Browse entries in the PDBbind-CN Database
HEADER LIGASE 07-OCT-11 4A49 TITLE STRUCTURE OF PHOSPHOTYR371-C-CBL-UBCH5B COMPLEX COMPND MOL_ID: 1; COMPND 2 MOLECULE: E3 UBIQUITIN-PROTEIN LIGASE CBL; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: C-CBL RESIDUES 354-435; COMPND 5 SYNONYM: CASITAS B-LINEAGE LYMPHOMA PROTO-ONCOGENE,PROTO-ONCOGENE C- COMPND 6 CBL,RING FINGER PROTEIN 55,RING-TYPE E3 UBIQUITIN TRANSFERASE CBL, COMPND 7 SIGNAL TRANSDUCTION PROTEIN CBL; COMPND 8 EC: 2.3.2.27; COMPND 9 ENGINEERED: YES; COMPND 10 MUTATION: YES; COMPND 11 OTHER_DETAILS: TYR371 IS PHOSPHORYLATED; COMPND 12 MOL_ID: 2; COMPND 13 MOLECULE: UBIQUITIN-CONJUGATING ENZYME E2 D2; COMPND 14 CHAIN: B; COMPND 15 SYNONYM: (E3-INDEPENDENT) E2 UBIQUITIN-CONJUGATING ENZYME D2,E2 COMPND 16 UBIQUITIN-CONJUGATING ENZYME D2,UBIQUITIN CARRIER PROTEIN D2, COMPND 17 UBIQUITIN-CONJUGATING ENZYME E2(17)KB 2,UBIQUITIN-CONJUGATING ENZYME COMPND 18 E2-17 KDA 2,UBIQUITIN-PROTEIN LIGASE D2,P53-REGULATED UBIQUITIN- COMPND 19 CONJUGATING ENZYME 1; COMPND 20 EC: 2.3.2.23,2.3.2.24; COMPND 21 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: CBL, CBL2, RNF55; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 10 ORGANISM_COMMON: HUMAN; SOURCE 11 ORGANISM_TAXID: 9606; SOURCE 12 GENE: UBE2D2, PUBC1, UBC4, UBC5B, UBCH4, UBCH5B; SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 14 EXPRESSION_SYSTEM_TAXID: 469008 KEYWDS LIGASE EXPDTA X-RAY DIFFRACTION AUTHOR H.DOU,L.BUETOW,A.HOCK,G.J.SIBBET,K.H.VOUSDEN,D.T.HUANG REVDAT 3 21-NOV-18 4A49 1 COMPND SOURCE JRNL REMARK REVDAT 3 2 1 DBREF ATOM REVDAT 2 29-FEB-12 4A49 1 JRNL REVDAT 1 25-JAN-12 4A49 0 JRNL AUTH H.DOU,L.BUETOW,A.HOCK,G.J.SIBBET,K.H.VOUSDEN,D.T.HUANG JRNL TITL STRUCTURAL BASIS FOR AUTOINHIBITION AND JRNL TITL 2 PHOSPHORYLATION-DEPENDENT ACTIVATION OF C-CBL. JRNL REF NAT. STRUCT. MOL. BIOL. V. 19 184 2012 JRNL REFN ESSN 1545-9985 JRNL PMID 22266821 JRNL DOI 10.1038/NSMB.2231 REMARK 2 REMARK 2 RESOLUTION. 2.21 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE) 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) : 2.21 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.30 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6 REMARK 3 NUMBER OF REFLECTIONS : 20424 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.170 REMARK 3 R VALUE (WORKING SET) : 0.168 REMARK 3 FREE R VALUE : 0.206 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100 REMARK 3 FREE R VALUE TEST SET COUNT : 1045 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 36.3022 - 4.2336 0.97 2814 137 0.1472 0.1745 REMARK 3 2 4.2336 - 3.3611 1.00 2797 152 0.1462 0.1766 REMARK 3 3 3.3611 - 2.9364 1.00 2773 147 0.1777 0.2346 REMARK 3 4 2.9364 - 2.6681 1.00 2766 148 0.1886 0.2317 REMARK 3 5 2.6681 - 2.4769 1.00 2754 131 0.2050 0.2207 REMARK 3 6 2.4769 - 2.3309 1.00 2727 164 0.2297 0.2857 REMARK 3 7 2.3309 - 2.2141 1.00 2748 166 0.2483 0.3027 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.10 REMARK 3 SHRINKAGE RADIUS : 0.83 REMARK 3 K_SOL : 0.31 REMARK 3 B_SOL : 45.77 REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.570 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.670 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 44.92 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 53.60 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 3.47770 REMARK 3 B22 (A**2) : 3.47770 REMARK 3 B33 (A**2) : -6.95540 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.008 1876 REMARK 3 ANGLE : 1.185 2559 REMARK 3 CHIRALITY : 0.095 273 REMARK 3 PLANARITY : 0.007 336 REMARK 3 DIHEDRAL : 13.764 718 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 15 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN A AND (RESSEQ 359:364) REMARK 3 ORIGIN FOR THE GROUP (A): 41.1821 -50.1133 -28.6102 REMARK 3 T TENSOR REMARK 3 T11: 0.5910 T22: 0.8916 REMARK 3 T33: 0.8482 T12: 0.0888 REMARK 3 T13: 0.1000 T23: -0.3282 REMARK 3 L TENSOR REMARK 3 L11: 2.3917 L22: 3.3741 REMARK 3 L33: 3.6118 L12: -0.6696 REMARK 3 L13: 1.5387 L23: -3.3213 REMARK 3 S TENSOR REMARK 3 S11: 0.1481 S12: 0.8680 S13: -0.0517 REMARK 3 S21: -0.7214 S22: -0.0541 S23: -0.4789 REMARK 3 S31: 0.5761 S32: 0.3215 S33: 0.0504 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN A AND (RESSEQ 365:373) REMARK 3 ORIGIN FOR THE GROUP (A): 39.2836 -52.8763 -15.3071 REMARK 3 T TENSOR REMARK 3 T11: 0.3138 T22: 0.4473 REMARK 3 T33: 0.7139 T12: -0.0028 REMARK 3 T13: -0.0186 T23: -0.0294 REMARK 3 L TENSOR REMARK 3 L11: 6.8057 L22: 3.0277 REMARK 3 L33: 6.9377 L12: -0.2329 REMARK 3 L13: -1.9290 L23: 2.1534 REMARK 3 S TENSOR REMARK 3 S11: -0.1460 S12: 0.2623 S13: -1.1689 REMARK 3 S21: 0.2013 S22: -0.1566 S23: 0.4536 REMARK 3 S31: 0.7178 S32: -0.2105 S33: 0.2786 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN A AND (RESSEQ 374:394) REMARK 3 ORIGIN FOR THE GROUP (A): 35.7505 -40.9603 -21.3664 REMARK 3 T TENSOR REMARK 3 T11: 0.2929 T22: 0.5521 REMARK 3 T33: 0.3446 T12: -0.0422 REMARK 3 T13: 0.0022 T23: -0.0805 REMARK 3 L TENSOR REMARK 3 L11: 3.2804 L22: 5.7584 REMARK 3 L33: 4.6355 L12: 0.6288 REMARK 3 L13: -0.2294 L23: -0.7340 REMARK 3 S TENSOR REMARK 3 S11: -0.0576 S12: 0.7977 S13: -0.5200 REMARK 3 S21: -0.4089 S22: -0.0138 S23: 0.0245 REMARK 3 S31: 0.0692 S32: 0.3612 S33: 0.0338 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN A AND (RESSEQ 395:401) REMARK 3 ORIGIN FOR THE GROUP (A): 43.7655 -36.7188 -23.4430 REMARK 3 T TENSOR REMARK 3 T11: 0.3217 T22: 0.7117 REMARK 3 T33: 0.4609 T12: -0.0896 REMARK 3 T13: 0.0470 T23: 0.0271 REMARK 3 L TENSOR REMARK 3 L11: 3.8192 L22: 1.8172 REMARK 3 L33: 0.7694 L12: -0.0478 REMARK 3 L13: -0.0218 L23: 0.6366 REMARK 3 S TENSOR REMARK 3 S11: -0.4983 S12: 0.4828 S13: -0.0120 REMARK 3 S21: -0.1837 S22: 0.4412 S23: -0.4096 REMARK 3 S31: -0.2685 S32: 0.7001 S33: 0.0699 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN A AND (RESSEQ 402:410) REMARK 3 ORIGIN FOR THE GROUP (A): 35.7007 -27.8773 -24.4576 REMARK 3 T TENSOR REMARK 3 T11: 0.6278 T22: 0.6336 REMARK 3 T33: 0.3924 T12: -0.1513 REMARK 3 T13: -0.0284 T23: 0.1286 REMARK 3 L TENSOR REMARK 3 L11: 7.6722 L22: 4.8148 REMARK 3 L33: 3.7658 L12: 4.7858 REMARK 3 L13: 2.8264 L23: 3.9952 REMARK 3 S TENSOR REMARK 3 S11: -0.3074 S12: 1.0465 S13: 0.7900 REMARK 3 S21: -1.2013 S22: 0.3823 S23: 0.3509 REMARK 3 S31: -1.1002 S32: 0.8083 S33: -0.1915 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN A AND (RESSEQ 411:424) REMARK 3 ORIGIN FOR THE GROUP (A): 45.0416 -27.3027 -20.9851 REMARK 3 T TENSOR REMARK 3 T11: 0.4636 T22: 0.8496 REMARK 3 T33: 0.4938 T12: -0.2777 REMARK 3 T13: 0.0642 T23: -0.0483 REMARK 3 L TENSOR REMARK 3 L11: 6.3620 L22: 5.9765 REMARK 3 L33: 6.6800 L12: -1.9638 REMARK 3 L13: -1.3395 L23: 0.3802 REMARK 3 S TENSOR REMARK 3 S11: 0.2800 S12: -0.1832 S13: 1.2508 REMARK 3 S21: -0.5287 S22: 0.1491 S23: -0.6665 REMARK 3 S31: -0.7017 S32: 1.7075 S33: -0.4015 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN A AND (RESSEQ 425:435) REMARK 3 ORIGIN FOR THE GROUP (A): 38.8810 -45.7955 -28.6155 REMARK 3 T TENSOR REMARK 3 T11: 0.4826 T22: 0.8613 REMARK 3 T33: 0.4752 T12: -0.1099 REMARK 3 T13: 0.0803 T23: -0.1946 REMARK 3 L TENSOR REMARK 3 L11: 2.3663 L22: 7.8556 REMARK 3 L33: 5.9466 L12: -3.4566 REMARK 3 L13: 2.7561 L23: -1.2493 REMARK 3 S TENSOR REMARK 3 S11: -0.1929 S12: 1.2987 S13: -0.6551 REMARK 3 S21: -1.3165 S22: 0.2740 S23: 0.0229 REMARK 3 S31: 0.4358 S32: -0.0892 S33: 0.0092 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN B AND (RESSEQ 2:28) REMARK 3 ORIGIN FOR THE GROUP (A): 30.2163 -38.7265 -4.7373 REMARK 3 T TENSOR REMARK 3 T11: 0.2807 T22: 0.4325 REMARK 3 T33: 0.3573 T12: -0.0679 REMARK 3 T13: -0.0582 T23: -0.0045 REMARK 3 L TENSOR REMARK 3 L11: 2.9514 L22: 5.4514 REMARK 3 L33: 4.8614 L12: 0.3043 REMARK 3 L13: -0.6538 L23: 0.3009 REMARK 3 S TENSOR REMARK 3 S11: -0.0599 S12: -0.2260 S13: -0.0562 REMARK 3 S21: 0.2340 S22: -0.0814 S23: -0.3963 REMARK 3 S31: 0.2031 S32: 0.4621 S33: 0.1252 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN B AND (RESSEQ 29:38) REMARK 3 ORIGIN FOR THE GROUP (A): 27.8672 -31.2185 -0.1020 REMARK 3 T TENSOR REMARK 3 T11: 0.2930 T22: 0.3523 REMARK 3 T33: 0.4118 T12: -0.0941 REMARK 3 T13: 0.0013 T23: -0.0114 REMARK 3 L TENSOR REMARK 3 L11: 3.7595 L22: 4.1320 REMARK 3 L33: 7.7109 L12: 0.0003 REMARK 3 L13: 5.3413 L23: 0.6384 REMARK 3 S TENSOR REMARK 3 S11: 0.1956 S12: -0.8114 S13: -0.2277 REMARK 3 S21: 0.3266 S22: -0.3375 S23: 0.1564 REMARK 3 S31: 0.0823 S32: -0.4662 S33: 0.1237 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN B AND (RESSEQ 39:55) REMARK 3 ORIGIN FOR THE GROUP (A): 38.5591 -29.7541 8.5432 REMARK 3 T TENSOR REMARK 3 T11: 0.3762 T22: 0.4179 REMARK 3 T33: 0.4282 T12: -0.2030 REMARK 3 T13: -0.0229 T23: -0.0042 REMARK 3 L TENSOR REMARK 3 L11: 4.9941 L22: 3.2592 REMARK 3 L33: 7.5258 L12: 0.4697 REMARK 3 L13: 2.6384 L23: -1.1766 REMARK 3 S TENSOR REMARK 3 S11: 0.0786 S12: -0.6226 S13: -0.4478 REMARK 3 S21: 0.4902 S22: -0.1506 S23: -0.0890 REMARK 3 S31: 0.0309 S32: 0.2070 S33: 0.0505 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN B AND (RESSEQ 56:74) REMARK 3 ORIGIN FOR THE GROUP (A): 33.3934 -24.5606 -3.3945 REMARK 3 T TENSOR REMARK 3 T11: 0.2815 T22: 0.3281 REMARK 3 T33: 0.3559 T12: -0.0889 REMARK 3 T13: -0.0035 T23: -0.0164 REMARK 3 L TENSOR REMARK 3 L11: 4.2893 L22: 2.0430 REMARK 3 L33: 3.8197 L12: 1.5514 REMARK 3 L13: 2.2786 L23: 0.9050 REMARK 3 S TENSOR REMARK 3 S11: -0.1231 S12: -0.1890 S13: 0.7475 REMARK 3 S21: -0.1168 S22: -0.0963 S23: 0.1621 REMARK 3 S31: -0.6748 S32: 0.2113 S33: 0.3420 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: CHAIN B AND (RESSEQ 75:84) REMARK 3 ORIGIN FOR THE GROUP (A): 39.7996 -18.6255 4.9878 REMARK 3 T TENSOR REMARK 3 T11: 0.3842 T22: 0.3764 REMARK 3 T33: 0.5380 T12: -0.0903 REMARK 3 T13: -0.0331 T23: -0.0630 REMARK 3 L TENSOR REMARK 3 L11: 4.3834 L22: 3.6542 REMARK 3 L33: 5.4135 L12: 2.8364 REMARK 3 L13: 0.2080 L23: 1.1110 REMARK 3 S TENSOR REMARK 3 S11: 0.0347 S12: -0.1454 S13: 0.9777 REMARK 3 S21: 0.1961 S22: 0.1726 S23: -0.0669 REMARK 3 S31: -0.7073 S32: 0.3120 S33: -0.1868 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: CHAIN B AND (RESSEQ 85:98) REMARK 3 ORIGIN FOR THE GROUP (A): 41.3748 -25.7887 -9.0010 REMARK 3 T TENSOR REMARK 3 T11: 0.3333 T22: 0.5151 REMARK 3 T33: 0.3824 T12: -0.1303 REMARK 3 T13: -0.0019 T23: 0.0251 REMARK 3 L TENSOR REMARK 3 L11: 4.6182 L22: 1.4307 REMARK 3 L33: 9.6612 L12: -0.7305 REMARK 3 L13: 0.6040 L23: 0.5121 REMARK 3 S TENSOR REMARK 3 S11: -0.2453 S12: 0.5768 S13: 0.1145 REMARK 3 S21: -0.7163 S22: 0.1543 S23: -0.7890 REMARK 3 S31: -1.0641 S32: 0.6197 S33: 0.1138 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: CHAIN B AND (RESSEQ 99:120) REMARK 3 ORIGIN FOR THE GROUP (A): 45.1213 -26.0400 1.3107 REMARK 3 T TENSOR REMARK 3 T11: 0.3308 T22: 0.4241 REMARK 3 T33: 0.4533 T12: -0.1023 REMARK 3 T13: -0.0324 T23: 0.0093 REMARK 3 L TENSOR REMARK 3 L11: 4.8923 L22: 5.0965 REMARK 3 L33: 2.6368 L12: 1.9868 REMARK 3 L13: 2.1366 L23: 1.8522 REMARK 3 S TENSOR REMARK 3 S11: -0.0147 S12: 0.1995 S13: -0.1092 REMARK 3 S21: -0.0055 S22: 0.1168 S23: -1.0009 REMARK 3 S31: -0.1964 S32: 0.3175 S33: -0.0941 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: CHAIN B AND (RESSEQ 121:147) REMARK 3 ORIGIN FOR THE GROUP (A): 47.3122 -20.3176 15.5586 REMARK 3 T TENSOR REMARK 3 T11: 0.5029 T22: 0.7138 REMARK 3 T33: 0.4485 T12: -0.2532 REMARK 3 T13: -0.0861 T23: -0.0396 REMARK 3 L TENSOR REMARK 3 L11: 3.1529 L22: 2.5032 REMARK 3 L33: 3.1543 L12: 1.2108 REMARK 3 L13: 0.0434 L23: -1.1940 REMARK 3 S TENSOR REMARK 3 S11: 0.7522 S12: -1.2742 S13: 0.1958 REMARK 3 S21: 0.8745 S22: -0.6022 S23: -0.1974 REMARK 3 S31: -0.3749 S32: 0.2715 S33: -0.1136 REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: CHAIN A RESIDUE 354-358 AND CHAIN B REMARK 3 RESIDUE 1 ARE DISORDERED. REMARK 4 REMARK 4 4A49 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 07-OCT-11. REMARK 100 THE DEPOSITION ID IS D_1290049936. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 19-SEP-11 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : DIAMOND REMARK 200 BEAMLINE : I02 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM REMARK 200 DATA SCALING SOFTWARE : SCALA REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20424 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.210 REMARK 200 RESOLUTION RANGE LOW (A) : 40.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6 REMARK 200 DATA REDUNDANCY : 6.000 REMARK 200 R MERGE (I) : 0.08000 REMARK 200 R SYM (I) : NULL REMARK 200
FOR THE DATA SET : 11.6000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.21 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.27 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 REMARK 200 DATA REDUNDANCY IN SHELL : 6.10 REMARK 200 R MERGE FOR SHELL (I) : 0.64000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200
FOR SHELL : 2.800 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: PDB ENTRIES 2ESK AND 1FBV REMARK 200 REMARK 200 REMARK: NONE REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 67.00 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.80 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 20% (W/V) PEG 3350 AND 0.2 M POTASSIUM REMARK 280 THIOCYANATE AT 18 DEGREES CELSIUS., TEMPERATURE 291K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z+2/3 REMARK 290 3555 -X+Y,-X,Z+1/3 REMARK 290 4555 Y,X,-Z REMARK 290 5555 X-Y,-Y,-Z+1/3 REMARK 290 6555 -X,-X+Y,-Z+2/3 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 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 35.04800 REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 17.52400 REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 4 0.866025 0.500000 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 0.00000 REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 17.52400 REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 35.04800 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 1360 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 11610 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.1 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 375 REMARK 375 SPECIAL POSITION REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL REMARK 375 POSITIONS. REMARK 375 REMARK 375 ATOM RES CSSEQI REMARK 375 K K B1148 LIES ON A SPECIAL POSITION. REMARK 400 REMARK 400 COMPOUND REMARK 400 ENGINEERED RESIDUE IN CHAIN A, TYR 368 TO PHE 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 GLY A 352 REMARK 465 SER A 353 REMARK 465 GLU A 354 REMARK 465 PRO A 355 REMARK 465 THR A 356 REMARK 465 PRO A 357 REMARK 465 GLN A 358 REMARK 465 MET B 1 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 GLU A 386 -61.84 -128.29 REMARK 500 GLU A 386 -62.99 -127.70 REMARK 500 GLU A 412 -1.22 84.41 REMARK 500 PRO B 61 39.99 -93.33 REMARK 500 HIS B 75 137.42 -173.88 REMARK 500 ARG B 90 -84.81 -125.86 REMARK 500 ASN B 114 79.24 -115.16 REMARK 500 THR B 129 -61.54 -104.76 REMARK 500 REMARK 500 REMARK: NULL REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN A1436 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A 384 SG REMARK 620 2 CYS A 381 SG 108.4 REMARK 620 3 CYS A 401 SG 109.7 116.2 REMARK 620 4 CYS A 404 SG 105.0 115.5 101.3 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN A1437 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A 396 SG REMARK 620 2 CYS A 416 SG 110.3 REMARK 620 3 CYS A 419 SG 108.2 113.1 REMARK 620 4 HIS A 398 ND1 84.7 121.7 114.3 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 K B1148 K REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS B 7 ND1 REMARK 620 2 HIS B 7 ND1 89.9 REMARK 620 N 1 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1436 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1437 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K B 1148 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 2CBL RELATED DB: PDB REMARK 900 N-TERMINAL DOMAIN OF CBL IN COMPLEX WITH ITS BINDING SITE ON ZAP-70 REMARK 900 RELATED ID: 2Y1N RELATED DB: PDB REMARK 900 STRUCTURAL BASIS FOR AUTOINHIBITION AND PHOSPHORYLATION- REMARK 900 DEPENDENTACTIVATION OF C-CBL: C-CBL-ZAP-70 PEPTIDE COMPLEX. REMARK 900 RELATED ID: 1W4U RELATED DB: PDB REMARK 900 NMR SOLUTION STRUCTURE OF THE UBIQUITIN CONJUGATING ENZYME UBCH5B REMARK 900 RELATED ID: 4A4B RELATED DB: PDB REMARK 900 STRUCTURE OF MODIFIED PHOSPHOTYR371-C-CBL-UBCH5B-ZAP- 70 COMPLEX REMARK 900 RELATED ID: 2ESQ RELATED DB: PDB REMARK 900 HUMAN UBIQUITIN-CONJUGATING ENZYME (E2) UBCH5B MUTANTSER94GLY REMARK 900 RELATED ID: 2C4O RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF HUMAN UBIQUITIN-CONJUGATING ENZYME UBCH5B REMARK 900 RELATED ID: 4A4C RELATED DB: PDB REMARK 900 STRUCTURE OF PHOSPHOTYR371-C-CBL-UBCH5B-ZAP-70 COMPLEX REMARK 900 RELATED ID: 2ESK RELATED DB: PDB REMARK 900 HUMAN UBIQUITIN-CONJUGATING ENZYME (E2) UBCH5B, WILD- TYPE REMARK 900 RELATED ID: 1UR6 RELATED DB: PDB REMARK 900 NMR BASED STRUCTURAL MODEL OF THE UBCH5B-CNOT4 COMPLEX REMARK 900 RELATED ID: 2Y1M RELATED DB: PDB REMARK 900 STRUCTURAL BASIS FOR AUTOINHIBITION AND PHOSPHORYLATION- REMARK 900 DEPENDENTACTIVATION OF C-CBL: NATIVE C-CBL. REMARK 900 RELATED ID: 1B47 RELATED DB: PDB REMARK 900 STRUCTURE OF THE N-TERMINAL DOMAIN OF CBL IN COMPLEX WITH ITS REMARK 900 BINDING SITE IN ZAP-70 REMARK 900 RELATED ID: 1FBV RELATED DB: PDB REMARK 900 STRUCTURE OF A CBL-UBCH7 COMPLEX: RING DOMAIN FUNCTION INUBIQUITIN- REMARK 900 PROTEIN LIGASES REMARK 900 RELATED ID: 2ESO RELATED DB: PDB REMARK 900 HUMAN UBIQUITIN-CONJUGATING ENZYME (E2) UBCH5B MUTANTILE37ALA REMARK 900 RELATED ID: 1YVH RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF THE C-CBL TKB DOMAIN IN COMPLEX WITHTHE APS REMARK 900 PTYR-618 PHOSPHOPEPTIDE REMARK 900 RELATED ID: 2ESP RELATED DB: PDB REMARK 900 HUMAN UBIQUITIN-CONJUGATING ENZYME (E2) UBCH5B MUTANTILE88ALA REMARK 900 RELATED ID: 2CLW RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF HUMAN UBIQUITIN-CONJUGATING ENZYME UBCH5B REMARK 999 REMARK 999 SEQUENCE REMARK 999 Y368 IS MUTATED TO PHE. Y371 IS PHOSPHORYLATED. N-TERMINAL REMARK 999 GS IS RESULTED FROM CLONING AND TEV CLEAVAGE. DBREF 4A49 A 354 435 UNP P22681 CBL_HUMAN 354 435 DBREF 4A49 B 1 147 UNP P62837 UB2D2_HUMAN 1 147 SEQADV 4A49 GLY A 352 UNP P22681 EXPRESSION TAG SEQADV 4A49 SER A 353 UNP P22681 EXPRESSION TAG SEQADV 4A49 PHE A 368 UNP P22681 TYR 368 ENGINEERED MUTATION SEQRES 1 A 84 GLY SER GLU PRO THR PRO GLN ASP HIS ILE LYS VAL THR SEQRES 2 A 84 GLN GLU GLN PHE GLU LEU PTR CYS GLU MET GLY SER THR SEQRES 3 A 84 PHE GLN LEU CYS LYS ILE CYS ALA GLU ASN ASP LYS ASP SEQRES 4 A 84 VAL LYS ILE GLU PRO CYS GLY HIS LEU MET CYS THR SER SEQRES 5 A 84 CYS LEU THR SER TRP GLN GLU SER GLU GLY GLN GLY CYS SEQRES 6 A 84 PRO PHE CYS ARG CYS GLU ILE LYS GLY THR GLU PRO ILE SEQRES 7 A 84 VAL VAL ASP PRO PHE ASP SEQRES 1 B 147 MET ALA LEU LYS ARG ILE HIS LYS GLU LEU ASN ASP LEU SEQRES 2 B 147 ALA ARG ASP PRO PRO ALA GLN CYS SER ALA GLY PRO VAL SEQRES 3 B 147 GLY ASP ASP MET PHE HIS TRP GLN ALA THR ILE MET GLY SEQRES 4 B 147 PRO ASN ASP SER PRO TYR GLN GLY GLY VAL PHE PHE LEU SEQRES 5 B 147 THR ILE HIS PHE PRO THR ASP TYR PRO PHE LYS PRO PRO SEQRES 6 B 147 LYS VAL ALA PHE THR THR ARG ILE TYR HIS PRO ASN ILE SEQRES 7 B 147 ASN SER ASN GLY SER ILE CYS LEU ASP ILE LEU ARG SER SEQRES 8 B 147 GLN TRP SER PRO ALA LEU THR ILE SER LYS VAL LEU LEU SEQRES 9 B 147 SER ILE CYS SER LEU LEU CYS ASP PRO ASN PRO ASP ASP SEQRES 10 B 147 PRO LEU VAL PRO GLU ILE ALA ARG ILE TYR LYS THR ASP SEQRES 11 B 147 ARG GLU LYS TYR ASN ARG ILE ALA ARG GLU TRP THR GLN SEQRES 12 B 147 LYS TYR ALA MET MODRES 4A49 PTR A 371 TYR MODIFIED RESIDUE HET PTR A 371 16 HET ZN A1436 1 HET ZN A1437 1 HET K B1148 1 HETNAM PTR O-PHOSPHOTYROSINE HETNAM ZN ZINC ION HETNAM K POTASSIUM ION HETSYN PTR PHOSPHONOTYROSINE FORMUL 1 PTR C9 H12 N O6 P FORMUL 3 ZN 2(ZN 2+) FORMUL 5 K K 1+ FORMUL 6 HOH *132(H2 O) HELIX 1 1 THR A 364 MET A 374 1 11 HELIX 2 2 CYS A 401 SER A 411 1 11 HELIX 3 3 ALA B 2 ASP B 16 1 15 HELIX 4 4 LEU B 86 ARG B 90 5 5 HELIX 5 5 THR B 98 ASP B 112 1 15 HELIX 6 6 VAL B 120 ASP B 130 1 11 HELIX 7 7 ASP B 130 ALA B 146 1 17 SHEET 1 AA 2 HIS A 360 LYS A 362 0 SHEET 2 AA 2 VAL A 430 ASP A 432 1 O VAL A 430 N ILE A 361 SHEET 1 AB 3 LEU A 399 MET A 400 0 SHEET 2 AB 3 VAL A 391 GLU A 394 -1 O VAL A 391 N MET A 400 SHEET 3 AB 3 GLY A 425 PRO A 428 -1 O GLY A 425 N GLU A 394 SHEET 1 BA 4 CYS B 21 VAL B 26 0 SHEET 2 BA 4 ASP B 29 MET B 38 -1 N ASP B 29 O VAL B 26 SHEET 3 BA 4 VAL B 49 HIS B 55 -1 O PHE B 50 N ILE B 37 SHEET 4 BA 4 LYS B 66 PHE B 69 -1 O LYS B 66 N HIS B 55 LINK C LEU A 370 N PTR A 371 1555 1555 1.33 LINK C PTR A 371 N CYS A 372 1555 1555 1.33 LINK ZN ZN A1436 SG CYS A 384 1555 1555 2.35 LINK ZN ZN A1436 SG CYS A 381 1555 1555 2.36 LINK ZN ZN A1436 SG CYS A 401 1555 1555 2.52 LINK ZN ZN A1436 SG CYS A 404 1555 1555 2.25 LINK ZN ZN A1437 SG CYS A 396 1555 1555 2.49 LINK ZN ZN A1437 SG CYS A 416 1555 1555 2.34 LINK ZN ZN A1437 SG CYS A 419 1555 1555 2.43 LINK ZN ZN A1437 ND1 HIS A 398 1555 1555 2.02 LINK K K B1148 ND1 HIS B 7 1555 6554 2.52 LINK K K B1148 ND1 HIS B 7 1555 1555 2.52 CISPEP 1 GLU A 394 PRO A 395 0 -4.51 CISPEP 2 TYR B 60 PRO B 61 0 -2.26 SITE 1 AC1 4 CYS A 381 CYS A 384 CYS A 401 CYS A 404 SITE 1 AC2 4 CYS A 396 HIS A 398 CYS A 416 CYS A 419 SITE 1 AC3 1 HIS B 7 CRYST1 115.877 115.877 52.572 90.00 90.00 120.00 P 32 2 1 6 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 0.008630 0.004982 0.000000 0.00000 SCALE2 0.000000 0.009965 0.000000 0.00000 SCALE3 0.000000 0.000000 0.019022 0.00000 ATOM 1 N ASP A 359 41.980 -44.839 -35.812 1.00110.93 N ANISOU 1 N ASP A 359 11747 16640 13760 866 1889 -2239 N ATOM 2 CA ASP A 359 42.753 -45.520 -34.777 1.00116.15 C ANISOU 2 CA ASP A 359 12362 17129 14643 969 1893 -2368 C ATOM 3 C ASP A 359 41.843 -46.089 -33.684 1.00109.54 C ANISOU 3 C ASP A 359 11677 16021 13922 869 1650 -2551 C ATOM 4 O ASP A 359 41.156 -45.345 -32.980 1.00100.60 O ANISOU 4 O ASP A 359 10481 14780 12962 714 1499 -2448 O ATOM 5 CB ASP A 359 43.795 -44.571 -34.168 1.00122.46 C ANISOU 5 CB ASP A 359 12828 17930 15772 942 1949 -2120 C ATOM 6 CG ASP A 359 44.642 -45.237 -33.084 1.00122.55 C ANISOU 6 CG ASP A 359 12769 17770 16024 1030 1937 -2218 C ATOM 7 OD1 ASP A 359 44.767 -46.483 -33.095 1.00124.10 O ANISOU 7 OD1 ASP A 359 13134 17918 16099 1187 1984 -2455 O ATOM 8 OD2 ASP A 359 45.191 -44.510 -32.224 1.00116.34 O ANISOU 8 OD2 ASP A 359 11776 16881 15549 935 1859 -2049 O ATOM 9 N HIS A 360 41.850 -47.413 -33.551 1.00106.25 N ANISOU 9 N HIS A 360 11468 15498 13405 979 1619 -2806 N ATOM 10 CA HIS A 360 41.004 -48.099 -32.579 1.00 94.57 C ANISOU 10 CA HIS A 360 10126 13784 12021 889 1388 -2956 C ATOM 11 C HIS A 360 41.778 -48.589 -31.359 1.00 90.93 C ANISOU 11 C HIS A 360 9570 13147 11834 962 1374 -3039 C ATOM 12 O HIS A 360 42.834 -49.212 -31.484 1.00 91.99 O ANISOU 12 O HIS A 360 9683 13297 11971 1141 1521 -3120 O ATOM 13 CB HIS A 360 40.269 -49.269 -33.236 1.00 94.92 C ANISOU 13 CB HIS A 360 10503 13790 11773 903 1276 -3165 C ATOM 14 CG HIS A 360 39.029 -48.866 -33.972 1.00 96.20 C ANISOU 14 CG HIS A 360 10775 14040 11736 731 1144 -3067 C ATOM 15 ND1 HIS A 360 37.767 -49.240 -33.564 1.00 94.41 N ANISOU 15 ND1 HIS A 360 10663 13691 11517 562 882 -3070 N ATOM 16 CD2 HIS A 360 38.857 -48.115 -35.086 1.00 97.19 C ANISOU 16 CD2 HIS A 360 10889 14379 11660 694 1233 -2925 C ATOM 17 CE1 HIS A 360 36.870 -48.741 -34.396 1.00 94.86 C ANISOU 17 CE1 HIS A 360 10773 13877 11394 425 809 -2929 C ATOM 18 NE2 HIS A 360 37.506 -48.055 -35.329 1.00 97.45 N ANISOU 18 NE2 HIS A 360 11037 14404 11587 501 1016 -2854 N ATOM 19 N ILE A 361 41.230 -48.302 -30.182 1.00 82.43 N ANISOU 19 N ILE A 361 8437 11909 10973 838 1204 -3001 N ATOM 20 CA ILE A 361 41.812 -48.723 -28.918 1.00 79.05 C ANISOU 20 CA ILE A 361 7935 11301 10798 875 1148 -3067 C ATOM 21 C ILE A 361 40.890 -49.745 -28.264 1.00 73.97 C ANISOU 21 C ILE A 361 7468 10495 10141 829 951 -3222 C ATOM 22 O ILE A 361 39.719 -49.451 -28.023 1.00 70.59 O ANISOU 22 O ILE A 361 7086 10049 9687 705 810 -3151 O ATOM 23 CB ILE A 361 41.956 -47.516 -27.972 1.00 84.15 C ANISOU 23 CB ILE A 361 8403 11878 11691 779 1093 -2886 C ATOM 24 CG1 ILE A 361 42.780 -46.415 -28.642 1.00 85.95 C ANISOU 24 CG1 ILE A 361 8445 12256 11954 777 1237 -2679 C ATOM 25 CG2 ILE A 361 42.570 -47.935 -26.642 1.00 83.55 C ANISOU 25 CG2 ILE A 361 8272 11617 11858 803 1012 -2948 C ATOM 26 CD1 ILE A 361 42.971 -45.191 -27.785 1.00 82.80 C ANISOU 26 CD1 ILE A 361 7922 11748 11792 671 1138 -2501 C ATOM 27 N LYS A 362 41.402 -50.941 -27.979 1.00 72.76 N ANISOU 27 N LYS A 362 7397 10231 10017 933 938 -3401 N ATOM 28 CA LYS A 362 40.584 -51.973 -27.334 1.00 71.26 C ANISOU 28 CA LYS A 362 7360 9876 9839 875 724 -3521 C ATOM 29 C LYS A 362 40.839 -52.077 -25.834 1.00 63.63 C ANISOU 29 C LYS A 362 6272 8758 9147 858 637 -3507 C ATOM 30 O LYS A 362 41.970 -52.257 -25.404 1.00 62.60 O ANISOU 30 O LYS A 362 6036 8577 9170 956 724 -3540 O ATOM 31 CB LYS A 362 40.812 -53.341 -27.976 1.00 79.19 C ANISOU 31 CB LYS A 362 8597 10809 10681 990 709 -3741 C ATOM 32 CG LYS A 362 40.106 -53.541 -29.299 1.00 90.79 C ANISOU 32 CG LYS A 362 10306 12364 11827 960 672 -3790 C ATOM 33 CD LYS A 362 41.016 -53.221 -30.478 1.00 94.82 C ANISOU 33 CD LYS A 362 10830 13051 12148 1137 938 -3809 C ATOM 34 CE LYS A 362 40.809 -54.223 -31.602 1.00 97.16 C ANISOU 34 CE LYS A 362 11496 13316 12103 1234 898 -4013 C ATOM 35 NZ LYS A 362 39.361 -54.402 -31.896 1.00 97.74 N ANISOU 35 NZ LYS A 362 11770 13338 12026 1003 608 -3994 N ATOM 36 N VAL A 363 39.782 -51.970 -25.040 1.00 66.76 N ANISOU 36 N VAL A 363 6676 9096 9594 742 469 -3431 N ATOM 37 CA VAL A 363 39.890 -52.140 -23.593 1.00 63.26 C ANISOU 37 CA VAL A 363 6155 8516 9363 735 374 -3419 C ATOM 38 C VAL A 363 40.476 -53.518 -23.287 1.00 64.38 C ANISOU 38 C VAL A 363 6359 8524 9577 805 319 -3589 C ATOM 39 O VAL A 363 40.004 -54.515 -23.825 1.00 57.80 O ANISOU 39 O VAL A 363 5692 7649 8620 796 223 -3695 O ATOM 40 CB VAL A 363 38.505 -52.040 -22.937 1.00 54.55 C ANISOU 40 CB VAL A 363 5074 7407 8245 638 216 -3297 C ATOM 41 CG1 VAL A 363 38.617 -52.108 -21.423 1.00 55.52 C ANISOU 41 CG1 VAL A 363 5129 7415 8550 657 140 -3269 C ATOM 42 CG2 VAL A 363 37.807 -50.767 -23.378 1.00 56.69 C ANISOU 42 CG2 VAL A 363 5307 7809 8425 595 274 -3124 C ATOM 43 N THR A 364 41.500 -53.583 -22.434 1.00 64.42 N ANISOU 43 N THR A 364 6247 8444 9785 866 355 -3607 N ATOM 44 CA THR A 364 42.049 -54.879 -22.039 1.00 59.61 C ANISOU 44 CA THR A 364 5679 7697 9274 940 299 -3746 C ATOM 45 C THR A 364 41.241 -55.453 -20.893 1.00 63.82 C ANISOU 45 C THR A 364 6235 8116 9896 848 85 -3724 C ATOM 46 O THR A 364 40.375 -54.777 -20.323 1.00 65.01 O ANISOU 46 O THR A 364 6351 8312 10039 761 16 -3589 O ATOM 47 CB THR A 364 43.494 -54.766 -21.530 1.00 60.96 C ANISOU 47 CB THR A 364 5680 7831 9651 1032 409 -3729 C ATOM 48 OG1 THR A 364 43.510 -54.060 -20.279 1.00 60.77 O ANISOU 48 OG1 THR A 364 5543 7754 9791 942 317 -3610 O ATOM 49 CG2 THR A 364 44.377 -54.043 -22.539 1.00 62.50 C ANISOU 49 CG2 THR A 364 5778 8175 9793 1121 632 -3667 C ATOM 50 N GLN A 365 41.578 -56.673 -20.499 1.00 58.15 N ANISOU 50 N GLN A 365 5387 6678 10028 139 -258 -1726 N ATOM 51 CA GLN A 365 40.832 -57.328 -19.440 1.00 62.02 C ANISOU 51 CA GLN A 365 5987 6756 10822 18 -102 -1569 C ATOM 52 C GLN A 365 41.132 -56.660 -18.116 1.00 57.85 C ANISOU 52 C GLN A 365 5583 6228 10167 127 -99 -1090 C ATOM 53 O GLN A 365 40.254 -56.522 -17.275 1.00 56.28 O ANISOU 53 O GLN A 365 5415 5939 10031 -14 -24 -917 O ATOM 54 CB GLN A 365 41.176 -58.804 -19.347 1.00 67.05 C ANISOU 54 CB GLN A 365 6760 6870 11845 57 78 -1686 C ATOM 55 CG GLN A 365 40.307 -59.534 -18.348 1.00 83.06 C ANISOU 55 CG GLN A 365 8930 8435 14193 -128 288 -1521 C ATOM 56 CD GLN A 365 40.829 -60.912 -18.034 1.00101.50 C ANISOU 56 CD GLN A 365 11499 10158 16910 -13 494 -1488 C ATOM 57 OE1 GLN A 365 41.975 -61.236 -18.351 1.00112.44 O ANISOU 57 OE1 GLN A 365 12936 11492 18296 286 453 -1519 O ATOM 58 NE2 GLN A 365 39.993 -61.738 -17.409 1.00101.41 N ANISOU 58 NE2 GLN A 365 11633 9665 17233 -244 737 -1423 N ATOM 59 N GLU A 366 42.381 -56.245 -17.940 1.00 56.98 N ANISOU 59 N GLU A 366 5517 6270 9864 361 -173 -916 N ATOM 60 CA GLU A 366 42.802 -55.625 -16.695 1.00 56.19 C ANISOU 60 CA GLU A 366 5505 6234 9609 466 -182 -521 C ATOM 61 C GLU A 366 42.234 -54.223 -16.577 1.00 54.68 C ANISOU 61 C GLU A 366 5244 6373 9160 345 -267 -444 C ATOM 62 O GLU A 366 41.888 -53.779 -15.483 1.00 55.63 O ANISOU 62 O GLU A 366 5421 6490 9225 311 -228 -196 O ATOM 63 CB GLU A 366 44.323 -55.594 -16.580 1.00 55.84 C ANISOU 63 CB GLU A 366 5465 6324 9427 734 -241 -427 C ATOM 64 CG GLU A 366 44.959 -56.936 -16.218 1.00 55.79 C ANISOU 64 CG GLU A 366 5572 5950 9676 967 -149 -359 C ATOM 65 CD GLU A 366 45.197 -57.809 -17.432 0.23 62.77 C ANISOU 65 CD GLU A 366 6406 6681 10763 1011 -116 -745 C ATOM 66 OE1 GLU A 366 45.052 -57.309 -18.568 1.00 57.84 O ANISOU 66 OE1 GLU A 366 5634 6341 10002 878 -189 -1054 O ATOM 67 OE2 GLU A 366 45.536 -58.996 -17.251 1.00 74.30 O ANISOU 67 OE2 GLU A 366 7987 7735 12510 1196 -8 -739 O ATOM 68 N GLN A 367 42.143 -53.524 -17.702 1.00 45.33 N ANISOU 68 N GLN A 367 3949 5469 7807 300 -374 -653 N ATOM 69 CA GLN A 367 41.465 -52.242 -17.717 1.00 40.85 C ANISOU 69 CA GLN A 367 3341 5141 7037 222 -443 -585 C ATOM 70 C GLN A 367 39.985 -52.428 -17.368 1.00 49.64 C ANISOU 70 C GLN A 367 4396 6151 8314 72 -392 -622 C ATOM 71 O GLN A 367 39.407 -51.654 -16.603 1.00 46.79 O ANISOU 71 O GLN A 367 4043 5850 7886 41 -377 -460 O ATOM 72 CB GLN A 367 41.584 -51.583 -19.083 1.00 46.31 C ANISOU 72 CB GLN A 367 3955 6131 7510 234 -555 -765 C ATOM 73 CG GLN A 367 42.953 -51.050 -19.421 1.00 49.96 C ANISOU 73 CG GLN A 367 4454 6776 7753 322 -576 -716 C ATOM 74 CD GLN A 367 42.974 -50.441 -20.806 1.00 53.11 C ANISOU 74 CD GLN A 367 4807 7467 7907 311 -652 -858 C ATOM 75 OE1 GLN A 367 42.348 -50.968 -21.725 1.00 49.80 O ANISOU 75 OE1 GLN A 367 4291 7121 7509 287 -702 -1098 O ATOM 76 NE2 GLN A 367 43.669 -49.312 -20.959 1.00 47.77 N ANISOU 76 NE2 GLN A 367 4200 6971 6978 311 -647 -715 N ATOM 77 N PHE A 368 39.366 -53.454 -17.937 1.00 49.42 N ANISOU 77 N PHE A 368 4286 5986 8506 -38 -350 -881 N ATOM 78 CA PHE A 368 37.972 -53.727 -17.644 1.00 49.26 C ANISOU 78 CA PHE A 368 4159 5901 8658 -230 -277 -976 C ATOM 79 C PHE A 368 37.772 -54.035 -16.152 1.00 52.00 C ANISOU 79 C PHE A 368 4633 5981 9144 -292 -103 -687 C ATOM 80 O PHE A 368 36.824 -53.543 -15.540 1.00 53.89 O ANISOU 80 O PHE A 368 4796 6311 9367 -392 -58 -622 O ATOM 81 CB PHE A 368 37.467 -54.869 -18.521 1.00 49.15 C ANISOU 81 CB PHE A 368 4026 5773 8877 -391 -232 -1366 C ATOM 82 CG PHE A 368 36.043 -55.260 -18.259 1.00 51.68 C ANISOU 82 CG PHE A 368 4187 6047 9401 -652 -129 -1532 C ATOM 83 CD1 PHE A 368 34.992 -54.493 -18.751 1.00 53.89 C ANISOU 83 CD1 PHE A 368 4212 6732 9531 -693 -261 -1702 C ATOM 84 CD2 PHE A 368 35.751 -56.412 -17.546 1.00 54.15 C ANISOU 84 CD2 PHE A 368 4596 5921 10056 -851 114 -1520 C ATOM 85 CE1 PHE A 368 33.665 -54.863 -18.524 1.00 57.92 C ANISOU 85 CE1 PHE A 368 4504 7274 10227 -946 -163 -1909 C ATOM 86 CE2 PHE A 368 34.427 -56.793 -17.317 1.00 60.32 C ANISOU 86 CE2 PHE A 368 5204 6679 11037 -1158 251 -1709 C ATOM 87 CZ PHE A 368 33.382 -56.014 -17.806 1.00 61.08 C ANISOU 87 CZ PHE A 368 4983 7246 10977 -1214 106 -1930 C ATOM 88 N GLU A 369 38.668 -54.832 -15.567 1.00 50.04 N ANISOU 88 N GLU A 369 4570 5438 9004 -204 -4 -506 N ATOM 89 CA GLU A 369 38.563 -55.183 -14.142 1.00 55.49 C ANISOU 89 CA GLU A 369 5414 5904 9767 -229 163 -176 C ATOM 90 C GLU A 369 38.744 -53.944 -13.276 1.00 53.00 C ANISOU 90 C GLU A 369 5108 5874 9156 -142 99 69 C ATOM 91 O GLU A 369 37.995 -53.722 -12.327 1.00 53.02 O ANISOU 91 O GLU A 369 5112 5891 9142 -253 210 210 O ATOM 92 CB GLU A 369 39.604 -56.228 -13.724 1.00 46.41 C ANISOU 92 CB GLU A 369 4474 4419 8742 -55 248 17 C ATOM 93 CG GLU A 369 39.523 -57.569 -14.406 1.00 86.51 C ANISOU 93 CG GLU A 369 9605 9093 14171 -122 367 -212 C ATOM 94 CD GLU A 369 40.702 -58.475 -14.036 1.00101.90 C ANISOU 94 CD GLU A 369 11772 10721 16227 164 423 3 C ATOM 95 OE1 GLU A 369 41.160 -58.423 -12.868 1.00105.41 O ANISOU 95 OE1 GLU A 369 12363 11145 16542 332 455 416 O ATOM 96 OE2 GLU A 369 41.180 -59.229 -14.916 1.00104.53 O ANISOU 96 OE2 GLU A 369 12111 10853 16750 250 428 -255 O ATOM 97 N LEU A 370 39.754 -53.146 -13.609 1.00 49.88 N ANISOU 97 N LEU A 370 4712 5710 8531 31 -55 86 N ATOM 98 CA LEU A 370 40.032 -51.922 -12.883 1.00 48.75 C ANISOU 98 CA LEU A 370 4580 5819 8124 84 -104 248 C ATOM 99 C LEU A 370 38.789 -51.038 -12.827 1.00 49.86 C ANISOU 99 C LEU A 370 4616 6096 8234 -38 -95 167 C ATOM 100 O LEU A 370 38.362 -50.608 -11.753 1.00 50.66 O ANISOU 100 O LEU A 370 4733 6251 8265 -82 -9 303 O ATOM 101 CB LEU A 370 41.200 -51.166 -13.528 1.00 47.97 C ANISOU 101 CB LEU A 370 4470 5937 7821 209 -242 192 C ATOM 102 CG LEU A 370 41.450 -49.748 -13.000 1.00 44.41 C ANISOU 102 CG LEU A 370 4028 5721 7126 205 -274 270 C ATOM 103 CD1 LEU A 370 41.717 -49.792 -11.509 1.00 35.73 C ANISOU 103 CD1 LEU A 370 2988 4655 5933 227 -201 485 C ATOM 104 CD2 LEU A 370 42.602 -49.048 -13.753 1.00 46.59 C ANISOU 104 CD2 LEU A 370 4293 6182 7226 258 -362 191 C HETATM 105 N PTR A 371 38.198 -50.772 -13.983 1.00 47.81 N ANISOU 105 N PTR A 371 4230 5929 8005 -65 -186 -65 N HETATM 106 CA PTR A 371 37.062 -49.856 -14.020 1.00 45.01 C ANISOU 106 CA PTR A 371 3751 5745 7605 -96 -210 -142 C HETATM 107 C PTR A 371 35.807 -50.442 -13.357 1.00 45.11 C ANISOU 107 C PTR A 371 3648 5689 7803 -269 -62 -186 C HETATM 108 O PTR A 371 35.036 -49.697 -12.760 1.00 45.00 O ANISOU 108 O PTR A 371 3553 5806 7737 -277 -20 -168 O HETATM 109 CB PTR A 371 36.876 -49.205 -15.400 1.00 37.67 C ANISOU 109 CB PTR A 371 2729 5012 6570 -4 -377 -317 C HETATM 110 CG PTR A 371 37.898 -48.107 -15.654 1.00 44.81 C ANISOU 110 CG PTR A 371 3774 6007 7244 127 -452 -197 C HETATM 111 CD1 PTR A 371 37.604 -46.764 -15.392 1.00 40.73 C ANISOU 111 CD1 PTR A 371 3303 5571 6603 207 -461 -113 C HETATM 112 CD2 PTR A 371 39.173 -48.413 -16.121 1.00 41.97 C ANISOU 112 CD2 PTR A 371 3501 5634 6811 156 -481 -186 C HETATM 113 CE1 PTR A 371 38.550 -45.764 -15.610 1.00 39.51 C ANISOU 113 CE1 PTR A 371 3303 5440 6269 266 -479 -17 C HETATM 114 CE2 PTR A 371 40.114 -47.425 -16.346 1.00 43.78 C ANISOU 114 CE2 PTR A 371 3837 5960 6838 211 -508 -103 C HETATM 115 CZ PTR A 371 39.799 -46.096 -16.102 1.00 46.48 C ANISOU 115 CZ PTR A 371 4250 6340 7069 243 -498 -14 C HETATM 116 OH PTR A 371 40.695 -45.254 -16.309 1.00 46.36 O ANISOU 116 OH PTR A 371 4351 6363 6900 240 -482 47 O HETATM 117 P PTR A 371 40.532 -43.701 -16.698 1.00 39.35 P ANISOU 117 P PTR A 371 3609 5464 5877 291 -464 131 P HETATM 118 O1P PTR A 371 40.422 -42.895 -15.464 1.00 48.63 O ANISOU 118 O1P PTR A 371 4857 6534 7084 250 -358 180 O HETATM 119 O2P PTR A 371 39.276 -43.466 -17.584 1.00 34.91 O ANISOU 119 O2P PTR A 371 2994 4963 5309 452 -568 117 O HETATM 120 O3P PTR A 371 41.828 -43.277 -17.404 1.00 50.36 O ANISOU 120 O3P PTR A 371 5114 6919 7100 218 -428 157 O ATOM 121 N CYS A 372 35.619 -51.755 -13.444 1.00 45.83 N ANISOU 121 N CYS A 372 3733 5561 8119 -417 44 -258 N ATOM 122 CA CYS A 372 34.541 -52.425 -12.710 1.00 53.83 C ANISOU 122 CA CYS A 372 4667 6462 9323 -648 250 -274 C ATOM 123 C CYS A 372 34.656 -52.173 -11.212 1.00 55.99 C ANISOU 123 C CYS A 372 5075 6714 9486 -650 400 36 C ATOM 124 O CYS A 372 33.682 -51.813 -10.559 1.00 60.55 O ANISOU 124 O CYS A 372 5528 7424 10053 -762 512 18 O ATOM 125 CB CYS A 372 34.566 -53.943 -12.942 1.00 59.89 C ANISOU 125 CB CYS A 372 5500 6878 10376 -823 394 -353 C ATOM 126 SG CYS A 372 33.768 -54.498 -14.447 1.00 85.04 S ANISOU 126 SG CYS A 372 8420 10136 13756 -992 321 -854 S ATOM 127 N GLU A 373 35.851 -52.403 -10.673 1.00 55.40 N ANISOU 127 N GLU A 373 5226 6515 9307 -517 400 296 N ATOM 128 CA GLU A 373 36.128 -52.167 -9.261 1.00 58.42 C ANISOU 128 CA GLU A 373 5735 6954 9507 -486 509 592 C ATOM 129 C GLU A 373 35.843 -50.716 -8.872 1.00 56.44 C ANISOU 129 C GLU A 373 5385 7023 9035 -432 448 536 C ATOM 130 O GLU A 373 35.466 -50.439 -7.734 1.00 60.89 O ANISOU 130 O GLU A 373 5956 7701 9477 -492 584 654 O ATOM 131 CB GLU A 373 37.577 -52.538 -8.924 1.00 56.38 C ANISOU 131 CB GLU A 373 5678 6618 9126 -284 448 835 C ATOM 132 CG GLU A 373 37.870 -54.021 -9.027 1.00 67.69 C ANISOU 132 CG GLU A 373 7263 7668 10788 -281 555 954 C ATOM 133 CD GLU A 373 39.359 -54.342 -9.004 1.00 75.17 C ANISOU 133 CD GLU A 373 8345 8583 11633 4 439 1123 C ATOM 134 OE1 GLU A 373 40.155 -53.502 -8.529 1.00 66.77 O ANISOU 134 OE1 GLU A 373 7264 7831 10275 153 316 1212 O ATOM 135 OE2 GLU A 373 39.729 -55.443 -9.468 1.00 83.52 O ANISOU 135 OE2 GLU A 373 9506 9311 12916 76 479 1130 O ATOM 136 N MET A 374 36.017 -49.799 -9.822 1.00 46.99 N ANISOU 136 N MET A 374 5766 4963 7125 69 100 44 N ATOM 137 CA MET A 374 35.719 -48.384 -9.595 1.00 45.90 C ANISOU 137 CA MET A 374 5655 5032 6753 -71 114 102 C ATOM 138 C MET A 374 34.292 -47.979 -9.998 1.00 38.92 C ANISOU 138 C MET A 374 4752 4140 5894 -209 274 -9 C ATOM 139 O MET A 374 33.940 -46.806 -9.960 1.00 46.70 O ANISOU 139 O MET A 374 5749 5274 6722 -294 308 16 O ATOM 140 CB MET A 374 36.769 -47.486 -10.248 1.00 45.61 C ANISOU 140 CB MET A 374 5437 5311 6583 -31 -4 65 C ATOM 141 CG MET A 374 38.161 -47.683 -9.643 1.00 50.22 C ANISOU 141 CG MET A 374 5998 5938 7144 78 -183 225 C ATOM 142 SD MET A 374 39.380 -46.540 -10.307 1.00 64.55 S ANISOU 142 SD MET A 374 7568 8136 8821 63 -301 213 S ATOM 143 CE MET A 374 38.972 -46.607 -12.057 1.00 56.79 C ANISOU 143 CE MET A 374 6373 7290 7915 105 -145 -80 C ATOM 144 N GLY A 375 33.481 -48.953 -10.395 1.00 47.83 N ANISOU 144 N GLY A 375 5844 5087 7242 -231 360 -128 N ATOM 145 CA GLY A 375 32.082 -48.699 -10.686 1.00 44.28 C ANISOU 145 CA GLY A 375 5332 4623 6871 -371 487 -206 C ATOM 146 C GLY A 375 31.866 -47.943 -11.979 1.00 43.38 C ANISOU 146 C GLY A 375 5008 4769 6704 -381 430 -383 C ATOM 147 O GLY A 375 30.917 -47.171 -12.104 1.00 48.02 O ANISOU 147 O GLY A 375 5530 5438 7276 -466 491 -380 O ATOM 148 N SER A 376 32.737 -48.182 -12.954 1.00 43.23 N ANISOU 148 N SER A 376 4888 4878 6659 -283 321 -528 N ATOM 149 CA SER A 376 32.678 -47.458 -14.229 1.00 42.21 C ANISOU 149 CA SER A 376 4606 5014 6419 -293 260 -679 C ATOM 150 C SER A 376 33.221 -48.287 -15.402 1.00 42.20 C ANISOU 150 C SER A 376 4526 5050 6460 -211 209 -912 C ATOM 151 O SER A 376 33.384 -49.508 -15.288 1.00 42.91 O ANISOU 151 O SER A 376 4669 4912 6723 -153 230 -988 O ATOM 152 CB SER A 376 33.419 -46.122 -14.119 1.00 41.93 C ANISOU 152 CB SER A 376 4575 5213 6144 -276 219 -555 C ATOM 153 OG SER A 376 32.977 -45.232 -15.124 1.00 45.85 O ANISOU 153 OG SER A 376 4975 5918 6529 -323 186 -632 O ATOM 154 N THR A 377 33.437 -47.630 -16.542 1.00 39.70 N ANISOU 154 N THR A 377 4113 4997 5975 -208 158 -1029 N ATOM 155 CA THR A 377 34.103 -48.257 -17.684 1.00 41.11 C ANISOU 155 CA THR A 377 4249 5252 6117 -117 150 -1256 C ATOM 156 C THR A 377 35.285 -47.418 -18.154 1.00 40.63 C ANISOU 156 C THR A 377 4114 5482 5841 -40 157 -1216 C ATOM 157 O THR A 377 35.310 -46.203 -17.973 1.00 37.08 O ANISOU 157 O THR A 377 3649 5203 5238 -110 129 -1059 O ATOM 158 CB THR A 377 33.155 -48.458 -18.889 1.00 43.82 C ANISOU 158 CB THR A 377 4572 5647 6431 -221 89 -1488 C ATOM 159 OG1 THR A 377 32.851 -47.187 -19.475 1.00 45.25 O ANISOU 159 OG1 THR A 377 4695 6103 6395 -291 24 -1430 O ATOM 160 CG2 THR A 377 31.858 -49.155 -18.464 1.00 41.06 C ANISOU 160 CG2 THR A 377 4241 5042 6320 -355 69 -1512 C ATOM 161 N PHE A 378 36.259 -48.070 -18.774 1.00 41.61 N ANISOU 161 N PHE A 378 4192 5648 5968 100 214 -1362 N ATOM 162 CA PHE A 378 37.392 -47.356 -19.323 1.00 41.24 C ANISOU 162 CA PHE A 378 4035 5894 5740 159 260 -1335 C ATOM 163 C PHE A 378 36.942 -46.348 -20.385 1.00 41.86 C ANISOU 163 C PHE A 378 4123 6229 5554 30 236 -1385 C ATOM 164 O PHE A 378 37.417 -45.213 -20.413 1.00 42.50 O ANISOU 164 O PHE A 378 4157 6523 5468 -29 234 -1231 O ATOM 165 CB PHE A 378 38.411 -48.333 -19.923 1.00 46.13 C ANISOU 165 CB PHE A 378 4586 6508 6432 358 378 -1517 C ATOM 166 CG PHE A 378 39.564 -47.643 -20.619 1.00 49.33 C ANISOU 166 CG PHE A 378 4838 7244 6662 407 476 -1505 C ATOM 167 CD1 PHE A 378 40.672 -47.215 -19.897 1.00 45.97 C ANISOU 167 CD1 PHE A 378 4243 6929 6296 464 472 -1288 C ATOM 168 CD2 PHE A 378 39.518 -47.390 -21.981 1.00 46.13 C ANISOU 168 CD2 PHE A 378 4462 7049 6017 368 564 -1695 C ATOM 169 CE1 PHE A 378 41.721 -46.566 -20.522 1.00 50.25 C ANISOU 169 CE1 PHE A 378 4605 7781 6706 473 577 -1260 C ATOM 170 CE2 PHE A 378 40.562 -46.745 -22.616 1.00 50.49 C ANISOU 170 CE2 PHE A 378 4877 7907 6399 390 695 -1665 C ATOM 171 CZ PHE A 378 41.669 -46.334 -21.888 1.00 55.28 C ANISOU 171 CZ PHE A 378 5273 8619 7110 438 714 -1446 C ATOM 172 N GLN A 379 36.022 -46.758 -21.255 1.00 40.30 N ANISOU 172 N GLN A 379 3999 5999 5313 -30 198 -1590 N ATOM 173 CA GLN A 379 35.701 -45.955 -22.437 1.00 41.15 C ANISOU 173 CA GLN A 379 4135 6361 5138 -125 153 -1651 C ATOM 174 C GLN A 379 34.948 -44.662 -22.109 1.00 43.92 C ANISOU 174 C GLN A 379 4488 6789 5410 -250 43 -1426 C ATOM 175 O GLN A 379 34.949 -43.716 -22.903 1.00 41.88 O ANISOU 175 O GLN A 379 4255 6754 4904 -311 7 -1380 O ATOM 176 CB GLN A 379 34.933 -46.781 -23.483 1.00 44.99 C ANISOU 176 CB GLN A 379 4719 6799 5577 -169 92 -1941 C ATOM 177 CG GLN A 379 33.526 -47.206 -23.068 1.00 47.39 C ANISOU 177 CG GLN A 379 5037 6883 6087 -286 -53 -1959 C ATOM 178 CD GLN A 379 33.491 -48.584 -22.429 1.00 52.83 C ANISOU 178 CD GLN A 379 5761 7238 7073 -233 3 -2073 C ATOM 179 OE1 GLN A 379 34.529 -49.149 -22.071 1.00 50.57 O ANISOU 179 OE1 GLN A 379 5481 6862 6872 -74 136 -2087 O ATOM 180 NE2 GLN A 379 32.292 -49.136 -22.289 1.00 51.36 N ANISOU 180 NE2 GLN A 379 5588 6861 7066 -369 -103 -2140 N ATOM 181 N LEU A 380 34.305 -44.620 -20.944 1.00 39.68 N ANISOU 181 N LEU A 380 3946 6055 5077 -278 8 -1282 N ATOM 182 CA LEU A 380 33.542 -43.437 -20.550 1.00 35.57 C ANISOU 182 CA LEU A 380 3437 5563 4516 -359 -57 -1084 C ATOM 183 C LEU A 380 34.470 -42.226 -20.378 1.00 40.27 C ANISOU 183 C LEU A 380 4055 6318 4928 -371 -19 -898 C ATOM 184 O LEU A 380 35.493 -42.315 -19.683 1.00 37.26 O ANISOU 184 O LEU A 380 3657 5918 4583 -335 45 -822 O ATOM 185 CB LEU A 380 32.779 -43.712 -19.245 1.00 36.97 C ANISOU 185 CB LEU A 380 3622 5486 4940 -374 -33 -979 C ATOM 186 CG LEU A 380 31.793 -42.648 -18.753 1.00 40.70 C ANISOU 186 CG LEU A 380 4102 5933 5428 -425 -51 -807 C ATOM 187 CD1 LEU A 380 30.579 -42.641 -19.682 1.00 43.79 C ANISOU 187 CD1 LEU A 380 4399 6386 5852 -472 -172 -897 C ATOM 188 CD2 LEU A 380 31.351 -42.887 -17.311 1.00 37.68 C ANISOU 188 CD2 LEU A 380 3765 5312 5240 -428 50 -689 C ATOM 189 N CYS A 381 34.113 -41.097 -20.993 1.00 37.12 N ANISOU 189 N CYS A 381 3696 6063 4346 -432 -80 -809 N ATOM 190 CA CYS A 381 34.811 -39.836 -20.721 1.00 34.90 C ANISOU 190 CA CYS A 381 3472 5872 3916 -484 -52 -609 C ATOM 191 C CYS A 381 34.628 -39.463 -19.246 1.00 34.84 C ANISOU 191 C CYS A 381 3528 5661 4048 -495 -30 -453 C ATOM 192 O CYS A 381 33.495 -39.330 -18.785 1.00 34.15 O ANISOU 192 O CYS A 381 3473 5426 4078 -483 -44 -416 O ATOM 193 CB CYS A 381 34.227 -38.719 -21.589 1.00 41.74 C ANISOU 193 CB CYS A 381 4411 6859 4591 -536 -134 -522 C ATOM 194 SG CYS A 381 34.964 -37.092 -21.290 1.00 37.81 S ANISOU 194 SG CYS A 381 4036 6408 3922 -632 -102 -270 S ATOM 195 N LYS A 382 35.728 -39.262 -18.519 1.00 33.46 N ANISOU 195 N LYS A 382 3371 5491 3852 -526 7 -359 N ATOM 196 CA LYS A 382 35.647 -39.006 -17.086 1.00 37.45 C ANISOU 196 CA LYS A 382 3989 5804 4437 -551 16 -230 C ATOM 197 C LYS A 382 35.423 -37.528 -16.757 1.00 37.70 C ANISOU 197 C LYS A 382 4188 5797 4340 -639 9 -73 C ATOM 198 O LYS A 382 35.204 -37.172 -15.608 1.00 44.93 O ANISOU 198 O LYS A 382 5256 6538 5278 -666 34 15 O ATOM 199 CB LYS A 382 36.869 -39.571 -16.331 1.00 34.74 C ANISOU 199 CB LYS A 382 3601 5459 4141 -545 5 -195 C ATOM 200 CG LYS A 382 37.073 -41.075 -16.550 1.00 35.45 C ANISOU 200 CG LYS A 382 3556 5519 4394 -418 27 -342 C ATOM 201 CD LYS A 382 35.734 -41.824 -16.380 1.00 33.25 C ANISOU 201 CD LYS A 382 3325 5038 4270 -374 55 -430 C ATOM 202 CE LYS A 382 35.894 -43.349 -16.377 1.00 33.85 C ANISOU 202 CE LYS A 382 3333 4994 4532 -268 77 -562 C ATOM 203 NZ LYS A 382 36.447 -43.898 -17.650 1.00 32.76 N ANISOU 203 NZ LYS A 382 3073 5010 4364 -196 98 -750 N ATOM 204 N ILE A 383 35.513 -36.657 -17.748 1.00 37.93 N ANISOU 204 N ILE A 383 4227 5971 4215 -688 -16 -37 N ATOM 205 CA ILE A 383 35.085 -35.289 -17.516 1.00 34.65 C ANISOU 205 CA ILE A 383 3997 5458 3709 -743 -19 105 C ATOM 206 C ILE A 383 33.568 -35.112 -17.461 1.00 39.13 C ANISOU 206 C ILE A 383 4597 5879 4391 -633 -3 107 C ATOM 207 O ILE A 383 33.051 -34.572 -16.479 1.00 36.43 O ANISOU 207 O ILE A 383 4403 5334 4103 -614 65 179 O ATOM 208 CB ILE A 383 35.698 -34.313 -18.537 1.00 41.22 C ANISOU 208 CB ILE A 383 4866 6459 4336 -843 -49 189 C ATOM 209 CG1 ILE A 383 37.227 -34.339 -18.437 1.00 42.55 C ANISOU 209 CG1 ILE A 383 4966 6772 4429 -977 -39 217 C ATOM 210 CG2 ILE A 383 35.148 -32.899 -18.313 1.00 30.20 C ANISOU 210 CG2 ILE A 383 3700 4900 2873 -876 -54 341 C ATOM 211 CD1 ILE A 383 37.908 -33.476 -19.485 1.00 48.91 C ANISOU 211 CD1 ILE A 383 5783 7763 5036 -1107 -25 306 C ATOM 212 N CYS A 384 32.853 -35.531 -18.516 1.00 30.32 N ANISOU 212 N CYS A 384 3340 4871 3309 -563 -64 26 N ATOM 213 CA CYS A 384 31.389 -35.424 -18.498 1.00 31.80 C ANISOU 213 CA CYS A 384 3478 4950 3655 -460 -76 38 C ATOM 214 C CYS A 384 30.660 -36.595 -17.832 1.00 34.51 C ANISOU 214 C CYS A 384 3693 5177 4244 -412 -16 -67 C ATOM 215 O CYS A 384 29.516 -36.446 -17.367 1.00 30.34 O ANISOU 215 O CYS A 384 3119 4516 3894 -341 42 -28 O ATOM 216 CB CYS A 384 30.820 -35.199 -19.915 1.00 32.81 C ANISOU 216 CB CYS A 384 3519 5243 3703 -426 -225 33 C ATOM 217 SG CYS A 384 31.187 -36.563 -21.033 1.00 39.23 S ANISOU 217 SG CYS A 384 4184 6273 4450 -466 -313 -187 S ATOM 218 N ALA A 385 31.331 -37.744 -17.789 1.00 31.85 N ANISOU 218 N ALA A 385 3292 4878 3930 -447 -12 -190 N ATOM 219 CA ALA A 385 30.728 -38.996 -17.326 1.00 36.66 C ANISOU 219 CA ALA A 385 3795 5367 4766 -428 33 -294 C ATOM 220 C ALA A 385 29.441 -39.336 -18.095 1.00 40.74 C ANISOU 220 C ALA A 385 4133 5916 5431 -409 -54 -372 C ATOM 221 O ALA A 385 28.535 -39.985 -17.563 1.00 38.60 O ANISOU 221 O ALA A 385 3761 5508 5395 -411 6 -399 O ATOM 222 CB ALA A 385 30.486 -38.966 -15.813 1.00 33.16 C ANISOU 222 CB ALA A 385 3468 4703 4429 -422 185 -199 C ATOM 223 N GLU A 386 29.388 -38.892 -19.351 1.00 38.04 N ANISOU 223 N GLU A 386 3752 5762 4938 -410 -205 -395 N ATOM 224 CA AGLU A 386 28.218 -39.092 -20.208 0.48 44.60 C ANISOU 224 CA AGLU A 386 4414 6664 5868 -408 -362 -453 C ATOM 225 CA BGLU A 386 28.221 -39.072 -20.207 0.52 45.04 C ANISOU 225 CA BGLU A 386 4471 6719 5921 -407 -361 -450 C ATOM 226 C GLU A 386 28.608 -39.711 -21.554 1.00 48.96 C ANISOU 226 C GLU A 386 4959 7407 6237 -465 -520 -629 C ATOM 227 O GLU A 386 28.152 -40.799 -21.897 1.00 51.91 O ANISOU 227 O GLU A 386 5233 7761 6727 -520 -594 -805 O ATOM 228 CB AGLU A 386 27.445 -37.782 -20.416 0.48 49.24 C ANISOU 228 CB AGLU A 386 4984 7276 6448 -329 -428 -272 C ATOM 229 CB BGLU A 386 27.510 -37.727 -20.414 0.52 48.04 C ANISOU 229 CB BGLU A 386 4846 7127 6281 -328 -424 -266 C ATOM 230 CG AGLU A 386 26.346 -37.850 -21.496 0.48 58.09 C ANISOU 230 CG AGLU A 386 5915 8529 7629 -322 -670 -299 C ATOM 231 CG BGLU A 386 26.215 -37.815 -21.215 0.52 58.27 C ANISOU 231 CG BGLU A 386 5922 8506 7713 -308 -628 -278 C ATOM 232 CD AGLU A 386 25.017 -38.436 -21.005 0.48 62.93 C ANISOU 232 CD AGLU A 386 6260 9037 8615 -318 -664 -320 C ATOM 233 CD BGLU A 386 25.335 -36.580 -21.061 0.52 67.01 C ANISOU 233 CD BGLU A 386 6973 9565 8924 -171 -645 -67 C ATOM 234 OE1AGLU A 386 25.003 -39.557 -20.453 0.48 57.55 O ANISOU 234 OE1AGLU A 386 5523 8246 8096 -401 -563 -449 O ATOM 235 OE1BGLU A 386 25.839 -35.530 -20.602 0.52 64.68 O ANISOU 235 OE1BGLU A 386 6877 9184 8513 -105 -523 75 O ATOM 236 OE2AGLU A 386 23.973 -37.767 -21.183 0.48 74.09 O ANISOU 236 OE2AGLU A 386 7504 10471 10177 -229 -759 -192 O ATOM 237 OE2BGLU A 386 24.131 -36.669 -21.394 0.52 74.73 O ANISOU 237 OE2BGLU A 386 7697 10578 10118 -129 -785 -44 O ATOM 238 N ASN A 387 29.428 -39.006 -22.326 1.00 47.99 N ANISOU 238 N ASN A 387 4963 7456 5815 -468 -557 -585 N ATOM 239 CA ASN A 387 29.954 -39.521 -23.594 1.00 48.23 C ANISOU 239 CA ASN A 387 5042 7680 5604 -518 -646 -755 C ATOM 240 C ASN A 387 31.144 -40.453 -23.434 1.00 44.68 C ANISOU 240 C ASN A 387 4633 7219 5125 -521 -491 -913 C ATOM 241 O ASN A 387 31.816 -40.438 -22.412 1.00 44.53 O ANISOU 241 O ASN A 387 4625 7089 5205 -492 -343 -836 O ATOM 242 CB ASN A 387 30.316 -38.378 -24.529 1.00 44.68 C ANISOU 242 CB ASN A 387 4720 7426 4831 -528 -719 -623 C ATOM 243 CG ASN A 387 29.192 -37.382 -24.674 1.00 48.81 C ANISOU 243 CG ASN A 387 5209 7936 5399 -482 -882 -432 C ATOM 244 OD1 ASN A 387 29.380 -36.180 -24.484 1.00 64.85 O ANISOU 244 OD1 ASN A 387 7346 9944 7350 -447 -846 -218 O ATOM 245 ND2 ASN A 387 28.011 -37.875 -24.992 1.00 44.23 N ANISOU 245 ND2 ASN A 387 4472 7356 4975 -480 -1069 -503 N ATOM 246 N ASP A 388 31.376 -41.299 -24.429 1.00 41.98 N ANISOU 246 N ASP A 388 4320 6979 4651 -546 -532 -1138 N ATOM 247 CA ASP A 388 32.613 -42.071 -24.496 1.00 43.60 C ANISOU 247 CA ASP A 388 4563 7203 4802 -506 -363 -1286 C ATOM 248 C ASP A 388 33.775 -41.231 -25.025 1.00 43.71 C ANISOU 248 C ASP A 388 4645 7436 4526 -507 -255 -1192 C ATOM 249 O ASP A 388 33.554 -40.242 -25.719 1.00 47.35 O ANISOU 249 O ASP A 388 5183 8051 4755 -560 -339 -1071 O ATOM 250 CB ASP A 388 32.428 -43.328 -25.340 1.00 54.85 C ANISOU 250 CB ASP A 388 6027 8615 6199 -521 -406 -1594 C ATOM 251 CG ASP A 388 31.588 -44.379 -24.638 1.00 58.66 C ANISOU 251 CG ASP A 388 6435 8831 7022 -541 -453 -1696 C ATOM 252 OD1 ASP A 388 31.263 -44.198 -23.433 1.00 56.14 O ANISOU 252 OD1 ASP A 388 6032 8347 6951 -527 -409 -1524 O ATOM 253 OD2 ASP A 388 31.265 -45.390 -25.298 1.00 64.52 O ANISOU 253 OD2 ASP A 388 7229 9518 7767 -589 -522 -1954 O ATOM 254 N LYS A 389 35.008 -41.624 -24.697 1.00 44.79 N ANISOU 254 N LYS A 389 4740 7585 4694 -450 -70 -1227 N ATOM 255 CA LYS A 389 36.182 -40.869 -25.112 1.00 40.52 C ANISOU 255 CA LYS A 389 4206 7259 3929 -475 62 -1125 C ATOM 256 C LYS A 389 36.320 -41.004 -26.634 1.00 50.16 C ANISOU 256 C LYS A 389 5536 8703 4821 -499 94 -1288 C ATOM 257 O LYS A 389 36.379 -42.111 -27.150 1.00 44.45 O ANISOU 257 O LYS A 389 4836 7963 4091 -436 147 -1553 O ATOM 258 CB LYS A 389 37.411 -41.523 -24.471 1.00 41.04 C ANISOU 258 CB LYS A 389 4139 7295 4161 -385 236 -1161 C ATOM 259 CG LYS A 389 37.437 -41.533 -22.935 1.00 40.82 C ANISOU 259 CG LYS A 389 4041 7054 4415 -363 199 -1009 C ATOM 260 CD LYS A 389 38.447 -42.556 -22.392 1.00 35.66 C ANISOU 260 CD LYS A 389 3254 6334 3961 -233 309 -1082 C ATOM 261 CE LYS A 389 38.603 -42.446 -20.858 1.00 36.54 C ANISOU 261 CE LYS A 389 3335 6268 4282 -233 245 -892 C ATOM 262 NZ LYS A 389 39.558 -43.456 -20.321 1.00 34.87 N ANISOU 262 NZ LYS A 389 2990 5985 4274 -86 305 -928 N ATOM 263 N ASP A 390 36.247 -39.887 -27.356 1.00 50.11 N ANISOU 263 N ASP A 390 5640 8873 4526 -594 47 -1133 N ATOM 264 CA ASP A 390 36.565 -39.839 -28.786 1.00 48.39 C ANISOU 264 CA ASP A 390 5569 8902 3917 -638 112 -1238 C ATOM 265 C ASP A 390 37.868 -39.163 -29.251 1.00 50.46 C ANISOU 265 C ASP A 390 5833 9393 3947 -695 358 -1122 C ATOM 266 O ASP A 390 38.140 -39.106 -30.453 1.00 47.90 O ANISOU 266 O ASP A 390 5657 9282 3261 -740 453 -1199 O ATOM 267 CB ASP A 390 35.338 -39.455 -29.638 1.00 44.96 C ANISOU 267 CB ASP A 390 5305 8517 3259 -706 -157 -1220 C ATOM 268 CG ASP A 390 34.726 -38.140 -29.220 1.00 64.07 C ANISOU 268 CG ASP A 390 7742 10886 5717 -752 -320 -899 C ATOM 269 OD1 ASP A 390 35.490 -37.229 -28.862 1.00 55.26 O ANISOU 269 OD1 ASP A 390 6625 9799 4574 -796 -189 -685 O ATOM 270 OD2 ASP A 390 33.486 -38.007 -29.250 1.00 74.31 O ANISOU 270 OD2 ASP A 390 9046 12103 7086 -744 -576 -860 O ATOM 271 N VAL A 391 38.641 -38.598 -28.328 1.00 49.26 N ANISOU 271 N VAL A 391 5531 9207 3978 -722 456 -925 N ATOM 272 CA VAL A 391 39.804 -37.817 -28.746 1.00 48.41 C ANISOU 272 CA VAL A 391 5396 9319 3677 -829 668 -774 C ATOM 273 C VAL A 391 41.021 -37.965 -27.824 1.00 52.57 C ANISOU 273 C VAL A 391 5652 9847 4476 -810 834 -716 C ATOM 274 O VAL A 391 40.899 -37.972 -26.600 1.00 50.56 O ANISOU 274 O VAL A 391 5299 9396 4514 -787 714 -634 O ATOM 275 CB VAL A 391 39.440 -36.310 -28.998 1.00 53.23 C ANISOU 275 CB VAL A 391 6190 9961 4075 -995 551 -476 C ATOM 276 CG1 VAL A 391 39.172 -35.567 -27.686 1.00 41.93 C ANISOU 276 CG1 VAL A 391 4714 8300 2918 -1034 411 -264 C ATOM 277 CG2 VAL A 391 40.520 -35.597 -29.824 1.00 50.49 C ANISOU 277 CG2 VAL A 391 5879 9870 3434 -1143 789 -346 C ATOM 278 N LYS A 392 42.190 -38.112 -28.439 1.00 48.51 N ANISOU 278 N LYS A 392 5013 9564 3853 -817 1112 -760 N ATOM 279 CA LYS A 392 43.448 -38.196 -27.722 1.00 52.67 C ANISOU 279 CA LYS A 392 5228 10153 4633 -808 1264 -683 C ATOM 280 C LYS A 392 44.241 -36.904 -27.898 1.00 58.02 C ANISOU 280 C LYS A 392 5862 11013 5171 -1050 1365 -411 C ATOM 281 O LYS A 392 44.488 -36.451 -29.019 1.00 54.92 O ANISOU 281 O LYS A 392 5582 10832 4454 -1154 1544 -382 O ATOM 282 CB LYS A 392 44.278 -39.384 -28.216 1.00 53.16 C ANISOU 282 CB LYS A 392 5101 10339 4758 -612 1541 -931 C ATOM 283 CG LYS A 392 45.590 -39.553 -27.471 1.00 56.20 C ANISOU 283 CG LYS A 392 5095 10802 5457 -565 1674 -839 C ATOM 284 CD LYS A 392 46.255 -40.866 -27.827 1.00 69.66 C ANISOU 284 CD LYS A 392 6610 12555 7302 -292 1929 -1100 C ATOM 285 CE LYS A 392 47.489 -41.100 -26.975 1.00 79.63 C ANISOU 285 CE LYS A 392 7437 13878 8942 -205 1999 -984 C ATOM 286 NZ LYS A 392 48.316 -42.232 -27.489 1.00 83.96 N ANISOU 286 NZ LYS A 392 7759 14516 9627 84 2323 -1212 N ATOM 287 N ILE A 393 44.640 -36.324 -26.776 1.00 52.79 N ANISOU 287 N ILE A 393 5062 10256 4739 -1161 1247 -212 N ATOM 288 CA ILE A 393 45.395 -35.083 -26.778 1.00 60.25 C ANISOU 288 CA ILE A 393 5965 11323 5603 -1435 1307 52 C ATOM 289 C ILE A 393 46.892 -35.375 -26.719 1.00 62.22 C ANISOU 289 C ILE A 393 5805 11809 6025 -1460 1540 71 C ATOM 290 O ILE A 393 47.320 -36.266 -25.986 1.00 57.69 O ANISOU 290 O ILE A 393 4966 11197 5758 -1286 1512 -23 O ATOM 291 CB ILE A 393 44.943 -34.194 -25.603 1.00 63.45 C ANISOU 291 CB ILE A 393 6499 11472 6136 -1575 1029 247 C ATOM 292 CG1 ILE A 393 43.512 -33.707 -25.868 1.00 61.00 C ANISOU 292 CG1 ILE A 393 6562 10970 5643 -1553 855 267 C ATOM 293 CG2 ILE A 393 45.919 -33.048 -25.364 1.00 57.79 C ANISOU 293 CG2 ILE A 393 5696 10843 5418 -1882 1069 498 C ATOM 294 CD1 ILE A 393 43.075 -32.600 -24.976 1.00 63.89 C ANISOU 294 CD1 ILE A 393 7117 11094 6065 -1697 659 469 C ATOM 295 N GLU A 394 47.676 -34.651 -27.522 1.00 57.55 N ANISOU 295 N GLU A 394 5194 11389 5284 -1635 1736 199 N ATOM 296 CA GLU A 394 49.124 -34.826 -27.557 1.00 62.68 C ANISOU 296 CA GLU A 394 5483 12172 6160 -1633 1924 234 C ATOM 297 C GLU A 394 49.841 -33.568 -27.086 1.00 66.54 C ANISOU 297 C GLU A 394 5915 12633 6734 -1949 1828 513 C ATOM 298 O GLU A 394 49.319 -32.464 -27.250 1.00 61.70 O ANISOU 298 O GLU A 394 5615 11918 5910 -2169 1724 669 O ATOM 299 CB GLU A 394 49.581 -35.161 -28.977 1.00 66.14 C ANISOU 299 CB GLU A 394 5951 12775 6404 -1538 2271 118 C ATOM 300 CG GLU A 394 49.013 -36.458 -29.516 1.00 76.85 C ANISOU 300 CG GLU A 394 7388 14138 7673 -1231 2383 -197 C ATOM 301 CD GLU A 394 49.552 -37.678 -28.788 1.00 86.48 C ANISOU 301 CD GLU A 394 8249 15329 9279 -959 2418 -352 C ATOM 302 OE1 GLU A 394 50.259 -37.512 -27.767 1.00 87.89 O ANISOU 302 OE1 GLU A 394 8120 15486 9787 -1009 2296 -197 O ATOM 303 OE2 GLU A 394 49.273 -38.808 -29.245 1.00 88.16 O ANISOU 303 OE2 GLU A 394 8514 15516 9467 -694 2548 -628 O ATOM 304 N PRO A 395 51.063 -33.718 -26.532 1.00 59.47 N ANISOU 304 N PRO A 395 4837 10684 7076 -2204 803 34 N ATOM 305 CA PRO A 395 51.844 -34.924 -26.202 1.00 57.59 C ANISOU 305 CA PRO A 395 4397 10561 6925 -2022 905 -192 C ATOM 306 C PRO A 395 51.376 -35.766 -24.991 1.00 61.37 C ANISOU 306 C PRO A 395 4915 10889 7515 -1662 812 -257 C ATOM 307 O PRO A 395 51.798 -36.915 -24.858 1.00 59.92 O ANISOU 307 O PRO A 395 4586 10779 7402 -1498 908 -414 O ATOM 308 CB PRO A 395 53.247 -34.367 -25.962 1.00 59.18 C ANISOU 308 CB PRO A 395 4387 10857 7240 -2138 903 -276 C ATOM 309 CG PRO A 395 53.003 -33.011 -25.407 1.00 65.58 C ANISOU 309 CG PRO A 395 5319 11495 8103 -2218 716 -121 C ATOM 310 CD PRO A 395 51.776 -32.492 -26.130 1.00 66.98 C ANISOU 310 CD PRO A 395 5734 11582 8132 -2347 697 93 C ATOM 311 N CYS A 396 50.553 -35.203 -24.111 1.00 63.40 N ANISOU 311 N CYS A 396 5353 10940 7796 -1541 634 -136 N ATOM 312 CA CYS A 396 50.230 -35.849 -22.820 1.00 60.44 C ANISOU 312 CA CYS A 396 5006 10440 7516 -1208 537 -177 C ATOM 313 C CYS A 396 49.499 -37.204 -22.885 1.00 58.20 C ANISOU 313 C CYS A 396 4757 10123 7232 -1001 638 -214 C ATOM 314 O CYS A 396 49.704 -38.057 -22.023 1.00 56.72 O ANISOU 314 O CYS A 396 4495 9908 7149 -742 627 -284 O ATOM 315 CB CYS A 396 49.435 -34.889 -21.945 1.00 54.43 C ANISOU 315 CB CYS A 396 4434 9485 6763 -1147 340 -48 C ATOM 316 SG CYS A 396 47.869 -34.433 -22.709 1.00 54.73 S ANISOU 316 SG CYS A 396 4731 9381 6681 -1263 329 136 S ATOM 317 N GLY A 397 48.639 -37.388 -23.888 1.00 57.61 N ANISOU 317 N GLY A 397 4791 10048 7051 -1112 729 -163 N ATOM 318 CA GLY A 397 47.941 -38.649 -24.091 1.00 44.45 C ANISOU 318 CA GLY A 397 3138 8347 5406 -948 837 -221 C ATOM 319 C GLY A 397 46.607 -38.812 -23.351 1.00 53.04 C ANISOU 319 C GLY A 397 4424 9213 6516 -744 745 -109 C ATOM 320 O GLY A 397 46.019 -39.902 -23.352 1.00 49.12 O ANISOU 320 O GLY A 397 3928 8655 6079 -580 830 -155 O ATOM 321 N HIS A 398 46.119 -37.744 -22.721 1.00 47.57 N ANISOU 321 N HIS A 398 3886 8394 5795 -753 579 26 N ATOM 322 CA HIS A 398 44.829 -37.802 -22.025 1.00 47.14 C ANISOU 322 CA HIS A 398 4017 8137 5757 -575 497 127 C ATOM 323 C HIS A 398 43.653 -37.995 -22.974 1.00 49.15 C ANISOU 323 C HIS A 398 4397 8336 5940 -658 557 179 C ATOM 324 O HIS A 398 43.574 -37.356 -24.028 1.00 43.72 O ANISOU 324 O HIS A 398 3747 7724 5140 -905 567 224 O ATOM 325 CB HIS A 398 44.607 -36.567 -21.139 1.00 44.25 C ANISOU 325 CB HIS A 398 3768 7655 5389 -572 307 226 C ATOM 326 CG HIS A 398 45.615 -36.438 -20.041 1.00 45.52 C ANISOU 326 CG HIS A 398 3812 7866 5618 -446 225 159 C ATOM 327 ND1 HIS A 398 46.721 -35.613 -20.132 1.00 42.12 N ANISOU 327 ND1 HIS A 398 3266 7539 5198 -614 173 111 N ATOM 328 CD2 HIS A 398 45.714 -37.075 -18.850 1.00 44.05 C ANISOU 328 CD2 HIS A 398 3592 7655 5491 -168 188 130 C ATOM 329 CE1 HIS A 398 47.441 -35.731 -19.030 1.00 57.55 C ANISOU 329 CE1 HIS A 398 5119 9532 7217 -440 93 37 C ATOM 330 NE2 HIS A 398 46.849 -36.607 -18.235 1.00 53.65 N ANISOU 330 NE2 HIS A 398 4677 8969 6738 -166 97 57 N ATOM 331 N LEU A 399 42.747 -38.885 -22.580 1.00 52.40 N ANISOU 331 N LEU A 399 4869 8622 6421 -449 595 178 N ATOM 332 CA LEU A 399 41.560 -39.207 -23.366 1.00 48.24 C ANISOU 332 CA LEU A 399 4446 8028 5856 -489 647 201 C ATOM 333 C LEU A 399 40.307 -38.542 -22.821 1.00 46.41 C ANISOU 333 C LEU A 399 4416 7595 5624 -428 516 340 C ATOM 334 O LEU A 399 40.086 -38.490 -21.611 1.00 46.99 O ANISOU 334 O LEU A 399 4538 7545 5769 -234 443 384 O ATOM 335 CB LEU A 399 41.340 -40.718 -23.403 1.00 41.97 C ANISOU 335 CB LEU A 399 3556 7210 5179 -310 797 86 C ATOM 336 CG LEU A 399 42.532 -41.503 -23.916 1.00 46.70 C ANISOU 336 CG LEU A 399 3935 