Browse entries in the PDBbind-CN Database
HEADER HYDROLASE 29-NOV-12 4I6L TITLE CRYSTAL STRUCTURE OF OTUB1 IN COMPLEX WITH UBIQUITIN VARIANT COMPND MOL_ID: 1; COMPND 2 MOLECULE: UBIQUITIN THIOESTERASE OTUB1; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: UNP RESIDUES 45-271; COMPND 5 SYNONYM: DEUBIQUITINATING ENZYME OTUB1, OTU DOMAIN-CONTAINING COMPND 6 UBIQUITIN ALDEHYDE-BINDING PROTEIN 1, OTUBAIN-1, HOTU1, UBIQUITIN- COMPND 7 SPECIFIC-PROCESSING PROTEASE OTUB1; COMPND 8 EC: 3.4.19.12; COMPND 9 ENGINEERED: YES; COMPND 10 MUTATION: YES; COMPND 11 MOL_ID: 2; COMPND 12 MOLECULE: UBIQUITIN; COMPND 13 CHAIN: B; COMPND 14 FRAGMENT: UNP RESIDUES 77-150; COMPND 15 SYNONYM: UBIQUITIN; COMPND 16 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: OTUB1, OTB1, OTU1, HSPC263; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 10 ORGANISM_COMMON: HUMAN; SOURCE 11 ORGANISM_TAXID: 9606; SOURCE 12 GENE: UBC; SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS DEUBIQUITINASE, HYDROLASE EXPDTA X-RAY DIFFRACTION AUTHOR Y.C.JUANG,F.SICHERI REVDAT 3 20-FEB-13 4I6L 1 JRNL REVDAT 2 06-FEB-13 4I6L 1 JRNL REVDAT 1 16-JAN-13 4I6L 0 JRNL AUTH A.ERNST,G.AVVAKUMOV,J.TONG,Y.FAN,Y.ZHAO,P.ALBERTS,A.PERSAUD, JRNL AUTH 2 J.R.WALKER,A.M.NECULAI,D.NECULAI,A.VOROBYOV,P.GARG,L.BEATTY, JRNL AUTH 3 P.K.CHAN,Y.C.JUANG,M.C.LANDRY,C.YEH,E.ZEQIRAJ,K.KARAMBOULAS, JRNL AUTH 4 A.ALLALI-HASSANI,M.VEDADI,M.TYERS,J.MOFFAT,F.SICHERI, JRNL AUTH 5 L.PELLETIER,D.DUROCHER,B.RAUGHT,D.ROTIN,J.YANG,M.F.MORAN, JRNL AUTH 6 S.DHE-PAGANON,S.S.SIDHU JRNL TITL A STRATEGY FOR MODULATION OF ENZYMES IN THE UBIQUITIN JRNL TITL 2 SYSTEM. JRNL REF SCIENCE V. 339 590 2013 JRNL REFN ISSN 0036-8075 JRNL PMID 23287719 JRNL DOI 10.1126/SCIENCE.1230161 REMARK 2 REMARK 2 RESOLUTION. 2.49 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7.3_928) REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE- REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO, REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH, REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER REMARK 3 : ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : MLHL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.49 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.22 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.370 REMARK 3 COMPLETENESS FOR RANGE (%) : 91.5 REMARK 3 NUMBER OF REFLECTIONS : 12212 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.222 REMARK 3 R VALUE (WORKING SET) : 0.220 REMARK 3 FREE R VALUE : 0.266 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.750 REMARK 3 FREE R VALUE TEST SET COUNT : 580 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 46.2300 - 3.9484 0.99 3286 141 0.1943 0.2401 REMARK 3 2 3.9484 - 3.1342 1.00 3148 162 0.2187 0.2531 REMARK 3 3 3.1342 - 2.7381 0.98 3065 159 0.2588 0.3232 REMARK 3 4 2.7381 - 2.4877 0.69 2133 118 0.2667 0.3026 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.20 REMARK 3 SHRINKAGE RADIUS : 0.98 REMARK 3 K_SOL : 0.30 REMARK 3 B_SOL : 16.12 REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.330 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.120 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 2.95160 REMARK 3 B22 (A**2) : -2.24830 REMARK 3 B33 (A**2) : -0.70330 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 : 0.003 2444 REMARK 3 ANGLE : 0.715 3288 REMARK 3 CHIRALITY : 0.053 361 REMARK 3 PLANARITY : 0.003 420 REMARK 3 DIHEDRAL : 13.329 925 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 11 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: chain 'A' and (resseq 43:76) REMARK 3 ORIGIN FOR THE GROUP (A): 2.3726 -16.8023 -3.8112 REMARK 3 T TENSOR REMARK 3 T11: 1.0223 T22: 0.4317 REMARK 3 T33: 0.5188 T12: 0.1146 REMARK 3 T13: -0.3390 T23: 0.0083 REMARK 3 L TENSOR REMARK 3 L11: 1.4048 L22: 0.4537 REMARK 3 L33: 1.7878 L12: 0.0217 REMARK 3 L13: -0.7367 L23: 0.7855 REMARK 3 S TENSOR REMARK 3 S11: -0.2528 S12: 0.3724 S13: 0.7957 REMARK 3 S21: -0.4403 S22: -0.0667 S23: 0.2119 REMARK 3 S31: -1.6882 S32: -0.2540 S33: 0.5852 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: chain 'A' and (resseq 77:185) REMARK 3 ORIGIN FOR THE GROUP (A): 11.7043 -36.5435 9.2864 REMARK 3 T TENSOR REMARK 3 T11: 0.0342 T22: 0.0440 REMARK 3 T33: 0.1010 T12: -0.0293 REMARK 3 T13: -0.0288 T23: -0.0115 REMARK 3 L TENSOR REMARK 3 L11: 1.4382 L22: 2.0351 REMARK 3 L33: 2.6274 L12: 0.2522 REMARK 3 L13: 0.3223 L23: 1.5403 REMARK 3 S TENSOR REMARK 3 S11: -0.0813 S12: 0.0198 S13: 0.0145 REMARK 3 S21: 0.0002 S22: -0.1274 S23: 0.2503 REMARK 3 S31: -0.0620 S32: -0.0729 S33: 0.1393 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: chain 'A' and (resseq 186:271) REMARK 3 ORIGIN FOR THE GROUP (A): 16.2813 -22.7732 12.8918 REMARK 3 T TENSOR REMARK 3 T11: 0.1834 T22: 0.0973 REMARK 3 T33: 0.1342 T12: -0.0571 REMARK 3 T13: -0.0404 T23: -0.0084 REMARK 3 L TENSOR REMARK 3 L11: 1.9826 L22: 3.0364 REMARK 3 L33: 3.0661 L12: 1.0877 REMARK 3 L13: 0.0773 L23: 1.5420 REMARK 3 S TENSOR REMARK 3 S11: -0.0668 S12: 0.0634 S13: 0.0007 REMARK 3 S21: -0.3599 S22: -0.0609 S23: 0.1775 REMARK 3 S31: -0.6619 S32: 0.1784 S33: 0.1046 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: chain 'B' and (resseq -1:7) REMARK 3 ORIGIN FOR THE GROUP (A): 34.2242 -7.2748 16.7792 REMARK 3 T TENSOR REMARK 3 T11: 0.4132 T22: 0.1719 REMARK 3 T33: 0.2507 T12: -0.0269 REMARK 3 T13: 0.1079 T23: -0.0449 REMARK 3 L TENSOR REMARK 3 L11: 4.3258 L22: 8.6330 REMARK 3 L33: 4.3369 L12: 5.3066 REMARK 3 L13: 4.1512 L23: 5.9585 REMARK 3 S TENSOR REMARK 3 S11: -0.4134 S12: 0.6132 S13: -0.3085 REMARK 3 S21: -0.6515 S22: 0.5048 S23: -0.6784 REMARK 3 S31: -0.1191 S32: 0.1180 S33: -0.2120 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: chain 'B' and (resseq 8:17) REMARK 3 ORIGIN FOR THE GROUP (A): 30.9758 -10.4917 12.8027 REMARK 3 T TENSOR REMARK 3 T11: 0.4294 T22: 0.2192 REMARK 3 T33: 0.2674 T12: -0.1335 REMARK 3 T13: 0.1549 T23: -0.0717 REMARK 3 L TENSOR REMARK 3 L11: 0.9809 L22: 1.3304 REMARK 3 L33: 1.7562 L12: -0.4821 REMARK 3 L13: -0.4520 L23: -1.0788 REMARK 3 S TENSOR REMARK 3 S11: -0.4120 S12: 0.3207 S13: -0.4330 REMARK 3 S21: -1.0004 S22: 0.5711 S23: -0.5149 REMARK 3 S31: 0.0692 S32: 0.0724 S33: 0.1605 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: chain 'B' and (resseq 18:22) REMARK 3 ORIGIN FOR THE GROUP (A): 32.1220 3.6116 21.0953 REMARK 3 T TENSOR REMARK 3 T11: 0.3047 T22: 0.1112 REMARK 3 T33: 0.3119 T12: -0.0231 REMARK 3 T13: -0.0087 T23: -0.0608 REMARK 3 L TENSOR REMARK 3 L11: 4.7367 L22: 1.6461 REMARK 3 L33: 9.4759 L12: -2.1923 REMARK 3 L13: 0.1249 L23: 0.7479 REMARK 3 S TENSOR REMARK 3 S11: -0.1271 S12: 0.1466 S13: 0.0023 REMARK 3 S21: -0.7812 S22: 0.2260 S23: -0.8336 REMARK 3 S31: -0.4394 S32: -0.0839 S33: -0.0634 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: chain 'B' and (resseq 23:34) REMARK 3 ORIGIN FOR THE GROUP (A): 25.8169 -1.5882 12.6243 REMARK 3 T TENSOR REMARK 3 T11: 0.3680 T22: 0.1721 REMARK 3 T33: 0.1144 T12: -0.0314 REMARK 3 T13: -0.0128 T23: 0.0150 REMARK 3 L TENSOR REMARK 3 L11: 2.2849 L22: 4.9469 REMARK 3 L33: 1.7649 L12: -0.1950 REMARK 3 L13: -0.0603 L23: 2.9536 REMARK 3 S TENSOR REMARK 3 S11: 0.0934 S12: 0.5634 S13: 0.1559 REMARK 3 S21: -1.2731 S22: -0.0723 S23: -0.0065 REMARK 3 S31: -0.7417 S32: 0.0136 S33: 0.0948 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: chain 'B' and (resseq 35:44) REMARK 3 ORIGIN FOR THE GROUP (A): 19.3449 -6.1251 14.5033 REMARK 3 T TENSOR REMARK 3 T11: 0.3092 T22: 0.3347 REMARK 3 T33: 0.3661 T12: -0.1115 REMARK 3 T13: -0.1489 T23: -0.0308 REMARK 3 L TENSOR REMARK 3 L11: 1.2334 L22: 3.4979 REMARK 3 L33: 5.4231 L12: -1.4438 REMARK 3 L13: 0.0656 L23: 0.4762 REMARK 3 S TENSOR REMARK 3 S11: -0.2430 S12: 0.2490 S13: 0.0128 REMARK 3 S21: -0.9403 S22: 0.0861 S23: 0.8034 REMARK 3 S31: -0.0210 S32: -1.1208 S33: 0.1274 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: chain 'B' and (resseq 45:56) REMARK 3 ORIGIN FOR THE GROUP (A): 23.8809 -4.7616 26.3390 REMARK 3 T TENSOR REMARK 3 T11: 0.2103 T22: 0.2572 REMARK 3 T33: 0.2118 T12: -0.0535 REMARK 3 T13: -0.0209 T23: -0.0461 REMARK 3 L TENSOR REMARK 3 L11: 4.5548 L22: 5.4037 REMARK 3 L33: 7.0214 L12: 3.4189 REMARK 3 L13: -3.7421 L23: -6.0066 REMARK 3 S TENSOR REMARK 3 S11: 0.2431 S12: -0.0708 S13: 0.4994 REMARK 3 S21: 0.1462 S22: 0.2592 S23: 0.8586 REMARK 3 S31: -0.0363 S32: -0.8247 S33: -0.3444 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: chain 'B' and (resseq 57:65) REMARK 3 ORIGIN FOR THE GROUP (A): 33.7687 -4.2419 26.4265 REMARK 3 T TENSOR REMARK 3 T11: 0.1784 T22: 0.2387 REMARK 3 T33: 0.2741 T12: -0.1074 REMARK 3 T13: -0.0128 T23: 0.0604 REMARK 3 L TENSOR REMARK 3 L11: 3.9820 L22: 2.1089 REMARK 3 L33: 4.3759 L12: 0.3138 REMARK 3 L13: 0.7904 L23: 1.0013 REMARK 3 S TENSOR REMARK 3 S11: -0.0642 S12: -0.4729 S13: -0.1779 REMARK 3 S21: -0.1605 S22: 0.0153 S23: -0.7548 REMARK 3 S31: -0.2835 S32: 0.4958 S33: -0.1142 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: chain 'B' and (resseq 66:73) REMARK 3 ORIGIN FOR THE GROUP (A): 22.4677 -11.5498 17.5928 REMARK 3 T TENSOR REMARK 3 T11: 0.2519 T22: 0.1929 REMARK 3 T33: 0.1735 T12: -0.1141 REMARK 3 T13: 0.0129 T23: 0.0080 REMARK 3 L TENSOR REMARK 3 L11: 3.1327 L22: 7.9952 REMARK 3 L33: 8.5766 L12: 1.8016 REMARK 3 L13: 1.7768 L23: 0.8256 REMARK 3 S TENSOR REMARK 3 S11: -0.1972 S12: 0.0416 S13: 0.2703 REMARK 3 S21: -0.6865 S22: 0.1937 S23: 0.2096 REMARK 3 S31: -0.0924 S32: -0.5478 S33: 0.1309 REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 4I6L COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-DEC-12. REMARK 100 THE RCSB ID CODE IS RCSB076368. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 03-JUL-12 REMARK 200 TEMPERATURE (KELVIN) : 93 REMARK 200 PH : 6.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 24-ID-E 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 : DECTRIS PILATUS 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 12681 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.400 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : NULL REMARK 200 DATA REDUNDANCY : NULL REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.59 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.69 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: 2ZFY, 1UBQ REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 52.92 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.61 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM SULFATE, 0.1 M MES, PH REMARK 280 6.5, AND 20% (W/V) PEG8000, VAPOR DIFFUSION, SITTING DROP, REMARK 280 TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z+1/2 REMARK 290 3555 -X,Y,-Z+1/2 REMARK 290 4555 X,-Y,-Z REMARK 290 5555 X+1/2,Y+1/2,Z REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2 REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2 REMARK 290 8555 X+1/2,-Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 36.61900 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 36.61900 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 46.22200 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 54.53450 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 46.22200 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 54.53450 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 36.61900 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 46.22200 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 54.53450 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 36.61900 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 46.22200 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 54.53450 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 1610 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 13660 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 ALA A 62 REMARK 465 GLU A 63 REMARK 465 ASP A 64 REMARK 465 ASP A 237 REMARK 465 ARG A 238 REMARK 465 GLY A 239 REMARK 465 GLU A 240 REMARK 465 GLY A 241 REMARK 465 GLY A 242 REMARK 465 THR A 243 REMARK 465 THR A 244 REMARK 465 ASN A 245 REMARK 465 ARG B 74 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 O TYR A 270 O HOH A 334 2.07 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 LYS A 59 44.51 -79.03 REMARK 500 GLU A 60 -12.60 -148.80 REMARK 500 GLU A 186 43.24 -102.77 REMARK 500 CYS A 212 -12.66 75.02 REMARK 500 ASP A 216 -164.09 -126.75 REMARK 500 PRO A 263 110.70 -39.31 REMARK 500 ASP B 32 30.18 -72.53 REMARK 500 LYS B 33 -21.70 -148.43 REMARK 500 REMARK 500 REMARK: NULL DBREF 4I6L A 45 271 UNP Q96FW1 OTUB1_HUMAN 45 271 DBREF 4I6L B 1 74 UNP P0CG48 UBC_HUMAN 77 150 SEQADV 4I6L GLY A 43 UNP Q96FW1 EXPRESSION TAG SEQADV 4I6L SER A 44 UNP Q96FW1 EXPRESSION TAG SEQADV 4I6L SER A 91 UNP Q96FW1 CYS 91 ENGINEERED MUTATION SEQADV 4I6L GLY B -1 UNP P0CG48 EXPRESSION TAG SEQADV 4I6L SER B 0 UNP P0CG48 EXPRESSION TAG SEQADV 4I6L LYS B 42 UNP P0CG48 ARG 118 VARIANT SEQADV 4I6L LEU B 44 UNP P0CG48 ILE 120 VARIANT SEQADV 4I6L ARG B 47 UNP P0CG48 GLY 123 VARIANT SEQADV 4I6L HIS B 62 UNP P0CG48 GLN 138 VARIANT SEQADV 4I6L PHE B 66 UNP P0CG48 THR 142 VARIANT SEQADV 4I6L TYR B 68 UNP P0CG48 HIS 144 VARIANT SEQRES 1 A 229 GLY SER ASN PRO LEU VAL SER GLU ARG LEU GLU LEU SER SEQRES 2 A 229 VAL LEU TYR LYS GLU TYR ALA GLU ASP ASP ASN ILE TYR SEQRES 3 A 229 GLN GLN LYS ILE LYS ASP LEU HIS LYS LYS TYR SER TYR SEQRES 4 A 229 ILE ARG LYS THR ARG PRO ASP GLY ASN SER PHE TYR ARG SEQRES 5 A 229 ALA PHE GLY PHE SER HIS LEU GLU ALA LEU LEU ASP ASP SEQRES 6 A 229 SER LYS GLU LEU GLN ARG PHE LYS ALA VAL SER ALA LYS SEQRES 7 A 229 SER LYS GLU ASP LEU VAL SER GLN GLY PHE THR GLU PHE SEQRES 8 A 229 THR ILE GLU ASP PHE HIS ASN THR PHE MET ASP LEU ILE SEQRES 9 A 229 GLU GLN VAL GLU LYS GLN THR SER VAL ALA ASP LEU LEU SEQRES 10 A 229 ALA SER PHE ASN ASP GLN SER THR SER ASP TYR LEU VAL SEQRES 11 A 229 VAL TYR LEU ARG LEU LEU THR SER GLY TYR LEU GLN ARG SEQRES 12 A 229 GLU SER LYS PHE PHE GLU HIS PHE ILE GLU GLY GLY ARG SEQRES 13 A 229 THR VAL LYS GLU PHE CYS GLN GLN GLU VAL GLU PRO MET SEQRES 14 A 229 CYS LYS GLU SER ASP HIS ILE HIS ILE ILE ALA LEU ALA SEQRES 15 A 229 GLN ALA LEU SER VAL SER ILE GLN VAL GLU TYR MET ASP SEQRES 16 A 229 ARG GLY GLU GLY GLY THR THR ASN PRO HIS ILE PHE PRO SEQRES 17 A 229 GLU GLY SER GLU PRO LYS VAL TYR LEU LEU TYR ARG PRO SEQRES 18 A 229 GLY HIS TYR ASP ILE LEU TYR LYS SEQRES 1 B 76 GLY SER MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS SEQRES 2 B 76 THR ILE THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU SEQRES 3 B 76 ASN VAL LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO SEQRES 4 B 76 PRO ASP GLN GLN LYS LEU LEU PHE ALA ARG LYS GLN LEU SEQRES 5 B 76 GLU ASP GLY ARG THR LEU SER ASP TYR ASN ILE HIS LYS SEQRES 6 B 76 GLU SER PHE LEU TYR LEU VAL LEU ARG LEU ARG FORMUL 3 HOH *84(H2 O) HELIX 1 1 SER A 55 TYR A 61 5 7 HELIX 2 2 ASN A 66 LYS A 77 1 12 HELIX 3 3 ASN A 90 LEU A 104 1 15 HELIX 4 4 ASP A 107 GLN A 128 1 22 HELIX 5 5 THR A 131 LYS A 151 1 21 HELIX 6 6 SER A 154 PHE A 162 1 9 HELIX 7 7 ASP A 164 GLU A 186 1 23 HELIX 8 8 GLU A 186 GLU A 191 1 6 HELIX 9 9 HIS A 192 ILE A 194 5 3 HELIX 10 10 THR A 199 VAL A 208 1 10 HELIX 11 11 ASP A 216 LEU A 227 1 12 HELIX 12 12 THR B 22 GLY B 35 1 14 HELIX 13 13 PRO B 37 ASP B 39 5 3 HELIX 14 14 THR B 55 ASN B 60 5 6 SHEET 1 A 6 VAL A 48 GLU A 53 0 SHEET 2 A 6 TYR A 81 THR A 85 -1 O ILE A 82 N LEU A 52 SHEET 3 A 6 HIS A 265 TYR A 270 -1 O ILE A 268 N ARG A 83 SHEET 4 A 6 VAL A 257 ARG A 262 -1 N TYR A 258 O LEU A 269 SHEET 5 A 6 ILE A 231 TYR A 235 1 N GLU A 234 O TYR A 261 SHEET 6 A 6 HIS A 247 PHE A 249 -1 O PHE A 249 N ILE A 231 SHEET 1 B 5 THR B 12 VAL B 17 0 SHEET 2 B 5 MET B 1 THR B 7 -1 N VAL B 5 O ILE B 13 SHEET 3 B 5 PHE B 66 LEU B 71 1 O LEU B 69 N LYS B 6 SHEET 4 B 5 GLN B 41 PHE B 45 -1 N LEU B 44 O TYR B 68 SHEET 5 B 5 LYS B 48 GLN B 49 -1 O LYS B 48 N PHE B 45 SSBOND 1 CYS A 212 CYS A 212 1555 3555 2.03 CISPEP 1 PHE A 249 PRO A 250 0 0.45 CRYST1 92.444 109.069 73.238 90.00 90.00 90.00 C 2 2 21 8 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.010817 0.000000 0.000000 0.00000 SCALE2 0.000000 0.009169 0.000000 0.00000 SCALE3 0.000000 0.000000 0.013654 0.00000 ATOM 1 N GLY A 43 -10.156 -30.965 1.693 1.00 56.68 N ANISOU 1 N GLY A 43 6659 8328 6550 1912 -1276 -1926 N ATOM 2 CA GLY A 43 -9.651 -30.322 2.891 1.00 56.03 C ANISOU 2 CA GLY A 43 6655 8122 6512 1931 -1337 -1910 C ATOM 3 C GLY A 43 -9.054 -28.960 2.601 1.00 56.39 C ANISOU 3 C GLY A 43 6904 8001 6521 2136 -1519 -1956 C ATOM 4 O GLY A 43 -8.048 -28.848 1.900 1.00 56.40 O ANISOU 4 O GLY A 43 6974 7938 6518 2152 -1524 -1924 O ATOM 5 N SER A 44 -9.676 -27.920 3.146 1.00 56.26 N ANISOU 5 N SER A 44 7005 7889 6483 2297 -1679 -2030 N ATOM 6 CA SER A 44 -9.223 -26.551 2.929 1.00 57.76 C ANISOU 6 CA SER A 44 7448 7861 6635 2496 -1892 -2065 C ATOM 7 C SER A 44 -7.940 -26.248 3.695 1.00 59.58 C ANISOU 7 C SER A 44 7766 7945 6928 2420 -1912 -1992 C ATOM 8 O SER A 44 -7.249 -25.274 3.392 1.00 63.41 O ANISOU 8 O SER A 44 8492 8208 7394 2531 -2082 -1982 O ATOM 9 CB SER A 44 -10.314 -25.560 3.336 1.00 57.14 C ANISOU 9 CB SER A 44 7475 7725 6512 2679 -2060 -2163 C ATOM 10 OG SER A 44 -10.690 -25.749 4.688 1.00 54.42 O ANISOU 10 OG SER A 44 7018 7434 6224 2589 -2005 -2165 O ATOM 11 N ASN A 45 -7.631 -27.083 4.686 1.00 55.02 N ANISOU 11 N ASN A 45 7013 7473 6420 2231 -1752 -1932 N ATOM 12 CA ASN A 45 -6.497 -26.841 5.573 1.00 51.12 C ANISOU 12 CA ASN A 45 6566 6875 5983 2164 -1761 -1873 C ATOM 13 C ASN A 45 -5.607 -28.073 5.789 1.00 45.70 C ANISOU 13 C ASN A 45 5702 6311 5352 1947 -1549 -1778 C ATOM 14 O ASN A 45 -5.461 -28.546 6.917 1.00 41.96 O ANISOU 14 O ASN A 45 5124 5892 4926 1834 -1450 -1742 O ATOM 15 CB ASN A 45 -7.018 -26.336 6.920 1.00 50.95 C ANISOU 15 CB ASN A 45 6543 6828 5987 2198 -1816 -1912 C ATOM 16 CG ASN A 45 -5.971 -25.580 7.709 1.00 50.90 C ANISOU 16 CG ASN A 45 6663 6659 6018 2214 -1912 -1885 C ATOM 17 OD1 ASN A 45 -5.042 -25.002 7.141 1.00 52.79 O ANISOU 17 OD1 ASN A 45 7080 6728 6249 2257 -2024 -1850 O ATOM 18 ND2 ASN A 45 -6.122 -25.570 9.029 1.00 49.11 N ANISOU 18 ND2 ASN A 45 6361 6468 5832 2177 -1877 -1900 N ATOM 19 N PRO A 46 -4.992 -28.592 4.711 1.00 43.10 N ANISOU 19 N PRO A 46 5353 6015 5008 1895 -1478 -1744 N ATOM 20 CA PRO A 46 -4.190 -29.812 4.855 1.00 38.92 C ANISOU 20 CA PRO A 46 4657 5611 4520 1683 -1276 -1654 C ATOM 21 C PRO A 46 -2.821 -29.540 5.471 1.00 38.65 C ANISOU 21 C PRO A 46 4656 5491 4539 1651 -1295 -1599 C ATOM 22 O PRO A 46 -2.292 -28.435 5.335 1.00 40.05 O ANISOU 22 O PRO A 46 5016 5445 4755 1832 -1447 -1628 O ATOM 23 CB PRO A 46 -4.027 -30.285 3.412 1.00 37.53 C ANISOU 23 CB PRO A 46 4459 5492 4310 1679 -1202 -1661 C ATOM 24 CG PRO A 46 -4.023 -29.021 2.620 1.00 40.53 C ANISOU 24 CG PRO A 46 5040 5691 4668 1937 -1425 -1724 C ATOM 25 CD PRO A 46 -4.958 -28.072 3.332 1.00 43.33 C ANISOU 25 CD PRO A 46 5524 5949 4992 2050 -1578 -1789 C ATOM 26 N LEU A 47 -2.261 -30.545 6.139 1.00 35.88 N ANISOU 26 N LEU A 47 4160 5247 4226 1468 -1116 -1528 N ATOM 27 CA LEU A 47 -0.942 -30.438 6.753 1.00 34.04 C ANISOU 27 CA LEU A 47 3916 4964 4051 1444 -1088 -1491 C ATOM 28 C LEU A 47 0.119 -30.084 5.715 1.00 35.45 C ANISOU 28 C LEU A 47 4189 5066 4213 1509 -1152 -1533 C ATOM 29 O LEU A 47 0.923 -29.178 5.924 1.00 39.19 O ANISOU 29 O LEU A 47 4884 5382 4626 1396 -1280 -1476 O ATOM 30 CB LEU A 47 -0.579 -31.747 7.456 1.00 31.49 C ANISOU 30 CB LEU A 47 3460 4779 3728 1207 -883 -1407 C ATOM 31 CG LEU A 47 -1.495 -32.166 8.608 1.00 30.64 C ANISOU 31 CG LEU A 47 3327 4694 3622 1151 -835 -1398 C ATOM 32 CD1 LEU A 47 -1.280 -33.627 8.962 1.00 28.16 C ANISOU 32 CD1 LEU A 47 2927 4467 3306 966 -672 -1320 C ATOM 33 CD2 LEU A 47 -1.266 -31.283 9.824 1.00 31.42 C ANISOU 33 CD2 LEU A 47 3473 4721 3742 1241 -927 -1444 C ATOM 34 N VAL A 48 0.120 -30.809 4.601 1.00 31.39 N ANISOU 34 N VAL A 48 3593 4673 3661 1416 -1050 -1497 N ATOM 35 CA VAL A 48 0.995 -30.492 3.478 1.00 32.49 C ANISOU 35 CA VAL A 48 3872 4783 3692 1190 -1137 -1343 C ATOM 36 C VAL A 48 0.166 -30.457 2.201 1.00 35.57 C ANISOU 36 C VAL A 48 4266 5210 4040 1269 -1197 -1339 C ATOM 37 O VAL A 48 -0.557 -31.405 1.896 1.00 36.08 O ANISOU 37 O VAL A 48 4134 5431 4141 1337 -1031 -1421 O ATOM 38 CB VAL A 48 2.130 -31.525 3.310 1.00 24.40 C ANISOU 38 CB VAL A 48 2705 3910 2655 929 -946 -1240 C ATOM 39 CG1 VAL A 48 3.097 -31.071 2.229 1.00 25.13 C ANISOU 39 CG1 VAL A 48 2947 3965 2634 686 -1058 -1078 C ATOM 40 CG2 VAL A 48 2.866 -31.736 4.621 1.00 23.43 C ANISOU 40 CG2 VAL A 48 2538 3789 2574 876 -852 -1253 C ATOM 41 N SER A 49 0.268 -29.363 1.455 1.00 38.01 N ANISOU 41 N SER A 49 4813 5370 4258 1258 -1425 -1251 N ATOM 42 CA SER A 49 -0.547 -29.191 0.260 1.00 38.56 C ANISOU 42 CA SER A 49 4905 5469 4276 1357 -1506 -1234 C ATOM 43 C SER A 49 0.072 -29.882 -0.946 1.00 39.37 C ANISOU 43 C SER A 49 4916 5730 4314 1123 -1422 -1099 C ATOM 44 O SER A 49 1.075 -30.584 -0.829 1.00 36.55 O ANISOU 44 O SER A 49 4462 5464 3963 897 -1284 -1034 O ATOM 45 CB SER A 49 -0.741 -27.705 -0.051 1.00 38.90 C ANISOU 45 CB SER A 49 5267 5269 4244 1470 -1789 -1182 C ATOM 46 OG SER A 49 0.404 -27.168 -0.691 1.00 38.14 O ANISOU 46 OG SER A 49 5371 5079 4043 1236 -1900 -1000 O ATOM 47 N GLU A 50 -0.546 -29.679 -2.104 1.00 44.40 N ANISOU 47 N GLU A 50 5580 6403 4886 1186 -1504 -1061 N ATOM 48 CA GLU A 50 0.008 -30.124 -3.372 1.00 45.11 C ANISOU 48 CA GLU A 50 5622 6622 4895 971 -1469 -924 C ATOM 49 C GLU A 50 1.091 -29.145 -3.802 1.00 45.05 C ANISOU 49 C GLU A 50 5886 6465 4765 790 -1654 -749 C ATOM 50 O GLU A 50 1.137 -28.018 -3.313 1.00 45.76 O ANISOU 50 O GLU A 50 6229 6324 4834 882 -1833 -738 O ATOM 51 CB GLU A 50 -1.090 -30.168 -4.436 1.00 49.17 C ANISOU 51 CB GLU A 50 6080 7230 5373 1117 -1501 -949 C ATOM 52 CG GLU A 50 -2.108 -31.282 -4.254 1.00 51.05 C ANISOU 52 CG GLU A 50 6048 7645 5706 1244 -1283 -1128 C ATOM 53 CD GLU A 50 -1.637 -32.598 -4.840 1.00 53.05 C ANISOU 53 CD GLU A 50 6087 8094 5976 1039 -1054 -1102 C ATOM 54 OE1 GLU A 50 -0.575 -32.609 -5.499 1.00 54.27 O ANISOU 54 OE1 GLU A 50 6292 8256 6070 803 -1082 -942 O ATOM 55 OE2 GLU A 50 -2.329 -33.619 -4.647 1.00 52.96 O ANISOU 55 OE2 GLU A 50 5885 8216 6021 1107 -837 -1255 O ATOM 56 N ARG A 51 1.966 -29.571 -4.708 1.00 47.11 N ANISOU 56 N ARG A 51 6112 6839 4948 528 -1604 -620 N ATOM 57 CA ARG A 51 2.934 -28.655 -5.296 1.00 50.32 C ANISOU 57 CA ARG A 51 6785 7113 5222 347 -1764 -453 C ATOM 58 C ARG A 51 2.198 -27.726 -6.244 1.00 52.08 C ANISOU 58 C ARG A 51 7206 7226 5354 505 -1958 -377 C ATOM 59 O ARG A 51 1.390 -28.171 -7.058 1.00 52.84 O ANISOU 59 O ARG A 51 7154 7485 5436 597 -1923 -396 O ATOM 60 CB ARG A 51 4.027 -29.411 -6.052 1.00 52.02 C ANISOU 60 CB ARG A 51 6883 7510 5372 28 -1641 -351 C ATOM 61 CG ARG A 51 5.096 -28.515 -6.670 1.00 57.58 C ANISOU 61 CG ARG A 51 7859 8054 5966 -176 -1752 -184 C ATOM 62 CD ARG A 51 6.146 -29.346 -7.400 1.00 60.58 C ANISOU 62 CD ARG A 51 8088 8589 6340 -435 -1576 -122 C ATOM 63 NE ARG A 51 7.328 -28.567 -7.759 1.00 67.57 N ANISOU 63 NE ARG A 51 9212 9296 7166 -702 -1615 49 N ATOM 64 CZ ARG A 51 8.469 -29.098 -8.185 1.00 71.41 C ANISOU 64 CZ ARG A 51 9606 9852 7675 -961 -1449 120 C ATOM 65 NH1 ARG A 51 8.589 -30.410 -8.306 1.00 70.47 N ANISOU 65 NH1 ARG A 51 9190 9933 7655 -973 -1233 52 N ATOM 66 NH2 ARG A 51 9.496 -28.319 -8.483 1.00 74.79 N ANISOU 66 NH2 ARG A 51 10255 10123 8037 -1209 -1494 265 N ATOM 67 N LEU A 52 2.469 -26.433 -6.128 1.00 54.66 N ANISOU 67 N LEU A 52 7883 7261 5627 530 -2155 -287 N ATOM 68 CA LEU A 52 1.803 -25.443 -6.959 1.00 58.32 C ANISOU 68 CA LEU A 52 8579 7574 6005 695 -2343 -194 C ATOM 69 C LEU A 52 2.837 -24.560 -7.637 1.00 61.00 C ANISOU 69 C LEU A 52 9246 7709 6223 464 -2456 20 C ATOM 70 O LEU A 52 4.037 -24.719 -7.424 1.00 59.75 O ANISOU 70 O LEU A 52 9119 7531 6053 172 -2385 79 O ATOM 71 CB LEU A 52 0.878 -24.574 -6.107 1.00 59.01 C ANISOU 71 CB LEU A 52 8822 7439 6160 1008 -2479 -299 C ATOM 72 CG LEU A 52 -0.029 -25.277 -5.093 1.00 57.08 C ANISOU 72 CG LEU A 52 8304 7326 6058 1218 -2358 -527 C ATOM 73 CD1 LEU A 52 -0.766 -24.255 -4.238 1.00 58.63 C ANISOU 73 CD1 LEU A 52 8700 7268 6307 1496 -2509 -622 C ATOM 74 CD2 LEU A 52 -1.013 -26.206 -5.788 1.00 55.42 C ANISOU 74 CD2 LEU A 52 7793 7396 5866 1322 -2233 -606 C ATOM 75 N GLU A 53 2.368 -23.633 -8.462 1.00 65.49 N ANISOU 75 N GLU A 53 10053 8126 6704 585 -2613 137 N ATOM 76 CA GLU A 53 3.227 -22.575 -8.968 1.00 70.59 C ANISOU 76 CA GLU A 53 11077 8500 7246 398 -2730 341 C ATOM 77 C GLU A 53 2.971 -21.353 -8.097 1.00 72.63 C ANISOU 77 C GLU A 53 11666 8393 7537 571 -2899 324 C ATOM 78 O GLU A 53 1.873 -21.186 -7.570 1.00 72.90 O ANISOU 78 O GLU A 53 11651 8401 7646 894 -2955 188 O ATOM 79 CB GLU A 53 2.909 -22.256 -10.430 1.00 75.21 C ANISOU 79 CB GLU A 53 11742 9124 7709 423 -2787 494 C ATOM 80 CG GLU A 53 2.546 -23.460 -11.286 1.00 75.55 C ANISOU 80 CG GLU A 53 11411 9565 7728 408 -2649 451 C ATOM 81 CD GLU A 53 1.059 -23.764 -11.265 1.00 77.17 C ANISOU 81 CD GLU A 53 11409 9931 7983 752 -2663 305 C ATOM 82 OE1 GLU A 53 0.460 -23.745 -10.170 1.00 77.66 O ANISOU 82 OE1 GLU A 53 11421 9925 8160 950 -2671 144 O ATOM 83 OE2 GLU A 53 0.487 -24.010 -12.348 1.00 77.88 O ANISOU 83 OE2 GLU A 53 11382 10216 7994 816 -2661 345 O ATOM 84 N LEU A 54 3.977 -20.498 -7.948 1.00 74.85 N ANISOU 84 N LEU A 54 12282 8394 7765 347 -2969 452 N ATOM 85 CA LEU A 54 3.884 -19.357 -7.034 1.00 78.81 C ANISOU 85 CA LEU A 54 13112 8532 8299 