832 3820 3830 3835 CONECT 3833 3831 CONECT 3834 3820 CONECT 3835 3832 CONECT 3836 3830 3831 CONECT 3837 3840 CONECT 3838 3839 3841 CONECT 3839 3838 3842 CONECT 3840 3837 3844 CONECT 3841 3838 3845 CONECT 3842 3839 3846 CONECT 3843 3857 3859 CONECT 3844 3840 3847 CONECT 3845 3841 3848 CONECT 3846 3842 3849 CONECT 3847 3844 3850 CONECT 3848 3845 3850 CONECT 3849 3846 3851 CONECT 3850 3847 3848 CONECT 3851 3849 3852 CONECT 3852 3851 3853 CONECT 3853 3852 3854 CONECT 3854 3853 3856 CONECT 3855 3857 3861 CONECT 3856 3854 3858 3861 CONECT 3857 3843 3855 3860 CONECT 3858 3856 CONECT 3859 3843 CONECT 3860 3857 CONECT 3861 3855 3856 CONECT 3862 3871 3873 CONECT 3863 3864 CONECT 3864 3863 3865 CONECT 3865 3864 3866 CONECT 3866 3865 3867 CONECT 3867 3866 3868 CONECT 3868 3867 3870 CONECT 3869 3871 3875 CONECT 3870 3868 3872 3875 CONECT 3871 3862 3869 3874 CONECT 3872 3870 CONECT 3873 3862 CONECT 3874 3871 CONECT 3875 3869 3870 CONECT 3951 3952 3953 3954 CONECT 3952 3951 CONECT 3953 3951 CONECT 3954 3951 3955 CONECT 3955 3954 3956 CONECT 3956 3955 3957 3958 CONECT 3957 3956 CONECT 3958 3956 MASTER 670 0 17 15 21 0 14 6 3978 3 199 46 END