7992 5819 -344 937 -81 C ATOM 337 CD1 LEU A 399 42.188 -42.965 -23.908 1.00 42.74 C ANISOU 337 CD1 LEU A 399 3342 7418 5479 -157 1075 -190 C ATOM 338 CD2 LEU A 399 42.932 -41.006 -25.335 1.00 54.44 C ANISOU 338 CD2 LEU A 399 4873 9181 6631 -649 992 -135 C ATOM 339 N MET A 400 39.483 -38.037 -23.726 1.00 36.35 N ANISOU 339 N MET A 400 3251 6299 4261 -591 485 406 N ATOM 340 CA MET A 400 38.218 -37.460 -23.334 1.00 44.62 C ANISOU 340 CA MET A 400 4476 7149 5330 -538 368 521 C ATOM 341 C MET A 400 37.306 -37.390 -24.554 1.00 45.76 C ANISOU 341 C MET A 400 4694 7303 5389 -689 376 554 C ATOM 342 O MET A 400 37.721 -37.710 -25.663 1.00 50.16 O ANISOU 342 O MET A 400 5171 8042 5847 -843 468 489 O ATOM 343 CB MET A 400 38.467 -36.057 -22.818 1.00 44.55 C ANISOU 343 CB MET A 400 4537 7084 5304 -624 203 624 C ATOM 344 CG MET A 400 38.912 -35.114 -23.921 1.00 46.76 C ANISOU 344 CG MET A 400 4816 7478 5474 -920 165 694 C ATOM 345 SD MET A 400 40.011 -33.868 -23.270 1.00 47.29 S ANISOU 345 SD MET A 400 4838 7552 5577 -1016 44 731 S ATOM 346 CE MET A 400 41.440 -34.871 -22.847 1.00 41.43 C ANISOU 346 CE MET A 400 3885 6993 4864 -907 173 561 C ATOM 347 N CYS A 401 36.066 -36.972 -24.349 1.00 43.32 N ANISOU 347 N CYS A 401 4531 6813 5114 -644 278 645 N ATOM 348 CA CYS A 401 35.186 -36.661 -25.472 1.00 45.83 C ANISOU 348 CA CYS A 401 4931 7140 5344 -798 237 703 C ATOM 349 C CYS A 401 35.436 -35.248 -26.034 1.00 51.65 C ANISOU 349 C CYS A 401 5735 7918 5974 -1038 103 855 C ATOM 350 O CYS A 401 35.994 -34.372 -25.354 1.00 47.63 O ANISOU 350 O CYS A 401 5237 7353 5507 -1059 13 920 O ATOM 351 CB CYS A 401 33.716 -36.907 -25.132 1.00 39.32 C ANISOU 351 CB CYS A 401 4212 6107 4622 -650 196 723 C ATOM 352 SG CYS A 401 32.860 -35.490 -24.487 1.00 43.83 S ANISOU 352 SG CYS A 401 4947 6455 5250 -652 -13 887 S ATOM 353 N THR A 402 35.051 -35.049 -27.287 1.00 47.95 N ANISOU 353 N THR A 402 5874 8297 4049 -691 -420 6 N ATOM 354 CA THR A 402 35.268 -33.784 -27.984 1.00 47.80 C ANISOU 354 CA THR A 402 6143 8348 3671 -1034 -339 283 C ATOM 355 C THR A 402 34.478 -32.606 -27.422 1.00 46.90 C ANISOU 355 C THR A 402 6313 7797 3709 -998 -501 685 C ATOM 356 O THR A 402 34.982 -31.484 -27.383 1.00 53.28 O ANISOU 356 O THR A 402 7298 8532 4414 -1257 -425 888 O ATOM 357 CB THR A 402 34.929 -33.917 -29.495 1.00 57.18 C ANISOU 357 CB THR A 402 7466 9836 4423 -1234 -380 318 C ATOM 358 OG1 THR A 402 35.902 -34.757 -30.119 1.00 60.88 O ANISOU 358 OG1 THR A 402 7634 10789 4708 -1393 -150 -145 O ATOM 359 CG2 THR A 402 34.954 -32.557 -30.168 1.00 63.92 C ANISOU 359 CG2 THR A 402 8716 10668 4904 -1631 -420 739 C ATOM 360 N SER A 403 33.232 -32.832 -27.019 1.00 40.89 N ANISOU 360 N SER A 403 5573 6744 3221 -698 -728 758 N ATOM 361 CA SER A 403 32.455 -31.718 -26.489 1.00 58.73 C ANISOU 361 CA SER A 403 8014 8585 5717 -649 -892 1016 C ATOM 362 C SER A 403 32.989 -31.229 -25.147 1.00 39.07 C ANISOU 362 C SER A 403 5414 5940 3491 -671 -739 947 C ATOM 363 O SER A 403 32.822 -30.058 -24.815 1.00 48.50 O ANISOU 363 O SER A 403 6741 6848 4838 -751 -790 1117 O ATOM 364 CB SER A 403 30.956 -32.020 -26.423 1.00 60.69 C ANISOU 364 CB SER A 403 8257 8594 6211 -353 -1158 1020 C ATOM 365 OG SER A 403 30.702 -33.268 -25.830 1.00 63.80 O ANISOU 365 OG SER A 403 8407 9083 6753 -148 -1113 744 O ATOM 366 N CYS A 404 33.649 -32.108 -24.386 1.00 36.89 N ANISOU 366 N CYS A 404 4890 5836 3290 -618 -589 695 N ATOM 367 CA CYS A 404 34.318 -31.664 -23.153 1.00 35.72 C ANISOU 367 CA CYS A 404 4641 5617 3314 -706 -446 636 C ATOM 368 C CYS A 404 35.538 -30.777 -23.457 1.00 48.42 C ANISOU 368 C CYS A 404 6323 7348 4724 -1000 -246 701 C ATOM 369 O CYS A 404 35.758 -29.761 -22.794 1.00 49.24 O ANISOU 369 O CYS A 404 6482 7275 4951 -1123 -173 781 O ATOM 370 CB CYS A 404 34.693 -32.849 -22.257 1.00 39.55 C ANISOU 370 CB CYS A 404 4875 6219 3931 -603 -438 409 C ATOM 371 SG CYS A 404 33.267 -33.578 -21.351 1.00 41.66 S ANISOU 371 SG CYS A 404 5087 6294 4448 -412 -631 362 S ATOM 372 N LEU A 405 36.316 -31.155 -24.470 1.00 43.33 N ANISOU 372 N LEU A 405 5660 7032 3773 -1147 -140 617 N ATOM 373 CA LEU A 405 37.433 -30.329 -24.915 1.00 42.81 C ANISOU 373 CA LEU A 405 5675 7146 3445 -1510 75 652 C ATOM 374 C LEU A 405 36.906 -28.958 -25.329 1.00 49.46 C ANISOU 374 C LEU A 405 6880 7697 4215 -1698 -38 1046 C ATOM 375 O LEU A 405 37.420 -27.911 -24.915 1.00 51.58 O ANISOU 375 O LEU A 405 7243 7824 4532 -1906 60 1157 O ATOM 376 CB LEU A 405 38.169 -30.996 -26.085 1.00 45.17 C ANISOU 376 CB LEU A 405 5870 7909 3384 -1699 215 426 C ATOM 377 CG LEU A 405 39.329 -30.180 -26.671 1.00 60.25 C ANISOU 377 CG LEU A 405 7858 10100 4933 -2181 479 413 C ATOM 378 CD1 LEU A 405 40.348 -29.812 -25.584 1.00 58.68 C ANISOU 378 CD1 LEU A 405 7471 9882 4943 -2229 666 250 C ATOM 379 CD2 LEU A 405 40.005 -30.906 -27.829 1.00 62.90 C ANISOU 379 CD2 LEU A 405 8021 10980 4897 -2424 659 66 C ATOM 380 N THR A 406 35.855 -28.989 -26.137 1.00 45.86 N ANISOU 380 N THR A 406 6620 7118 3687 -1615 -291 1253 N ATOM 381 CA THR A 406 35.188 -27.798 -26.643 1.00 53.66 C ANISOU 381 CA THR A 406 7963 7749 4677 -1746 -548 1659 C ATOM 382 C THR A 406 34.594 -26.913 -25.539 1.00 49.12 C ANISOU 382 C THR A 406 7380 6665 4621 -1566 -676 1717 C ATOM 383 O THR A 406 34.786 -25.700 -25.535 1.00 50.78 O ANISOU 383 O THR A 406 7792 6589 4915 -1777 -744 1947 O ATOM 384 CB THR A 406 34.071 -28.204 -27.630 1.00 60.50 C ANISOU 384 CB THR A 406 8976 8581 5429 -1617 -862 1817 C ATOM 385 OG1 THR A 406 34.664 -28.602 -28.872 1.00 76.70 O ANISOU 385 OG1 THR A 406 11123 11103 6915 -1953 -759 1830 O ATOM 386 CG2 THR A 406 33.136 -27.048 -27.877 1.00 68.58 C ANISOU 386 CG2 THR A 406 10305 9085 6667 -1613 -1267 2209 C ATOM 387 N SER A 407 33.852 -27.521 -24.620 1.00 44.42 N ANISOU 387 N SER A 407 6541 5963 4375 -1218 -711 1479 N ATOM 388 CA SER A 407 33.298 -26.796 -23.484 1.00 47.40 C ANISOU 388 CA SER A 407 6816 5960 5233 -1091 -765 1390 C ATOM 389 C SER A 407 34.388 -26.179 -22.602 1.00 50.10 C ANISOU 389 C SER A 407 7071 6342 5622 -1305 -485 1296 C ATOM 390 O SER A 407 34.205 -25.095 -22.043 1.00 51.58 O ANISOU 390 O SER A 407 7273 6185 6138 -1351 -529 1308 O ATOM 391 CB SER A 407 32.410 -27.720 -22.648 1.00 41.46 C ANISOU 391 CB SER A 407 5799 5229 4723 -798 -785 1098 C ATOM 392 OG SER A 407 31.229 -28.006 -23.359 1.00 46.50 O ANISOU 392 OG SER A 407 6506 5732 5430 -589 -1073 1161 O ATOM 393 N TRP A 408 35.511 -26.878 -22.471 1.00 51.12 N ANISOU 393 N TRP A 408 7071 6878 5474 -1422 -220 1156 N ATOM 394 CA TRP A 408 36.653 -26.382 -21.695 1.00 50.14 C ANISOU 394 CA TRP A 408 6843 6851 5356 -1635 43 1045 C ATOM 395 C TRP A 408 37.176 -25.103 -22.328 1.00 53.99 C ANISOU 395 C TRP A 408 7595 7185 5734 -1956 66 1298 C ATOM 396 O TRP A 408 37.308 -24.067 -21.665 1.00 54.53 O ANISOU 396 O TRP A 408 7675 6986 6059 -2061 108 1307 O ATOM 397 CB TRP A 408 37.746 -27.456 -21.647 1.00 45.01 C ANISOU 397 CB TRP A 408 5985 6654 4464 -1672 241 825 C ATOM 398 CG TRP A 408 39.035 -27.096 -20.958 1.00 49.07 C ANISOU 398 CG TRP A 408 6354 7335 4956 -1885 492 673 C ATOM 399 CD1 TRP A 408 40.296 -27.225 -21.474 1.00 53.77 C ANISOU 399 CD1 TRP A 408 6876 8268 5284 -2109 695 550 C ATOM 400 CD2 TRP A 408 39.198 -26.579 -19.627 1.00 41.60 C ANISOU 400 CD2 TRP A 408 5277 6271 4258 -1919 576 568 C ATOM 401 NE1 TRP A 408 41.230 -26.820 -20.550 1.00 49.94 N ANISOU 401 NE1 TRP A 408 6230 7853 4891 -2245 876 396 N ATOM 402 CE2 TRP A 408 40.586 -26.422 -19.406 1.00 51.16 C ANISOU 402 CE2 TRP A 408 6360 7737 5341 -2139 804 424 C ATOM 403 CE3 TRP A 408 38.310 -26.228 -18.605 1.00 41.64 C ANISOU 403 CE3 TRP A 408 5228 6023 4569 -1822 500 523 C ATOM 404 CZ2 TRP A 408 41.108 -25.927 -18.197 1.00 42.68 C ANISOU 404 CZ2 TRP A 408 5136 6656 4423 -2249 931 291 C ATOM 405 CZ3 TRP A 408 38.830 -25.741 -17.402 1.00 44.48 C ANISOU 405 CZ3 TRP A 408 5429 6411 5059 -1970 655 362 C ATOM 406 CH2 TRP A 408 40.214 -25.595 -17.216 1.00 41.24 C ANISOU 406 CH2 TRP A 408 4925 6241 4501 -2173 855 275 C ATOM 407 N GLN A 409 37.458 -25.161 -23.625 1.00 56.03 N ANISOU 407 N GLN A 409 8074 7617 5599 -2161 31 1499 N ATOM 408 CA GLN A 409 37.961 -23.976 -24.318 1.00 56.63 C ANISOU 408 CA GLN A 409 8467 7564 5484 -2574 19 1804 C ATOM 409 C GLN A 409 36.915 -22.862 -24.347 1.00 55.26 C ANISOU 409 C GLN A 409 8540 6760 5697 -2505 -363 2113 C ATOM 410 O GLN A 409 37.240 -21.684 -24.256 1.00 60.28 O ANISOU 410 O GLN A 409 9351 7088 6465 -2754 -401 2295 O ATOM 411 CB GLN A 409 38.399 -24.322 -25.733 1.00 64.46 C ANISOU 411 CB GLN A 409 9655 8942 5894 -2901 51 1946 C ATOM 412 CG GLN A 409 39.424 -25.425 -25.810 1.00 73.25 C ANISOU 412 CG GLN A 409 10456 10662 6715 -2958 399 1537 C ATOM 413 CD GLN A 409 40.010 -25.567 -27.205 1.00 86.22 C ANISOU 413 CD GLN A 409 12253 12758 7749 -3421 513 1578 C ATOM 414 OE1 GLN A 409 39.404 -25.146 -28.201 1.00 94.44 O ANISOU 414 OE1 GLN A 409 13628 13667 8587 -3586 252 1923 O ATOM 415 NE2 GLN A 409 41.203 -26.151 -27.285 1.00 79.12 N ANISOU 415 NE2 GLN A 409 11036 12346 6678 -3562 849 1127 N ATOM 416 N GLU A 410 35.655 -23.243 -24.485 1.00 62.39 N ANISOU 416 N GLU A 410 9432 7446 6829 -2160 -673 2141 N ATOM 417 CA GLU A 410 34.566 -22.281 -24.513 1.00 77.13 C ANISOU 417 CA GLU A 410 11450 8683 9175 -2021 -1105 2344 C ATOM 418 C GLU A 410 34.450 -21.574 -23.162 1.00 76.76 C ANISOU 418 C GLU A 410 11149 8307 9708 -1890 -1018 2057 C ATOM 419 O GLU A 410 33.942 -20.458 -23.074 1.00 77.43 O ANISOU 419 O GLU A 410 11326 7825 10267 -1875 -1317 2165 O ATOM 420 CB GLU A 410 33.266 -23.001 -24.862 1.00 89.80 C ANISOU 420 CB GLU A 410 12999 10208 10911 -1654 -1410 2312 C ATOM 421 CG GLU A 410 32.061 -22.108 -25.031 1.00104.59 C ANISOU 421 CG GLU A 410 14985 11426 13329 -1464 -1938 2475 C ATOM 422 CD GLU A 410 30.816 -22.900 -25.398 1.00115.55 C ANISOU 422 CD GLU A 410 16282 12804 14820 -1109 -2213 2391 C ATOM 423 OE1 GLU A 410 30.874 -24.154 -25.367 1.00115.68 O ANISOU 423 OE1 GLU A 410 16130 13305 14519 -1003 -1955 2181 O ATOM 424 OE2 GLU A 410 29.782 -22.268 -25.718 1.00118.61 O ANISOU 424 OE2 GLU A 410 16750 12670 15645 -932 -2718 2518 O ATOM 425 N SER A 411 34.933 -22.232 -22.112 1.00 61.48 N ANISOU 425 N SER A 411 8503 6453 8403 -1938 340 755 N ATOM 426 CA SER A 411 34.839 -21.698 -20.760 1.00 62.61 C ANISOU 426 CA SER A 411 8545 6470 8772 -2047 464 421 C ATOM 427 C SER A 411 36.072 -20.875 -20.396 1.00 67.43 C ANISOU 427 C SER A 411 9159 7008 9453 -2454 717 188 C ATOM 428 O SER A 411 36.205 -20.419 -19.257 1.00 69.33 O ANISOU 428 O SER A 411 9323 7191 9829 -2597 807 -170 O ATOM 429 CB SER A 411 34.622 -22.817 -19.736 1.00 61.81 C ANISOU 429 CB SER A 411 8188 6757 8539 -1944 322 187 C ATOM 430 OG SER A 411 35.774 -23.636 -19.628 1.00 66.67 O ANISOU 430 OG SER A 411 8651 7811 8872 -2098 297 57 O ATOM 431 N GLU A 412 36.970 -20.695 -21.361 1.00 63.13 N ANISOU 431 N GLU A 412 8692 6485 8811 -2650 835 375 N ATOM 432 CA GLU A 412 38.196 -19.927 -21.135 1.00 70.10 C ANISOU 432 CA GLU A 412 9519 7308 9808 -3100 1092 172 C ATOM 433 C GLU A 412 39.311 -20.771 -20.517 1.00 62.38 C ANISOU 433 C GLU A 412 8179 6925 8598 -3285 1028 -144 C ATOM 434 O GLU A 412 40.401 -20.273 -20.249 1.00 68.50 O ANISOU 434 O GLU A 412 8798 7771 9460 -3679 1193 -372 O ATOM 435 CB GLU A 412 37.945 -18.643 -20.332 1.00 77.50 C ANISOU 435 CB GLU A 412 10584 7730 11130 -3279 1268 -76 C ATOM 436 CG GLU A 412 37.237 -17.544 -21.117 1.00 85.15 C ANISOU 436 CG GLU A 412 11942 8035 12377 -3170 1434 281 C ATOM 437 CD GLU A 412 37.394 -16.168 -20.486 1.00103.93 C ANISOU 437 CD GLU A 412 14486 9834 15170 -3463 1700 19 C ATOM 438 OE1 GLU A 412 38.486 -15.877 -19.948 1.00110.37 O ANISOU 438 OE1 GLU A 412 15090 10836 16007 -3806 1751 -321 O ATOM 439 OE2 GLU A 412 36.431 -15.370 -20.539 1.00109.64 O ANISOU 439 OE2 GLU A 412 15497 10005 16157 -3223 1772 160 O ATOM 440 N GLY A 413 39.014 -22.038 -20.255 1.00 55.99 N ANISOU 440 N GLY A 413 7223 6531 7521 -2997 786 -163 N ATOM 441 CA GLY A 413 40.022 -22.973 -19.794 1.00 59.52 C ANISOU 441 CA GLY A 413 7355 7555 7706 -3057 705 -379 C ATOM 442 C GLY A 413 41.237 -23.040 -20.705 1.00 61.42 C ANISOU 442 C GLY A 413 7487 8023 7826 -3264 854 -264 C ATOM 443 O GLY A 413 41.124 -22.909 -21.933 1.00 63.06 O ANISOU 443 O GLY A 413 7906 8060 7993 -3208 951 90 O ATOM 444 N GLN A 414 42.406 -23.253 -20.111 1.00 54.44 N ANISOU 444 N GLN A 414 6256 7568 6860 -3477 874 -556 N ATOM 445 CA GLN A 414 43.638 -23.301 -20.892 1.00 63.35 C ANISOU 445 CA GLN A 414 7192 8972 7906 -3687 1056 -475 C ATOM 446 C GLN A 414 44.180 -24.723 -21.046 1.00 54.91 C ANISOU 446 C GLN A 414 5907 8486 6472 -3393 913 -454 C ATOM 447 O GLN A 414 44.057 -25.550 -20.141 1.00 51.74 O ANISOU 447 O GLN A 414 5366 8375 5916 -3166 687 -641 O ATOM 448 CB GLN A 414 44.712 -22.373 -20.305 1.00 78.63 C ANISOU 448 CB GLN A 414 8852 10948 10075 -4117 1201 -799 C ATOM 449 CG GLN A 414 45.466 -22.945 -19.105 1.00 92.37 C ANISOU 449 CG GLN A 414 10203 13235 11658 -4050 982 -1205 C ATOM 450 CD GLN A 414 46.879 -22.369 -18.963 1.00 98.85 C ANISOU 450 CD GLN A 414 10702 14251 12607 -4314 1081 -1413 C ATOM 451 OE1 GLN A 414 47.146 -21.236 -19.370 1.00104.05 O ANISOU 451 OE1 GLN A 414 11449 14507 13579 -4611 1298 -1363 O ATOM 452 NE2 GLN A 414 47.788 -23.158 -18.393 1.00 92.95 N ANISOU 452 NE2 GLN A 414 9573 14116 11628 -4193 920 -1625 N ATOM 453 N GLY A 415 44.767 -24.993 -22.208 1.00 52.63 N ANISOU 453 N GLY A 415 5624 8341 6034 -3370 1077 -207 N ATOM 454 CA GLY A 415 45.386 -26.270 -22.494 1.00 51.43 C ANISOU 454 CA GLY A 415 5288 8701 5550 -3081 1001 -189 C ATOM 455 C GLY A 415 44.491 -27.490 -22.376 1.00 60.45 C ANISOU 455 C GLY A 415 6623 9869 6476 -2613 715 -128 C ATOM 456 O GLY A 415 43.266 -27.426 -22.539 1.00 57.22 O ANISOU 456 O GLY A 415 6537 9073 6133 -2475 593 15 O ATOM 457 N CYS A 416 45.130 -28.619 -22.095 1.00 56.93 N ANISOU 457 N CYS A 416 5953 9881 5796 -2367 617 -234 N ATOM 458 CA CYS A 416 44.443 -29.878 -21.891 1.00 49.79 C ANISOU 458 CA CYS A 416 5205 8997 4716 -1951 379 -197 C ATOM 459 C CYS A 416 43.534 -29.820 -20.657 1.00 52.43 C ANISOU 459 C CYS A 416 5582 9152 5188 -1924 197 -321 C ATOM 460 O CYS A 416 43.948 -29.365 -19.596 1.00 49.74 O ANISOU 460 O CYS A 416 5003 8982 4915 -2085 189 -556 O ATOM 461 CB CYS A 416 45.470 -30.989 -21.699 1.00 47.57 C ANISOU 461 CB CYS A 416 4657 9230 4189 -1691 352 -295 C ATOM 462 SG CYS A 416 44.737 -32.537 -21.200 1.00 50.22 S ANISOU 462 SG CYS A 416 5180 9535 4365 -1212 97 -266 S ATOM 463 N PRO A 417 42.293 -30.306 -20.795 1.00 55.71 N ANISOU 463 N PRO A 417 6283 9252 5631 -1716 54 -179 N ATOM 464 CA PRO A 417 41.344 -30.306 -19.678 1.00 52.36 C ANISOU 464 CA PRO A 417 5897 8661 5337 -1664 -62 -255 C ATOM 465 C PRO A 417 41.822 -31.131 -18.487 1.00 51.71 C ANISOU 465 C PRO A 417 5617 8948 5084 -1483 -142 -409 C ATOM 466 O PRO A 417 41.311 -30.930 -17.399 1.00 57.36 O ANISOU 466 O PRO A 417 6315 9623 5855 -1482 -177 -512 O ATOM 467 CB PRO A 417 40.089 -30.939 -20.290 1.00 48.55 C ANISOU 467 CB PRO A 417 5688 7856 4904 -1460 -193 -51 C ATOM 468 CG PRO A 417 40.219 -30.669 -21.773 1.00 55.33 C ANISOU 468 CG PRO A 417 6712 8607 5703 -1498 -148 116 C ATOM 469 CD PRO A 417 41.677 -30.756 -22.058 1.00 51.28 C ANISOU 469 CD PRO A 417 6014 8475 4995 -1552 3 48 C ATOM 470 N PHE A 418 42.766 -32.046 -18.691 1.00 56.39 N ANISOU 470 N PHE A 418 6079 9900 5447 -1287 -157 -410 N ATOM 471 CA PHE A 418 43.323 -32.820 -17.580 1.00 52.63 C ANISOU 471 CA PHE A 418 5415 9811 4772 -1054 -241 -519 C ATOM 472 C PHE A 418 44.502 -32.124 -16.927 1.00 53.25 C ANISOU 472 C PHE A 418 5115 10332 4786 -1244 -222 -779 C ATOM 473 O PHE A 418 44.437 -31.764 -15.755 1.00 57.89 O ANISOU 473 O PHE A 418 5604 11050 5343 -1293 -293 -961 O ATOM 474 CB PHE A 418 43.738 -34.226 -18.037 1.00 59.80 C ANISOU 474 CB PHE A 418 6372 10875 5475 -674 -280 -394 C ATOM 475 CG PHE A 418 42.611 -35.205 -18.042 1.00 54.98 C ANISOU 475 CG PHE A 418 6078 9903 4908 -444 -356 -219 C ATOM 476 CD1 PHE A 418 41.728 -35.246 -19.101 1.00 47.76 C ANISOU 476 CD1 PHE A 418 5427 8584 4138 -508 -375 -98 C ATOM 477 CD2 PHE A 418 42.413 -36.065 -16.971 1.00 57.77 C ANISOU 477 CD2 PHE A 418 6460 10326 5164 -177 -409 -171 C ATOM 478 CE1 PHE A 418 40.664 -36.136 -19.105 1.00 51.20 C ANISOU 478 CE1 PHE A 418 6100 8682 4671 -359 -461 22 C ATOM 479 CE2 PHE A 418 41.346 -36.955 -16.966 1.00 54.41 C ANISOU 479 CE2 PHE A 418 6310 9520 4845 -28 -437 1 C ATOM 480 CZ PHE A 418 40.463 -36.983 -18.035 1.00 42.42 C ANISOU 480 CZ PHE A 418 5002 7590 3525 -148 -471 74 C ATOM 481 N CYS A 419 45.601 -31.990 -17.674 1.00 51.30 N ANISOU 481 N CYS A 419 4638 10354 4501 -1340 -126 -812 N ATOM 482 CA CYS A 419 46.842 -31.427 -17.121 1.00 54.46 C ANISOU 482 CA CYS A 419 4581 11241 4870 -1543 -122 -1082 C ATOM 483 C CYS A 419 47.100 -29.936 -17.413 1.00 58.56 C ANISOU 483 C CYS A 419 4981 11599 5669 -2093 35 -1230 C ATOM 484 O CYS A 419 48.069 -29.367 -16.922 1.00 62.17 O ANISOU 484 O CYS A 419 5055 12401 6167 -2339 33 -1500 O ATOM 485 CB CYS A 419 48.025 -32.271 -17.580 1.00 56.27 C ANISOU 485 CB CYS A 419 4520 11957 4903 -1288 -94 -1051 C ATOM 486 SG CYS A 419 48.266 -32.279 -19.382 1.00 59.69 S ANISOU 486 SG CYS A 419 5081 12214 5383 -1345 173 -822 S ATOM 487 N ARG A 420 46.221 -29.323 -18.204 1.00 63.37 N ANISOU 487 N ARG A 420 5940 11657 6482 -2262 165 -1047 N ATOM 488 CA AARG A 420 46.361 -27.920 -18.620 0.52 60.44 C ANISOU 488 CA AARG A 420 5560 11002 6404 -2749 365 -1101 C ATOM 489 CA BARG A 420 46.354 -27.926 -18.637 0.48 61.64 C ANISOU 489 CA BARG A 420 5716 11149 6555 -2747 366 -1097 C ATOM 490 C ARG A 420 47.649 -27.636 -19.409 1.00 62.03 C ANISOU 490 C ARG A 420 5435 11494 6638 -2994 586 -1098 C ATOM 491 O ARG A 420 48.091 -26.487 -19.507 1.00 61.47 O ANISOU 491 O ARG A 420 5290 11236 6828 -3398 755 -1195 O ATOM 492 CB AARG A 420 46.242 -26.976 -17.414 0.52 55.80 C ANISOU 492 CB AARG A 420 4877 10340 5982 -3034 294 -1445 C ATOM 493 CB BARG A 420 46.170 -26.959 -17.460 0.48 58.26 C ANISOU 493 CB BARG A 420 5217 10615 6303 -3032 300 -1427 C ATOM 494 CG AARG A 420 44.867 -26.998 -16.752 0.52 57.42 C ANISOU 494 CG AARG A 420 5430 10180 6208 -2841 177 -1419 C ATOM 495 CG BARG A 420 44.865 -27.178 -16.704 0.48 57.83 C ANISOU 495 CG BARG A 420 5475 10280 6218 -2783 154 -1409 C ATOM 496 CD AARG A 420 44.798 -26.134 -15.497 0.52 61.99 C ANISOU 496 CD AARG A 420 5951 10723 6880 -3040 121 -1797 C ATOM 497 CD BARG A 420 44.482 -25.987 -15.842 0.48 61.15 C ANISOU 497 CD BARG A 420 5951 10428 6854 -3076 173 -1702 C ATOM 498 NE AARG A 420 44.952 -24.710 -15.789 0.52 66.73 N ANISOU 498 NE AARG A 420 6643 10885 7828 -3424 312 -1890 N ATOM 499 NE BARG A 420 45.649 -25.346 -15.245 0.48 65.41 N ANISOU 499 NE BARG A 420 6235 11188 7431 -3265 182 -2014 N ATOM 500 CZ AARG A 420 45.983 -23.971 -15.386 0.52 66.10 C ANISOU 500 CZ AARG A 420 6359 10908 7849 -3649 347 -2157 C ATOM 501 CZ BARG A 420 46.374 -25.867 -14.261 0.48 61.81 C ANISOU 501 CZ BARG A 420 5528 11236 6719 -3074 14 -2229 C ATOM 502 NH1AARG A 420 46.951 -24.520 -14.666 0.52 63.92 N ANISOU 502 NH1AARG A 420 5759 11191 7335 -3519 194 -2360 N ATOM 503 NH1BARG A 420 46.065 -27.051 -13.754 0.48 63.91 N ANISOU 503 NH1BARG A 420 5793 11821 6671 -2669 -149 -2138 N ATOM 504 NH2AARG A 420 46.046 -22.684 -15.701 0.52 65.33 N ANISOU 504 NH2AARG A 420 6382 10339 8102 -3991 530 -2206 N ATOM 505 NH2BARG A 420 47.418 -25.207 -13.791 0.48 62.16 N ANISOU 505 NH2BARG A 420 5333 11452 6833 -3277 10 -2513 N ATOM 506 N CYS A 421 48.238 -28.680 -19.984 1.00 60.03 N ANISOU 506 N CYS A 421 5063 11607 6139 -2676 603 -966 N ATOM 507 CA CYS A 421 49.427 -28.529 -20.821 1.00 67.38 C ANISOU 507 CA CYS A 421 5672 12853 7074 -2841 864 -922 C ATOM 508 C CYS A 421 49.024 -28.091 -22.223 1.00 67.43 C ANISOU 508 C CYS A 421 6051 12444 7125 -2938 1139 -584 C ATOM 509 O CYS A 421 47.894 -28.328 -22.636 1.00 60.22 O ANISOU 509 O CYS A 421 5612 11126 6144 -2720 1047 -379 O ATOM 510 CB CYS A 421 50.239 -29.823 -20.876 1.00 69.77 C ANISOU 510 CB CYS A 421 5702 13728 7078 -2397 799 -926 C ATOM 511 SG CYS A 421 51.152 -30.175 -19.332 1.00103.16 S ANISOU 511 SG CYS A 421 9474 18500 11221 -2241 498 -1288 S ATOM 512 N GLU A 422 49.930 -27.432 -22.939 1.00 62.07 N ANISOU 512 N GLU A 422 5172 11848 6563 -3242 1460 -517 N ATOM 513 CA GLU A 422 49.649 -27.051 -24.319 1.00 65.24 C ANISOU 513 CA GLU A 422 5917 11950 6921 -3312 1772 -149 C ATOM 514 C GLU A 422 49.227 -28.269 -25.134 1.00 68.30 C ANISOU 514 C GLU A 422 6625 12411 6916 -2758 1683 54 C ATOM 515 O GLU A 422 49.814 -29.347 -25.029 1.00 59.61 O ANISOU 515 O GLU A 422 5299 11759 5589 -2420 1608 -47 O ATOM 516 CB GLU A 422 50.861 -26.380 -24.990 1.00 68.41 C ANISOU 516 CB GLU A 422 6096 12407 7489 -3539 2111 -79 C ATOM 517 CG GLU A 422 50.571 -25.912 -26.428 1.00 74.71 C ANISOU 517 CG GLU A 422 7302 12879 8205 -3574 2463 349 C ATOM 518 CD GLU A 422 51.811 -25.496 -27.211 1.00 87.75 C ANISOU 518 CD GLU A 422 8715 14668 9960 -3709 2858 478 C ATOM 519 OE1 GLU A 422 52.916 -25.462 -26.622 1.00 92.10 O ANISOU 519 OE1 GLU A 422 8750 15537 10708 -3840 2852 221 O ATOM 520 OE2 GLU A 422 51.676 -25.208 -28.423 1.00 90.48 O ANISOU 520 OE2 GLU A 422 9393 14815 10170 -3665 3174 853 O ATOM 521 N ILE A 423 48.219 -28.083 -25.973 1.00 67.58 N ANISOU 521 N ILE A 423 7063 11871 6744 -2655 1684 328 N ATOM 522 CA ILE A 423 47.790 -29.143 -26.859 1.00 58.37 C ANISOU 522 CA ILE A 423 6231 10739 5207 -2185 1589 480 C ATOM 523 C ILE A 423 48.560 -28.970 -28.164 1.00 61.85 C ANISOU 523 C ILE A 423 6708 11366 5426 -2198 1988 712 C ATOM 524 O ILE A 423 48.379 -27.985 -28.879 1.00 67.70 O ANISOU 524 O ILE A 423 7678 11821 6223 -2436 2231 975 O ATOM 525 CB ILE A 423 46.275 -29.045 -27.099 1.00 57.56 C ANISOU 525 CB ILE A 423 6641 10120 5111 -2054 1335 629 C ATOM 526 CG1 ILE A 423 45.535 -29.154 -25.752 1.00 56.22 C ANISOU 526 CG1 ILE A 423 6399 9785 5178 -2061 1016 414 C ATOM 527 CG2 ILE A 423 45.817 -30.106 -28.094 1.00 53.55 C ANISOU 527 CG2 ILE A 423 6485 9640 4222 -1616 1204 736 C ATOM 528 CD1 ILE A 423 44.051 -28.850 -25.814 1.00 47.34 C ANISOU 528 CD1 ILE A 423 5658 8161 4169 -2001 801 540 C ATOM 529 N LYS A 424 49.458 -29.907 -28.451 1.00 65.33 N ANISOU 529 N LYS A 424 6918 12293 5612 -1921 2094 629 N ATOM 530 CA LYS A 424 50.228 -29.854 -29.688 1.00 70.54 C ANISOU 530 CA LYS A 424 7600 13186 6015 -1869 2512 836 C ATOM 531 C LYS A 424 49.535 -30.654 -30.781 1.00 65.98 C ANISOU 531 C LYS A 424 7576 12513 4980 -1410 2415 975 C ATOM 532 O LYS A 424 49.890 -30.564 -31.958 1.00 75.56 O ANISOU 532 O LYS A 424 9006 13734 5969 -1277 2689 1163 O ATOM 533 CB LYS A 424 51.645 -30.384 -29.467 1.00 70.08 C ANISOU 533 CB LYS A 424 7006 13609 6013 -1742 2652 642 C ATOM 534 CG LYS A 424 52.440 -29.667 -28.387 1.00 79.75 C ANISOU 534 CG LYS A 424 7653 14967 7680 -2157 2658 437 C ATOM 535 CD LYS A 424 53.865 -30.221 -28.358 1.00 96.45 C ANISOU 535 CD LYS A 424 9256 17587 9805 -1976 2785 292 C ATOM 536 CE LYS A 424 54.711 -29.618 -27.251 1.00101.00 C ANISOU 536 CE LYS A 424 9251 18346 10779 -2334 2696 37 C ATOM 537 NZ LYS A 424 54.969 -28.174 -27.490 1.00105.50 N ANISOU 537 NZ LYS A 424 9778 18583 11724 -2892 2981 147 N ATOM 538 N GLY A 425 48.530 -31.421 -30.383 1.00 69.41 N ANISOU 538 N GLY A 425 7130 11163 8080 -2913 1146 2393 N ATOM 539 CA GLY A 425 47.767 -32.213 -31.321 1.00 68.92 C ANISOU 539 CA GLY A 425 7295 11504 7390 -2759 1523 2104 C ATOM 540 C GLY A 425 46.526 -32.810 -30.693 1.00 64.99 C ANISOU 540 C GLY A 425 7037 10952 6704 -2404 1169 1703 C ATOM 541 O GLY A 425 46.442 -32.999 -29.473 1.00 59.49 O ANISOU 541 O GLY A 425 6228 9970 6405 -2207 815 1565 O ATOM 542 N THR A 426 45.554 -33.098 -31.550 1.00 63.13 N ANISOU 542 N THR A 426 7140 10987 5861 -2316 1262 1538 N ATOM 543 CA THR A 426 44.320 -33.769 -31.166 1.00 59.90 C ANISOU 543 CA THR A 426 6894 10598 5269 -2027 1000 1180 C ATOM 544 C THR A 426 44.071 -34.884 -32.175 1.00 63.23 C ANISOU 544 C THR A 426 7364 11351 5308 -1973 1405 851 C ATOM 545 O THR A 426 43.850 -34.624 -33.366 1.00 63.97 O ANISOU 545 O THR A 426 7761 11672 4871 -2058 1573 926 O ATOM 546 CB THR A 426 43.134 -32.790 -31.200 1.00 63.14 C ANISOU 546 CB THR A 426 7741 10950 5298 -1956 503 1334 C ATOM 547 OG1 THR A 426 43.160 -32.044 -32.438 1.00 68.15 O ANISOU 547 OG1 THR A 426 8697 11755 5444 -2162 636 1583 O ATOM 548 CG2 THR A 426 43.218 -31.822 -30.040 1.00 56.62 C ANISOU 548 CG2 THR A 426 6951 9745 4818 -1888 9 1578 C ATOM 549 N GLU A 427 44.110 -36.120 -31.699 1.00 58.44 N ANISOU 549 N GLU A 427 6522 10737 4946 -1808 1525 484 N ATOM 550 CA GLU A 427 43.908 -37.280 -32.553 1.00 66.84 C ANISOU 550 CA GLU A 427 7666 12040 5690 -1723 1831 128 C ATOM 551 C GLU A 427 42.550 -37.912 -32.297 1.00 66.81 C ANISOU 551 C GLU A 427 7815 12003 5566 -1571 1475 -162 C ATOM 552 O GLU A 427 42.242 -38.290 -31.161 1.00 61.24 O ANISOU 552 O GLU A 427 6922 11094 5254 -1451 1256 -262 O ATOM 553 CB GLU A 427 45.008 -38.306 -32.312 1.00 68.42 C ANISOU 553 CB GLU A 427 7506 12245 6247 -1651 2238 -85 C ATOM 554 CG GLU A 427 46.402 -37.727 -32.463 1.00 88.25 C ANISOU 554 CG GLU A 427 9724 14800 9007 -1809 2601 230 C ATOM 555 CD GLU A 427 47.489 -38.699 -32.040 1.00100.54 C ANISOU 555 CD GLU A 427 10852 16342 11006 -1688 2935 18 C ATOM 556 OE1 GLU A 427 47.148 -39.733 -31.419 1.00104.97 O ANISOU 556 OE1 GLU A 427 11384 16777 11722 -1484 2808 -358 O ATOM 557 OE2 GLU A 427 48.678 -38.427 -32.330 1.00 99.76 O ANISOU 557 OE2 GLU A 427 10434 16357 11113 -1796 3324 244 O ATOM 558 N PRO A 428 41.721 -38.013 -33.349 1.00 67.10 N ANISOU 558 N PRO A 428 8196 12229 5071 -1570 1402 -276 N ATOM 559 CA PRO A 428 40.452 -38.731 -33.203 1.00 57.69 C ANISOU 559 CA PRO A 428 7075 11015 3830 -1468 1060 -555 C ATOM 560 C PRO A 428 40.744 -40.182 -32.845 1.00 61.03 C ANISOU 560 C PRO A 428 7292 11354 4542 -1385 1239 -918 C ATOM 561 O PRO A 428 41.702 -40.749 -33.368 1.00 66.92 O ANISOU 561 O PRO A 428 8030 12180 5218 -1364 1639 -1057 O ATOM 562 CB PRO A 428 39.832 -38.653 -34.610 1.00 61.66 C ANISOU 562 CB PRO A 428 8006 11726 3697 -1487 991 -642 C ATOM 563 CG PRO A 428 40.584 -37.548 -35.322 1.00 67.17 C ANISOU 563 CG PRO A 428 8909 12536 4076 -1589 1238 -301 C ATOM 564 CD PRO A 428 41.960 -37.562 -34.733 1.00 69.34 C ANISOU 564 CD PRO A 428 8818 12741 4787 -1652 1641 -160 C ATOM 565 N ILE A 429 39.953 -40.766 -31.951 1.00 60.45 N ANISOU 565 N ILE A 429 7061 11122 4786 -1319 967 -1046 N ATOM 566 CA ILE A 429 40.114 -42.174 -31.597 1.00 64.25 C ANISOU 566 CA ILE A 429 7407 11472 5532 -1256 1078 -1383 C ATOM 567 C ILE A 429 38.765 -42.845 -31.361 1.00 58.76 C ANISOU 567 C ILE A 429 6704 10699 4923 -1269 714 -1532 C ATOM 568 O ILE A 429 37.749 -42.175 -31.215 1.00 59.46 O ANISOU 568 O ILE A 429 6789 10841 4963 -1286 396 -1345 O ATOM 569 CB ILE A 429 41.039 -42.371 -30.368 1.00 65.67 C ANISOU 569 CB ILE A 429 7281 11440 6233 -1162 1252 -1341 C ATOM 570 CG1 ILE A 429 40.593 -41.492 -29.196 1.00 63.14 C ANISOU 570 CG1 ILE A 429 6836 10968 6186 -1096 977 -1042 C ATOM 571 CG2 ILE A 429 42.473 -42.046 -30.727 1.00 65.85 C ANISOU 571 CG2 ILE A 429 7222 11546 6254 -1174 1642 -1261 C ATOM 572 CD1 ILE A 429 39.567 -42.131 -28.321 1.00 60.83 C ANISOU 572 CD1 ILE A 429 6451 10528 6134 -1002 752 -1111 C ATOM 573 N VAL A 430 38.760 -44.172 -31.355 1.00 62.83 N ANISOU 573 N VAL A 430 7210 11086 5576 -1262 750 -1857 N ATOM 574 CA VAL A 430 37.561 -44.945 -31.072 1.00 53.98 C ANISOU 574 CA VAL A 430 6021 9842 4645 -1332 416 -1974 C ATOM 575 C VAL A 430 37.954 -46.026 -30.092 1.00 63.01 C ANISOU 575 C VAL A 430 6991 10715 6233 -1277 551 -2122 C ATOM 576 O VAL A 430 38.911 -46.768 -30.324 1.00 63.45 O ANISOU 576 O VAL A 430 7146 10695 6267 -1206 798 -2375 O ATOM 577 CB VAL A 430 36.981 -45.629 -32.329 1.00 59.73 C ANISOU 577 CB VAL A 430 7050 10618 5026 -1425 187 -2274 C ATOM 578 CG1 VAL A 430 35.657 -46.320 -31.992 1.00 61.93 C ANISOU 578 CG1 VAL A 430 7170 10753 5605 -1565 -229 -2325 C ATOM 579 CG2 VAL A 430 36.786 -44.623 -33.447 1.00 60.75 C ANISOU 579 CG2 VAL A 430 7463 11000 4618 -1430 95 -2173 C ATOM 580 N VAL A 431 37.222 -46.109 -28.989 1.00 56.64 N ANISOU 580 N VAL A 431 5945 9768 5808 -1270 408 -1950 N ATOM 581 CA VAL A 431 37.524 -47.081 -27.959 1.00 56.54 C ANISOU 581 CA VAL A 431 5811 9465 6207 -1200 529 -2041 C ATOM 582 C VAL A 431 36.522 -48.215 -28.024 1.00 58.36 C ANISOU 582 C VAL A 431 6020 9539 6614 -1374 288 -2187 C ATOM 583 O VAL A 431 35.318 -48.008 -27.901 1.00 64.33 O ANISOU 583 O VAL A 431 6607 10359 7475 -1487 37 -1992 O ATOM 584 CB VAL A 431 37.524 -46.432 -26.551 1.00 59.53 C ANISOU 584 CB VAL A 431 5987 9744 6888 -1015 586 -1717 C ATOM 585 CG1 VAL A 431 37.670 -47.490 -25.460 1.00 54.84 C ANISOU 585 CG1 VAL A 431 5324 8823 6689 -923 686 -1793 C ATOM 586 CG2 VAL A 431 38.641 -45.401 -26.463 1.00 50.01 C ANISOU 586 CG2 VAL A 431 4815 8605 5582 -876 751 -1597 C ATOM 587 N ASP A 432 37.031 -49.420 -28.226 1.00 60.89 N ANISOU 587 N ASP A 432 6504 9644 6989 -1393 347 -2521 N ATOM 588 CA ASP A 432 36.181 -50.590 -28.302 1.00 64.46 C ANISOU 588 CA ASP A 432 6982 9864 7646 -1596 71 -2674 C ATOM 589 C ASP A 432 36.053 -51.212 -26.932 1.00 61.34 C ANISOU 589 C ASP A 432 6399 9175 7731 -1567 171 -2531 C ATOM 590 O ASP A 432 37.043 -51.679 -26.372 1.00 66.42 O ANISOU 590 O ASP A 432 7141 9623 8474 -1386 410 -2667 O ATOM 591 CB ASP A 432 36.767 -51.601 -29.287 1.00 72.07 C ANISOU 591 CB ASP A 432 8324 10699 8360 -1595 23 -3131 C ATOM 592 CG ASP A 432 36.767 -51.084 -30.707 1.00 83.16 C ANISOU 592 CG ASP A 432 9995 12373 9230 -1593 -88 -3268 C ATOM 593 OD1 ASP A 432 35.891 -50.248 -31.028 1.00 82.87 O ANISOU 593 OD1 ASP A 432 9853 12543 9092 -1710 -310 -3054 O ATOM 594 OD2 ASP A 432 37.636 -51.511 -31.497 1.00 93.17 O ANISOU 594 OD2 ASP A 432 11598 13648 10154 -1434 56 -3585 O ATOM 595 N PRO A 433 34.826 -51.233 -26.392 1.00 65.71 N ANISOU 595 