471 -3118 431 C ATOM 86 C LEU A 54 2.932 -18.251 -7.478 1.00 82.11 C ANISOU 86 C LEU A 54 13789 8709 8699 765 -3270 490 C ATOM 87 O LEU A 54 2.783 -17.250 -6.776 1.00 83.72 O ANISOU 87 O LEU A 54 14272 8595 8944 889 -3382 470 O ATOM 88 CB LEU A 54 5.272 -18.778 -6.753 1.00 81.12 C ANISOU 88 CB LEU A 54 13638 8607 8575 106 -3072 525 C ATOM 89 CG LEU A 54 6.289 -19.012 -7.863 1.00 82.45 C ANISOU 89 CG LEU A 54 13840 8869 8618 -250 -3006 709 C ATOM 90 CD1 LEU A 54 6.037 -18.018 -8.974 1.00 86.23 C ANISOU 90 CD1 LEU A 54 14645 9130 8988 -195 -3131 902 C ATOM 91 CD2 LEU A 54 7.715 -18.916 -7.335 1.00 82.03 C ANISOU 91 CD2 LEU A 54 13843 8742 8583 -637 -2889 719 C ATOM 92 N SER A 55 2.289 -18.435 -8.629 1.00 83.62 N ANISOU 92 N SER A 55 13876 9064 8833 877 -3262 553 N ATOM 93 CA SER A 55 1.303 -17.476 -9.118 1.00 88.25 C ANISOU 93 CA SER A 55 14652 9482 9395 1171 -3387 595 C ATOM 94 C SER A 55 0.209 -17.215 -8.080 1.00 89.76 C ANISOU 94 C SER A 55 14797 9602 9707 1523 -3446 392 C ATOM 95 O SER A 55 -0.409 -16.151 -8.069 1.00 92.61 O ANISOU 95 O SER A 55 15397 9720 10071 1741 -3559 404 O ATOM 96 CB SER A 55 0.683 -17.968 -10.427 1.00 88.40 C ANISOU 96 CB SER A 55 14472 9784 9332 1250 -3353 655 C ATOM 97 OG SER A 55 0.045 -19.220 -10.255 1.00 85.55 O ANISOU 97 OG SER A 55 13680 9792 9033 1349 -3242 481 O ATOM 98 N VAL A 56 -0.009 -18.188 -7.198 1.00 88.01 N ANISOU 98 N VAL A 56 14259 9598 9584 1566 -3354 197 N ATOM 99 CA VAL A 56 -0.986 -18.060 -6.124 1.00 89.11 C ANISOU 99 CA VAL A 56 14315 9699 9844 1867 -3381 -19 C ATOM 100 C VAL A 56 -0.428 -17.244 -4.953 1.00 90.22 C ANISOU 100 C VAL A 56 14729 9508 10044 1830 -3459 -51 C ATOM 101 O VAL A 56 -0.976 -17.271 -3.851 1.00 90.06 O ANISOU 101 O VAL A 56 14616 9472 10131 2013 -3458 -245 O ATOM 102 CB VAL A 56 -1.448 -19.441 -5.614 1.00 86.36 C ANISOU 102 CB VAL A 56 13515 9715 9584 1916 -3222 -221 C ATOM 103 CG1 VAL A 56 -2.911 -19.390 -5.196 1.00 87.29 C ANISOU 103 CG1 VAL A 56 13488 9897 9781 2268 -3227 -423 C ATOM 104 CG2 VAL A 56 -1.243 -20.495 -6.688 1.00 84.32 C ANISOU 104 CG2 VAL A 56 12994 9786 9259 1748 -3096 -148 C ATOM 105 N LEU A 57 0.668 -16.529 -5.190 1.00 90.56 N ANISOU 105 N LEU A 57 15104 9289 10014 1575 -3513 134 N ATOM 106 CA LEU A 57 1.182 -15.583 -4.204 1.00 89.43 C ANISOU 106 CA LEU A 57 15271 8786 9923 1529 -3587 122 C ATOM 107 C LEU A 57 0.670 -14.172 -4.488 1.00 93.96 C ANISOU 107 C LEU A 57 16183 9030 10489 1697 -3691 180 C ATOM 108 O LEU A 57 0.505 -13.372 -3.569 1.00 95.93 O ANISOU 108 O LEU A 57 16598 9033 10818 1800 -3737 81 O ATOM 109 CB LEU A 57 2.713 -15.607 -4.143 1.00 85.73 C ANISOU 109 CB LEU A 57 14906 8248 9419 1086 -3491 230 C ATOM 110 CG LEU A 57 3.353 -16.838 -3.494 1.00 78.86 C ANISOU 110 CG LEU A 57 13656 7698 8609 867 -3300 100 C ATOM 111 CD1 LEU A 57 4.863 -16.679 -3.405 1.00 77.03 C ANISOU 111 CD1 LEU A 57 13536 7384 8349 431 -3197 186 C ATOM 112 CD2 LEU A 57 2.759 -17.090 -2.119 1.00 76.29 C ANISOU 112 CD2 LEU A 57 13143 7421 8423 1077 -3270 -143 C ATOM 113 N TYR A 58 0.432 -13.867 -5.761 1.00 95.94 N ANISOU 113 N TYR A 58 16519 9298 10637 1716 -3715 335 N ATOM 114 CA TYR A 58 -0.239 -12.629 -6.122 1.00 99.09 C ANISOU 114 CA TYR A 58 17182 9454 11015 1924 -3807 384 C ATOM 115 C TYR A 58 -1.675 -12.750 -5.649 1.00101.57 C ANISOU 115 C TYR A 58 17278 9910 11405 2307 -3835 176 C ATOM 116 O TYR A 58 -2.194 -11.890 -4.933 1.00102.86 O ANISOU 116 O TYR A 58 17580 9873 11629 2486 -3891 75 O ATOM 117 CB TYR A 58 -0.263 -12.434 -7.640 1.00 98.61 C ANISOU 117 CB TYR A 58 17206 9441 10820 1886 -3821 593 C ATOM 118 CG TYR A 58 1.065 -12.560 -8.352 1.00 96.52 C ANISOU 118 CG TYR A 58 17070 9146 10459 1488 -3764 795 C ATOM 119 CD1 TYR A 58 1.996 -11.532 -8.317 1.00 98.07 C ANISOU 119 CD1 TYR A 58 17643 8993 10626 1257 -3773 920 C ATOM 120 CD2 TYR A 58 1.367 -13.692 -9.097 1.00 93.49 C ANISOU 120 CD2 TYR A 58 16414 9098 10010 1330 -3682 849 C ATOM 121 CE1 TYR A 58 3.203 -11.638 -8.982 1.00 97.23 C ANISOU 121 CE1 TYR A 58 17638 8877 10428 872 -3702 1087 C ATOM 122 CE2 TYR A 58 2.572 -13.807 -9.766 1.00 92.60 C ANISOU 122 CE2 TYR A 58 16398 8980 9804 952 -3617 1021 C ATOM 123 CZ TYR A 58 3.485 -12.777 -9.704 1.00 94.20 C ANISOU 123 CZ TYR A 58 16978 8836 9979 722 -3629 1138 C ATOM 124 OH TYR A 58 4.684 -12.885 -10.368 1.00 93.31 O ANISOU 124 OH TYR A 58 16943 8735 9775 328 -3546 1289 O ATOM 125 N LYS A 59 -2.301 -13.853 -6.049 1.00103.22 N ANISOU 125 N LYS A 59 17125 10488 11607 2404 -3775 102 N ATOM 126 CA LYS A 59 -3.716 -14.100 -5.807 1.00107.15 C ANISOU 126 CA LYS A 59 17377 11179 12156 2734 -3774 -94 C ATOM 127 C LYS A 59 -3.940 -14.573 -4.372 1.00108.56 C ANISOU 127 C LYS A 59 17361 11424 12463 2797 -3719 -339 C ATOM 128 O LYS A 59 -4.684 -15.521 -4.115 1.00106.43 O ANISOU 128 O LYS A 59 16743 11455 12241 2913 -3633 -514 O ATOM 129 CB LYS A 59 -4.248 -15.129 -6.809 1.00106.01 C ANISOU 129 CB LYS A 59 16913 11412 11954 2773 -3703 -85 C ATOM 130 CG LYS A 59 -3.495 -15.152 -8.146 1.00106.60 C ANISOU 130 CG LYS A 59 17094 11510 11899 2559 -3705 170 C ATOM 131 CD LYS A 59 -3.571 -13.820 -8.893 1.00110.44 C ANISOU 131 CD LYS A 59 17952 11713 12296 2633 -3823 353 C ATOM 132 CE LYS A 59 -2.611 -13.793 -10.079 1.00110.39 C ANISOU 132 CE LYS A 59 18085 11697 12163 2361 -3809 608 C ATOM 133 NZ LYS A 59 -2.474 -12.432 -10.673 1.00113.61 N ANISOU 133 NZ LYS A 59 18896 11778 12492 2385 -3903 796 N ATOM 134 N GLU A 60 -3.276 -13.890 -3.448 1.00112.87 N ANISOU 134 N GLU A 60 18137 11688 13061 2702 -3757 -351 N ATOM 135 CA GLU A 60 -3.354 -14.166 -2.025 1.00114.78 C ANISOU 135 CA GLU A 60 18240 11954 13418 2739 -3714 -565 C ATOM 136 C GLU A 60 -3.157 -12.821 -1.341 1.00119.03 C ANISOU 136 C GLU A 60 19107 12131 13986 2751 -3794 -562 C ATOM 137 O GLU A 60 -3.401 -12.663 -0.144 1.00119.06 O ANISOU 137 O GLU A 60 19048 12113 14077 2820 -3777 -736 O ATOM 138 CB GLU A 60 -2.242 -15.137 -1.621 1.00113.26 C ANISOU 138 CB GLU A 60 17916 11865 13254 2478 -3629 -551 C ATOM 139 CG GLU A 60 -2.270 -15.576 -0.163 1.00112.96 C ANISOU 139 CG GLU A 60 17695 11894 13332 2511 -3567 -768 C ATOM 140 CD GLU A 60 -1.068 -16.423 0.215 1.00111.65 C ANISOU 140 CD GLU A 60 17439 11802 13181 2253 -3501 -726 C ATOM 141 OE1 GLU A 60 -0.187 -16.627 -0.646 1.00111.59 O ANISOU 141 OE1 GLU A 60 17498 11821 13082 1992 -3477 -536 O ATOM 142 OE2 GLU A 60 -1.004 -16.883 1.374 1.00110.38 O ANISOU 142 OE2 GLU A 60 17101 11724 13114 2261 -3425 -898 O ATOM 143 N TYR A 61 -2.717 -11.849 -2.135 1.00122.66 N ANISOU 143 N TYR A 61 19908 12327 14371 2668 -3863 -358 N ATOM 144 CA TYR A 61 -2.377 -10.520 -1.643 1.00126.05 C ANISOU 144 CA TYR A 61 20676 12394 14822 2628 -3913 -323 C ATOM 145 C TYR A 61 -3.278 -9.466 -2.276 1.00129.40 C ANISOU 145 C TYR A 61 21286 12684 15197 2865 -3998 -261 C ATOM 146 O TYR A 61 -3.247 -9.259 -3.489 1.00130.66 O ANISOU 146 O TYR A 61 21571 12815 15258 2855 -4030 -77 O ATOM 147 CB TYR A 61 -0.912 -10.202 -1.953 1.00127.23 C ANISOU 147 CB TYR A 61 21102 12314 14927 2269 -3891 -133 C ATOM 148 CG TYR A 61 0.086 -10.914 -1.064 1.00125.16 C ANISOU 148 CG TYR A 61 20731 12097 14727 2019 -3812 -205 C ATOM 149 CD1 TYR A 61 -0.014 -12.278 -0.822 1.00122.16 C ANISOU 149 CD1 TYR A 61 20001 12035 14380 2038 -3757 -303 C ATOM 150 CD2 TYR A 61 1.137 -10.224 -0.479 1.00126.52 C ANISOU 150 CD2 TYR A 61 21140 12006 14927 1756 -3775 -178 C ATOM 151 CE1 TYR A 61 0.891 -12.932 -0.017 1.00119.81 C ANISOU 151 CE1 TYR A 61 19608 11774 14142 1825 -3683 -364 C ATOM 152 CE2 TYR A 61 2.050 -10.872 0.330 1.00124.23 C ANISOU 152 CE2 TYR A 61 20736 11773 14693 1519 -3689 -255 C ATOM 153 CZ TYR A 61 1.922 -12.226 0.556 1.00120.95 C ANISOU 153 CZ TYR A 61 19990 11653 14313 1562 -3649 -346 C ATOM 154 OH TYR A 61 2.829 -12.879 1.359 1.00118.59 O ANISOU 154 OH TYR A 61 19516 11482 14062 1302 -3519 -441 O ATOM 155 N ASP A 65 -1.424 -3.708 -1.796 1.00146.44 N ANISOU 155 N ASP A 65 24995 13268 17377 2537 -4056 123 N ATOM 156 CA ASP A 65 -0.249 -4.358 -1.231 1.00143.37 C ANISOU 156 CA ASP A 65 24527 12931 17016 2199 -3967 85 C ATOM 157 C ASP A 65 0.859 -4.417 -2.277 1.00143.20 C ANISOU 157 C ASP A 65 24689 12834 16888 1879 -3925 304 C ATOM 158 O ASP A 65 1.787 -5.220 -2.167 1.00140.28 O ANISOU 158 O ASP A 65 24211 12583 16506 1597 -3859 308 O ATOM 159 CB ASP A 65 -0.599 -5.773 -0.764 1.00139.36 C ANISOU 159 CB ASP A 65 23617 12789 16545 2272 -3958 -72 C ATOM 160 CG ASP A 65 -2.071 -5.932 -0.429 1.00139.51 C ANISOU 160 CG ASP A 65 23409 12990 16606 2658 -4019 -231 C ATOM 161 OD1 ASP A 65 -2.914 -5.354 -1.148 1.00142.34 O ANISOU 161 OD1 ASP A 65 23869 13296 16917 2890 -4090 -163 O ATOM 162 OD2 ASP A 65 -2.388 -6.636 0.553 1.00136.77 O ANISOU 162 OD2 ASP A 65 22776 12852 16338 2721 -3987 -427 O ATOM 163 N ASN A 66 0.758 -3.543 -3.276 1.00146.43 N ANISOU 163 N ASN A 66 25372 13049 17217 1919 -3957 486 N ATOM 164 CA ASN A 66 1.610 -3.582 -4.466 1.00146.39 C ANISOU 164 CA ASN A 66 25524 13008 17089 1656 -3923 710 C ATOM 165 C ASN A 66 3.122 -3.703 -4.243 1.00144.98 C ANISOU 165 C ASN A 66 25426 12762 16897 1198 -3810 748 C ATOM 166 O ASN A 66 3.837 -4.192 -5.119 1.00144.27 O ANISOU 166 O ASN A 66 25337 12769 16708 955 -3771 891 O ATOM 167 CB ASN A 66 1.310 -2.386 -5.376 1.00150.50 C ANISOU 167 CB ASN A 66 26366 13275 17542 1768 -3959 887 C ATOM 168 CG ASN A 66 -0.011 -2.528 -6.109 1.00151.08 C ANISOU 168 CG ASN A 66 26331 13502 17572 2156 -4063 919 C ATOM 169 OD1 ASN A 66 -0.109 -3.259 -7.095 1.00149.79 O ANISOU 169 OD1 ASN A 66 26037 13562 17315 2158 -4080 1023 O ATOM 170 ND2 ASN A 66 -1.032 -1.824 -5.635 1.00153.11 N ANISOU 170 ND2 ASN A 66 26626 13656 17893 2480 -4125 825 N ATOM 171 N ILE A 67 3.607 -3.268 -3.083 1.00144.55 N ANISOU 171 N ILE A 67 25416 12568 16939 1071 -3747 612 N ATOM 172 CA ILE A 67 5.033 -3.369 -2.784 1.00142.88 C ANISOU 172 CA ILE A 67 25247 12324 16716 632 -3626 619 C ATOM 173 C ILE A 67 5.468 -4.830 -2.665 1.00137.63 C ANISOU 173 C ILE A 67 24271 11982 16041 479 -3597 570 C ATOM 174 O ILE A 67 6.619 -5.175 -2.933 1.00136.55 O ANISOU 174 O ILE A 67 24135 11904 15845 109 -3507 639 O ATOM 175 CB ILE A 67 5.420 -2.583 -1.509 1.00144.10 C ANISOU 175 CB ILE A 67 25479 12290 16982 540 -3552 464 C ATOM 176 CG1 ILE A 67 6.943 -2.494 -1.377 1.00143.84 C ANISOU 176 CG1 ILE A 67 25515 12219 16917 69 -3411 488 C ATOM 177 CG2 ILE A 67 4.793 -3.206 -0.269 1.00141.50 C ANISOU 177 CG2 ILE A 67 24855 12138 16772 742 -3577 235 C ATOM 178 CD1 ILE A 67 7.415 -1.819 -0.113 1.00144.72 C ANISOU 178 CD1 ILE A 67 25655 12196 17137 -53 -3319 321 C ATOM 179 N TYR A 68 4.532 -5.687 -2.279 1.00134.25 N ANISOU 179 N TYR A 68 23565 11775 15668 766 -3666 448 N ATOM 180 CA TYR A 68 4.797 -7.114 -2.186 1.00129.04 C ANISOU 180 CA TYR A 68 22603 11419 15009 671 -3641 401 C ATOM 181 C TYR A 68 4.805 -7.779 -3.564 1.00126.59 C ANISOU 181 C TYR A 68 22246 11274 14577 629 -3665 586 C ATOM 182 O TYR A 68 5.427 -8.819 -3.753 1.00123.83 O ANISOU 182 O TYR A 68 21719 11135 14196 417 -3614 616 O ATOM 183 CB TYR A 68 3.769 -7.784 -1.270 1.00127.31 C ANISOU 183 CB TYR A 68 22089 11387 14895 997 -3688 193 C ATOM 184 CG TYR A 68 4.146 -7.754 0.196 1.00126.62 C ANISOU 184 CG TYR A 68 21901 11287 14923 913 -3617 -7 C ATOM 185 CD1 TYR A 68 5.472 -7.635 0.588 1.00126.46 C ANISOU 185 CD1 TYR A 68 21945 11205 14899 520 -3503 -4 C ATOM 186 CD2 TYR A 68 3.178 -7.853 1.187 1.00126.11 C ANISOU 186 CD2 TYR A 68 21643 11313 14961 1215 -3646 -207 C ATOM 187 CE1 TYR A 68 5.826 -7.614 1.923 1.00125.47 C ANISOU 187 CE1 TYR A 68 21689 11112 14870 442 -3422 -192 C ATOM 188 CE2 TYR A 68 3.522 -7.834 2.527 1.00125.10 C ANISOU 188 CE2 TYR A 68 21395 11207 14930 1134 -3567 -386 C ATOM 189 CZ TYR A 68 4.847 -7.713 2.889 1.00124.69 C ANISOU 189 CZ TYR A 68 21406 11097 14874 753 -3456 -377 C ATOM 190 OH TYR A 68 5.197 -7.692 4.219 1.00123.78 O ANISOU 190 OH TYR A 68 21142 11042 14848 674 -3365 -557 O ATOM 191 N GLN A 69 4.128 -7.166 -4.529 1.00127.02 N ANISOU 191 N GLN A 69 22451 11249 14564 823 -3734 712 N ATOM 192 CA GLN A 69 3.960 -7.774 -5.849 1.00124.02 C ANISOU 192 CA GLN A 69 21986 11067 14071 833 -3754 871 C ATOM 193 C GLN A 69 5.261 -7.914 -6.648 1.00121.25 C ANISOU 193 C GLN A 69 21733 10724 13612 403 -3665 1043 C ATOM 194 O GLN A 69 5.384 -8.808 -7.485 1.00119.37 O ANISOU 194 O GLN A 69 21319 10740 13296 321 -3646 1134 O ATOM 195 CB GLN A 69 2.918 -7.004 -6.667 1.00127.29 C ANISOU 195 CB GLN A 69 22533 11394 14437 1150 -3840 958 C ATOM 196 CG GLN A 69 1.555 -6.895 -5.999 1.00127.71 C ANISOU 196 CG GLN A 69 22455 11488 14581 1576 -3922 783 C ATOM 197 CD GLN A 69 0.843 -8.230 -5.875 1.00124.29 C ANISOU 197 CD GLN A 69 21615 11431 14177 1754 -3933 656 C ATOM 198 OE1 GLN A 69 1.174 -9.191 -6.567 1.00122.57 O ANISOU 198 OE1 GLN A 69 21221 11455 13895 1618 -3896 733 O ATOM 199 NE2 GLN A 69 -0.145 -8.293 -4.989 1.00123.53 N ANISOU 199 NE2 GLN A 69 21355 11403 14179 2050 -3971 451 N ATOM 200 N GLN A 70 6.223 -7.034 -6.388 1.00120.50 N ANISOU 200 N GLN A 70 21893 10379 13513 123 -3594 1074 N ATOM 201 CA GLN A 70 7.495 -7.049 -7.110 1.00117.66 C ANISOU 201 CA GLN A 70 21624 10032 13049 -303 -3492 1214 C ATOM 202 C GLN A 70 8.416 -8.180 -6.653 1.00110.79 C ANISOU 202 C GLN A 70 20503 9403 12191 -610 -3402 1146 C ATOM 203 O GLN A 70 9.082 -8.818 -7.470 1.00109.66 O ANISOU 203 O GLN A 70 20261 9450 11953 -862 -3341 1254 O ATOM 204 CB GLN A 70 8.207 -5.697 -6.966 1.00121.01 C ANISOU 204 CB GLN A 70 22380 10132 13465 -498 -3428 1249 C ATOM 205 CG GLN A 70 9.721 -5.739 -7.171 1.00120.66 C ANISOU 205 CG GLN A 70 22369 10125 13351 -988 -3288 1298 C ATOM 206 CD GLN A 70 10.127 -5.802 -8.632 1.00121.72 C ANISOU 206 CD GLN A 70 22567 10338 13344 -1155 -3260 1497 C ATOM 207 OE1 GLN A 70 9.397 -5.348 -9.513 1.00124.17 O ANISOU 207 OE1 GLN A 70 23015 10561 13602 -932 -3333 1625 O ATOM 208 NE2 GLN A 70 11.302 -6.364 -8.895 1.00120.03 N ANISOU 208 NE2 GLN A 70 22234 10309 13065 -1547 -3147 1516 N ATOM 209 N LYS A 71 8.446 -8.430 -5.348 1.00105.99 N ANISOU 209 N LYS A 71 19775 8798 11698 -585 -3386 962 N ATOM 210 CA LYS A 71 9.375 -9.405 -4.779 1.00100.27 C ANISOU 210 CA LYS A 71 18821 8283 10996 -883 -3286 883 C ATOM 211 C LYS A 71 9.073 -10.863 -5.143 1.00 94.39 C ANISOU 211 C LYS A 71 17769 7861 10232 -825 -3302 910 C ATOM 212 O LYS A 71 9.945 -11.722 -5.021 1.00 92.21 O ANISOU 212 O LYS A 71 17294 7799 9943 -1117 -3198 893 O ATOM 213 CB LYS A 71 9.492 -9.231 -3.260 1.00 99.44 C ANISOU 213 CB LYS A 71 18652 8110 11022 -867 -3249 665 C ATOM 214 CG LYS A 71 8.235 -8.709 -2.595 1.00100.07 C ANISOU 214 CG LYS A 71 18776 8044 11203 -438 -3356 548 C ATOM 215 CD LYS A 71 8.363 -8.680 -1.082 1.00 98.12 C ANISOU 215 CD LYS A 71 18401 7799 11082 -431 -3304 319 C ATOM 216 CE LYS A 71 9.391 -7.659 -0.625 1.00 99.23 C ANISOU 216 CE LYS A 71 18715 7770 11219 -725 -3194 298 C ATOM 217 NZ LYS A 71 9.460 -7.584 0.861 1.00 97.81 N ANISOU 217 NZ LYS A 71 18384 7622 11158 -696 -3136 74 N ATOM 218 N ILE A 72 7.851 -11.147 -5.585 1.00 91.82 N ANISOU 218 N ILE A 72 17358 7626 9903 -448 -3410 933 N ATOM 219 CA ILE A 72 7.538 -12.481 -6.091 1.00 87.02 C ANISOU 219 CA ILE A 72 16409 7403 9253 -387 -3398 956 C ATOM 220 C ILE A 72 8.194 -12.659 -7.454 1.00 87.08 C ANISOU 220 C ILE A 72 16442 7530 9116 -655 -3343 1151 C ATOM 221 O ILE A 72 8.687 -13.738 -7.789 1.00 85.22 O ANISOU 221 O ILE A 72 15937 7611 8830 -847 -3257 1171 O ATOM 222 CB ILE A 72 6.021 -12.728 -6.209 1.00 85.42 C ANISOU 222 CB ILE A 72 16064 7312 9080 91 -3513 894 C ATOM 223 CG1 ILE A 72 5.374 -12.738 -4.823 1.00 83.77 C ANISOU 223 CG1 ILE A 72 15733 7071 9025 344 -3533 658 C ATOM 224 CG2 ILE A 72 5.747 -14.048 -6.925 1.00 81.99 C ANISOU 224 CG2 ILE A 72 15255 7313 8585 116 -3468 909 C ATOM 225 CD1 ILE A 72 4.357 -11.640 -4.612 1.00 86.43 C ANISOU 225 CD1 ILE A 72 16287 7140 9412 690 -3649 609 C ATOM 226 N LYS A 73 8.204 -11.586 -8.235 1.00 89.45 N ANISOU 226 N LYS A 73 17021 7611 9355 -666 -3367 1266 N ATOM 227 CA LYS A 73 8.909 -11.586 -9.505 1.00 89.57 C ANISOU 227 CA LYS A 73 17075 7713 9244 -937 -3298 1430 C ATOM 228 C LYS A 73 10.399 -11.743 -9.228 1.00 87.90 C ANISOU 228 C LYS A 73 16860 7529 9011 -1408 -3164 1422 C ATOM 229 O LYS A 73 11.117 -12.396 -9.985 1.00 86.02 O ANISOU 229 O LYS A 73 16466 7523 8693 -1675 -3073 1492 O ATOM 230 CB LYS A 73 8.635 -10.295 -10.273 1.00 93.38 C ANISOU 230 CB LYS A 73 17888 7924 9670 -841 -3349 1552 C ATOM 231 CG LYS A 73 7.160 -9.952 -10.400 1.00 94.80 C ANISOU 231 CG LYS A 73 18091 8048 9881 -362 -3478 1538 C ATOM 232 CD LYS A 73 6.945 -8.849 -11.424 1.00 99.10 C ANISOU 232 CD LYS A 73 18924 8390 10340 -290 -3513 1701 C ATOM 233 CE LYS A 73 7.642 -7.564 -11.011 1.00101.36 C ANISOU 233 CE LYS A 73 19568 8306 10639 -464 -3479 1718 C ATOM 234 NZ LYS A 73 7.865 -6.658 -12.173 1.00104.18 N ANISOU 234 NZ LYS A 73 20193 8505 10885 -535 -3467 1909 N ATOM 235 N ASP A 74 10.851 -11.147 -8.127 1.00 88.59 N ANISOU 235 N ASP A 74 17081 7406 9173 -1501 -3141 1313 N ATOM 236 CA ASP A 74 12.219 -11.323 -7.651 1.00 87.42 C ANISOU 236 CA ASP A 74 16864 7333 9018 -1915 -3001 1252 C ATOM 237 C ASP A 74 12.444 -12.764 -7.205 1.00 83.98 C ANISOU 237 C ASP A 74 16069 7219 8619 -2006 -2942 1180 C ATOM 238 O ASP A 74 13.579 -13.231 -7.126 1.00 82.44 O ANISOU 238 O ASP A 74 15714 7215 8395 -2352 -2808 1146 O ATOM 239 CB ASP A 74 12.510 -10.376 -6.484 1.00 88.43 C ANISOU 239 CB ASP A 74 17156 7213 9230 -1940 -2979 1118 C ATOM 240 CG ASP A 74 12.853 -8.969 -6.939 1.00 92.36 C ANISOU 240 CG ASP A 74 17991 7434 9668 -2025 -2963 1197 C ATOM 241 OD1 ASP A 74 13.715 -8.823 -7.829 1.00 93.11 O ANISOU 241 OD1 ASP A 74 18134 7592 9653 -2305 -2883 1301 O ATOM 242 OD2 ASP A 74 12.260 -8.010 -6.402 1.00 94.39 O ANISOU 242 OD2 ASP A 74 18457 7414 9993 -1807 -3025 1149 O ATOM 243 N LEU A 75 11.350 -13.458 -6.906 1.00 83.46 N ANISOU 243 N LEU A 75 15804 7289 8619 -1659 -3014 1117 N ATOM 244 CA LEU A 75 11.409 -14.832 -6.427 1.00 80.59 C ANISOU 244 CA LEU A 75 14962 7344 8315 -1656 -2906 968 C ATOM 245 C LEU A 75 11.146 -15.807 -7.574 1.00 79.72 C ANISOU 245 C LEU A 75 14622 7551 8116 -1636 -2886 1071 C ATOM 246 O LEU A 75 11.616 -16.945 -7.556 1.00 77.06 O ANISOU 246 O LEU A 75 13935 7557 7787 -1783 -2759 1010 O ATOM 247 CB LEU A 75 10.391 -15.038 -5.300 1.00 79.23 C ANISOU 247 CB LEU A 75 14621 7202 8282 -1287 -2948 769 C ATOM 248 CG LEU A 75 10.738 -16.087 -4.242 1.00 75.69 C ANISOU 248 CG LEU A 75 13776 7057 7926 -1342 -2814 573 C ATOM 249 CD1 LEU A 75 12.099 -15.783 -3.655 1.00 75.74 C ANISOU 249 CD1 LEU A 75 13849 7000 7930 -1720 -2715 533 C ATOM 250 CD2 LEU A 75 9.695 -16.116 -3.140 1.00 75.06 C ANISOU 250 CD2 LEU A 75 13588 6959 7975 -976 -2865 386 C ATOM 251 N HIS A 76 10.405 -15.341 -8.577 1.00 82.35 N ANISOU 251 N HIS A 76 15160 7767 8363 -1452 -3010 1227 N ATOM 252 CA HIS A 76 10.038 -16.157 -9.733 1.00 81.90 C ANISOU 252 CA HIS A 76 14884 8008 8226 -1403 -2993 1308 C ATOM 253 C HIS A 76 11.241 -16.384 -10.645 1.00 80.51 C ANISOU 253 C HIS A 76 14663 7956 7970 -1817 -2860 1406 C ATOM 254 O HIS A 76 11.206 -17.223 -11.548 1.00 78.64 O ANISOU 254 O HIS A 76 14162 8014 7704 -1853 -2784 1433 O ATOM 255 CB HIS A 76 8.899 -15.482 -10.504 1.00 86.66 C ANISOU 255 CB HIS A 76 15632 8482 8812 -1066 -3110 1376 C ATOM 256 CG HIS A 76 8.030 -16.437 -11.261 1.00 87.47 C ANISOU 256 CG HIS A 76 15402 8930 8903 -853 -3092 1355 C ATOM 257 ND1 HIS A 76 8.398 -17.742 -11.504 1.00 85.24 N ANISOU 257 ND1 HIS A 76 14739 9025 8621 -1010 -2955 1305 N ATOM 258 CD2 HIS A 76 6.808 -16.278 -11.819 1.00 90.18 C ANISOU 258 CD2 HIS A 76 15718 9308 9238 -497 -3178 1363 C ATOM 259 CE1 HIS A 76 7.439 -18.347 -12.185 1.00 85.57 C ANISOU 259 CE1 HIS A 76 14542 9311 8658 -769 -2954 1281 C ATOM 260 NE2 HIS A 76 6.463 -17.480 -12.387 1.00 88.71 N ANISOU 260 NE2 HIS A 76 15145 9517 9043 -458 -3093 1317 N ATOM 261 N LYS A 77 12.305 -15.625 -10.403 1.00 66.81 N ANISOU 261 N LYS A 77 12151 6346 6888 -684 -2038 839 N ATOM 262 CA LYS A 77 13.526 -15.735 -11.194 1.00 69.83 C ANISOU 262 CA LYS A 77 12646 6781 7107 -931 -1879 921 C ATOM 263 C LYS A 77 14.538 -16.677 -10.547 1.00 67.78 C ANISOU 263 C LYS A 77 12113 6727 6912 -1069 -1660 892 C ATOM 264 O LYS A 77 15.641 -16.853 -11.061 1.00 67.93 O ANISOU 264 O LYS A 77 12172 6823 6815 -1281 -1506 932 O ATOM 265 CB LYS A 77 14.155 -14.355 -11.396 1.00 75.09 C ANISOU 265 CB LYS A 77 13619 7282 7631 -1078 -1892 995 C ATOM 266 CG LYS A 77 14.708 -13.734 -10.120 1.00 76.19 C ANISOU 266 CG LYS A 77 13680 7414 7853 -1136 -1827 970 C ATOM 267 CD LYS A 77 14.768 -12.216 -10.222 1.00 80.63 C ANISOU 267 CD LYS A 77 14566 7756 8312 -1180 -1927 1028 C ATOM 268 CE LYS A 77 15.540 -11.623 -9.053 1.00 80.38 C ANISOU 268 CE LYS A 77 14463 7737 8340 -1281 -1827 1014 C ATOM 269 NZ LYS A 77 15.338 -10.151 -8.954 1.00 83.70 N ANISOU 269 NZ LYS A 77 15173 7927 8702 -1266 -1956 1056 N ATOM 270 N LYS A 78 14.161 -17.274 -9.419 1.00 66.22 N ANISOU 270 N LYS A 78 11644 6621 6897 -950 -1649 814 N ATOM 271 CA LYS A 78 15.033 -18.213 -8.721 1.00 64.51 C ANISOU 271 CA LYS A 78 11167 6594 6750 -1051 -1463 779 C ATOM 272 C LYS A 78 14.247 -19.422 -8.233 1.00 61.24 C ANISOU 272 C LYS A 78 10485 6291 6494 -885 -1477 708 C ATOM 273 O LYS A 78 14.827 -20.447 -7.872 1.00 58.12 O ANISOU 273 O LYS A 78 9880 6056 6148 -946 -1340 682 O ATOM 274 CB LYS A 78 15.728 -17.530 -7.539 1.00 65.78 C ANISOU 274 CB LYS A 78 11282 6753 6960 -1127 -1398 765 C ATOM 275 CG LYS A 78 17.232 -17.374 -7.713 1.00 68.09 C ANISOU 275 CG LYS A 78 11609 7123 7141 -1378 -1219 796 C ATOM 276 CD LYS A 78 17.820 -16.385 -6.710 1.00 69.60 C ANISOU 276 CD LYS A 78 11823 7266 7354 -1445 -1185 794 C ATOM 277 CE LYS A 78 17.481 -16.765 -5.277 1.00 67.98 C ANISOU 277 CE LYS A 78 11368 7133 7328 -1309 -1189 729 C ATOM 278 NZ LYS A 78 17.997 -15.762 -4.301 1.00 68.54 N ANISOU 278 NZ LYS A 78 11467 7152 7423 -1361 -1162 729 N ATOM 279 N TYR A 79 12.924 -19.296 -8.219 1.00 62.68 N ANISOU 279 N TYR A 79 10677 6388 6752 -677 -1645 667 N ATOM 280 CA TYR A 79 12.062 -20.378 -7.764 1.00 62.05 C ANISOU 280 CA TYR A 79 10351 6404 6822 -517 -1663 588 C ATOM 281 C TYR A 79 10.871 -20.523 -8.709 1.00 64.88 C ANISOU 281 C TYR A 79 10778 6709 7165 -352 -1816 568 C ATOM 282 O TYR A 79 10.289 -19.527 -9.147 1.00 66.86 O ANISOU 282 O TYR A 79 11235 6808 7362 -274 -1971 578 O ATOM 283 CB TYR A 79 11.608 -20.144 -6.317 1.00 60.90 C ANISOU 283 CB TYR A 79 10055 6248 6836 -414 -1695 512 C ATOM 284 CG TYR A 79 12.747 -20.102 -5.320 1.00 59.52 C ANISOU 284 CG TYR A 79 9787 6149 6681 -557 -1549 525 C ATOM 285 CD1 TYR A 79 13.321 -21.272 -4.840 1.00 57.31 C ANISOU 285 CD1 TYR A 79 9287 6030 6457 -616 -1406 507 C ATOM 286 CD2 TYR A 79 13.249 -18.893 -4.865 1.00 61.08 C ANISOU 286 CD2 TYR A 79 10116 6256 6834 -627 -1561 554 C ATOM 287 CE1 TYR A 79 14.366 -21.236 -3.934 1.00 57.05 C ANISOU 287 CE1 TYR A 79 9164 6074 6436 -734 -1284 511 C ATOM 288 CE2 TYR A 79 14.289 -18.846 -3.961 1.00 61.14 C ANISOU 288 CE2 TYR A 79 10029 6345 6858 -748 -1429 560 C ATOM 289 CZ TYR A 79 14.844 -20.020 -3.499 1.00 59.42 C ANISOU 289 CZ TYR A 79 9586 6295 6694 -797 -1293 535 C ATOM 290 OH TYR A 79 15.881 -19.985 -2.598 1.00 59.25 O ANISOU 290 OH TYR A 79 9464 6362 6686 -901 -1170 534 O ATOM 291 N SER A 80 10.525 -21.763 -9.040 1.00 64.82 N ANISOU 291 N SER A 80 10601 6828 7197 -296 -1777 536 N ATOM 292 CA SER A 80 9.453 -22.008 -9.991 1.00 66.50 C ANISOU 292 CA SER A 80 10857 7023 7387 -145 -1912 509 C ATOM 293 C SER A 80 8.164 -22.457 -9.293 1.00 66.07 C ANISOU 293 C SER A 80 10593 7000 7512 63 -1999 382 C ATOM 294 O SER A 80 7.065 -22.098 -9.726 1.00 68.25 O ANISOU 294 O SER A 80 10928 7202 7801 226 -2167 326 O ATOM 295 CB SER A 80 9.886 -23.046 -11.032 1.00 65.87 C ANISOU 295 CB SER A 80 10749 7075 7203 -225 -1822 551 C ATOM 296 OG SER A 80 11.218 -22.835 -11.466 1.00 66.10 O ANISOU 296 OG SER A 80 10905 7121 7090 -445 -1691 642 O ATOM 297 N TYR A 81 8.308 -23.225 -8.208 1.00 62.38 N ANISOU 297 N TYR A 81 9884 6641 7177 54 -1884 330 N ATOM 298 CA TYR A 81 7.166 -23.864 -7.533 1.00 60.85 C ANISOU 298 CA TYR A 81 9462 6508 7151 219 -1922 203 C ATOM 299 C TYR A 81 7.108 -23.708 -5.999 1.00 56.75 C ANISOU 299 C TYR A 81 8795 5989 6776 237 -1876 138 C ATOM 300 O TYR A 81 8.111 -23.425 -5.340 1.00 55.11 O ANISOU 300 O TYR A 81 8608 5777 6553 108 -1781 195 O ATOM 301 CB TYR A 81 7.099 -25.357 -7.887 1.00 61.64 C ANISOU 301 CB TYR A 81 9374 6776 7269 216 -1829 180 C ATOM 302 CG TYR A 81 7.040 -25.668 -9.368 1.00 65.39 C ANISOU 302 CG TYR A 81 9958 7283 7605 212 -1875 222 C ATOM 303 CD1 TYR A 81 5.825 -25.892 -10.008 1.00 67.46 C ANISOU 303 CD1 TYR A 81 10187 7555 7888 369 -2008 140 C ATOM 304 CD2 TYR A 81 8.200 -25.747 -10.124 1.00 66.73 C ANISOU 304 CD2 TYR A 81 10255 7481 7617 46 -1784 333 C ATOM 305 CE1 TYR A 81 5.775 -26.179 -11.360 1.00 69.54 C ANISOU 305 CE1 TYR A 81 10552 7855 8015 366 -2057 177 C ATOM 306 CE2 TYR A 81 8.157 -26.033 -11.472 1.00 68.88 C ANISOU 306 CE2 TYR A 81 10630 7791 7750 37 -1822 368 C ATOM 307 CZ TYR A 81 6.942 -26.247 -12.085 1.00 70.35 C ANISOU 307 CZ TYR A 81 10790 7984 7954 200 -1963 295 C ATOM 308 OH TYR A 81 6.887 -26.533 -13.433 1.00 72.34 O ANISOU 308 OH TYR A 81 11147 8281 8058 193 -2009 327 O ATOM 309 N ILE A 82 5.914 -23.931 -5.453 1.00 56.13 N ANISOU 309 N ILE A 82 8560 5930 6835 394 -1941 6 N ATOM 310 CA ILE A 82 5.644 -23.759 -4.032 1.00 55.42 C ANISOU 310 CA ILE A 82 8330 5844 6881 432 -1912 -78 C ATOM 311 C ILE A 82 4.865 -24.930 -3.463 1.00 51.10 