N PRO A 433 6680 9703 8586 -1726 -3 -2243 N ATOM 596 CA PRO A 433 34.596 -51.779 -25.050 1.00 63.95 C ANISOU 596 CA PRO A 433 6291 9213 8794 -1679 142 -2029 C ATOM 597 C PRO A 433 35.076 -53.220 -24.960 1.00 68.20 C ANISOU 597 C PRO A 433 7067 9346 9499 -1752 137 -2341 C ATOM 598 O PRO A 433 35.206 -53.896 -25.978 1.00 68.02 O ANISOU 598 O PRO A 433 7293 9243 9311 -1898 -80 -2696 O ATOM 599 CB PRO A 433 33.074 -51.728 -24.908 1.00 62.20 C ANISOU 599 CB PRO A 433 5719 9079 8836 -1913 -80 -1704 C ATOM 600 CG PRO A 433 32.647 -50.622 -25.815 1.00 67.61 C ANISOU 600 CG PRO A 433 6340 10151 9197 -1930 -274 -1652 C ATOM 601 CD PRO A 433 33.597 -50.675 -26.984 1.00 69.17 C ANISOU 601 CD PRO A 433 6929 10383 8969 -1917 -317 -2067 C ATOM 602 N PHE A 434 35.360 -53.670 -23.745 1.00 68.44 N ANISOU 602 N PHE A 434 7089 9102 9813 -1602 355 -2219 N ATOM 603 CA PHE A 434 35.814 -55.032 -23.517 1.00 74.50 C ANISOU 603 CA PHE A 434 8119 9439 10747 -1636 345 -2489 C ATOM 604 C PHE A 434 34.649 -56.013 -23.615 1.00 86.22 C ANISOU 604 C PHE A 434 9525 10679 12556 -2041 53 -2406 C ATOM 605 O PHE A 434 34.634 -56.878 -24.487 1.00 86.33 O ANISOU 605 O PHE A 434 9785 10503 12514 -2249 -249 -2745 O ATOM 606 CB PHE A 434 36.511 -55.142 -22.161 1.00 62.13 C ANISOU 606 CB PHE A 434 6617 7635 9355 -1310 650 -2376 C ATOM 607 CG PHE A 434 37.067 -56.504 -21.868 1.00 62.54 C ANISOU 607 CG PHE A 434 6990 7223 9549 -1287 639 -2664 C ATOM 608 CD1 PHE A 434 38.228 -56.939 -22.484 1.00 76.66 C ANISOU 608 CD1 PHE A 434 9076 8943 11108 -1117 640 -3133 C ATOM 609 CD2 PHE A 434 36.434 -57.349 -20.975 1.00 65.94 C ANISOU 609 CD2 PHE A 434 7433 7286 10333 -1410 645 -2446 C ATOM 610 CE1 PHE A 434 38.744 -58.198 -22.219 1.00 80.09 C ANISOU 610 CE1 PHE A 434 9846 8938 11645 -1044 597 -3422 C ATOM 611 CE2 PHE A 434 36.947 -58.606 -20.700 1.00 71.05 C ANISOU 611 CE2 PHE A 434 8439 7463 11093 -1383 602 -2711 C ATOM 612 CZ PHE A 434 38.102 -59.031 -21.323 1.00 74.41 C ANISOU 612 CZ PHE A 434 9190 7811 11270 -1186 554 -3220 C ATOM 613 N ASP A 435 33.689 -55.880 -22.703 1.00104.92 N ANISOU 613 N ASP A 435 11556 13038 15269 -2133 140 -1939 N ATOM 614 CA ASP A 435 32.506 -56.746 -22.665 1.00125.99 C ANISOU 614 CA ASP A 435 14025 15486 18359 -2564 -103 -1743 C ATOM 615 C ASP A 435 32.844 -58.209 -22.360 1.00132.48 C ANISOU 615 C ASP A 435 15183 15748 19407 -2695 -174 -1945 C ATOM 616 O ASP A 435 32.367 -58.778 -21.373 1.00132.04 O ANISOU 616 O ASP A 435 15014 15420 19733 -2796 -29 -1611 O ATOM 617 CB ASP A 435 31.708 -56.647 -23.971 1.00135.00 C ANISOU 617 CB ASP A 435 15040 16810 19442 -2914 -572 -1867 C ATOM 618 CG ASP A 435 31.198 -55.243 -24.235 1.00134.72 C ANISOU 618 CG ASP A 435 14671 17299 19218 -2806 -545 -1624 C ATOM 619 OD1 ASP A 435 30.998 -54.487 -23.258 1.00130.49 O ANISOU 619 OD1 ASP A 435 13868 16953 18759 -2566 -211 -1223 O ATOM 620 OD2 ASP A 435 31.001 -54.896 -25.421 1.00136.80 O ANISOU 620 OD2 ASP A 435 14996 17762 19220 -2920 -877 -1842 O TER 621 ASP A 435 ATOM 622 N ALA B 2 25.905 -31.154 -16.219 1.00 38.07 N ANISOU 622 N ALA B 2 5144 4995 4327 -819 -695 251 N ATOM 623 CA ALA B 2 26.584 -31.269 -14.923 1.00 33.02 C ANISOU 623 CA ALA B 2 4302 4381 3864 -881 -589 179 C ATOM 624 C ALA B 2 26.093 -32.467 -14.111 1.00 33.94 C ANISOU 624 C ALA B 2 4235 4607 4054 -841 -626 55 C ATOM 625 O ALA B 2 26.863 -33.090 -13.392 1.00 34.42 O ANISOU 625 O ALA B 2 4174 4727 4176 -886 -525 10 O ATOM 626 CB ALA B 2 26.424 -29.981 -14.129 1.00 32.74 C ANISOU 626 CB ALA B 2 4263 4216 3961 -878 -630 195 C ATOM 627 N LEU B 3 24.806 -32.792 -14.238 1.00 36.92 N ANISOU 627 N LEU B 3 4590 5009 4427 -762 -777 9 N ATOM 628 CA LEU B 3 24.206 -33.866 -13.460 1.00 36.88 C ANISOU 628 CA LEU B 3 4429 5084 4502 -757 -793 -101 C ATOM 629 C LEU B 3 24.983 -35.191 -13.557 1.00 37.70 C ANISOU 629 C LEU B 3 4537 5241 4549 -810 -669 -140 C ATOM 630 O LEU B 3 25.205 -35.867 -12.558 1.00 33.40 O ANISOU 630 O LEU B 3 3886 4720 4084 -822 -605 -187 O ATOM 631 CB LEU B 3 22.737 -34.073 -13.871 1.00 32.39 C ANISOU 631 CB LEU B 3 3818 4551 3938 -700 -970 -146 C ATOM 632 CG LEU B 3 21.973 -35.230 -13.195 1.00 33.41 C ANISOU 632 CG LEU B 3 3789 4753 4154 -738 -970 -261 C ATOM 633 CD1 LEU B 3 20.432 -34.988 -13.099 1.00 34.28 C ANISOU 633 CD1 LEU B 3 3735 4910 4380 -682 -1128 -313 C ATOM 634 CD2 LEU B 3 22.249 -36.552 -13.881 1.00 36.36 C ANISOU 634 CD2 LEU B 3 4253 5153 4410 -817 -935 -308 C ATOM 635 N LYS B 4 25.395 -35.565 -14.758 1.00 34.11 N ANISOU 635 N LYS B 4 4230 4789 3941 -827 -628 -117 N ATOM 636 CA LYS B 4 26.012 -36.862 -14.940 1.00 29.80 C ANISOU 636 CA LYS B 4 3710 4264 3349 -843 -500 -172 C ATOM 637 C LYS B 4 27.356 -36.939 -14.236 1.00 32.83 C ANISOU 637 C LYS B 4 3989 4663 3824 -838 -336 -140 C ATOM 638 O LYS B 4 27.732 -37.981 -13.687 1.00 30.70 O ANISOU 638 O LYS B 4 3656 4401 3609 -807 -263 -180 O ATOM 639 CB LYS B 4 26.143 -37.191 -16.428 1.00 36.06 C ANISOU 639 CB LYS B 4 4721 5050 3929 -858 -469 -176 C ATOM 640 CG LYS B 4 24.816 -37.552 -17.065 1.00 37.24 C ANISOU 640 CG LYS B 4 4956 5214 3981 -876 -672 -245 C ATOM 641 CD LYS B 4 24.329 -38.897 -16.496 1.00 50.91 C ANISOU 641 CD LYS B 4 6610 6938 5795 -913 -669 -370 C ATOM 642 CE LYS B 4 22.976 -39.333 -17.074 1.00 51.45 C ANISOU 642 CE LYS B 4 6713 7036 5801 -979 -883 -465 C ATOM 643 NZ LYS B 4 22.913 -39.233 -18.564 1.00 60.56 N ANISOU 643 NZ LYS B 4 8115 8203 6691 -998 -976 -470 N ATOM 644 N ARG B 5 28.076 -35.831 -14.263 1.00 29.59 N ANISOU 644 N ARG B 5 3559 4247 3438 -871 -290 -61 N ATOM 645 CA ARG B 5 29.353 -35.751 -13.597 1.00 36.24 C ANISOU 645 CA ARG B 5 4252 5130 4389 -891 -174 -35 C ATOM 646 C ARG B 5 29.158 -35.724 -12.066 1.00 35.79 C ANISOU 646 C ARG B 5 4047 5092 4459 -883 -271 -66 C ATOM 647 O ARG B 5 29.850 -36.428 -11.350 1.00 30.87 O ANISOU 647 O ARG B 5 3308 4521 3901 -848 -234 -75 O ATOM 648 CB ARG B 5 30.144 -34.534 -14.085 1.00 31.52 C ANISOU 648 CB ARG B 5 3677 4512 3788 -982 -92 48 C ATOM 649 CG ARG B 5 31.424 -34.316 -13.314 1.00 34.30 C ANISOU 649 CG ARG B 5 3816 4929 4287 -1041 -12 62 C ATOM 650 CD ARG B 5 32.345 -35.530 -13.396 1.00 43.06 C ANISOU 650 CD ARG B 5 4796 6129 5436 -961 125 41 C ATOM 651 NE ARG B 5 33.538 -35.298 -12.589 1.00 39.81 N ANISOU 651 NE ARG B 5 4125 5810 5189 -1004 147 57 N ATOM 652 CZ ARG B 5 34.583 -34.573 -12.981 1.00 34.51 C ANISOU 652 CZ ARG B 5 3340 5183 4588 -1124 281 101 C ATOM 653 NH1 ARG B 5 34.610 -34.032 -14.186 1.00 35.62 N ANISOU 653 NH1 ARG B 5 3647 5265 4623 -1204 439 149 N ATOM 654 NH2 ARG B 5 35.604 -34.382 -12.162 1.00 36.54 N ANISOU 654 NH2 ARG B 5 3320 5548 5015 -1180 253 100 N ATOM 655 N ILE B 6 28.203 -34.935 -11.578 1.00 35.22 N ANISOU 655 N ILE B 6 3997 4976 4411 -896 -390 -83 N ATOM 656 CA ILE B 6 27.929 -34.901 -10.141 1.00 33.36 C ANISOU 656 CA ILE B 6 3669 4754 4252 -893 -452 -128 C ATOM 657 C ILE B 6 27.515 -36.297 -9.642 1.00 36.83 C ANISOU 657 C ILE B 6 4087 5224 4683 -841 -443 -168 C ATOM 658 O ILE B 6 27.931 -36.726 -8.568 1.00 32.44 O ANISOU 658 O ILE B 6 3473 4702 4153 -829 -442 -169 O ATOM 659 CB ILE B 6 26.853 -33.842 -9.779 1.00 35.56 C ANISOU 659 CB ILE B 6 3985 4964 4561 -889 -539 -159 C ATOM 660 CG1 ILE B 6 27.388 -32.434 -10.053 1.00 37.66 C ANISOU 660 CG1 ILE B 6 4312 5150 4849 -949 -537 -113 C ATOM 661 CG2 ILE B 6 26.371 -34.006 -8.307 1.00 26.73 C ANISOU 661 CG2 ILE B 6 2807 3865 3482 -879 -559 -229 C ATOM 662 CD1 ILE B 6 26.307 -31.367 -10.085 1.00 34.89 C ANISOU 662 CD1 ILE B 6 4044 4686 4529 -894 -613 -123 C ATOM 663 N HIS B 7 26.701 -36.987 -10.445 1.00 36.26 N ANISOU 663 N HIS B 7 4087 5129 4562 -824 -446 -198 N ATOM 664 CA HIS B 7 26.236 -38.337 -10.148 1.00 26.62 C ANISOU 664 CA HIS B 7 2884 3894 3337 -811 -419 -241 C ATOM 665 C HIS B 7 27.392 -39.323 -10.028 1.00 40.07 C ANISOU 665 C HIS B 7 4593 5593 5039 -754 -322 -209 C ATOM 666 O HIS B 7 27.400 -40.125 -9.111 1.00 28.95 O ANISOU 666 O HIS B 7 3184 4164 3653 -726 -306 -201 O ATOM 667 CB HIS B 7 25.233 -38.790 -11.221 1.00 30.19 C ANISOU 667 CB HIS B 7 3416 4321 3734 -841 -463 -297 C ATOM 668 CG HIS B 7 25.056 -40.284 -11.332 1.00 39.50 C ANISOU 668 CG HIS B 7 4671 5446 4892 -860 -403 -350 C ATOM 669 ND1 HIS B 7 24.292 -41.024 -10.460 1.00 34.61 N ANISOU 669 ND1 HIS B 7 4026 4793 4330 -909 -391 -387 N ATOM 670 CD2 HIS B 7 25.504 -41.162 -12.257 1.00 36.54 C ANISOU 670 CD2 HIS B 7 4426 5018 4438 -848 -333 -381 C ATOM 671 CE1 HIS B 7 24.278 -42.290 -10.830 1.00 28.58 C ANISOU 671 CE1 HIS B 7 3381 3940 3536 -937 -329 -432 C ATOM 672 NE2 HIS B 7 25.020 -42.403 -11.909 1.00 42.86 N ANISOU 672 NE2 HIS B 7 5290 5734 5263 -889 -294 -438 N ATOM 673 N LYS B 8 28.367 -39.246 -10.938 1.00 28.45 N ANISOU 673 N LYS B 8 3131 4136 3542 -725 -245 -181 N ATOM 674 CA LYS B 8 29.544 -40.106 -10.864 1.00 35.70 C ANISOU 674 CA LYS B 8 4007 5060 4497 -630 -138 -152 C ATOM 675 C LYS B 8 30.435 -39.774 -9.652 1.00 30.68 C ANISOU 675 C LYS B 8 3204 4502 3951 -598 -189 -91 C ATOM 676 O LYS B 8 30.958 -40.671 -9.008 1.00 38.36 O ANISOU 676 O LYS B 8 4142 5469 4962 -495 -182 -57 O ATOM 677 CB LYS B 8 30.367 -40.082 -12.168 1.00 29.68 C ANISOU 677 CB LYS B 8 3276 4309 3692 -605 5 -150 C ATOM 678 CG LYS B 8 31.591 -40.941 -12.059 1.00 33.45 C ANISOU 678 CG LYS B 8 3660 4800 4249 -470 136 -127 C ATOM 679 CD LYS B 8 32.085 -41.496 -13.377 1.00 39.99 C ANISOU 679 CD LYS B 8 4595 5591 5010 -412 338 -171 C ATOM 680 CE LYS B 8 33.317 -42.361 -13.151 1.00 39.76 C ANISOU 680 CE LYS B 8 4428 5572 5109 -228 479 -149 C ATOM 681 NZ LYS B 8 34.423 -41.511 -12.577 1.00 44.25 N ANISOU 681 NZ LYS B 8 4689 6298 5825 -233 459 -69 N ATOM 682 N GLU B 9 30.586 -38.491 -9.341 1.00 29.44 N ANISOU 682 N GLU B 9 2964 4402 3818 -688 -259 -78 N ATOM 683 CA GLU B 9 31.272 -38.076 -8.107 1.00 30.55 C ANISOU 683 CA GLU B 9 2972 4621 4015 -701 -356 -49 C ATOM 684 C GLU B 9 30.682 -38.731 -6.841 1.00 28.39 C ANISOU 684 C GLU B 9 2763 4327 3695 -659 -439 -49 C ATOM 685 O GLU B 9 31.412 -39.233 -5.989 1.00 30.44 O ANISOU 685 O GLU B 9 2959 4639 3966 -586 -501 2 O ATOM 686 CB GLU B 9 31.258 -36.544 -7.974 1.00 29.13 C ANISOU 686 CB GLU B 9 2764 4453 3850 -838 -416 -68 C ATOM 687 CG GLU B 9 32.063 -35.802 -9.075 1.00 41.05 C ANISOU 687 CG GLU B 9 4216 5977 5404 -912 -316 -39 C ATOM 688 CD GLU B 9 33.577 -35.920 -8.900 1.00 44.15 C ANISOU 688 CD GLU B 9 4378 6490 5908 -916 -284 -3 C ATOM 689 OE1 GLU B 9 34.051 -36.091 -7.754 1.00 52.47 O ANISOU 689 OE1 GLU B 9 5307 7624 7005 -897 -414 -3 O ATOM 690 OE2 GLU B 9 34.305 -35.825 -9.910 1.00 43.82 O ANISOU 690 OE2 GLU B 9 4268 6473 5907 -938 -128 25 O ATOM 691 N LEU B 10 29.359 -38.714 -6.719 1.00 31.13 N ANISOU 691 N LEU B 10 3232 4606 3989 -705 -438 -97 N ATOM 692 CA LEU B 10 28.711 -39.362 -5.582 1.00 33.33 C ANISOU 692 CA LEU B 10 3595 4856 4213 -693 -458 -95 C ATOM 693 C LEU B 10 29.003 -40.869 -5.563 1.00 36.36 C ANISOU 693 C LEU B 10 4049 5177 4590 -588 -403 -38 C ATOM 694 O LEU B 10 29.359 -41.408 -4.530 1.00 34.80 O ANISOU 694 O LEU B 10 3891 4983 4349 -527 -448 29 O ATOM 695 CB LEU B 10 27.206 -39.078 -5.564 1.00 28.09 C ANISOU 695 CB LEU B 10 2997 4144 3533 -769 -429 -167 C ATOM 696 CG LEU B 10 26.518 -39.553 -4.275 1.00 32.47 C ANISOU 696 CG LEU B 10 3635 4680 4023 -791 -401 -169 C ATOM 697 CD1 LEU B 10 27.156 -38.889 -3.002 1.00 29.13 C ANISOU 697 CD1 LEU B 10 3223 4325 3520 -795 -482 -153 C ATOM 698 CD2 LEU B 10 24.990 -39.322 -4.372 1.00 33.81 C ANISOU 698 CD2 LEU B 10 3799 4821 4225 -865 -337 -252 C ATOM 699 N ASN B 11 28.878 -41.544 -6.709 1.00 32.78 N ANISOU 699 N ASN B 11 3642 4650 4162 -560 -311 -62 N ATOM 700 CA ASN B 11 29.310 -42.951 -6.803 1.00 33.60 C ANISOU 700 CA ASN B 11 3837 4654 4278 -439 -237 -19 C ATOM 701 C ASN B 11 30.771 -43.186 -6.420 1.00 34.03 C ANISOU 701 C ASN B 11 3775 4769 4387 -275 -271 72 C ATOM 702 O ASN B 11 31.072 -44.146 -5.720 1.00 35.50 O ANISOU 702 O ASN B 11 4036 4885 4566 -151 -285 152 O ATOM 703 CB ASN B 11 29.062 -43.546 -8.202 1.00 32.15 C ANISOU 703 CB ASN B 11 3744 4375 4095 -441 -125 -93 C ATOM 704 CG ASN B 11 27.587 -43.759 -8.492 1.00 36.25 C ANISOU 704 CG ASN B 11 4379 4821 4574 -590 -122 -179 C ATOM 705 OD1 ASN B 11 26.782 -43.858 -7.575 1.00 41.88 O ANISOU 705 OD1 ASN B 11 5117 5514 5280 -665 -145 -172 O ATOM 706 ND2 ASN B 11 27.231 -43.846 -9.777 1.00 35.97 N ANISOU 706 ND2 ASN B 11 4409 4755 4505 -640 -91 -265 N ATOM 707 N ASP B 12 31.671 -42.338 -6.926 1.00 30.95 N ANISOU 707 N ASP B 12 3196 4503 4062 -273 -281 67 N ATOM 708 CA ASP B 12 33.095 -42.460 -6.641 1.00 32.72 C ANISOU 708 CA ASP B 12 3224 4826 4382 -132 -321 140 C ATOM 709 C ASP B 12 33.404 -42.355 -5.129 1.00 38.48 C ANISOU 709 C ASP B 12 3909 5637 5076 -105 -520 218 C ATOM 710 O ASP B 12 34.329 -42.987 -4.632 1.00 38.46 O ANISOU 710 O ASP B 12 3812 5673 5127 71 -595 307 O ATOM 711 CB ASP B 12 33.910 -41.389 -7.394 1.00 32.98 C ANISOU 711 CB ASP B 12 3042 4991 4499 -207 -281 112 C ATOM 712 CG ASP B 12 33.969 -41.622 -8.902 1.00 48.03 C ANISOU 712 CG ASP B 12 4996 6838 6413 -190 -68 60 C ATOM 713 OD1 ASP B 12 33.606 -42.724 -9.374 1.00 47.35 O ANISOU 713 OD1 ASP B 12 5082 6617 6291 -89 39 34 O ATOM 714 OD2 ASP B 12 34.375 -40.683 -9.623 1.00 51.89 O ANISOU 714 OD2 ASP B 12 5386 7404 6927 -295 2 41 O ATOM 715 N LEU B 13 32.646 -41.532 -4.417 1.00 36.41 N ANISOU 715 N LEU B 13 3719 5401 4713 -264 -609 180 N ATOM 716 CA LEU B 13 32.820 -41.382 -2.968 1.00 43.09 C ANISOU 716 CA LEU B 13 4592 6319 5462 -266 -790 232 C ATOM 717 C LEU B 13 32.307 -42.607 -2.223 1.00 41.43 C ANISOU 717 C LEU B 13 4615 5985 5143 -163 -778 318 C ATOM 718 O LEU B 13 32.860 -42.979 -1.213 1.00 40.78 O ANISOU 718 O LEU B 13 4562 5946 4986 -62 -927 419 O ATOM 719 CB LEU B 13 32.139 -40.111 -2.472 1.00 42.94 C ANISOU 719 CB LEU B 13 4617 6340 5358 -463 -842 140 C ATOM 720 CG LEU B 13 32.902 -38.838 -2.855 1.00 41.75 C ANISOU 720 CG LEU B 13 4262 6299 5301 -576 -902 82 C ATOM 721 CD1 LEU B 13 31.962 -37.650 -2.816 1.00 42.61 C ANISOU 721 CD1 LEU B 13 4472 6359 5361 -743 -873 -23 C ATOM 722 CD2 LEU B 13 34.125 -38.624 -1.957 1.00 42.10 C ANISOU 722 CD2 LEU B 13 4142 6501 5353 -563 -1117 123 C ATOM 723 N ALA B 14 31.266 -43.248 -2.748 1.00 39.99 N ANISOU 723 N ALA B 14 4604 5641 4948 -198 -610 285 N ATOM 724 CA ALA B 14 30.785 -44.510 -2.196 1.00 45.98 C ANISOU 724 CA ALA B 14 5606 6237 5629 -129 -552 370 C ATOM 725 C ALA B 14 31.759 -45.672 -2.457 1.00 45.89 C ANISOU 725 C ALA B 14 5601 6135 5702 116 -545 476 C ATOM 726 O ALA B 14 31.993 -46.498 -1.580 1.00 48.47 O ANISOU 726 O ALA B 14 6081 6380 5953 248 -608 612 O ATOM 727 CB ALA B 14 29.399 -44.839 -2.765 1.00 48.60 C ANISOU 727 CB ALA B 14 6081 6427 5958 -277 -375 280 C ATOM 728 N ARG B 15 32.308 -45.740 -3.670 1.00 41.60 N ANISOU 728 N ARG B 15 4913 5591 5303 190 -454 418 N ATOM 729 CA ARG B 15 33.261 -46.787 -4.050 1.00 43.81 C ANISOU 729 CA ARG B 15 5173 5779 5695 453 -403 490 C ATOM 730 C ARG B 15 34.577 -46.663 -3.292 1.00 51.13 C ANISOU 730 C ARG B 15 5878 6870 6681 650 -603 612 C ATOM 731 O ARG B 15 35.119 -47.652 -2.788 1.00 51.19 O ANISOU 731 O ARG B 15 5959 6782 6708 895 -660 747 O ATOM 732 CB ARG B 15 33.561 -46.723 -5.548 1.00 53.74 C ANISOU 732 CB ARG B 15 6321 7028 7070 468 -227 374 C ATOM 733 CG ARG B 15 32.490 -47.312 -6.441 1.00 60.19 C ANISOU 733 CG ARG B 15 7388 7643 7839 354 -48 264 C ATOM 734 CD ARG B 15 32.671 -48.801 -6.556 1.00 69.91 C ANISOU 734 CD ARG B 15 8836 8618 9108 550 68 304 C ATOM 735 NE ARG B 15 31.435 -49.443 -6.973 1.00 78.33 N ANISOU 735 NE ARG B 15 10192 9469 10101 376 184 210 N ATOM 736 CZ ARG B 15 31.279 -50.754 -7.095 1.00 87.15 C ANISOU 736 CZ ARG B 15 11582 10299 11231 463 305 214 C ATOM 737 NH1 ARG B 15 32.290 -51.572 -6.830 1.00 89.68 N ANISOU 737 NH1 ARG B 15 11935 10501 11638 771 331 325 N ATOM 738 NH2 ARG B 15 30.110 -51.244 -7.482 1.00 95.98 N ANISOU 738 NH2 ARG B 15 12935 11242 12293 242 392 106 N ATOM 739 N ASP B 16 35.093 -45.438 -3.230 1.00 57.18 N ANISOU 739 N ASP B 16 6371 7874 7482 539 -721 565 N ATOM 740 CA ASP B 16 36.401 -45.180 -2.635 1.00 61.58 C ANISOU 740 CA ASP B 16 6638 8633 8126 679 -935 649 C ATOM 741 C ASP B 16 36.339 -44.003 -1.667 1.00 57.26 C ANISOU 741 C ASP B 16 6031 8270 7457 471 -1160 624 C ATOM 742 O ASP B 16 36.720 -42.886 -2.012 1.00 57.12 O ANISOU 742 O ASP B 16 5780 8408 7518 309 -1185 532 O ATOM 743 CB ASP B 16 37.437 -44.923 -3.735 1.00 64.72 C ANISOU 743 CB ASP B 16 6691 9145 8754 754 -819 593 C ATOM 744 CG ASP B 16 37.560 -46.093 -4.720 1.00 74.10 C ANISOU 744 CG ASP B 16 7966 10141 10048 977 -568 590 C ATOM 745 OD1 ASP B 16 38.103 -47.149 -4.320 1.00 78.85 O ANISOU 745 OD1 ASP B 16 8588 10656 10713 1272 -614 707 O ATOM 746 OD2 ASP B 16 37.130 -45.956 -5.893 1.00 72.79 O ANISOU 746 OD2 ASP B 16 7868 9899 9890 869 -331 470 O ATOM 747 N PRO B 17 35.829 -44.245 -0.452 1.00 58.71 N ANISOU 747 N PRO B 17 6465 8413 7429 460 -1302 700 N ATOM 748 CA PRO B 17 35.693 -43.169 0.535 1.00 63.88 C ANISOU 748 CA PRO B 17 7133 9217 7923 261 -1498 653 C ATOM 749 C PRO B 17 37.062 -42.587 0.880 1.00 72.58 C ANISOU 749 C PRO B 17 7888 10567 9122 295 -1767 668 C ATOM 750 O PRO B 17 37.983 -43.341 1.203 1.00 66.83 O ANISOU 750 O PRO B 17 7032 9901 8458 541 -1929 802 O ATOM 751 CB PRO B 17 35.116 -43.886 1.763 1.00 62.96 C ANISOU 751 CB PRO B 17 7373 9002 7549 318 -1580 772 C ATOM 752 CG PRO B 17 34.504 -45.138 1.235 1.00 64.50 C ANISOU 752 CG PRO B 17 7783 8945 7781 441 -1349 839 C ATOM 753 CD PRO B 17 35.350 -45.539 0.062 1.00 66.18 C ANISOU 753 CD PRO B 17 7735 9151 8261 619 -1263 832 C ATOM 754 N PRO B 18 37.199 -41.254 0.826 1.00 74.49 N ANISOU 754 N PRO B 18 7972 10943 9386 48 -1824 533 N ATOM 755 CA PRO B 18 38.504 -40.665 1.134 1.00 73.65 C ANISOU 755 CA PRO B 18 7507 11080 9396 22 -2084 527 C ATOM 756 C PRO B 18 38.840 -40.898 2.598 1.00 82.20 C ANISOU 756 C PRO B 18 8695 12274 10263 91 -2438 618 C ATOM 757 O PRO B 18 37.953 -41.200 3.408 1.00 72.79 O ANISOU 757 O PRO B 18 7895 10967 8794 84 -2445 656 O ATOM 758 CB PRO B 18 38.295 -39.166 0.878 1.00 76.10 C ANISOU 758 CB PRO B 18 7759 11433 9723 -308 -2043 353 C ATOM 759 CG PRO B 18 37.028 -39.067 0.089 1.00 71.84 C ANISOU 759 CG PRO B 18 7466 10681 9148 -382 -1731 287 C ATOM 760 CD PRO B 18 36.190 -40.235 0.502 1.00 69.93 C ANISOU 760 CD PRO B 18 7534 10290 8747 -213 -1666 383 C ATOM 761 N ALA B 19 40.121 -40.772 2.929 1.00 89.78 N ANISOU 761 N ALA B 19 9301 13467 11344 155 -2730 657 N ATOM 762 CA ALA B 19 40.551 -40.910 4.303 1.00 87.74 C ANISOU 762 CA ALA B 19 9123 13352 10863 213 -3133 742 C ATOM 763 C ALA B 19 40.225 -39.619 5.029 1.00 78.32 C ANISOU 763 C ALA B 19 8072 12232 9455 -138 -3272 570 C ATOM 764 O ALA B 19 40.660 -38.538 4.616 1.00 81.02 O ANISOU 764 O ALA B 19 8147 12677 9961 -383 -3280 416 O ATOM 765 CB ALA B 19 42.049 -41.205 4.367 1.00 95.07 C ANISOU 765 CB ALA B 19 9567 14532 12026 407 -3432 834 C ATOM 766 N GLN B 20 39.450 -39.745 6.104 1.00 69.68 N ANISOU 766 N GLN B 20 7427 11062 7988 -166 -3352 593 N ATOM 767 CA GLN B 20 39.148 -38.625 7.001 1.00 72.55 C ANISOU 767 CA GLN B 20 7998 11483 8083 -462 -3501 424 C ATOM 768 C GLN B 20 38.356 -37.499 6.334 1.00 61.46 C ANISOU 768 C GLN B 20 6648 9944 6761 -737 -3194 212 C ATOM 769 O GLN B 20 38.379 -36.358 6.796 1.00 62.65 O ANISOU 769 O GLN B 20 6863 10123 6819 -986 -3279 25 O ATOM 770 CB GLN B 20 40.440 -38.064 7.611 1.00 71.40 C ANISOU 770 CB GLN B 20 7598 11535 7995 -489 -3812 315 C ATOM 771 CG GLN B 20 41.149 -39.018 8.568 1.00 80.04 C ANISOU 771 CG GLN B 20 8724 12761 8928 -203 -4133 482 C ATOM 772 CD GLN B 20 42.290 -38.354 9.338 1.00 96.87 C ANISOU 772 CD GLN B 20 10650 15109 11047 -263 -4449 327 C ATOM 773 OE1 GLN B 20 42.268 -38.285 10.571 1.00 99.92 O ANISOU 773 OE1 GLN B 20 11318 15573 11072 -271 -4667 310 O ATOM 774 NE2 GLN B 20 43.295 -37.872 8.613 1.00103.42 N ANISOU 774 NE2 GLN B 20 10989 16044 12263 -318 -4464 213 N ATOM 775 N CYS B 21 37.644 -37.847 5.266 1.00 50.53 N ANISOU 775 N CYS B 21 5273 8378 5548 -663 -2826 233 N ATOM 776 CA CYS B 21 36.830 -36.910 4.508 1.00 53.32 C ANISOU 776 CA CYS B 21 5678 8588 5994 -860 -2537 72 C ATOM 777 C CYS B 21 35.557 -37.610 4.066 1.00 53.52 C ANISOU 777 C CYS B 21 5951 8404 5981 -749 -2211 122 C ATOM 778 O CYS B 21 35.581 -38.794 3.754 1.00 58.45 O ANISOU 778 O CYS B 21 6569 8981 6660 -534 -2143 271 O ATOM 779 CB CYS B 21 37.575 -36.454 3.247 1.00 46.78 C ANISOU 779 CB CYS B 21 4454 7805 5515 -920 -2447 38 C ATOM 780 SG CYS B 21 39.059 -35.538 3.581 1.00 81.59 S ANISOU 780 SG CYS B 21 8490 12458 10050 -1120 -2780 -44 S ATOM 781 N SER B 22 34.455 -36.867 4.023 1.00 53.35 N ANISOU 781 N SER B 22 6134 8251 5885 -898 -2013 -12 N ATOM 782 CA SER B 22 33.221 -37.334 3.396 1.00 51.49 C ANISOU 782 CA SER B 22 6042 7840 5684 -839 -1703 1 C ATOM 783 C SER B 22 32.494 -36.131 2.799 1.00 37.70 C ANISOU 783 C SER B 22 4299 5996 4027 -999 -1535 -162 C ATOM 784 O SER B 22 32.725 -34.992 3.221 1.00 38.93 O ANISOU 784 O SER B 22 4475 6179 4139 -1159 -1633 -290 O ATOM 785 CB SER B 22 32.315 -38.044 4.414 1.00 51.28 C ANISOU 785 CB SER B 22 6355 7743 5388 -788 -1635 54 C ATOM 786 OG SER B 22 31.733 -37.104 5.306 1.00 54.09 O ANISOU 786 OG SER B 22 6924 8091 5536 -942 -1625 -91 O ATOM 787 N ALA B 23 31.651 -36.388 1.800 1.00 35.34 N ANISOU 787 N ALA B 23 3992 5578 3857 -952 -1302 -155 N ATOM 788 CA ALA B 23 30.808 -35.360 1.179 1.00 44.33 C ANISOU 788 CA ALA B 23 5153 6609 5082 -1050 -1148 -277 C ATOM 789 C ALA B 23 29.586 -35.995 0.547 1.00 42.70 C ANISOU 789 C ALA B 23 5005 6296 4922 -974 -935 -256 C ATOM 790 O ALA B 23 29.633 -37.143 0.123 1.00 43.36 O ANISOU 790 O ALA B 23 5059 6372 5044 -872 -891 -153 O ATOM 791 CB ALA B 23 31.588 -34.582 0.114 1.00 33.51 C ANISOU 791 CB ALA B 23 3572 5249 3911 -1123 -1171 -296 C ATOM 792 N GLY B 24 28.506 -35.235 0.429 1.00 38.44 N ANISOU 792 N GLY B 24 4535 5668 4401 -1021 -809 -360 N ATOM 793 CA GLY B 24 27.320 -35.743 -0.221 1.00 29.98 C ANISOU 793 CA GLY B 24 3464 4523 3404 -969 -641 -355 C ATOM 794 C GLY B 24 26.264 -34.675 -0.247 1.00 36.75 C ANISOU 794 C GLY B 24 4353 5305 4306 -997 -543 -477 C ATOM 795 O GLY B 24 26.398 -33.672 0.451 1.00 34.66 O ANISOU 795 O GLY B 24 4173 5020 3977 -1051 -575 -571 O ATOM 796 N PRO B 25 25.216 -34.874 -1.061 1.00 32.72 N ANISOU 796 N PRO B 25 3774 4748 3912 -953 -436 -485 N ATOM 797 CA PRO B 25 24.187 -33.836 -1.197 1.00 32.86 C ANISOU 797 CA PRO B 25 3777 4695 4014 -929 -361 -588 C ATOM 798 C PRO B 25 23.411 -33.580 0.083 1.00 39.56 C ANISOU 798 C PRO B 25 4731 5534 4766 -936 -229 -692 C ATOM 799 O PRO B 25 23.194 -34.477 0.899 1.00 40.17 O ANISOU 799 O PRO B 25 4882 5660 4720 -963 -146 -668 O ATOM 800 CB PRO B 25 23.252 -34.389 -2.287 1.00 31.41 C ANISOU 800 CB PRO B 25 3466 4507 3963 -880 -316 -559 C ATOM 801 CG PRO B 25 23.579 -35.840 -2.397 1.00 33.17 C ANISOU 801 CG PRO B 25 3692 4775 4137 -905 -310 -472 C ATOM 802 CD PRO B 25 25.035 -35.958 -2.042 1.00 36.70 C ANISOU 802 CD PRO B 25 4197 5255 4490 -918 -413 -406 C ATOM 803 N VAL B 26 22.998 -32.332 0.240 1.00 44.95 N ANISOU 803 N VAL B 26 5448 6134 5498 -905 -190 -805 N ATOM 804 CA VAL B 26 22.101 -31.933 1.314 1.00 49.62 C ANISOU 804 CA VAL B 26 6131 6698 6024 -882 -12 -935 C ATOM 805 C VAL B 26 20.675 -32.092 0.792 1.00 46.92 C ANISOU 805 C VAL B 26 5602 6356 5870 -785 133 -960 C ATOM 806 O VAL B 26 20.286 -31.460 -0.209 1.00 54.30 O ANISOU 806 O VAL B 26 6410 7232 6989 -691 72 -958 O ATOM 807 CB VAL B 26 22.326 -30.454 1.679 1.00 51.68 C ANISOU 807 CB VAL B 26 6529 6833 6274 -874 -27 -1067 C ATOM 808 CG1 VAL B 26 21.556 -30.090 2.954 1.00 55.72 C ANISOU 808 CG1 VAL B 26 7192 7316 6665 -852 185 -1226 C ATOM 809 CG2 VAL B 26 23.816 -30.157 1.822 1.00 48.66 C ANISOU 809 CG2 VAL B 26 6253 6455 5781 -1000 -229 -1040 C ATOM 810 N GLY B 27 19.907 -32.954 1.441 1.00 44.70 N ANISOU 810 N GLY B 27 5296 6145 5541 -817 312 -972 N ATOM 811 CA GLY B 27 18.535 -33.192 1.021 1.00 49.61 C ANISOU 811 CA GLY B 27 5684 6799 6364 -760 451 -1006 C ATOM 812 C GLY B 27 18.385 -33.565 -0.455 1.00 48.20 C ANISOU 812 C GLY B 27 5302 6643 6366 -734 283 -919 C ATOM 813 O GLY B 27 19.121 -34.404 -0.970 1.00 41.95 O ANISOU 813 O GLY B 27 4550 5876 5515 -809 162 -813 O ATOM 814 N ASP B 28 17.419 -32.932 -1.119 1.00 45.26 N ANISOU 814 N ASP B 28 4726 6263 6207 -612 275 -970 N ATOM 815 CA ASP B 28 17.000 -33.283 -2.476 1.00 45.06 C ANISOU 815 CA ASP B 28 4504 6282 6336 -586 111 -907 C ATOM 816 C ASP B 28 17.684 -32.456 -3.558 1.00 41.67 C ANISOU 816 C ASP B 28 4144 5770 5918 -499 -113 -836 C ATOM 817 O ASP B 28 17.308 -32.529 -4.724 1.00 46.88 O ANISOU 817 O ASP B 28 4683 6457 6673 -452 -267 -786 O ATOM 818 CB ASP B 28 15.474 -33.178 -2.623 1.00 45.84 C ANISOU 818 CB ASP B 28 4299 6452 6667 -502 194 -987 C ATOM 819 CG ASP B 28 14.731 -34.319 -1.929 1.00 54.15 C ANISOU 819 CG ASP B 28 5229 7607 7737 -655 412 -1029 C ATOM 820 OD1 ASP B 28 15.354 -35.366 -1.638 1.00 48.57 O ANISOU 820 OD1 ASP B 28 4685 6901 6869 -821 444 -965 O ATOM 821 OD2 ASP B 28 13.507 -34.173 -1.693 1.00 64.97 O ANISOU 821 OD2 ASP B 28 6333 9050 9301 -606 560 -1121 O ATOM 822 N ASP B 29 18.641 -31.625 -3.169 1.00 41.88 N ANISOU 822 N ASP B 29 3421 6054 6439 -834 100 -1070 N ATOM 823 CA ASP B 29 19.324 -30.760 -4.124 1.00 41.33 C ANISOU 823 CA ASP B 29 3676 5557 6471 -524 -49 -1239 C ATOM 824 C ASP B 29 20.701 -31.301 -4.469 1.00 42.81 C ANISOU 824 C ASP B 29 4197 5382 6686 -592 -91 -970 C ATOM 825 O ASP B 29 21.648 -31.195 -3.668 1.00 39.23 O ANISOU 825 O ASP B 29 3824 4999 6084 -652 -9 -857 O ATOM 826 CB ASP B 29 19.480 -29.356 -3.525 1.00 51.40 C ANISOU 826 CB ASP B 29 4961 6992 7575 -273 -33 -1534 C ATOM 827 CG ASP B 29 19.963 -28.326 -4.551 1.00 62.47 C ANISOU 827 CG ASP B 29 6702 7966 9069 -9 -254 -1708 C ATOM 828 OD1 ASP B 29 20.199 -28.688 -5.735 1.00 54.83 O ANISOU 828 OD1 ASP B 29 5937 6631 8266 -14 -366 -1605 O ATOM 829 OD2 ASP B 29 20.109 -27.147 -4.161 1.00 70.40 O ANISOU 829 OD2 ASP B 29 7798 9000 9952 191 -345 -1943 O ATOM 830 N MET B 30 20.842 -31.816 -5.685 1.00 36.09 N ANISOU 830 N MET B 30 3537 4163 6013 -539 -236 -906 N ATOM 831 CA MET B 30 22.099 -32.443 -6.080 1.00 34.66 C ANISOU 831 CA MET B 30 3615 3712 5841 -547 -277 -695 C ATOM 832 C MET B 30 23.241 -31.435 -6.264 1.00 30.18 C ANISOU 832 C MET B 30 3228 3060 5178 -398 -251 -756 C ATOM 833 O MET B 30 24.409 -31.823 -6.280 1.00 34.30 O ANISOU 833 O MET B 30 3866 3507 5658 -412 -235 -596 O ATOM 834 CB MET B 30 21.909 -33.358 -7.316 1.00 37.51 C ANISOU 834 CB MET B 30 4134 3742 6375 -494 -455 -635 C ATOM 835 CG MET B 30 22.349 -32.782 -8.672 1.00 42.03 C ANISOU 835 CG MET B 30 4954 4037 6981 -243 -539 -768 C ATOM 836 SD MET B 30 21.991 -33.894 -10.075 1.00 41.20 S ANISOU 836 SD MET B 30 5053 3565 7035 -137 -773 -741 S ATOM 837 CE MET B 30 22.950 -35.348 -9.661 1.00 40.18 C ANISOU 837 CE MET B 30 5021 3366 6879 -202 -836 -490 C ATOM 838 N PHE B 31 22.901 -30.152 -6.384 1.00 35.50 N ANISOU 838 N PHE B 31 3919 3754 5814 -265 -287 -988 N ATOM 839 CA PHE B 31 23.902 -29.088 -6.616 1.00 39.82 C ANISOU 839 CA PHE B 31 4672 4189 6267 -196 -334 -1016 C ATOM 840 C PHE B 31 24.466 -28.435 -5.353 1.00 37.83 C ANISOU 840 C PHE B 31 4379 4137 5859 -256 -280 -1011 C ATOM 841 O PHE B 31 25.407 -27.647 -5.440 1.00 32.12 O ANISOU 841 O PHE B 31 3821 3322 5061 -268 -349 -975 O ATOM 842 CB PHE B 31 23.381 -28.023 -7.614 1.00 33.72 C ANISOU 842 CB PHE B 31 4079 3201 5533 -35 -525 -1239 C ATOM 843 CG PHE B 31 23.236 -28.551 -9.023 1.00 39.76 C ANISOU 843 CG PHE B 31 4991 3714 6404 23 -601 -1204 C ATOM 844 CD1 PHE B 31 22.148 -29.343 -9.372 1.00 43.50 C ANISOU 844 CD1 PHE B 31 5347 4151 7029 64 -642 -1266 C ATOM 845 CD2 PHE B 31 24.214 -28.305 -9.978 1.00 44.24 C ANISOU 845 CD2 PHE B 31 5795 4155 6860 14 -618 -1067 C ATOM 846 CE1 PHE B 31 22.013 -29.853 -10.651 1.00 45.14 C ANISOU 846 CE1 PHE B 31 5710 4252 7188 133 -693 -1136 C ATOM 847 CE2 PHE B 31 24.095 -28.812 -11.265 1.00 43.60 C ANISOU 847 CE2 PHE B 31 5842 4002 6722 86 -625 -977 C ATOM 848 CZ PHE B 31 22.991 -29.598 -11.600 1.00 48.80 C ANISOU 848 CZ PHE B 31 6419 4659 7465 157 -664 -1002 C ATOM 849 N HIS B 32 23.880 -28.754 -4.194 1.00 38.29 N ANISOU 849 N HIS B 32 4221 4482 5845 -319 -172 -1035 N ATOM 850 CA AHIS B 32 24.399 -28.286 -2.915 0.52 37.70 C ANISOU 850 CA AHIS B 32 4123 4611 5589 -367 -121 -1026 C ATOM 851 CA BHIS B 32 24.405 -28.286 -2.901 0.48 37.65 C ANISOU 851 CA BHIS B 32 4117 4608 5582 -368 -120 -1025 C ATOM 852 C HIS B 32 24.799 -29.477 -2.050 1.00 39.03 C ANISOU 852 C HIS B 32 4190 4941 5701 -580 16 -762 C ATOM 853 O HIS B 32 23.944 -30.237 -1.601 1.00 37.02 O ANISOU 853 O HIS B 32 3750 4895 5422 -700 108 -717 O ATOM 854 CB AHIS B 32 23.355 -27.426 -2.195 0.52 39.56 C ANISOU 854 CB AHIS B 32 4224 5103 5702 -212 -138 -1339 C ATOM 855 CB BHIS B 32 23.383 -27.435 -2.127 0.48 39.32 C ANISOU 855 CB BHIS B 32 4191 5086 5662 -218 -131 -1333 C ATOM 856 CG AHIS B 32 23.158 -26.071 -2.807 0.52 44.49 C ANISOU 856 CG AHIS B 32 5043 5514 6349 29 -383 -1623 C ATOM 857 CG BHIS B 32 23.875 -26.963 -0.785 0.48 39.40 C ANISOU 857 CG BHIS B 32 4213 5311 5446 -232 -100 -1353 C ATOM 858 ND1AHIS B 32 22.263 -25.835 -3.832 0.52 43.63 N ANISOU 858 ND1AHIS B 32 4942 5254 6382 186 -512 -1816 N ATOM 859 ND1BHIS B 32 23.021 -26.603 0.240 0.48 44.53 N ANISOU 859 ND1BHIS B 32 4671 6354 5894 -119 -27 -1588 N ATOM 860 CD2AHIS B 32 23.746 -24.879 -2.538 0.52 42.98 C ANISOU 860 CD2AHIS B 32 5090 5185 6055 124 -590 -1735 C ATOM 861 CD2BHIS B 32 25.133 -26.786 -0.304 0.48 30.82 C ANISOU 861 CD2BHIS B 32 3300 4123 4289 -330 -145 -1181 C ATOM 862 CE1AHIS B 32 22.304 -24.556 -4.162 0.52 47.50 C ANISOU 862 CE1AHIS B 32 5687 5515 6846 373 -797 -2038 C ATOM 863 CE1BHIS B 32 23.730 -26.230 1.292 0.48 36.58 C ANISOU 863 CE1BHIS B 32 3767 5443 4688 -138 -39 -1560 C ATOM 864 NE2AHIS B 32 23.196 -23.954 -3.392 0.52 47.94 N ANISOU 864 NE2AHIS B 32 5895 5567 6755 327 -861 -1986 N ATOM 865 NE2BHIS B 32 25.014 -26.335 0.989 0.48 33.42 N ANISOU 865 NE2BHIS B 32 3591 4725 4384 -278 -125 -1305 N ATOM 866 N TRP B 33 26.095 -29.635 -1.808 1.00 32.96 N ANISOU 866 N TRP B 33 3540 4081 4901 -651 -2 -576 N ATOM 867 CA TRP B 33 26.518 -30.732 -0.956 1.00 37.37 C ANISOU 867 CA TRP B 33 4058 4738 5402 -831 52 -340 C ATOM 868 C TRP B 33 27.076 -30.180 0.354 1.00 35.98 C ANISOU 868 C TRP B 33 3906 4738 5027 -884 66 -330 C ATOM 869 O TRP B 33 27.344 -28.992 0.472 1.00 35.00 O ANISOU 869 O TRP B 33 3858 4601 4841 -773 0 -485 O ATOM 870 CB TRP B 33 27.666 -31.501 -1.635 1.00 26.97 C ANISOU 870 CB TRP B 33 2848 3194 4208 -818 -25 -156 C ATOM 871 CG TRP B 33 27.274 -32.391 -2.784 1.00 32.18 C ANISOU 871 CG TRP B 33 3534 3664 5029 -758 -78 -130 C ATOM 872 CD1 TRP B 33 26.129 -32.325 -3.557 1.00 26.55 C ANISOU 872 CD1 TRP B 33 2787 2894 4408 -706 -84 -259 C ATOM 873 CD2 TRP B 33 28.039 -33.477 -3.294 1.00 29.84 C ANISOU 873 CD2 TRP B 33 3323 3198 4819 -700 -182 4 C ATOM 874 NE1 TRP B 33 26.145 -33.333 -4.506 1.00 33.11 N ANISOU 874 NE1 TRP B 33 3705 3504 5372 -648 -190 -187 N ATOM 875 CE2 TRP B 33 27.308 -34.045 -4.372 1.00 31.34 C ANISOU 875 CE2 TRP B 33 3562 3210 5136 -618 -255 -44 C ATOM 876 CE3 TRP B 33 29.288 -34.026 -2.954 1.00 27.83 C ANISOU 876 CE3 TRP B 33 3108 2922 4545 -668 -257 128 C ATOM 877 CZ2 TRP B 33 27.776 -35.149 -5.095 1.00 31.60 C ANISOU 877 CZ2 TRP B 33 3716 3036 5254 -486 -411 17 C ATOM 878 CZ3 TRP B 33 29.751 -35.122 -3.678 1.00 34.25 C ANISOU 878 CZ3 TRP B 33 4005 3559 5451 -512 -406 167 C ATOM 879 CH2 TRP B 33 29.001 -35.664 -4.743 1.00 29.46 C ANISOU 879 CH2 TRP B 33 3478 2767 4947 -411 -485 105 C ATOM 880 N GLN B 34 27.369 -31.087 1.275 1.00 37.30 N ANISOU 880 N GLN B 34 4068 5006 5100 -1063 89 -124 N ATOM 881 CA GLN B 34 28.060 -30.769 2.508 1.00 35.94 C ANISOU 881 CA GLN B 34 3963 4956 4737 -1127 68 -70 C ATOM 882 C GLN B 34 29.272 -31.693 2.566 1.00 40.26 C ANISOU 882 C GLN B 34 4610 5319 5369 -1206 -51 176 C ATOM 883 O GLN B 34 29.254 -32.778 1.983 1.00 35.46 O ANISOU 883 O GLN B 34 4014 4565 4895 -1239 -104 304 O ATOM 884 CB GLN B 34 27.150 -31.035 3.718 1.00 36.49 C ANISOU 884 CB GLN B 34 3937 5385 4544 -1283 194 -60 C ATOM 885 CG GLN B 34 27.876 -30.882 5.056 1.00 69.62 C ANISOU 885 CG GLN B 34 8250 9697 8504 -1365 154 24 C ATOM 886 CD GLN B 34 26.951 -31.040 6.245 1.00 87.48 C ANISOU 886 CD GLN B 34 10412 12400 10425 -1519 313 18 C ATOM 887 OE1 GLN B 34 26.104 -30.181 6.503 1.00 91.49 O ANISOU 887 OE1 GLN B 34 10783 13214 10765 -1365 429 -261 O ATOM 888 NE2 GLN B 34 27.095 -32.151 6.966 1.00 89.96 N ANISOU 888 NE2 GLN B 34 10796 12773 10611 -1821 297 320 N ATOM 889 N ALA B 35 30.324 -31.261 3.256 1.00 36.54 N ANISOU 889 N ALA B 35 4219 4839 4826 -1206 -140 219 N ATOM 890 CA ALA B 35 31.489 -32.099 3.451 1.00 33.85 C ANISOU 890 CA ALA B 35 3941 4365 4555 -1242 -286 413 C ATOM 891 C ALA B 35 31.965 -32.022 4.894 1.00 37.29 C ANISOU 891 C ALA B 35 4481 4898 4790 -1361 -366 501 C ATOM 892 O ALA B 35 31.721 -31.043 5.597 1.00 35.29 O ANISOU 892 O ALA B 35 4258 4793 4358 -1359 -325 380 O ATOM 893 CB ALA B 35 32.618 -31.698 2.488 1.00 29.93 C ANISOU 893 CB ALA B 35 3388 3744 4238 -1096 -355 387 C ATOM 894 N THR B 36 32.646 -33.066 5.329 1.00 37.20 N ANISOU 894 N THR B 36 4559 4779 4796 -1434 -528 690 N ATOM 895 CA THR B 36 33.331 -33.017 6.600 1.00 45.91 C ANISOU 895 CA THR B 36 5793 5915 5735 -1527 -665 784 C ATOM 896 C THR B 36 34.791 -33.390 6.396 1.00 43.29 C ANISOU 896 C THR B 36 5453 5404 5592 -1412 -897 854 C ATOM 897 O THR B 36 35.136 -34.241 5.575 1.00 44.78 O ANISOU 897 O THR B 36 5590 5454 5970 -1294 -985 884 O ATOM 898 CB THR B 36 32.696 -33.934 7.667 1.00 50.90 C ANISOU 898 CB THR B 36 6584 6631 6123 -1778 -693 966 C ATOM 899 OG1 THR B 36 32.979 -35.297 7.352 1.00 67.93 O ANISOU 899 OG1 THR B 36 8841 8549 8419 -1824 -904 1145 O ATOM 900 CG2 THR B 36 31.207 -33.729 7.716 1.00 48.53 C ANISOU 900 CG2 THR B 36 6187 6605 5647 -1897 -435 898 C ATOM 901 N ILE B 37 35.642 -32.728 7.161 1.00 43.45 N ANISOU 901 N ILE B 37 5510 5450 5550 -1421 -1017 856 N ATOM 902 CA ILE B 37 37.059 -32.990 7.130 1.00 40.29 C ANISOU 902 CA ILE B 37 5044 4952 5313 -1323 -1250 911 C ATOM 903 C ILE B 37 37.540 -33.152 8.558 1.00 41.41 C ANISOU 903 C ILE B 37 5392 5055 5287 -1436 -1472 1019 C ATOM 904 O ILE B 37 37.242 -32.332 9.429 1.00 44.82 O ANISOU 904 O ILE B 37 5948 5580 5502 -1538 -1437 987 O ATOM 905 CB ILE B 37 37.784 -31.841 6.425 1.00 42.30 C ANISOU 905 CB ILE B 37 5087 5283 5702 -1252 -1213 818 C ATOM 906 CG1 ILE B 37 37.493 -31.922 4.923 1.00 46.85 C ANISOU 906 CG1 ILE B 37 5481 5885 6435 -1132 -1035 741 C ATOM 907 CG2 ILE B 37 39.266 -31.882 6.699 1.00 51.75 C ANISOU 907 CG2 ILE B 37 6164 6482 7018 -1209 -1455 880 C ATOM 908 CD1 ILE B 37 38.270 -30.928 4.111 1.00 57.82 C ANISOU 908 CD1 ILE B 37 6660 7380 7928 -1126 -1009 707 C ATOM 909 N MET B 38 38.257 -34.232 8.811 1.00 43.60 N ANISOU 909 N MET B 38 5742 5180 5644 -1388 -1738 1124 N ATOM 910 CA MET B 38 38.940 -34.359 10.085 1.00 46.45 C ANISOU 910 CA MET B 38 6304 5464 5880 -1470 -2017 1224 C ATOM 911 C MET B 38 40.235 -33.594 9.991 1.00 50.20 C ANISOU 911 C MET B 38 6567 5976 6532 -1353 -2159 1157 C ATOM 912 O MET B 38 40.955 -33.690 8.985 1.00 51.80 O ANISOU 912 O MET B 38 6468 6227 6987 -1174 -2167 1090 O ATOM 913 CB MET B 38 39.212 -35.816 10.413 1.00 48.48 C ANISOU 913 CB MET B 38 6768 5493 6157 -1460 -2337 1359 C ATOM 914 CG MET B 38 37.951 -36.623 10.655 1.00 49.51 C ANISOU 914 CG MET B 38 7149 5581 6081 -1692 -2265 1504 C ATOM 915 SD MET B 38 38.389 -38.340 10.931 1.00 81.33 S ANISOU 915 SD MET B 38 11503 9233 10165 -1689 -2784 1678 S ATOM 916 CE MET B 38 39.383 -38.169 12.423 1.00 96.43 C ANISOU 916 CE MET B 38 13657 11066 11916 -1763 -3124 1768 C ATOM 917 N GLY B 39 40.515 -32.811 11.029 1.00 50.32 N ANISOU 917 N GLY B 39 6007 6530 6584 -1959 -552 648 N ATOM 918 CA GLY B 39 41.771 -32.093 11.103 1.00 40.00 C ANISOU 918 CA GLY B 39 4605 5404 5187 -1946 -654 616 C ATOM 919 C GLY B 39 42.871 -33.128 11.001 1.00 44.61 C ANISOU 919 C GLY B 39 5065 5957 5927 -1763 -797 775 C ATOM 920 O GLY B 39 42.854 -34.132 11.722 1.00 47.55 O ANISOU 920 O GLY B 39 5496 6240 6331 -1720 -893 995 O ATOM 921 N PRO B 40 43.819 -32.908 10.084 1.00 43.12 N ANISOU 921 N PRO B 40 4696 5854 5832 -1641 -815 676 N ATOM 922 CA PRO B 40 44.896 -33.887 9.933 1.00 48.50 C ANISOU 922 CA PRO B 40 5217 6550 6662 -1382 -937 795 C ATOM 923 C PRO B 40 45.708 -34.031 11.217 1.00 52.24 C ANISOU 923 C PRO B 40 5634 7210 7006 -1414 -1131 1048 C ATOM 924 O PRO B 40 45.926 -33.059 11.955 1.00 51.37 O ANISOU 924 O PRO B 40 5526 7330 6662 -1647 -1183 1076 O ATOM 925 CB PRO B 40 45.740 -33.331 8.773 1.00 49.18 C ANISOU 925 CB PRO B 40 5065 6841 6782 -1295 -880 636 C ATOM 926 CG PRO B 40 45.239 -31.933 8.530 1.00 52.66 C ANISOU 926 CG PRO B 40 5575 7365 7070 -1581 -788 495 C ATOM 927 CD PRO B 40 43.843 -31.866 9.043 1.00 44.93 C ANISOU 927 CD PRO B 40 4861 6164 6047 -1708 -715 462 C ATOM 928 N ASN B 41 46.140 -35.255 11.485 1.00 51.32 N ANISOU 928 N ASN B 41 5498 6966 7037 -1175 -1268 1229 N ATOM 929 CA ASN B 41 46.835 -35.546 12.720 1.00 59.77 C ANISOU 929 CA ASN B 41 6530 8186 7994 -1188 -1484 1512 C ATOM 930 C ASN B 41 48.186 -34.830 12.804 1.00 71.59 C ANISOU 930 C ASN B 41 7718 10098 9383 -1192 -1595 1543 C ATOM 931 O ASN B 41 48.723 -34.607 13.895 1.00 73.87 O ANISOU 931 O ASN B 41 7973 10610 9486 -1328 -1777 1745 O ATOM 932 CB ASN B 41 46.991 -37.055 12.873 1.00 73.04 C ANISOU 932 CB ASN B 41 8281 9575 9896 -895 -1642 1710 C ATOM 933 CG ASN B 41 46.594 -37.536 14.253 1.00 90.88 C ANISOU 933 CG ASN B 41 10745 11767 12018 -1069 -1796 2032 C ATOM 934 OD1 ASN B 41 47.450 -37.766 15.109 1.00 92.61 O ANISOU 934 OD1 ASN B 41 10874 12158 12156 -1016 -2017 2281 O ATOM 935 ND2 ASN B 41 45.288 -37.681 14.482 1.00 95.82 N ANISOU 935 ND2 ASN B 41 11621 12192 12593 -1294 -1684 2051 N ATOM 936 N ASP B 42 48.708 -34.440 11.647 1.00 76.86 N ANISOU 936 N ASP B 42 8157 10907 10141 -1084 -1491 1357 N ATOM 937 CA ASP B 42 50.029 -33.823 11.553 1.00 89.63 C ANISOU 937 CA ASP B 42 9411 12969 11674 -1107 -1588 1413 C ATOM 938 C ASP B 42 49.977 -32.310 11.708 1.00 80.35 C ANISOU 938 C ASP B 42 8270 11999 10261 -1543 -1576 1334 C ATOM 939 O ASP B 42 50.975 -31.629 11.511 1.00 88.27 O ANISOU 939 O ASP B 42 8988 13367 11182 -1670 -1658 1378 O ATOM 940 CB ASP B 42 50.676 -34.162 10.207 1.00104.22 C ANISOU 940 CB ASP B 42 10958 14943 13697 -783 -1472 1275 C ATOM 941 CG ASP B 42 51.922 -35.013 10.357 1.00116.63 C ANISOU 941 CG ASP B 42 12187 16752 15374 -398 -1631 1445 C ATOM 942 OD1 ASP B 42 52.005 -35.773 11.348 1.00120.31 O ANISOU 942 OD1 ASP B 42 12755 17078 15879 -279 -1830 1661 O ATOM 943 OD2 ASP B 42 52.816 -34.919 9.488 1.00120.04 O ANISOU 943 OD2 ASP B 42 12234 17540 15836 -205 -1561 1376 O ATOM 944 N SER B 43 48.798 -31.782 12.004 1.00 72.94 N ANISOU 944 N SER B 43 7675 10822 9216 -1765 -1482 1212 N ATOM 945 CA SER B 43 48.614 -30.345 12.062 1.00 58.49 C ANISOU 945 CA SER B 43 5959 9080 7186 -2120 -1481 1084 C ATOM 946 C SER B 43 48.053 -29.907 13.411 1.00 52.66 C ANISOU 946 C SER B 43 5518 8298 6192 -2340 -1572 1112 C ATOM 947 O SER B 43 47.672 -30.736 14.227 1.00 57.12 O ANISOU 947 O SER B 43 6194 8781 6729 -2245 -1596 1247 O ATOM 948 CB SER B 43 47.621 -29.944 10.967 1.00 44.19 C ANISOU 948 CB SER B 43 4289 7034 5469 -2123 -1255 838 C ATOM 949 OG SER B 43 46.319 -30.408 11.289 1.00 49.03 O ANISOU 949 OG SER B 43 5172 7350 6106 -2060 -1136 777 O ATOM 950 N PRO B 44 47.947 -28.587 13.619 1.00 56.96 N ANISOU 950 N PRO B 44 6224 8884 6533 -2636 -1625 974 N ATOM 951 CA PRO B 44 47.301 -27.941 14.773 1.00 54.32 C ANISOU 951 CA PRO B 44 6225 8506 5908 -2821 -1679 894 C ATOM 952 C PRO B 44 45.776 -28.146 14.809 1.00 57.29 C ANISOU 952 C PRO B 44 6846 8635 6286 -2703 -1439 744 C ATOM 953 O PRO B 44 45.134 -27.736 15.771 1.00 52.93 O ANISOU 953 O PRO B 44 6542 8095 5473 -2789 -1433 666 O ATOM 954 CB PRO B 44 47.709 -26.464 14.648 1.00 48.53 C ANISOU 954 CB PRO B 44 5596 7818 5025 -3126 -1824 749 C ATOM 955 CG PRO B 44 48.096 -26.302 13.208 1.00 56.16 C ANISOU 955 CG PRO B 44 6334 8773 6231 -3088 -1734 726 C ATOM 956 CD PRO B 44 48.680 -27.611 12.787 1.00 54.70 C ANISOU 956 CD PRO B 44 5787 8737 6259 -2827 -1687 914 C ATOM 957 N TYR B 45 45.206 -28.661 13.722 1.00 48.43 N ANISOU 957 N TYR B 45 5645 7326 5428 -2524 -1246 681 N ATOM 958 CA TYR B 45 43.768 -28.925 13.637 1.00 44.19 C ANISOU 958 CA TYR B 45 5271 6595 4924 -2433 -1031 573 C ATOM 959 C TYR B 45 43.390 -30.330 14.102 1.00 42.77 C ANISOU 959 C TYR B 45 5065 6364 4821 -2308 -993 790 C ATOM 960 O TYR B 45 42.213 -30.696 14.119 1.00 45.11 O ANISOU 960 O TYR B 45 5457 6546 5138 -2280 -834 767 O ATOM 961 CB TYR B 45 43.292 -28.677 12.189 1.00 39.38 C ANISOU 961 CB TYR B 45 4615 5806 4541 -2356 -883 395 C ATOM 962 CG TYR B 45 43.794 -27.345 11.705 1.00 43.51 C ANISOU 962 CG TYR B 45 5170 6364 4998 -2517 -969 254 C ATOM 963 CD1 TYR B 45 43.292 -26.172 12.241 1.00 39.60 C ANISOU 963 CD1 TYR B 45 4935 5819 4293 -2646 -1006 81 C ATOM 964 CD2 TYR B 45 44.824 -27.258 10.770 1.00 39.73 C ANISOU 964 CD2 TYR B 45 4466 5984 4645 -2547 -1033 305 C ATOM 965 CE1 TYR B 45 43.760 -24.957 11.847 1.00 40.04 C ANISOU 965 CE1 TYR B 45 5079 5837 4296 -2829 -1142 -23 C ATOM 966 CE2 TYR B 45 45.305 -26.040 10.364 1.00 39.62 C ANISOU 966 CE2 TYR B 45 4486 6012 4556 -2768 -1143 238 C ATOM 967 CZ TYR B 45 44.768 -24.888 10.907 1.00 43.14 C ANISOU 967 CZ TYR B 45 5257 6304 4829 -2847 -1182 86 C ATOM 968 OH TYR B 45 45.238 -23.668 10.521 1.00 40.96 O ANISOU 968 OH TYR B 45 5094 5954 4515 -2909 -1253 53 O ATOM 969 N GLN B 46 44.395 -31.100 14.499 1.00 46.07 N ANISOU 969 N GLN B 46 5350 6875 5280 -2248 -1165 1026 N ATOM 970 CA GLN B 46 44.206 -32.478 14.946 1.00 46.35 C ANISOU 970 CA GLN B 46 5393 6806 5411 -2133 -1203 1281 C ATOM 971 C GLN B 46 43.111 -32.569 16.014 1.00 52.97 C ANISOU 971 C GLN B 46 6434 7687 6005 -2280 -1123 1364 C ATOM 972 O GLN B 46 43.077 -31.770 16.957 1.00 53.64 O ANISOU 972 O GLN B 46 6627 7996 5757 -2435 -1150 1322 O ATOM 973 CB GLN B 46 45.524 -33.002 15.515 1.00 49.21 C ANISOU 973 CB GLN B 46 5606 7323 5767 -2061 -1455 1532 C ATOM 974 CG GLN B 46 45.378 -34.250 16.338 1.00 53.78 C ANISOU 974 CG GLN B 46 6266 7808 6360 -1999 -1569 1849 C ATOM 975 CD GLN B 46 46.561 -34.491 17.241 1.00 62.94 C ANISOU 975 CD GLN B 46 7317 9193 7402 -1984 -1849 2114 C ATOM 976 OE1 GLN B 46 46.995 -33.601 17.984 1.00 67.41 O ANISOU 976 OE1 GLN B 46 7887 10051 7674 -2184 -1947 2102 O ATOM 977 NE2 GLN B 46 47.092 -35.701 17.192 1.00 70.63 N ANISOU 977 NE2 GLN B 46 8212 10017 8605 -1737 -2009 2352 N ATOM 978 N GLY B 47 42.203 -33.530 15.847 1.00 52.61 N ANISOU 978 N GLY B 47 6440 7447 6103 -2244 -1028 1475 N ATOM 979 CA GLY B 47 41.089 -33.696 16.766 1.00 48.60 C ANISOU 979 CA GLY B 47 6061 7044 5360 -2406 -920 1592 C ATOM 980 C GLY B 47 39.850 -32.886 16.400 1.00 54.75 C ANISOU 980 C GLY B 47 6874 7866 6062 -2454 -666 1324 C ATOM 981 O GLY B 47 38.785 -33.054 17.000 1.00 51.98 O ANISOU 981 O GLY B 47 6565 7652 5534 -2564 -528 1407 O ATOM 982 N GLY B 48 39.978 -32.007 15.411 1.00 44.12 N ANISOU 982 N GLY B 48 5490 6435 4839 -2369 -608 1025 N ATOM 983 CA GLY B 48 38.860 -31.178 15.009 1.00 51.89 C ANISOU 983 CA GLY B 48 6505 7438 5773 -2367 -404 769 C ATOM 984 C GLY B 48 38.017 -31.842 13.939 1.00 45.10 C ANISOU 984 C GLY B 48 5567 6360 5209 -2321 -295 762 C ATOM 985 O GLY B 48 38.514 -32.651 13.168 1.00 46.94 O ANISOU 985 O GLY B 48 5750 6366 5718 -2251 -386 837 O ATOM 986 N VAL B 49 36.735 -31.506 13.902 1.00 48.79 N ANISOU 986 N VAL B 49 6020 6915 5604 -2346 -111 662 N ATOM 987 CA VAL B 49 35.872 -31.931 12.804 1.00 49.41 C ANISOU 987 CA VAL B 49 6015 6815 5944 -2330 -27 620 C ATOM 988 C VAL B 49 35.312 -30.685 12.128 1.00 48.96 C ANISOU 988 C VAL B 49 5946 6785 5873 -2230 85 309 C ATOM 989 O VAL B 49 34.626 -29.880 12.759 1.00 48.39 O ANISOU 989 O VAL B 49 5889 6934 5563 -2197 204 192 O ATOM 990 CB VAL B 49 34.755 -32.876 13.269 1.00 50.60 C ANISOU 990 CB VAL B 49 6103 7051 6070 -2485 56 864 C ATOM 991 CG1 VAL B 49 33.808 -33.203 12.104 1.00 52.01 C ANISOU 991 CG1 VAL B 49 6191 7064 6504 -2505 114 801 C ATOM 992 CG2 VAL B 49 35.365 -34.154 13.816 1.00 47.73 C ANISOU 992 CG2 VAL B 49 5805 6562 5766 -2587 -115 1202 C ATOM 993 N PHE B 50 35.659 -30.512 10.854 1.00 48.72 N ANISOU 993 N PHE B 50 5899 6534 6077 -2159 34 173 N ATOM 994 CA PHE B 50 35.316 -29.303 10.121 1.00 39.33 C ANISOU 994 CA PHE B 50 4731 5318 4892 -2073 80 -86 C ATOM 995 C PHE B 50 34.266 -29.573 9.053 1.00 45.86 C ANISOU 995 C PHE B 50 5460 6050 5915 -2054 155 -134 C ATOM 996 O PHE B 50 34.410 -30.497 8.249 1.00 40.17 O ANISOU 996 O PHE B 50 4700 5157 5405 -2087 102 -61 O ATOM 997 CB PHE B 50 36.571 -28.688 9.504 1.00 38.21 C ANISOU 997 CB PHE B 50 4646 5068 4805 -2056 -54 -182 C ATOM 998 CG PHE B 50 37.614 -28.309 10.522 1.00 37.56 C ANISOU 998 CG PHE B 50 4645 5103 4524 -2111 -167 -136 C ATOM 999 CD1 PHE B 50 38.520 -29.253 10.987 1.00 35.32 C ANISOU 999 CD1 PHE B 50 4303 4854 4261 -2144 -262 74 C ATOM 1000 CD2 PHE B 50 37.660 -27.013 11.040 1.00 36.62 C ANISOU 1000 CD2 PHE B 50 4679 5043 4192 -2123 -207 -304 C ATOM 1001 CE1 PHE B 50 39.477 -28.914 11.932 1.00 38.92 C ANISOU 1001 CE1 PHE B 50 4811 5453 4524 -2214 -395 137 C ATOM 1002 CE2 PHE B 50 38.621 -26.658 11.993 1.00 44.39 C ANISOU 1002 CE2 PHE B 50 5760 6137 4972 -2216 -349 -268 C ATOM 1003 CZ PHE B 50 39.534 -27.611 12.439 1.00 38.78 C ANISOU 1003 CZ PHE B 50 4947 5513 4276 -2274 -441 -34 C ATOM 1004 N PHE B 51 33.206 -28.767 9.067 1.00 42.31 N ANISOU 1004 N PHE B 51 4976 5718 5382 -1981 261 -268 N ATOM 1005 CA PHE B 51 32.133 -28.880 8.089 1.00 40.07 C ANISOU 1005 CA PHE B 51 4568 5396 5261 -1963 313 -310 C ATOM 1006 C PHE B 51 32.303 -27.856 6.958 1.00 39.12 C ANISOU 1006 C PHE B 51 4517 5119 5229 -1860 244 -511 C ATOM 1007 O PHE B 51 32.709 -26.724 7.194 1.00 37.14 O ANISOU 1007 O PHE B 51 4401 4852 4860 -1775 201 -651 O ATOM 1008 CB PHE B 51 30.757 -28.737 8.757 1.00 42.82 C ANISOU 1008 CB PHE B 51 4763 6034 5473 -1928 473 -291 C ATOM 1009 CG PHE B 51 30.433 -29.845 9.725 1.00 43.85 C ANISOU 1009 CG PHE B 51 4794 6353 5513 -2103 540 -25 C ATOM 1010 CD1 PHE B 51 29.841 -31.012 9.286 1.00 52.98 C ANISOU 1010 CD1 PHE B 51 5828 7456 6846 -2298 515 179 C ATOM 1011 CD2 PHE B 51 30.732 -29.722 11.072 1.00 53.48 C ANISOU 1011 CD2 PHE B 51 6071 7795 6455 -2107 599 36 C ATOM 1012 CE1 PHE B 51 29.548 -32.037 10.171 1.00 61.54 C ANISOU 1012 CE1 PHE B 51 6849 8684 7850 -2514 538 475 C ATOM 1013 CE2 PHE B 51 30.445 -30.741 11.963 1.00 55.41 C ANISOU 1013 CE2 PHE B 51 6233 8230 6591 -2303 645 329 C ATOM 1014 CZ PHE B 51 29.848 -31.902 11.509 1.00 56.20 C ANISOU 1014 CZ PHE B 51 6211 8254 6889 -2518 611 567 C ATOM 1015 N LEU B 52 31.986 -28.276 5.732 1.00 35.46 N ANISOU 1015 N LEU B 52 3986 4529 4960 -1895 206 -512 N ATOM 1016 CA LEU B 52 32.086 -27.418 4.552 1.00 39.29 C ANISOU 1016 CA LEU B 52 4527 4888 5515 -1834 130 -652 C ATOM 1017 C LEU B 52 30.816 -27.499 3.687 1.00 36.66 C ANISOU 1017 C LEU B 52 4061 4575 5294 -1815 144 -673 C ATOM 1018 O LEU B 52 30.070 -28.470 3.749 1.00 37.28 O ANISOU 1018 O LEU B 52 4001 4723 5441 -1909 186 -564 O ATOM 1019 CB LEU B 52 33.314 -27.800 3.704 1.00 40.86 C ANISOU 1019 CB LEU B 52 4790 4947 5787 -1860 31 -623 C ATOM 1020 CG LEU B 52 34.689 -27.819 4.381 1.00 44.20 C ANISOU 1020 CG LEU B 52 5278 5388 6129 -1895 -10 -577 C ATOM 1021 CD1 LEU B 52 34.917 -29.151 5.112 1.00 43.90 C ANISOU 1021 CD1 LEU B 52 5189 5362 6128 -1962 14 -438 C ATOM 1022 CD2 LEU B 52 35.795 -27.573 3.358 1.00 38.87 C ANISOU 1022 CD2 LEU B 52 4621 4671 5476 -1821 -96 -571 C ATOM 1023 N THR B 53 30.567 -26.451 2.913 1.00 40.83 N ANISOU 1023 N THR B 53 4636 5043 5835 -1718 79 -788 N ATOM 1024 CA THR B 53 29.549 -26.486 1.871 1.00 40.22 C ANISOU 1024 CA THR B 53 4440 4974 5868 -1709 41 -797 C ATOM 1025 C THR B 53 30.243 -26.552 0.505 1.00 38.52 C ANISOU 1025 C THR B 53 4335 4602 5700 -1746 -86 -789 C ATOM 1026 O THR B 53 31.327 -26.005 0.305 1.00 34.79 O ANISOU 1026 O THR B 53 4012 4049 5156 -1703 -147 -784 O ATOM 1027 CB THR B 53 28.630 -25.248 1.891 1.00 45.42 C ANISOU 1027 CB THR B 53 5072 5694 6492 -1496 27 -893 C ATOM 1028 OG1 THR B 53 29.431 -24.053 1.913 1.00 51.21 O ANISOU 1028 OG1 THR B 53 6049 6257 7151 -1411 -68 -993 O ATOM 1029 CG2 THR B 53 27.715 -25.268 3.100 1.00 51.18 C ANISOU 1029 CG2 THR B 53 5635 6682 7129 -1368 180 -890 C ATOM 1030 N ILE B 54 29.603 -27.236 -0.421 1.00 37.31 N ANISOU 1030 N ILE B 54 4114 4448 5616 -1757 -142 -725 N ATOM 1031 CA ILE B 54 30.082 -27.344 -1.781 1.00 40.10 C ANISOU 1031 CA ILE B 54 4569 4715 5951 -1714 -256 -698 C ATOM 1032 C ILE B 54 28.917 -26.980 -2.692 1.00 35.65 C ANISOU 1032 C ILE B 54 3919 4189 5438 -1750 -340 -722 C ATOM 1033 O ILE B 54 27.874 -27.615 -2.652 1.00 34.31 O ANISOU 1033 O ILE B 54 3598 4093 5344 -1818 -341 -687 O ATOM 1034 CB ILE B 54 30.527 -28.789 -2.098 1.00 36.46 C ANISOU 1034 CB ILE B 54 4142 4191 5521 -1725 -275 -646 C ATOM 1035 CG1 ILE B 54 31.710 -29.187 -1.201 1.00 36.76 C ANISOU 1035 CG1 ILE B 54 4230 4204 5533 -1704 -211 -630 C ATOM 1036 CG2 ILE B 54 30.875 -28.926 -3.574 1.00 36.79 C ANISOU 1036 CG2 ILE B 54 4255 4196 5528 -1709 -359 -696 C ATOM 1037 CD1 ILE B 54 32.077 -30.672 -1.275 1.00 33.29 C ANISOU 1037 CD1 ILE B 54 3827 3659 5163 -1740 -239 -617 C ATOM 1038 N HIS B 55 29.077 -25.941 -3.493 1.00 37.66 N ANISOU 1038 N HIS B 55 4249 4404 5656 -1731 -431 -761 N ATOM 1039 CA AHIS B 55 28.050 -25.587 -4.470 0.55 38.94 C ANISOU 1039 CA AHIS B 55 4326 4603 5864 -1778 -550 -781 C ATOM 1040 CA BHIS B 55 28.055 -25.591 -4.458 0.45 38.57 C ANISOU 1040 CA BHIS B 55 4280 4557 5818 -1778 -549 -781 C ATOM 1041 C HIS B 55 28.575 -25.803 -5.886 1.00 36.28 C ANISOU 1041 C HIS B 55 4094 4223 5469 -1783 -646 -753 C ATOM 1042 O HIS B 55 29.564 -25.193 -6.290 1.00 36.98 O ANISOU 1042 O HIS B 55 4298 4279 5475 -1765 -650 -756 O ATOM 1043 CB AHIS B 55 27.565 -24.133 -4.308 0.55 35.32 C ANISOU 1043 CB AHIS B 55 3865 4120 5436 -1685 -621 -847 C ATOM 1044 CB BHIS B 55 27.576 -24.150 -4.216 0.45 35.76 C ANISOU 1044 CB BHIS B 55 3917 4177 5492 -1680 -610 -849 C ATOM 1045 CG AHIS B 55 26.508 -23.743 -5.302 0.55 40.18 C ANISOU 1045 CG AHIS B 55 4388 4788 6092 -1639 -783 -803 C ATOM 1046 CG BHIS B 55 26.794 -23.988 -2.946 0.45 39.94 C ANISOU 1046 CG BHIS B 55 4303 4812 6061 -1493 -498 -872 C ATOM 1047 ND1AHIS B 55 26.435 -22.486 -5.864 0.55 50.24 N ANISOU 1047 ND1AHIS B 55 5798 5950 7343 -1526 -952 -768 N ATOM 1048 ND1BHIS B 55 27.377 -23.617 -1.748 0.45 35.62 N ANISOU 1048 ND1BHIS B 55 3859 4225 5449 -1399 -395 -926 N ATOM 1049 CD2AHIS B 55 25.491 -24.454 -5.846 0.55 37.72 C ANISOU 1049 CD2AHIS B 55 3868 4622 5841 -1712 -835 -766 C ATOM 1050 CD2BHIS B 55 25.480 -24.171 -2.680 0.45 43.85 C ANISOU 1050 CD2BHIS B 55 4533 5509 6620 -1389 -465 -845 C ATOM 1051 CE1AHIS B 55 25.421 -22.441 -6.708 0.55 43.87 C ANISOU 1051 CE1AHIS B 55 4854 5235 6578 -1500 -1094 -709 C ATOM 1052 CE1BHIS B 55 26.453 -23.564 -0.808 0.45 40.42 C ANISOU 1052 CE1BHIS B 55 4293 5009 6057 -1223 -287 -951 C ATOM 1053 NE2AHIS B 55 24.832 -23.622 -6.716 0.55 43.30 N ANISOU 1053 NE2AHIS B 55 4560 5339 6554 -1621 -1025 -712 N ATOM 1054 NE2BHIS B 55 25.293 -23.899 -1.346 0.45 50.13 N ANISOU 1054 NE2BHIS B 55 5271 6408 7369 -1212 -316 -892 N ATOM 1055 N PHE B 56 27.920 -26.685 -6.626 1.00 30.48 N ANISOU 1055 N PHE B 56 3426 3803 4350 -269 -188 18 N ATOM 1056 CA PHE B 56 28.273 -26.919 -8.026 1.00 39.74 C ANISOU 1056 CA PHE B 56 4688 4956 5457 -321 -231 217 C ATOM 1057 C PHE B 56 27.523 -25.927 -8.906 1.00 35.63 C ANISOU 1057 C PHE B 56 4261 4207 5071 -268 -386 292 C ATOM 1058 O PHE B 56 26.303 -25.884 -8.881 1.00 40.54 O ANISOU 1058 O PHE B 56 4832 4772 5800 -124 -450 221 O ATOM 1059 CB PHE B 56 27.900 -28.340 -8.482 1.00 32.38 C ANISOU 1059 CB PHE B 56 3703 4190 4411 -280 -190 264 C ATOM 1060 CG PHE B 56 28.600 -29.442 -7.729 1.00 35.81 C ANISOU 1060 CG PHE B 56 4063 4809 4733 -321 -94 220 C ATOM 1061 CD1 PHE B 56 29.849 -29.902 -8.130 1.00 37.14 C ANISOU 1061 CD1 PHE B 56 4242 5073 4797 -401 -53 281 C ATOM 1062 CD2 PHE B 56 27.990 -30.051 -6.637 1.00 35.15 C ANISOU 1062 CD2 PHE B 56 3891 4821 4646 -288 -61 118 C ATOM 1063 CE1 PHE B 56 30.488 -30.944 -7.449 1.00 34.05 C ANISOU 1063 CE1 PHE B 56 3781 4818 4337 -411 -10 239 C ATOM 1064 CE2 PHE B 56 28.621 -31.085 -5.955 1.00 32.22 C ANISOU 1064 CE2 PHE B 56 3475 4589 4179 -342 -22 116 C ATOM 1065 CZ PHE B 56 29.867 -31.541 -6.366 1.00 27.77 C ANISOU 1065 CZ PHE B 56 2931 4070 3550 -385 -11 175 C ATOM 1066 N PRO B 57 28.258 -25.138 -9.699 1.00 38.68 N ANISOU 1066 N PRO B 57 4776 4471 5448 -400 -462 448 N ATOM 1067 CA PRO B 57 27.653 -24.232 -10.686 1.00 41.15 C ANISOU 1067 CA PRO B 57 5213 4551 5872 -389 -656 586 C ATOM 1068 C PRO B 57 27.038 -25.007 -11.864 1.00 38.51 C ANISOU 1068 C PRO B 57 4885 4315 5432 -361 -688 719 C ATOM 1069 O PRO B 57 27.303 -26.197 -12.017 1.00 38.21 O ANISOU 1069 O PRO B 57 4776 4515 5227 -376 -557 710 O ATOM 1070 CB PRO B 57 28.838 -23.357 -11.137 1.00 36.82 C ANISOU 1070 CB PRO B 57 4800 3914 5275 -620 -708 749 C ATOM 1071 CG PRO B 57 30.034 -24.214 -10.942 1.00 40.44 C ANISOU 1071 CG PRO B 57 5178 4662 5525 -745 -512 739 C ATOM 1072 CD PRO B 57 29.728 -25.207 -9.821 1.00 34.27 C ANISOU 1072 CD PRO B 57 4243 4035 4744 -592 -376 531 C ATOM 1073 N THR B 58 26.203 -24.360 -12.671 1.00 40.25 N ANISOU 1073 N THR B 58 5191 4343 5759 -312 -884 831 N ATOM 1074 CA THR B 58 25.562 -25.067 -13.786 1.00 42.82 C ANISOU 1074 CA THR B 58 5523 4770 5975 -292 -931 951 C ATOM 1075 C THR B 58 26.550 -25.531 -14.888 1.00 43.20 C ANISOU 1075 C THR B 58 5645 5015 5753 -508 -867 1134 C ATOM 1076 O THR B 58 26.298 -26.507 -15.591 1.00 41.11 O ANISOU 1076 O THR B 58 5346 4934 5338 -499 -823 1157 O ATOM 1077 CB THR B 58 24.358 -24.269 -14.370 1.00 52.21 C ANISOU 1077 CB THR B 58 6774 5711 7354 -174 -1188 1028 C ATOM 1078 OG1 THR B 58 24.755 -22.927 -14.688 1.00 53.20 O ANISOU 1078 OG1 THR B 58 7068 5560 7587 -282 -1380 1178 O ATOM 1079 CG2 THR B 58 23.232 -24.218 -13.349 1.00 52.91 C ANISOU 1079 CG2 THR B 58 6705 5732 7666 76 -1200 778 C ATOM 1080 N ASP B 59 27.672 -24.834 -15.008 1.00 40.29 N ANISOU 1080 N ASP B 59 5363 4629 5317 -710 -859 1238 N ATOM 1081 CA ASP B 59 28.720 -25.176 -15.975 1.00 49.74 C ANISOU 1081 CA ASP B 59 6590 6073 6237 -940 -774 1377 C ATOM 1082 C ASP B 59 29.844 -26.075 -15.419 1.00 38.23 C ANISOU 1082 C ASP B 59 4995 4889 4642 -973 -538 1226 C ATOM 1083 O ASP B 59 30.862 -26.284 -16.060 1.00 42.43 O ANISOU 1083 O ASP B 59 5508 5654 4960 -1155 -447 1285 O ATOM 1084 CB ASP B 59 29.264 -23.933 -16.712 1.00 59.22 C ANISOU 1084 CB ASP B 59 7960 7149 7392 -1202 -925 1630 C ATOM 1085 CG ASP B 59 29.522 -22.753 -15.785 1.00 71.39 C ANISOU 1085 CG ASP B 59 9569 8398 9157 -1225 -1019 1609 C ATOM 1086 OD1 ASP B 59 29.496 -22.922 -14.543 1.00 66.08 O ANISOU 1086 OD1 ASP B 59 8793 7687 8629 -1062 -921 1380 O ATOM 1087 OD2 ASP B 59 29.755 -21.643 -16.311 1.00 84.82 O ANISOU 1087 OD2 ASP B 59 11438 9906 10884 -1425 -1208 1829 O ATOM 1088 N TYR B 60 29.685 -26.562 -14.198 1.00 37.45 N ANISOU 1088 N TYR B 60 4789 4774 4665 -806 -451 1028 N ATOM 1089 CA TYR B 60 30.558 -27.643 -13.726 1.00 39.24 C ANISOU 1089 CA TYR B 60 4884 5246 4781 -794 -275 891 C ATOM 1090 C TYR B 60 30.463 -28.884 -14.663 1.00 41.18 C ANISOU 1090 C TYR B 60 5081 5707 4860 -755 -226 871 C ATOM 1091 O TYR B 60 29.390 -29.216 -15.135 1.00 43.25 O ANISOU 1091 O TYR B 60 5373 5913 5145 -660 -304 894 O ATOM 1092 CB TYR B 60 30.177 -27.980 -12.283 1.00 33.11 C ANISOU 1092 CB TYR B 60 4023 4404 4153 -637 -233 717 C ATOM 1093 CG TYR B 60 30.874 -29.176 -11.687 1.00 34.04 C ANISOU 1093 CG TYR B 60 4021 4720 4195 -598 -110 594 C ATOM 1094 CD1 TYR B 60 32.118 -29.050 -11.067 1.00 32.87 C ANISOU 1094 CD1 TYR B 60 3814 4665 4011 -687 -32 547 C ATOM 1095 CD2 TYR B 60 30.278 -30.430 -11.723 1.00 27.78 C ANISOU 1095 CD2 TYR B 60 3175 4000 3381 -474 -103 529 C ATOM 1096 CE1 TYR B 60 32.759 -30.153 -10.518 1.00 32.86 C ANISOU 1096 CE1 TYR B 60 3700 4821 3965 -633 37 440 C ATOM 1097 CE2 TYR B 60 30.909 -31.534 -11.168 1.00 34.11 C ANISOU 1097 CE2 TYR B 60 3885 4931 4143 -433 -43 430 C ATOM 1098 CZ TYR B 60 32.147 -31.389 -10.564 1.00 33.01 C ANISOU 1098 CZ TYR B 60 3686 4876 3980 -501 20 386 C ATOM 1099 OH TYR B 60 32.762 -32.492 -10.024 1.00 37.15 O ANISOU 1099 OH TYR B 60 4121 5506 4490 -442 38 295 O ATOM 1100 N PRO B 61 31.574 -29.616 -14.857 1.00 42.68 N ANISOU 1100 N PRO B 61 5174 6143 4897 -810 -102 794 N ATOM 1101 CA PRO B 61 32.846 -29.226 -14.244 1.00 34.11 C ANISOU 1101 CA PRO B 61 4024 5142 3794 -921 -16 759 C ATOM 1102 C PRO B 61 33.764 -28.364 -15.093 1.00 39.86 C ANISOU 1102 C PRO B 61 4784 6000 4362 -1180 2 896 C ATOM 1103 O PRO B 61 34.972 -28.517 -14.877 1.00 37.84 O ANISOU 1103 O PRO B 61 4408 5948 4021 -1267 110 822 O ATOM 1104 CB PRO B 61 33.547 -30.584 -14.159 1.00 34.76 C ANISOU 1104 CB PRO B 61 3956 5454 3797 -826 86 586 C ATOM 1105 CG PRO B 61 33.154 -31.248 -15.512 1.00 36.65 C ANISOU 1105 CG PRO B 61 4209 5831 3885 -812 76 591 C ATOM 1106 CD PRO B 61 31.730 -30.749 -15.795 1.00 35.18 C ANISOU 1106 CD PRO B 61 4167 5419 3783 -779 -53 725 C ATOM 1107 N PHE B 62 33.279 -27.385 -15.855 1.00 41.16 N ANISOU 1107 N PHE B 62 5099 6035 4506 -1318 -118 1098 N ATOM 1108 CA PHE B 62 34.210 -26.559 -16.629 1.00 44.02 C ANISOU 1108 CA PHE B 62 5499 6538 4687 -1628 -114 1264 C ATOM 1109 C PHE B 62 34.577 -25.333 -15.829 1.00 40.90 C ANISOU 1109 C PHE B 62 5183 5916 4442 -1752 -186 1344 C ATOM 1110 O PHE B 62 35.552 -24.669 -16.114 1.00 45.81 O ANISOU 1110 O PHE B 62 5811 6653 4943 -2026 -168 1456 O ATOM 1111 CB PHE B 62 33.664 -26.267 -18.041 1.00 44.25 C ANISOU 1111 CB PHE B 62 5653 6605 4553 -1772 -221 1470 C ATOM 1112 CG PHE B 62 33.315 -27.524 -18.777 1.00 47.06 C ANISOU 1112 CG PHE B 62 5926 7193 4761 -1643 -147 1348 C ATOM 1113 CD1 PHE B 62 34.322 -28.326 -19.308 1.00 40.56 C ANISOU 1113 CD1 PHE B 62 4938 6774 3698 -1714 26 1208 C ATOM 1114 CD2 PHE B 62 32.000 -27.968 -18.836 1.00 39.33 C ANISOU 1114 CD2 PHE B 62 5006 6034 3903 -1429 -250 1328 C ATOM 1115 CE1 PHE B 62 34.015 -29.533 -19.918 1.00 41.59 C ANISOU 1115 CE1 PHE B 62 4991 7090 3721 -1568 79 1046 C ATOM 1116 CE2 PHE B 62 31.679 -29.172 -19.451 1.00 43.08 C ANISOU 1116 CE2 PHE B 62 5411 6699 4258 -1312 -196 1198 C ATOM 1117 CZ PHE B 62 32.686 -29.958 -19.992 1.00 42.26 C ANISOU 1117 CZ PHE B 62 5168 6964 3926 -1376 -38 1051 C ATOM 1118 N LYS B 63 33.796 -25.117 -14.778 1.00 39.87 N ANISOU 1118 N LYS B 63 5093 5488 4568 -1547 -260 1256 N ATOM 1119 CA LYS B 63 34.044 -24.132 -13.737 1.00 41.92 C ANISOU 1119 CA LYS B 63 5403 5516 5010 -1588 -320 1234 C ATOM 1120 C LYS B 63 34.099 -24.896 -12.412 1.00 38.72 C ANISOU 1120 C LYS B 63 4856 5156 4699 -1380 -204 990 C ATOM 1121 O LYS B 63 33.381 -25.884 -12.228 1.00 38.11 O ANISOU 1121 O LYS B 63 4713 5123 4645 -1167 -164 880 O ATOM 1122 CB LYS B 63 32.912 -23.096 -13.690 1.00 47.13 C ANISOU 1122 CB LYS B 63 6238 5775 5895 -1518 -543 1320 C ATOM 1123 CG LYS B 63 32.831 -22.184 -14.919 1.00 48.59 C ANISOU 1123 CG LYS B 63 6604 5844 6015 -1748 -727 1609 C ATOM 1124 CD LYS B 63 34.081 -21.335 -15.059 1.00 58.93 C ANISOU 1124 CD LYS B 63 7969 7200 7223 -2095 -738 1757 C ATOM 1125 CE LYS B 63 33.975 -20.408 -16.275 1.00 68.40 C ANISOU 1125 CE LYS B 63 9373 8276 8341 -2374 -955 2091 C ATOM 1126 NZ LYS B 63 35.244 -19.683 -16.537 1.00 66.90 N ANISOU 1126 NZ LYS B 63 9191 8230 7998 -2679 -942 2176 N ATOM 1127 N PRO B 64 34.943 -24.444 -11.480 1.00 37.90 N ANISOU 1127 N PRO B 64 4712 5045 4642 -1465 -165 921 N ATOM 1128 CA PRO B 64 35.129 -25.199 -10.235 1.00 40.04 C ANISOU 1128 CA PRO B 64 4849 5403 4962 -1312 -67 716 C ATOM 1129 C PRO B 64 33.886 -25.144 -9.363 1.00 35.00 C