C ANISOU 311 C ILE A 82 7521 5425 6470 505 -1843 -191 C ATOM 312 O ILE A 82 3.885 -25.380 -4.060 1.00 53.03 O ANISOU 312 O ILE A 82 7698 5709 6744 612 -1907 -274 O ATOM 313 CB ILE A 82 4.724 -22.565 -3.802 1.00 61.10 C ANISOU 313 CB ILE A 82 9132 6443 7640 568 -2084 -168 C ATOM 314 CG1 ILE A 82 5.221 -21.345 -4.559 1.00 66.04 C ANISOU 314 CG1 ILE A 82 10048 6922 8121 524 -2187 -68 C ATOM 315 CG2 ILE A 82 4.576 -22.275 -2.320 1.00 59.90 C ANISOU 315 CG2 ILE A 82 8852 6302 7607 587 -2050 -249 C ATOM 316 CD1 ILE A 82 6.434 -20.724 -3.977 1.00 66.74 C ANISOU 316 CD1 ILE A 82 10230 6974 8153 368 -2103 30 C ATOM 317 N ARG A 83 5.268 -25.396 -2.287 1.00 47.25 N ANISOU 317 N ARG A 83 6888 5000 6063 447 -1715 -202 N ATOM 318 CA ARG A 83 4.425 -26.313 -1.536 1.00 45.64 C ANISOU 318 CA ARG A 83 6451 4899 5993 515 -1649 -325 C ATOM 319 C ARG A 83 4.130 -25.741 -0.151 1.00 43.84 C ANISOU 319 C ARG A 83 6149 4640 5867 548 -1645 -410 C ATOM 320 O ARG A 83 5.021 -25.222 0.526 1.00 45.21 O ANISOU 320 O ARG A 83 6385 4775 6019 463 -1609 -341 O ATOM 321 CB ARG A 83 5.063 -27.696 -1.440 1.00 43.85 C ANISOU 321 CB ARG A 83 6096 4802 5763 418 -1484 -272 C ATOM 322 CG ARG A 83 4.085 -28.786 -1.045 1.00 44.37 C ANISOU 322 CG ARG A 83 5945 4979 5935 476 -1418 -396 C ATOM 323 CD ARG A 83 4.784 -30.125 -0.914 1.00 44.05 C ANISOU 323 CD ARG A 83 5802 5058 5878 372 -1260 -341 C ATOM 324 NE ARG A 83 5.396 -30.557 -2.168 1.00 45.54 N ANISOU 324 NE ARG A 83 6071 5282 5951 316 -1267 -258 N ATOM 325 CZ ARG A 83 4.795 -31.334 -3.064 1.00 45.16 C ANISOU 325 CZ ARG A 83 5968 5304 5888 347 -1285 -307 C ATOM 326 NH1 ARG A 83 5.430 -31.682 -4.175 1.00 44.57 N ANISOU 326 NH1 ARG A 83 5973 5265 5696 290 -1289 -235 N ATOM 327 NH2 ARG A 83 3.559 -31.764 -2.849 1.00 44.88 N ANISOU 327 NH2 ARG A 83 5796 5305 5950 428 -1297 -441 N ATOM 328 N LYS A 84 2.869 -25.832 0.258 1.00 41.03 N ANISOU 328 N LYS A 84 5656 4315 5617 664 -1684 -573 N ATOM 329 CA LYS A 84 2.416 -25.206 1.498 1.00 41.21 C ANISOU 329 CA LYS A 84 5608 4319 5730 709 -1699 -683 C ATOM 330 C LYS A 84 2.274 -26.180 2.665 1.00 39.80 C ANISOU 330 C LYS A 84 5222 4252 5649 671 -1533 -748 C ATOM 331 O LYS A 84 1.933 -27.352 2.474 1.00 41.56 O ANISOU 331 O LYS A 84 5319 4575 5899 660 -1436 -774 O ATOM 332 CB LYS A 84 1.088 -24.475 1.270 1.00 44.79 C ANISOU 332 CB LYS A 84 6054 4732 6231 863 -1863 -846 C ATOM 333 CG LYS A 84 1.235 -22.974 1.066 1.00 49.17 C ANISOU 333 CG LYS A 84 6809 5151 6724 907 -2032 -818 C ATOM 334 CD LYS A 84 -0.112 -22.259 1.089 1.00 53.63 C ANISOU 334 CD LYS A 84 7337 5686 7354 1074 -2197 -1004 C ATOM 335 CE LYS A 84 0.059 -20.811 1.529 1.00 55.93 C ANISOU 335 CE LYS A 84 7765 5867 7617 1109 -2325 -997 C ATOM 336 NZ LYS A 84 0.635 -20.739 2.901 1.00 54.48 N ANISOU 336 NZ LYS A 84 7489 5731 7478 1021 -2212 -983 N ATOM 337 N THR A 85 2.535 -25.683 3.872 1.00 34.41 N ANISOU 337 N THR A 85 4505 3565 5002 644 -1494 -762 N ATOM 338 CA THR A 85 2.255 -26.437 5.087 1.00 31.92 C ANISOU 338 CA THR A 85 3999 3365 4764 616 -1334 -824 C ATOM 339 C THR A 85 1.202 -25.692 5.905 1.00 30.08 C ANISOU 339 C THR A 85 3672 3155 4602 695 -1384 -982 C ATOM 340 O THR A 85 1.019 -24.489 5.736 1.00 27.99 O ANISOU 340 O THR A 85 3503 2810 4323 761 -1538 -1008 O ATOM 341 CB THR A 85 3.520 -26.669 5.947 1.00 31.27 C ANISOU 341 CB THR A 85 3926 3305 4652 507 -1205 -689 C ATOM 342 OG1 THR A 85 4.055 -25.413 6.379 1.00 35.54 O ANISOU 342 OG1 THR A 85 4566 3781 5157 496 -1280 -641 O ATOM 343 CG2 THR A 85 4.581 -27.430 5.164 1.00 29.31 C ANISOU 343 CG2 THR A 85 3755 3046 4334 426 -1159 -546 C ATOM 344 N ARG A 86 0.506 -26.407 6.782 1.00 30.51 N ANISOU 344 N ARG A 86 3546 3318 4727 683 -1259 -1093 N ATOM 345 CA ARG A 86 -0.502 -25.786 7.636 1.00 35.33 C ANISOU 345 CA ARG A 86 4047 3971 5405 741 -1289 -1258 C ATOM 346 C ARG A 86 0.149 -24.866 8.667 1.00 37.79 C ANISOU 346 C ARG A 86 4392 4257 5709 717 -1295 -1209 C ATOM 347 O ARG A 86 1.040 -25.286 9.404 1.00 36.56 O ANISOU 347 O ARG A 86 4229 4129 5531 626 -1165 -1110 O ATOM 348 CB ARG A 86 -1.336 -26.859 8.339 1.00 37.09 C ANISOU 348 CB ARG A 86 4081 4324 5689 699 -1131 -1384 C ATOM 349 CG ARG A 86 -2.351 -26.316 9.332 1.00 40.32 C ANISOU 349 CG ARG A 86 4358 4796 6165 733 -1137 -1566 C ATOM 350 CD ARG A 86 -2.990 -27.442 10.129 1.00 39.22 C ANISOU 350 CD ARG A 86 4057 4783 6060 646 -950 -1668 C ATOM 351 NE ARG A 86 -3.778 -28.333 9.284 1.00 40.39 N ANISOU 351 NE ARG A 86 4144 4975 6229 657 -938 -1750 N ATOM 352 CZ ARG A 86 -4.320 -29.473 9.702 1.00 41.36 C ANISOU 352 CZ ARG A 86 4151 5195 6369 569 -780 -1828 C ATOM 353 NH1 ARG A 86 -4.153 -29.866 10.957 1.00 42.23 N ANISOU 353 NH1 ARG A 86 4210 5364 6470 461 -621 -1830 N ATOM 354 NH2 ARG A 86 -5.024 -30.222 8.865 1.00 41.71 N ANISOU 354 NH2 ARG A 86 4141 5275 6433 584 -784 -1907 N ATOM 355 N PRO A 87 -0.292 -23.599 8.715 1.00 39.09 N ANISOU 355 N PRO A 87 4596 4365 5893 809 -1458 -1286 N ATOM 356 CA PRO A 87 0.241 -22.639 9.689 1.00 37.68 C ANISOU 356 CA PRO A 87 4440 4161 5717 804 -1486 -1258 C ATOM 357 C PRO A 87 -0.216 -22.974 11.106 1.00 40.07 C ANISOU 357 C PRO A 87 4554 4583 6088 771 -1348 -1372 C ATOM 358 O PRO A 87 -1.186 -22.394 11.598 1.00 43.17 O ANISOU 358 O PRO A 87 4847 5008 6547 845 -1409 -1542 O ATOM 359 CB PRO A 87 -0.363 -21.308 9.233 1.00 37.26 C ANISOU 359 CB PRO A 87 4473 4010 5675 935 -1712 -1346 C ATOM 360 CG PRO A 87 -1.611 -21.689 8.511 1.00 39.03 C ANISOU 360 CG PRO A 87 4622 4267 5940 1018 -1767 -1497 C ATOM 361 CD PRO A 87 -1.306 -22.993 7.835 1.00 39.63 C ANISOU 361 CD PRO A 87 4694 4382 5982 938 -1641 -1410 C ATOM 362 N ASP A 88 0.484 -23.900 11.753 1.00 37.70 N ANISOU 362 N ASP A 88 4210 4348 5767 661 -1168 -1287 N ATOM 363 CA ASP A 88 0.085 -24.366 13.076 1.00 38.55 C ANISOU 363 CA ASP A 88 4157 4570 5919 606 -1017 -1389 C ATOM 364 C ASP A 88 1.211 -24.265 14.102 1.00 37.54 C ANISOU 364 C ASP A 88 4042 4449 5771 550 -931 -1289 C ATOM 365 O ASP A 88 1.087 -24.762 15.222 1.00 41.20 O ANISOU 365 O ASP A 88 4398 5004 6251 487 -784 -1353 O ATOM 366 CB ASP A 88 -0.427 -25.807 12.996 1.00 39.85 C ANISOU 366 CB ASP A 88 4242 4818 6081 530 -859 -1432 C ATOM 367 CG ASP A 88 0.616 -26.769 12.458 1.00 41.68 C ANISOU 367 CG ASP A 88 4572 5014 6249 468 -771 -1261 C ATOM 368 OD1 ASP A 88 1.643 -26.302 11.922 1.00 41.07 O ANISOU 368 OD1 ASP A 88 4628 4850 6127 479 -848 -1115 O ATOM 369 OD2 ASP A 88 0.405 -27.996 12.565 1.00 43.78 O ANISOU 369 OD2 ASP A 88 4777 5346 6513 408 -628 -1275 O ATOM 370 N GLY A 89 2.308 -23.620 13.720 1.00 33.12 N ANISOU 370 N GLY A 89 3629 3787 5168 567 -1021 -1144 N ATOM 371 CA GLY A 89 3.462 -23.512 14.592 1.00 31.89 C ANISOU 371 CA GLY A 89 3506 3617 4992 519 -956 -1060 C ATOM 372 C GLY A 89 4.411 -24.684 14.420 1.00 30.48 C ANISOU 372 C GLY A 89 3369 3455 4756 428 -827 -926 C ATOM 373 O GLY A 89 5.411 -24.803 15.128 1.00 30.45 O ANISOU 373 O GLY A 89 3448 3446 4678 338 -722 -843 O ATOM 374 N ASN A 90 4.090 -25.557 13.472 1.00 28.83 N ANISOU 374 N ASN A 90 3158 3263 4533 419 -804 -897 N ATOM 375 CA ASN A 90 4.926 -26.708 13.165 1.00 26.44 C ANISOU 375 CA ASN A 90 2893 2968 4185 346 -706 -786 C ATOM 376 C ASN A 90 5.415 -26.645 11.728 1.00 24.40 C ANISOU 376 C ASN A 90 2766 2633 3873 351 -803 -662 C ATOM 377 O ASN A 90 5.934 -27.626 11.196 1.00 23.10 O ANISOU 377 O ASN A 90 2631 2486 3660 287 -737 -580 O ATOM 378 CB ASN A 90 4.146 -28.004 13.386 1.00 27.77 C ANISOU 378 CB ASN A 90 2950 3230 4371 304 -559 -874 C ATOM 379 CG ASN A 90 3.765 -28.216 14.836 1.00 30.78 C ANISOU 379 CG ASN A 90 3224 3700 4771 254 -427 -985 C ATOM 380 OD1 ASN A 90 4.604 -28.125 15.732 1.00 32.66 O ANISOU 380 OD1 ASN A 90 3524 3946 4940 174 -369 -920 O ATOM 381 ND2 ASN A 90 2.490 -28.496 15.076 1.00 32.31 N ANISOU 381 ND2 ASN A 90 3319 3963 4995 249 -370 -1124 N ATOM 382 N SER A 91 5.251 -25.477 11.111 1.00 23.90 N ANISOU 382 N SER A 91 2791 2498 3793 405 -954 -651 N ATOM 383 CA SER A 91 5.503 -25.306 9.683 1.00 23.41 C ANISOU 383 CA SER A 91 2859 2370 3665 403 -1049 -560 C ATOM 384 C SER A 91 6.926 -25.652 9.244 1.00 22.86 C ANISOU 384 C SER A 91 2902 2272 3511 306 -1012 -396 C ATOM 385 O SER A 91 7.108 -26.330 8.237 1.00 25.70 O ANISOU 385 O SER A 91 3306 2624 3834 276 -996 -344 O ATOM 386 CB SER A 91 5.144 -23.886 9.235 1.00 25.69 C ANISOU 386 CB SER A 91 3258 2570 3933 450 -1233 -604 C ATOM 387 OG SER A 91 5.988 -22.924 9.841 1.00 28.56 O ANISOU 387 OG SER A 91 3705 2877 4271 431 -1278 -539 O ATOM 388 N PHE A 92 7.926 -25.192 9.993 1.00 21.60 N ANISOU 388 N PHE A 92 2786 2100 3322 253 -1002 -329 N ATOM 389 CA PHE A 92 9.320 -25.407 9.605 1.00 21.77 C ANISOU 389 CA PHE A 92 2909 2126 3235 131 -939 -189 C ATOM 390 C PHE A 92 9.697 -26.881 9.539 1.00 21.59 C ANISOU 390 C PHE A 92 2817 2198 3189 65 -795 -160 C ATOM 391 O PHE A 92 10.295 -27.333 8.563 1.00 20.87 O ANISOU 391 O PHE A 92 2780 2114 3036 15 -790 -81 O ATOM 392 CB PHE A 92 10.284 -24.684 10.548 1.00 22.69 C ANISOU 392 CB PHE A 92 3075 2241 3306 57 -878 -158 C ATOM 393 CG PHE A 92 11.714 -25.128 10.397 1.00 20.84 C ANISOU 393 CG PHE A 92 2880 2060 2977 -65 -777 -58 C ATOM 394 CD1 PHE A 92 12.455 -24.753 9.290 1.00 21.65 C ANISOU 394 CD1 PHE A 92 3097 2131 2997 -128 -822 31 C ATOM 395 CD2 PHE A 92 12.311 -25.928 11.357 1.00 19.72 C ANISOU 395 CD2 PHE A 92 2661 2012 2820 -116 -642 -67 C ATOM 396 CE1 PHE A 92 13.766 -25.167 9.143 1.00 22.06 C ANISOU 396 CE1 PHE A 92 3155 2255 2973 -232 -723 93 C ATOM 397 CE2 PHE A 92 13.621 -26.343 11.217 1.00 19.60 C ANISOU 397 CE2 PHE A 92 2659 2059 2728 -201 -566 -2 C ATOM 398 CZ PHE A 92 14.350 -25.962 10.109 1.00 20.82 C ANISOU 398 CZ PHE A 92 2898 2192 2821 -256 -601 70 C ATOM 399 N TYR A 93 9.350 -27.620 10.587 1.00 23.44 N ANISOU 399 N TYR A 93 2940 2511 3457 58 -681 -229 N ATOM 400 CA TYR A 93 9.701 -29.032 10.680 1.00 23.48 C ANISOU 400 CA TYR A 93 2893 2609 3418 -6 -554 -202 C ATOM 401 C TYR A 93 8.968 -29.879 9.644 1.00 24.87 C ANISOU 401 C TYR A 93 3031 2800 3617 24 -563 -224 C ATOM 402 O TYR A 93 9.537 -30.814 9.081 1.00 23.83 O ANISOU 402 O TYR A 93 2910 2715 3430 -26 -508 -167 O ATOM 403 CB TYR A 93 9.432 -29.556 12.091 1.00 22.25 C ANISOU 403 CB TYR A 93 2663 2515 3275 -30 -452 -265 C ATOM 404 CG TYR A 93 10.270 -28.878 13.150 1.00 20.59 C ANISOU 404 CG TYR A 93 2495 2302 3026 -71 -432 -246 C ATOM 405 CD1 TYR A 93 11.616 -29.187 13.299 1.00 18.57 C ANISOU 405 CD1 TYR A 93 2286 2083 2688 -139 -383 -165 C ATOM 406 CD2 TYR A 93 9.718 -27.928 14.000 1.00 21.52 C ANISOU 406 CD2 TYR A 93 2594 2387 3194 -32 -463 -330 C ATOM 407 CE1 TYR A 93 12.391 -28.566 14.263 1.00 18.85 C ANISOU 407 CE1 TYR A 93 2351 2121 2690 -174 -370 -163 C ATOM 408 CE2 TYR A 93 10.483 -27.304 14.969 1.00 20.63 C ANISOU 408 CE2 TYR A 93 2526 2273 3041 -72 -444 -321 C ATOM 409 CZ TYR A 93 11.819 -27.627 15.094 1.00 20.93 C ANISOU 409 CZ TYR A 93 2611 2346 2995 -147 -399 -236 C ATOM 410 OH TYR A 93 12.586 -27.010 16.055 1.00 24.68 O ANISOU 410 OH TYR A 93 3118 2825 3433 -186 -386 -242 O ATOM 411 N ARG A 94 7.708 -29.545 9.391 1.00 27.38 N ANISOU 411 N ARG A 94 3303 3083 4020 114 -635 -324 N ATOM 412 CA ARG A 94 6.913 -30.289 8.422 1.00 27.29 C ANISOU 412 CA ARG A 94 3253 3090 4028 144 -644 -367 C ATOM 413 C ARG A 94 7.357 -29.969 6.996 1.00 24.75 C ANISOU 413 C ARG A 94 3041 2706 3655 147 -743 -290 C ATOM 414 O ARG A 94 7.305 -30.825 6.115 1.00 24.70 O ANISOU 414 O ARG A 94 3026 2743 3617 126 -719 -275 O ATOM 415 CB ARG A 94 5.422 -29.993 8.598 1.00 29.69 C ANISOU 415 CB ARG A 94 3467 3381 4433 241 -686 -527 C ATOM 416 CG ARG A 94 4.516 -31.139 8.179 1.00 30.96 C ANISOU 416 CG ARG A 94 3538 3612 4614 235 -623 -601 C ATOM 417 CD ARG A 94 3.046 -30.767 8.282 1.00 32.97 C ANISOU 417 CD ARG A 94 3703 3863 4962 326 -668 -786 C ATOM 418 NE ARG A 94 2.687 -30.281 9.611 1.00 35.19 N ANISOU 418 NE ARG A 94 3914 4159 5298 340 -622 -886 N ATOM 419 CZ ARG A 94 2.343 -31.064 10.629 1.00 35.83 C ANISOU 419 CZ ARG A 94 3899 4326 5389 271 -474 -948 C ATOM 420 NH1 ARG A 94 2.317 -32.381 10.478 1.00 34.75 N ANISOU 420 NH1 ARG A 94 3740 4250 5213 187 -369 -912 N ATOM 421 NH2 ARG A 94 2.028 -30.530 11.802 1.00 36.36 N ANISOU 421 NH2 ARG A 94 3910 4422 5483 267 -433 -1030 N ATOM 422 N ALA A 95 7.800 -28.734 6.779 1.00 24.35 N ANISOU 422 N ALA A 95 3110 2552 3590 165 -854 -242 N ATOM 423 CA ALA A 95 8.272 -28.310 5.465 1.00 26.10 C ANISOU 423 CA ALA A 95 3478 2697 3741 139 -948 -165 C ATOM 424 C ALA A 95 9.625 -28.933 5.159 1.00 30.25 C ANISOU 424 C ALA A 95 4034 3290 4170 21 -859 -47 C ATOM 425 O ALA A 95 9.855 -29.437 4.059 1.00 34.45 O ANISOU 425 O ALA A 95 4602 3845 4644 -15 -860 -12 O ATOM 426 CB ALA A 95 8.361 -26.796 5.393 1.00 22.89 C ANISOU 426 CB ALA A 95 3202 2196 3301 146 -1060 -153 C ATOM 427 N PHE A 96 10.518 -28.884 6.140 1.00 28.41 N ANISOU 427 N PHE A 96 3779 3103 3914 -36 -780 -4 N ATOM 428 CA PHE A 96 11.837 -29.482 6.010 1.00 25.09 C ANISOU 428 CA PHE A 96 3363 2761 3408 -136 -683 70 C ATOM 429 C PHE A 96 11.727 -30.980 5.774 1.00 23.01 C ANISOU 429 C PHE A 96 3004 2593 3147 -139 -586 39 C ATOM 430 O PHE A 96 12.352 -31.524 4.864 1.00 23.12 O ANISOU 430 O PHE A 96 3039 2643 3102 -186 -566 76 O ATOM 431 CB PHE A 96 12.663 -29.231 7.271 1.00 24.67 C ANISOU 431 CB PHE A 96 3280 2752 3340 -174 -605 78 C ATOM 432 CG PHE A 96 13.940 -30.014 7.317 1.00 22.89 C ANISOU 432 CG PHE A 96 3026 2619 3051 -241 -498 110 C ATOM 433 CD1 PHE A 96 15.086 -29.515 6.731 1.00 23.45 C ANISOU 433 CD1 PHE A 96 3164 2700 3044 -319 -501 168 C ATOM 434 CD2 PHE A 96 13.993 -31.254 7.937 1.00 22.52 C ANISOU 434 CD2 PHE A 96 2891 2646 3019 -224 -402 72 C ATOM 435 CE1 PHE A 96 16.257 -30.229 6.764 1.00 22.57 C ANISOU 435 CE1 PHE A 96 3006 2678 2892 -362 -413 169 C ATOM 436 CE2 PHE A 96 15.167 -31.978 7.967 1.00 21.32 C ANISOU 436 CE2 PHE A 96 2717 2561 2822 -257 -334 86 C ATOM 437 CZ PHE A 96 16.301 -31.464 7.382 1.00 20.87 C ANISOU 437 CZ PHE A 96 2700 2520 2708 -318 -339 126 C ATOM 438 N GLY A 97 10.939 -31.637 6.620 1.00 24.23 N ANISOU 438 N GLY A 97 3061 2786 3358 -99 -527 -33 N ATOM 439 CA GLY A 97 10.766 -33.076 6.566 1.00 24.18 C ANISOU 439 CA GLY A 97 2985 2855 3348 -110 -439 -62 C ATOM 440 C GLY A 97 10.330 -33.578 5.205 1.00 24.14 C ANISOU 440 C GLY A 97 2981 2856 3335 -98 -478 -75 C ATOM 441 O GLY A 97 10.872 -34.557 4.697 1.00 24.31 O ANISOU 441 O GLY A 97 2991 2930 3316 -132 -426 -62 O ATOM 442 N PHE A 98 9.357 -32.904 4.603 1.00 23.83 N ANISOU 442 N PHE A 98 2959 2763 3333 -39 -579 -113 N ATOM 443 CA PHE A 98 8.870 -33.326 3.297 1.00 25.40 C ANISOU 443 CA PHE A 98 3163 2973 3513 -20 -627 -134 C ATOM 444 C PHE A 98 9.875 -33.022 2.194 1.00 23.29 C ANISOU 444 C PHE A 98 3001 2694 3154 -72 -671 -52 C ATOM 445 O PHE A 98 10.139 -33.866 1.343 1.00 21.93 O ANISOU 445 O PHE A 98 2817 2580 2935 -100 -645 -51 O ATOM 446 CB PHE A 98 7.520 -32.686 2.966 1.00 26.75 C ANISOU 446 CB PHE A 98 3327 3092 3744 73 -733 -214 C ATOM 447 CG PHE A 98 6.888 -33.239 1.723 1.00 28.06 C ANISOU 447 CG PHE A 98 3481 3287 3892 101 -777 -252 C ATOM 448 CD1 PHE A 98 6.097 -34.374 1.781 1.00 29.05 C ANISOU 448 CD1 PHE A 98 3495 3479 4062 104 -712 -331 C ATOM 449 CD2 PHE A 98 7.098 -32.637 0.494 1.00 28.29 C ANISOU 449 CD2 PHE A 98 3625 3275 3850 113 -883 -207 C ATOM 450 CE1 PHE A 98 5.521 -34.893 0.639 1.00 28.51 C ANISOU 450 CE1 PHE A 98 3412 3440 3979 127 -757 -373 C ATOM 451 CE2 PHE A 98 6.525 -33.154 -0.651 1.00 28.80 C ANISOU 451 CE2 PHE A 98 3679 3376 3887 142 -928 -245 C ATOM 452 CZ PHE A 98 5.734 -34.281 -0.578 1.00 27.78 C ANISOU 452 CZ PHE A 98 3422 3319 3815 152 -868 -332 C ATOM 453 N SER A 99 10.428 -31.813 2.218 1.00 23.49 N ANISOU 453 N SER A 99 3137 2641 3146 -95 -737 12 N ATOM 454 CA SER A 99 11.352 -31.360 1.183 1.00 26.65 C ANISOU 454 CA SER A 99 3668 3017 3440 -173 -777 95 C ATOM 455 C SER A 99 12.573 -32.264 1.044 1.00 25.51 C ANISOU 455 C SER A 99 3484 2972 3236 -263 -669 128 C ATOM 456 O SER A 99 12.988 -32.590 -0.068 1.00 25.65 O ANISOU 456 O SER A 99 3546 3028 3172 -313 -671 149 O ATOM 457 CB SER A 99 11.797 -29.921 1.457 1.00 29.93 C ANISOU 457 CB SER A 99 4223 3319 3831 -216 -848 156 C ATOM 458 OG SER A 99 12.760 -29.497 0.508 1.00 32.82 O ANISOU 458 OG SER A 99 4727 3668 4076 -335 -859 233 O ATOM 459 N HIS A 100 13.143 -32.669 2.173 1.00 23.74 N ANISOU 459 N HIS A 100 3177 2795 3047 -274 -574 121 N ATOM 460 CA HIS A 100 14.330 -33.515 2.156 1.00 22.77 C ANISOU 460 CA HIS A 100 3008 2761 2882 -332 -477 129 C ATOM 461 C HIS A 100 14.001 -34.950 1.746 1.00 21.57 C ANISOU 461 C HIS A 100 2771 2671 2755 -296 -431 64 C ATOM 462 O HIS A 100 14.651 -35.510 0.865 1.00 22.85 O ANISOU 462 O HIS A 100 2935 2886 2861 -340 -413 63 O ATOM 463 CB HIS A 100 15.039 -33.492 3.512 1.00 20.17 C ANISOU 463 CB HIS A 100 2630 2456 2580 -328 -403 127 C ATOM 464 CG HIS A 100 16.430 -34.044 3.472 1.00 18.15 C ANISOU 464 CG HIS A 100 2339 2277 2278 -376 -330 127 C ATOM 465 ND1 HIS A 100 17.390 -33.579 2.599 1.00 16.13 N ANISOU 465 ND1 HIS A 100 2138 2059 1932 -474 -330 166 N ATOM 466 CD2 HIS A 100 17.023 -35.023 4.195 1.00 17.24 C ANISOU 466 CD2 HIS A 100 2148 2207 2194 -342 -263 85 C ATOM 467 CE1 HIS A 100 18.514 -34.246 2.786 1.00 14.82 C ANISOU 467 CE1 HIS A 100 1903 1973 1757 -487 -258 132 C ATOM 468 NE2 HIS A 100 18.319 -35.129 3.749 1.00 14.50 N ANISOU 468 NE2 HIS A 100 1789 1926 1795 -399 -231 87 N ATOM 469 N LEU A 101 12.992 -35.538 2.384 1.00 19.85 N ANISOU 469 N LEU A 101 2485 2449 2610 -232 -410 5 N ATOM 470 CA LEU A 101 12.570 -36.902 2.069 1.00 20.04 C ANISOU 470 CA LEU A 101 2443 2518 2653 -217 -367 -56 C ATOM 471 C LEU A 101 12.158 -37.049 0.607 1.00 20.49 C ANISOU 471 C LEU A 101 2519 2594 2672 -219 -429 -76 C ATOM 472 O LEU A 101 12.405 -38.081 -0.014 1.00 22.91 O ANISOU 472 O LEU A 101 2793 2950 2962 -235 -399 -113 O ATOM 473 CB LEU A 101 11.418 -37.340 2.976 1.00 20.33 C ANISOU 473 CB LEU A 101 2431 2541 2753 -184 -337 -98 C ATOM 474 CG LEU A 101 11.743 -37.636 4.440 1.00 22.25 C ANISOU 474 CG LEU A 101 2659 2780 3014 -190 -267 -89 C ATOM 475 CD1 LEU A 101 10.474 -37.997 5.193 1.00 25.09 C ANISOU 475 CD1 LEU A 101 2983 3121 3428 -175 -248 -129 C ATOM 476 CD2 LEU A 101 12.771 -38.750 4.554 1.00 21.98 C ANISOU 476 CD2 LEU A 101 2618 2774 2958 -213 -211 -83 C ATOM 477 N GLU A 102 11.526 -36.011 0.069 1.00 20.48 N ANISOU 477 N GLU A 102 2581 2545 2654 -196 -526 -56 N ATOM 478 CA GLU A 102 11.117 -35.990 -1.329 1.00 24.28 C ANISOU 478 CA GLU A 102 3108 3039 3078 -187 -603 -68 C ATOM 479 C GLU A 102 12.338 -35.952 -2.237 1.00 24.71 C ANISOU 479 C GLU A 102 3238 3128 3021 -265 -598 -17 C ATOM 480 O GLU A 102 12.354 -36.566 -3.303 1.00 28.81 O ANISOU 480 O GLU A 102 3762 3702 3483 -277 -608 -49 O ATOM 481 CB GLU A 102 10.231 -34.772 -1.598 1.00 27.91 C ANISOU 481 CB GLU A 102 3645 3418 3540 -129 -721 -54 C ATOM 482 CG GLU A 102 9.664 -34.682 -3.002 1.00 31.44 C ANISOU 482 CG GLU A 102 4153 3870 3921 -99 -814 -68 C ATOM 483 CD GLU A 102 8.831 -33.430 -3.205 1.00 35.99 C ANISOU 483 CD GLU A 102 4822 4347 4506 -23 -942 -61 C ATOM 484 OE1 GLU A 102 9.075 -32.433 -2.492 1.00 36.46 O ANISOU 484 OE1 GLU A 102 4945 4321 4586 -26 -964 -18 O ATOM 485 OE2 GLU A 102 7.928 -33.443 -4.068 1.00 39.22 O ANISOU 485 OE2 GLU A 102 5242 4756 4903 43 -1026 -106 O ATOM 486 N ALA A 103 13.363 -35.227 -1.803 1.00 21.69 N ANISOU 486 N ALA A 103 2916 2725 2602 -334 -573 55 N ATOM 487 CA ALA A 103 14.586 -35.087 -2.580 1.00 20.48 C ANISOU 487 CA ALA A 103 2835 2621 2327 -446 -542 104 C ATOM 488 C ALA A 103 15.397 -36.378 -2.573 1.00 23.86 C ANISOU 488 C ALA A 103 3156 3148 2763 -468 -446 48 C ATOM 489 O ALA A 103 16.092 -36.686 -3.541 1.00 25.75 O ANISOU 489 O ALA A 103 3419 3462 2903 -541 -415 41 O ATOM 490 CB ALA A 103 15.421 -33.932 -2.047 1.00 18.61 C ANISOU 490 CB ALA A 103 2679 2343 2050 -536 -531 184 C ATOM 491 N LEU A 104 15.299 -37.134 -1.483 1.00 22.07 N ANISOU 491 N LEU A 104 2822 2916 2649 -403 -396 3 N ATOM 492 CA LEU A 104 16.087 -38.353 -1.327 1.00 22.02 C ANISOU 492 CA LEU A 104 2730 2968 2668 -401 -322 -49 C ATOM 493 C LEU A 104 15.628 -39.490 -2.239 1.00 22.47 C ANISOU 493 C LEU A 104 2755 3053 2731 -376 -334 -121 C ATOM 494 O LEU A 104 16.300 -40.515 -2.345 1.00 19.45 O ANISOU 494 O LEU A 104 2318 2716 2356 -381 -285 -165 O ATOM 495 CB LEU A 104 16.105 -38.810 0.133 1.00 20.11 C ANISOU 495 CB LEU A 104 2423 2686 2531 -338 -280 -64 C ATOM 496 CG LEU A 104 16.791 -37.857 1.113 1.00 20.42 C ANISOU 496 CG LEU A 104 2482 2715 2563 -356 -258 -11 C ATOM 497 CD1 LEU A 104 17.030 -38.537 2.449 1.00 19.77 C ANISOU 497 CD1 LEU A 104 2346 2612 2554 -300 -218 -36 C ATOM 498 CD2 LEU A 104 18.092 -37.327 0.530 1.00 21.79 C ANISOU 498 CD2 LEU A 104 2678 2962 2639 -450 -231 16 C ATOM 499 N LEU A 105 14.489 -39.304 -2.897 1.00 23.02 N ANISOU 499 N LEU A 105 2853 3099 2793 -344 -404 -142 N ATOM 500 CA LEU A 105 14.033 -40.254 -3.905 1.00 24.37 C ANISOU 500 CA LEU A 105 3005 3298 2955 -325 -430 -216 C ATOM 501 C LEU A 105 14.994 -40.290 -5.091 1.00 27.04 C ANISOU 501 C LEU A 105 3396 3725 3153 -404 -406 -210 C ATOM 502 O LEU A 105 15.078 -41.290 -5.801 1.00 28.11 O ANISOU 502 O LEU A 105 3501 3905 3273 -404 -386 -279 O ATOM 503 CB LEU A 105 12.624 -39.897 -4.385 1.00 24.40 C ANISOU 503 CB LEU A 105 3013 3301 2955 -279 -500 -251 C ATOM 504 CG LEU A 105 11.474 -40.207 -3.426 1.00 23.80 C ANISOU 504 CG LEU A 105 2879 3197 2967 -268 -471 -251 C ATOM 505 CD1 LEU A 105 10.177 -39.598 -3.927 1.00 22.32 C ANISOU 505 CD1 LEU A 105 2714 2983 2786 -216 -561 -260 C ATOM 506 CD2 LEU A 105 11.324 -41.711 -3.249 1.00 24.89 C ANISOU 506 CD2 LEU A 105 2983 3304 3172 -281 -428 -272 C ATOM 507 N ASP A 106 15.721 -39.194 -5.294 1.00 28.88 N ANISOU 507 N ASP A 106 3709 3983 3279 -485 -393 -133 N ATOM 508 CA ASP A 106 16.622 -39.066 -6.437 1.00 30.39 C ANISOU 508 CA ASP A 106 3960 4271 3318 -588 -347 -130 C ATOM 509 C ASP A 106 18.101 -39.169 -6.062 1.00 30.04 C ANISOU 509 C ASP A 106 3850 4319 3244 -676 -232 -144 C ATOM 510 O ASP A 106 18.972 -38.922 -6.895 1.00 33.82 O ANISOU 510 O ASP A 106 4362 4893 3594 -787 -167 -151 O ATOM 511 CB ASP A 106 16.366 -37.746 -7.170 1.00 33.10 C ANISOU 511 CB ASP A 106 4465 4570 3541 -640 -409 -40 C ATOM 512 CG ASP A 106 15.037 -37.732 -7.899 1.00 37.39 C ANISOU 512 CG ASP A 106 5061 5064 4082 -543 -524 -58 C ATOM 513 OD1 ASP A 106 14.187 -38.600 -7.611 1.00 36.63 O ANISOU 513 OD1 ASP A 106 4862 4958 4098 -444 -557 -139 O ATOM 514 OD2 ASP A 106 14.841 -36.849 -8.760 1.00 41.61 O ANISOU 514 OD2 ASP A 106 5737 5569 4504 -568 -580 2 O ATOM 515 N ASP A 107 18.383 -39.530 -4.815 1.00 26.88 N ANISOU 515 N ASP A 107 3354 3897 2964 -622 -203 -157 N ATOM 516 CA ASP A 107 19.762 -39.688 -4.363 1.00 27.45 C ANISOU 516 CA ASP A 107 3341 4061 3029 -668 -110 -193 C ATOM 517 C ASP A 107 19.866 -40.816 -3.340 1.00 26.99 C ANISOU 517 C ASP A 107 3174 3970 3111 -548 -97 -249 C ATOM 518 O ASP A 107 19.689 -40.596 -2.143 1.00 26.94 O ANISOU 518 O ASP A 107 3164 3881 3193 -491 -119 -202 O ATOM 519 CB ASP A 107 20.286 -38.379 -3.765 1.00 29.00 C ANISOU 519 CB ASP A 107 3587 4241 3191 -747 -98 -112 C ATOM 520 CG ASP A 107 21.804 -38.315 -3.727 1.00 31.62 C ANISOU 520 CG ASP A 107 3844 4703 3467 -829 5 -167 C ATOM 521 OD1 ASP A 107 22.458 -39.380 -3.762 1.00 30.93 O ANISOU 521 OD1 ASP A 107 3639 4698 3415 -774 56 -272 O ATOM 522 OD2 ASP A 107 22.347 -37.192 -3.657 1.00 33.71 O ANISOU 522 OD2 ASP A 107 4172 4981 3654 -938 30 -118 O ATOM 523 N SER A 108 20.158 -42.021 -3.820 1.00 29.47 N ANISOU 523 N SER A 108 3415 4343 3437 -512 -66 -352 N ATOM 524 CA SER A 108 20.231 -43.204 -2.966 1.00 31.65 C ANISOU 524 CA SER A 108 3618 4574 3835 -404 -67 -407 C ATOM 525 C SER A 108 21.327 -43.091 -1.913 1.00 32.92 C ANISOU 525 C SER A 108 3720 4758 4032 -373 -41 -407 C ATOM 526 O SER A 108 21.141 -43.485 -0.763 1.00 34.40 O ANISOU 526 O SER A 108 3901 4860 4310 -297 -72 -384 O ATOM 527 CB SER A 108 20.466 -44.455 -3.814 1.00 33.34 C ANISOU 527 CB SER A 108 3769 4852 4046 -373 -42 -538 C ATOM 528 OG SER A 108 19.389 -44.684 -4.701 1.00 36.44 O ANISOU 528 OG SER A 108 4220 5210 4417 -383 -76 -544 O ATOM 529 N LYS A 109 22.469 -42.549 -2.321 1.00 34.65 N ANISOU 529 N LYS A 109 3900 5096 4168 -440 18 -441 N ATOM 530 CA LYS A 109 23.644 -42.473 -1.459 1.00 37.13 C ANISOU 530 CA LYS A 109 4150 5450 4509 -404 39 -470 C ATOM 531 C LYS A 109 23.492 -41.431 -0.350 1.00 35.92 C ANISOU 531 C LYS A 109 4055 5212 4381 -413 7 -360 C ATOM 532 O LYS A 109 24.034 -41.598 0.744 1.00 35.71 O ANISOU 532 O LYS A 109 3991 5165 4412 -345 -13 -365 O ATOM 533 CB LYS A 109 24.899 -42.221 -2.303 1.00 39.66 C ANISOU 533 CB LYS A 109 4407 5932 4730 -484 118 -567 C ATOM 534 CG LYS A 109 25.675 -40.958 -1.970 1.00 40.50 C ANISOU 534 CG LYS A 109 4535 6075 4778 -574 147 -528 C ATOM 535 CD LYS A 109 27.027 -41.309 -1.371 1.00 44.11 C ANISOU 535 CD LYS A 109 4885 6604 5271 -514 160 -632 C ATOM 536 CE LYS A 109 27.743 -42.357 -2.208 1.00 47.23 C ANISOU 536 CE LYS A 109 5181 7116 5650 -482 195 -795 C ATOM 537 NZ LYS A 109 28.673 -43.179 -1.382 1.00 48.71 N ANISOU 537 NZ LYS A 109 5267 7318 5923 -345 155 -894 N ATOM 538 N GLU A 110 22.753 -40.363 -0.636 1.00 34.24 N ANISOU 538 N GLU A 110 3937 4953 4121 -492 -6 -270 N ATOM 539 CA GLU A 110 22.466 -39.347 0.370 1.00 35.79 C ANISOU 539 CA GLU A 110 4191 5061 4347 -491 -40 -181 C ATOM 540 C GLU A 110 21.414 -39.872 1.337 1.00 34.39 C ANISOU 540 C GLU A 110 4032 4759 4274 -393 -97 -145 C ATOM 541 O GLU A 110 21.403 -39.528 2.519 1.00 35.63 O ANISOU 541 