ANISOU 1129 C PRO B 64 4245 4550 4505 -1102 -128 599 C ATOM 1130 O PRO B 64 33.120 -24.201 -9.481 1.00 35.38 O ANISOU 1130 O PRO B 64 4412 4341 4691 -1083 -256 639 O ATOM 1131 CB PRO B 64 36.316 -24.472 -9.565 1.00 37.27 C ANISOU 1131 CB PRO B 64 4470 5079 4610 -1501 -45 700 C ATOM 1132 CG PRO B 64 36.240 -23.067 -10.115 1.00 38.68 C ANISOU 1132 CG PRO B 64 4826 5020 4850 -1696 -189 869 C ATOM 1133 CD PRO B 64 35.776 -23.234 -11.538 1.00 35.19 C ANISOU 1133 CD PRO B 64 4452 4621 4299 -1735 -230 1042 C ATOM 1134 N PRO B 65 33.689 -26.142 -8.488 1.00 33.97 N ANISOU 1134 N PRO B 65 4002 4533 4372 -954 -50 454 N ATOM 1135 CA PRO B 65 32.622 -25.990 -7.488 1.00 37.85 C ANISOU 1135 CA PRO B 65 4492 4887 5001 -807 -84 320 C ATOM 1136 C PRO B 65 33.044 -24.920 -6.495 1.00 39.20 C ANISOU 1136 C PRO B 65 4690 4941 5265 -885 -111 225 C ATOM 1137 O PRO B 65 34.236 -24.652 -6.362 1.00 37.75 O ANISOU 1137 O PRO B 65 4494 4831 5019 -1044 -80 255 O ATOM 1138 CB PRO B 65 32.584 -27.356 -6.794 1.00 32.78 C ANISOU 1138 CB PRO B 65 3730 4442 4285 -714 -1 230 C ATOM 1139 CG PRO B 65 33.948 -27.880 -6.929 1.00 34.20 C ANISOU 1139 CG PRO B 65 3841 4805 4347 -810 61 261 C ATOM 1140 CD PRO B 65 34.519 -27.329 -8.239 1.00 31.16 C ANISOU 1140 CD PRO B 65 3511 4430 3899 -938 52 396 C ATOM 1141 N LYS B 66 32.084 -24.286 -5.840 1.00 33.98 N ANISOU 1141 N LYS B 66 4052 4107 4750 -776 -172 91 N ATOM 1142 CA LYS B 66 32.418 -23.338 -4.784 1.00 31.08 C ANISOU 1142 CA LYS B 66 3701 3637 4472 -829 -198 -59 C ATOM 1143 C LYS B 66 32.453 -24.078 -3.444 1.00 32.55 C ANISOU 1143 C LYS B 66 3755 4039 4572 -791 -88 -230 C ATOM 1144 O LYS B 66 31.485 -24.734 -3.055 1.00 37.13 O ANISOU 1144 O LYS B 66 4258 4711 5138 -663 -50 -317 O ATOM 1145 CB LYS B 66 31.427 -22.176 -4.757 1.00 46.53 C ANISOU 1145 CB LYS B 66 5741 5290 6648 -721 -341 -161 C ATOM 1146 CG LYS B 66 31.584 -21.204 -5.930 1.00 72.56 C ANISOU 1146 CG LYS B 66 9207 8319 10042 -817 -508 38 C ATOM 1147 CD LYS B 66 30.818 -21.662 -7.186 1.00 81.38 C ANISOU 1147 CD LYS B 66 10356 9426 11138 -740 -560 213 C ATOM 1148 CE LYS B 66 29.354 -21.195 -7.153 1.00 83.27 C ANISOU 1148 CE LYS B 66 10599 9447 11592 -509 -695 91 C ATOM 1149 NZ LYS B 66 28.403 -22.089 -7.888 1.00 73.17 N ANISOU 1149 NZ LYS B 66 9261 8281 10260 -380 -680 163 N ATOM 1150 N VAL B 67 33.591 -24.015 -2.769 1.00 31.87 N ANISOU 1150 N VAL B 67 3640 4058 4411 -930 -47 -256 N ATOM 1151 CA VAL B 67 33.774 -24.733 -1.518 1.00 34.31 C ANISOU 1151 CA VAL B 67 3838 4586 4610 -935 30 -375 C ATOM 1152 C VAL B 67 34.123 -23.757 -0.396 1.00 36.49 C ANISOU 1152 C VAL B 67 4124 4817 4925 -1017 11 -560 C ATOM 1153 O VAL B 67 34.971 -22.881 -0.561 1.00 39.85 O ANISOU 1153 O VAL B 67 4618 5122 5401 -1147 -41 -531 O ATOM 1154 CB VAL B 67 34.871 -25.798 -1.671 1.00 37.15 C ANISOU 1154 CB VAL B 67 4128 5159 4830 -1010 76 -245 C ATOM 1155 CG1 VAL B 67 34.970 -26.674 -0.418 1.00 31.96 C ANISOU 1155 CG1 VAL B 67 3375 4710 4060 -1016 108 -321 C ATOM 1156 CG2 VAL B 67 34.578 -26.655 -2.901 1.00 32.10 C ANISOU 1156 CG2 VAL B 67 3489 4542 4164 -927 82 -98 C ATOM 1157 N ALA B 68 33.461 -23.897 0.744 1.00 38.67 N ANISOU 1157 N ALA B 68 4327 5206 5161 -964 52 -756 N ATOM 1158 CA ALA B 68 33.705 -22.996 1.864 1.00 38.98 C ANISOU 1158 CA ALA B 68 4365 5230 5217 -1033 39 -981 C ATOM 1159 C ALA B 68 33.547 -23.720 3.192 1.00 34.13 C ANISOU 1159 C ALA B 68 3631 4919 4417 -1072 119 -1109 C ATOM 1160 O ALA B 68 32.712 -24.611 3.325 1.00 40.25 O ANISOU 1160 O ALA B 68 4333 5853 5108 -1004 171 -1094 O ATOM 1161 CB ALA B 68 32.756 -21.790 1.806 1.00 40.88 C ANISOU 1161 CB ALA B 68 4660 5207 5664 -908 -36 -1186 C ATOM 1162 N PHE B 69 34.352 -23.332 4.172 1.00 35.58 N ANISOU 1162 N PHE B 69 3802 5192 4523 -1211 117 -1220 N ATOM 1163 CA PHE B 69 34.168 -23.827 5.533 1.00 42.76 C ANISOU 1163 CA PHE B 69 4613 6402 5234 -1284 175 -1360 C ATOM 1164 C PHE B 69 32.917 -23.239 6.163 1.00 44.03 C ANISOU 1164 C PHE B 69 4715 6595 5420 -1186 221 -1672 C ATOM 1165 O PHE B 69 32.567 -22.084 5.947 1.00 48.87 O ANISOU 1165 O PHE B 69 5377 6964 6228 -1088 173 -1864 O ATOM 1166 CB PHE B 69 35.386 -23.524 6.422 1.00 33.58 C ANISOU 1166 CB PHE B 69 3449 5343 3969 -1471 146 -1406 C ATOM 1167 CG PHE B 69 36.540 -24.452 6.198 1.00 34.30 C ANISOU 1167 CG PHE B 69 3518 5546 3969 -1567 112 -1141 C ATOM 1168 CD1 PHE B 69 37.352 -24.311 5.090 1.00 38.06 C ANISOU 1168 CD1 PHE B 69 4038 5862 4561 -1569 74 -966 C ATOM 1169 CD2 PHE B 69 36.807 -25.470 7.088 1.00 40.67 C ANISOU 1169 CD2 PHE B 69 4250 6629 4571 -1659 103 -1073 C ATOM 1170 CE1 PHE B 69 38.424 -25.167 4.876 1.00 40.06 C ANISOU 1170 CE1 PHE B 69 4230 6245 4744 -1628 44 -774 C ATOM 1171 CE2 PHE B 69 37.877 -26.329 6.883 1.00 42.35 C ANISOU 1171 CE2 PHE B 69 4429 6920 4740 -1710 36 -854 C ATOM 1172 CZ PHE B 69 38.685 -26.179 5.771 1.00 36.73 C ANISOU 1172 CZ PHE B 69 3731 6062 4162 -1676 15 -728 C ATOM 1173 N THR B 70 32.259 -24.076 6.945 1.00 45.39 N ANISOU 1173 N THR B 70 4774 7080 5392 -1221 299 -1719 N ATOM 1174 CA THR B 70 31.129 -23.724 7.794 1.00 42.74 C ANISOU 1174 CA THR B 70 4320 6927 4993 -1175 377 -2045 C ATOM 1175 C THR B 70 31.703 -23.476 9.184 1.00 50.00 C ANISOU 1175 C THR B 70 5197 8098 5704 -1361 405 -2233 C ATOM 1176 O THR B 70 31.447 -22.450 9.816 1.00 60.43 O ANISOU 1176 O THR B 70 6482 9414 7064 -1330 422 -2589 O ATOM 1177 CB THR B 70 30.061 -24.840 7.793 1.00 38.98 C ANISOU 1177 CB THR B 70 3734 6699 4379 -1161 449 -1957 C ATOM 1178 OG1 THR B 70 29.329 -24.772 6.566 1.00 54.37 O ANISOU 1178 OG1 THR B 70 5706 8406 6546 -961 420 -1883 O ATOM 1179 CG2 THR B 70 29.102 -24.665 8.955 1.00 62.85 C ANISOU 1179 CG2 THR B 70 6587 10065 7229 -1203 558 -2289 C ATOM 1180 N THR B 71 32.367 -24.501 9.698 1.00 48.43 N ANISOU 1180 N THR B 71 4991 8140 5272 -1550 398 -2007 N ATOM 1181 CA THR B 71 33.163 -24.411 10.913 1.00 48.44 C ANISOU 1181 CA THR B 71 4974 8373 5056 -1762 386 -2092 C ATOM 1182 C THR B 71 34.230 -23.301 10.854 1.00 47.41 C ANISOU 1182 C THR B 71 4936 8000 5077 -1782 312 -2191 C ATOM 1183 O THR B 71 35.005 -23.216 9.900 1.00 45.91 O ANISOU 1183 O THR B 71 4837 7543 5062 -1743 238 -1978 O ATOM 1184 CB THR B 71 33.840 -25.759 11.140 1.00 44.38 C ANISOU 1184 CB THR B 71 4469 8046 4347 -1924 323 -1742 C ATOM 1185 OG1 THR B 71 32.849 -26.790 11.025 1.00 48.53 O ANISOU 1185 OG1 THR B 71 4939 8729 4771 -1917 361 -1611 O ATOM 1186 CG2 THR B 71 34.516 -25.826 12.507 1.00 40.74 C ANISOU 1186 CG2 THR B 71 3987 7863 3628 -2142 305 -1775 C ATOM 1187 N ARG B 72 34.264 -22.452 11.880 1.00 48.89 N ANISOU 1187 N ARG B 72 5092 8302 5181 -1862 332 -2525 N ATOM 1188 CA ARG B 72 35.297 -21.429 11.998 1.00 52.18 C ANISOU 1188 CA ARG B 72 5598 8518 5712 -1930 246 -2630 C ATOM 1189 C ARG B 72 36.673 -22.075 12.134 1.00 55.50 C ANISOU 1189 C ARG B 72 6051 9018 6018 -2098 175 -2302 C ATOM 1190 O ARG B 72 36.836 -23.098 12.799 1.00 48.90 O ANISOU 1190 O ARG B 72 5165 8465 4949 -2188 194 -2113 O ATOM 1191 CB ARG B 72 35.022 -20.495 13.185 1.00 64.08 C ANISOU 1191 CB ARG B 72 7065 10122 7161 -1923 297 -2982 C ATOM 1192 CG ARG B 72 33.808 -19.597 12.988 1.00 77.36 C ANISOU 1192 CG ARG B 72 8707 11642 9044 -1698 331 -3346 C ATOM 1193 CD ARG B 72 34.154 -18.344 12.190 1.00 85.22 C ANISOU 1193 CD ARG B 72 9852 12137 10391 -1597 187 -3462 C ATOM 1194 NE ARG B 72 34.593 -17.255 13.062 1.00 89.62 N ANISOU 1194 NE ARG B 72 10450 12621 10982 -1625 138 -3705 N ATOM 1195 CZ ARG B 72 35.722 -16.570 12.904 1.00 96.95 C ANISOU 1195 CZ ARG B 72 11524 13292 12022 -1744 5 -3630 C ATOM 1196 NH1 ARG B 72 36.548 -16.857 11.898 1.00 91.10 N ANISOU 1196 NH1 ARG B 72 10878 12370 11368 -1853 -75 -3309 N ATOM 1197 NH2 ARG B 72 36.030 -15.594 13.757 1.00104.81 N ANISOU 1197 NH2 ARG B 72 12555 14231 13035 -1768 -46 -3873 N ATOM 1198 N ILE B 73 37.664 -21.480 11.486 1.00 47.67 N ANISOU 1198 N ILE B 73 5141 7765 5205 -2134 83 -2220 N ATOM 1199 CA ILE B 73 39.000 -22.030 11.527 1.00 45.57 C ANISOU 1199 CA ILE B 73 4878 7571 4866 -2250 16 -1930 C ATOM 1200 C ILE B 73 40.049 -20.930 11.438 1.00 47.94 C ANISOU 1200 C ILE B 73 5249 7666 5299 -2338 -63 -1981 C ATOM 1201 O ILE B 73 39.843 -19.898 10.800 1.00 54.58 O ANISOU 1201 O ILE B 73 6171 8207 6359 -2309 -98 -2120 O ATOM 1202 CB ILE B 73 39.201 -23.119 10.448 1.00 47.91 C ANISOU 1202 CB ILE B 73 5147 7845 5212 -2197 -7 -1607 C ATOM 1203 CG1 ILE B 73 40.550 -23.831 10.629 1.00 40.30 C ANISOU 1203 CG1 ILE B 73 4155 6991 4167 -2262 -80 -1343 C ATOM 1204 CG2 ILE B 73 38.997 -22.540 9.029 1.00 43.48 C ANISOU 1204 CG2 ILE B 73 4663 6939 4920 -2060 -2 -1549 C ATOM 1205 CD1 ILE B 73 40.750 -24.993 9.640 1.00 40.56 C ANISOU 1205 CD1 ILE B 73 4148 7011 4253 -2164 -109 -1062 C ATOM 1206 N TYR B 74 41.161 -21.147 12.125 1.00 50.61 N ANISOU 1206 N TYR B 74 5565 8157 5509 -2453 -108 -1862 N ATOM 1207 CA TYR B 74 42.251 -20.193 12.145 1.00 43.81 C ANISOU 1207 CA TYR B 74 4752 7150 4742 -2565 -189 -1885 C ATOM 1208 C TYR B 74 43.343 -20.642 11.168 1.00 47.19 C ANISOU 1208 C TYR B 74 5147 7535 5249 -2593 -238 -1582 C ATOM 1209 O TYR B 74 44.017 -21.637 11.396 1.00 49.19 O ANISOU 1209 O TYR B 74 5318 7989 5382 -2591 -257 -1385 O ATOM 1210 CB TYR B 74 42.770 -20.058 13.581 1.00 45.38 C ANISOU 1210 CB TYR B 74 4929 7567 4746 -2675 -206 -1985 C ATOM 1211 CG TYR B 74 43.838 -19.014 13.796 1.00 47.63 C ANISOU 1211 CG TYR B 74 5263 7723 5110 -2805 -297 -2047 C ATOM 1212 CD1 TYR B 74 43.503 -17.697 14.104 1.00 53.29 C ANISOU 1212 CD1 TYR B 74 6073 8236 5941 -2824 -330 -2347 C ATOM 1213 CD2 TYR B 74 45.187 -19.345 13.706 1.00 47.28 C ANISOU 1213 CD2 TYR B 74 5167 7758 5040 -2898 -365 -1817 C ATOM 1214 CE1 TYR B 74 44.488 -16.730 14.318 1.00 52.10 C ANISOU 1214 CE1 TYR B 74 5979 7949 5866 -2963 -439 -2393 C ATOM 1215 CE2 TYR B 74 46.179 -18.394 13.917 1.00 49.40 C ANISOU 1215 CE2 TYR B 74 5466 7931 5372 -3037 -450 -1866 C ATOM 1216 CZ TYR B 74 45.823 -17.087 14.220 1.00 55.52 C ANISOU 1216 CZ TYR B 74 6351 8491 6253 -3083 -491 -2143 C ATOM 1217 OH TYR B 74 46.806 -16.147 14.429 1.00 54.09 O ANISOU 1217 OH TYR B 74 6212 8198 6142 -3237 -598 -2181 O ATOM 1218 N HIS B 75 43.573 -19.862 10.117 1.00 44.75 N ANISOU 1218 N HIS B 75 5067 5814 6124 -1267 -859 -1523 N ATOM 1219 CA HIS B 75 44.395 -20.312 8.994 1.00 42.13 C ANISOU 1219 CA HIS B 75 4541 5577 5889 -1235 -898 -1403 C ATOM 1220 C HIS B 75 44.608 -19.156 8.010 1.00 40.44 C ANISOU 1220 C HIS B 75 4297 5188 5879 -1383 -738 -1384 C ATOM 1221 O HIS B 75 43.678 -18.417 7.693 1.00 43.97 O ANISOU 1221 O HIS B 75 4889 5388 6428 -1369 -596 -1321 O ATOM 1222 CB HIS B 75 43.662 -21.465 8.272 1.00 38.67 C ANISOU 1222 CB HIS B 75 4122 5165 5405 -1021 -886 -1198 C ATOM 1223 CG HIS B 75 44.516 -22.237 7.312 1.00 44.23 C ANISOU 1223 CG HIS B 75 4632 6011 6164 -966 -933 -1127 C ATOM 1224 ND1 HIS B 75 44.891 -21.742 6.080 1.00 40.21 N ANISOU 1224 ND1 HIS B 75 4010 5476 5794 -1067 -801 -1079 N ATOM 1225 CD2 HIS B 75 45.056 -23.478 7.400 1.00 42.95 C ANISOU 1225 CD2 HIS B 75 4373 6007 5941 -824 -1088 -1111 C ATOM 1226 CE1 HIS B 75 45.635 -22.639 5.456 1.00 38.16 C ANISOU 1226 CE1 HIS B 75 3566 5385 5547 -1001 -842 -1077 C ATOM 1227 NE2 HIS B 75 45.743 -23.704 6.231 1.00 45.88 N ANISOU 1227 NE2 HIS B 75 4546 6455 6432 -825 -1019 -1098 N ATOM 1228 N PRO B 76 45.844 -19.012 7.510 1.00 47.42 N ANISOU 1228 N PRO B 76 4987 6206 6826 -1533 -770 -1432 N ATOM 1229 CA PRO B 76 46.241 -17.891 6.643 1.00 41.47 C ANISOU 1229 CA PRO B 76 4222 5311 6223 -1763 -632 -1420 C ATOM 1230 C PRO B 76 45.437 -17.819 5.341 1.00 44.49 C ANISOU 1230 C PRO B 76 4689 5532 6684 -1703 -499 -1176 C ATOM 1231 O PRO B 76 45.218 -16.730 4.817 1.00 41.33 O ANISOU 1231 O PRO B 76 4414 4885 6405 -1852 -395 -1105 O ATOM 1232 CB PRO B 76 47.707 -18.201 6.326 1.00 44.99 C ANISOU 1232 CB PRO B 76 4375 6052 6668 -1904 -701 -1519 C ATOM 1233 CG PRO B 76 48.156 -19.096 7.417 1.00 44.07 C ANISOU 1233 CG PRO B 76 4139 6171 6433 -1768 -915 -1635 C ATOM 1234 CD PRO B 76 46.974 -19.907 7.810 1.00 40.80 C ANISOU 1234 CD PRO B 76 3913 5672 5919 -1502 -952 -1512 C ATOM 1235 N ASN B 77 45.031 -18.976 4.823 1.00 39.29 N ANISOU 1235 N ASN B 77 3974 5006 5949 -1506 -519 -1042 N ATOM 1236 CA ASN B 77 44.302 -19.059 3.557 1.00 41.22 C ANISOU 1236 CA ASN B 77 4276 5168 6217 -1476 -416 -807 C ATOM 1237 C ASN B 77 42.787 -19.173 3.624 1.00 44.69 C ANISOU 1237 C ASN B 77 4885 5448 6646 -1277 -394 -658 C ATOM 1238 O ASN B 77 42.143 -19.387 2.596 1.00 40.56 O ANISOU 1238 O ASN B 77 4389 4909 6113 -1246 -344 -451 O ATOM 1239 CB ASN B 77 44.890 -20.155 2.687 1.00 36.03 C ANISOU 1239 CB ASN B 77 3435 4768 5486 -1458 -410 -777 C ATOM 1240 CG ASN B 77 46.364 -19.987 2.515 1.00 38.08 C ANISOU 1240 CG ASN B 77 3467 5220 5782 -1657 -406 -945 C ATOM 1241 OD1 ASN B 77 47.150 -20.774 3.041 1.00 48.70 O ANISOU 1241 OD1 ASN B 77 4621 6777 7107 -1558 -512 -1103 O ATOM 1242 ND2 ASN B 77 46.764 -18.919 1.818 1.00 39.91 N ANISOU 1242 ND2 ASN B 77 3714 5378 6074 -1950 -298 -912 N ATOM 1243 N ILE B 78 42.229 -19.092 4.831 1.00 44.05 N ANISOU 1243 N ILE B 78 4897 5296 6543 -1164 -431 -778 N ATOM 1244 CA ILE B 78 40.795 -19.263 5.025 1.00 39.04 C ANISOU 1244 CA ILE B 78 4372 4568 5891 -979 -395 -689 C ATOM 1245 C ILE B 78 40.240 -18.132 5.881 1.00 47.27 C ANISOU 1245 C ILE B 78 5534 5369 7059 -971 -336 -827 C ATOM 1246 O ILE B 78 40.673 -17.946 7.015 1.00 51.40 O ANISOU 1246 O ILE B 78 6084 5918 7528 -1037 -362 -1056 O ATOM 1247 CB ILE B 78 40.474 -20.624 5.680 1.00 34.22 C ANISOU 1247 CB ILE B 78 3757 4166 5076 -842 -471 -722 C ATOM 1248 CG1 ILE B 78 41.170 -21.768 4.922 1.00 34.19 C ANISOU 1248 CG1 ILE B 78 3644 4361 4987 -832 -528 -643 C ATOM 1249 CG2 ILE B 78 38.946 -20.855 5.745 1.00 31.52 C ANISOU 1249 CG2 ILE B 78 3498 3784 4695 -697 -409 -630 C ATOM 1250 CD1 ILE B 78 41.090 -23.161 5.641 1.00 36.29 C ANISOU 1250 CD1 ILE B 78 3941 4779 5067 -706 -642 -675 C ATOM 1251 N ASN B 79 39.295 -17.360 5.351 1.00 41.76 N ANISOU 1251 N ASN B 79 4902 4431 6533 -892 -262 -700 N ATOM 1252 CA ASN B 79 38.849 -16.176 6.088 1.00 45.61 C ANISOU 1252 CA ASN B 79 5497 4629 7205 -866 -185 -867 C ATOM 1253 C ASN B 79 37.662 -16.465 7.023 1.00 45.84 C ANISOU 1253 C ASN B 79 5534 4696 7186 -679 -123 -1005 C ATOM 1254 O ASN B 79 37.258 -17.612 7.186 1.00 43.92 O ANISOU 1254 O ASN B 79 5237 4715 6735 -608 -155 -964 O ATOM 1255 CB ASN B 79 38.580 -14.984 5.155 1.00 44.54 C ANISOU 1255 CB ASN B 79 5443 4140 7340 -874 -153 -688 C ATOM 1256 CG ASN B 79 37.343 -15.180 4.285 1.00 45.83 C ANISOU 1256 CG ASN B 79 5567 4269 7576 -664 -170 -413 C ATOM 1257 OD1 ASN B 79 36.514 -16.053 4.538 1.00 44.08 O ANISOU 1257 OD1 ASN B 79 5261 4257 7231 -506 -164 -415 O ATOM 1258 ND2 ASN B 79 37.214 -14.353 3.258 1.00 48.35 N ANISOU 1258 ND2 ASN B 79 5957 4333 8081 -691 -205 -164 N ATOM 1259 N SER B 80 37.123 -15.428 7.648 1.00 50.09 N ANISOU 1259 N SER B 80 6146 4971 7915 -621 -18 -1192 N ATOM 1260 CA SER B 80 36.098 -15.620 8.663 1.00 55.07 C ANISOU 1260 CA SER B 80 6763 5674 8488 -493 83 -1407 C ATOM 1261 C SER B 80 34.756 -16.044 8.054 1.00 59.75 C ANISOU 1261 C SER B 80 7243 6327 9133 -261 107 -1218 C ATOM 1262 O SER B 80 33.886 -16.539 8.762 1.00 55.67 O ANISOU 1262 O SER B 80 6671 5985 8494 -186 187 -1359 O ATOM 1263 CB SER B 80 35.951 -14.362 9.536 1.00 53.67 C ANISOU 1263 CB SER B 80 6682 5196 8514 -505 223 -1730 C ATOM 1264 OG SER B 80 35.526 -13.247 8.774 1.00 58.86 O ANISOU 1264 OG SER B 80 7371 5447 9546 -364 258 -1618 O ATOM 1265 N ASN B 81 34.608 -15.863 6.741 1.00 62.64 N ANISOU 1265 N ASN B 81 7569 6581 9649 -188 33 -899 N ATOM 1266 CA ASN B 81 33.430 -16.334 6.014 1.00 55.57 C ANISOU 1266 CA ASN B 81 6545 5798 8772 -5 12 -676 C ATOM 1267 C ASN B 81 33.581 -17.763 5.509 1.00 52.33 C ANISOU 1267 C ASN B 81 6090 5745 8049 -94 -67 -497 C ATOM 1268 O ASN B 81 32.680 -18.296 4.858 1.00 53.03 O ANISOU 1268 O ASN B 81 6078 5978 8093 -3 -91 -309 O ATOM 1269 CB ASN B 81 33.132 -15.431 4.819 1.00 60.96 C ANISOU 1269 CB ASN B 81 7224 6193 9746 97 -62 -387 C ATOM 1270 CG ASN B 81 32.839 -14.007 5.225 1.00 72.71 C ANISOU 1270 CG ASN B 81 8774 7250 11604 235 5 -540 C ATOM 1271 OD1 ASN B 81 32.201 -13.759 6.250 1.00 76.96 O ANISOU 1271 OD1 ASN B 81 9262 7752 12227 368 139 -849 O ATOM 1272 ND2 ASN B 81 33.303 -13.058 4.419 1.00 73.18 N ANISOU 1272 ND2 ASN B 81 8957 6966 11881 187 -77 -335 N ATOM 1273 N GLY B 82 34.727 -18.372 5.786 1.00 41.68 N ANISOU 1273 N GLY B 82 4807 4531 6498 -269 -114 -562 N ATOM 1274 CA GLY B 82 34.991 -19.720 5.332 1.00 41.92 C ANISOU 1274 CA GLY B 82 4815 4839 6273 -335 -185 -427 C ATOM 1275 C GLY B 82 35.518 -19.833 3.905 1.00 41.76 C ANISOU 1275 C GLY B 82 4768 4825 6272 -413 -247 -167 C ATOM 1276 O GLY B 82 35.772 -20.940 3.421 1.00 43.90 O ANISOU 1276 O GLY B 82 5022 5305 6354 -468 -283 -80 O ATOM 1277 N SER B 83 35.693 -18.700 3.236 1.00 33.90 N ANISOU 1277 N SER B 83 3792 3592 5496 -441 -251 -54 N ATOM 1278 CA SER B 83 36.299 -18.696 1.912 1.00 40.78 C ANISOU 1278 CA SER B 83 4661 4484 6350 -590 -295 177 C ATOM 1279 C SER B 83 37.712 -19.264 1.948 1.00 45.82 C ANISOU 1279 C SER B 83 5281 5277 6852 -763 -301 58 C ATOM 1280 O SER B 83 38.473 -19.016 2.885 1.00 40.59 O ANISOU 1280 O SER B 83 4630 4580 6211 -805 -300 -166 O ATOM 1281 CB SER B 83 36.312 -17.286 1.325 1.00 42.46 C ANISOU 1281 CB SER B 83 4947 4375 6809 -632 -314 324 C ATOM 1282 OG SER B 83 34.986 -16.798 1.197 1.00 55.40 O ANISOU 1282 OG SER B 83 6566 5868 8616 -421 -340 456 O ATOM 1283 N ILE B 84 38.057 -20.027 0.917 1.00 36.84 N ANISOU 1283 N ILE B 84 4094 4328 5577 -865 -306 192 N ATOM 1284 CA ILE B 84 39.322 -20.730 0.891 1.00 35.03 C ANISOU 1284 CA ILE B 84 3790 4276 5242 -977 -302 56 C ATOM 1285 C ILE B 84 40.169 -20.219 -0.256 1.00 43.87 C ANISOU 1285 C ILE B 84 4877 5405 6386 -1217 -260 151 C ATOM 1286 O ILE B 84 39.741 -20.283 -1.398 1.00 42.82 O ANISOU 1286 O ILE B 84 4764 5318 6189 -1305 -239 367 O ATOM 1287 CB ILE B 84 39.101 -22.243 0.672 1.00 32.66 C ANISOU 1287 CB ILE B 84 3454 4205 4749 -906 -308 62 C ATOM 1288 CG1 ILE B 84 38.131 -22.811 1.726 1.00 36.05 C ANISOU 1288 CG1 ILE B 84 3948 4645 5105 -727 -343 3 C ATOM 1289 CG2 ILE B 84 40.434 -22.976 0.658 1.00 36.28 C ANISOU 1289 CG2 ILE B 84 3808 4817 5158 -962 -314 -101 C ATOM 1290 CD1 ILE B 84 37.547 -24.198 1.373 1.00 31.44 C ANISOU 1290 CD1 ILE B 84 3388 4230 4328 -688 -341 70 C ATOM 1291 N CYS B 85 41.382 -19.747 0.024 1.00 47.86 N ANISOU 1291 N CYS B 85 6094 5995 6096 -1048 -1804 -89 N ATOM 1292 CA CYS B 85 42.238 -19.370 -1.076 1.00 47.21 C ANISOU 1292 CA CYS B 85 6171 5731 6035 -1524 -1589 7 C ATOM 1293 C CYS B 85 43.089 -20.594 -1.394 1.00 43.83 C ANISOU 1293 C CYS B 85 5146 5706 5799 -1693 -1338 29 C ATOM 1294 O CYS B 85 44.057 -20.902 -0.680 1.00 44.08 O ANISOU 1294 O CYS B 85 4766 5980 6004 -1871 -1327 -62 O ATOM 1295 CB CYS B 85 43.145 -18.230 -0.610 1.00 52.41 C ANISOU 1295 CB CYS B 85 7072 6111 6730 -1961 -1687 -81 C ATOM 1296 SG CYS B 85 44.312 -17.652 -1.852 1.00 66.46 S ANISOU 1296 SG CYS B 85 9031 7715 8507 -2679 -1419 60 S ATOM 1297 N LEU B 86 42.739 -21.250 -2.500 1.00 38.71 N ANISOU 1297 N LEU B 86 4476 5139 5092 -1614 -1143 136 N ATOM 1298 CA LEU B 86 43.409 -22.452 -2.994 1.00 44.60 C ANISOU 1298 CA LEU B 86 4747 6221 5977 -1686 -895 141 C ATOM 1299 C LEU B 86 43.391 -22.438 -4.520 1.00 45.54 C ANISOU 1299 C LEU B 86 5062 6287 5953 -1839 -663 251 C ATOM 1300 O LEU B 86 42.319 -22.317 -5.125 1.00 39.29 O ANISOU 1300 O LEU B 86 4594 5361 4973 -1616 -701 319 O ATOM 1301 CB LEU B 86 42.697 -23.700 -2.471 1.00 39.54 C ANISOU 1301 CB LEU B 86 3807 5802 5413 -1267 -947 107 C ATOM 1302 CG LEU B 86 43.265 -25.089 -2.774 1.00 45.26 C ANISOU 1302 CG LEU B 86 4098 6806 6293 -1221 -741 85 C ATOM 1303 CD1 LEU B 86 44.665 -25.285 -2.212 1.00 40.07 C ANISOU 1303 CD1 LEU B 86 3077 6334 5812 -1355 -657 7 C ATOM 1304 CD2 LEU B 86 42.319 -26.173 -2.247 1.00 48.81 C ANISOU 1304 CD2 LEU B 86 4419 7346 6780 -848 -831 87 C ATOM 1305 N ASP B 87 44.551 -22.636 -5.139 1.00 41.39 N ANISOU 1305 N ASP B 87 4289 5953 5484 -2184 -422 260 N ATOM 1306 CA ASP B 87 44.687 -22.423 -6.574 1.00 49.50 C ANISOU 1306 CA ASP B 87 5515 6960 6333 -2400 -193 375 C ATOM 1307 C ASP B 87 43.820 -23.319 -7.461 1.00 45.07 C ANISOU 1307 C ASP B 87 4970 6492 5662 -2076 -97 381 C ATOM 1308 O ASP B 87 43.312 -22.861 -8.483 1.00 43.28 O ANISOU 1308 O ASP B 87 5104 6140 5201 -2105 -34 495 O ATOM 1309 CB ASP B 87 46.159 -22.498 -6.991 1.00 57.31 C ANISOU 1309 CB ASP B 87 6148 8255 7374 -2834 57 368 C ATOM 1310 CG ASP B 87 46.883 -21.181 -6.774 1.00 83.10 C ANISOU 1310 CG ASP B 87 9632 11341 10599 -3367 17 437 C ATOM 1311 OD1 ASP B 87 46.269 -20.259 -6.189 1.00 85.15 O ANISOU 1311 OD1 ASP B 87 10345 11184 10823 -3342 -227 460 O ATOM 1312 OD2 ASP B 87 48.056 -21.059 -7.196 1.00 96.94 O ANISOU 1312 OD2 ASP B 87 11166 13330 12337 -3651 218 438 O ATOM 1313 N ILE B 88 43.643 -24.578 -7.066 1.00 38.40 N ANISOU 1313 N ILE B 88 3767 5856 4969 -1781 -96 263 N ATOM 1314 CA ILE B 88 42.839 -25.512 -7.864 1.00 39.29 C ANISOU 1314 CA ILE B 88 3894 6049 4986 -1531 -16 229 C ATOM 1315 C ILE B 88 41.366 -25.185 -7.806 1.00 40.31 C ANISOU 1315 C ILE B 88 4360 6016 4938 -1279 -222 277 C ATOM 1316 O ILE B 88 40.580 -25.710 -8.582 1.00 49.20 O ANISOU 1316 O ILE B 88 5561 7219 5913 -1133 -179 258 O ATOM 1317 CB ILE B 88 43.016 -26.972 -7.442 1.00 39.88 C ANISOU 1317 CB ILE B 88 3575 6310 5266 -1308 28 95 C ATOM 1318 CG1 ILE B 88 42.762 -27.128 -5.932 1.00 45.95 C ANISOU 1318 CG1 ILE B 88 4208 7039 6211 -1127 -205 81 C ATOM 1319 CG2 ILE B 88 44.398 -27.467 -7.850 1.00 44.45 C ANISOU 1319 CG2 ILE B 88 3809 7140 5939 -1448 275 21 C ATOM 1320 CD1 ILE B 88 42.234 -28.502 -5.529 1.00 40.67 C ANISOU 1320 CD1 ILE B 88 3366 6428 5659 -844 -240 19 C ATOM 1321 N LEU B 89 40.986 -24.325 -6.873 1.00 42.17 N ANISOU 1321 N LEU B 89 4781 6073 5168 -1209 -454 316 N ATOM 1322 CA LEU B 89 39.619 -23.842 -6.839 1.00 36.82 C ANISOU 1322 CA LEU B 89 4428 5299 4263 -924 -656 361 C ATOM 1323 C LEU B 89 39.447 -22.574 -7.666 1.00 43.51 C ANISOU 1323 C LEU B 89 5784 5901 4848 -1009 -659 497 C ATOM 1324 O LEU B 89 38.321 -22.119 -7.828 1.00 47.94 O ANISOU 1324 O LEU B 89 6643 6412 5161 -715 -814 543 O ATOM 1325 CB LEU B 89 39.175 -23.574 -5.400 1.00 38.99 C ANISOU 1325 CB LEU B 89 4666 5539 4610 -708 -920 315 C ATOM 1326 CG LEU B 89 39.008 -24.783 -4.480 1.00 42.06 C ANISOU 1326 CG LEU B 89 4627 6167 5187 -549 -965 234 C ATOM 1327 CD1 LEU B 89 38.744 -24.330 -3.033 1.00 43.66 C ANISOU 1327 CD1 LEU B 89 4797 6367 5425 -372 -1216 202 C ATOM 1328 CD2 LEU B 89 37.891 -25.674 -4.987 1.00 42.77 C ANISOU 1328 CD2 LEU B 89 4662 6446 5142 -362 -955 225 C ATOM 1329 N ARG B 90 40.538 -21.940 -8.112 1.00 46.46 N ANISOU 1329 N ARG B 90 6273 6129 5249 -1400 -508 576 N ATOM 1330 CA ARG B 90 40.358 -20.881 -9.088 1.00 45.91 C ANISOU 1330 CA ARG B 90 6726 5817 4900 -1505 -473 753 C ATOM 1331 C ARG B 90 41.165 -21.020 -10.372 1.00 47.69 C ANISOU 1331 C ARG B 90 6910 6173 5038 -1853 -166 850 C ATOM 1332 O ARG B 90 40.719 -21.680 -11.310 1.00 53.67 O ANISOU 1332 O ARG B 90 7591 7160 5640 -1711 -45 842 O ATOM 1333 CB ARG B 90 40.748 -19.540 -8.442 1.00 68.31 C ANISOU 1333 CB ARG B 90 9970 8236 7751 -1701 -625 819 C ATOM 1334 CG ARG B 90 39.954 -19.141 -7.193 1.00 82.33 C ANISOU 1334 CG ARG B 90 11885 9852 9544 -1328 -947 715 C ATOM 1335 CD ARG B 90 40.624 -19.580 -5.885 1.00 89.42 C ANISOU 1335 CD ARG B 90 12339 10885 10752 -1427 -1017 545 C ATOM 1336 NE ARG B 90 41.993 -19.083 -5.779 1.00 97.35 N ANISOU 1336 NE ARG B 90 13309 11776 11905 -1974 -912 553 N ATOM 1337 CZ ARG B 90 42.330 -17.898 -5.277 1.00 99.79 C ANISOU 1337 CZ ARG B 90 14017 11700 12199 -2205 -1059 551 C ATOM 1338 NH1 ARG B 90 41.395 -17.073 -4.821 1.00100.18 N ANISOU 1338 NH1 ARG B 90 14568 11403 12092 -1857 -1325 532 N ATOM 1339 NH2 ARG B 90 43.607 -17.538 -5.234 1.00 99.80 N ANISOU 1339 NH2 ARG B 90 13916 11682 12322 -2787 -945 551 N ATOM 1340 N SER B 91 42.418 -20.567 -10.370 1.00 46.95 N ANISOU 1340 N SER B 91 6762 6029 5047 -2328 -26 904 N ATOM 1341 CA SER B 91 43.108 -20.396 -11.662 1.00 48.79 C ANISOU 1341 CA SER B 91 7052 6386 5100 -2687 261 1052 C ATOM 1342 C SER B 91 43.660 -21.724 -12.145 1.00 47.95 C ANISOU 1342 C SER B 91 6368 6767 5083 -2672 505 902 C ATOM 1343 O SER B 91 43.895 -21.914 -13.332 1.00 51.60 O ANISOU 1343 O SER B 91 6818 7446 5343 -2786 738 968 O ATOM 1344 CB SER B 91 44.211 -19.322 -11.615 1.00 55.90 C ANISOU 1344 CB SER B 91 8141 7090 6008 -3278 338 1198 C ATOM 1345 OG SER B 91 45.227 -19.668 -10.691 1.00 62.02 O ANISOU 1345 OG SER B 91 8422 8071 7072 -3515 356 1038 O ATOM 1346 N GLN B 92 43.897 -22.616 -11.190 1.00 44.28 N ANISOU 1346 N GLN B 92 5452 6466 4905 -2513 445 701 N ATOM 1347 CA GLN B 92 44.472 -23.932 -11.432 1.00 43.44 C ANISOU 1347 CA GLN B 92 4826 6758 4922 -2425 640 528 C ATOM 1348 C GLN B 92 43.435 -25.050 -11.552 1.00 40.41 C ANISOU 1348 C GLN B 92 4382 6432 4541 -1985 575 388 C ATOM 1349 O GLN B 92 43.785 -26.227 -11.596 1.00 45.73 O ANISOU 1349 O GLN B 92 4699 7332 5343 -1846 688 219 O ATOM 1350 CB GLN B 92 45.473 -24.267 -10.334 1.00 51.95 C ANISOU 1350 CB GLN B 92 5458 7989 6292 -2513 622 411 C ATOM 1351 CG GLN B 92 46.666 -23.337 -10.305 1.00 65.24 C ANISOU 1351 CG GLN B 92 7080 9747 7960 -3036 725 505 C ATOM 1352 CD GLN B 92 47.509 -23.473 -11.545 1.00 84.06 C ANISOU 1352 CD GLN B 92 9294 12482 10162 -3283 1048 547 C ATOM 1353 OE1 GLN B 92 48.150 -24.505 -11.760 1.00 89.72 O ANISOU 1353 OE1 GLN B 92 9594 13545 10952 -3047 1186 381 O ATOM 1354 NE2 GLN B 92 47.505 -22.439 -12.385 1.00 89.80 N ANISOU 1354 NE2 GLN B 92 10426 13053 10641 -3622 1128 761 N ATOM 1355 N TRP B 93 42.159 -24.688 -11.521 1.00 42.70 N ANISOU 1355 N TRP B 93 5020 6519 4684 -1763 376 447 N ATOM 1356 CA TRP B 93 41.104 -25.673 -11.701 1.00 37.89 C ANISOU 1356 CA TRP B 93 4357 6011 4028 -1436 310 322 C ATOM 1357 C TRP B 93 41.265 -26.429 -13.020 1.00 42.64 C ANISOU 1357 C TRP B 93 4871 6858 4471 -1454 550 231 C ATOM 1358 O TRP B 93 41.608 -25.842 -14.065 1.00 43.00 O ANISOU 1358 O TRP B 93 5081 6978 4277 -1637 715 343 O ATOM 1359 CB TRP B 93 39.720 -25.021 -11.646 1.00 36.32 C ANISOU 1359 CB TRP B 93 4522 5676 3602 -1207 76 411 C ATOM 1360 CG TRP B 93 38.615 -25.984 -12.036 1.00 40.17 C ANISOU 1360 CG TRP B 93 4934 6363 3968 -962 28 284 C ATOM 1361 CD1 TRP B 93 37.932 -26.026 -13.234 1.00 38.53 C ANISOU 1361 CD1 TRP B 93 4891 6316 3434 -893 83 286 C ATOM 1362 CD2 TRP B 93 38.087 -27.057 -11.236 1.00 33.25 C ANISOU 1362 CD2 TRP B 93 3796 5566 3271 -806 -83 139 C ATOM 1363 NE1 TRP B 93 37.010 -27.052 -13.214 1.00 36.57 N ANISOU 1363 NE1 TRP B 93 4482 6254 3159 -734 4 120 N ATOM 1364 CE2 TRP B 93 37.084 -27.700 -12.006 1.00 35.90 C ANISOU 1364 CE2 TRP B 93 4155 6100 3386 -699 -92 43 C ATOM 1365 CE3 TRP B 93 38.363 -27.537 -9.944 1.00 40.00 C ANISOU 1365 CE3 TRP B 93 4408 6358 4431 -766 -176 93 C ATOM 1366 CZ2 TRP B 93 36.362 -28.800 -11.528 1.00 37.26 C ANISOU 1366 CZ2 TRP B 93 4136 6376 3646 -619 -186 -93 C ATOM 1367 CZ3 TRP B 93 37.648 -28.631 -9.469 1.00 38.26 C ANISOU 1367 CZ3 TRP B 93 4015 6231 4292 -642 -262 -10 C ATOM 1368 CH2 TRP B 93 36.655 -29.249 -10.258 1.00 38.40 C ANISOU 1368 CH2 TRP B 93 4081 6412 4098 -600 -265 -100 C ATOM 1369 N SER B 94 41.056 -27.739 -12.963 1.00 41.31 N ANISOU 1369 N SER B 94 4464 6807 4424 -1276 573 26 N ATOM 1370 CA SER B 94 40.834 -28.511 -14.183 1.00 48.78 C ANISOU 1370 CA SER B 94 5407 7951 5177 -1223 732 -116 C ATOM 1371 C SER B 94 39.628 -29.422 -14.008 1.00 46.64 C ANISOU 1371 C SER B 94 5153 7667 4901 -1019 573 -264 C ATOM 1372 O SER B 94 39.380 -29.957 -12.909 1.00 42.79 O ANISOU 1372 O SER B 94 4540 7061 4659 -923 425 -306 O ATOM 1373 CB SER B 94 42.088 -29.276 -14.643 1.00 56.44 C ANISOU 1373 CB SER B 94 6083 9118 6243 -1278 1000 -269 C ATOM 1374 OG SER B 94 42.232 -30.533 -14.008 1.00 54.21 O ANISOU 1374 OG SER B 94 5577 8791 6229 -1086 974 -470 O ATOM 1375 N PRO B 95 38.856 -29.584 -15.092 1.00 45.48 N ANISOU 1375 N PRO B 95 5154 7679 4446 -982 598 -334 N ATOM 1376 CA PRO B 95 37.580 -30.303 -15.044 1.00 45.29 C ANISOU 1376 CA PRO B 95 5155 7713 4338 -868 433 -467 C ATOM 1377 C PRO B 95 37.726 -31.736 -14.542 1.00 38.65 C ANISOU 1377 C PRO B 95 4129 6774 3781 -847 445 -686 C ATOM 1378 O PRO B 95 36.768 -32.272 -14.009 1.00 45.48 O ANISOU 1378 O PRO B 95 4985 7618 4677 -823 272 -737 O ATOM 1379 CB PRO B 95 37.115 -30.283 -16.502 1.00 43.02 C ANISOU 1379 CB PRO B 95 5009 7683 3655 -875 524 -543 C ATOM 1380 CG PRO B 95 37.777 -29.092 -17.078 1.00 48.69 C ANISOU 1380 CG PRO B 95 5881 8423 4197 -951 650 -319 C ATOM 1381 CD PRO B 95 39.121 -29.028 -16.429 1.00 46.32 C ANISOU 1381 CD PRO B 95 5408 7970 4223 -1074 778 -272 C ATOM 1382 N ALA B 96 38.902 -32.331 -14.704 1.00 38.88 N ANISOU 1382 N ALA B 96 4023 6759 3992 -847 643 -803 N ATOM 1383 CA ALA B 96 39.125 -33.712 -14.290 1.00 42.35 C ANISOU 1383 CA ALA B 96 4364 7041 4686 -764 661 -1007 C ATOM 1384 C ALA B 96 39.326 -33.935 -12.775 1.00 47.36 C ANISOU 1384 C ALA B 96 4870 7463 5661 -695 525 -897 C ATOM 1385 O ALA B 96 39.373 -35.082 -12.328 1.00 51.01 O ANISOU 1385 O ALA B 96 5313 7744 6324 -614 507 -1018 O ATOM 1386 CB ALA B 96 40.298 -34.309 -15.072 1.00 44.52 C ANISOU 1386 CB ALA B 96 4546 7393 4979 -687 920 -1201 C ATOM 1387 N LEU B 97 39.458 -32.863 -11.994 1.00 45.31 N ANISOU 1387 N LEU B 97 4557 7209 5452 -722 426 -672 N ATOM 1388 CA LEU B 97 39.602 -33.005 -10.532 1.00 42.06 C ANISOU 1388 CA LEU B 97 4008 6656 5316 -647 282 -568 C ATOM 1389 C LEU B 97 38.332 -33.549 -9.891 1.00 40.49 C ANISOU 1389 C LEU B 97 3875 6394 5117 -637 78 -553 C ATOM 1390 O LEU B 97 37.236 -33.034 -10.132 1.00 41.30 O ANISOU 1390 O LEU B 97 4087 6625 4979 -687 -44 -508 O ATOM 1391 CB LEU B 97 39.968 -31.665 -9.886 1.00 45.20 C ANISOU 1391 CB LEU B 97 4367 7081 5725 -698 204 -371 C ATOM 1392 CG LEU B 97 41.347 -31.121 -10.266 1.00 53.67 C ANISOU 1392 CG LEU B 97 5316 8247 6829 -797 398 -355 C ATOM 1393 CD1 LEU B 97 41.594 -29.741 -9.666 1.00 45.68 C ANISOU 1393 CD1 LEU B 97 4347 7202 5805 -931 297 -175 C ATOM 1394 CD2 LEU B 97 42.428 -32.107 -9.818 1.00 58.33 C ANISOU 1394 CD2 LEU B 97 5627 8863 7673 -666 505 -465 C ATOM 1395 N THR B 98 38.478 -34.615 -9.110 1.00 38.89 N ANISOU 1395 N THR B 98 3602 6023 5151 -568 45 -584 N ATOM 1396 CA THR B 98 37.371 -35.155 -8.324 1.00 43.18 C ANISOU 1396 CA THR B 98 4176 6524 5706 -617 -140 -522 C ATOM 1397 C THR B 98 37.149 -34.360 -7.030 1.00 42.32 C ANISOU 1397 C THR B 98 3938 6500 5640 -555 -320 -310 C ATOM 1398 O THR B 98 38.046 -33.655 -6.569 1.00 39.22 O ANISOU 1398 O THR B 98 3438 6108 5357 -469 -303 -235 O ATOM 1399 CB THR B 98 37.560 -36.652 -7.999 1.00 45.72 C ANISOU 1399 CB THR B 98 4553 6575 6242 -593 -108 -606 C ATOM 1400 OG1 THR B 98 38.687 -36.833 -7.130 1.00 41.16 O ANISOU 1400 OG1 THR B 98 3836 5876 5926 -390 -74 -524 O ATOM 1401 CG2 THR B 98 37.772 -37.458 -9.283 1.00 44.88 C ANISOU 1401 CG2 THR B 98 4617 6358 6076 -621 58 -870 C ATOM 1402 N ILE B 99 35.938 -34.439 -6.482 1.00 37.55 N ANISOU 1402 N ILE B 99 4605 5504 4158 -579 161 -514 N ATOM 1403 CA ILE B 99 35.649 -33.890 -5.165 1.00 35.16 C ANISOU 1403 CA ILE B 99 4315 5150 3895 -586 52 -351 C ATOM 1404 C ILE B 99 36.609 -34.456 -4.112 1.00 39.17 C ANISOU 1404 C ILE B 99 4700 5543 4641 -585 -11 -322 C ATOM 1405 O ILE B 99 37.067 -33.758 -3.205 1.00 34.10 O ANISOU 1405 O ILE B 99 4055 4881 4022 -613 -51 -215 O ATOM 1406 CB ILE B 99 34.204 -34.185 -4.751 1.00 34.74 C ANISOU 1406 CB ILE B 99 4309 5098 3793 -578 -59 -318 C ATOM 1407 CG1 ILE B 99 33.277 -33.273 -5.541 1.00 38.85 C ANISOU 1407 CG1 ILE B 99 4942 5703 4118 -565 -66 -318 C ATOM 1408 CG2 ILE B 99 34.002 -33.941 -3.252 1.00 29.46 C ANISOU 1408 CG2 ILE B 99 3624 4401 3167 -619 -138 -200 C ATOM 1409 CD1 ILE B 99 33.643 -31.805 -5.387 1.00 39.51 C ANISOU 1409 CD1 ILE B 99 5091 5800 4120 -581 -56 -220 C ATOM 1410 N SER B 100 36.905 -35.735 -4.257 1.00 39.36 N ANISOU 1410 N SER B 100 4624 5470 4859 -550 -53 -427 N ATOM 1411 CA SER B 100 37.861 -36.428 -3.411 1.00 43.33 C ANISOU 1411 CA SER B 100 5004 5815 5646 -535 -177 -412 C ATOM 1412 C SER B 100 39.251 -35.753 -3.439 1.00 42.62 C ANISOU 1412 C SER B 100 4799 5732 5663 -529 -94 -454 C ATOM 1413 O SER B 100 39.883 -35.537 -2.396 1.00 38.22 O ANISOU 1413 O SER B 100 4202 5089 5230 -546 -221 -347 O ATOM 1414 CB SER B 100 37.944 -37.882 -3.882 1.00 50.11 C ANISOU 1414 CB SER B 100 5760 6540 6740 -475 -244 -573 C ATOM 1415 OG SER B 100 38.334 -38.732 -2.837 1.00 59.61 O ANISOU 1415 OG SER B 100 6906 7531 8212 -476 -480 -482 O ATOM 1416 N LYS B 101 39.725 -35.395 -4.627 1.00 42.52 N ANISOU 1416 N LYS B 101 4736 5834 5584 -532 119 -610 N ATOM 1417 CA LYS B 101 41.003 -34.699 -4.722 1.00 38.68 C ANISOU 1417 CA LYS B 101 4123 5380 5193 -567 237 -658 C ATOM 1418 C LYS B 101 40.926 -33.256 -4.192 1.00 37.34 C ANISOU 1418 C LYS B 101 4079 5267 4840 -643 237 -457 C ATOM 1419 O LYS B 101 41.884 -32.736 -3.621 1.00 37.72 O ANISOU 1419 O LYS B 101 4029 5270 5031 -670 215 -424 O ATOM 1420 CB LYS B 101 41.565 -34.774 -6.146 1.00 42.58 C ANISOU 1420 CB LYS B 101 4525 6012 5641 -600 503 -897 C ATOM 1421 CG LYS B 101 42.413 -36.013 -6.366 1.00 62.94 C ANISOU 1421 CG LYS B 101 6837 8491 8585 -511 508 -1178 C ATOM 1422 CD LYS B 101 42.016 -36.788 -7.621 1.00 79.05 C ANISOU 1422 CD LYS B 101 8876 10629 10530 -495 656 -1433 C ATOM 1423 CE LYS B 101 42.181 -35.956 -8.893 1.00 78.93 C ANISOU 1423 CE LYS B 101 8942 10886 10160 -643 975 -1520 C ATOM 1424 NZ LYS B 101 41.272 -36.425 -9.987 1.00 70.97 N ANISOU 1424 NZ LYS B 101 8085 10000 8880 -659 1046 -1646 N ATOM 1425 N VAL B 102 39.774 -32.619 -4.340 1.00 36.28 N ANISOU 1425 N VAL B 102 4145 5207 4431 -668 230 -343 N ATOM 1426 CA VAL B 102 39.615 -31.288 -3.780 1.00 37.86 C ANISOU 1426 CA VAL B 102 4452 5422 4512 -717 190 -188 C ATOM 1427 C VAL B 102 39.740 -31.335 -2.247 1.00 39.05 C ANISOU 1427 C VAL B 102 4572 5476 4788 -701 7 -97 C ATOM 1428 O VAL B 102 40.448 -30.526 -1.650 1.00 38.58 O ANISOU 1428 O VAL B 102 4485 5387 4788 -739 -27 -42 O ATOM 1429 CB VAL B 102 38.272 -30.654 -4.208 1.00 36.36 C ANISOU 1429 CB VAL B 102 4449 5296 4070 -718 170 -121 C ATOM 1430 CG1 VAL B 102 38.022 -29.356 -3.437 1.00 29.82 C ANISOU 1430 CG1 VAL B 102 3701 4438 3191 -737 81 -4 C ATOM 1431 CG2 VAL B 102 38.266 -30.405 -5.715 1.00 33.04 C ANISOU 1431 CG2 VAL B 102 4111 4972 3471 -775 313 -167 C ATOM 1432 N LEU B 103 39.052 -32.295 -1.627 1.00 35.21 N ANISOU 1432 N LEU B 103 4106 4947 4327 -672 -118 -76 N ATOM 1433 CA LEU B 103 39.059 -32.446 -0.179 1.00 32.42 C ANISOU 1433 CA LEU B 103 3773 4529 4016 -706 -298 31 C ATOM 1434 C LEU B 103 40.451 -32.766 0.344 1.00 32.43 C ANISOU 1434 C LEU B 103 3639 4407 4276 -702 -410 30 C ATOM 1435 O LEU B 103 40.899 -32.180 1.322 1.00 37.24 O ANISOU 1435 O LEU B 103 4266 4992 4892 -746 -523 109 O ATOM 1436 CB LEU B 103 38.065 -33.533 0.261 1.00 30.91 C ANISOU 1436 CB LEU B 103 3640 4317 3788 -728 -396 72 C ATOM 1437 CG LEU B 103 36.622 -33.111 -0.021 1.00 39.65 C ANISOU 1437 CG LEU B 103 4846 5549 4669 -738 -313 58 C ATOM 1438 CD1 LEU B 103 35.642 -34.259 0.269 1.00 34.99 C ANISOU 1438 CD1 LEU B 103 4282 4946 4066 -787 -378 81 C ATOM 1439 CD2 LEU B 103 36.275 -31.852 0.777 1.00 37.86 C ANISOU 1439 CD2 LEU B 103 4686 5404 4294 -777 -312 94 C ATOM 1440 N LEU B 104 41.129 -33.698 -0.320 1.00 37.91 N ANISOU 1440 N LEU B 104 4181 5019 5205 -643 -395 -90 N ATOM 1441 CA LEU B 104 42.507 -34.013 0.018 1.00 41.09 C ANISOU 1441 CA LEU B 104 4393 5287 5934 -612 -509 -146 C ATOM 1442 C LEU B 104 43.436 -32.809 -0.160 1.00 38.21 C ANISOU 1442 C LEU B 104 3940 4984 5595 -649 -384 -182 C ATOM 1443 O LEU B 104 44.383 -32.667 0.600 1.00 34.94 O ANISOU 1443 O LEU B 104 3418 4470 5387 -655 -539 -162 O ATOM 1444 CB LEU B 104 43.020 -35.225 -0.776 1.00 47.03 C ANISOU 1444 CB LEU B 104 4952 5938 6981 -521 -494 -345 C ATOM 1445 CG LEU B 104 42.305 -36.565 -0.513 1.00 56.27 C ANISOU 1445 CG LEU B 104 6181 6969 8232 -489 -686 -308 C ATOM 1446 CD1 LEU B 104 42.804 -37.683 -1.455 1.00 53.25 C ANISOU 1446 CD1 LEU B 104 5585 6477 8170 -379 -655 -573 C ATOM 1447 CD2 LEU B 104 42.423 -36.990 0.957 1.00 57.59 C ANISOU 1447 CD2 LEU B 104 6426 6961 8496 -539 -1037 -93 C ATOM 1448 N SER B 105 43.175 -31.951 -1.154 1.00 32.81 N ANISOU 1448 N SER B 105 3309 4447 4710 -692 -134 -220 N ATOM 1449 CA SER B 105 43.993 -30.746 -1.332 1.00 34.93 C ANISOU 1449 CA SER B 105 3521 4761 4988 -771 -21 -218 C ATOM 1450 C SER B 105 43.754 -29.754 -0.191 1.00 31.29 C ANISOU 1450 C SER B 105 3193 4270 4424 -811 -179 -61 C ATOM 1451 O SER B 105 44.657 -29.043 0.220 1.00 38.58 O ANISOU 1451 O SER B 105 4030 5151 5478 -860 -219 -53 O ATOM 1452 CB SER B 105 43.729 -30.068 -2.682 1.00 39.86 C ANISOU 1452 CB SER B 105 4222 5532 5390 -849 248 -251 C ATOM 1453 OG SER B 105 44.093 -30.924 -3.743 1.00 48.69 O ANISOU 1453 OG SER B 105 5205 6713 6583 -838 425 -444 O ATOM 1454 N ILE B 106 42.524 -29.713 0.301 1.00 33.77 N ANISOU 1454 N ILE B 106 3699 4618 4514 -797 -258 29 N ATOM 1455 CA ILE B 106 42.180 -28.843 1.411 1.00 31.92 C ANISOU 1455 CA ILE B 106 3582 4382 4164 -834 -389 117 C ATOM 1456 C ILE B 106 42.879 -29.341 2.696 1.00 40.42 C ANISOU 1456 C ILE B 106 4607 5365 5385 -849 -627 159 C ATOM 1457 O ILE B 106 43.460 -28.540 3.437 1.00 39.99 O ANISOU 1457 O ILE B 106 4547 5279 5368 -894 -730 179 O ATOM 1458 CB ILE B 106 40.645 -28.686 1.561 1.00 31.47 C ANISOU 1458 CB ILE B 106 3697 4411 3848 -823 -378 144 C ATOM 1459 CG1 ILE B 106 40.066 -27.949 0.344 1.00 32.89 C ANISOU 1459 CG1 ILE B 106 3941 4643 3913 -809 -223 122 C ATOM 1460 CG2 ILE B 106 40.287 -27.933 2.840 1.00 34.00 C ANISOU 1460 CG2 ILE B 106 4108 4753 4057 -865 -499 167 C ATOM 1461 CD1 ILE B 106 38.506 -28.025 0.253 1.00 30.16 C ANISOU 1461 CD1 ILE B 106 3707 4367 3384 -769 -223 106 C ATOM 1462 N CYS B 107 42.875 -30.658 2.923 1.00 33.58 N ANISOU 1462 N CYS B 107 3709 4432 4620 -821 -747 177 N ATOM 1463 CA CYS B 107 43.639 -31.249 4.030 1.00 34.15 C ANISOU 1463 CA CYS B 107 3742 4372 4862 -842 -1036 244 C ATOM 1464 C CYS B 107 45.139 -30.945 3.928 1.00 43.00 C ANISOU 1464 C CYS B 107 4637 5389 6311 -815 -1092 162 C ATOM 1465 O CYS B 107 45.757 -30.599 4.931 1.00 38.57 O ANISOU 1465 O CYS B 107 4078 4762 5813 -859 -1313 217 O ATOM 1466 CB CYS B 107 43.424 -32.764 4.125 1.00 39.24 C ANISOU 1466 CB CYS B 107 4384 4904 5620 -817 -1190 288 C ATOM 1467 SG CYS B 107 41.734 -33.262 4.488 1.00 50.71 S ANISOU 1467 SG CYS B 107 6079 6465 6722 -901 -1166 403 S ATOM 1468 N SER B 108 45.731 -31.071 2.734 1.00 40.95 N ANISOU 1468 N SER B 108 4174 5130 6256 -761 -888 11 N ATOM 1469 CA SER B 108 47.141 -30.691 2.569 1.00 38.15 C ANISOU 1469 CA SER B 108 3560 4710 6224 -763 -882 -104 C ATOM 1470 C SER B 108 47.346 -29.227 2.916 1.00 36.37 C ANISOU 1470 C SER B 108 3400 4542 5880 -857 -844 -49 C ATOM 1471 O SER B 108 48.368 -28.847 3.483 1.00 42.75 O ANISOU 1471 O SER B 108 4065 5262 6914 -884 -992 -73 O ATOM 1472 CB SER B 108 47.653 -30.927 1.147 1.00 37.60 C ANISOU 1472 CB SER B 108 3267 4701 6319 -740 -582 -308 C ATOM 1473 OG SER B 108 47.680 -32.298 0.847 1.00 58.50 O ANISOU 1473 OG SER B 108 5795 7259 9174 -635 -645 -423 O ATOM 1474 N LEU B 109 46.379 -28.399 2.542 1.00 37.39 N ANISOU 1474 N LEU B 109 3727 4792 5688 -902 -669 10 N ATOM 1475 CA LEU B 109 46.470 -26.983 2.849 1.00 40.91 C ANISOU 1475 CA LEU B 109 4247 5253 6043 -983 -660 53 C ATOM 1476 C LEU B 109 46.392 -26.739 4.367 1.00 41.47 C ANISOU 1476 C LEU B 109 4431 5275 6051 -999 -949 119 C ATOM 1477 O LEU B 109 46.992 -25.789 4.870 1.00 39.52 O ANISOU 1477 O LEU B 109 4156 4982 5877 -1056 -1036 108 O ATOM 1478 CB LEU B 109 45.390 -26.196 2.114 1.00 34.28 C ANISOU 1478 CB LEU B 109 3593 4509 4921 -1008 -471 95 C ATOM 1479 CG LEU B 109 45.424 -24.687 2.359 1.00 38.67 C ANISOU 1479 CG LEU B 109 4232 5033 5428 -1083 -492 131 C ATOM 1480 CD1 LEU B 109 46.620 -24.069 1.671 1.00 34.38 C ANISOU 1480 CD1 LEU B 109 3522 4449 5092 -1192 -368 110 C ATOM 1481 CD2 LEU B 109 44.129 -24.014 1.914 1.00 38.14 C ANISOU 1481 CD2 LEU B 109 4371 5011 5110 -1069 -421 172 C ATOM 1482 N LEU B 110 45.652 -27.581 5.094 1.00 39.61 N ANISOU 1482 N LEU B 110 4334 5058 5659 -975 -1094 183 N ATOM 1483 CA LEU B 110 45.632 -27.477 6.556 1.00 41.96 C ANISOU 1483 CA LEU B 110 4759 5341 5841 -1035 -1367 245 C ATOM 1484 C LEU B 110 46.990 -27.852 7.161 1.00 38.84 C ANISOU 1484 C LEU B 110 4207 4794 5756 -1039 -1646 252 C ATOM 1485 O LEU B 110 47.446 -27.219 8.114 1.00 44.18 O ANISOU 1485 O LEU B 110 4924 5443 6418 -1102 -1847 259 O ATOM 1486 CB LEU B 110 44.496 -28.295 7.193 1.00 38.10 C ANISOU 1486 CB LEU B 110 4473 4933 5069 -1069 -1435 333 C ATOM 1487 CG LEU B 110 43.038 -27.969 6.822 1.00 45.59 C ANISOU 1487 CG LEU B 110 5559 6036 5725 -1068 -1206 301 C ATOM 1488 CD1 LEU B 110 42.089 -28.470 7.906 1.00 40.85 C ANISOU 1488 CD1 LEU B 110 5150 5546 4826 -1172 -1300 364 C ATOM 1489 CD2 LEU B 110 42.805 -26.489 6.558 1.00 39.06 C ANISOU 1489 CD2 LEU B 110 4747 5255 4839 -1057 -1071 204 C ATOM 1490 N CYS B 111 47.635 -28.878 6.610 1.00 37.39 N ANISOU 1490 N CYS B 111 3828 4501 5878 -965 -1681 222 N ATOM 1491 CA CYS B 111 48.976 -29.244 7.046 1.00 39.91 C ANISOU 1491 CA CYS B 111 3932 4645 6589 -940 -1962 187 C ATOM 1492 C CYS B 111 50.028 -28.211 6.687 1.00 46.85 C ANISOU 1492 C CYS B 111 4580 5504 7715 -964 -1863 61 C ATOM 1493 O CYS B 111 50.947 -27.947 7.471 1.00 48.00 O ANISOU 1493 O CYS B 111 4629 5541 8069 -990 -2138 50 O ATOM 1494 CB CYS B 111 49.403 -30.581 6.445 1.00 56.15 C ANISOU 1494 CB CYS B 111 5780 6568 8984 -831 -2012 119 C ATOM 1495 SG CYS B 111 48.501 -31.972 7.075 1.00 70.62 S ANISOU 1495 SG CYS B 111 7850 8323 10660 -830 -2270 299 S ATOM 1496 N ASP B 112 49.932 -27.687 5.468 1.00 46.30 N ANISOU 1496 N ASP B 112 4420 5534 7637 -974 -1485 -28 N ATOM 1497 CA ASP B 112 50.940 -26.772 4.946 1.00 46.42 C ANISOU 1497 CA ASP B 112 4204 5541 7893 -1042 -1337 -137 C ATOM 1498 C ASP B 112 50.318 -25.581 4.233 1.00 50.15 C ANISOU 1498 C ASP B 112 4826 6133 8097 -1136 -1038 -99 C ATOM 1499 O ASP B 112 50.053 -25.636 3.032 1.00 48.58 O ANISOU 1499 O ASP B 112 4603 6028 7828 -1156 -731 -132 O ATOM 1500 CB ASP B 112 51.944 -27.509 4.063 1.00 44.93 C ANISOU 1500 CB ASP B 112 3646 5312 8113 -998 -1207 -321 C ATOM 1501 CG ASP B 112 52.828 -28.459 4.859 1.00 62.55 C ANISOU 1501 CG ASP B 112 5669 7352 10747 -899 -1593 -381 C ATOM 1502 OD1 ASP B 112 53.779 -27.983 5.533 1.00 75.84 O ANISOU 1502 OD1 ASP B 112 7198 8931 12687 -935 -1820 -414 O ATOM 1503 OD2 ASP B 112 52.569 -29.679 4.814 1.00 64.32 O ANISOU 1503 OD2 ASP B 112 5883 7503 11051 -788 -1706 -393 O ATOM 1504 N PRO B 113 50.041 -24.517 4.998 1.00 49.23 N ANISOU 1504 N PRO B 113 4881 6000 7823 -1195 -1161 -34 N ATOM 1505 CA PRO B 113 49.503 -23.251 4.501 1.00 45.98 C ANISOU 1505 CA PRO B 113 4614 5630 7225 -1277 -979 6 C ATOM 1506 C PRO B 113 50.402 -22.601 3.449 1.00 47.22 C ANISOU 1506 C PRO B 113 4576 5776 7589 -1407 -746 -29 C ATOM 1507 O PRO B 113 51.599 -22.899 3.364 1.00 42.18 O ANISOU 1507 O PRO B 113 3645 5097 7283 -1444 -746 -126 O ATOM 1508 CB PRO B 113 49.452 -22.381 5.764 1.00 40.49 C ANISOU 1508 CB PRO B 113 4046 4871 6469 -1304 -1241 11 C ATOM 1509 CG PRO B 113 49.288 -23.376 6.884 1.00 39.34 C ANISOU 1509 CG PRO B 113 3969 4733 6245 -1235 -1507 26 C ATOM 1510 CD PRO B 113 50.146 -24.530 6.471 1.00 42.44 C ANISOU 1510 CD PRO B 113 4116 5072 6936 -1185 -1525 -1 C ATOM 1511 N ASN B 114 49.813 -21.697 2.669 1.00 42.54 N ANISOU 1511 N ASN B 114 4141 5213 6807 -1493 -562 50 N ATOM 1512 CA ASN B 114 50.560 -20.920 1.689 1.00 45.69 C ANISOU 1512 CA ASN B 114 4426 5607 7327 -1685 -341 68 C ATOM 1513 C ASN B 114 50.486 -19.472 2.136 1.00 47.94 C ANISOU 1513 C ASN B 114 4846 5755 7613 -1779 -481 145 C ATOM 1514 O ASN B 114 49.694 -18.683 1.614 1.00 47.84 O ANISOU 1514 O ASN B 114 5057 5712 7408 -1829 -431 256 O ATOM 1515 CB ASN B 114 49.966 -21.066 0.282 1.00 52.80 C ANISOU 1515 CB ASN B 114 5438 6633 7991 -1749 -43 132 C ATOM 1516 CG ASN B 114 50.025 -22.503 -0.238 1.00 65.91 C ANISOU 1516 CG ASN B 114 6956 8424 9664 -1655 106 12 C ATOM 1517 OD1 ASN B 114 51.075 -23.145 -0.204 1.00 68.97 O ANISOU 1517 OD1 ASN B 114 7039 8821 10347 -1654 147 -140 O ATOM 1518 ND2 ASN B 114 48.886 -23.012 -0.717 1.00 60.81 N ANISOU 1518 ND2 ASN B 114 6510 7858 8735 -1566 166 55 N ATOM 1519 N PRO B 115 51.322 -19.117 3.125 1.00 46.09 N ANISOU 1519 N PRO B 115 4473 5413 7626 -1797 -698 75 N ATOM 1520 CA PRO B 115 51.229 -17.798 3.747 1.00 45.43 C ANISOU 1520 CA PRO B 115 4515 5178 7570 -1858 -886 101 C ATOM 1521 C PRO B 115 51.628 -16.654 2.795 1.00 52.13 C ANISOU 1521 C PRO B 115 5363 5936 8508 -2091 -729 209 C ATOM 1522 O PRO B 115 51.283 -15.512 3.080 1.00 52.81 O ANISOU 1522 O PRO B 115 5608 5864 8594 -2134 -879 254 O ATOM 1523 CB PRO B 115 52.211 -17.906 4.915 1.00 45.35 C ANISOU 1523 CB PRO B 115 4315 5095 7822 -1841 -1147 -17 C ATOM 1524 CG PRO B 115 53.260 -18.840 4.410 1.00 48.74 C ANISOU 1524 CG PRO B 115 4423 5588 8507 -1871 -1011 -81 C ATOM 1525 CD PRO B 115 52.491 -19.874 3.616 1.00 48.97 C ANISOU 1525 CD PRO B 115 4529 5768 8308 -1773 -794 -50 C ATOM 1526 N ASP B 116 52.335 -16.933 1.702 1.00 57.79 N ANISOU 1526 N ASP B 116 5909 6746 9304 -2255 -438 240 N ATOM 1527 CA ASP B 116 52.716 -15.845 0.792 1.00 67.03 C ANISOU 1527 CA ASP B 116 7113 7844 10511 -2540 -281 381 C ATOM 1528 C ASP B 116 51.596 -15.489 -0.180 1.00 66.02 C ANISOU 1528 C ASP B 116 7310 7728 10045 -2583 -181 568 C ATOM 1529 O ASP B 116 51.695 -14.516 -0.920 1.00 80.18 O ANISOU 1529 O ASP B 116 9225 9426 11812 -2827 -117 744 O ATOM 1530 CB ASP B 116 54.012 -16.150 0.043 1.00 74.38 C ANISOU 1530 CB ASP B 116 7714 8894 11655 -2766 15 318 C ATOM 1531 CG ASP B 116 55.202 -16.226 0.965 1.00 85.53 C ANISOU 1531 CG ASP B 116 8781 10232 13482 -2757 -139 143 C ATOM 1532 OD1 ASP B 116 55.125 -15.648 2.069 1.00 79.04 O ANISOU 1532 OD1 ASP B 116 8032 9237 12762 -2669 -475 127 O ATOM 1533 OD2 ASP B 116 56.207 -16.870 0.595 1.00 98.82 O ANISOU 1533 OD2 ASP B 116 10112 12034 15403 -2834 61 -7 O ATOM 1534 N ASP B 117 50.529 -16.276 -0.155 1.00 60.79 N ANISOU 1534 N ASP B 117 6794 7166 9138 -2358 -200 542 N ATOM 1535 CA ASP B 117 49.314 -15.962 -0.891 1.00 60.65 C ANISOU 1535 CA ASP B 117 7084 7133 8828 -2341 -195 692 C ATOM 1536 C ASP B 117 48.104 -16.022 0.047 1.00 53.71 C ANISOU 1536 C ASP B 117 6360 6193 7854 -2063 -450 614 C ATOM 1537 O ASP B 117 47.211 -16.868 -0.120 1.00 45.71 O ANISOU 1537 O ASP B 117 5425 5307 6633 -1904 -405 583 O ATOM 1538 CB ASP B 117 49.130 -16.933 -2.051 1.00 72.90 C ANISOU 1538 CB ASP B 117 8643 8910 10147 -2379 96 714 C ATOM 1539 CG ASP B 117 48.036 -16.499 -2.992 1.00 81.88 C ANISOU 1539 CG ASP B 117 10101 10020 10988 -2424 87 900 C ATOM 1540 OD1 ASP B 117 47.907 -15.273 -3.203 1.00 74.91 O ANISOU 1540 OD1 ASP B 117 9397 8940 10127 -2570 -53 1075 O ATOM 1541 OD2 ASP B 117 47.307 -17.379 -3.507 1.00 90.01 O ANISOU 1541 OD2 ASP B 117 11207 11203 11791 -2312 181 873 O ATOM 1542 N PRO B 118 48.099 -15.146 1.043 1.00 49.39 N ANISOU 1542 N PRO B 118 5839 5462 7466 -2018 -708 553 N ATOM 1543 CA PRO B 118 47.152 -15.238 2.153 1.00 48.71 C ANISOU 1543 CA PRO B 118 5840 5354 7313 -1786 -924 403 C ATOM 1544 C PRO B 118 45.788 -14.627 1.880 1.00 52.95 C ANISOU 1544 C PRO B 118 6605 5806 7708 -1681 -1021 431 C ATOM 1545 O PRO B 118 45.638 -13.770 1.014 1.00 57.63 O ANISOU 1545 O PRO B 118 7329 6231 8335 -1797 -1062 586 O ATOM 1546 CB PRO B 118 47.851 -14.442 3.251 1.00 43.32 C ANISOU 1546 CB PRO B 118 5080 4507 6871 -1826 -1140 299 C ATOM 1547 CG PRO B 118 48.602 -13.403 2.514 1.00 48.38 C ANISOU 1547 CG PRO B 118 5712 4977 7691 -2068 -1104 457 C ATOM 1548 CD PRO B 118 49.024 -14.012 1.205 1.00 47.76 C ANISOU 1548 CD PRO B 118 5575 5060 7513 -2219 -795 605 C ATOM 1549 N LEU B 119 44.802 -15.078 2.643 1.00 48.02 N ANISOU 1549 N LEU B 119 6020 5294 6934 -1477 -1067 289 N ATOM 1550 CA LEU B 119 43.481 -14.484 2.639 1.00 52.89 C ANISOU 1550 CA LEU B 119 6774 5807 7516 -1338 -1224 197 C ATOM 1551 C LEU B 119 43.360 -13.656 3.905 1.00 53.74 C ANISOU 1551 C LEU B 119 6858 5780 7781 -1277 -1445 -20 C ATOM 1552 O LEU B 119 42.604 -12.690 3.962 1.00 56.17 O ANISOU 1552 O LEU B 119 7245 5885 8211 -1215 -1623 -99 O ATOM 1553 CB LEU B 119 42.405 -15.566 2.613 1.00 48.19 C ANISOU 1553 CB LEU B 119 6203 5414 6695 -1176 -1138 115 C ATOM 1554 CG LEU B 119 41.110 -15.218 1.881 1.00 48.85 C ANISOU 1554 CG LEU B 119 6416 5420 6726 -1089 -1197 146 C ATOM 1555 CD1 LEU B 119 41.401 -14.840 0.442 1.00 49.12 C ANISOU 1555 CD1 LEU B 119 6572 5310 6780 -1250 -1188 417 C ATOM 1556 CD2 LEU B 119 40.132 -16.375 1.947 1.00 40.37 C ANISOU 1556 CD2 LEU B 119 5328 4571 5438 -970 -1071 83 C ATOM 1557 N VAL B 120 44.122 -14.043 4.921 1.00 49.24 N ANISOU 1557 N VAL B 120 6179 5314 7217 -1291 -1459 -134 N ATOM 1558 CA VAL B 120 44.144 -13.307 6.187 1.00 52.08 C ANISOU 1558 CA VAL B 120 6523 5598 7668 -1250 -1658 -374 C ATOM 1559 C VAL B 120 45.585 -12.913 6.519 1.00 50.89 C ANISOU 1559 C VAL B 120 6268 5341 7728 -1401 -1744 -334 C ATOM 1560 O VAL B 120 46.335 -13.706 7.086 1.00 49.34 O ANISOU 1560 O VAL B 120 5972 5285 7489 -1434 -1727 -344 O ATOM 1561 CB VAL B 120 43.543 -14.119 7.365 1.00 53.31 C ANISOU 1561 CB VAL B 120 6676 6002 7577 -1145 -1647 -586 C ATOM 1562 CG1 VAL B 120 43.267 -13.195 8.555 1.00 43.72 C ANISOU 1562 CG1 VAL B 120 5476 4727 6407 -1101 -1832 -894 C ATOM 1563 CG2 VAL B 120 42.267 -14.832 6.938 1.00 49.90 C ANISOU 1563 CG2 VAL B 120 6298 5723 6937 -1032 -1506 -592 C ATOM 1564 N PRO B 121 45.989 -11.698 6.112 1.00 50.85 N ANISOU 1564 N PRO B 121 5999 5605 7717 -897 660 -1262 N ATOM 1565 CA PRO B 121 47.383 -11.246 6.255 1.00 52.17 C ANISOU 1565 CA PRO B 121 6172 5798 7854 -1102 558 -1282 C ATOM 1566 C PRO B 121 47.944 -11.366 7.689 1.00 53.34 C ANISOU 1566 C PRO B 121 6384 6154 7727 -1411 470 -1408 C ATOM 1567 O PRO B 121 49.091 -11.783 7.867 1.00 48.74 O ANISOU 1567 O PRO B 121 5723 5740 7054 -1558 274 -1298 O ATOM 1568 CB PRO B 121 47.326 -9.775 5.814 1.00 45.31 C ANISOU 1568 CB PRO B 121 5395 4634 7189 -1094 739 -1421 C ATOM 1569 CG PRO B 121 46.111 -9.682 4.928 1.00 47.81 C ANISOU 1569 CG PRO B 121 5685 4775 7703 -800 880 -1357 C ATOM 1570 CD PRO B 121 45.122 -10.666 5.504 1.00 48.54 C ANISOU 1570 CD PRO B 121 5753 5040 7651 -732 878 -1344 C ATOM 1571 N GLU B 122 47.154 -11.012 8.696 1.00 47.56 N ANISOU 1571 N GLU B 122 5784 5428 6857 -1513 615 -1627 N ATOM 1572 CA GLU B 122 47.668 -10.993 10.064 1.00 47.51 C ANISOU 1572 CA GLU B 122 5868 5623 6561 -1841 545 -1769 C ATOM 1573 C GLU B 122 48.016 -12.401 10.539 1.00 49.65 C ANISOU 1573 C GLU B 122 6027 6210 6628 -1906 303 -1559 C ATOM 1574 O GLU B 122 48.964 -12.589 11.288 1.00 58.28 O ANISOU 1574 O GLU B 122 7113 7502 7530 -2166 128 -1536 O ATOM 1575 CB GLU B 122 46.689 -10.304 11.014 1.00 50.39 C ANISOU 1575 CB GLU B 122 6411 5928 6807 -1924 787 -2069 C ATOM 1576 CG GLU B 122 45.223 -10.333 10.538 1.00 77.15 C ANISOU 1576 CG GLU B 122 9778 9178 10357 -1619 1001 -2077 C ATOM 1577 CD GLU B 122 44.918 -9.366 9.378 1.00 85.58 C ANISOU 1577 CD GLU B 122 10845 9898 11775 -1385 1159 -2088 C ATOM 1578 OE1 GLU B 122 45.423 -8.216 9.387 1.00 88.09 O ANISOU 1578 OE1 GLU B 122 11280 10008 12181 -1496 1245 -2256 O ATOM 1579 OE2 GLU B 122 44.154 -9.758 8.465 1.00 79.52 O ANISOU 1579 OE2 GLU B 122 9962 9064 11188 -1106 1187 -1918 O ATOM 1580 N ILE B 123 47.264 -13.389 10.068 1.00 43.39 N ANISOU 1580 N ILE B 123 5144 5452 5889 -1673 279 -1387 N ATOM 1581 CA ILE B 123 47.524 -14.780 10.419 1.00 45.17 C ANISOU 1581 CA ILE B 123 5273 5926 5963 -1702 51 -1166 C ATOM 1582 C ILE B 123 48.733 -15.272 9.644 1.00 42.76 C ANISOU 1582 C ILE B 123 4824 5645 5780 -1637 -155 -940 C ATOM 1583 O ILE B 123 49.569 -16.002 10.175 1.00 44.18 O ANISOU 1583 O ILE B 123 4926 6033 5826 -1771 -372 -796 O ATOM 1584 CB ILE B 123 46.288 -15.670 10.150 1.00 45.66 C ANISOU 1584 CB ILE B 123 5303 5994 6051 -1493 93 -1061 C ATOM 1585 CG1 ILE B 123 45.124 -15.213 11.024 1.00 43.03 C ANISOU 1585 CG1 ILE B 123 5082 5685 5582 -1567 309 -1275 C ATOM 1586 CG2 ILE B 123 46.592 -17.163 10.376 1.00 42.91 C ANISOU 1586 CG2 ILE B 123 4864 5849 5589 -1502 -158 -805 C ATOM 1587 CD1 ILE B 123 43.904 -16.097 10.895 1.00 38.10 C ANISOU 1587 CD1 ILE B 123 4406 5112 4958 -1409 340 -1157 C ATOM 1588 N ALA B 124 48.842 -14.841 8.392 1.00 36.68 N ANISOU 1588 N ALA B 124 4007 4669 5263 -1433 -81 -903 N ATOM 1589 CA ALA B 124 49.987 -15.209 7.575 1.00 39.45 C ANISOU 1589 CA ALA B 124 4213 5040 5735 -1356 -231 -708 C ATOM 1590 C ALA B 124 51.270 -14.647 8.172 1.00 40.25 C ANISOU 1590 C ALA B 124 4283 5257 5754 -1630 -335 -738 C ATOM 1591 O ALA B 124 52.327 -15.285 8.116 1.00 44.32 O ANISOU 1591 O ALA B 124 4650 5928 6264 -1655 -526 -549 O ATOM 1592 CB ALA B 124 49.796 -14.736 6.121 1.00 39.86 C ANISOU 1592 CB ALA B 124 4238 4861 6046 -1112 -106 -675 C ATOM 1593 N ARG B 125 51.172 -13.447 8.738 1.00 47.32 N ANISOU 1593 N ARG B 125 5316 6070 6594 -1835 -208 -976 N ATOM 1594 CA ARG B 125 52.318 -12.774 9.344 1.00 49.39 C ANISOU 1594 CA ARG B 125 5578 6427 6763 -2147 -304 -1035 C ATOM 1595 C ARG B 125 52.822 -13.582 10.536 1.00 53.87 C ANISOU 1595 C ARG B 125 6100 7309 7059 -2378 -523 -950 C ATOM 1596 O ARG B 125 54.025 -13.785 10.699 1.00 52.54 O ANISOU 1596 O ARG B 125 5793 7315 6857 -2526 -723 -799 O ATOM 1597 CB ARG B 125 51.934 -11.361 9.786 1.00 47.26 C ANISOU 1597 CB ARG B 125 5516 5970 6472 -2325 -106 -1345 C ATOM 1598 CG ARG B 125 52.984 -10.635 10.611 1.00 48.29 C ANISOU 1598 CG ARG B 125 5698 6200 6451 -2715 -206 -1452 C ATOM 1599 CD ARG B 125 52.388 -9.394 11.276 1.00 49.79 C ANISOU 1599 CD ARG B 125 6152 6198 6569 -2897 7 -1808 C ATOM 1600 NE ARG B 125 53.427 -8.601 11.927 1.00 63.67 N ANISOU 1600 NE ARG B 125 7982 8012 8200 -3291 -91 -1923 N ATOM 1601 CZ ARG B 125 53.227 -7.440 12.551 1.00 69.26 C ANISOU 1601 CZ ARG B 125 8937 8549 8830 -3524 61 -2247 C ATOM 1602 NH1 ARG B 125 52.013 -6.912 12.630 1.00 75.12 N ANISOU 1602 NH1 ARG B 125 9866 9050 9625 -3375 340 -2492 N ATOM 1603 NH2 ARG B 125 54.250 -6.801 13.100 1.00 62.58 N ANISOU 1603 NH2 ARG B 125 8142 7774 7863 -3787 -64 -2253 N ATOM 1604 N ILE B 126 51.886 -14.058 11.350 1.00 51.55 N ANISOU 1604 N ILE B 126 5908 7101 6577 -2407 -488 -1022 N ATOM 1605 CA ILE B 126 52.227 -14.862 12.516 1.00 51.37 C ANISOU 1605 CA ILE B 126 5858 7384 6277 -2633 -696 -922 C ATOM 1606 C ILE B 126 52.804 -16.207 12.094 1.00 50.94 C ANISOU 1606 C ILE B 126 5593 7461 6303 -2461 -924 -579 C ATOM 1607 O ILE B 126 53.755 -16.697 12.703 1.00 56.68 O ANISOU 1607 O ILE B 126 6205 8422 6907 -2639 -1160 -410 O ATOM 1608 CB ILE B 126 51.012 -15.057 13.453 1.00 51.75 C ANISOU 1608 CB ILE B 126 6065 7499 6097 -2702 -581 -1072 C ATOM 1609 CG1 ILE B 126 50.584 -13.710 14.038 1.00 56.97 C ANISOU 1609 CG1 ILE B 126 6944 8049 6654 -2899 -351 -1436 C ATOM 1610 CG2 ILE B 126 51.345 -16.031 14.582 1.00 52.20 C ANISOU 1610 CG2 ILE B 126 6082 7889 5865 -2924 -819 -911 C ATOM 1611 CD1 ILE B 126 49.344 -13.781 14.897 1.00 60.12 C ANISOU 1611 CD1 ILE B 126 7493 8509 6843 -2943 -179 -1614 C ATOM 1612 N TYR B 127 52.238 -16.793 11.040 1.00 48.29 N ANISOU 1612 N TYR B 127 5206 6966 6177 -2117 -856 -476 N ATOM 1613 CA TYR B 127 52.736 -18.063 10.515 1.00 42.06 C ANISOU 1613 CA TYR B 127 4243 6242 5494 -1915 -1039 -180 C ATOM 1614 C TYR B 127 54.177 -17.934 10.001 1.00 47.15 C ANISOU 1614 C TYR B 127 4700 6938 6276 -1915 -1160 -35 C ATOM 1615 O TYR B 127 55.016 -18.796 10.264 1.00 47.58 O ANISOU 1615 O TYR B 127 4595 7169 6313 -1926 -1377 199 O ATOM 1616 CB TYR B 127 51.826 -18.577 9.401 1.00 42.29 C ANISOU 1616 CB TYR B 127 4289 6066 5712 -1570 -920 -141 C ATOM 1617 CG TYR B 127 52.230 -19.938 8.886 1.00 46.91 C ANISOU 1617 CG TYR B 127 4742 6683 6399 -1358 -1088 127 C ATOM 1618 CD1 TYR B 127 53.174 -20.073 7.875 1.00 44.30 C ANISOU 1618 CD1 TYR B 127 4265 6298 6269 -1179 -1121 252 C ATOM 1619 CD2 TYR B 127 51.672 -21.091 9.424 1.00 42.31 C ANISOU 1619 CD2 TYR B 127 4186 6178 5711 -1339 -1203 254 C ATOM 1620 CE1 TYR B 127 53.549 -21.321 7.413 1.00 46.71 C ANISOU 1620 CE1 TYR B 127 4464 6609 6676 -966 -1250 472 C ATOM 1621 CE2 TYR B 127 52.036 -22.334 8.972 1.00 46.88 C ANISOU 1621 CE2 TYR B 127 4669 6744 6399 -1142 -1352 488 C ATOM 1622 CZ TYR B 127 52.974 -22.450 7.965 1.00 48.58 C ANISOU 1622 CZ TYR B 127 4749 6886 6822 -945 -1369 585 C ATOM 1623 OH TYR B 127 53.326 -23.701 7.524 1.00 46.24 O ANISOU 1623 OH TYR B 127 4372 6554 6642 -729 -1494 795 O ATOM 1624 N LYS B 128 54.462 -16.854 9.275 1.00 48.85 N ANISOU 1624 N LYS B 128 4922 7003 6636 -1902 -1020 -155 N ATOM 1625 CA LYS B 128 55.811 -16.613 8.741 1.00 48.04 C ANISOU 1625 CA LYS B 128 4628 6960 6666 -1919 -1108 -21 C ATOM 1626 C LYS B 128 56.845 -16.279 9.808 1.00 55.11 C ANISOU 1626 C LYS B 128 5451 8098 7392 -2284 -1292 11 C ATOM 1627 O LYS B 128 58.025 -16.573 9.632 1.00 58.57 O ANISOU 1627 O LYS B 128 5663 8686 7904 -2297 -1448 221 O ATOM 1628 CB LYS B 128 55.794 -15.528 7.651 1.00 48.38 C ANISOU 1628 CB LYS B 128 4703 6774 6905 -1827 -908 -139 C ATOM 1629 CG LYS B 128 55.109 -15.981 6.349 1.00 49.28 C ANISOU 1629 CG LYS B 128 4819 6696 7210 -1453 -776 -86 C ATOM 1630 CD LYS B 128 54.853 -14.834 5.363 1.00 47.95 C ANISOU 1630 CD LYS B 128 4719 6293 7206 -1384 -572 -207 C ATOM 1631 CE LYS B 128 56.152 -14.187 4.880 1.00 49.72 C ANISOU 1631 CE LYS B 128 4792 6564 7536 -1483 -601 -125 C ATOM 1632 NZ LYS B 128 57.008 -15.110 4.068 1.00 55.78 N ANISOU 1632 NZ LYS B 128 5335 7447 8413 -1272 -684 116 N ATOM 1633 N THR B 129 56.408 -15.684 10.916 1.00 58.51 N ANISOU 1633 N THR B 129 6065 8581 7587 -2583 -1273 -193 N ATOM 1634 CA THR B 129 57.336 -15.210 11.950 1.00 67.08 C ANISOU 1634 CA THR B 129 7122 9893 8473 -2988 -1444 -202 C ATOM 1635 C THR B 129 57.398 -16.082 13.213 1.00 77.93 C ANISOU 1635 C THR B 129 8518 11508 9583 -3092 -1620 -78 C ATOM 1636 O THR B 129 58.470 -16.569 13.568 1.00 85.93 O ANISOU 1636 O THR B 129 9382 12697 10570 -3106 -1802 156 O ATOM 1637 CB THR B 129 57.146 -13.712 12.297 1.00 68.27 C ANISOU 1637 CB THR B 129 7493 9906 8541 -3261 -1284 -528 C ATOM 1638 OG1 THR B 129 55.822 -13.482 12.786 1.00 67.14 O ANISOU 1638 OG1 THR B 129 7602 9642 8265 -3262 -1096 -784 O ATOM 1639 CG2 THR B 129 57.384 -12.851 11.060 1.00 66.36 C ANISOU 1639 CG2 THR B 129 7218 9413 8583 -3118 -1127 -574 C ATOM 1640 N ASP B 130 56.284 -16.224 13.930 1.00 75.65 N ANISOU 1640 N ASP B 130 8422 11228 9094 -3169 -1545 -230 N ATOM 1641 CA ASP B 130 56.271 -17.124 15.081 1.00 69.72 C ANISOU 1641 CA ASP B 130 7696 10699 8094 -3250 -1696 -79 C ATOM 1642 C ASP B 130 55.341 -18.327 14.846 1.00 66.43 C ANISOU 1642 C ASP B 130 7254 10270 7716 -3031 -1717 50 C ATOM 1643 O ASP B 130 54.124 -18.239 15.023 1.00 58.70 O ANISOU 1643 O ASP B 130 6427 9236 6639 -3059 -1575 -134 O ATOM 1644 CB ASP B 130 55.788 -16.330 16.294 1.00 69.99 C ANISOU 1644 CB ASP B 130 7983 10799 7809 -3560 -1595 -344 C ATOM 1645 CG ASP B 130 56.074 -17.022 17.607 1.00 75.78 C ANISOU 1645 CG ASP B 130 8741 11801 8252 -3727 -1759 -174 C ATOM 1646 OD1 ASP B 130 56.563 -18.172 17.602 1.00 78.48 O ANISOU 1646 OD1 ASP B 130 8914 12253 8652 -3591 -1948 151 O ATOM 1647 OD2 ASP B 130 55.814 -16.396 18.653 1.00 78.47 O ANISOU 1647 OD2 ASP B 130 9278 12231 8307 -3999 -1685 -369 O ATOM 1648 N ARG B 131 55.940 -19.480 14.569 1.00 64.46 N ANISOU 1648 N ARG B 131 6821 10079 7592 -2827 -1893 370 N ATOM 1649 CA ARG B 131 55.190 -20.657 14.140 1.00 64.56 C ANISOU 1649 CA ARG B 131 6800 10027 7702 -2580 -1927 520 C ATOM 1650 C ARG B 131 54.582 -21.377 15.332 1.00 58.99 C ANISOU 1650 C ARG B 131 6217 9469 6727 -2708 -1994 589 C ATOM 1651 O ARG B 131 53.457 -21.871 15.262 1.00 55.25 O ANISOU 1651 O ARG B 131 5823 8942 6226 -2637 -1938 563 O ATOM 1652 CB ARG B 131 56.072 -21.606 