O GLU A 110 4198 4859 4480 -356 -118 -111 O ATOM 542 CB GLU A 110 21.977 -38.059 -0.295 1.00 39.59 C ANISOU 542 CB GLU A 110 4775 5526 4741 -598 -48 -109 C ATOM 543 CG GLU A 110 21.713 -36.910 0.665 1.00 44.83 C ANISOU 543 CG GLU A 110 5500 6104 5430 -596 -82 -36 C ATOM 544 CD GLU A 110 22.977 -36.383 1.323 1.00 52.49 C ANISOU 544 CD GLU A 110 6430 7126 6388 -625 -43 -61 C ATOM 545 OE1 GLU A 110 24.087 -36.709 0.849 1.00 56.14 O ANISOU 545 OE1 GLU A 110 6826 7702 6803 -668 13 -133 O ATOM 546 OE2 GLU A 110 22.860 -35.636 2.318 1.00 53.64 O ANISOU 546 OE2 GLU A 110 6603 7206 6572 -603 -69 -23 O ATOM 547 N LEU A 111 20.525 -40.710 0.818 1.00 32.43 N ANISOU 547 N LEU A 111 3789 4479 4052 -363 -117 -164 N ATOM 548 CA LEU A 111 19.510 -41.356 1.632 1.00 30.60 C ANISOU 548 CA LEU A 111 3570 4145 3912 -297 -155 -147 C ATOM 549 C LEU A 111 20.149 -42.274 2.668 1.00 30.49 C ANISOU 549 C LEU A 111 3502 4136 3946 -238 -154 -176 C ATOM 550 O LEU A 111 19.729 -42.308 3.825 1.00 26.87 O ANISOU 550 O LEU A 111 3062 3615 3534 -213 -176 -139 O ATOM 551 CB LEU A 111 18.570 -42.167 0.745 1.00 29.53 C ANISOU 551 CB LEU A 111 3442 3991 3788 -291 -168 -184 C ATOM 552 CG LEU A 111 17.703 -43.189 1.476 1.00 30.60 C ANISOU 552 CG LEU A 111 3575 4046 4005 -247 -178 -197 C ATOM 553 CD1 LEU A 111 16.432 -42.545 2.005 1.00 28.83 C ANISOU 553 CD1 LEU A 111 3403 3750 3800 -258 -203 -133 C ATOM 554 CD2 LEU A 111 17.393 -44.349 0.555 1.00 34.35 C ANISOU 554 CD2 LEU A 111 4029 4528 4496 -232 -169 -285 C ATOM 555 N GLN A 112 21.169 -43.013 2.243 1.00 33.11 N ANISOU 555 N GLN A 112 3764 4553 4264 -210 -132 -259 N ATOM 556 CA GLN A 112 21.832 -43.977 3.114 1.00 33.78 C ANISOU 556 CA GLN A 112 3792 4642 4402 -115 -156 -315 C ATOM 557 C GLN A 112 22.490 -43.334 4.331 1.00 33.85 C ANISOU 557 C GLN A 112 3798 4656 4407 -98 -176 -271 C ATOM 558 O GLN A 112 22.444 -43.887 5.428 1.00 35.15 O ANISOU 558 O GLN A 112 3966 4772 4618 -19 -225 -269 O ATOM 559 CB GLN A 112 22.857 -44.802 2.331 1.00 36.49 C ANISOU 559 CB GLN A 112 4051 5078 4736 -65 -136 -435 C ATOM 560 CG GLN A 112 22.240 -45.739 1.311 1.00 38.05 C ANISOU 560 CG GLN A 112 4239 5262 4955 -55 -130 -507 C ATOM 561 CD GLN A 112 21.287 -46.736 1.939 1.00 39.66 C ANISOU 561 CD GLN A 112 4528 5301 5239 16 -160 -478 C ATOM 562 OE1 GLN A 112 21.489 -47.178 3.070 1.00 42.48 O ANISOU 562 OE1 GLN A 112 4924 5577 5638 98 -193 -450 O ATOM 563 NE2 GLN A 112 20.236 -47.091 1.209 1.00 37.94 N ANISOU 563 NE2 GLN A 112 4354 5028 5033 -25 -146 -487 N ATOM 564 N ARG A 113 23.105 -42.172 4.146 1.00 34.56 N ANISOU 564 N ARG A 113 3891 4796 4444 -167 -147 -245 N ATOM 565 CA ARG A 113 23.731 -41.501 5.276 1.00 39.18 C ANISOU 565 CA ARG A 113 4473 5385 5030 -159 -167 -218 C ATOM 566 C ARG A 113 22.705 -40.765 6.135 1.00 36.50 C ANISOU 566 C ARG A 113 4211 4946 4712 -183 -191 -129 C ATOM 567 O ARG A 113 22.879 -40.648 7.346 1.00 40.05 O ANISOU 567 O ARG A 113 4664 5381 5175 -152 -225 -111 O ATOM 568 CB ARG A 113 24.869 -40.576 4.834 1.00 44.89 C ANISOU 568 CB ARG A 113 5159 6199 5699 -224 -123 -253 C ATOM 569 CG ARG A 113 24.489 -39.554 3.788 1.00 50.96 C ANISOU 569 CG ARG A 113 5982 6971 6408 -331 -79 -218 C ATOM 570 CD ARG A 113 25.450 -38.381 3.821 1.00 57.32 C ANISOU 570 CD ARG A 113 6778 7840 7162 -411 -44 -229 C ATOM 571 NE ARG A 113 25.583 -37.847 5.175 1.00 61.20 N ANISOU 571 NE ARG A 113 7278 8282 7694 -382 -82 -198 N ATOM 572 CZ ARG A 113 24.746 -36.972 5.722 1.00 62.67 C ANISOU 572 CZ ARG A 113 7543 8375 7894 -397 -105 -126 C ATOM 573 NH1 ARG A 113 23.705 -36.520 5.034 1.00 62.57 N ANISOU 573 NH1 ARG A 113 7608 8305 7859 -432 -102 -75 N ATOM 574 NH2 ARG A 113 24.949 -36.550 6.960 1.00 63.64 N ANISOU 574 NH2 ARG A 113 7663 8470 8046 -371 -135 -117 N ATOM 575 N PHE A 114 21.633 -40.280 5.514 1.00 30.30 N ANISOU 575 N PHE A 114 3486 4101 3927 -227 -178 -93 N ATOM 576 CA PHE A 114 20.521 -39.708 6.268 1.00 24.86 C ANISOU 576 CA PHE A 114 2856 3327 3263 -223 -186 -58 C ATOM 577 C PHE A 114 19.872 -40.802 7.107 1.00 22.86 C ANISOU 577 C PHE A 114 2598 3050 3039 -188 -201 -61 C ATOM 578 O PHE A 114 19.515 -40.583 8.264 1.00 24.29 O ANISOU 578 O PHE A 114 2814 3190 3224 -183 -213 -19 O ATOM 579 CB PHE A 114 19.488 -39.072 5.333 1.00 23.38 C ANISOU 579 CB PHE A 114 2720 3106 3058 -252 -172 -42 C ATOM 580 CG PHE A 114 18.336 -38.418 6.051 1.00 20.83 C ANISOU 580 CG PHE A 114 2446 2727 2743 -242 -170 -19 C ATOM 581 CD1 PHE A 114 18.524 -37.249 6.769 1.00 21.69 C ANISOU 581 CD1 PHE A 114 2582 2826 2833 -254 -174 9 C ATOM 582 CD2 PHE A 114 17.066 -38.967 5.999 1.00 19.01 C ANISOU 582 CD2 PHE A 114 2227 2461 2537 -227 -165 -29 C ATOM 583 CE1 PHE A 114 17.467 -36.643 7.430 1.00 22.69 C ANISOU 583 CE1 PHE A 114 2742 2906 2973 -240 -181 24 C ATOM 584 CE2 PHE A 114 16.005 -38.365 6.657 1.00 19.63 C ANISOU 584 CE2 PHE A 114 2333 2499 2625 -218 -165 -17 C ATOM 585 CZ PHE A 114 16.206 -37.203 7.372 1.00 20.24 C ANISOU 585 CZ PHE A 114 2433 2566 2692 -220 -176 8 C ATOM 586 N LYS A 115 19.732 -41.984 6.515 1.00 20.52 N ANISOU 586 N LYS A 115 2277 2749 2770 -171 -213 -80 N ATOM 587 CA LYS A 115 19.191 -43.141 7.216 1.00 22.69 C ANISOU 587 CA LYS A 115 2605 2920 3095 -109 -213 -77 C ATOM 588 C LYS A 115 20.104 -43.578 8.358 1.00 25.36 C ANISOU 588 C LYS A 115 2964 3251 3419 -24 -245 -68 C ATOM 589 O LYS A 115 19.633 -43.958 9.429 1.00 27.15 O ANISOU 589 O LYS A 115 3281 3387 3649 0 -244 -23 O ATOM 590 CB LYS A 115 18.985 -44.302 6.243 1.00 25.23 C ANISOU 590 CB LYS A 115 2924 3216 3446 -82 -197 -132 C ATOM 591 CG LYS A 115 18.499 -45.585 6.897 1.00 29.36 C ANISOU 591 CG LYS A 115 3535 3612 4011 -30 -186 -126 C ATOM 592 CD LYS A 115 18.462 -46.726 5.898 1.00 32.87 C ANISOU 592 CD LYS A 115 3975 4028 4487 0 -177 -196 C ATOM 593 CE LYS A 115 18.115 -48.040 6.573 1.00 36.71 C ANISOU 593 CE LYS A 115 4575 4363 5010 46 -169 -187 C ATOM 594 NZ LYS A 115 18.145 -49.173 5.608 1.00 39.59 N ANISOU 594 NZ LYS A 115 4941 4688 5412 81 -165 -268 N ATOM 595 N ALA A 116 21.411 -43.521 8.125 1.00 26.96 N ANISOU 595 N ALA A 116 3086 3556 3600 18 -275 -119 N ATOM 596 CA ALA A 116 22.386 -43.930 9.131 1.00 25.99 C ANISOU 596 CA ALA A 116 2966 3444 3464 123 -334 -133 C ATOM 597 C ALA A 116 22.413 -42.960 10.308 1.00 25.79 C ANISOU 597 C ALA A 116 2967 3427 3404 95 -354 -80 C ATOM 598 O ALA A 116 22.496 -43.375 11.464 1.00 28.58 O ANISOU 598 O ALA A 116 3402 3722 3737 168 -396 -47 O ATOM 599 CB ALA A 116 23.771 -44.059 8.511 1.00 24.99 C ANISOU 599 CB ALA A 116 2708 3452 3334 174 -360 -236 C ATOM 600 N VAL A 117 22.344 -41.668 10.005 1.00 23.24 N ANISOU 600 N VAL A 117 2592 3170 3068 -11 -329 -73 N ATOM 601 CA VAL A 117 22.316 -40.639 11.039 1.00 23.18 C ANISOU 601 CA VAL A 117 2607 3169 3033 -49 -346 -36 C ATOM 602 C VAL A 117 21.030 -40.733 11.856 1.00 23.91 C ANISOU 602 C VAL A 117 2814 3142 3129 -59 -321 30 C ATOM 603 O VAL A 117 21.052 -40.635 13.083 1.00 25.77 O ANISOU 603 O VAL A 117 3108 3354 3331 -31 -343 57 O ATOM 604 CB VAL A 117 22.444 -39.225 10.429 1.00 21.52 C ANISOU 604 CB VAL A 117 2393 2964 2821 -133 -288 -54 C ATOM 605 CG1 VAL A 117 22.115 -38.159 11.462 1.00 19.99 C ANISOU 605 CG1 VAL A 117 2243 2749 2601 -160 -280 -31 C ATOM 606 CG2 VAL A 117 23.841 -39.013 9.869 1.00 21.49 C ANISOU 606 CG2 VAL A 117 2328 3031 2808 -148 -281 -85 C ATOM 607 N SER A 118 19.914 -40.942 11.166 1.00 22.36 N ANISOU 607 N SER A 118 2643 2884 2970 -103 -274 43 N ATOM 608 CA SER A 118 18.605 -40.997 11.806 1.00 19.81 C ANISOU 608 CA SER A 118 2396 2469 2661 -133 -233 77 C ATOM 609 C SER A 118 18.431 -42.236 12.676 1.00 22.92 C ANISOU 609 C SER A 118 2894 2776 3037 -80 -220 104 C ATOM 610 O SER A 118 17.745 -42.193 13.697 1.00 25.47 O ANISOU 610 O SER A 118 3296 3046 3337 -107 -185 134 O ATOM 611 CB SER A 118 17.498 -40.946 10.753 1.00 16.58 C ANISOU 611 CB SER A 118 1964 2032 2302 -188 -197 58 C ATOM 612 OG SER A 118 17.551 -39.740 10.011 1.00 15.44 O ANISOU 612 OG SER A 118 1791 1946 2131 -207 -191 41 O ATOM 613 N ALA A 119 19.047 -43.340 12.266 1.00 23.29 N ANISOU 613 N ALA A 119 2954 2804 3091 -8 -245 88 N ATOM 614 CA ALA A 119 18.949 -44.590 13.013 1.00 28.05 C ANISOU 614 CA ALA A 119 3691 3295 3671 49 -246 121 C ATOM 615 C ALA A 119 19.706 -44.498 14.333 1.00 31.24 C ANISOU 615 C ALA A 119 4168 3703 3999 118 -307 158 C ATOM 616 O ALA A 119 19.231 -44.966 15.368 1.00 34.43 O ANISOU 616 O ALA A 119 4720 4013 4350 113 -286 214 O ATOM 617 CB ALA A 119 19.469 -45.752 12.180 1.00 28.88 C ANISOU 617 CB ALA A 119 3795 3368 3811 127 -274 82 C ATOM 618 N LYS A 120 20.885 -43.888 14.284 1.00 30.14 N ANISOU 618 N LYS A 120 3927 3678 3845 173 -380 120 N ATOM 619 CA LYS A 120 21.725 -43.726 15.464 1.00 32.43 C ANISOU 619 CA LYS A 120 4260 3999 4064 251 -461 133 C ATOM 620 C LYS A 120 21.146 -42.681 16.415 1.00 30.95 C ANISOU 620 C LYS A 120 4107 3824 3830 167 -426 168 C ATOM 621 O LYS A 120 21.414 -42.703 17.616 1.00 32.64 O ANISOU 621 O LYS A 120 4415 4025 3962 211 -471 198 O ATOM 622 CB LYS A 120 23.144 -43.321 15.048 1.00 38.39 C ANISOU 622 CB LYS A 120 4860 4896 4831 316 -541 50 C ATOM 623 CG LYS A 120 24.140 -43.235 16.198 1.00 46.38 C ANISOU 623 CG LYS A 120 5888 5955 5779 400 -622 35 C ATOM 624 CD LYS A 120 25.521 -42.803 15.725 1.00 52.68 C ANISOU 624 CD LYS A 120 6514 6894 6608 406 -632 -63 C ATOM 625 CE LYS A 120 25.523 -41.366 15.225 1.00 56.96 C ANISOU 625 CE LYS A 120 6944 7527 7171 263 -569 -81 C ATOM 626 NZ LYS A 120 26.890 -40.932 14.820 1.00 60.99 N ANISOU 626 NZ LYS A 120 7328 8144 7702 246 -562 -166 N ATOM 627 N SER A 121 20.339 -41.777 15.869 1.00 26.97 N ANISOU 627 N SER A 121 3533 3342 3373 55 -353 157 N ATOM 628 CA SER A 121 19.859 -40.618 16.617 1.00 23.76 C ANISOU 628 CA SER A 121 3128 2959 2940 -17 -327 163 C ATOM 629 C SER A 121 19.032 -40.955 17.861 1.00 21.07 C ANISOU 629 C SER A 121 2932 2541 2533 -38 -280 208 C ATOM 630 O SER A 121 19.025 -40.187 18.824 1.00 20.67 O ANISOU 630 O SER A 121 2905 2523 2427 -59 -285 206 O ATOM 631 CB SER A 121 19.091 -39.659 15.698 1.00 22.98 C ANISOU 631 CB SER A 121 2942 2878 2912 -109 -277 137 C ATOM 632 OG SER A 121 17.984 -40.294 15.083 1.00 22.89 O ANISOU 632 OG SER A 121 2952 2797 2950 -143 -212 141 O ATOM 633 N LYS A 122 18.345 -42.094 17.849 1.00 21.30 N ANISOU 633 N LYS A 122 3063 2468 2560 -46 -225 243 N ATOM 634 CA LYS A 122 17.529 -42.487 18.998 1.00 27.27 C ANISOU 634 CA LYS A 122 3974 3149 3239 -97 -155 285 C ATOM 635 C LYS A 122 18.366 -42.739 20.249 1.00 31.66 C ANISOU 635 C LYS A 122 4664 3698 3668 -18 -232 332 C ATOM 636 O LYS A 122 18.157 -42.101 21.279 1.00 32.31 O ANISOU 636 O LYS A 122 4793 3810 3672 -56 -212 335 O ATOM 637 CB LYS A 122 16.677 -43.719 18.691 1.00 28.36 C ANISOU 637 CB LYS A 122 4208 3169 3399 -143 -74 309 C ATOM 638 CG LYS A 122 15.885 -44.203 19.899 1.00 29.82 C ANISOU 638 CG LYS A 122 4561 3280 3490 -220 18 348 C ATOM 639 CD LYS A 122 14.873 -45.273 19.530 1.00 31.97 C ANISOU 639 CD LYS A 122 4848 3486 3815 -289 116 325 C ATOM 640 CE LYS A 122 15.551 -46.539 19.038 1.00 32.05 C ANISOU 640 CE LYS A 122 4927 3414 3836 -202 52 356 C ATOM 641 NZ LYS A 122 14.563 -47.627 18.799 1.00 31.45 N ANISOU 641 NZ LYS A 122 4887 3268 3795 -280 142 337 N ATOM 642 N GLU A 123 19.308 -43.673 20.154 1.00 34.88 N ANISOU 642 N GLU A 123 5133 4067 4052 101 -329 357 N ATOM 643 CA GLU A 123 20.201 -43.975 21.268 1.00 41.01 C ANISOU 643 CA GLU A 123 5995 4856 4732 198 -415 373 C ATOM 644 C GLU A 123 21.045 -42.750 21.615 1.00 41.19 C ANISOU 644 C GLU A 123 5897 5016 4735 229 -495 323 C ATOM 645 O GLU A 123 21.481 -42.581 22.754 1.00 41.59 O ANISOU 645 O GLU A 123 6000 5097 4704 261 -533 324 O ATOM 646 CB GLU A 123 21.094 -45.175 20.931 1.00 46.01 C ANISOU 646 CB GLU A 123 6647 5445 5390 324 -496 363 C ATOM 647 CG GLU A 123 22.027 -45.595 22.058 1.00 53.11 C ANISOU 647 CG GLU A 123 7628 6347 6205 426 -590 366 C ATOM 648 CD GLU A 123 21.285 -45.903 23.345 1.00 58.08 C ANISOU 648 CD GLU A 123 8451 6895 6721 361 -531 431 C ATOM 649 OE1 GLU A 123 20.287 -46.654 23.293 1.00 59.26 O ANISOU 649 OE1 GLU A 123 8717 6935 6865 278 -432 473 O ATOM 650 OE2 GLU A 123 21.694 -45.389 24.408 1.00 59.08 O ANISOU 650 OE2 GLU A 123 8607 7076 6765 383 -576 431 O ATOM 651 N ASP A 124 21.260 -41.893 20.620 1.00 39.85 N ANISOU 651 N ASP A 124 5556 4934 4652 203 -508 269 N ATOM 652 CA ASP A 124 22.014 -40.658 20.799 1.00 40.96 C ANISOU 652 CA ASP A 124 5564 5205 4795 198 -565 205 C ATOM 653 C ASP A 124 21.276 -39.683 21.714 1.00 36.50 C ANISOU 653 C ASP A 124 5040 4649 4177 105 -504 207 C ATOM 654 O ASP A 124 21.888 -39.029 22.561 1.00 35.97 O ANISOU 654 O ASP A 124 4964 4654 4049 126 -565 176 O ATOM 655 CB ASP A 124 22.271 -40.000 19.444 1.00 46.78 C ANISOU 655 CB ASP A 124 6111 6014 5648 149 -545 144 C ATOM 656 CG ASP A 124 23.192 -38.801 19.541 1.00 51.31 C ANISOU 656 CG ASP A 124 6550 6713 6230 124 -585 72 C ATOM 657 OD1 ASP A 124 24.418 -38.983 19.383 1.00 53.33 O ANISOU 657 OD1 ASP A 124 6716 7043 6505 174 -620 26 O ATOM 658 OD2 ASP A 124 22.697 -37.674 19.763 1.00 52.93 O ANISOU 658 OD2 ASP A 124 6742 6931 6439 33 -556 61 O ATOM 659 N LEU A 125 19.962 -39.579 21.533 1.00 33.39 N ANISOU 659 N LEU A 125 4674 4194 3819 4 -382 224 N ATOM 660 CA LEU A 125 19.135 -38.750 22.404 1.00 30.65 C ANISOU 660 CA LEU A 125 4363 3855 3428 -79 -312 207 C ATOM 661 C LEU A 125 19.059 -39.352 23.802 1.00 35.07 C ANISOU 661 C LEU A 125 5113 4378 3834 -61 -310 257 C ATOM 662 O LEU A 125 19.072 -38.633 24.802 1.00 36.79 O ANISOU 662 O LEU A 125 5364 4645 3969 -82 -315 231 O ATOM 663 CB LEU A 125 17.724 -38.606 21.831 1.00 26.02 C ANISOU 663 CB LEU A 125 3740 3221 2925 -178 -186 188 C ATOM 664 CG LEU A 125 17.544 -37.707 20.608 1.00 24.69 C ANISOU 664 CG LEU A 125 3412 3083 2887 -209 -188 137 C ATOM 665 CD1 LEU A 125 16.141 -37.844 20.031 1.00 25.04 C ANISOU 665 CD1 LEU A 125 3430 3077 3009 -277 -88 114 C ATOM 666 CD2 LEU A 125 17.830 -36.261 20.977 1.00 25.05 C ANISOU 666 CD2 LEU A 125 3394 3190 2935 -230 -225 82 C ATOM 667 N VAL A 126 18.978 -40.677 23.861 1.00 37.11 N ANISOU 667 N VAL A 126 5515 4542 4045 -26 -303 328 N ATOM 668 CA VAL A 126 18.865 -41.395 25.125 1.00 39.06 C ANISOU 668 CA VAL A 126 5928 4736 4176 -17 -280 371 C ATOM 669 C VAL A 126 20.083 -41.176 26.017 1.00 42.16 C ANISOU 669 C VAL A 126 6318 5199 4501 89 -406 356 C ATOM 670 O VAL A 126 19.950 -40.944 27.219 1.00 44.77 O ANISOU 670 O VAL A 126 6738 5546 4726 67 -391 360 O ATOM 671 CB VAL A 126 18.672 -42.905 24.889 1.00 39.73 C ANISOU 671 CB VAL A 126 6119 4700 4276 4 -254 423 C ATOM 672 CG1 VAL A 126 18.694 -43.667 26.207 1.00 41.12 C ANISOU 672 CG1 VAL A 126 6476 4818 4331 14 -252 467 C ATOM 673 CG2 VAL A 126 17.377 -43.153 24.148 1.00 38.14 C ANISOU 673 CG2 VAL A 126 5905 4439 4147 -120 -112 419 C ATOM 674 N SER A 127 21.269 -41.240 25.421 1.00 42.89 N ANISOU 674 N SER A 127 6294 5342 4658 196 -522 325 N ATOM 675 CA SER A 127 22.509 -41.095 26.174 1.00 46.62 C ANISOU 675 CA SER A 127 6735 5891 5089 293 -638 292 C ATOM 676 C SER A 127 22.650 -39.707 26.794 1.00 48.44 C ANISOU 676 C SER A 127 6887 6234 5286 245 -648 233 C ATOM 677 O SER A 127 23.361 -39.534 27.784 1.00 50.49 O ANISOU 677 O SER A 127 7164 6545 5474 293 -718 214 O ATOM 678 CB SER A 127 23.719 -41.403 25.288 1.00 48.27 C ANISOU 678 CB SER A 127 6801 6146 5394 393 -732 242 C ATOM 679 OG SER A 127 23.816 -40.480 24.217 1.00 49.31 O ANISOU 679 OG SER A 127 6749 6360 5626 339 -713 184 O ATOM 680 N GLN A 128 21.971 -38.721 26.216 1.00 48.11 N ANISOU 680 N GLN A 128 6765 6221 5294 151 -585 198 N ATOM 681 CA GLN A 128 22.057 -37.357 26.727 1.00 48.31 C ANISOU 681 CA GLN A 128 6718 6337 5301 99 -592 127 C ATOM 682 C GLN A 128 20.823 -36.929 27.522 1.00 48.36 C ANISOU 682 C GLN A 128 6843 6312 5221 4 -492 130 C ATOM 683 O GLN A 128 20.502 -35.742 27.589 1.00 49.01 O ANISOU 683 O GLN A 128 6862 6440 5319 -66 -470 59 O ATOM 684 CB GLN A 128 22.350 -36.361 25.601 1.00 47.65 C ANISOU 684 CB GLN A 128 6451 6311 5343 55 -606 58 C ATOM 685 CG GLN A 128 21.331 -36.343 24.480 1.00 47.40 C ANISOU 685 CG GLN A 128 6404 6209 5395 -21 -530 78 C ATOM 686 CD GLN A 128 21.595 -35.234 23.480 1.00 48.59 C ANISOU 686 CD GLN A 128 6385 6405 5671 -79 -531 14 C ATOM 687 OE1 GLN A 128 21.599 -35.461 22.270 1.00 48.61 O ANISOU 687 OE1 GLN A 128 6311 6390 5768 -90 -512 25 O ATOM 688 NE2 GLN A 128 21.814 -34.025 23.984 1.00 49.02 N ANISOU 688 NE2 GLN A 128 6396 6510 5720 -124 -551 -53 N ATOM 689 N GLY A 129 20.135 -37.896 28.122 1.00 46.52 N ANISOU 689 N GLY A 129 6773 5998 4904 -12 -419 201 N ATOM 690 CA GLY A 129 19.082 -37.587 29.074 1.00 44.13 C ANISOU 690 CA GLY A 129 6573 5687 4507 -109 -303 190 C ATOM 691 C GLY A 129 17.662 -37.958 28.690 1.00 41.04 C ANISOU 691 C GLY A 129 6233 5223 4139 -227 -141 205 C ATOM 692 O GLY A 129 16.777 -37.975 29.544 1.00 43.14 O ANISOU 692 O GLY A 129 6580 5481 4331 -312 -24 191 O ATOM 693 N PHE A 130 17.431 -38.251 27.415 1.00 36.82 N ANISOU 693 N PHE A 130 5633 4645 3711 -240 -126 221 N ATOM 694 CA PHE A 130 16.083 -38.577 26.958 1.00 35.71 C ANISOU 694 CA PHE A 130 5479 4449 3641 -350 34 208 C ATOM 695 C PHE A 130 15.688 -40.008 27.311 1.00 38.95 C ANISOU 695 C PHE A 130 6042 4759 4000 -372 99 283 C ATOM 696 O PHE A 130 16.534 -40.898 27.388 1.00 39.38 O ANISOU 696 O PHE A 130 6169 4762 4031 -274 2 349 O ATOM 697 CB PHE A 130 15.942 -38.339 25.453 1.00 32.56 C ANISOU 697 CB PHE A 130 4892 4043 3436 -339 23 175 C ATOM 698 CG PHE A 130 15.927 -36.887 25.068 1.00 31.81 C ANISOU 698 CG PHE A 130 4624 4019 3445 -343 -5 82 C ATOM 699 CD1 PHE A 130 17.111 -36.189 24.893 1.00 30.46 C ANISOU 699 CD1 PHE A 130 4381 3901 3289 -274 -134 69 C ATOM 700 CD2 PHE A 130 14.727 -36.219 24.876 1.00 32.32 C ANISOU 700 CD2 PHE A 130 4599 4089 3592 -416 93 -4 C ATOM 701 CE1 PHE A 130 17.099 -34.853 24.538 1.00 28.82 C ANISOU 701 CE1 PHE A 130 4047 3732 3170 -293 -157 -9 C ATOM 702 CE2 PHE A 130 14.710 -34.882 24.520 1.00 30.66 C ANISOU 702 CE2 PHE A 130 4261 3916 3475 -406 50 -85 C ATOM 703 CZ PHE A 130 15.897 -34.199 24.351 1.00 28.91 C ANISOU 703 CZ PHE A 130 4000 3726 3260 -352 -72 -78 C ATOM 704 N THR A 131 14.395 -40.217 27.532 1.00 40.19 N ANISOU 704 N THR A 131 6213 4890 4166 -498 259 246 N ATOM 705 CA THR A 131 13.877 -41.543 27.836 1.00 42.19 C ANISOU 705 CA THR A 131 6588 5048 4396 -543 328 290 C ATOM 706 C THR A 131 13.556 -42.275 26.541 1.00 41.17 C ANISOU 706 C THR A 131 6392 4855 4396 -548 347 295 C ATOM 707 O THR A 131 12.707 -41.831 25.767 1.00 38.79 O ANISOU 707 O THR A 131 5951 4584 4204 -617 426 222 O ATOM 708 CB THR A 131 12.612 -41.468 28.710 1.00 44.37 C ANISOU 708 CB THR A 131 6894 5340 4625 -687 490 224 C ATOM 709 OG1 THR A 131 12.915 -40.784 29.932 1.00 45.43 O ANISOU 709 OG1 THR A 131 7089 5539 4634 -680 473 213 O ATOM 710 CG2 THR A 131 12.094 -42.863 29.030 1.00 45.86 C ANISOU 710 CG2 THR A 131 7225 5426 4774 -750 557 265 C ATOM 711 N GLU A 132 14.247 -43.389 26.308 1.00 43.89 N ANISOU 711 N GLU A 132 6828 5116 4733 -467 265 369 N ATOM 712 CA GLU A 132 14.056 -44.177 25.093 1.00 46.64 C ANISOU 712 CA GLU A 132 7122 5404 5196 -459 271 372 C ATOM 713 C GLU A 132 12.597 -44.543 24.881 1.00 45.68 C ANISOU 713 C GLU A 132 6960 5265 5129 -597 425 306 C ATOM 714 O GLU A 132 12.086 -44.471 23.765 1.00 43.55 O ANISOU 714 O GLU A 132 6549 5011 4985 -617 453 255 O ATOM 715 CB GLU A 132 14.902 -45.454 25.124 1.00 50.16 C ANISOU 715 CB GLU A 132 7701 5755 5605 -360 177 446 C ATOM 716 CG GLU A 132 14.591 -46.408 23.977 1.00 51.68 C ANISOU 716 CG GLU A 132 7857 5878 5901 -366 199 440 C ATOM 717 CD GLU A 132 15.658 -47.463 23.775 1.00 53.64 C ANISOU 717 CD GLU A 132 8201 6046 6136 -236 78 495 C ATOM 718 OE1 GLU A 132 16.621 -47.500 24.570 1.00 54.80 O ANISOU 718 OE1 GLU A 132 8438 6190 6193 -137 -28 534 O ATOM 719 OE2 GLU A 132 15.536 -48.254 22.815 1.00 54.57 O ANISOU 719 OE2 GLU A 132 8292 6107 6336 -228 83 488 O ATOM 720 N PHE A 133 11.927 -44.922 25.963 1.00 47.53 N ANISOU 720 N PHE A 133 7314 5477 5268 -690 518 298 N ATOM 721 CA PHE A 133 10.540 -45.363 25.886 1.00 48.50 C ANISOU 721 CA PHE A 133 7407 5591 5429 -827 663 222 C ATOM 722 C PHE A 133 9.599 -44.218 25.518 1.00 45.69 C ANISOU 722 C PHE A 133 6848 5344 5169 -889 740 97 C ATOM 723 O PHE A 133 8.532 -44.443 24.949 1.00 44.86 O ANISOU 723 O PHE A 133 6640 5254 5151 -959 823 9 O ATOM 724 CB PHE A 133 10.103 -46.010 27.200 1.00 51.41 C ANISOU 724 CB PHE A 133 7966 5910 5658 -925 747 240 C ATOM 725 CG PHE A 133 8.716 -46.588 27.154 1.00 54.59 C ANISOU 725 CG PHE A 133 8353 6301 6090 -1076 899 155 C ATOM 726 CD1 PHE A 133 8.475 -47.791 26.507 1.00 55.46 C ANISOU 726 CD1 PHE A 133 8511 6324 6238 -1096 915 173 C ATOM 727 CD2 PHE A 133 7.654 -45.931 27.758 1.00 55.66 C ANISOU 727 CD2 PHE A 133 8418 6518 6214 -1198 1026 43 C ATOM 728 CE1 PHE A 133 7.200 -48.327 26.459 1.00 56.40 C ANISOU 728 CE1 PHE A 133 8611 6439 6378 -1241 1054 85 C ATOM 729 CE2 PHE A 133 6.377 -46.461 27.715 1.00 56.89 C ANISOU 729 CE2 PHE A 133 8546 6674 6396 -1338 1163 -55 C ATOM 730 CZ PHE A 133 6.149 -47.661 27.065 1.00 57.41 C ANISOU 730 CZ PHE A 133 8664 6655 6495 -1363 1179 -32 C ATOM 731 N THR A 134 10.001 -42.992 25.842 1.00 44.31 N ANISOU 731 N THR A 134 6614 5244 4976 -855 705 80 N ATOM 732 CA THR A 134 9.170 -41.824 25.572 1.00 42.61 C ANISOU 732 CA THR A 134 6212 5127 4850 -899 765 -48 C ATOM 733 C THR A 134 9.253 -41.418 24.100 1.00 41.66 C ANISOU 733 C THR A 134 5920 5026 4884 -832 700 -75 C ATOM 734 O THR A 134 8.274 -40.946 23.517 1.00 43.12 O ANISOU 734 O THR A 134 5942 5263 5180 -858 743 -192 O ATOM 735 CB THR A 134 9.571 -40.631 26.467 1.00 41.19 C ANISOU 735 CB THR A 134 6037 5021 4591 -890 753 -66 C ATOM 736 OG1 THR A 134 9.488 -41.021 27.843 1.00 42.67 O ANISOU 736 OG1 THR A 134 6386 5195 4633 -947 805 -40 O ATOM 737 CG2 THR A 134 8.659 -39.438 26.228 1.00 39.90 C ANISOU 737 CG2 THR A 134 5677 4953 4529 -929 816 -221 C ATOM 738 N ILE A 135 10.424 -41.618 23.502 1.00 39.34 N ANISOU 738 N ILE A 135 5662 4691 4596 -737 582 26 N ATOM 739 CA ILE A 135 10.685 -41.158 22.143 1.00 36.59 C ANISOU 739 CA ILE A 135 5164 4357 4380 -675 504 11 C ATOM 740 C ILE A 135 10.654 -42.290 21.120 1.00 36.88 C ANISOU 740 C ILE A 135 5191 4337 4485 -643 478 39 C ATOM 741 O ILE A 135 10.748 -42.044 19.919 1.00 36.60 O ANISOU 741 O ILE A 135 5032 4317 4556 -594 417 19 O ATOM 742 CB ILE A 135 12.055 -40.463 22.055 1.00 34.50 C ANISOU 742 CB ILE A 135 4918 4105 4086 -592 381 81 C ATOM 743 CG1 ILE A 135 13.182 -41.489 22.184 1.00 33.74 C ANISOU 743 CG1 ILE A 135 4978 3939 3904 -518 300 199 C ATOM 744 CG2 ILE A 135 12.180 -39.395 23.130 1.00 32.48 C ANISOU 744 CG2 ILE A 135 4666 3922 3754 -590 376 44 C ATOM 745 CD1 ILE A 135 14.568 -40.887 22.107 1.00 32.86 C ANISOU 745 CD1 ILE A 135 4829 3880 3778 -392 145 227 C ATOM 746 N GLU A 136 10.521 -43.521 21.610 1.00 39.43 N ANISOU 746 N GLU A 136 5650 4592 4738 -673 521 81 N ATOM 747 CA GLU A 136 10.575 -44.730 20.783 1.00 39.32 C ANISOU 747 CA GLU A 136 5658 4511 4771 -649 501 110 C ATOM 748 C GLU A 136 9.739 -44.672 19.508 1.00 36.30 C ANISOU 748 C GLU A 136 5103 4167 4521 -658 511 27 C ATOM 749 O GLU A 136 10.267 -44.792 18.403 1.00 35.41 O ANISOU 749 O GLU A 136 4927 4046 4479 -590 432 46 O ATOM 750 CB GLU A 136 10.137 -45.945 21.605 1.00 43.08 C ANISOU 750 CB GLU A 136 6299 4910 5158 -720 578 135 C ATOM 751 CG GLU A 136 11.244 -46.938 21.904 1.00 46.29 C ANISOU 751 CG GLU A 136 6884 5216 5488 -646 498 244 C ATOM 752 CD GLU A 136 10.792 -48.034 22.846 1.00 50.95 C ANISOU 752 CD GLU A 136 7662 5720 5975 -726 573 271 C ATOM 753 OE1 GLU A 136 9.576 -48.121 23.117 1.00 52.10 O ANISOU 753 OE1 GLU A 136 7787 5887 6122 -853 699 199 O ATOM 754 OE2 GLU A 136 11.653 -48.806 23.319 1.00 54.22 O ANISOU 754 OE2 GLU A 136 8248 6047 6307 -660 501 358 O ATOM 755 N ASP A 137 8.432 -44.496 19.671 1.00 36.64 N ANISOU 755 N ASP A 137 5074 4258 4591 -736 605 -73 N ATOM 756 CA ASP A 137 7.505 -44.569 18.547 1.00 36.83 C ANISOU 756 CA ASP A 137 4953 4319 4722 -737 611 -160 C ATOM 757 C ASP A 137 7.645 -43.399 17.581 1.00 35.01 C ANISOU 757 C ASP A 137 4569 4155 4580 -652 516 -193 C ATOM 758 O ASP A 137 7.381 -43.542 16.387 1.00 34.88 O ANISOU 758 O ASP A 137 4467 4152 4636 -613 466 -220 O ATOM 759 CB ASP A 137 6.066 -44.685 19.049 1.00 39.97 C ANISOU 759 CB ASP A 137 5317 4753 5118 -839 736 -277 C ATOM 760 CG ASP A 137 5.808 -45.993 19.768 1.00 44.20 C ANISOU 760 CG ASP A 137 6011 5212 5572 -939 830 -249 C ATOM 761 OD1 ASP A 137 6.371 -47.024 19.343 1.00 46.28 O ANISOU 761 OD1 ASP A 137 6361 5393 5828 -917 793 -170 O ATOM 762 OD2 ASP A 137 5.048 -45.992 20.759 1.00 45.71 O ANISOU 762 OD2 ASP A 137 6245 5419 5703 -1041 941 -312 O ATOM 763 N PHE A 138 8.058 -42.246 18.096 1.00 33.45 N ANISOU 763 N PHE A 138 4351 3993 4364 -629 488 -191 N ATOM 764 CA PHE A 138 8.290 -41.084 17.249 1.00 30.38 C ANISOU 764 CA PHE A 138 3845 3650 4047 -550 388 -212 C ATOM 765 C PHE A 138 9.445 -41.360 16.296 1.00 26.20 C ANISOU 765 C PHE A 138 3333 3090 3531 -486 285 -126 C ATOM 766 O PHE A 138 9.359 -41.081 15.100 1.00 24.30 O ANISOU 766 O PHE A 138 3014 2873 3344 -435 214 -141 O ATOM 767 CB PHE A 138 8.589 -39.843 18.092 1.00 31.07 C ANISOU 767 CB PHE A 138 3925 3771 4111 -551 382 -229 C ATOM 768 CG PHE A 138 7.490 -39.479 19.047 1.00 35.10 C ANISOU 768 CG PHE A 138 4407 4323 4608 -617 490 -337 C ATOM 769 CD1 PHE A 138 6.242 -39.103 18.578 1.00 36.54 C ANISOU 769 CD1 PHE A 138 4462 4551 4871 -605 509 -463 C ATOM 770 CD2 PHE A 138 7.708 -39.501 20.415 1.00 36.83 C ANISOU 770 CD2 PHE A 138 4730 4539 4724 -690 570 -323 C ATOM 771 CE1 PHE A 138 5.229 -38.765 19.455 1.00 37.05 C ANISOU 771 CE1 PHE A 138 4485 4664 4931 -667 611 -591 C ATOM 772 CE2 PHE A 138 6.700 -39.163 21.298 1.00 37.01 C ANISOU 772 CE2 PHE A 138 4724 4612 4728 -762 676 -439 C ATOM 773 CZ PHE A 138 5.459 -38.795 20.817 1.00 36.90 C ANISOU 773 CZ PHE A 138 4563 4648 4810 -752 699 -582 C ATOM 774 N HIS A 139 10.523 -41.916 16.839 1.00 26.22 N ANISOU 774 N HIS A 139 3452 3041 3471 -487 280 -41 N ATOM 775 CA HIS A 139 11.700 -42.251 16.048 1.00 28.81 C ANISOU 775 CA HIS A 139 3798 3338 3810 -430 198 21 C ATOM 776 C HIS A 139 11.388 -43.320 15.010 1.00 30.74 C ANISOU 776 C HIS A 139 4025 3555 4101 -423 195 10 C ATOM 777 O HIS A 139 11.892 -43.275 13.889 1.00 32.78 O ANISOU 777 O HIS A 139 4232 3825 4398 -381 127 10 O ATOM 778 CB HIS A 139 12.835 -42.731 16.953 1.00 30.59 C ANISOU 778 CB HIS A 139 4178 3504 3940 -416 187 108 C ATOM 779 CG HIS A 139 14.019 -43.258 16.204 1.00 31.21 C ANISOU 779 CG HIS A 139 4286 3550 4024 -342 102 156 C ATOM 780 ND1 HIS A 139 14.365 -44.592 16.203 1.00 32.53 N ANISOU 780 ND1 HIS A 139 4567 3627 4165 -310 99 198 N ATOM 781 CD2 HIS A 139 14.932 -42.631 15.424 1.00 30.35 C ANISOU 781 CD2 HIS A 139 4079 3513 3942 -271 8 149 C ATOM 782 CE1 HIS A 139 15.443 -44.764 15.458 1.00 32.82 C ANISOU 782 CE1 HIS A 139 4566 3684 4219 -213 5 205 C ATOM 783 NE2 HIS A 139 15.806 -43.591 14.973 1.00 30.72 N ANISOU 783 NE2 HIS A 139 4164 3526 3981 -197 -43 173 N ATOM 784 N ASN A 140 10.554 -44.280 15.390 1.00 30.23 N ANISOU 784 N ASN A 140 4010 3456 4022 -476 273 -9 N ATOM 785 CA ASN A 140 10.221 -45.386 14.503 1.00 30.40 C ANISOU 785 CA ASN A 140 4028 3440 4081 -483 278 -26 C ATOM 786 C ASN A 140 9.386 -44.945 13.305 1.00 26.09 C ANISOU 786 C ASN A 140 3350 2964 3599 -470 250 -102 C ATOM 787 O ASN A 140 9.561 -45.453 12.199 1.00 27.41 O ANISOU 787 O ASN A 140 3495 3123 3795 -446 210 -110 O ATOM 788 CB ASN A 140 9.515 -46.502 15.273 1.00 33.66 C ANISOU 788 CB ASN A 140 4541 3793 4455 -559 376 -30 C ATOM 789 CG ASN A 140 9.250 -47.718 14.415 1.00 35.23 C ANISOU 789 CG ASN A 140 4753 3939 4694 -574 382 -47 C ATOM 790 OD1 ASN A 140 10.181 -48.400 13.983 1.00 36.35 O ANISOU 790 OD1 ASN A 140 4958 4013 4841 -525 328 0 O ATOM 791 ND2 ASN A 140 7.977 -48.002 14.164 1.00 35.13 N ANISOU 791 ND2 ASN A 140 4683 3954 4712 -640 450 -128 N ATOM 792 N THR A 141 8.477 -44.002 13.532 1.00 22.57 N ANISOU 792 N THR A 141 2827 2581 3168 -479 271 -163 N ATOM 793 CA THR A 141 7.681 -43.427 12.454 1.00 21.94 C ANISOU 793 CA THR A 141 2638 2559 3137 -445 233 -233 C ATOM 794 C THR A 141 8.596 -42.668 11.500 1.00 21.36 C ANISOU 794 C THR A 141 2548 2511 3059 -374 127 -189 C ATOM 795 O THR A 141 8.418 -42.706 10.283 1.00 22.34 O ANISOU 795 O THR A 141 2633 2655 3199 -344 84 -211 O ATOM 796 CB THR A 141 6.596 -42.475 13.001 1.00 24.27 C ANISOU 796 CB THR A 141 2861 2904 3456 -455 272 -319 C ATOM 797 OG1 THR A 141 5.669 -43.216 13.804 1.00 28.01 O ANISOU 797 OG1 THR A 141 3350 3369 3925 -539 390 -382 O ATOM 798 CG2 THR A 141 5.840 -41.798 11.867 1.00 22.31 C ANISOU 798 CG2 THR A 141 2514 2700 3263 -398 213 -390 C ATOM 799 N PHE A 142 9.585 -41.989 12.073 1.00 20.40 N ANISOU 799 N PHE A 142 2459 2388 2903 -358 93 -132 N ATOM 800 CA PHE A 142 10.583 -41.259 11.300 1.00 20.01 C ANISOU 800 CA PHE A 142 2407 2368 2829 -314 15 -95 C ATOM 801 C PHE A 142 11.379 -42.203 10.397 1.00 18.75 C ANISOU 801 C PHE A 142 2269 2191 2664 -305 0 -77 C ATOM 802 O PHE A 142 11.516 -41.959 9.198 1.00 18.64 O ANISOU 802 O PHE A 142 2224 2212 2646 -277 -37 -90 O ATOM 803 CB PHE A 142 11.512 -40.493 12.246 1.00 19.32 C ANISOU 803 CB PHE A 142 2350 2281 2709 -316 0 -54 C ATOM 804 CG PHE A 142 12.570 -39.683 11.548 1.00 19.87 C ANISOU 804 CG PHE A 142 2410 2391 2749 -280 -47 -42 C ATOM 805 CD1 PHE A 142 12.273 -38.962 10.407 1.00 21.41 C ANISOU 805 CD1 PHE A 142 2574 2619 2941 -249 -83 -60 C ATOM 806 CD2 PHE A 142 13.857 -39.624 12.055 1.00 20.37 C ANISOU 806 CD2 PHE A 142 2488 2444 2806 -267 -66 -4 C ATOM 807 CE1 PHE A 142 13.245 -38.209 9.773 1.00 21.19 C ANISOU 807 CE1 PHE A 142 2547 2614 2890 -222 -117 -40 C ATOM 808 CE2 PHE A 142 14.831 -38.871 11.428 1.00 18.80 C ANISOU 808 CE2 PHE A 142 2269 2289 2585 -234 -117 13 C ATOM 809 CZ PHE A 142 14.525 -38.164 10.286 1.00 18.88 C ANISOU 809 CZ PHE A 142 2265 2327 2582 -218 -128 -8 C ATOM 810 N MET A 143 11.893 -43.284 10.974 1.00 18.70 N ANISOU 810 N MET A 143 2324 2118 2663 -326 32 -50 N ATOM 811 CA MET A 143 12.647 -44.275 10.212 1.00 22.45 C ANISOU 811 CA MET A 143 2821 2552 3158 -310 22 -49 C ATOM 812 C MET A 143 11.764 -44.966 9.179 1.00 25.14 C ANISOU 812 C MET A 143 3128 2899 3524 -318 33 -100 C ATOM 813 O MET A 143 12.239 -45.408 8.133 1.00 25.67 O ANISOU 813 O MET A 143 3176 2968 3610 -296 9 -122 O ATOM 814 CB MET A 143 13.257 -45.318 11.147 1.00 22.28 C ANISOU 814 CB MET A 143 2912 2418 3136 -313 51 -4 C ATOM 815 CG MET A 143 14.216 -44.746 12.171 1.00 21.57 C ANISOU 815 CG MET A 143 2868 2320 3006 -279 27 56 C ATOM 816 SD MET A 143 15.569 -43.848 11.398 1.00 28.90 S ANISOU 816 SD MET A 143 3698 3364 3919 -199 -73 57 S ATOM 817 CE MET A 143 16.281 -45.126 10.366 1.00 21.68 C ANISOU 817 CE MET A 143 2786 2425 3025 -133 -101 29 C ATOM 818 N ASP A 144 10.475 -45.052 9.484 1.00 26.05 N ANISOU 818 N ASP A 144 3226 3021 3653 -351 73 -132 N ATOM 819 CA ASP A 144 9.514 -45.695 8.599 1.00 27.88 C ANISOU 819 CA ASP A 144 3416 3259 3917 -366 90 -194 C ATOM 820 C ASP A 144 9.340 -44.912 7.299 1.00 26.06 C ANISOU 820 C ASP A 144 3117 3097 3688 -321 30 -223 C ATOM 821 O ASP A 144 9.205 -45.499 6.225 1.00 24.72 O ANISOU 821 O ASP A 144 2927 2931 3536 -316 17 -260 O ATOM 822 CB ASP A 144 8.171 -45.854 9.311 1.00 32.80 C ANISOU 822 CB ASP A 144 4018 3882 4562 -417 160 -243 C ATOM 823 CG ASP A 144 7.183 -46.667 8.510 1.00 38.07 C ANISOU 823 CG ASP A 144 4644 4550 5271 -445 190 -319 C ATOM 824 OD1 ASP A 144 7.362 -47.900 8.426 1.00 41.10 O ANISOU 824 OD1 ASP A 144 5085 4869 5663 -482 221 -315 O ATOM 825 OD2 ASP A 144 6.224 -46.074 7.971 1.00 39.29 O ANISOU 825 OD2 ASP A 144 4712 4761 5454 -429 177 -388 O ATOM 826 N LEU A 145 9.345 -43.587 7.402 1.00 27.51 N ANISOU 826 N LEU A 145 3279 3326 3850 -292 -8 -206 N ATOM 827 CA LEU A 145 9.232 -42.727 6.228 1.00 26.69 C ANISOU 827 CA LEU A 145 3141 3266 3733 -254 -70 -218 C ATOM 828 C LEU A 145 10.480 -42.833 5.357 1.00 25.55 C ANISOU 828 C LEU A 145 3021 3137 3552 -242 -104 -183 C ATOM 829 O LEU A 145 10.396 -42.816 4.129 1.00 24.65 O ANISOU 829 O LEU A 145 2891 3047 3427 -232 -139 -204 O ATOM 830 CB LEU A 145 9.003 -41.273 6.646 1.00 25.51 C ANISOU 830 CB LEU A 145 2982 3138 3573 -230 -101 -208 C ATOM 831 CG LEU A 145 7.643 -40.946 7.267 1.00 26.87 C ANISOU 831 CG LEU A 145 3101 3309 3799 -229 -77 -276 C ATOM 832 CD1 LEU A 145 7.615 -39.516 7.775 1.00 26.81 C ANISOU 832 CD1 LEU A 145 3088 3308 3792 -199 -112 -271 C ATOM 833 CD2 LEU A 145 6.529 -41.173 6.259 1.00 28.79 C ANISOU 833 CD2 LEU A 145 3283 3566 4088 -210 -98 -358 C ATOM 834 N ILE A 146 11.635 -42.943 6.004 1.00 23.79 N ANISOU 834 N ILE A 146 2828 2902 3310 -246 -92 -142 N ATOM 835 CA ILE A 146 12.902 -43.101 5.300 1.00 23.37 C ANISOU 835 CA ILE A 146 2773 2870 3237 -235 -116 -130 C ATOM 836 C ILE A 146 12.918 -44.401 4.499 1.00 24.36 C ANISOU 836 C ILE A 146 2887 2970 3401 -237 -108 -179 C ATOM 837 O ILE A 146 13.401 -44.439 3.366 1.00 24.72 O ANISOU 837 O ILE A 146 2912 3056 3424 -231 -136 -199 O ATOM 838 CB ILE A 146 14.093 -43.068 6.279 1.00 22.84 C ANISOU 838 CB ILE A 146 2717 2789 3172 -229 -113 -96 C ATOM 839 CG1 ILE A 146 14.150 -41.715 6.995 1.00 18.66 C ANISOU 839 CG1 ILE A 146 2199 2291 2602 -227 -118 -63 C ATOM 840 CG2 ILE A 146 15.401 -43.342 5.551 1.00 23.88 C ANISOU 840 CG2 ILE A 146 2817 2958 3299 -215 -143 -106 C ATOM 841 CD1 ILE A 146 15.285 -41.588 7.980 1.00 14.92 C ANISOU 841 CD1 ILE A 146 1728 1810 2132 -219 -130 -29 C ATOM 842 N GLU A 147 12.372 -45.459 5.088 1.00 25.01 N ANISOU 842 N GLU A 147 2989 2983 3532 -254 -64 -203 N ATOM 843 CA GLU A 147 12.305 -46.756 4.427 1.00 25.62 C ANISOU 843 CA GLU A 147 3070 3016 3650 -259 -47 -260 C ATOM 844 C GLU A 147 11.394 -46.706 3.201 1.00 24.50 C ANISOU 844 C GLU A 147 2885 2923 3500 -261 -67 -308 C ATOM 845 O GLU A 147 11.678 -47.337 2.182 1.00 21.57 O ANISOU 845 O GLU A 147 2500 2560 3137 -254 -80 -359 O ATOM 846 CB GLU A 147 11.821 -47.831 5.403 1.00 29.58 C ANISOU 846 CB GLU A 147 3638 3420 4183 -294 11 -259 C ATOM 847 CG GLU A 147 11.947 -49.249 4.872 1.00 33.65 C ANISOU 847 CG GLU A 147 4191 3859 4736 -297 28 -309 C ATOM 848 CD GLU A 147 11.434 -50.287 5.851 1.00 39.87 C ANISOU 848 CD GLU A 147 5081 4538 5530 -342 82 -287 C ATOM 849 OE1 GLU A 147 10.989 -49.899 6.952 1.00 42.10 O ANISOU 849 OE1 GLU A 147 5391 4817 5790 -374 110 -240 O ATOM 850 OE2 GLU A 147 11.474 -51.491 5.519 1.00 42.13 O ANISOU 850 OE2 GLU A 147 5426 4741 5840 -346 92 -320 O ATOM 851 N GLN A 148 10.300 -45.957 3.308 1.00 24.56 N ANISOU 851 N GLN A 148 2872 2961 3498 -266 -73 -306 N ATOM 852 CA GLN A 148 9.384 -45.776 2.186 1.00 23.69 C ANISOU 852 CA GLN A 148 2721 2891 3389 -258 -107 -357 C ATOM 853 C GLN A 148 10.099 -45.109 1.019 1.00 23.83 C ANISOU 853 C GLN A 148 2743 2961 3350 -238 -170 -341 C ATOM 854 O GLN A 148 9.935 -45.508 -0.133 1.00 26.27 O ANISOU 854 O GLN A 148 3037 3294 3651 -237 -196 -390 O ATOM 855 CB GLN A 148 8.172 -44.941 2.605 1.00 25.26 C ANISOU 855 CB GLN A 148 2886 3106 3604 -252 -114 -372 C ATOM 856 CG GLN A 148 7.257 -45.630 3.604 1.00 31.45 C ANISOU 856 CG GLN A 148 3653 3857 4439 -290 -42 -412 C ATOM 857 CD GLN A 148 6.114 -44.740 4.060 1.00 37.42 C ANISOU 857 CD GLN A 148 4357 4640 5222 -279 -43 -453 C ATOM 858 OE1 GLN A 148 5.793 -43.741 3.416 1.00 40.31 O ANISOU 858 OE1 GLN A 148 4693 5039 5582 -233 -111 -469 O ATOM 859 NE2 GLN A 148 5.497 -45.099 5.180 1.00 39.09 N ANISOU 859 NE2 GLN A 148 4558 4833 5462 -322 32 -480 N ATOM 860 N VAL A 149 10.894 -44.091 1.330 1.00 22.72 N ANISOU 860 N VAL A 149 2627 2844 3163 -234 -190 -275 N ATOM 861 CA VAL A 149 11.685 -43.394 0.326 1.00 22.11 C ANISOU 861 CA VAL A 149 2565 2819 3016 -242 -239 -251 C ATOM 862 C VAL A 149 12.734 -44.333 -0.266 1.00 21.02 C ANISOU 862 C VAL A 149 2417 2697 2873 -245 -225 -285 C ATOM 863 O VAL A 149 12.996 -44.312 -1.470 1.00 20.81 O ANISOU 863 O VAL A 149 2392 2718 2799 -256 -257 -313 O ATOM 864 CB VAL A 149 12.369 -42.145 0.926 1.00 21.67 C ANISOU 864 CB VAL A 149 2534 2786 2914 -253 -246 -183 C ATOM 865 CG1 VAL A 149 13.353 -41.535 -0.059 1.00 21.08 C ANISOU 865 CG1 VAL A 149 2478 2772 2759 -286 -277 -165 C ATOM 866 CG2 VAL A 149 11.322 -41.124 1.344 1.00 21.96 C ANISOU 866 CG2 VAL A 149 2571 2809 2963 -233 -266 -181 C ATOM 867 N GLU A 150 13.319 -45.167 0.588 1.00 21.64 N ANISOU 867 N GLU A 150 2487 2736 3000 -234 -180 -298 N ATOM 868 CA GLU A 150 14.330 -46.125 0.157 1.00 26.81 C ANISOU 868 CA GLU A 150 3116 3403 3666 -221 -165 -363 C ATOM 869 C GLU A 150 13.763 -47.126 -0.843 1.00 26.52 C ANISOU 869 C GLU A 150 3068 3359 3650 -220 -162 -449 C ATOM 870 O GLU A 150 14.455 -47.559 -1.764 1.00 28.08 O ANISOU 870 O GLU A 150 3243 3608 3817 -213 -164 -516 O ATOM 871 CB GLU A 150 14.924 -46.858 1.363 1.00 31.89 C ANISOU 871 CB GLU A 150 3761 3975 4382 -201 -140 -374 C ATOM 872 CG GLU A 150 16.119 -47.736 1.029 1.00 36.94 C ANISOU 872 CG GLU A 150 4376 4630 5031 -154 -140 -447 C ATOM 873 CD GLU A 150 16.833 -48.244 2.265 1.00 42.30 C ANISOU 873 CD GLU A 150 5100 5236 5738 -87 -132 -407 C ATOM 874 OE1 GLU A 150 16.160 -48.477 3.291 1.00 45.65 O ANISOU 874 OE1 GLU A 150 5590 5553 6204 -102 -115 -359 O ATOM 875 OE2 GLU A 150 18.071 -48.402 2.214 1.00 43.86 O ANISOU 875 OE2 GLU A 150 5265 5491 5909 -19 -146 -431 O ATOM 876 N LYS A 151 12.495 -47.481 -0.661 1.00 25.20 N ANISOU 876 N LYS A 151 2909 3141 3526 -230 -150 -458 N ATOM 877 CA LYS A 151 11.826 -48.420 -1.552 1.00 25.47 C ANISOU 877 CA LYS A 151 2928 3168 3583 -236 -147 -539 C ATOM 878 C LYS A 151 11.096 -47.691 -2.672 1.00 26.82 C ANISOU 878 C LYS A 151 3087 3406 3696 -239 -202 -546 C ATOM 879 O LYS A 151 10.186 -48.239 -3.294 1.00 27.99 O ANISOU 879 O LYS A 151 3214 3553 3866 -244 -209 -608 O ATOM 880 CB LYS A 151 10.863 -49.310 -0.765 1.00 25.59 C ANISOU 880 CB LYS A 151 2953 3098 3672 -260 -99 -556 C ATOM 881 CG LYS A 151 11.561 -50.207 0.243 1.00 27.56 C ANISOU 881 CG LYS A 151 3253 3250 3970 -262 -54 -547 C ATOM 882 CD LYS A 151 10.573 -51.013 1.066 1.00 31.44 C ANISOU 882 CD LYS A 151 3786 3656 4504 -311 0 -542 C ATOM 883 CE LYS A 151 11.302 -51.952 2.015 1.00 35.74 C ANISOU 883 CE LYS A 151 4431 4075 5073 -308 31 -516 C ATOM 884 NZ LYS A 151 10.363 -52.726 2.873 1.00 40.22 N ANISOU 884 NZ LYS A 151 5069 4556 5656 -374 86 -497 N ATOM 885 N GLN A 152 11.508 -46.449 -2.912 1.00 26.47 N ANISOU 885 N GLN A 152 3064 3414 3580 -240 -246 -483 N ATOM 886 CA GLN A 152 11.006 -45.639 -4.021 1.00 24.68 C ANISOU 886 CA GLN A 152 2854 3239 3284 -246 -319 -480 C ATOM 887 C GLN A 152 9.491 -45.456 -4.020 1.00 26.81 C ANISOU 887 C GLN A 152 3100 3492 3595 -231 -349 -505 C ATOM 888 O GLN A 152 8.829 -45.705 -5.027 1.00 27.42 O ANISOU 888 O GLN A 152 3164 3597 3657 -225 -392 -565 O ATOM 889 CB GLN A 152 11.474 -46.208 -5.364 1.00 22.24 C ANISOU 889 CB GLN A 152 2549 2988 2915 -254 -334 -549 C ATOM 890 CG GLN A 152 12.983 -46.217 -5.539 1.00 24.19 C ANISOU 890 CG GLN A 152 2800 3288 3103 -267 -300 -550 C ATOM 891 CD GLN A 152 13.588 -44.827 -5.480 1.00 27.64 C ANISOU 891 CD GLN A 152 3281 3760 3460 -296 -332 -465 C ATOM 892 OE1 GLN A 152 12.992 -43.856 -5.948 1.00 30.34 O ANISOU 892 OE1 GLN A 152 3679 4099 3749 -306 -410 -422 O ATOM 893 NE2 GLN A 152 14.777 -44.724 -4.899 1.00 27.30 N ANISOU 893 NE2 GLN A 152 3217 3747 3408 -307 -278 -448 N ATOM 894 N THR A 153 8.949 -45.021 -2.887 1.00 29.45 N ANISOU 894 N THR A 153 3421 3789 3979 -222 -327 -472 N ATOM 895 CA THR A 153 7.536 -44.676 -2.803 1.00 31.60 C ANISOU 895 CA THR A 153 3652 4060 4295 -199 -354 -513 C ATOM 896 C THR A 153 7.234 -43.547 -3.782 1.00 33.69 C ANISOU 896 C THR A 153 3940 4366 4496 -173 -457 -504 C ATOM 897 O THR A 153 8.100 -42.721 -4.073 1.00 35.94 O ANISOU 897 O THR A 153 4285 4671 4699 -187 -493 -437 O ATOM 898 CB THR A 153 7.141 -44.233 -1.377 1.00 31.65 C ANISOU 898 CB THR A 153 3642 4030 4351 -194 -310 -485 C ATOM 899 OG1 THR A 153 5.750 -43.888 -1.343 1.00 33.60 O ANISOU 899 OG1 THR A 153 3831 4285 4649 -165 -336 -554 O ATOM 900 CG2 THR A 153 7.962 -43.029 -0.940 1.00 30.78 C ANISOU 900 CG2 THR A 153 3581 3923 4190 -189 -333 -396 C ATOM 901 N SER A 154 6.014 -43.522 -4.305 1.00 34.46 N ANISOU 901 N SER A 154 3992 4478 4624 -138 -509 -579 N ATOM 902 CA SER A 154 5.603 -42.434 -5.181 1.00 34.13 C ANISOU 902 CA SER A 154 3980 4464 4524 -94 -625 -577 C ATOM 903 C SER A 154 5.543 -41.142 -4.375 1.00 30.17 C ANISOU 903 C SER A 154 3500 3931 4032 -59 -651 -524 C ATOM 904 O SER A 154 5.407 -41.173 -3.152 1.00 26.64 O ANISOU 904 O SER A 154 3016 3452 3654 -63 -581 -521 O ATOM 905 CB SER A 154 4.240 -42.728 -5.809 1.00 34.20 C ANISOU 905 CB SER A 154 3921 4493 4580 -46 -682 -688 C ATOM 906 OG SER A 154 3.217 -42.730 -4.829 1.00 33.80 O ANISOU 906 OG SER A 154 3785 4420 4637 -18 -644 -753 O ATOM 907 N VAL A 155 5.656 -40.009 -5.058 1.00 31.90 N ANISOU 907 N VAL A 155 3791 4155 4176 -25 -753 -485 N ATOM 908 CA VAL A 155 5.563 -38.716 -4.393 1.00 35.05 C ANISOU 908 CA VAL A 155 4225 4504 4591 22 -795 -445 C ATOM 909 C VAL A 155 4.152 -38.512 -3.845 1.00 35.18 C ANISOU 909 C VAL A 155 4156 4493 4717 100 -823 -541 C ATOM 910 O VAL A 155 3.961 -37.872 -2.811 1.00 35.43 O ANISOU 910 O VAL A 155 4172 4484 4806 125 -807 -540 O ATOM 911 CB VAL A 155 5.932 -37.561 -5.345 1.00 37.52 C ANISOU 911 CB VAL A 155 4662 4801 4794 50 -911 -383 C ATOM 912 CG1 VAL A 155 5.989 -36.244 -4.589 1.00 37.32 C ANISOU 912 CG1 VAL A 155 4695 4694 4790 93 -953 -334 C ATOM 913 CG2 VAL A 155 7.265 -37.841 -6.020 1.00 38.82 C ANISOU 913 CG2 VAL A 155 4897 5016 4835 -35 -874 -317 C ATOM 914 N ALA A 156 3.170 -39.078 -4.539 1.00 35.53 N ANISOU 914 N ALA A 156 4139 4569 4792 135 -863 -639 N ATOM 915 CA ALA A 156 1.778 -38.999 -4.111 1.00 35.54 C ANISOU 915 CA ALA A 156 4037 4565 4901 206 -884 -766 C ATOM 916 C ALA A 156 1.559 -39.722 -2.784 1.00 34.62 C ANISOU 916 C ALA A 156 3832 4450 4873 153 -742 -805 C ATOM 917 O ALA A 156 0.870 -39.215 -1.898 1.00 34.95 O ANISOU 917 O ALA A 156 3818 4474 4986 191 -731 -868 O ATOM 918 CB ALA A 156 0.862 -39.569 -5.185 1.00 36.41 C ANISOU 918 CB ALA A 156 4092 4721 5020 244 -949 -873 C ATOM 919 N ASP A 157 2.145 -40.908 -2.651 1.00 33.98 N ANISOU 919 N ASP A 157 3747 4383 4780 66 -638 -775 N ATOM 920 CA ASP A 157 2.018 -41.686 -1.424 1.00 37.13 C ANISOU 920 CA ASP A 157 4093 4772 5241 8 -507 -797 C ATOM 921 C ASP A 157 2.772 -41.036 -0.268 1.00 35.86 C ANISOU 921 C ASP A 157 3982 4576 5067 -9 -462 -705 C ATOM 922 O ASP A 157 2.347 -41.117 0.885 1.00 35.32 O ANISOU 922 O ASP A 157 3869 4499 5052 -26 -387 -741 O ATOM 923 CB ASP A 157 2.503 -43.124 -1.636 1.00 39.64 C ANISOU 923 CB ASP A 157 4418 5095 5548 -67 -426 -787 C ATOM 924 CG ASP A 157 1.534 -43.951 -2.463 1.00 44.72 C ANISOU 924 CG ASP A 157 4986 5773 6231 -65 -439 -908 C ATOM 925 OD1 ASP A 157 0.792 -43.365 -3.279 1.00 47.18 O ANISOU 925 OD1 ASP A 157 5265 6116 6546 3 -543 -975 O ATOM 926 OD2 ASP A 157 1.514 -45.189 -2.294 1.00 45.58 O ANISOU 926 OD2 ASP A 157 5074 5876 6369 -129 -353 -940 O ATOM 927 N LEU A 158 3.893 -40.392 -0.582 1.00 34.37 N ANISOU 927 N LEU A 158 3884 4374 4801 -11 -505 -596 N ATOM 928 CA LEU A 158 4.675 -39.684 0.426 1.00 31.20 C ANISOU 928 CA LEU A 158 3529 3943 4382 -25 -474 -514 C ATOM 929 C LEU A 158 3.880 -38.507 0.976 1.00 30.84 C ANISOU 929 C LEU A 158 3457 3873 4389 43 -527 -563 C ATOM 930 O LEU A 158 3.922 -38.219 2.172 1.00 30.48 O ANISOU 930 O LEU A 158 3398 3811 4373 33 -472 -557 O ATOM 931 CB LEU A 158 6.000 -39.196 -0.164 1.00 29.47 C ANISOU 931 CB LEU A 158 3403 3725 4070 -47 -510 -409 C ATOM 932 CG LEU A 158 6.933 -38.437 0.786 1.00 27.58 C ANISOU 932 CG LEU A 158 3211 3461 3808 -65 -482 -330 C ATOM 933 CD1 LEU A 158 7.349 -39.318 1.954 1.00 24.18 C ANISOU 933 CD1 LEU A 158 2761 3029 3396 -113 -370 -312 C ATOM 934 CD2 LEU A 158 8.154 -37.909 0.046 1.00 26.58 C ANISOU 934 CD2 LEU A 158 3164 3344 3589 -92 -519 -253 C ATOM 935 N LEU A 159 3.149 -37.836 0.092 1.00 32.18 N ANISOU 935 N LEU A 159 3622 4037 4567 120 -643 -619 N ATOM 936 CA LEU A 159 2.311 -36.707 0.475 1.00 33.23 C ANISOU 936 CA LEU A 159 3732 4134 4758 208 -718 -692 C ATOM 937 C LEU A 159 1.162 -37.153 1.375 1.00 36.08 C ANISOU 937 C LEU A 159 3968 4524 5216 213 -644 -829 C ATOM 938 O LEU A 159 0.777 -36.443 2.304 1.00 37.00 O ANISOU 938 O LEU A 159 4055 4622 5383 246 -639 -882 O ATOM 939 CB LEU A 159 1.766 -36.007 -0.770 1.00 32.97 C ANISOU 939 CB LEU A 159 3739 4083 4705 301 -873 -730 C ATOM 940 CG LEU A 159 0.845 -34.809 -0.537 1.00 34.90 C ANISOU 940 CG LEU A 159 3975 4275 5009 416 -982 -825 C ATOM 941 CD1 LEU A 159 1.551 -33.751 0.293 1.00 33.30 C ANISOU 941 CD1 LEU A 159 3853 4002 4799 416 -991 -749 C ATOM 942 CD2 LEU A 159 0.372 -34.231 -1.863 1.00 35.14 C ANISOU 942 CD2 LEU A 159 4072 4277 5001 511 -1148 -852 C ATOM 943 N ALA A 160 0.622 -38.335 1.095 1.00 37.87 N ANISOU 943 N ALA A 160 4123 4799 5466 173 -583 -897 N ATOM 944 CA ALA A 160 -0.482 -38.879 1.878 1.00 39.38 C ANISOU 944 CA ALA A 160 4197 5026 5740 154 -496 -1038 C ATOM 945 C ALA A 160 -0.059 -39.160 3.318 1.00 41.44 C ANISOU 945 C ALA A 160 4464 5280 6003 74 -364 -995 C ATOM 946 O ALA A 160 -0.821 -38.917 4.255 1.00 44.98 O ANISOU 946 O ALA A 160 4840 5743 6506 74 -313 -1101 O ATOM 947 CB ALA A 160 -1.025 -40.142 1.226 1.00 37.96 C ANISOU 947 CB ALA A 160 3957 4891 5577 111 -455 -1110 C ATOM 948 N SER A 161 1.157 -39.671 3.485 1.00 38.14 N ANISOU 948 N SER A 161 4132 4841 5518 7 -314 -852 N ATOM 949 CA SER A 161 1.692 -39.958 4.812 1.00 34.99 C ANISOU 949 CA SER A 161 3760 4430 5104 -62 -206 -796 C ATOM 950 C SER A 161 1.901 -38.672 5.603 1.00 32.52 C ANISOU 950 C SER A 161 3463 4096 4796 -20 -238 -779 C ATOM 951 O SER A 161 1.736 -38.648 6.823 1.00 31.69 O ANISOU 951 O SER A 161 3336 3998 4708 -57 -157 -807 O ATOM 952 CB SER A 161 3.010 -40.726 4.706 1.00 33.75 C ANISOU 952 CB SER A 161 3696 4252 4875 -119 -173 -659 C ATOM 953 OG SER A 161 2.808 -42.012 4.150 1.00 35.35 O ANISOU 953 OG SER A 161 3885 4463 5083 -163 -133 -688 O ATOM 954 N PHE A 162 2.263 -37.607 4.897 1.00 30.78 N ANISOU 954 N PHE A 162 3288 3848 4557 51 -356 -736 N ATOM 955 CA PHE A 162 2.462 -36.305 5.519 1.00 33.12 C ANISOU 955 CA PHE A 162 3610 4110 4867 99 -406 -726 C ATOM 956 C PHE A 162 1.138 -35.608 5.808 1.00 36.68 C ANISOU 956 C PHE A 162 3970 4563 5403 176 -447 -893 C ATOM 957 O PHE A 162 1.106 -34.566 6.462 1.00 36.24 O ANISOU 957 O PHE A 162 3918 4476 5375 222 -484 -921 O ATOM 958 CB PHE A 162 3.348 -35.420 4.641 1.00 33.45 C ANISOU 958 CB PHE A 162 3754 4103 4852 138 -520 -622 C ATOM 959 CG PHE A 162 4.811 -35.535 4.952 1.00 33.24 C ANISOU 959 CG PHE A 162 3810 4070 4749 68 -473 -481 C ATOM 960 CD1 PHE A 162 5.542 -36.632 4.526 1.00 31.57 C ANISOU 960 CD1 PHE A 162 3625 3891 4480 1 -415 -415 C ATOM 961 CD2 PHE A 162 5.456 -34.544 5.673 1.00 32.34 C ANISOU 961 CD2 PHE A 162 3743 3918 4625 73 -492 -431 C ATOM 962 CE1 PHE A 162 6.889 -36.738 4.813 1.00 30.19 C ANISOU 962 CE1 PHE A 162 3515 3718 4238 -52 -376 -312 C ATOM 963 CE2 PHE A 162 6.801 -34.642 5.960 1.00 31.56 C ANISOU 963 CE2 PHE A 162 3711 3824 4457 10 -449 -321 C ATOM 964 CZ PHE A 162 7.519 -35.743 5.532 1.00 31.20 C ANISOU 964 CZ PHE A 162 3683 3818 4353 -49 -389 -267 C ATOM 965 N ASN A 163 0.046 -36.183 5.314 1.00 40.19 N ANISOU 965 N ASN A 163 4330 5048 5894 192 -444 -1019 N ATOM 966 CA ASN A 163 -1.282 -35.644 5.584 1.00 41.03 C ANISOU 966 CA ASN A 163 4334 5173 6083 261 -476 -1212 C ATOM 967 C ASN A 163 -2.070 -36.489 6.579 1.00 41.14 C ANISOU 967 C ASN A 163 4244 5252 6136 177 -324 -1335 C ATOM 968 O ASN A 163 -3.201 -36.156 6.933 1.00 41.35 O ANISOU 968 O ASN A 163 4170 5314 6229 211 -326 -1523 O ATOM 969 CB ASN A 163 -2.071 -35.440 4.290 1.00 40.27 C ANISOU 969 CB ASN A 163 4212 5078 6011 356 -608 -1302 C ATOM 970 CG ASN A 163 -1.753 -34.118 3.623 1.00 41.07 C ANISOU 970 CG ASN A 163 4414 5100 6090 465 -781 -1254 C ATOM 971 OD1 ASN A 163 -2.116 -33.056 4.128 1.00 44.61 O ANISOU 971 OD1 ASN A 163 4861 5510 6580 537 -849 -1334 O ATOM 972 ND2 ASN A 163 -1.075 -34.173 2.483 1.00 39.10 N ANISOU 972 ND2 ASN A 163 4264 4823 5770 471 -856 -1130 N ATOM 973 N ASP A 164 -1.467 -37.586 7.024 1.00 40.40 N ANISOU 973 N ASP A 164 4184 5172 5995 63 -198 -1238 N ATOM 974 CA ASP A 164 -2.019 -38.353 8.130 1.00 42.97 C ANISOU 974 CA ASP A 164 4452 5540 6333 -40 -43 -1324 C ATOM 975 C ASP A 164 -1.572 -37.700 9.429 1.00 46.00 C ANISOU 975 C ASP A 164 4866 5913 6699 -64 7 -1295 C ATOM 976 O ASP A 164 -0.378 -37.658 9.727 1.00 45.03 O ANISOU 976 O ASP A 164 4840 5753 6516 -87 11 -1131 O ATOM 977 CB ASP A 164 -1.545 -39.804 8.082 1.00 43.70 C ANISOU 977 CB ASP A 164 4597 5631 6378 -149 56 -1230 C ATOM 978 CG ASP A 164 -2.045 -40.614 9.260 1.00 46.51 C ANISOU 978 CG ASP A 164 4929 6012 6729 -271 219 -1302 C ATOM 979 OD1 ASP A 164 -3.182 -40.366 9.712 1.00 50.54 O ANISOU 979 OD1 ASP A 164 5339 6572 7291 -283 263 -1484 O ATOM 980 OD2 ASP A 164 -1.301 -41.495 9.739 1.00 45.64 O ANISOU 980 OD2 ASP A 164 4909 5871 6559 -359 298 -1185 O ATOM 981 N GLN A 165 -2.538 -37.192 10.190 1.00 49.31 N ANISOU 981 N GLN A 165 5196 6370 7170 -60 41 -1471 N ATOM 982 CA GLN A 165 -2.272 -36.418 11.400 1.00 49.56 C ANISOU 982 CA GLN A 165 5239 6399 7192 -72 77 -1482 C ATOM 983 C GLN A 165 -1.291 -37.106 12.344 1.00 46.85 C ANISOU 983 C GLN A 165 4989 6046 6767 -185 196 -1334 C ATOM 984 O GLN A 165 -0.299 -36.509 12.761 1.00 45.06 O ANISOU 984 O GLN A 165 4830 5787 6505 -166 167 -1219 O ATOM 985 CB GLN A 165 -3.581 -36.125 12.138 1.00 54.85 C ANISOU 985 CB GLN A 165 5793 7136 7913 -98 125 -1701 C ATOM 986 CG GLN A 165 -3.449 -35.131 13.282 1.00 57.77 C ANISOU 986 CG GLN A 165 6158 7514 8276 -99 128 -1717 C ATOM 987 CD GLN A 165 -3.297 -33.699 12.800 1.00 60.25 C ANISOU 987 CD GLN A 165 6478 7785 8629 46 -52 -1701 C ATOM 988 OE1 GLN A 165 -3.480 -33.406 11.618 1.00 60.71 O ANISOU 988 OE1 GLN A 165 6540 7809 8717 147 -184 -1701 O ATOM 989 NE2 GLN A 165 -2.962 -32.798 13.718 1.00 60.73 N ANISOU 989 NE2 GLN A 165 6550 7841 8684 54 -62 -1692 N ATOM 990 N SER A 166 -1.568 -38.365 12.666 1.00 46.10 N ANISOU 990 N SER A 166 4904 5972 6640 -302 323 -1343 N ATOM 991 CA SER A 166 -0.727 -39.125 13.585 1.00 43.77 C ANISOU 991 CA SER A 166 4717 5654 6259 -410 428 -1214 C ATOM 992 C SER A 166 0.691 -39.307 13.048 1.00 39.49 C ANISOU 992 C SER A 166 4283 5056 5667 -377 352 -1004 C ATOM 993 O SER A 166 1.664 -39.080 13.761 1.00 40.06 O ANISOU 993 O SER A 166 4434 5104 5683 -395 360 -897 O ATOM 994 CB SER A 166 -1.357 -40.487 13.883 1.00 44.86 C ANISOU 994 CB SER A 166 4865 5806 6375 -539 562 -1267 C ATOM 995 OG SER A 166 -0.589 -41.209 14.830 1.00 44.87 O ANISOU 995 OG SER A 166 4994 5769 6287 -639 653 -1147 O ATOM 996 N THR A 167 0.800 -39.708 11.786 1.00 34.20 N ANISOU 996 N THR A 167 3613 4369 5011 -333 279 -961 N ATOM 997 CA THR A 167 2.100 -39.957 11.172 1.00 31.73 C ANISOU 997 CA THR A 167 3396 4013 4646 -312 210 -789 C ATOM 998 C THR A 167 2.900 -38.669 10.984 1.00 33.06 