13.323 1.00 63.70 C ANISOU 1652 CB ARG B 131 6474 9875 7856 -2283 -2056 814 C ATOM 1653 CG ARG B 131 55.357 -22.857 12.828 1.00 65.10 C ANISOU 1653 CG ARG B 131 6643 9939 8154 -2010 -2092 968 C ATOM 1654 CD ARG B 131 54.448 -22.577 11.617 1.00 56.16 C ANISOU 1654 CD ARG B 131 5592 8537 7208 -1759 -1865 798 C ATOM 1655 NE ARG B 131 55.182 -21.889 10.564 1.00 64.42 N ANISOU 1655 NE ARG B 131 6534 9473 8471 -1621 -1764 748 N ATOM 1656 CZ ARG B 131 55.947 -22.495 9.660 1.00 66.26 C ANISOU 1656 CZ ARG B 131 6597 9646 8933 -1360 -1815 928 C ATOM 1657 NH1 ARG B 131 56.063 -23.817 9.668 1.00 59.21 N ANISOU 1657 NH1 ARG B 131 5633 8758 8104 -1190 -1966 1160 N ATOM 1658 NH2 ARG B 131 56.593 -21.774 8.747 1.00 64.88 N ANISOU 1658 NH2 ARG B 131 6327 9400 8923 -1270 -1705 876 N ATOM 1659 N GLU B 132 55.347 -21.428 16.421 1.00 62.68 N ANISOU 1659 N GLU B 132 6689 10130 6995 -2912 -2115 695 N ATOM 1660 CA GLU B 132 54.881 -21.964 17.697 1.00 62.50 C ANISOU 1660 CA GLU B 132 6787 10283 6679 -3098 -2170 765 C ATOM 1661 C GLU B 132 53.628 -21.231 18.165 1.00 63.03 C ANISOU 1661 C GLU B 132 7066 10361 6521 -3281 -1969 447 C ATOM 1662 O GLU B 132 52.712 -21.844 18.717 1.00 69.88 O ANISOU 1662 O GLU B 132 8021 11302 7230 -3321 -1950 482 O ATOM 1663 CB GLU B 132 55.981 -21.859 18.753 1.00 62.14 C ANISOU 1663 CB GLU B 132 6713 10449 6450 -3335 -2313 898 C ATOM 1664 CG GLU B 132 55.561 -22.369 20.123 1.00 86.38 C ANISOU 1664 CG GLU B 132 9902 13722 9197 -3564 -2368 987 C ATOM 1665 CD GLU B 132 56.679 -22.285 21.156 1.00106.75 C ANISOU 1665 CD GLU B 132 12442 16520 11597 -3815 -2523 1145 C ATOM 1666 OE1 GLU B 132 57.844 -22.586 20.813 1.00116.36 O ANISOU 1666 OE1 GLU B 132 13470 17739 13001 -3711 -2671 1367 O ATOM 1667 OE2 GLU B 132 56.393 -21.911 22.314 1.00108.83 O ANISOU 1667 OE2 GLU B 132 12858 16963 11528 -4125 -2489 1048 O ATOM 1668 N LYS B 133 53.588 -19.919 17.943 1.00 58.79 N ANISOU 1668 N LYS B 133 6613 9744 5980 -3393 -1804 138 N ATOM 1669 CA LYS B 133 52.421 -19.124 18.312 1.00 58.86 C ANISOU 1669 CA LYS B 133 6827 9726 5809 -3542 -1566 -206 C ATOM 1670 C LYS B 133 51.243 -19.437 17.398 1.00 52.27 C ANISOU 1670 C LYS B 133 5983 8729 5149 -3325 -1440 -275 C ATOM 1671 O LYS B 133 50.137 -19.694 17.864 1.00 58.93 O ANISOU 1671 O LYS B 133 6932 9620 5836 -3352 -1324 -351 O ATOM 1672 CB LYS B 133 52.728 -17.628 18.268 1.00 62.18 C ANISOU 1672 CB LYS B 133 7358 10045 6223 -3697 -1407 -523 C ATOM 1673 CG LYS B 133 51.511 -16.769 18.569 1.00 67.95 C ANISOU 1673 CG LYS B 133 8309 10694 6814 -3806 -1115 -912 C ATOM 1674 CD LYS B 133 51.829 -15.286 18.494 1.00 79.30 C ANISOU 1674 CD LYS B 133 9881 11965 8284 -3933 -945 -1225 C ATOM 1675 CE LYS B 133 50.578 -14.455 18.724 1.00 85.51 C ANISOU 1675 CE LYS B 133 10889 12618 8982 -3979 -614 -1625 C ATOM 1676 NZ LYS B 133 50.877 -13.000 18.802 1.00 91.04 N ANISOU 1676 NZ LYS B 133 11759 13126 9706 -4101 -438 -1929 N ATOM 1677 N TYR B 134 51.488 -19.413 16.094 1.00 51.00 N ANISOU 1677 N TYR B 134 5712 8330 5335 -3020 -1404 -219 N ATOM 1678 CA TYR B 134 50.467 -19.795 15.126 1.00 49.97 C ANISOU 1678 CA TYR B 134 5592 7967 5428 -2673 -1242 -215 C ATOM 1679 C TYR B 134 49.846 -21.139 15.510 1.00 47.21 C ANISOU 1679 C TYR B 134 5224 7730 4985 -2627 -1367 10 C ATOM 1680 O TYR B 134 48.627 -21.257 15.586 1.00 46.74 O ANISOU 1680 O TYR B 134 5257 7626 4876 -2568 -1207 -78 O ATOM 1681 CB TYR B 134 51.041 -19.868 13.714 1.00 53.82 C ANISOU 1681 CB TYR B 134 5945 8238 6266 -2365 -1253 -106 C ATOM 1682 CG TYR B 134 50.192 -20.721 12.794 1.00 55.46 C ANISOU 1682 CG TYR B 134 6136 8273 6665 -2036 -1200 5 C ATOM 1683 CD1 TYR B 134 49.070 -20.200 12.156 1.00 52.18 C ANISOU 1683 CD1 TYR B 134 5813 7656 6357 -1872 -950 -175 C ATOM 1684 CD2 TYR B 134 50.499 -22.056 12.589 1.00 56.92 C ANISOU 1684 CD2 TYR B 134 6216 8492 6920 -1900 -1408 295 C ATOM 1685 CE1 TYR B 134 48.288 -20.995 11.336 1.00 54.40 C ANISOU 1685 CE1 TYR B 134 6080 7801 6789 -1610 -927 -64 C ATOM 1686 CE2 TYR B 134 49.730 -22.851 11.774 1.00 53.17 C ANISOU 1686 CE2 TYR B 134 5752 7850 6599 -1635 -1372 382 C ATOM 1687 CZ TYR B 134 48.631 -22.321 11.153 1.00 52.75 C ANISOU 1687 CZ TYR B 134 5790 7626 6627 -1506 -1140 204 C ATOM 1688 OH TYR B 134 47.891 -23.132 10.340 1.00 56.12 O ANISOU 1688 OH TYR B 134 6226 7906 7191 -1275 -1131 302 O ATOM 1689 N ASN B 135 50.689 -22.134 15.780 1.00 47.81 N ANISOU 1689 N ASN B 135 5172 7951 5041 -2664 -1656 314 N ATOM 1690 CA ASN B 135 50.209 -23.463 16.165 1.00 53.65 C ANISOU 1690 CA ASN B 135 5898 8778 5707 -2637 -1808 565 C ATOM 1691 C ASN B 135 49.338 -23.410 17.413 1.00 56.15 C ANISOU 1691 C ASN B 135 6353 9313 5668 -2924 -1750 471 C ATOM 1692 O ASN B 135 48.294 -24.048 17.483 1.00 58.49 O ANISOU 1692 O ASN B 135 6700 9594 5928 -2861 -1694 524 O ATOM 1693 CB ASN B 135 51.373 -24.441 16.375 1.00 54.58 C ANISOU 1693 CB ASN B 135 5895 8952 5891 -2570 -2058 901 C ATOM 1694 CG ASN B 135 52.025 -24.870 15.064 1.00 57.04 C ANISOU 1694 CG ASN B 135 6054 9061 6559 -2246 -2125 1038 C ATOM 1695 OD1 ASN B 135 51.406 -24.813 14.006 1.00 50.66 O ANISOU 1695 OD1 ASN B 135 5257 8048 5944 -2028 -2002 947 O ATOM 1696 ND2 ASN B 135 53.280 -25.305 15.136 1.00 64.88 N ANISOU 1696 ND2 ASN B 135 6926 10083 7644 -2177 -2266 1247 N ATOM 1697 N ARG B 136 49.784 -22.636 18.393 1.00 59.49 N ANISOU 1697 N ARG B 136 6858 9900 5846 -3190 -1710 333 N ATOM 1698 CA AARG B 136 49.065 -22.512 19.649 0.47 57.53 C ANISOU 1698 CA AARG B 136 6756 9867 5236 -3462 -1616 227 C ATOM 1699 CA BARG B 136 49.078 -22.482 19.657 0.53 57.42 C ANISOU 1699 CA BARG B 136 6743 9854 5219 -3466 -1614 221 C ATOM 1700 C ARG B 136 47.660 -21.961 19.412 1.00 54.86 C ANISOU 1700 C ARG B 136 6518 9463 4862 -3443 -1338 -69 C ATOM 1701 O ARG B 136 46.673 -22.545 19.859 1.00 58.34 O ANISOU 1701 O ARG B 136 7001 10004 5160 -3475 -1283 -15 O ATOM 1702 CB AARG B 136 49.847 -21.627 20.624 0.47 59.09 C ANISOU 1702 CB AARG B 136 7040 10215 5198 -3739 -1595 93 C ATOM 1703 CB BARG B 136 49.868 -21.520 20.554 0.53 59.04 C ANISOU 1703 CB BARG B 136 7034 10192 5206 -3734 -1583 67 C ATOM 1704 CG AARG B 136 49.271 -21.578 22.021 0.47 59.23 C ANISOU 1704 CG AARG B 136 7203 10483 4818 -4038 -1511 18 C ATOM 1705 CG BARG B 136 49.779 -21.786 22.041 0.53 63.55 C ANISOU 1705 CG BARG B 136 7703 11038 5405 -4025 -1610 137 C ATOM 1706 CD AARG B 136 50.109 -20.685 22.939 0.47 69.77 C ANISOU 1706 CD AARG B 136 8629 11949 5930 -4319 -1500 -113 C ATOM 1707 CD BARG B 136 50.987 -21.184 22.794 0.53 67.01 C ANISOU 1707 CD BARG B 136 8164 11597 5700 -4250 -1696 137 C ATOM 1708 NE AARG B 136 50.204 -19.309 22.456 0.47 69.56 N ANISOU 1708 NE AARG B 136 8689 11758 5983 -4332 -1313 -479 N ATOM 1709 NE BARG B 136 51.179 -19.758 22.528 0.53 68.46 N ANISOU 1709 NE BARG B 136 8441 11669 5899 -4325 -1525 -222 N ATOM 1710 CZ AARG B 136 49.222 -18.414 22.531 0.47 69.06 C ANISOU 1710 CZ AARG B 136 8788 11632 5820 -4397 -1020 -864 C ATOM 1711 CZ BARG B 136 52.334 -19.213 22.150 0.53 68.38 C ANISOU 1711 CZ BARG B 136 8362 11583 6036 -4317 -1617 -206 C ATOM 1712 NH1AARG B 136 48.054 -18.745 23.062 0.47 67.62 N ANISOU 1712 NH1AARG B 136 8681 11576 5435 -4457 -877 -940 N ATOM 1713 NH1BARG B 136 53.408 -19.975 21.996 0.53 65.37 N ANISOU 1713 NH1BARG B 136 7802 11244 5792 -4226 -1868 141 N ATOM 1714 NH2AARG B 136 49.407 -17.184 22.072 0.47 68.34 N ANISOU 1714 NH2AARG B 136 8779 11340 5845 -4394 -857 -1172 N ATOM 1715 NH2BARG B 136 52.418 -17.907 21.930 0.53 63.65 N ANISOU 1715 NH2BARG B 136 7871 10856 5456 -4398 -1448 -535 N ATOM 1716 N ILE B 137 47.564 -20.856 18.687 1.00 60.68 N ANISOU 1716 N ILE B 137 7298 9967 5789 -3301 -1104 -345 N ATOM 1717 CA ILE B 137 46.271 -20.253 18.381 1.00 57.21 C ANISOU 1717 CA ILE B 137 6950 9372 5415 -3152 -766 -598 C ATOM 1718 C ILE B 137 45.372 -21.183 17.544 1.00 57.45 C ANISOU 1718 C ILE B 137 6898 9264 5667 -2851 -753 -409 C ATOM 1719 O ILE B 137 44.175 -21.315 17.826 1.00 59.29 O ANISOU 1719 O ILE B 137 7172 9544 5811 -2839 -583 -468 O ATOM 1720 CB ILE B 137 46.445 -18.876 17.696 1.00 51.25 C ANISOU 1720 CB ILE B 137 6251 8362 4862 -3047 -546 -892 C ATOM 1721 CG1 ILE B 137 47.262 -17.949 18.603 1.00 59.39 C ANISOU 1721 CG1 ILE B 137 7395 9526 5647 -3392 -558 -1101 C ATOM 1722 CG2 ILE B 137 45.098 -18.256 17.407 1.00 48.79 C ANISOU 1722 CG2 ILE B 137 6012 7886 4639 -2875 -201 -1127 C ATOM 1723 CD1 ILE B 137 47.681 -16.652 17.961 1.00 60.78 C ANISOU 1723 CD1 ILE B 137 7624 9443 6026 -3334 -404 -1345 C ATOM 1724 N ALA B 138 45.949 -21.838 16.536 1.00 49.88 N ANISOU 1724 N ALA B 138 5823 8147 4983 -2621 -929 -183 N ATOM 1725 CA ALA B 138 45.176 -22.736 15.674 1.00 52.42 C ANISOU 1725 CA ALA B 138 6088 8318 5511 -2354 -939 -12 C ATOM 1726 C ALA B 138 44.531 -23.851 16.493 1.00 46.24 C ANISOU 1726 C ALA B 138 5315 7735 4519 -2492 -1055 189 C ATOM 1727 O ALA B 138 43.357 -24.167 16.288 1.00 45.08 O ANISOU 1727 O ALA B 138 5178 7548 4402 -2402 -935 198 O ATOM 1728 CB ALA B 138 46.039 -23.306 14.521 1.00 40.65 C ANISOU 1728 CB ALA B 138 4492 6636 4317 -2107 -1115 184 C ATOM 1729 N ARG B 139 45.291 -24.427 17.426 1.00 49.00 N ANISOU 1729 N ARG B 139 5652 8309 4654 -2727 -1296 370 N ATOM 1730 CA AARG B 139 44.782 -25.468 18.331 0.57 50.90 C ANISOU 1730 CA AARG B 139 5909 8767 4664 -2908 -1432 591 C ATOM 1731 CA BARG B 139 44.757 -25.474 18.299 0.43 50.26 C ANISOU 1731 CA BARG B 139 5827 8679 4591 -2899 -1428 590 C ATOM 1732 C ARG B 139 43.642 -24.966 19.212 1.00 52.08 C ANISOU 1732 C ARG B 139 6152 9107 4529 -3102 -1184 388 C ATOM 1733 O ARG B 139 42.626 -25.633 19.371 1.00 62.48 O ANISOU 1733 O ARG B 139 7468 10481 5790 -3106 -1147 497 O ATOM 1734 CB AARG B 139 45.899 -25.999 19.231 0.57 56.25 C ANISOU 1734 CB AARG B 139 6553 9669 5151 -3146 -1734 819 C ATOM 1735 CB BARG B 139 45.870 -26.131 19.118 0.43 56.14 C ANISOU 1735 CB BARG B 139 6530 9630 5171 -3114 -1750 849 C ATOM 1736 CG AARG B 139 46.947 -26.849 18.532 0.57 58.88 C ANISOU 1736 CG AARG B 139 6787 9799 5786 -2895 -1950 1101 C ATOM 1737 CG BARG B 139 46.744 -27.083 18.312 0.43 58.01 C ANISOU 1737 CG BARG B 139 6670 9642 5729 -2838 -1958 1136 C ATOM 1738 CD AARG B 139 47.889 -27.497 19.546 0.57 62.23 C ANISOU 1738 CD AARG B 139 7200 10349 6095 -3022 -2120 1356 C ATOM 1739 CD BARG B 139 47.780 -27.778 19.181 0.43 62.24 C ANISOU 1739 CD BARG B 139 7185 10269 6196 -2924 -2140 1402 C ATOM 1740 NE AARG B 139 49.292 -27.181 19.287 0.57 64.16 N ANISOU 1740 NE AARG B 139 7354 10541 6482 -2947 -2217 1391 N ATOM 1741 NE BARG B 139 48.646 -28.655 18.397 0.43 63.73 N ANISOU 1741 NE BARG B 139 7275 10236 6703 -2652 -2304 1638 N ATOM 1742 CZ AARG B 139 50.065 -26.479 20.108 0.57 64.47 C ANISOU 1742 CZ AARG B 139 7404 10758 6332 -3168 -2225 1324 C ATOM 1743 CZ BARG B 139 48.351 -29.913 18.082 0.43 65.49 C ANISOU 1743 CZ BARG B 139 7500 10300 7085 -2497 -2402 1870 C ATOM 1744 NH1AARG B 139 49.584 -26.020 21.256 0.57 76.99 N ANISOU 1744 NH1AARG B 139 9106 12576 7572 -3474 -2133 1202 N ATOM 1745 NH1BARG B 139 47.204 -30.453 18.479 0.43 66.64 N ANISOU 1745 NH1BARG B 139 7725 10489 7104 -2599 -2371 1926 N ATOM 1746 NH2AARG B 139 51.323 -26.249 19.789 0.57 57.70 N ANISOU 1746 NH2AARG B 139 6441 9855 5627 -3092 -2321 1383 N ATOM 1747 NH2BARG B 139 49.205 -30.631 17.368 0.43 64.72 N ANISOU 1747 NH2BARG B 139 7322 9994 7274 -2248 -2519 2035 N ATOM 1748 N GLU B 140 43.826 -23.790 19.803 1.00 55.54 N ANISOU 1748 N GLU B 140 6673 9647 4783 -3274 -1009 88 N ATOM 1749 CA GLU B 140 42.783 -23.190 20.635 1.00 59.71 C ANISOU 1749 CA GLU B 140 7299 10344 5043 -3438 -724 -157 C ATOM 1750 C GLU B 140 41.481 -22.974 19.834 1.00 59.33 C ANISOU 1750 C GLU B 140 7219 10104 5222 -3163 -446 -269 C ATOM 1751 O GLU B 140 40.389 -23.234 20.337 1.00 55.44 O ANISOU 1751 O GLU B 140 6727 9763 4573 -3230 -302 -269 O ATOM 1752 CB GLU B 140 43.284 -21.886 21.286 1.00 75.00 C ANISOU 1752 CB GLU B 140 9358 12359 6778 -3647 -571 -500 C ATOM 1753 CG GLU B 140 42.408 -20.645 21.060 1.00 91.36 C ANISOU 1753 CG GLU B 140 11512 14277 8925 -3526 -161 -893 C ATOM 1754 CD GLU B 140 43.103 -19.331 21.454 1.00101.73 C ANISOU 1754 CD GLU B 140 12964 15562 10127 -3695 -41 -1233 C ATOM 1755 OE1 GLU B 140 44.211 -19.379 22.039 1.00104.35 O ANISOU 1755 OE1 GLU B 140 13329 16054 10264 -3959 -277 -1169 O ATOM 1756 OE2 GLU B 140 42.539 -18.247 21.174 1.00101.26 O ANISOU 1756 OE2 GLU B 140 12979 15311 10184 -3568 282 -1554 O ATOM 1757 N TRP B 141 41.595 -22.515 18.587 1.00 48.40 N ANISOU 1757 N TRP B 141 5788 8405 4198 -2862 -378 -342 N ATOM 1758 CA TRP B 141 40.409 -22.345 17.740 1.00 46.76 C ANISOU 1758 CA TRP B 141 5528 8016 4224 -2598 -155 -403 C ATOM 1759 C TRP B 141 39.782 -23.671 17.365 1.00 47.10 C ANISOU 1759 C TRP B 141 5486 8063 4346 -2514 -314 -89 C ATOM 1760 O TRP B 141 38.555 -23.783 17.271 1.00 52.82 O ANISOU 1760 O TRP B 141 6165 8811 5093 -2448 -149 -91 O ATOM 1761 CB TRP B 141 40.751 -21.590 16.471 1.00 44.45 C ANISOU 1761 CB TRP B 141 5209 7400 4282 -2320 -81 -516 C ATOM 1762 CG TRP B 141 40.848 -20.129 16.661 1.00 63.02 C ANISOU 1762 CG TRP B 141 7645 9675 6624 -2346 177 -863 C ATOM 1763 CD1 TRP B 141 41.627 -19.457 17.570 1.00 58.02 C ANISOU 1763 CD1 TRP B 141 7124 9164 5759 -2603 184 -1047 C ATOM 1764 CD2 TRP B 141 40.162 -19.136 15.901 1.00 63.77 C ANISOU 1764 CD2 TRP B 141 7732 9533 6965 -2112 455 -1063 C ATOM 1765 NE1 TRP B 141 41.458 -18.101 17.416 1.00 63.75 N ANISOU 1765 NE1 TRP B 141 7930 9716 6578 -2541 462 -1372 N ATOM 1766 CE2 TRP B 141 40.564 -17.878 16.400 1.00 64.78 C ANISOU 1766 CE2 TRP B 141 7983 9619 7013 -2229 634 -1378 C ATOM 1767 CE3 TRP B 141 39.247 -19.187 14.842 1.00 59.65 C ANISOU 1767 CE3 TRP B 141 7112 8827 6725 -1824 558 -995 C ATOM 1768 CZ2 TRP B 141 40.074 -16.682 15.881 1.00 70.97 C ANISOU 1768 CZ2 TRP B 141 8796 10158 8012 -2046 921 -1620 C ATOM 1769 CZ3 TRP B 141 38.765 -17.999 14.326 1.00 66.78 C ANISOU 1769 CZ3 TRP B 141 8022 9518 7833 -1645 831 -1215 C ATOM 1770 CH2 TRP B 141 39.178 -16.763 14.845 1.00 73.22 C ANISOU 1770 CH2 TRP B 141 8963 10269 8586 -1745 1014 -1522 C ATOM 1771 N THR B 142 40.624 -24.675 17.146 1.00 44.63 N ANISOU 1771 N THR B 142 5149 7722 4089 -2515 -634 184 N ATOM 1772 CA THR B 142 40.143 -26.016 16.850 1.00 50.90 C ANISOU 1772 CA THR B 142 5897 8494 4951 -2464 -818 490 C ATOM 1773 C THR B 142 39.343 -26.503 18.041 1.00 53.59 C ANISOU 1773 C THR B 142 6253 9134 4973 -2731 -795 577 C ATOM 1774 O THR B 142 38.197 -26.941 17.917 1.00 60.36 O ANISOU 1774 O THR B 142 7069 10017 5849 -2704 -713 657 O ATOM 1775 CB THR B 142 41.303 -26.996 16.593 1.00 48.67 C ANISOU 1775 CB THR B 142 5599 8130 4764 -2435 -1161 759 C ATOM 1776 OG1 THR B 142 42.021 -26.591 15.422 1.00 49.74 O ANISOU 1776 OG1 THR B 142 5706 8000 5193 -2178 -1165 686 O ATOM 1777 CG2 THR B 142 40.766 -28.411 16.390 1.00 44.78 C ANISOU 1777 CG2 THR B 142 5094 7592 4330 -2410 -1350 1066 C ATOM 1778 N GLN B 143 39.974 -26.421 19.201 1.00 53.68 N ANISOU 1778 N GLN B 143 6320 9396 4680 -3009 -874 574 N ATOM 1779 CA GLN B 143 39.357 -26.815 20.449 1.00 51.58 C ANISOU 1779 CA GLN B 143 6083 9462 4053 -3308 -853 652 C ATOM 1780 C GLN B 143 38.069 -26.040 20.684 1.00 52.56 C ANISOU 1780 C GLN B 143 6201 9682 4087 -3305 -472 396 C ATOM 1781 O GLN B 143 37.074 -26.612 21.097 1.00 54.14 O ANISOU 1781 O GLN B 143 6362 10053 4158 -3404 -416 521 O ATOM 1782 CB GLN B 143 40.345 -26.605 21.603 1.00 55.62 C ANISOU 1782 CB GLN B 143 6668 10230 4236 -3615 -980 637 C ATOM 1783 CG GLN B 143 41.475 -27.621 21.616 1.00 62.05 C ANISOU 1783 CG GLN B 143 7451 11026 5099 -3658 -1385 984 C ATOM 1784 CD GLN B 143 42.692 -27.127 22.365 1.00 74.09 C ANISOU 1784 CD GLN B 143 9016 12687 6446 -3850 -1484 933 C ATOM 1785 OE1 GLN B 143 42.683 -26.035 22.930 1.00 69.26 O ANISOU 1785 OE1 GLN B 143 8483 12233 5598 -4027 -1296 620 O ATOM 1786 NE2 GLN B 143 43.753 -27.924 22.363 1.00 82.82 N ANISOU 1786 NE2 GLN B 143 10079 13668 7723 -3765 -1722 1231 N ATOM 1787 N LYS B 144 38.067 -24.742 20.410 1.00 61.66 N ANISOU 1787 N LYS B 144 7383 10720 5324 -3184 -202 49 N ATOM 1788 CA LYS B 144 36.840 -23.995 20.629 1.00 65.19 C ANISOU 1788 CA LYS B 144 7810 11240 5718 -3146 178 -191 C ATOM 1789 C LYS B 144 35.722 -24.312 19.632 1.00 63.82 C ANISOU 1789 C LYS B 144 7503 10906 5841 -2884 268 -85 C ATOM 1790 O LYS B 144 34.624 -24.687 20.039 1.00 68.24 O ANISOU 1790 O LYS B 144 7990 11654 6285 -2957 390 -8 O ATOM 1791 CB LYS B 144 37.107 -22.487 20.622 1.00 69.77 C ANISOU 1791 CB LYS B 144 8473 11705 6331 -3080 453 -596 C ATOM 1792 CG LYS B 144 35.849 -21.670 20.873 1.00 78.04 C ANISOU 1792 CG LYS B 144 9496 12807 7349 -3007 874 -858 C ATOM 1793 CD LYS B 144 36.143 -20.189 20.964 1.00 84.82 C ANISOU 1793 CD LYS B 144 10470 13525 8232 -2960 1146 -1267 C ATOM 1794 CE LYS B 144 34.891 -19.419 21.365 1.00 95.94 C ANISOU 1794 CE LYS B 144 11857 15004 9592 -2889 1586 -1532 C ATOM 1795 NZ LYS B 144 35.170 -17.970 21.599 1.00107.27 N ANISOU 1795 NZ LYS B 144 13443 16289 11024 -2869 1868 -1958 N ATOM 1796 N TYR B 145 35.976 -24.128 18.337 1.00 60.85 N ANISOU 1796 N TYR B 145 7087 10204 5831 -2597 215 -80 N ATOM 1797 CA TYR B 145 34.914 -24.366 17.346 1.00 55.50 C ANISOU 1797 CA TYR B 145 6284 9382 5423 -2366 290 18 C ATOM 1798 C TYR B 145 34.780 -25.731 16.648 1.00 53.20 C ANISOU 1798 C TYR B 145 5942 9000 5271 -2320 -7 367 C ATOM 1799 O TYR B 145 33.732 -26.025 16.065 1.00 46.75 O ANISOU 1799 O TYR B 145 5021 8144 4597 -2214 51 467 O ATOM 1800 CB TYR B 145 35.011 -23.301 16.255 1.00 53.18 C ANISOU 1800 CB TYR B 145 5971 8789 5448 -2074 445 -184 C ATOM 1801 CG TYR B 145 35.146 -21.890 16.758 1.00 57.93 C ANISOU 1801 CG TYR B 145 6641 9389 5980 -2082 741 -543 C ATOM 1802 CD1 TYR B 145 34.036 -21.177 17.204 1.00 62.71 C ANISOU 1802 CD1 TYR B 145 7195 10096 6536 -2052 1093 -734 C ATOM 1803 CD2 TYR B 145 36.385 -21.254 16.761 1.00 59.22 C ANISOU 1803 CD2 TYR B 145 6919 9436 6145 -2113 676 -694 C ATOM 1804 CE1 TYR B 145 34.165 -19.868 17.646 1.00 71.37 C ANISOU 1804 CE1 TYR B 145 8382 11146 7588 -2046 1379 -1088 C ATOM 1805 CE2 TYR B 145 36.524 -19.953 17.197 1.00 57.95 C ANISOU 1805 CE2 TYR B 145 6849 9239 5929 -2139 938 -1033 C ATOM 1806 CZ TYR B 145 35.412 -19.264 17.634 1.00 72.55 C ANISOU 1806 CZ TYR B 145 8675 11157 7735 -2099 1291 -1240 C ATOM 1807 OH TYR B 145 35.558 -17.971 18.072 1.00 88.55 O ANISOU 1807 OH TYR B 145 10819 13110 9717 -2119 1562 -1599 O ATOM 1808 N ALA B 146 35.840 -26.530 16.651 1.00 57.02 N ANISOU 1808 N ALA B 146 6498 9434 5735 -2390 -320 549 N ATOM 1809 CA ALA B 146 35.840 -27.795 15.905 1.00 51.23 C ANISOU 1809 CA ALA B 146 5751 8548 5166 -2320 -598 849 C ATOM 1810 C ALA B 146 35.630 -29.073 16.716 1.00 54.52 C ANISOU 1810 C ALA B 146 6186 9150 5380 -2566 -813 1146 C ATOM 1811 O ALA B 146 35.695 -30.171 16.170 1.00 57.47 O ANISOU 1811 O ALA B 146 6577 9371 5887 -2526 -1058 1395 O ATOM 1812 CB ALA B 146 37.050 -27.900 14.972 1.00 46.44 C ANISOU 1812 CB ALA B 146 5192 7666 4788 -2133 -789 873 C ATOM 1813 N MET B 147 35.453 -28.927 18.023 1.00 60.91 N ANISOU 1813 N MET B 147 7008 10277 5859 -2831 -728 1119 N ATOM 1814 CA MET B 147 35.260 -30.070 18.912 1.00 66.73 C ANISOU 1814 CA MET B 147 7763 11227 6366 -3102 -925 1415 C ATOM 1815 C MET B 147 34.005 -29.841 19.733 1.00 77.91 C ANISOU 1815 C MET B 147 9108 12953 7539 -3282 -669 1366 C ATOM 1816 O MET B 147 33.583 -28.692 19.907 1.00 79.11 O ANISOU 1816 O MET B 147 9225 13191 7640 -3227 -341 1064 O ATOM 1817 CB MET B 147 36.448 -30.244 19.866 1.00 64.51 C ANISOU 1817 CB MET B 147 7566 11093 5852 -3309 -1121 1488 C ATOM 1818 CG MET B 147 37.791 -30.390 19.181 1.00 76.36 C ANISOU 1818 CG MET B 147 9105 12332 7577 -3137 -1353 1534 C ATOM 1819 SD MET B 147 39.157 -30.661 20.331 1.00 72.02 S ANISOU 1819 SD MET B 147 8610 11992 6764 -3396 -1616 1680 S ATOM 1820 CE MET B 147 38.882 -32.366 20.796 1.00 73.13 C ANISOU 1820 CE MET B 147 8764 12122 6900 -3525 -1867 2127 C ATOM 1821 OXT MET B 147 33.407 -30.788 20.245 1.00 83.83 O ANISOU 1821 OXT MET B 147 9835 13872 8146 -3483 -777 1628 O TER 1822 MET B 147 HETATM 1823 ZN ZN A1436 33.165 -35.732 -21.995 1.00 42.42 ZN HETATM 1824 ZN ZN A1437 46.714 -33.656 -20.649 1.00 50.41 ZN HETATM 1825 K K B1148 22.947 -39.746 -8.762 0.50 21.67 K HETATM 1826 O HOH A2001 44.939 -44.314 -21.264 1.00 56.67 O HETATM 1827 O HOH A2002 28.326 -42.897 -14.106 1.00 54.26 O HETATM 1828 O HOH A2003 29.290 -31.936 -18.262 1.00 36.73 O HETATM 1829 O HOH A2004 38.998 -21.918 -14.958 1.00 62.86 O HETATM 1830 O HOH A2005 34.608 -51.887 -16.717 1.00 47.05 O HETATM 1831 O HOH A2006 38.578 -42.573 -13.357 1.00 53.14 O HETATM 1832 O HOH A2007 40.303 -40.364 -18.099 1.00 44.88 O HETATM 1833 O HOH A2008 40.387 -39.975 -15.273 1.00 58.91 O HETATM 1834 O HOH A2009 42.306 -42.786 -20.298 1.00 41.86 O HETATM 1835 O HOH A2010 40.491 -53.545 -5.529 1.00 65.66 O HETATM 1836 O HOH A2011 35.213 -44.578 -11.000 1.00 67.35 O HETATM 1837 O HOH A2012 31.910 -44.364 -9.889 1.00 57.12 O HETATM 1838 O HOH A2013 28.434 -47.374 -14.729 1.00 64.63 O HETATM 1839 O HOH A2014 30.450 -44.622 -14.310 1.00 58.30 O HETATM 1840 O HOH A2015 29.451 -44.337 -11.520 1.00 57.07 O HETATM 1841 O HOH A2016 30.769 -50.809 -14.457 1.00 63.79 O HETATM 1842 O HOH A2017 29.925 -46.612 -19.764 1.00 59.09 O HETATM 1843 O HOH A2018 35.840 -50.973 -18.921 1.00 38.95 O HETATM 1844 O HOH A2019 34.652 -51.725 -21.322 1.00 44.48 O HETATM 1845 O HOH A2020 38.230 -39.274 -19.586 1.00 36.63 O HETATM 1846 O HOH A2021 34.640 -39.030 -13.405 1.00 44.62 O HETATM 1847 O HOH A2022 37.859 -37.046 -13.720 1.00 52.86 O HETATM 1848 O HOH A2023 28.196 -34.245 -16.959 1.00 34.46 O HETATM 1849 O HOH A2024 27.099 -42.652 -17.925 1.00 61.71 O HETATM 1850 O HOH A2025 27.426 -40.473 -14.730 1.00 34.84 O HETATM 1851 O HOH A2026 29.296 -41.379 -26.631 1.00 56.75 O HETATM 1852 O HOH A2027 32.129 -39.795 -27.850 1.00 61.78 O HETATM 1853 O HOH A2028 29.656 -43.999 -27.704 1.00 78.34 O HETATM 1854 O HOH A2029 33.568 -46.031 -27.284 1.00 54.40 O HETATM 1855 O HOH A2030 34.904 -43.961 -28.631 1.00 54.13 O HETATM 1856 O HOH A2031 42.640 -40.126 -19.992 1.00 47.33 O HETATM 1857 O HOH A2032 30.768 -28.015 -26.108 1.00 60.92 O HETATM 1858 O HOH A2033 30.585 -32.381 -22.679 1.00 48.03 O HETATM 1859 O HOH A2034 31.136 -24.330 -20.668 1.00 68.15 O HETATM 1860 O HOH A2035 29.566 -29.906 -22.614 1.00 65.49 O HETATM 1861 O HOH A2036 28.920 -25.517 -22.752 1.00 76.49 O HETATM 1862 O HOH A2037 36.978 -22.562 -16.757 1.00 55.27 O HETATM 1863 O HOH A2038 42.794 -22.626 -17.254 1.00 55.82 O HETATM 1864 O HOH A2039 41.935 -23.371 -14.643 1.00 48.01 O HETATM 1865 O HOH A2040 44.905 -20.366 -15.385 1.00 74.59 O HETATM 1866 O HOH A2041 52.524 -27.066 -21.980 1.00 63.29 O HETATM 1867 O HOH A2042 47.001 -25.427 -25.736 1.00 59.84 O HETATM 1868 O HOH A2043 46.412 -26.185 -29.624 1.00 65.26 O HETATM 1869 O HOH A2044 50.726 -32.865 -33.216 1.00 83.43 O HETATM 1870 O HOH A2045 44.303 -29.495 -32.511 1.00 50.86 O HETATM 1871 O HOH B2001 28.237 -29.693 -17.471 1.00 37.68 O HETATM 1872 O HOH B2002 25.523 -33.827 -17.160 1.00 38.84 O HETATM 1873 O HOH B2003 24.489 -42.048 -17.063 1.00 79.65 O HETATM 1874 O HOH B2004 34.100 -38.307 -10.769 1.00 52.22 O HETATM 1875 O HOH B2005 25.729 -44.771 -13.001 1.00 50.07 O HETATM 1876 O HOH B2006 36.386 -43.740 -12.961 1.00 48.91 O HETATM 1877 O HOH B2007 34.787 -37.924 -5.850 1.00 50.43 O HETATM 1878 O HOH B2008 28.458 -41.872 -1.527 1.00 59.77 O HETATM 1879 O HOH B2009 38.547 -41.370 -3.305 1.00 61.21 O HETATM 1880 O HOH B2010 45.603 -37.229 9.543 1.00 65.56 O HETATM 1881 O HOH B2011 42.984 -35.527 7.146 1.00 66.84 O HETATM 1882 O HOH B2012 30.519 -38.381 7.747 1.00 71.79 O HETATM 1883 O HOH B2013 29.086 -34.902 4.988 1.00 68.23 O HETATM 1884 O HOH B2014 31.678 -39.697 1.351 1.00 52.38 O HETATM 1885 O HOH B2015 28.342 -39.656 0.231 1.00 49.46 O HETATM 1886 O HOH B2016 24.628 -37.175 1.464 1.00 47.38 O HETATM 1887 O HOH B2017 20.591 -36.260 0.274 1.00 44.60 O HETATM 1888 O HOH B2018 20.898 -34.882 3.460 1.00 74.38 O HETATM 1889 O HOH B2019 16.209 -30.353 -0.236 1.00 54.97 O HETATM 1890 O HOH B2020 18.451 -32.345 -7.345 1.00 50.51 O HETATM 1891 O HOH B2021 28.032 -27.465 6.335 1.00 65.92 O HETATM 1892 O HOH B2022 22.322 -29.713 6.893 1.00 71.16 O HETATM 1893 O HOH B2023 26.326 -28.655 9.896 1.00 70.63 O HETATM 1894 O HOH B2024 34.819 -37.134 7.907 1.00 67.81 O HETATM 1895 O HOH B2025 41.996 -35.357 13.780 1.00 49.75 O HETATM 1896 O HOH B2026 48.493 -36.026 9.089 1.00 70.81 O HETATM 1897 O HOH B2027 49.474 -32.497 15.971 1.00 54.08 O HETATM 1898 O HOH B2028 51.395 -29.486 14.258 1.00 54.44 O HETATM 1899 O HOH B2029 51.468 -29.261 9.769 1.00 56.87 O HETATM 1900 O HOH B2030 52.314 -28.403 12.103 1.00 70.18 O HETATM 1901 O HOH B2031 35.810 -33.915 17.326 1.00 80.90 O HETATM 1902 O HOH B2032 39.069 -35.117 14.086 1.00 58.09 O HETATM 1903 O HOH B2033 32.312 -28.940 14.443 1.00 64.61 O HETATM 1904 O HOH B2034 29.845 -23.418 -1.018 1.00 45.50 O HETATM 1905 O HOH B2035 23.764 -24.598 -9.647 1.00 58.79 O HETATM 1906 O HOH B2036 25.653 -21.626 -11.695 1.00 61.47 O HETATM 1907 O HOH B2037 30.456 -20.585 -12.344 1.00 66.03 O HETATM 1908 O HOH B2038 35.018 -32.372 -8.761 1.00 39.25 O HETATM 1909 O HOH B2039 32.559 -21.536 -10.389 1.00 60.08 O HETATM 1910 O HOH B2040 35.624 -22.235 -6.693 1.00 38.68 O HETATM 1911 O HOH B2041 35.650 -22.179 -3.906 1.00 44.45 O HETATM 1912 O HOH B2042 35.713 -20.387 -0.966 1.00 44.13 O HETATM 1913 O HOH B2043 30.575 -20.127 5.608 1.00 69.09 O HETATM 1914 O HOH B2044 34.617 -20.603 8.507 1.00 51.90 O HETATM 1915 O HOH B2045 32.261 -19.201 8.539 1.00 64.59 O HETATM 1916 O HOH B2046 31.050 -26.928 13.601 1.00 63.30 O HETATM 1917 O HOH B2047 32.096 -22.662 13.951 1.00 52.98 O HETATM 1918 O HOH B2048 38.700 -24.200 14.438 1.00 41.16 O HETATM 1919 O HOH B2049 36.773 -19.245 9.621 1.00 42.89 O HETATM 1920 O HOH B2050 41.320 -17.966 9.597 1.00 45.22 O HETATM 1921 O HOH B2051 41.509 -23.540 13.884 1.00 39.93 O HETATM 1922 O HOH B2052 45.811 -13.286 14.833 1.00 63.28 O HETATM 1923 O HOH B2053 34.775 -14.127 1.511 1.00 61.31 O HETATM 1924 O HOH B2054 39.171 -13.614 8.503 1.00 54.95 O HETATM 1925 O HOH B2055 33.665 -18.683 -0.568 1.00 57.85 O HETATM 1926 O HOH B2056 37.749 -20.350 -3.010 1.00 56.76 O HETATM 1927 O HOH B2057 46.709 -21.362 -1.288 1.00 40.49 O HETATM 1928 O HOH B2058 45.969 -25.433 -5.454 1.00 53.71 O HETATM 1929 O HOH B2059 47.146 -22.715 -3.591 1.00 49.42 O HETATM 1930 O HOH B2060 38.482 -21.433 -12.467 1.00 51.64 O HETATM 1931 O HOH B2061 39.004 -16.481 -2.337 1.00 64.08 O HETATM 1932 O HOH B2062 40.095 -39.311 -6.794 1.00 56.28 O HETATM 1933 O HOH B2063 46.827 -28.131 -1.300 1.00 50.00 O HETATM 1934 O HOH B2064 47.147 -33.016 -2.017 1.00 63.74 O HETATM 1935 O HOH B2065 53.031 -26.163 8.873 1.00 56.61 O HETATM 1936 O HOH B2066 49.752 -27.282 0.430 1.00 65.58 O HETATM 1937 O HOH B2067 53.695 -24.048 4.656 1.00 47.70 O HETATM 1938 O HOH B2068 52.801 -19.467 0.023 1.00 56.10 O HETATM 1939 O HOH B2069 46.810 -13.121 -1.886 1.00 56.59 O HETATM 1940 O HOH B2070 59.031 -19.434 13.604 1.00 64.59 O HETATM 1941 O HOH B2071 61.443 -16.411 13.057 1.00 61.55 O HETATM 1942 O HOH B2072 54.810 -12.492 14.833 1.00 59.24 O HETATM 1943 O HOH B2073 58.199 -20.412 16.602 1.00 58.54 O HETATM 1944 O HOH B2074 55.798 -18.094 21.001 1.00 67.78 O HETATM 1945 O HOH B2075 53.133 -24.418 19.769 1.00 55.03 O HETATM 1946 O HOH B2076 53.557 -25.901 12.135 1.00 64.01 O HETATM 1947 O HOH B2077 56.566 -25.778 15.651 1.00 67.25 O HETATM 1948 O HOH B2078 39.109 -17.971 21.134 1.00 81.46 O HETATM 1949 O HOH B2079 31.628 -24.620 15.183 1.00 70.32 O HETATM 1950 O HOH B2080 37.758 -16.329 19.375 1.00 71.39 O HETATM 1951 O HOH B2081 31.485 -30.114 23.016 1.00 62.84 O HETATM 1952 O HOH B2082 28.074 -27.420 -19.419 1.00 53.21 O HETATM 1953 O HOH B2083 24.462 -44.114 -15.568 1.00 61.56 O HETATM 1954 O HOH B2084 34.551 -39.546 7.827 1.00 67.52 O HETATM 1955 O HOH B2085 40.205 -15.379 10.182 1.00 50.17 O HETATM 1956 O HOH B2086 42.775 -13.086 13.267 1.00 69.73 O HETATM 1957 O HOH B2087 46.384 -28.129 -4.356 1.00 58.50 O CONECT 99 105 CONECT 105 99 106 CONECT 106 105 107 109 CONECT 107 106 108 121 CONECT 108 107 CONECT 109 106 110 CONECT 110 109 111 112 CONECT 111 110 113 CONECT 112 110 114 CONECT 113 111 115 CONECT 114 112 115 CONECT 115 113 114 116 CONECT 116 115 117 CONECT 117 116 118 119 120 CONECT 118 117 CONECT 119 117 CONECT 120 117 CONECT 121 107 CONECT 194 1823 CONECT 217 1823 CONECT 316 1824 CONECT 327 1824 CONECT 352 1823 CONECT 371 1823 CONECT 462 1824 CONECT 486 1824 CONECT 669 1825 CONECT 1823 194 217 352 371 CONECT 1824 316 327 462 486 CONECT 1825 669 MASTER 568 0 4 7 9 0 3 6 1911 2 30 19 END
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Related entries of code: 4a49
Entries with 90% protein sequence similarity cutoff in PDBbind
PDB Code
Check Database
Protein Sequence Similarity
2fuh
RCSB PDB
PDBbind
146aa, >2FUH_1|Chain... at 100%
5edv
RCSB PDB
PDBbind
149aa, >5EDV_2|Chains... at 93%
Complexes with the same small molecule ligand
PDB Code
Check Database
Ligand Name
No complexes with the same small molecule ligand are found!
Entry Information
PDB ID
4a49
Complex Type
Protein-Protein
PDBbind Subset
general set
Protein Name
E3 UBIQUITIN-PROTEIN LIGASE CBL锛354-435锛
Ligand Name
UBIQUITIN-CONJUGATING ENZYME E2 D2
EC.Number
E.C.6.3.2
Resolution
2.21(Å)
Affinity (Kd/Ki/IC50)
Kd=42uM
Release Year
2012
Protein/NA Sequence
Check fasta file
Primary Reference
(2012) Nat.Struct.Mol.Biol. Vol. 19: pp. 184-192.
Links to External Databases
RCSB PDB
The mother database
PDBsum
Enhanced annotations on PDB entries
Pubchem
Comprehensive collection of chemical and biological data
UniProtKB AC
UniProt accession number (AC):
P22681
P62837
Entrez Gene ID
NCBI Entrez Gene ID:
867
7322
ASD
Information of known allosteric effects of PDB entries
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