C ANISOU 998 C THR A 167 3591 4164 4806 -230 101 -717 C ATOM 999 O THR A 167 4.088 -38.613 11.305 1.00 33.51 O ANISOU 999 O THR A 167 3732 4196 4805 -245 88 -593 O ATOM 1000 CB THR A 167 1.949 -40.675 9.812 1.00 30.53 C ANISOU 1000 CB THR A 167 3234 3857 4509 -292 163 -784 C ATOM 1001 OG1 THR A 167 1.360 -41.966 10.015 1.00 32.39 O ANISOU 1001 OG1 THR A 167 3461 4096 4749 -381 266 -837 O ATOM 1002 CG2 THR A 167 3.302 -40.845 9.139 1.00 27.66 C ANISOU 1002 CG2 THR A 167 2963 3459 4089 -271 93 -632 C ATOM 1003 N SER A 168 2.241 -37.635 10.473 1.00 32.26 N ANISOU 1003 N SER A 168 3424 4071 4764 -145 19 -805 N ATOM 1004 CA SER A 168 2.910 -36.377 10.164 1.00 31.53 C ANISOU 1004 CA SER A 168 3369 3944 4667 -68 -94 -744 C ATOM 1005 C SER A 168 3.369 -35.630 11.417 1.00 33.95 C ANISOU 1005 C SER A 168 3692 4246 4963 -82 -66 -730 C ATOM 1006 O SER A 168 4.419 -34.986 11.413 1.00 31.82 O ANISOU 1006 O SER A 168 3493 3945 4654 -67 -125 -626 O ATOM 1007 CB SER A 168 1.997 -35.482 9.326 1.00 29.85 C ANISOU 1007 CB SER A 168 3098 3721 4524 36 -205 -854 C ATOM 1008 OG SER A 168 2.711 -34.381 8.793 1.00 28.22 O ANISOU 1008 OG SER A 168 2962 3458 4302 104 -328 -775 O ATOM 1009 N ASP A 169 2.579 -35.716 12.484 1.00 34.05 N ANISOU 1009 N ASP A 169 3640 4295 5003 -121 30 -848 N ATOM 1010 CA ASP A 169 2.911 -35.031 13.730 1.00 33.76 C ANISOU 1010 CA ASP A 169 3609 4265 4954 -141 68 -860 C ATOM 1011 C ASP A 169 3.937 -35.801 14.555 1.00 33.03 C ANISOU 1011 C ASP A 169 3611 4168 4771 -239 149 -736 C ATOM 1012 O ASP A 169 4.757 -35.199 15.245 1.00 32.59 O ANISOU 1012 O ASP A 169 3601 4101 4682 -246 135 -681 O ATOM 1013 CB ASP A 169 1.653 -34.750 14.556 1.00 36.21 C ANISOU 1013 CB ASP A 169 3816 4624 5319 -151 143 -1060 C ATOM 1014 CG ASP A 169 0.875 -33.555 14.040 1.00 39.42 C ANISOU 1014 CG ASP A 169 4144 5016 5817 -25 24 -1196 C ATOM 1015 OD1 ASP A 169 1.164 -33.097 12.915 1.00 38.72 O ANISOU 1015 OD1 ASP A 169 4090 4875 5747 64 -110 -1130 O ATOM 1016 OD2 ASP A 169 -0.028 -33.075 14.757 1.00 43.31 O ANISOU 1016 OD2 ASP A 169 4561 5553 6342 -32 48 -1340 O ATOM 1017 N TYR A 170 3.885 -37.129 14.482 1.00 33.14 N ANISOU 1017 N TYR A 170 3661 4184 4749 -309 224 -701 N ATOM 1018 CA TYR A 170 4.911 -37.968 15.093 1.00 32.37 C ANISOU 1018 CA TYR A 170 3671 4059 4568 -381 273 -579 C ATOM 1019 C TYR A 170 6.273 -37.600 14.518 1.00 31.56 C ANISOU 1019 C TYR A 170 3634 3923 4433 -332 164 -445 C ATOM 1020 O TYR A 170 7.280 -37.602 15.225 1.00 33.36 O ANISOU 1020 O TYR A 170 3934 4134 4606 -359 168 -368 O ATOM 1021 CB TYR A 170 4.623 -39.450 14.835 1.00 32.38 C ANISOU 1021 CB TYR A 170 3707 4046 4551 -442 340 -565 C ATOM 1022 CG TYR A 170 3.916 -40.166 15.967 1.00 34.74 C ANISOU 1022 CG TYR A 170 4030 4355 4816 -549 484 -633 C ATOM 1023 CD1 TYR A 170 2.766 -39.638 16.543 1.00 35.57 C ANISOU 1023 CD1 TYR A 170 4049 4512 4954 -577 554 -790 C ATOM 1024 CD2 TYR A 170 4.390 -41.381 16.448 1.00 34.69 C ANISOU 1024 CD2 TYR A 170 4141 4300 4739 -625 549 -550 C ATOM 1025 CE1 TYR A 170 2.115 -40.294 17.572 1.00 36.32 C ANISOU 1025 CE1 TYR A 170 4179 4618 5001 -697 694 -859 C ATOM 1026 CE2 TYR A 170 3.745 -42.044 17.477 1.00 35.70 C ANISOU 1026 CE2 TYR A 170 4322 4425 4817 -736 682 -603 C ATOM 1027 CZ TYR A 170 2.608 -41.497 18.035 1.00 37.06 C ANISOU 1027 CZ TYR A 170 4411 4657 5012 -781 759 -757 C ATOM 1028 OH TYR A 170 1.964 -42.153 19.059 1.00 37.27 O ANISOU 1028 OH TYR A 170 4500 4684 4977 -911 897 -816 O ATOM 1029 N LEU A 171 6.288 -37.283 13.226 1.00 29.52 N ANISOU 1029 N LEU A 171 3355 3660 4201 -266 71 -429 N ATOM 1030 CA LEU A 171 7.505 -36.864 12.547 1.00 30.83 C ANISOU 1030 CA LEU A 171 3583 3807 4324 -234 -18 -322 C ATOM 1031 C LEU A 171 8.040 -35.561 13.129 1.00 32.95 C ANISOU 1031 C LEU A 171 3869 4066 4585 -214 -63 -310 C ATOM 1032 O LEU A 171 9.202 -35.478 13.527 1.00 36.02 O ANISOU 1032 O LEU A 171 4319 4449 4917 -237 -74 -234 O ATOM 1033 CB LEU A 171 7.246 -36.677 11.054 1.00 29.78 C ANISOU 1033 CB LEU A 171 3433 3672 4212 -182 -91 -327 C ATOM 1034 CG LEU A 171 8.409 -36.015 10.312 1.00 29.54 C ANISOU 1034 CG LEU A 171 3465 3629 4131 -161 -165 -241 C ATOM 1035 CD1 LEU A 171 9.439 -37.043 9.886 1.00 26.78 C ANISOU 1035 CD1 LEU A 171 3164 3293 3719 -195 -141 -169 C ATOM 1036 CD2 LEU A 171 7.919 -35.212 9.126 1.00 31.00 C ANISOU 1036 CD2 LEU A 171 3636 3794 4350 -101 -252 -269 C ATOM 1037 N VAL A 172 7.179 -34.548 13.166 1.00 30.90 N ANISOU 1037 N VAL A 172 3548 3803 4389 -164 -95 -401 N ATOM 1038 CA VAL A 172 7.541 -33.234 13.686 1.00 28.11 C ANISOU 1038 CA VAL A 172 3210 3428 4044 -135 -149 -409 C ATOM 1039 C VAL A 172 8.030 -33.320 15.129 1.00 29.50 C ANISOU 1039 C VAL A 172 3409 3619 4179 -198 -80 -406 C ATOM 1040 O VAL A 172 9.005 -32.665 15.498 1.00 31.35 O ANISOU 1040 O VAL A 172 3702 3837 4373 -205 -119 -352 O ATOM 1041 CB VAL A 172 6.358 -32.248 13.589 1.00 25.35 C ANISOU 1041 CB VAL A 172 2777 3065 3789 -55 -200 -539 C ATOM 1042 CG1 VAL A 172 6.700 -30.925 14.259 1.00 25.64 C ANISOU 1042 CG1 VAL A 172 2835 3068 3837 -24 -256 -557 C ATOM 1043 CG2 VAL A 172 5.974 -32.028 12.136 1.00 21.70 C ANISOU 1043 CG2 VAL A 172 2315 2569 3362 17 -298 -539 C ATOM 1044 N VAL A 173 7.355 -34.138 15.934 1.00 28.68 N ANISOU 1044 N VAL A 173 3270 3550 4079 -252 30 -470 N ATOM 1045 CA VAL A 173 7.765 -34.363 17.317 1.00 27.83 C ANISOU 1045 CA VAL A 173 3202 3456 3915 -328 114 -471 C ATOM 1046 C VAL A 173 9.223 -34.803 17.386 1.00 27.03 C ANISOU 1046 C VAL A 173 3200 3328 3740 -354 82 -340 C ATOM 1047 O VAL A 173 10.006 -34.261 18.165 1.00 27.26 O ANISOU 1047 O VAL A 173 3274 3356 3728 -373 66 -326 O ATOM 1048 CB VAL A 173 6.893 -35.429 18.016 1.00 29.40 C ANISOU 1048 CB VAL A 173 3388 3687 4095 -411 260 -535 C ATOM 1049 CG1 VAL A 173 7.544 -35.886 19.311 1.00 28.57 C ANISOU 1049 CG1 VAL A 173 3384 3581 3891 -506 348 -492 C ATOM 1050 CG2 VAL A 173 5.501 -34.891 18.288 1.00 32.16 C ANISOU 1050 CG2 VAL A 173 3623 4085 4513 -400 313 -707 C ATOM 1051 N TYR A 174 9.591 -35.771 16.554 1.00 26.12 N ANISOU 1051 N TYR A 174 3113 3198 3612 -350 68 -263 N ATOM 1052 CA TYR A 174 10.948 -36.301 16.601 1.00 23.36 C ANISOU 1052 CA TYR A 174 2837 2830 3211 -365 41 -166 C ATOM 1053 C TYR A 174 11.980 -35.325 16.046 1.00 18.63 C ANISOU 1053 C TYR A 174 2245 2236 2599 -327 -63 -121 C ATOM 1054 O TYR A 174 13.108 -35.270 16.533 1.00 13.94 O ANISOU 1054 O TYR A 174 1683 1642 1972 -343 -84 -86 O ATOM 1055 CB TYR A 174 11.064 -37.654 15.898 1.00 22.55 C ANISOU 1055 CB TYR A 174 2756 2707 3103 -367 58 -116 C ATOM 1056 CG TYR A 174 12.374 -38.327 16.220 1.00 22.85 C ANISOU 1056 CG TYR A 174 2875 2717 3090 -383 53 -41 C ATOM 1057 CD1 TYR A 174 12.579 -38.918 17.458 1.00 22.29 C ANISOU 1057 CD1 TYR A 174 2912 2625 2933 -419 115 -8 C ATOM 1058 CD2 TYR A 174 13.418 -38.338 15.306 1.00 22.84 C ANISOU 1058 CD2 TYR A 174 2861 2724 3094 -344 -23 2 C ATOM 1059 CE1 TYR A 174 13.779 -39.517 17.772 1.00 22.37 C ANISOU 1059 CE1 TYR A 174 3011 2623 2867 -370 67 73 C ATOM 1060 CE2 TYR A 174 14.623 -38.940 15.610 1.00 23.12 C ANISOU 1060 CE2 TYR A 174 2959 2761 3063 -309 -55 66 C ATOM 1061 CZ TYR A 174 14.797 -39.528 16.846 1.00 22.34 C ANISOU 1061 CZ TYR A 174 2964 2638 2885 -308 -21 100 C ATOM 1062 OH TYR A 174 15.993 -40.129 17.160 1.00 22.59 O ANISOU 1062 OH TYR A 174 3059 2671 2853 -243 -78 153 O ATOM 1063 N LEU A 175 11.595 -34.562 15.029 1.00 19.14 N ANISOU 1063 N LEU A 175 2284 2308 2680 -282 -107 -136 N ATOM 1064 CA LEU A 175 12.469 -33.527 14.492 1.00 18.79 C ANISOU 1064 CA LEU A 175 2261 2268 2611 -255 -160 -111 C ATOM 1065 C LEU A 175 12.740 -32.456 15.549 1.00 20.34 C ANISOU 1065 C LEU A 175 2471 2454 2802 -266 -180 -135 C ATOM 1066 O LEU A 175 13.838 -31.906 15.622 1.00 20.52 O ANISOU 1066 O LEU A 175 2518 2485 2794 -267 -205 -106 O ATOM 1067 CB LEU A 175 11.868 -32.902 13.232 1.00 19.38 C ANISOU 1067 CB LEU A 175 2324 2321 2720 -209 -208 -119 C ATOM 1068 CG LEU A 175 11.855 -33.770 11.971 1.00 18.65 C ANISOU 1068 CG LEU A 175 2226 2240 2619 -198 -204 -94 C ATOM 1069 CD1 LEU A 175 11.370 -32.968 10.773 1.00 18.32 C ANISOU 1069 CD1 LEU A 175 2190 2163 2610 -158 -276 -98 C ATOM 1070 CD2 LEU A 175 13.232 -34.355 11.700 1.00 16.27 C ANISOU 1070 CD2 LEU A 175 1948 1965 2267 -211 -185 -44 C ATOM 1071 N ARG A 176 11.732 -32.174 16.371 1.00 20.54 N ANISOU 1071 N ARG A 176 2470 2465 2869 -268 -165 -206 N ATOM 1072 CA ARG A 176 11.878 -31.239 17.481 1.00 19.06 C ANISOU 1072 CA ARG A 176 2295 2271 2677 -278 -176 -256 C ATOM 1073 C ARG A 176 12.798 -31.805 18.558 1.00 19.36 C ANISOU 1073 C ARG A 176 2367 2335 2654 -335 -149 -241 C ATOM 1074 O ARG A 176 13.548 -31.069 19.197 1.00 19.62 O ANISOU 1074 O ARG A 176 2433 2378 2645 -341 -186 -243 O ATOM 1075 CB ARG A 176 10.514 -30.901 18.086 1.00 18.45 C ANISOU 1075 CB ARG A 176 2156 2196 2659 -257 -134 -379 C ATOM 1076 CG ARG A 176 9.628 -30.046 17.194 1.00 18.68 C ANISOU 1076 CG ARG A 176 2141 2190 2765 -178 -196 -428 C ATOM 1077 CD ARG A 176 8.305 -29.721 17.871 1.00 19.00 C ANISOU 1077 CD ARG A 176 2089 2253 2876 -148 -153 -582 C ATOM 1078 NE ARG A 176 7.444 -28.904 17.021 1.00 19.79 N ANISOU 1078 NE ARG A 176 2136 2316 3067 -49 -241 -645 N ATOM 1079 CZ ARG A 176 7.460 -27.575 16.999 1.00 20.33 C ANISOU 1079 CZ ARG A 176 2230 2325 3169 17 -336 -672 C ATOM 1080 NH1 ARG A 176 8.295 -26.908 17.783 1.00 19.77 N ANISOU 1080 NH1 ARG A 176 2233 2234 3044 -15 -339 -644 N ATOM 1081 NH2 ARG A 176 6.643 -26.913 16.193 1.00 22.08 N ANISOU 1081 NH2 ARG A 176 2408 2504 3476 119 -439 -731 N ATOM 1082 N LEU A 177 12.733 -33.116 18.758 1.00 20.61 N ANISOU 1082 N LEU A 177 2546 2514 2773 -357 -78 -203 N ATOM 1083 CA LEU A 177 13.587 -33.779 19.736 1.00 21.90 C ANISOU 1083 CA LEU A 177 2788 2706 2825 -367 -54 -144 C ATOM 1084 C LEU A 177 15.036 -33.802 19.267 1.00 22.60 C ANISOU 1084 C LEU A 177 2889 2812 2887 -342 -140 -73 C ATOM 1085 O LEU A 177 15.958 -33.674 20.072 1.00 25.07 O ANISOU 1085 O LEU A 177 3242 3161 3122 -331 -173 -56 O ATOM 1086 CB LEU A 177 13.093 -35.201 20.005 1.00 23.61 C ANISOU 1086 CB LEU A 177 3055 2912 3004 -397 38 -115 C ATOM 1087 CG LEU A 177 11.727 -35.312 20.682 1.00 23.92 C ANISOU 1087 CG LEU A 177 3082 2956 3048 -455 156 -199 C ATOM 1088 CD1 LEU A 177 11.285 -36.763 20.754 1.00 24.36 C ANISOU 1088 CD1 LEU A 177 3202 2983 3071 -511 253 -163 C ATOM 1089 CD2 LEU A 177 11.767 -34.690 22.067 1.00 24.90 C ANISOU 1089 CD2 LEU A 177 3257 3120 3085 -473 187 -240 C ATOM 1090 N LEU A 178 15.231 -33.974 17.963 1.00 21.57 N ANISOU 1090 N LEU A 178 2716 2667 2814 -333 -175 -45 N ATOM 1091 CA LEU A 178 16.561 -33.908 17.369 1.00 21.14 C ANISOU 1091 CA LEU A 178 2647 2645 2742 -323 -240 -3 C ATOM 1092 C LEU A 178 17.146 -32.518 17.567 1.00 23.89 C ANISOU 1092 C LEU A 178 2986 3009 3083 -313 -263 -33 C ATOM 1093 O LEU A 178 18.292 -32.365 17.989 1.00 27.13 O ANISOU 1093 O LEU A 178 3393 3466 3449 -314 -297 -29 O ATOM 1094 CB LEU A 178 16.497 -34.223 15.875 1.00 20.47 C ANISOU 1094 CB LEU A 178 2530 2552 2697 -284 -219 12 C ATOM 1095 CG LEU A 178 16.217 -35.674 15.490 1.00 21.45 C ANISOU 1095 CG LEU A 178 2656 2660 2834 -287 -200 40 C ATOM 1096 CD1 LEU A 178 16.097 -35.816 13.980 1.00 20.23 C ANISOU 1096 CD1 LEU A 178 2475 2509 2702 -252 -183 34 C ATOM 1097 CD2 LEU A 178 17.312 -36.569 16.032 1.00 20.72 C ANISOU 1097 CD2 LEU A 178 2594 2596 2683 -265 -227 79 C ATOM 1098 N THR A 179 16.340 -31.510 17.253 1.00 22.77 N ANISOU 1098 N THR A 179 2837 2826 2987 -304 -249 -72 N ATOM 1099 CA THR A 179 16.733 -30.117 17.395 1.00 19.95 C ANISOU 1099 CA THR A 179 2489 2459 2630 -312 -271 -99 C ATOM 1100 C THR A 179 17.097 -29.805 18.841 1.00 21.49 C ANISOU 1100 C THR A 179 2700 2680 2788 -334 -293 -138 C ATOM 1101 O THR A 179 18.143 -29.217 19.116 1.00 24.42 O ANISOU 1101 O THR A 179 3068 3078 3133 -346 -315 -145 O ATOM 1102 CB THR A 179 15.596 -29.184 16.946 1.00 16.90 C ANISOU 1102 CB THR A 179 2116 2015 2292 -299 -276 -131 C ATOM 1103 OG1 THR A 179 15.211 -29.514 15.605 1.00 16.94 O ANISOU 1103 OG1 THR A 179 2118 2002 2316 -275 -276 -94 O ATOM 1104 CG2 THR A 179 16.033 -27.730 17.006 1.00 15.20 C ANISOU 1104 CG2 THR A 179 1934 1764 2079 -314 -310 -146 C ATOM 1105 N SER A 180 16.229 -30.211 19.761 1.00 19.72 N ANISOU 1105 N SER A 180 2496 2450 2549 -352 -281 -174 N ATOM 1106 CA SER A 180 16.451 -29.982 21.183 1.00 22.58 C ANISOU 1106 CA SER A 180 2898 2850 2833 -373 -286 -218 C ATOM 1107 C SER A 180 17.673 -30.738 21.687 1.00 24.24 C ANISOU 1107 C SER A 180 3132 3131 2948 -361 -314 -168 C ATOM 1108 O SER A 180 18.444 -30.220 22.494 1.00 24.30 O ANISOU 1108 O SER A 180 3151 3184 2898 -367 -358 -200 O ATOM 1109 CB SER A 180 15.222 -30.402 21.985 1.00 23.88 C ANISOU 1109 CB SER A 180 3080 3015 2977 -366 -197 -264 C ATOM 1110 OG SER A 180 15.504 -30.407 23.373 1.00 25.58 O ANISOU 1110 OG SER A 180 3353 3282 3084 -373 -176 -289 O ATOM 1111 N GLY A 181 17.838 -31.967 21.209 1.00 23.94 N ANISOU 1111 N GLY A 181 3098 3101 2898 -335 -299 -101 N ATOM 1112 CA GLY A 181 18.969 -32.790 21.590 1.00 25.24 C ANISOU 1112 CA GLY A 181 3284 3322 2983 -293 -345 -61 C ATOM 1113 C GLY A 181 20.290 -32.154 21.206 1.00 26.66 C ANISOU 1113 C GLY A 181 3392 3558 3181 -298 -417 -86 C ATOM 1114 O GLY A 181 21.240 -32.157 21.989 1.00 28.38 O ANISOU 1114 O GLY A 181 3608 3838 3339 -260 -464 -110 O ATOM 1115 N TYR A 182 20.346 -31.602 19.999 1.00 24.94 N ANISOU 1115 N TYR A 182 3115 3305 3056 -310 -382 -87 N ATOM 1116 CA TYR A 182 21.550 -30.937 19.520 1.00 24.43 C ANISOU 1116 CA TYR A 182 2992 3271 3021 -309 -387 -120 C ATOM 1117 C TYR A 182 21.837 -29.658 20.306 1.00 25.52 C ANISOU 1117 C TYR A 182 3132 3406 3157 -335 -406 -178 C ATOM 1118 O TYR A 182 22.984 -29.386 20.659 1.00 27.34 O ANISOU 1118 O TYR A 182 3327 3682 3379 -331 -445 -218 O ATOM 1119 CB TYR A 182 21.440 -30.626 18.025 1.00 26.39 C ANISOU 1119 CB TYR A 182 3222 3476 3330 -328 -340 -99 C ATOM 1120 CG TYR A 182 22.695 -30.013 17.447 1.00 30.26 C ANISOU 1120 CG TYR A 182 3668 3991 3839 -356 -343 -128 C ATOM 1121 CD1 TYR A 182 23.736 -30.813 16.994 1.00 31.48 C ANISOU 1121 CD1 TYR A 182 3769 4201 3992 -337 -356 -136 C ATOM 1122 CD2 TYR A 182 22.844 -28.633 17.360 1.00 30.94 C ANISOU 1122 CD2 TYR A 182 3769 4041 3945 -409 -337 -150 C ATOM 1123 CE1 TYR A 182 24.887 -30.258 16.470 1.00 33.22 C ANISOU 1123 CE1 TYR A 182 3945 4447 4229 -384 -356 -162 C ATOM 1124 CE2 TYR A 182 23.991 -28.070 16.838 1.00 32.92 C ANISOU 1124 CE2 TYR A 182 3987 4312 4207 -462 -337 -169 C ATOM 1125 CZ TYR A 182 25.010 -28.887 16.397 1.00 35.36 C ANISOU 1125 CZ TYR A 182 4237 4687 4512 -455 -341 -175 C ATOM 1126 OH TYR A 182 26.154 -28.331 15.873 1.00 39.06 O ANISOU 1126 OH TYR A 182 4667 5194 4983 -527 -329 -199 O ATOM 1127 N LEU A 183 20.792 -28.877 20.572 1.00 24.52 N ANISOU 1127 N LEU A 183 3045 3221 3052 -359 -387 -193 N ATOM 1128 CA LEU A 183 20.933 -27.615 21.294 1.00 22.82 C ANISOU 1128 CA LEU A 183 2838 2989 2843 -384 -406 -257 C ATOM 1129 C LEU A 183 21.511 -27.818 22.689 1.00 26.79 C ANISOU 1129 C LEU A 183 3352 3561 3266 -366 -457 -297 C ATOM 1130 O LEU A 183 22.449 -27.125 23.087 1.00 28.87 O ANISOU 1130 O LEU A 183 3594 3842 3532 -376 -497 -343 O ATOM 1131 CB LEU A 183 19.586 -26.891 21.388 1.00 19.57 C ANISOU 1131 CB LEU A 183 2464 2503 2469 -392 -384 -285 C ATOM 1132 CG LEU A 183 19.041 -26.259 20.106 1.00 18.75 C ANISOU 1132 CG LEU A 183 2369 2325 2430 -402 -356 -259 C ATOM 1133 CD1 LEU A 183 17.614 -25.773 20.310 1.00 18.07 C ANISOU 1133 CD1 LEU A 183 2316 2178 2374 -391 -346 -298 C ATOM 1134 CD2 LEU A 183 19.933 -25.118 19.645 1.00 16.63 C ANISOU 1134 CD2 LEU A 183 2105 2032 2182 -447 -365 -269 C ATOM 1135 N GLN A 184 20.946 -28.766 23.430 1.00 28.22 N ANISOU 1135 N GLN A 184 3584 3775 3364 -345 -459 -278 N ATOM 1136 CA GLN A 184 21.432 -29.085 24.767 1.00 31.25 C ANISOU 1136 CA GLN A 184 4010 4231 3634 -313 -505 -306 C ATOM 1137 C GLN A 184 22.835 -29.675 24.710 1.00 32.75 C ANISOU 1137 C GLN A 184 4156 4481 3807 -255 -570 -297 C ATOM 1138 O GLN A 184 23.659 -29.427 25.593 1.00 33.20 O ANISOU 1138 O GLN A 184 4231 4567 3817 -237 -638 -329 O ATOM 1139 CB GLN A 184 20.494 -30.071 25.457 1.00 33.75 C ANISOU 1139 CB GLN A 184 4428 4559 3838 -310 -474 -271 C ATOM 1140 CG GLN A 184 19.075 -29.584 25.628 1.00 36.56 C ANISOU 1140 CG GLN A 184 4817 4855 4218 -355 -392 -310 C ATOM 1141 CD GLN A 184 18.260 -30.524 26.486 1.00 40.42 C ANISOU 1141 CD GLN A 184 5401 5348 4607 -338 -311 -283 C ATOM 1142 OE1 GLN A 184 18.727 -30.987 27.526 1.00 43.02 O ANISOU 1142 OE1 GLN A 184 5816 5729 4799 -313 -336 -269 O ATOM 1143 NE2 GLN A 184 17.042 -30.822 26.051 1.00 41.22 N ANISOU 1143 NE2 GLN A 184 5495 5396 4769 -359 -215 -280 N ATOM 1144 N ARG A 185 23.098 -30.466 23.675 1.00 33.63 N ANISOU 1144 N ARG A 185 4225 4592 3961 -234 -559 -250 N ATOM 1145 CA ARG A 185 24.414 -31.075 23.492 1.00 35.80 C ANISOU 1145 CA ARG A 185 4468 4892 4241 -191 -626 -237 C ATOM 1146 C ARG A 185 25.466 -30.000 23.243 1.00 37.81 C ANISOU 1146 C ARG A 185 4654 5153 4558 -257 -644 -277 C ATOM 1147 O ARG A 185 26.580 -30.078 23.765 1.00 40.77 O ANISOU 1147 O ARG A 185 4996 5598 4898 -257 -695 -294 O ATOM 1148 CB ARG A 185 24.395 -32.064 22.322 1.00 37.61 C ANISOU 1148 CB ARG A 185 4661 5114 4513 -163 -599 -194 C ATOM 1149 CG ARG A 185 25.705 -32.837 22.137 1.00 42.84 C ANISOU 1149 CG ARG A 185 5276 5834 5165 -152 -653 -163 C ATOM 1150 CD ARG A 185 26.174 -32.858 20.674 1.00 46.81 C ANISOU 1150 CD ARG A 185 5695 6328 5763 -174 -613 -174 C ATOM 1151 NE ARG A 185 25.431 -33.800 19.832 1.00 49.56 N ANISOU 1151 NE ARG A 185 6062 6638 6131 -141 -580 -132 N ATOM 1152 CZ ARG A 185 25.632 -33.970 18.525 1.00 51.35 C ANISOU 1152 CZ ARG A 185 6233 6858 6421 -159 -536 -136 C ATOM 1153 NH1 ARG A 185 26.555 -33.263 17.886 1.00 52.63 N ANISOU 1153 NH1 ARG A 185 6324 7052 6619 -214 -509 -173 N ATOM 1154 NH2 ARG A 185 24.903 -34.851 17.851 1.00 50.28 N ANISOU 1154 NH2 ARG A 185 6115 6693 6295 -127 -510 -107 N ATOM 1155 N GLU A 186 25.104 -28.999 22.442 1.00 40.36 N ANISOU 1155 N GLU A 186 4348 5675 5312 -662 -490 329 N ATOM 1156 CA GLU A 186 25.996 -27.880 22.164 1.00 39.13 C ANISOU 1156 CA GLU A 186 4186 5587 5093 -742 -448 238 C ATOM 1157 C GLU A 186 25.586 -26.654 22.967 1.00 37.89 C ANISOU 1157 C GLU A 186 4183 5440 4775 -861 -431 258 C ATOM 1158 O GLU A 186 25.580 -25.537 22.450 1.00 38.34 O ANISOU 1158 O GLU A 186 4325 5475 4765 -926 -353 193 O ATOM 1159 CB GLU A 186 25.987 -27.546 20.671 1.00 39.32 C ANISOU 1159 CB GLU A 186 4214 5558 5165 -735 -337 138 C ATOM 1160 CG GLU A 186 26.466 -28.678 19.787 1.00 41.89 C ANISOU 1160 CG GLU A 186 4385 5880 5651 -636 -331 83 C ATOM 1161 CD GLU A 186 27.907 -29.048 20.059 1.00 47.05 C ANISOU 1161 CD GLU A 186 4855 6635 6388 -615 -400 36 C ATOM 1162 OE1 GLU A 186 28.743 -28.128 20.180 1.00 46.72 O ANISOU 1162 OE1 GLU A 186 4802 6662 6289 -711 -391 0 O ATOM 1163 OE2 GLU A 186 28.202 -30.257 20.159 1.00 50.94 O ANISOU 1163 OE2 GLU A 186 5214 7146 6995 -496 -467 30 O ATOM 1164 N SER A 187 25.260 -26.871 24.237 1.00 37.18 N ANISOU 1164 N SER A 187 4137 5377 4613 -897 -508 349 N ATOM 1165 CA SER A 187 24.739 -25.816 25.101 1.00 35.60 C ANISOU 1165 CA SER A 187 4087 5181 4258 -1014 -482 352 C ATOM 1166 C SER A 187 25.709 -24.649 25.272 1.00 34.40 C ANISOU 1166 C SER A 187 3949 5107 4016 -1111 -465 287 C ATOM 1167 O SER A 187 25.284 -23.507 25.429 1.00 33.53 O ANISOU 1167 O SER A 187 3974 4963 3804 -1192 -398 243 O ATOM 1168 CB SER A 187 24.337 -26.388 26.466 1.00 38.06 C ANISOU 1168 CB SER A 187 4442 5526 4494 -1066 -573 463 C ATOM 1169 OG SER A 187 25.455 -26.937 27.144 1.00 42.02 O ANISOU 1169 OG SER A 187 4845 6130 4992 -1058 -708 524 O ATOM 1170 N LYS A 188 27.007 -24.934 25.235 1.00 34.65 N ANISOU 1170 N LYS A 188 3834 5235 4097 -1101 -528 267 N ATOM 1171 CA LYS A 188 28.015 -23.883 25.366 1.00 37.77 C ANISOU 1171 CA LYS A 188 4219 5714 4420 -1207 -509 193 C ATOM 1172 C LYS A 188 27.962 -22.881 24.222 1.00 37.32 C ANISOU 1172 C LYS A 188 4240 5593 4345 -1252 -381 110 C ATOM 1173 O LYS A 188 28.142 -21.681 24.430 1.00 39.73 O ANISOU 1173 O LYS A 188 4650 5911 4537 -1368 -331 69 O ATOM 1174 CB LYS A 188 29.421 -24.478 25.487 1.00 41.95 C ANISOU 1174 CB LYS A 188 4541 6361 5037 -1172 -610 163 C ATOM 1175 CG LYS A 188 29.792 -24.866 26.907 1.00 46.67 C ANISOU 1175 CG LYS A 188 5105 7051 5576 -1184 -763 234 C ATOM 1176 CD LYS A 188 29.502 -23.709 27.858 1.00 48.47 C ANISOU 1176 CD LYS A 188 5496 7304 5617 -1342 -729 240 C ATOM 1177 CE LYS A 188 29.358 -24.165 29.302 1.00 50.72 C ANISOU 1177 CE LYS A 188 5826 7641 5804 -1367 -861 342 C ATOM 1178 NZ LYS A 188 28.722 -23.091 30.123 1.00 50.96 N ANISOU 1178 NZ LYS A 188 6044 7660 5658 -1523 -785 338 N ATOM 1179 N PHE A 189 27.720 -23.378 23.014 1.00 34.67 N ANISOU 1179 N PHE A 189 3869 5190 4113 -1167 -333 88 N ATOM 1180 CA PHE A 189 27.605 -22.512 21.848 1.00 34.77 C ANISOU 1180 CA PHE A 189 3980 5140 4091 -1214 -229 28 C ATOM 1181 C PHE A 189 26.326 -21.680 21.891 1.00 33.34 C ANISOU 1181 C PHE A 189 4004 4841 3824 -1230 -189 45 C ATOM 1182 O PHE A 189 26.369 -20.453 21.792 1.00 34.86 O ANISOU 1182 O PHE A 189 4329 5006 3909 -1328 -141 9 O ATOM 1183 CB PHE A 189 27.639 -23.344 20.562 1.00 35.60 C ANISOU 1183 CB PHE A 189 3998 5210 4319 -1128 -195 3 C ATOM 1184 CG PHE A 189 27.467 -22.534 19.308 1.00 37.32 C ANISOU 1184 CG PHE A 189 4338 5367 4473 -1189 -101 -43 C ATOM 1185 CD1 PHE A 189 28.549 -21.891 18.731 1.00 40.45 C ANISOU 1185 CD1 PHE A 189 4722 5836 4812 -1306 -39 -114 C ATOM 1186 CD2 PHE A 189 26.225 -22.423 18.702 1.00 35.96 C ANISOU 1186 CD2 PHE A 189 4299 5074 4289 -1142 -81 -19 C ATOM 1187 CE1 PHE A 189 28.394 -21.147 17.576 1.00 41.65 C ANISOU 1187 CE1 PHE A 189 5020 5935 4872 -1385 44 -150 C ATOM 1188 CE2 PHE A 189 26.066 -21.680 17.548 1.00 37.10 C ANISOU 1188 CE2 PHE A 189 4578 5163 4357 -1207 -18 -52 C ATOM 1189 CZ PHE A 189 27.152 -21.042 16.985 1.00 40.24 C ANISOU 1189 CZ PHE A 189 4989 5628 4673 -1334 46 -111 C ATOM 1190 N PHE A 190 25.191 -22.359 22.043 1.00 28.81 N ANISOU 1190 N PHE A 190 3448 4193 3305 -1134 -212 90 N ATOM 1191 CA PHE A 190 23.885 -21.716 21.929 1.00 25.48 C ANISOU 1191 CA PHE A 190 3183 3649 2850 -1120 -179 82 C ATOM 1192 C PHE A 190 23.478 -20.884 23.144 1.00 25.18 C ANISOU 1192 C PHE A 190 3254 3606 2708 -1194 -180 77 C ATOM 1193 O PHE A 190 22.525 -20.110 23.071 1.00 23.93 O ANISOU 1193 O PHE A 190 3224 3340 2527 -1194 -146 42 O ATOM 1194 CB PHE A 190 22.807 -22.752 21.602 1.00 24.27 C ANISOU 1194 CB PHE A 190 2990 3425 2807 -1001 -191 108 C ATOM 1195 CG PHE A 190 22.989 -23.408 20.264 1.00 21.83 C ANISOU 1195 CG PHE A 190 2609 3096 2590 -937 -172 95 C ATOM 1196 CD1 PHE A 190 22.641 -22.742 19.101 1.00 19.45 C ANISOU 1196 CD1 PHE A 190 2409 2719 2264 -952 -135 60 C ATOM 1197 CD2 PHE A 190 23.510 -24.688 20.168 1.00 22.78 C ANISOU 1197 CD2 PHE A 190 2573 3268 2813 -871 -198 116 C ATOM 1198 CE1 PHE A 190 22.810 -23.339 17.868 1.00 18.88 C ANISOU 1198 CE1 PHE A 190 2284 2640 2251 -919 -113 43 C ATOM 1199 CE2 PHE A 190 23.679 -25.291 18.936 1.00 21.59 C ANISOU 1199 CE2 PHE A 190 2356 3099 2748 -821 -167 83 C ATOM 1200 CZ PHE A 190 23.329 -24.615 17.784 1.00 20.45 C ANISOU 1200 CZ PHE A 190 2314 2895 2560 -853 -120 47 C ATOM 1201 N GLU A 191 24.193 -21.042 24.255 1.00 27.90 N ANISOU 1201 N GLU A 191 3544 4062 2994 -1260 -221 103 N ATOM 1202 CA GLU A 191 23.951 -20.216 25.438 1.00 26.99 C ANISOU 1202 CA GLU A 191 3537 3960 2759 -1359 -210 87 C ATOM 1203 C GLU A 191 24.203 -18.746 25.134 1.00 25.87 C ANISOU 1203 C GLU A 191 3520 3770 2539 -1447 -147 20 C ATOM 1204 O GLU A 191 23.540 -17.866 25.681 1.00 25.60 O ANISOU 1204 O GLU A 191 3618 3667 2444 -1494 -107 -20 O ATOM 1205 CB GLU A 191 24.836 -20.655 26.603 1.00 29.02 C ANISOU 1205 CB GLU A 191 3712 4360 2954 -1433 -281 136 C ATOM 1206 CG GLU A 191 24.136 -21.544 27.616 1.00 33.59 C ANISOU 1206 CG GLU A 191 4292 4959 3512 -1426 -330 204 C ATOM 1207 CD GLU A 191 25.109 -22.275 28.523 1.00 39.33 C ANISOU 1207 CD GLU A 191 4918 5821 4206 -1470 -444 283 C ATOM 1208 OE1 GLU A 191 26.297 -21.889 28.564 1.00 41.22 O ANISOU 1208 OE1 GLU A 191 5084 6148 4430 -1514 -476 256 O ATOM 1209 OE2 GLU A 191 24.686 -23.242 29.191 1.00 41.84 O ANISOU 1209 OE2 GLU A 191 5230 6153 4513 -1461 -512 369 O ATOM 1210 N HIS A 192 25.166 -18.490 24.256 1.00 26.34 N ANISOU 1210 N HIS A 192 3544 3862 2603 -1478 -131 2 N ATOM 1211 CA HIS A 192 25.527 -17.127 23.889 1.00 26.68 C ANISOU 1211 CA HIS A 192 3720 3860 2558 -1586 -70 -52 C ATOM 1212 C HIS A 192 24.373 -16.411 23.197 1.00 28.23 C ANISOU 1212 C HIS A 192 4086 3875 2764 -1540 -34 -70 C ATOM 1213 O HIS A 192 24.277 -15.187 23.241 1.00 31.35 O ANISOU 1213 O HIS A 192 4639 4187 3086 -1617 7 -106 O ATOM 1214 CB HIS A 192 26.749 -17.129 22.972 1.00 25.35 C ANISOU 1214 CB HIS A 192 3474 3768 2389 -1640 -48 -77 C ATOM 1215 CG HIS A 192 27.952 -17.795 23.564 1.00 27.25 C ANISOU 1215 CG HIS A 192 3522 4178 2653 -1673 -94 -78 C ATOM 1216 ND1 HIS A 192 28.511 -17.399 24.760 1.00 29.25 N ANISOU 1216 ND1 HIS A 192 3758 4525 2830 -1772 -120 -88 N ATOM 1217 CD2 HIS A 192 28.712 -18.823 23.117 1.00 27.18 C ANISOU 1217 CD2 HIS A 192 3324 4257 2748 -1616 -127 -78 C ATOM 1218 CE1 HIS A 192 29.558 -18.157 25.027 1.00 29.15 C ANISOU 1218 CE1 HIS A 192 3550 4653 2874 -1768 -185 -90 C ATOM 1219 NE2 HIS A 192 29.702 -19.029 24.045 1.00 27.76 N ANISOU 1219 NE2 HIS A 192 3261 4470 2816 -1669 -189 -88 N ATOM 1220 N PHE A 193 23.497 -17.183 22.561 1.00 27.90 N ANISOU 1220 N PHE A 193 4012 3765 2824 -1413 -58 -46 N ATOM 1221 CA PHE A 193 22.402 -16.614 21.785 1.00 25.74 C ANISOU 1221 CA PHE A 193 3881 3317 2583 -1353 -49 -61 C ATOM 1222 C PHE A 193 21.078 -16.610 22.544 1.00 26.42 C ANISOU 1222 C PHE A 193 3999 3313 2726 -1281 -58 -90 C ATOM 1223 O PHE A 193 20.082 -16.069 22.065 1.00 28.74 O ANISOU 1223 O PHE A 193 4404 3448 3069 -1215 -66 -122 O ATOM 1224 CB PHE A 193 22.248 -17.360 20.460 1.00 21.49 C ANISOU 1224 CB PHE A 193 3296 2753 2115 -1274 -67 -35 C ATOM 1225 CG PHE A 193 23.482 -17.332 19.604 1.00 21.57 C ANISOU 1225 CG PHE A 193 3280 2845 2069 -1356 -36 -35 C ATOM 1226 CD1 PHE A 193 23.694 -16.300 18.705 1.00 20.21 C ANISOU 1226 CD1 PHE A 193 3284 2594 1801 -1439 -3 -48 C ATOM 1227 CD2 PHE A 193 24.429 -18.338 19.696 1.00 20.35 C ANISOU 1227 CD2 PHE A 193 2932 2839 1959 -1354 -39 -30 C ATOM 1228 CE1 PHE A 193 24.827 -16.272 17.915 1.00 21.08 C ANISOU 1228 CE1 PHE A 193 3374 2789 1846 -1540 45 -70 C ATOM 1229 CE2 PHE A 193 25.564 -18.316 18.909 1.00 20.91 C ANISOU 1229 CE2 PHE A 193 2960 2988 1995 -1433 3 -59 C ATOM 1230 CZ PHE A 193 25.763 -17.280 18.017 1.00 22.10 C ANISOU 1230 CZ PHE A 193 3284 3077 2035 -1537 55 -86 C ATOM 1231 N ILE A 194 21.070 -17.210 23.729 1.00 26.45 N ANISOU 1231 N ILE A 194 3912 3417 2722 -1297 -60 -86 N ATOM 1232 CA ILE A 194 19.870 -17.240 24.556 1.00 27.23 C ANISOU 1232 CA ILE A 194 4035 3456 2857 -1260 -42 -136 C ATOM 1233 C ILE A 194 20.068 -16.387 25.800 1.00 29.89 C ANISOU 1233 C ILE A 194 4449 3821 3086 -1374 1 -183 C ATOM 1234 O ILE A 194 21.040 -16.565 26.533 1.00 33.19 O ANISOU 1234 O ILE A 194 4822 4380 3409 -1470 -9 -146 O ATOM 1235 CB ILE A 194 19.510 -18.673 24.980 1.00 28.91 C ANISOU 1235 CB ILE A 194 4110 3751 3123 -1210 -63 -98 C ATOM 1236 CG1 ILE A 194 19.371 -19.575 23.752 1.00 27.70 C ANISOU 1236 CG1 ILE A 194 3869 3572 3083 -1102 -98 -56 C ATOM 1237 CG2 ILE A 194 18.227 -18.680 25.800 1.00 30.28 C ANISOU 1237 CG2 ILE A 194 4311 3870 3323 -1199 -16 -175 C ATOM 1238 CD1 ILE A 194 19.135 -21.031 24.092 1.00 27.07 C ANISOU 1238 CD1 ILE A 194 3658 3561 3065 -1053 -116 -5 C ATOM 1239 N GLU A 195 19.143 -15.461 26.032 1.00 30.99 N ANISOU 1239 N GLU A 195 4701 3822 3251 -1356 41 -274 N ATOM 1240 CA GLU A 195 19.242 -14.546 27.162 1.00 36.26 C ANISOU 1240 CA GLU A 195 5454 4497 3828 -1462 97 -339 C ATOM 1241 C GLU A 195 19.273 -15.288 28.493 1.00 40.85 C ANISOU 1241 C GLU A 195 5966 5228 4328 -1543 122 -332 C ATOM 1242 O GLU A 195 18.707 -16.373 28.621 1.00 43.05 O ANISOU 1242 O GLU A 195 6160 5550 4648 -1493 113 -314 O ATOM 1243 CB GLU A 195 18.084 -13.548 27.149 1.00 38.38 C ANISOU 1243 CB GLU A 195 5833 4573 4176 -1389 130 -461 C ATOM 1244 CG GLU A 195 17.986 -12.729 25.874 1.00 40.72 C ANISOU 1244 CG GLU A 195 6240 4696 4536 -1307 82 -457 C ATOM 1245 CD GLU A 195 17.066 -11.535 26.024 1.00 43.72 C ANISOU 1245 CD GLU A 195 6747 4880 4984 -1235 93 -582 C ATOM 1246 OE1 GLU A 195 16.416 -11.155 25.028 1.00 44.81 O ANISOU 1246 OE1 GLU A 195 6954 4849 5224 -1099 28 -601 O ATOM 1247 OE2 GLU A 195 16.999 -10.973 27.137 1.00 45.53 O ANISOU 1247 OE2 GLU A 195 7008 5123 5167 -1308 159 -665 O ATOM 1248 N GLY A 196 19.946 -14.697 29.476 1.00 43.34 N ANISOU 1248 N GLY A 196 6329 5620 4516 -1682 151 -344 N ATOM 1249 CA GLY A 196 20.006 -15.265 30.809 1.00 44.58 C ANISOU 1249 CA GLY A 196 6458 5914 4565 -1788 169 -332 C ATOM 1250 C GLY A 196 18.624 -15.362 31.425 1.00 45.20 C ANISOU 1250 C GLY A 196 6566 5933 4675 -1765 255 -437 C ATOM 1251 O GLY A 196 17.738 -14.569 31.107 1.00 46.76 O ANISOU 1251 O GLY A 196 6818 5979 4970 -1686 309 -554 O ATOM 1252 N GLY A 197 18.440 -16.338 32.307 1.00 44.03 N ANISOU 1252 N GLY A 197 6382 5902 4446 -1837 266 -401 N ATOM 1253 CA GLY A 197 17.146 -16.581 32.916 1.00 44.26 C ANISOU 1253 CA GLY A 197 6424 5902 4491 -1842 376 -512 C ATOM 1254 C GLY A 197 16.680 -18.000 32.663 1.00 43.81 C ANISOU 1254 C GLY A 197 6288 5888 4468 -1796 351 -451 C ATOM 1255 O GLY A 197 15.807 -18.516 33.361 1.00 48.57 O ANISOU 1255 O GLY A 197 6898 6519 5036 -1856 447 -515 O ATOM 1256 N ARG A 198 17.272 -18.630 31.654 1.00 38.64 N ANISOU 1256 N ARG A 198 5557 5238 3888 -1697 234 -335 N ATOM 1257 CA ARG A 198 16.940 -20.000 31.297 1.00 36.63 C ANISOU 1257 CA ARG A 198 5215 5005 3696 -1635 192 -262 C ATOM 1258 C ARG A 198 18.171 -20.733 30.793 1.00 36.19 C ANISOU 1258 C ARG A 198 5085 5024 3641 -1600 44 -98 C ATOM 1259 O ARG A 198 19.007 -20.162 30.095 1.00 34.46 O ANISOU 1259 O ARG A 198 4845 4795 3454 -1558 -6 -75 O ATOM 1260 CB ARG A 198 15.859 -20.035 30.213 1.00 34.27 C ANISOU 1260 CB ARG A 198 4848 4567 3604 -1479 237 -345 C ATOM 1261 CG ARG A 198 14.451 -19.735 30.696 1.00 31.33 C ANISOU 1261 CG ARG A 198 4487 4135 3282 -1489 384 -526 C ATOM 1262 CD ARG A 198 13.457 -19.828 29.547 1.00 29.72 C ANISOU 1262 CD ARG A 198 4190 3805 3296 -1321 390 -611 C ATOM 1263 NE ARG A 198 13.764 -18.874 28.486 1.00 28.51 N ANISOU 1263 NE ARG A 198 4075 3534 3222 -1206 302 -616 N ATOM 1264 CZ ARG A 198 13.087 -18.774 27.347 1.00 28.25 C ANISOU 1264 CZ ARG A 198 4001 3379 3354 -1052 259 -674 C ATOM 1265 NH1 ARG A 198 12.057 -19.576 27.110 1.00 27.35 N ANISOU 1265 NH1 ARG A 198 3769 3256 3366 -982 302 -750 N ATOM 1266 NH2 ARG A 198 13.443 -17.871 26.443 1.00 25.83 N ANISOU 1266 NH2 ARG A 198 3776 2959 3077 -974 171 -657 N ATOM 1267 N THR A 199 18.276 -22.005 31.154 1.00 37.85 N ANISOU 1267 N THR A 199 5254 5302 3826 -1620 -18 9 N ATOM 1268 CA THR A 199 19.287 -22.874 30.584 1.00 39.06 C ANISOU 1268 CA THR A 199 5302 5504 4034 -1559 -153 153 C ATOM 1269 C THR A 199 18.814 -23.244 29.177 1.00 34.38 C ANISOU 1269 C THR A 199 4613 4801 3650 -1380 -130 138 C ATOM 1270 O THR A 199 17.647 -23.042 28.840 1.00 32.57 O ANISOU 1270 O THR A 199 4394 4474 3506 -1322 -32 42 O ATOM 1271 CB THR A 199 19.466 -24.139 31.455 1.00 44.67 C ANISOU 1271 CB THR A 199 6018 6289 4665 -1643 -238 290 C ATOM 1272 OG1 THR A 199 19.725 -23.749 32.809 1.00 48.22 O ANISOU 1272 OG1 THR A 199 6581 6834 4905 -1839 -265 283 O ATOM 1273 CG2 THR A 199 20.626 -25.000 30.962 1.00 46.32 C ANISOU 1273 CG2 THR A 199 6101 6555 4944 -1595 -398 442 C ATOM 1274 N VAL A 200 19.727 -23.747 28.353 1.00 31.31 N ANISOU 1274 N VAL A 200 4122 4435 3341 -1303 -217 219 N ATOM 1275 CA VAL A 200 19.385 -24.280 27.044 1.00 30.32 C ANISOU 1275 CA VAL A 200 3909 4223 3388 -1155 -203 215 C ATOM 1276 C VAL A 200 18.285 -25.337 27.158 1.00 32.45 C ANISOU 1276 C VAL A 200 4159 4435 3736 -1113 -156 231 C ATOM 1277 O VAL A 200 17.409 -25.426 26.297 1.00 32.18 O ANISOU 1277 O VAL A 200 4091 4310 3827 -1018 -98 167 O ATOM 1278 CB VAL A 200 20.624 -24.893 26.358 1.00 28.48 C ANISOU 1278 CB VAL A 200 3561 4046 3216 -1102 -292 293 C ATOM 1279 CG1 VAL A 200 20.262 -25.470 24.998 1.00 24.98 C ANISOU 1279 CG1 VAL A 200 3042 3517 2932 -967 -264 274 C ATOM 1280 CG2 VAL A 200 21.718 -23.847 26.222 1.00 30.11 C ANISOU 1280 CG2 VAL A 200 3779 4311 3351 -1153 -305 258 C ATOM 1281 N LYS A 201 18.322 -26.123 28.231 1.00 34.57 N ANISOU 1281 N LYS A 201 4460 4754 3922 -1199 -182 320 N ATOM 1282 CA LYS A 201 17.328 -27.173 28.442 1.00 36.73 C ANISOU 1282 CA LYS A 201 4741 4965 4249 -1177 -115 342 C ATOM 1283 C LYS A 201 15.941 -26.581 28.666 1.00 36.54 C ANISOU 1283 C LYS A 201 4761 4888 4233 -1190 35 188 C ATOM 1284 O LYS A 201 14.958 -27.037 28.074 1.00 36.94 O ANISOU 1284 O LYS A 201 4754 4867 4416 -1115 109 128 O ATOM 1285 CB LYS A 201 17.702 -28.056 29.635 1.00 39.24 C ANISOU 1285 CB LYS A 201 5138 5333 4439 -1283 -176 487 C ATOM 1286 CG LYS A 201 16.865 -29.329 29.735 1.00 41.49 C ANISOU 1286 CG LYS A 201 5447 5531 4786 -1251 -115 532 C ATOM 1287 CD LYS A 201 16.831 -29.880 31.154 1.00 45.56 C ANISOU 1287 CD LYS A 201 6117 6071 5124 -1372 -128 621 C ATOM 1288 CE LYS A 201 16.357 -31.328 31.177 1.00 48.00 C ANISOU 1288 CE LYS A 201 6466 6276 5497 -1338 -106 711 C ATOM 1289 NZ LYS A 201 17.336 -32.240 30.518 1.00 49.15 N ANISOU 1289 NZ LYS A 201 6550 6376 5750 -1239 -265 880 N ATOM 1290 N GLU A 202 15.869 -25.570 29.528 1.00 35.20 N ANISOU 1290 N GLU A 202 4682 4764 3928 -1298 78 111 N ATOM 1291 CA GLU A 202 14.610 -24.903 29.830 1.00 35.83 C ANISOU 1291 CA GLU A 202 4790 4804 4019 -1330 226 -60 C ATOM 1292 C GLU A 202 14.066 -24.216 28.584 1.00 31.72 C ANISOU 1292 C GLU A 202 4193 4191 3668 -1210 243 -172 C ATOM 1293 O GLU A 202 12.859 -24.197 28.348 1.00 31.69 O ANISOU 1293 O GLU A 202 4134 4131 3775 -1173 339 -305 O ATOM 1294 CB GLU A 202 14.810 -23.892 30.958 1.00 40.41 C ANISOU 1294 CB GLU A 202 5489 5448 4417 -1480 265 -130 C ATOM 1295 CG GLU A 202 15.531 -24.470 32.167 1.00 46.13 C ANISOU 1295 CG GLU A 202 6309 6272 4947 -1613 197 -9 C ATOM 1296 CD GLU A 202 15.596 -23.507 33.338 1.00 51.73 C ANISOU 1296 CD GLU A 202 7143 7047 5464 -1785 246 -106 C ATOM 1297 OE1 GLU A 202 15.330 -22.302 33.143 1.00 52.85 O ANISOU 1297 OE1 GLU A 202 7301 7159 5622 -1796 325 -250 O ATOM 1298 OE2 GLU A 202 15.916 -23.961 34.458 1.00 54.30 O ANISOU 1298 OE2 GLU A 202 7557 7440 5636 -1911 199 -41 O ATOM 1299 N PHE A 203 14.971 -23.649 27.794 1.00 28.69 N ANISOU 1299 N PHE A 203 3808 3793 3300 -1157 142 -128 N ATOM 1300 CA PHE A 203 14.609 -23.041 26.522 1.00 25.20 C ANISOU 1300 CA PHE A 203 3334 3250 2991 -1049 121 -204 C ATOM 1301 C PHE A 203 14.045 -24.085 25.562 1.00 26.06 C ANISOU 1301 C PHE A 203 3331 3318 3252 -943 111 -188 C ATOM 1302 O PHE A 203 13.072 -23.829 24.852 1.00 26.83 O ANISOU 1302 O PHE A 203 3389 3336 3469 -844 129 -301 O ATOM 1303 CB PHE A 203 15.829 -22.361 25.894 1.00 21.25 C ANISOU 1303 CB PHE A 203 2875 2755 2444 -1036 29 -139 C ATOM 1304 CG PHE A 203 15.581 -21.824 24.515 1.00 19.78 C ANISOU 1304 CG PHE A 203 2698 2459 2359 -940 -10 -185 C ATOM 1305 CD1 PHE A 203 14.964 -20.598 24.338 1.00 20.74 C ANISOU 1305 CD1 PHE A 203 2920 2465 2497 -921 2 -305 C ATOM 1306 CD2 PHE A 203 15.970 -22.543 23.395 1.00 18.33 C ANISOU 1306 CD2 PHE A 203 2442 2275 2246 -866 -65 -113 C ATOM 1307 CE1 PHE A 203 14.735 -20.101 23.069 1.00 21.00 C ANISOU 1307 CE1 PHE A 203 3004 2376 2598 -827 -62 -332 C ATOM 1308 CE2 PHE A 203 15.743 -22.049 22.125 1.00 17.00 C ANISOU 1308 CE2 PHE A 203 2317 2008 2135 -800 -108 -149 C ATOM 1309 CZ PHE A 203 15.125 -20.828 21.963 1.00 18.11 C ANISOU 1309 CZ PHE A 203 2582 2025 2274 -781 -118 -249 C ATOM 1310 N CYS A 204 14.664 -25.261 25.543 1.00 25.21 N ANISOU 1310 N CYS A 204 3174 3260 3145 -926 70 -53 N ATOM 1311 CA CYS A 204 14.225 -26.345 24.671 1.00 25.03 C ANISOU 1311 CA CYS A 204 3054 3196 3261 -835 66 -36 C ATOM 1312 C CYS A 204 12.833 -26.843 25.043 1.00 27.07 C ANISOU 1312 C CYS A 204 3272 3428 3587 -841 174 -133 C ATOM 1313 O CYS A 204 11.991 -27.060 24.173 1.00 27.42 O ANISOU 1313 O CYS A 204 3232 3421 3765 -755 188 -222 O ATOM 1314 CB CYS A 204 15.220 -27.505 24.707 1.00 21.73 C ANISOU 1314 CB CYS A 204 2605 2815 2835 -822 5 112 C ATOM 1315 SG CYS A 204 16.732 -27.227 23.761 1.00 26.07 S ANISOU 1315 SG CYS A 204 3122 3401 3380 -771 -99 173 S ATOM 1316 N GLN A 205 12.598 -27.016 26.340 1.00 29.58 N ANISOU 1316 N GLN A 205 3649 3790 3800 -945 251 -128 N ATOM 1317 CA GLN A 205 11.328 -27.537 26.831 1.00 33.33 C ANISOU 1317 CA GLN A 205 4094 4258 4314 -974 378 -226 C ATOM 1318 C GLN A 205 10.197 -26.521 26.709 1.00 34.36 C ANISOU 1318 C GLN A 205 4166 4368 4523 -953 464 -449 C ATOM 1319 O GLN A 205 9.028 -26.863 26.878 1.00 36.94 O ANISOU 1319 O GLN A 205 4418 4697 4922 -951 572 -579 O ATOM 1320 CB GLN A 205 11.463 -27.990 28.286 1.00 38.84 C ANISOU 1320 CB GLN A 205 4903 5010 4845 -1112 436 -158 C ATOM 1321 CG GLN A 205 12.414 -29.158 28.491 1.00 43.13 C ANISOU 1321 CG GLN A 205 5499 5550 5340 -1126 347 44 C ATOM 1322 CD GLN A 205 12.636 -29.477 29.958 1.00 49.47 C ANISOU 1322 CD GLN A 205 6447 6402 5949 -1270 368 120 C ATOM 1323 OE1 GLN A 205 12.509 -28.608 30.822 1.00 51.71 O ANISOU 1323 OE1 GLN A 205 6804 6745 6099 -1368 418 42 O ATOM 1324 NE2 GLN A 205 12.967 -30.731 30.247 1.00 50.29 N ANISOU 1324 NE2 GLN A 205 6609 6469 6030 -1290 325 267 N ATOM 1325 N GLN A 206 10.547 -25.272 26.421 1.00 32.25 N ANISOU 1325 N GLN A 206 3932 4071 4250 -929 411 -506 N ATOM 1326 CA GLN A 206 9.549 -24.217 26.296 1.00 31.70 C ANISOU 1326 CA GLN A 206 3823 3952 4270 -849 453 -716 C ATOM 1327 C GLN A 206 9.352 -23.771 24.851 1.00 31.24 C ANISOU 1327 C GLN A 206 3719 3802 4349 -658 324 -751 C ATOM 1328 O GLN A 206 8.252 -23.379 24.463 1.00 31.16 O ANISOU 1328 O GLN A 206 3619 3743 4477 -540 329 -924 O ATOM 1329 CB GLN A 206 9.928 -23.010 27.160 1.00 31.90 C ANISOU 1329 CB GLN A 206 3971 3980 4169 -930 481 -767 C ATOM 1330 CG GLN A 206 9.885 -23.271 28.657 1.00 34.51 C ANISOU 1330 CG GLN A 206 4362 4405 4346 -1129 621 -780 C ATOM 1331 CD GLN A 206 10.324 -22.068 29.469 1.00 36.89 C ANISOU 1331 CD GLN A 206 4791 4713 4511 -1220 643 -840 C ATOM 1332 OE1 GLN A 206 9.900 -20.942 29.210 1.00 39.27 O ANISOU 1332 OE1 GLN A 206 5099 4931 4891 -1129 645 -995 O ATOM 1333 NE2 GLN A 206 11.184 -22.300 30.454 1.00 36.65 N ANISOU 1333 NE2 GLN A 206 4874 4775 4275 -1392 647 -716 N ATOM 1334 N GLU A 207 10.416 -23.838 24.055 1.00 30.55 N ANISOU 1334 N GLU A 207 3691 3696 4219 -630 204 -596 N ATOM 1335 CA GLU A 207 10.390 -23.241 22.723 1.00 31.05 C ANISOU 1335 CA GLU A 207 3774 3668 4355 -485 79 -611 C ATOM 1336 C GLU A 207 10.616 -24.225 21.574 1.00 29.64 C ANISOU 1336 C GLU A 207 3531 3494 4236 -423 9 -523 C ATOM 1337 O GLU A 207 10.215 -23.957 20.442 1.00 31.90 O ANISOU 1337 O GLU A 207 3812 3713 4595 -299 -84 -567 O ATOM 1338 CB GLU A 207 11.412 -22.102 22.636 1.00 34.84 C ANISOU 1338 CB GLU A 207 4417 4102 4719 -525 14 -547 C ATOM 1339 CG GLU A 207 11.416 -21.160 23.836 1.00 40.30 C ANISOU 1339 CG GLU A 207 5193 4792 5325 -617 88 -624 C ATOM 1340 CD GLU A 207 10.136 -20.352 23.974 1.00 45.91 C ANISOU 1340 CD GLU A 207 5882 5414 6149 -506 118 -830 C ATOM 1341 OE1 GLU A 207 9.350 -20.292 23.005 1.00 48.14 O ANISOU 1341 OE1 GLU A 207 6105 5617 6568 -339 39 -900 O ATOM 1342 OE2 GLU A 207 9.918 -19.772 25.059 1.00 47.77 O ANISOU 1342 OE2 GLU A 207 6153 5661 6337 -584 216 -934 O ATOM 1343 N VAL A 208 11.253 -25.357 21.855 1.00 26.98 N ANISOU 1343 N VAL A 208 3158 3228 3865 -505 45 -404 N ATOM 1344 CA VAL A 208 11.603 -26.300 20.795 1.00 24.90 C ANISOU 1344 CA VAL A 208 2840 2964 3657 -454 -10 -331 C ATOM 1345 C VAL A 208 10.798 -27.601 20.845 1.00 25.79 C ANISOU 1345 C VAL A 208 2837 3091 3870 -446 56 -363 C ATOM 1346 O VAL A 208 10.118 -27.953 19.881 1.00 25.11 O ANISOU 1346 O VAL A 208 2687 2980 3875 -348 23 -429 O ATOM 1347 CB VAL A 208 13.109 -26.630 20.808 1.00 24.20 C ANISOU 1347 CB VAL A 208 2793 2924 3479 -523 -42 -175 C ATOM 1348 CG1 VAL A 208 13.466 -27.521 19.628 1.00 24.18 C ANISOU 1348 CG1 VAL A 208 2729 2914 3544 -463 -85 -134 C ATOM 1349 CG2 VAL A 208 13.930 -25.352 20.780 1.00 22.59 C ANISOU 1349 CG2 VAL A 208 2702 2715 3165 -565 -89 -154 C ATOM 1350 N GLU A 209 10.886 -28.311 21.966 1.00 26.22 N ANISOU 1350 N GLU A 209 2908 3190 3865 -539 138 -299 N ATOM 1351 CA GLU A 209 10.185 -29.588 22.138 1.00 25.17 C ANISOU 1351 CA GLU A 209 2729 3060 3773 -541 204 -299 C ATOM 1352 C GLU A 209 8.655 -29.547 22.009 1.00 25.18 C ANISOU 1352 C GLU A 209 2640 3055 3870 -496 273 -481 C ATOM 1353 O GLU A 209 8.077 -30.427 21.373 1.00 26.38 O ANISOU 1353 O GLU A 209 2741 3193 4091 -446 278 -512 O ATOM 1354 CB GLU A 209 10.587 -30.265 23.456 1.00 26.02 C ANISOU 1354 CB GLU A 209 2907 3194 3787 -668 263 -187 C ATOM 1355 CG GLU A 209 12.027 -30.747 23.484 1.00 28.78 C ANISOU 1355 CG GLU A 209 3299 3542 4094 -693 182 -11 C ATOM 1356 CD GLU A 209 12.392 -31.440 24.781 1.00 32.85 C ANISOU 1356 CD GLU A 209 3897 4058 4525 -802 220 102 C ATOM 1357 OE1 GLU A 209 11.473 -31.845 25.524 1.00 35.88 O ANISOU 1357 OE1 GLU A 209 4314 4439 4880 -867 315 62 O ATOM 1358 OE2 GLU A 209 13.601 -31.578 25.059 1.00 33.45 O ANISOU 1358 OE2 GLU A 209 4023 4156 4532 -819 142 227 O ATOM 1359 N PRO A 210 7.988 -28.547 22.618 1.00 27.32 N ANISOU 1359 N PRO A 210 2886 3340 4153 -518 330 -621 N ATOM 1360 CA PRO A 210 6.527 -28.564 22.484 1.00 26.98 C ANISOU 1360 CA PRO A 210 2721 3304 4228 -465 394 -822 C ATOM 1361 C PRO A 210 6.061 -28.334 21.052 1.00 26.52 C ANISOU 1361 C PRO A 210 2575 3203 4297 -304 270 -907 C ATOM 1362 O PRO A 210 6.647 -27.526 20.332 1.00 26.26 O ANISOU 1362 O PRO A 210 2573 3129 4274 -232 141 -876 O ATOM 1363 CB PRO A 210 6.079 -27.387 23.359 1.00 24.72 C ANISOU 1363 CB PRO A 210 2411 3036 3947 -507 467 -976 C ATOM 1364 CG PRO A 210 7.200 -27.156 24.297 1.00 25.59 C ANISOU 1364 CG PRO A 210 2671 3165 3889 -637 490 -827 C ATOM 1365 CD PRO A 210 8.436 -27.475 23.526 1.00 25.62 C ANISOU 1365 CD PRO A 210 2745 3140 3850 -601 357 -631 C ATOM 1366 N MET A 211 5.013 -29.045 20.650 1.00 25.90 N ANISOU 1366 N MET A 211 2418 3128 4297 -263 295 -1012 N ATOM 1367 CA MET A 211 4.366 -28.791 19.372 1.00 25.64 C ANISOU 1367 CA MET A 211 2321 3055 4365 -123 162 -1117 C ATOM 1368 C MET A 211 3.769 -27.390 19.394 1.00 27.47 C ANISOU 1368 C MET A 211 2489 3263 4687 -44 76 -1285 C ATOM 1369 O MET A 211 3.636 -26.789 20.462 1.00 28.85 O ANISOU 1369 O MET A 211 2634 3461 4868 -102 170 -1363 O ATOM 1370 CB MET A 211 3.268 -29.824 19.113 1.00 27.36 C ANISOU 1370 CB MET A 211 2481 3284 4632 -142 208 -1216 C ATOM 1371 CG MET A 211 3.770 -31.255 19.016 1.00 27.80 C ANISOU 1371 CG MET A 211 2594 3343 4626 -213 270 -1072 C ATOM 1372 SD MET A 211 4.768 -31.539 17.543 1.00 33.91 S ANISOU 1372 SD MET A 211 3433 4078 5375 -129 131 -936 S ATOM 1373 CE MET A 211 3.514 -31.487 16.264 1.00 31.35 C ANISOU 1373 CE MET A 211 3031 3740 5142 -34 26 -1114 C ATOM 1374 N CYS A 212 3.419 -26.883 18.213 1.00 25.79 N ANISOU 1374 N CYS A 212 2263 3019 4517 70 -120 -1314 N ATOM 1375 CA CYS A 212 2.804 -25.561 18.037 1.00 27.80 C ANISOU 1375 CA CYS A 212 2473 3271 4820 182 -258 -1395 C ATOM 1376 C CYS A 212 3.782 -24.390 18.194 1.00 30.05 C ANISOU 1376 C CYS A 212 2893 3495 5030 254 -304 -1287 C ATOM 1377 O CYS A 212 3.455 -23.256 17.846 1.00 34.96 O ANISOU 1377 O CYS A 212 3576 4058 5652 378 -433 -1310 O ATOM 1378 CB CYS A 212 1.583 -25.365 18.953 1.00 31.33 C ANISOU 1378 CB CYS A 212 2787 3765 5352 145 -166 -1582 C ATOM 1379 SG CYS A 212 0.525 -26.822 19.178 1.00 44.00 S ANISOU 1379 SG CYS A 212 4305 5412 7002 25 -26 -1716 S ATOM 1380 N LYS A 213 4.975 -24.660 18.714 1.00 29.50 N ANISOU 1380 N LYS A 213 2926 3406 4877 160 -200 -1176 N ATOM 1381 CA LYS A 213 5.988 -23.619 18.877 1.00 28.58 C ANISOU 1381 CA LYS A 213 3020 3201 4637 157 -241 -1076 C ATOM 1382 C LYS A 213 6.762 -23.377 17.583 1.00 27.34 C ANISOU 1382 C LYS A 213 3017 2971 4401 213 -402 -942 C ATOM 1383 O LYS A 213 7.587 -24.198 17.179 1.00 28.40 O ANISOU 1383 O LYS A 213 3178 3137 4475 129 -387 -825 O ATOM 1384 CB LYS A 213 6.950 -23.972 20.014 1.00 28.22 C ANISOU 1384 CB LYS A 213 3042 3203 4477 -35 -91 -980 C ATOM 1385 CG LYS A 213 6.481 -23.519 21.386 1.00 30.95 C ANISOU 1385 CG LYS A 213 3357 3578 4823 -107 52 -1103 C ATOM 1386 CD LYS A 213 6.382 -22.001 21.450 1.00 33.42 C ANISOU 1386 CD LYS A 213 3778 3795 5126 -10 -17 -1168 C ATOM 1387 CE LYS A 213 5.981 -21.522 22.836 1.00 34.99 C ANISOU 1387 CE LYS A 213 3954 4034 5307 -93 139 -1290 C ATOM 1388 NZ LYS A 213 5.968 -20.033 22.919 1.00 35.83 N ANISOU 1388 NZ LYS A 213 4185 4038 5390 -4 74 -1323 N ATOM 1389 N GLU A 214 6.494 -22.244 16.942 1.00 28.31 N ANISOU 1389 N GLU A 214 3248 3010 4500 337 -545 -941 N ATOM 1390 CA GLU A 214 7.104 -21.932 15.653 1.00 30.16 C ANISOU 1390 CA GLU A 214 3655 3167 4637 376 -696 -825 C ATOM 1391 C GLU A 214 8.609 -21.704 15.765 1.00 30.25 C ANISOU 1391 C GLU A 214 3858 3137 4499 230 -652 -685 C ATOM 1392 O GLU A 214 9.111 -21.278 16.806 1.00 27.59 O ANISOU 1392 O GLU A 214 3567 2798 4119 134 -556 -676 O ATOM 1393 CB GLU A 214 6.419 -20.728 14.999 1.00 33.20 C ANISOU 1393 CB GLU A 214 4139 3457 5019 528 -868 -852 C ATOM 1394 CG GLU A 214 6.722 -20.575 13.515 1.00 36.18 C ANISOU 1394 CG GLU A 214 4682 3765 5298 574 -1044 -760 C ATOM 1395 CD GLU A 214 6.491 -21.860 12.738 1.00 39.80 C ANISOU 1395 CD GLU A 214 5009 4312 5800 572 -1070 -784 C ATOM 1396 OE1 GLU A 214 5.331 -22.130 12.363 1.00 42.14 O ANISOU 1396 OE1 GLU A 214 5160 4659 6192 662 -1159 -902 O ATOM 1397 OE2 GLU A 214 7.469 -22.602 12.503 1.00 39.64 O ANISOU 1397 OE2 GLU A 214 5031 4314 5714 459 -997 -700 O ATOM 1398 N SER A 215 9.318 -21.986 14.678 1.00 31.33 N ANISOU 1398 N SER A 215 4097 3261 4546 194 -719 -584 N ATOM 1399 CA SER A 215 10.774 -21.983 14.672 1.00 30.46 C ANISOU 1399 CA SER A 215 4103 3186 4285 27 -647 -441 C ATOM 1400 C SER A 215 11.376 -20.641 14.266 1.00 32.55 C ANISOU 1400 C SER A 215 4633 3323 4413 -9 -720 -378 C ATOM 1401 O SER A 215 10.778 -19.884 13.500 1.00 35.49 O ANISOU 1401 O SER A 215 5127 3591 4767 108 -850 -386 O ATOM 1402 CB SER A 215 11.278 -23.063 13.714 1.00 28.64 C ANISOU 1402 CB SER A 215 3824 3034 4026 -18 -639 -382 C ATOM 1403 OG SER A 215 10.715 -24.321 14.029 1.00 29.61 O ANISOU 1403 OG SER A 215 3729 3246 4276 7 -574 -439 O ATOM 1404 N ASP A 216 12.563 -20.350 14.791 1.00 32.01 N ANISOU 1404 N ASP A 216 4637 3291 4234 -175 -625 -298 N ATOM 1405 CA ASP A 216 13.366 -19.233 14.300 1.00 32.68 C ANISOU 1405 CA ASP A 216 4955 3302 4161 -260 -642 -216 C ATOM 1406 C ASP A 216 14.762 -19.753 13.951 1.00 27.32 C ANISOU 1406 C ASP A 216 4270 2739 3373 -440 -552 -129 C ATOM 1407 O ASP A 216 14.959 -20.966 13.824 1.00 27.49 O ANISOU 1407 O ASP A 216 4130 2865 3449 -459 -515 -131 O ATOM 1408 CB ASP A 216 13.428 -18.085 15.314 1.00 37.73 C ANISOU 1408 CB ASP A 216 5674 3885 4777 -287 -599 -238 C ATOM 1409 CG ASP A 216 14.369 -18.372 16.469 1.00 42.40 C ANISOU 1409 CG ASP A 216 6173 4602 5335 -448 -465 -221 C ATOM 1410 OD1 ASP A 216 14.009 -19.190 17.339 1.00 42.95 O ANISOU 1410 OD1 ASP A 216 6079 4745 5494 -443 -421 -273 O ATOM 1411 OD2 ASP A 216 15.463 -17.770 16.513 1.00 46.92 O ANISOU 1411 OD2 ASP A 216 6836 5209 5783 -582 -412 -155 O ATOM 1412 N HIS A 217 15.725 -18.849 13.799 1.00 24.29 N ANISOU 1412 N HIS A 217 4036 2347 2845 -564 -508 -66 N ATOM 1413 CA HIS A 217 17.059 -19.222 13.328 1.00 22.04 C ANISOU 1413 CA HIS A 217 3730 2185 2459 -724 -416 -11 C ATOM 1414 C HIS A 217 17.791 -20.241 14.203 1.00 20.78 C ANISOU 1414 C HIS A 217 3328 2200 2369 -780 -318 -17 C ATOM 1415 O HIS A 217 18.627 -20.996 13.707 1.00 21.18 O ANISOU 1415 O HIS A 217 3282 2361 2406 -844 -261 -3 O ATOM 1416 CB HIS A 217 17.925 -17.978 13.117 1.00 24.77 C ANISOU 1416 CB HIS A 217 4271 2501 2638 -853 -377 34 C ATOM 1417 CG HIS A 217 17.555 -17.192 11.898 1.00 27.24 C ANISOU 1417 CG HIS A 217 4850 2667 2833 -838 -471 72 C ATOM 1418 ND1 HIS A 217 18.207 -16.034 11.536 1.00 30.81 N ANISOU 1418 ND1 HIS A 217 5526 3069 3112 -959 -450 109 N ATOM 1419 CD2 HIS A 217 16.606 -17.400 10.957 1.00 28.20 C ANISOU 1419 CD2 HIS A 217 5062 2685 2969 -717 -600 74 C ATOM 1420 CE1 HIS A 217 17.672 -15.559 10.422 1.00 34.18 C ANISOU 1420 CE1 HIS A 217 6188 3359 3439 -918 -567 143 C ATOM 1421 NE2 HIS A 217 16.697 -16.374 10.052 1.00 31.72 N ANISOU 1421 NE2 HIS A 217 5798 3014 3240 -765 -668 127 N ATOM 1422 N ILE A 218 17.482 -20.269 15.495 1.00 20.92 N ANISOU 1422 N ILE A 218 3253 2240 2456 -751 -302 -40 N ATOM 1423 CA ILE A 218 18.152 -21.199 16.400 1.00 21.83 C ANISOU 1423 CA ILE A 218 3168 2509 2618 -786 -236 -24 C ATOM 1424 C ILE A 218 17.655 -22.633 16.194 1.00 21.58 C ANISOU 1424 C ILE A 218 2973 2516 2711 -708 -247 -32 C ATOM 1425 O ILE A 218 18.392 -23.592 16.418 1.00 21.12 O ANISOU 1425 O ILE A 218 2765 2571 2690 -714 -204 -3 O ATOM 1426 CB ILE A 218 18.020 -20.766 17.881 1.00 23.31 C ANISOU 1426 CB ILE A 218 3340 2714 2801 -804 -214 -39 C ATOM 1427 CG1 ILE A 218 19.030 -21.514 18.752 1.00 25.44 C ANISOU 1427 CG1 ILE A 218 3459 3143 3065 -848 -172 1 C ATOM 1428 CG2 ILE A 218 16.600 -20.964 18.388 1.00 22.77 C ANISOU 1428 CG2 ILE A 218 3253 2564 2836 -716 -244 -103 C ATOM 1429 CD1 ILE A 218 19.082 -21.025 20.181 1.00 27.91 C ANISOU 1429 CD1 ILE A 218 3789 3490 3326 -898 -155 -7 C ATOM 1430 N HIS A 219 16.409 -22.770 15.750 1.00 21.71 N ANISOU 1430 N HIS A 219 3017 2433 2800 -608 -311 -79 N ATOM 1431 CA HIS A 219 15.851 -24.079 15.436 1.00 21.31 C ANISOU 1431 CA HIS A 219 2810 2422 2867 -510 -307 -97 C ATOM 1432 C HIS A 219 16.497 -24.625 14.174 1.00 20.03 C ANISOU 1432 C HIS A 219 2640 2293 2677 -538 -301 -83 C ATOM 1433 O HIS A 219 16.870 -25.795 14.106 1.00 19.06 O ANISOU 1433 O HIS A 219 2368 2246 2627 -529 -257 -76 O ATOM 1434 CB HIS A 219 14.343 -23.981 15.207 1.00 20.45 C ANISOU 1434 CB HIS A 219 2705 2222 2842 -368 -371 -177 C ATOM 1435 CG HIS A 219 13.574 -23.501 16.398 1.00 21.14 C ANISOU 1435 CG HIS A 219 2776 2282 2975 -336 -353 -232 C ATOM 1436 ND1 HIS A 219 12.645 -24.284 17.047 1.00 21.48 N ANISOU 1436 ND1 HIS A 219 2670 2357 3134 -280 -309 -294 N ATOM 1437 CD2 HIS A 219 13.589 -22.315 17.050 1.00 20.91 C ANISOU 1437 CD2 HIS A 219 2864 2194 2888 -368 -356 -251 C ATOM 1438 CE1 HIS A 219 12.124 -23.603 18.052 1.00 21.55 C ANISOU 1438 CE1 HIS A 219 2696 2341 3150 -282 -277 -356 C ATOM 1439 NE2 HIS A 219 12.680 -22.406 18.076 1.00 22.82 N ANISOU 1439 NE2 HIS A 219 3016 2443 3211 -325 -310 -334 N ATOM 1440 N ILE A 220 16.621 -23.757 13.176 1.00 19.94 N ANISOU 1440 N ILE A 220 2807 2213 2554 -576 -344 -82 N ATOM 1441 CA ILE A 220 17.092 -24.148 11.854 1.00 20.12 C ANISOU 1441 CA ILE A 220 2863 2262 2519 -619 -332 -87 C ATOM 1442 C ILE A 220 18.546 -24.611 11.864 1.00 18.82 C ANISOU 1442 C ILE A 220 2595 2225 2330 -751 -224 -74 C ATOM 1443 O ILE A 220 18.878 -25.634 11.268 1.00 19.75 O ANISOU 1443 O ILE A 220 2593 2411 2501 -741 -177 -106 O ATOM 1444 CB ILE A 220 16.916 -23.003 10.841 1.00 23.14 C ANISOU 1444 CB ILE A 220 3514 2528 2749 -658 -407 -75 C ATOM 1445 CG1 ILE A 220 15.476 -22.485 10.879 1.00 24.03 C ANISOU 1445 CG1 ILE A 220 3709 2509 2912 -492 -545 -101 C ATOM 1446 CG2 ILE A 220 17.283 -23.465 9.442 1.00 23.75 C ANISOU 1446 CG2 ILE A 220 3644 2639 2741 -717 -388 -89 C ATOM 1447 CD1 ILE A 220 15.212 -21.331 9.940 1.00 26.30 C ANISOU 1447 CD1 ILE A 220 4291 2647 3056 -496 -663 -73 C ATOM 1448 N ILE A 221 19.409 -23.863 12.546 1.00 17.48 N ANISOU 1448 N ILE A 221 2447 2100 2093 -826 -176 -42 N ATOM 1449 CA ILE A 221 20.821 -24.223 12.616 1.00 15.03 C ANISOU 1449 CA ILE A 221 2010 1925 1775 -890 -86 -48 C ATOM 1450 C ILE A 221 21.022 -25.532 13.382 1.00 19.33 C ANISOU 1450 C ILE A 221 2325 2542 2479 -791 -77 -46 C ATOM 1451 O ILE A 221 21.851 -26.356 13.008 1.00 20.11 O ANISOU 1451 O ILE A 221 2292 2714 2635 -784 -31 -74 O ATOM 1452 CB ILE A 221 21.690 -23.084 13.219 1.00 19.28 C ANISOU 1452 CB ILE A 221 2625 2499 2204 -983 -55 -30 C ATOM 1453 CG1 ILE A 221 23.173 -23.462 13.192 1.00 19.36 C ANISOU 1453 CG1 ILE A 221 2492 2648 2217 -1040 20 -65 C ATOM 1454 CG2 ILE A 221 21.242 -22.728 14.633 1.00 15.26 C ANISOU 1454 CG2 ILE A 221 2105 1966 1729 -933 -98 -1 C ATOM 1455 CD1 ILE A 221 23.739 -23.607 11.800 1.00 20.63 C ANISOU 1455 CD1 ILE A 221 2681 2847 2311 -1128 94 -121 C ATOM 1456 N ALA A 222 20.240 -25.729 14.438 1.00 19.63 N ANISOU 1456 N ALA A 222 2330 2543 2585 -715 -121 -16 N ATOM 1457 CA ALA A 222 20.339 -26.939 15.244 1.00 20.13 C ANISOU 1457 CA ALA A 222 2231 2644 2772 -629 -119 1 C ATOM 1458 C ALA A 222 19.944 -28.175 14.445 1.00 21.50 C ANISOU 1458 C ALA A 222 2310 2799 3059 -561 -107 -33 C ATOM 1459 O ALA A 222 20.641 -29.187 14.477 1.00 24.12 O ANISOU 1459 O ALA A 222 2519 3179 3467 -519 -77 -51 O ATOM 1460 CB ALA A 222 19.481 -26.817 16.486 1.00 19.59 C ANISOU 1460 CB ALA A 222 2187 2542 2712 -596 -147 32 C ATOM 1461 N LEU A 223 18.828 -28.087 13.726 1.00 19.43 N ANISOU 1461 N LEU A 223 2115 2471 2798 -551 -137 -62 N ATOM 1462 CA LEU A 223 18.355 -29.203 12.914 1.00 19.18 C ANISOU 1462 CA LEU A 223 2017 2420 2852 -479 -126 -106 C ATOM 1463 C LEU A 223 19.274 -29.459 11.720 1.00 18.61 C ANISOU 1463 C LEU A 223 1919 2398 2755 -535 -73 -160 C ATOM 1464 O LEU A 223 19.508 -30.607 11.344 1.00 14.21 O ANISOU 1464 O LEU A 223 1266 1857 2276 -471 -34 -189 O ATOM 1465 CB LEU A 223 16.923 -28.958 12.432 1.00 17.12 C ANISOU 1465 CB LEU A 223 1835 2068 2602 -417 -184 -152 C ATOM 1466 CG LEU A 223 16.261 -30.139 11.717 1.00 15.31 C ANISOU 1466 CG LEU A 223 1528 1815 2473 -343 -175 -217 C ATOM 1467 CD1 LEU A 223 16.182 -31.341 12.645 1.00 16.19 C ANISOU 1467 CD1 LEU A 223 1556 1935 2662 -270 -120 -175 C ATOM 1468 CD2 LEU A 223 14.880 -29.768 11.200 1.00 12.88 C ANISOU 1468 CD2 LEU A 223 1288 1443 2162 -280 -256 -278 C ATOM 1469 N ALA A 224 19.795 -28.385 11.133 1.00 21.76 N ANISOU 1469 N ALA A 224 2439 2819 3009 -656 -58 -173 N ATOM 1470 CA ALA A 224 20.682 -28.496 9.978 1.00 21.99 C ANISOU 1470 CA ALA A 224 2474 2909 2973 -739 22 -237 C ATOM 1471 C ALA A 224 22.003 -29.151 10.356 1.00 25.48 C ANISOU 1471 C ALA A 224 2745 3444 3494 -708 85 -242 C ATOM 1472 O ALA A 224 22.609 -29.855 9.550 1.00 27.18 O ANISOU 1472 O ALA A 224 2881 3708 3739 -712 159 -321 O ATOM 1473 CB ALA A 224 20.928 -27.128 9.361 1.00 20.12 C ANISOU 1473 CB ALA A 224 2454 2656 2534 -884 29 -228 C ATOM 1474 N GLN A 225 22.447 -28.914 11.585 1.00 26.98 N ANISOU 1474 N GLN A 225 2885 3650 3715 -678 46 -169 N ATOM 1475 CA GLN A 225 23.690 -29.498 12.069 1.00 29.31 C ANISOU 1475 CA GLN A 225 3025 4021 4088 -644 61 -165 C ATOM 1476 C GLN A 225 23.470 -30.905 12.618 1.00 28.87 C ANISOU 1476 C GLN A 225 2849 3956 4163 -513 19 -121 C ATOM 1477 O GLN A 225 24.339 -31.769 12.493 1.00 33.67 O ANISOU 1477 O GLN A 225 3332 4617 4845 -461 42 -158 O ATOM 1478 CB GLN A 225 24.321 -28.606 13.141 1.00 32.66 C ANISOU 1478 CB GLN A 225 3464 4478 4468 -689 29 -121 C ATOM 1479 CG GLN A 225 24.812 -27.252 12.643 1.00 36.70 C ANISOU 1479 CG GLN A 225 4106 5030 4807 -836 85 -162 C ATOM 1480 CD GLN A 225 26.169 -27.323 11.968 1.00 41.53 C ANISOU 1480 CD GLN A 225 4630 5748 5401 -910 169 -250 C ATOM 1481 OE1 GLN A 225 26.422 -28.196 11.139 1.00 43.40 O ANISOU 1481 OE1 GLN A 225 4777 6012 5700 -881 221 -317 O ATOM 1482 NE2 GLN A 225 27.053 -26.398 12.326 1.00 43.27 N ANISOU 1482 NE2 GLN A 225 4873 6034 5535 -1011 190 -267 N ATOM 1483 N ALA A 226 22.307 -31.130 13.222 1.00 24.11 N ANISOU 1483 N ALA A 226 2302 3297 3560 -463 -27 -73 N ATOM 1484 CA ALA A 226 21.977 -32.431 13.796 1.00 23.85 C ANISOU 1484 CA ALA A 226 2213 3218 3629 -341 -43 -67 C ATOM 1485 C ALA A 226 21.819 -33.498 12.720 1.00 27.17 C ANISOU 1485 C ALA A 226 2595 3579 4148 -274 6 -143 C ATOM 1486 O ALA A 226 22.193 -34.655 12.921 1.00 28.46 O ANISOU 1486 O ALA A 226 2679 3706 4428 -185 3 -151 O ATOM 1487 CB ALA A 226 20.711 -32.339 14.634 1.00 22.10 C ANISOU 1487 CB ALA A 226 2078 2912 3405 -316 -77 -18 C ATOM 1488 N LEU A 227 21.263 -33.102 11.579 1.00 27.01 N ANISOU 1488 N LEU A 227 2637 3539 4086 -322 43 -209 N ATOM 1489 CA LEU A 227 21.009 -34.034 10.487 1.00 25.20 C ANISOU 1489 CA LEU A 227 2381 3262 3932 -283 96 -310 C ATOM 1490 C LEU A 227 22.009 -33.860 9.351 1.00 27.92 C ANISOU 1490 C LEU A 227 2684 3686 4239 -359 180 -417 C ATOM 1491 O LEU A 227 21.988 -34.611 8.377 1.00 27.41 O ANISOU 1491 O LEU A 227 2588 3603 4224 -347 244 -530 O ATOM 1492 CB LEU A 227 19.579 -33.869 9.969 1.00 22.52 C ANISOU 1492 CB LEU A 227 2127 2853 3576 -288 75 -340 C ATOM 1493 CG LEU A 227 18.481 -34.310 10.938 1.00 21.67 C ANISOU 1493 CG LEU A 227 2048 2662 3523 -213 26 -276 C ATOM 1494 CD1 LEU A 227 17.102 -34.030 10.364 1.00 19.06 C ANISOU 1494 CD1 LEU A 227 1778 2287 3178 -215 -4 -328 C ATOM 1495 CD2 LEU A 227 18.637 -35.787 11.271 1.00 22.73 C ANISOU 1495 CD2 LEU A 227 2120 2723 3793 -134 49 -279 C ATOM 1496 N SER A 228 22.883 -32.867 9.489 1.00 31.66 N ANISOU 1496 N SER A 228 3164 4247 4618 -453 193 -398 N ATOM 1497 CA SER A 228 23.919 -32.580 8.497 1.00 32.48 C ANISOU 1497 CA SER A 228 3244 4439 4657 -555 295 -510 C ATOM 1498 C SER A 228 23.359 -32.312 7.102 1.00 28.17 C ANISOU 1498 C SER A 228 2808 3893 4003 -669 368 -615 C ATOM 1499 O SER A 228 23.883 -32.814 6.111 1.00 29.23 O ANISOU 1499 O SER A 228 2900 4073 4135 -711 472 -748 O ATOM 1500 CB SER A 228 24.952 -33.710 8.436 1.00 35.51 C ANISOU 1500 CB SER A 228 3466 4852 5173 -468 337 -585 C ATOM 1501 OG SER A 228 25.557 -33.922 9.696 1.00 38.58 O ANISOU 1501 OG SER A 228 3762 5259 5637 -386 257 -487 O ATOM 1502 N VAL A 229 22.284 -31.538 7.022 1.00 25.79 N ANISOU 1502 N VAL A 229 2656 3538 3606 -727 304 -563 N ATOM 1503 CA VAL A 229 21.793 -31.084 5.726 1.00 26.98 C ANISOU 1503 CA VAL A 229 2971 3684 3597 -870 333 -638 C ATOM 1504 C VAL A 229 21.613 -29.565 5.738 1.00 27.66 C ANISOU 1504 C VAL A 229 3294 3739 3475 -982 272 -545 C ATOM 1505 O VAL A 229 21.177 -28.990 6.736 1.00 27.46 O ANISOU 1505 O VAL A 229 3301 3659 3473 -923 177 -442 O ATOM 1506 CB VAL A 229 20.507 -31.844 5.262 1.00 28.81 C ANISOU 1506 CB VAL A 229 3240 3825 3881 -754 261 -662 C ATOM 1507 CG1 VAL A 229 20.359 -33.178 5.997 1.00 27.29 C ANISOU 1507 CG1 VAL A 229 2834 3596 3937 -601 264 -679 C ATOM 1508 CG2 VAL A 229 19.265 -30.993 5.425 1.00 26.99 C ANISOU 1508 CG2 VAL A 229 3193 3504 3558 -713 109 -568 C ATOM 1509 N SER A 230 21.988 -28.915 4.640 1.00 29.96 N ANISOU 1509 N SER A 230 3767 4058 3558 -1155 337 -587 N ATOM 1510 CA SER A 230 21.996 -27.455 4.583 1.00 30.00 C ANISOU 1510 CA SER A 230 4030 4013 3355 -1286 293 -499 C ATOM 1511 C SER A 230 20.632 -26.889 4.209 1.00 29.30 C ANISOU 1511 C SER A 230 4189 3781 3163 -1206 119 -420 C ATOM 1512 O SER A 230 19.898 -27.481 3.419 1.00 30.13 O ANISOU 1512 O SER A 230 4327 3861 3258 -1140 69 -464 O ATOM 1513 CB SER A 230 23.065 -26.953 3.610 1.00 32.45 C ANISOU 1513 CB SER A 230 4454 4409 3465 -1510 448 -561 C ATOM 1514 OG SER A 230 23.051 -25.538 3.513 1.00 35.24 O ANISOU 1514 OG SER A 230 5093 4689 3608 -1628 408 -458 O ATOM 1515 N ILE A 231 20.296 -25.739 4.786 1.00 28.44 N ANISOU 1515 N ILE A 231 4243 3577 2986 -1204 20 -315 N ATOM 1516 CA ILE A 231 18.990 -25.125 4.574 1.00 28.10 C ANISOU 1516 CA ILE A 231 4407 3387 2882 -1090 -170 -249 C ATOM 1517 C ILE A 231 19.118 -23.648 4.214 1.00 31.08 C ANISOU 1517 C ILE A 231 5103 3659 3046 -1197 -214 -151 C ATOM 1518 O ILE A 231 19.851 -22.903 4.866 1.00 31.15 O ANISOU 1518 O ILE A 231 5136 3674 3028 -1293 -144 -108 O ATOM 1519 CB ILE A 231 18.108 -25.241 5.836 1.00 25.25 C ANISOU 1519 CB ILE A 231 3898 2975 2720 -891 -270 -215 C ATOM 1520 CG1 ILE A 231 18.095 -26.679 6.360 1.00 21.70 C ANISOU 1520 CG1 ILE A 231 3140 2615 2489 -790 -203 -277 C ATOM 1521 CG2 ILE A 231 16.694 -24.756 5.547 1.00 26.26 C ANISOU 1521 CG2 ILE A 231 4179 2971 2828 -746 -467 -191 C ATOM 1522 CD1 ILE A 231 17.390 -26.842 7.685 1.00 19.54 C ANISOU 1522 CD1 ILE A 231 2728 2309 2388 -647 -259 -246 C ATOM 1523 N GLN A 232 18.405 -23.228 3.173 1.00 31.05 N ANISOU 1523 N GLN A 232 5336 3555 2908 -1168 -331 -106 N ATOM 1524 CA GLN A 232 18.349 -21.817 2.807 1.00 31.10 C ANISOU 1524 CA GLN A 232 5664 3402 2750 -1237 -401 12 C ATOM 1525 C GLN A 232 16.935 -21.267 2.971 1.00 32.72 C ANISOU 1525 C GLN A 232 5986 3439 3009 -1014 -646 63 C ATOM 1526 O GLN A 232 15.968 -21.866 2.502 1.00 32.15 O ANISOU 1526 O GLN A 232 5857 3368 2990 -861 -772 23 O ATOM 1527 CB GLN A 232 18.842 -21.601 1.374 1.00 34.06 C ANISOU 1527 CB GLN A 232 6249 3759 2934 -1421 -333 31 C ATOM 1528 CG GLN A 232 18.715 -20.163 0.889 1.00 38.63 C ANISOU 1528 CG GLN A 232 7183 4113 3380 -1502 -430 133 C ATOM 1529 CD GLN A 232 19.453 -19.912 -0.412 1.00 43.34 C ANISOU 1529 CD GLN A 232 7969 4695 3802 -1745 -328 121 C ATOM 1530 OE1 GLN A 232 20.472 -20.542 -0.695 1.00 43.22 O ANISOU 1530 OE1 GLN A 232 7812 4846 3764 -1923 -121 39 O ATOM 1531 NE2 GLN A 232 18.939 -18.985 -1.214 1.00 47.01 N ANISOU 1531 NE2 GLN A 232 8754 4959 4148 -1753 -480 184 N ATOM 1532 N VAL A 233 16.822 -20.124 3.641 1.00 35.05 N ANISOU 1532 N VAL A 233 6432 3590 3297 -996 -713 134 N ATOM 1533 CA VAL A 233 15.521 -19.514 3.893 1.00 36.24 C ANISOU 1533 CA VAL A 233 6682 3570 3519 -773 -946 155 C ATOM 1534 C VAL A 233 15.358 -18.188 3.155 1.00 39.72 C ANISOU 1534 C VAL A 233 7495 3769 3828 -818 -1065 220 C ATOM 1535 O VAL A 233 16.213 -17.308 3.243 1.00 40.72 O ANISOU 1535 O VAL A 233 7760 3857 3855 -991 -969 231 O ATOM 1536 CB VAL A 233 15.296 -19.278 5.399 1.00 35.00 C ANISOU 1536 CB VAL A 233 6373 3411 3514 -671 -953 128 C ATOM 1537 CG1 VAL A 233 13.938 -18.634 5.641 1.00 36.77 C ANISOU 1537 CG1 VAL A 233 6683 3463 3824 -430 -1192 117 C ATOM 1538 CG2 VAL A 233 15.416 -20.586 6.164 1.00 32.36 C ANISOU 1538 CG2 VAL A 233 5665 3267 3365 -638 -835 31 C ATOM 1539 N GLU A 234 14.258 -18.057 2.422 1.00 42.06 N ANISOU 1539 N GLU A 234 7888 3960 4134 -648 -1273 211 N ATOM 1540 CA GLU A 234 13.916 -16.799 1.771 1.00 45.78 C ANISOU 1540 CA GLU A 234 8681 4216 4496 -642 -1428 225 C ATOM 1541 C GLU A 234 12.796 -16.117 2.547 1.00 47.51 C ANISOU 1541 C GLU A 234 8880 4329 4841 -390 -1631 165 C ATOM 1542 O GLU A 234 11.939 -16.785 3.128 1.00 47.26 O ANISOU 1542 O GLU A 234 8599 4364 4995 -188 -1704 106 O ATOM 1543 CB GLU A 234 13.492 -17.036 0.320 1.00 48.09 C ANISOU 1543 CB GLU A 234 9106 4482 4685 -635 -1528 253 C ATOM 1544 CG GLU A 234 14.558 -17.690 -0.550 1.00 49.88 C ANISOU 1544 CG GLU A 234 9344 4844 4763 -888 -1323 282 C ATOM 1545 CD GLU A 234 15.688 -16.746 -0.926 1.00 52.71 C ANISOU 1545 CD GLU A 234 9965 5116 4948 -1167 -1198 310 C ATOM 1546 OE1 GLU A 234 15.614 -15.547 -0.581 1.00 55.18 O ANISOU 1546 OE1 GLU A 234 10477 5263 5227 -1159 -1288 309 O ATOM 1547 OE2 GLU A 234 16.653 -17.206 -1.573 1.00 52.51 O ANISOU 1547 OE2 GLU A 234 9931 5207 4814 -1397 -1008 304 O ATOM 1548 N TYR A 235 12.803 -14.789 2.556 1.00 49.11 N ANISOU 1548 N TYR A 235 9323 4397 4941 -404 -1713 171 N ATOM 1549 CA TYR A 235 11.844 -14.033 3.353 1.00 50.86 C ANISOU 1549 CA TYR A 235 9496 4556 5274 -172 -1870 123 C ATOM 1550 C TYR A 235 10.928 -13.176 2.490 1.00 55.35 C ANISOU 1550 C TYR A 235 10288 4944 5799 -32 -2113 123 C ATOM 1551 O TYR A 235 11.125 -13.059 1.281 1.00 56.24 O ANISOU 1551 O TYR A 235 10637 4970 5761 -135 -2159 175 O ATOM 1552 CB TYR A 235 12.572 -13.166 4.381 1.00 49.73 C ANISOU 1552 CB TYR A 235 9386 4427 5083 -266 -1744 149 C ATOM 1553 CG TYR A 235 13.563 -13.941 5.216 1.00 47.49 C ANISOU 1553 CG TYR A 235 8890 4331 4824 -417 -1507 161 C ATOM 1554 CD1 TYR A 235 13.166 -14.586 6.379 1.00 46.26 C ANISOU 1554 CD1 TYR A 235 8421 4283 4874 -282 -1458 132 C ATOM 1555 CD2 TYR A 235 14.896 -14.034 4.836 1.00 48.24 C ANISOU 1555 CD2 TYR A 235 9067 4498 4763 -694 -1315 194 C ATOM 1556 CE1 TYR A 235 14.069 -15.300 7.143 1.00 46.69 C ANISOU 1556 CE1 TYR A 235 8278 4495 4968 -414 -1243 151 C ATOM 1557 CE2 TYR A 235 15.805 -14.745 5.592 1.00 47.56 C ANISOU 1557 CE2 TYR A 235 8741 4605 4725 -811 -1096 204 C ATOM 1558 CZ TYR A 235 15.388 -15.376 6.744 1.00 47.76 C ANISOU 1558 CZ TYR A 235 8503 4717 4929 -673 -1080 192 C ATOM 1559 OH TYR A 235 16.292 -16.084 7.501 1.00 48.04 O ANISOU 1559 OH TYR A 235 8302 4922 5029 -791 -872 194 O ATOM 1560 N MET A 236 9.928 -12.573 3.124 1.00 58.85 N ANISOU 1560 N MET A 236 10645 5333 6380 201 -2261 65 N ATOM 1561 CA MET A 236 8.927 -11.800 2.405 1.00 65.13 C ANISOU 1561 CA MET A 236 11610 5965 7173 375 -2517 49 C ATOM 1562 C MET A 236 8.178 -10.853 3.337 1.00 67.48 C ANISOU 1562 C MET A 236 11837 6192 7611 575 -2613 -5 C ATOM 1563 O MET A 236 8.492 -9.665 3.415 1.00 70.39 O ANISOU 1563 O MET A 236 12454 6416 7877 534 -2637 51 O ATOM 1564 CB MET A 236 7.943 -12.742 1.714 1.00 66.29 C ANISOU 1564 CB MET A 236 11593 6162 7431 528 -2653 -16 C ATOM 1565 CG MET A 236 6.966 -12.053 0.788 1.00 70.45 C ANISOU 1565 CG MET A 236 12304 6530 7935 691 -2929 -24 C ATOM 1566 SD MET A 236 5.942 -13.240 -0.095 1.00 89.91 S ANISOU 1566 SD MET A 236 14567 9089 10504 833 -3060 -94 S ATOM 1567 CE MET A 236 4.965 -12.140 -1.109 1.00158.98 C ANISOU 1567 CE MET A 236 23594 17623 19187 1007 -3401 -82 C ATOM 1568 N PRO A 246 18.329 -14.236 2.419 1.00 68.66 N ANISOU 1568 N PRO A 246 11880 7249 6960 -1470 -813 221 N ATOM 1569 CA PRO A 246 19.024 -15.466 2.030 1.00 65.84 C ANISOU 1569 CA PRO A 246 11311 7067 6637 -1595 -640 199 C ATOM 1570 C PRO A 246 20.067 -15.908 3.058 1.00 59.56 C ANISOU 1570 C PRO A 246 10213 6501 5918 -1669 -438 146 C ATOM 1571 O PRO A 246 21.256 -15.614 2.910 1.00 59.10 O ANISOU 1571 O PRO A 246 10145 6540 5772 -1870 -283 94 O ATOM 1572 CB PRO A 246 19.694 -15.074 0.714 1.00 69.35 C ANISOU 1572 CB PRO A 246 12002 7457 6892 -1834 -581 192 C ATOM 1573 CG PRO A 246 18.741 -14.095 0.114 1.00 72.08 C ANISOU 1573 CG PRO A 246 12706 7545 7137 -1746 -816 241 C ATOM 1574 CD PRO A 246 18.130 -13.331 1.271 1.00 72.01 C ANISOU 1574 CD PRO A 246 12684 7471 7207 -1548 -935 245 C ATOM 1575 N HIS A 247 19.611 -16.613 4.088 1.00 53.79 N ANISOU 1575 N HIS A 247 9242 5856 5341 -1505 -455 151 N ATOM 1576 CA HIS A 247 20.504 -17.200 5.076 1.00 49.51 C ANISOU 1576 CA HIS A 247 8416 5537 4860 -1550 -290 111 C ATOM 1577 C HIS A 247 20.752 -18.665 4.741 1.00 43.98 C ANISOU 1577 C HIS A 247 7500 4996 4215 -1572 -186 89 C ATOM 1578 O HIS A 247 19.838 -19.376 4.327 1.00 42.25 O ANISOU 1578 O HIS A 247 7295 4701 4056 -1481 -274 131 O ATOM 1579 CB HIS A 247 19.902 -17.092 6.477 1.00 50.47 C ANISOU 1579 CB HIS A 247 8435 5648 5094 -1389 -356 145 C ATOM 1580 CG HIS A 247 19.738 -15.685 6.962 1.00 54.41 C ANISOU 1580 CG HIS A 247 9124 6017 5533 -1373 -427 158 C ATOM 1581 ND1 HIS A 247 18.932 -14.767 6.325 1.00 58.26 N ANISOU 1581 ND1 HIS A 247 9893 6298 5946 -1303 -591 185 N ATOM 1582 CD2 HIS A 247 20.273 -15.041 8.026 1.00 55.04 C ANISOU 1582 CD2 HIS A 247 9165 6140 5607 -1421 -362 142 C ATOM 1583 CE1 HIS A 247 18.979 -13.617 6.974 1.00 59.95 C ANISOU 1583 CE1 HIS A 247 10241 6432 6106 -1309 -616 188 C ATOM 1584 NE2 HIS A 247 19.785 -13.757 8.010 1.00 58.35 N ANISOU 1584 NE2 HIS A 247 9848 6378 5943 -1387 -471 164 N ATOM 1585 N ILE A 248 21.988 -19.116 4.919 1.00 40.81 N ANISOU 1585 N ILE A 248 6906 4789 3813 -1707 -9 0 N ATOM 1586 CA ILE A 248 22.320 -20.517 4.695 1.00 37.77 C ANISOU 1586 CA ILE A 248 6292 4569 3490 -1730 103 -63 C ATOM 1587 C ILE A 248 22.785 -21.166 5.991 1.00 36.17 C ANISOU 1587 C ILE A 248 5760 4508 3473 -1645 158 -114 C ATOM 1588 O ILE A 248 23.737 -20.708 6.619 1.00 36.85 O ANISOU 1588 O ILE A 248 5767 4681 3553 -1705 226 -155 O ATOM 1589 CB ILE A 248 23.401 -20.686 3.611 1.00 37.99 C ANISOU 1589 CB ILE A 248 6313 4697 3423 -1916 248 -174 C ATOM 1590 CG1 ILE A 248 22.912 -20.111 2.282 1.00 41.09 C ANISOU 1590 CG1 ILE A 248 7002 4892 3716 -2014 176 -120 C ATOM 1591 CG2 ILE A 248 23.769 -22.155 3.447 1.00 36.67 C ANISOU 1591 CG2 ILE A 248 5883 4713 3337 -1917 375 -278 C ATOM 1592 CD1 ILE A 248 23.892 -20.287 1.144 1.00 44.92 C ANISOU 1592 CD1 ILE A 248 7510 5462 4094 -2231 325 -225 C ATOM 1593 N PHE A 249 22.095 -22.230 6.388 1.00 34.09 N ANISOU 1593 N PHE A 249 5290 4248 3416 -1484 102 -123 N ATOM 1594 CA PHE A 249 22.404 -22.936 7.622 1.00 32.19 C ANISOU 1594 CA PHE A 249 4740 4105 3385 -1370 121 -151 C ATOM 1595 C PHE A 249 22.928 -24.328 7.290 1.00 34.16 C ANISOU 1595 C PHE A 249 4736 4484 3760 -1345 210 -246 C ATOM 1596 O PHE A 249 22.181 -25.163 6.784 1.00 35.69 O ANISOU 1596 O PHE A 249 4897 4644 4020 -1278 172 -275 O ATOM 1597 CB PHE A 249 21.150 -23.061 8.493 1.00 30.27 C ANISOU 1597 CB PHE A 249 4467 3753 3280 -1194 -20 -101 C ATOM 1598 CG PHE A 249 20.436 -21.757 8.736 1.00 30.41 C ANISOU 1598 CG PHE A 249 4731 3616 3207 -1172 -124 -28 C ATOM 1599 CD1 PHE A 249 19.527 -21.264 7.813 1.00 30.90 C ANISOU 1599 CD1 PHE A 249 5045 3526 3170 -1141 -239 5 C ATOM 1600 CD2 PHE A 249 20.658 -21.037 9.899 1.00 30.30 C ANISOU 1600 CD2 PHE A 249 4697 3602 3212 -1162 -122 -1 C ATOM 1601 CE1 PHE A 249 18.864 -20.072 8.037 1.00 31.47 C ANISOU 1601 CE1 PHE A 249 5336 3439 3183 -1084 -351 66 C ATOM 1602 CE2 PHE A 249 19.996 -19.845 10.128 1.00 31.73 C ANISOU 1602 CE2 PHE A 249 5095 3635 3328 -1129 -210 45 C ATOM 1603 CZ PHE A 249 19.099 -19.362 9.195 1.00 32.67 C ANISOU 1603 CZ PHE A 249 5455 3593 3367 -1079 -327 79 C ATOM 1604 N PRO A 250 24.213 -24.588 7.581 1.00 34.71 N ANISOU 1604 N PRO A 250 4624 4693 3872 -1378 313 -312 N ATOM 1605 CA PRO A 250 25.145 -23.642 8.200 1.00 37.22 C ANISOU 1605 CA PRO A 250 4965 5060 4118 -1456 343 -307 C ATOM 1606 C PRO A 250 25.839 -22.748 7.180 1.00 40.11 C ANISOU 1606 C PRO A 250 5533 5448 4258 -1665 436 -363 C ATOM 1607 O PRO A 250 25.795 -23.017 5.980 1.00 42.09 O ANISOU 1607 O PRO A 250 5878 5705 4411 -1755 499 -418 O ATOM 1608 CB PRO A 250 26.173 -24.564 8.853 1.00 36.72 C ANISOU 1608 CB PRO A 250 4600 5123 4229 -1376 381 -370 C ATOM 1609 CG PRO A 250 26.224 -25.735 7.938 1.00 35.79 C ANISOU 1609 CG PRO A 250 4367 5046 4186 -1344 444 -456 C ATOM 1610 CD PRO A 250 24.813 -25.927 7.435 1.00 33.91 C ANISOU 1610 CD PRO A 250 4262 4696 3928 -1306 382 -406 C ATOM 1611 N GLU A 251 26.475 -21.690 7.672 1.00 42.46 N ANISOU 1611 N GLU A 251 5911 5757 4466 -1754 447 -360 N ATOM 1612 CA GLU A 251 27.170 -20.729 6.824 1.00 46.85 C ANISOU 1612 CA GLU A 251 6677 6319 4805 -1969 526 -423 C ATOM 1613 C GLU A 251 28.241 -21.396 5.961 1.00 49.20 C ANISOU 1613 C GLU A 251 6841 6758 5096 -2076 668 -576 C ATOM 1614 O GLU A 251 28.985 -22.259 6.433 1.00 49.67 O ANISOU 1614 O GLU A 251 6603 6942 5329 -1994 711 -646 O ATOM 1615 CB GLU A 251 27.812 -19.646 7.691 1.00 50.12 C ANISOU 1615 CB GLU A 251 7129 6744 5169 -2038 523 -419 C ATOM 1616 CG GLU A 251 28.644 -18.626 6.933 1.00 54.31 C ANISOU 1616 CG GLU A 251 7865 7281 5489 -2278 610 -503 C ATOM 1617 CD GLU A 251 27.800 -17.546 6.289 1.00 57.42 C ANISOU 1617 CD GLU A 251 8625 7468 5725 -2339 530 -419 C ATOM 1618 OE1 GLU A 251 26.596 -17.461 6.611 1.00 57.84 O ANISOU 1618 OE1 GLU A 251 8764 7384 5829 -2184 402 -299 O ATOM 1619 OE2 GLU A 251 28.341 -16.776 5.467 1.00 59.98 O ANISOU 1619 OE2 GLU A 251 9128 7747 5917 -2517 588 -459 O ATOM 1620 N GLY A 252 28.303 -20.995 4.695 1.00 51.69 N ANISOU 1620 N GLY A 252 7387 7037 5215 -2259 725 -635 N ATOM 1621 CA GLY A 252 29.325 -21.480 3.789 1.00 55.06 C ANISOU 1621 CA GLY A 252 7721 7588 5612 -2399 874 -806 C ATOM 1622 C GLY A 252 29.108 -22.908 3.330 1.00 55.53 C ANISOU 1622 C GLY A 252 7581 7708 5809 -2288 916 -867 C ATOM 1623 O GLY A 252 30.069 -23.631 3.073 1.00 57.08 O ANISOU 1623 O GLY A 252 7557 8035 6097 -2306 1029 -1019 O ATOM 1624 N SER A 253 27.848 -23.318 3.228 1.00 52.52 N ANISOU 1624 N SER A 253 7275 7228 5452 -2173 824 -762 N ATOM 1625 CA SER A 253 27.512 -24.656 2.756 1.00 50.54 C ANISOU 1625 CA SER A 253 6859 7019 5324 -2077 863 -824 C ATOM 1626 C SER A 253 26.566 -24.567 1.567 1.00 50.14 C ANISOU 1626 C SER A 253 7092 6867 5093 -2187 837 -796 C ATOM 1627 O SER A 253 26.028 -23.500 1.277 1.00 50.40 O ANISOU 1627 O SER A 253 7400 6743 5006 -2246 738 -652 O ATOM 1628 CB SER A 253 26.867 -25.475 3.874 1.00 47.41 C ANISOU 1628 CB SER A 253 6234 6601 5180 -1820 762 -735 C ATOM 1629 OG SER A 253 25.658 -24.875 4.302 1.00 45.15 O ANISOU 1629 OG SER A 253 6130 6175 4851 -1765 622 -572 O ATOM 1630 N GLU A 254 26.363 -25.687 0.882 1.00 49.98 N ANISOU 1630 N GLU A 254 6961 6894 5135 -2163 903 -890 N ATOM 1631 CA GLU A 254 25.462 -25.722 -0.264 1.00 51.99 C ANISOU 1631 CA GLU A 254 7420 7031 5304 -2235 863 -805 C ATOM 1632 C GLU A 254 24.076 -26.194 0.153 1.00 49.84 C ANISOU 1632 C GLU A 254 7159 6688 5090 -2058 744 -684 C ATOM 1633 O GLU A 254 23.899 -27.350 0.537 1.00 49.23 O ANISOU 1633 O GLU A 254 6828 6667 5210 -1892 739 -790 O ATOM 1634 CB GLU A 254 26.019 -26.628 -1.360 1.00 56.38 C ANISOU 1634 CB GLU A 254 7870 7681 5871 -2343 1014 -984 C ATOM 1635 CG GLU A 254 27.402 -26.233 -1.838 1.00 62.01 C ANISOU 1635 CG GLU A 254 8570 8478 6515 -2529 1142 -1136 C ATOM 1636 CD GLU A 254 27.843 -27.033 -3.044 1.00 66.44 C ANISOU 1636 CD GLU A 254 9068 9107 7068 -2663 1286 -1308 C ATOM 1637 OE1 GLU A 254 29.022 -27.440 -3.092 1.00 68.79 O ANISOU 1637 OE1 GLU A 254 9171 9533 7434 -2711 1416 -1523 O ATOM 1638 OE2 GLU A 254 27.009 -27.252 -3.947 1.00 67.10 O ANISOU 1638 OE2 GLU A 254 9304 9120 7070 -2727 1274 -1235 O ATOM 1639 N PRO A 255 23.086 -25.294 0.071 1.00 49.32 N ANISOU 1639 N PRO A 255 7370 6443 4927 -1990 547 -511 N ATOM 1640 CA PRO A 255 21.718 -25.565 0.522 1.00 47.84 C ANISOU 1640 CA PRO A 255 7185 6153 4840 -1726 324 -449 C ATOM 1641 C PRO A 255 21.041 -26.669 -0.279 1.00 48.60 C ANISOU 1641 C PRO A 255 7220 6273 4974 -1625 288 -536 C ATOM 1642 O PRO A 255 21.035 -26.633 -1.509 1.00 52.05 O ANISOU 1642 O PRO A 255 7815 6707 5256 -1726 318 -542 O ATOM 1643 CB PRO A 255 21.004 -24.232 0.287 1.00 48.77 C ANISOU 1643 CB PRO A 255 7633 6082 4814 -1717 154 -278 C ATOM 1644 CG PRO A 255 21.794 -23.561 -0.779 1.00 50.88 C ANISOU 1644 CG PRO A 255 8109 6325 4898 -1977 270 -262 C ATOM 1645 CD PRO A 255 23.215 -23.953 -0.523 1.00 50.98 C ANISOU 1645 CD PRO A 255 7898 6510 4963 -2168 513 -397 C ATOM 1646 N LYS A 256 20.478 -27.644 0.425 1.00 45.87 N ANISOU 1646 N LYS A 256 6644 5939 4847 -1443 226 -602 N ATOM 1647 CA LYS A 256 19.724 -28.711 -0.217 1.00 46.04 C ANISOU 1647 CA LYS A 256 6597 5967 4928 -1341 182 -691 C ATOM 1648 C LYS A 256 18.226 -28.517 0.002 1.00 41.53 C ANISOU 1648 C LYS A 256 6105 5279 4396 -1152 -65 -615 C ATOM 1649 O LYS A 256 17.410 -28.963 -0.803 1.00 41.82 O ANISOU 1649 O LYS A 256 6189 5302 4400 -1090 -156 -654 O ATOM 1650 CB LYS A 256 20.192 -30.081 0.283 1.00 50.42 C ANISOU 1650 CB LYS A 256 6816 6605 5735 -1278 313 -833 C ATOM 1651 CG LYS A 256 20.752 -30.070 1.694 1.00 54.83 C ANISOU 1651 CG LYS A 256 7156 7178 6498 -1198 345 -777 C ATOM 1652 CD LYS A 256 21.925 -31.028 1.826 1.00 59.65 C ANISOU 1652 CD LYS A 256 7493 7901 7271 -1220 533 -908 C ATOM 1653 CE LYS A 256 23.068 -30.623 0.907 1.00 65.96 C ANISOU 1653 CE LYS A 256 8362 8812 7887 -1461 716 -1013 C ATOM 1654 NZ LYS A 256 24.225 -31.556 1.006 1.00 69.55 N ANISOU 1654 NZ LYS A 256 8519 9383 8525 -1447 893 -1169 N ATOM 1655 N VAL A 257 17.875 -27.833 1.087 1.00 37.33 N ANISOU 1655 N VAL A 257 5574 4670 3939 -1067 -169 -521 N ATOM 1656 CA VAL A 257 16.481 -27.512 1.380 1.00 34.70 C ANISOU 1656 CA VAL A 257 5294 4229 3659 -885 -395 -466 C ATOM 1657 C VAL A 257 16.222 -26.011 1.251 1.00 35.22 C ANISOU 1657 C VAL A 257 5632 4180 3570 -882 -519 -325 C ATOM 1658 O VAL A 257 16.932 -25.197 1.841 1.00 35.92 O ANISOU 1658 O VAL A 257 5787 4243 3619 -966 -455 -255 O ATOM 1659 CB VAL A 257 16.076 -27.989 2.789 1.00 32.66 C ANISOU 1659 CB VAL A 257 4767 3966 3677 -721 -399 -459 C ATOM 1660 CG1 VAL A 257 14.644 -27.573 3.107 1.00 31.01 C ANISOU 1660 CG1 VAL A 257 4590 3660 3531 -546 -608 -431 C ATOM 1661 CG2 VAL A 257 16.235 -29.497 2.902 1.00 32.47 C ANISOU 1661 CG2 VAL A 257 4476 4021 3842 -682 -279 -563 C ATOM 1662 N TYR A 258 15.204 -25.654 0.474 1.00 36.85 N ANISOU 1662 N TYR A 258 5992 4310 3699 -786 -698 -290 N ATOM 1663 CA TYR A 258 14.852 -24.255 0.250 1.00 38.21 C ANISOU 1663 CA TYR A 258 6440 4331 3747 -764 -840 -159 C ATOM 1664 C TYR A 258 13.473 -23.939 0.821 1.00 38.94 C ANISOU 1664 C TYR A 258 6486 4324 3984 -523 -1062 -152 C ATOM 1665 O TYR A 258 12.482 -24.574 0.461 1.00 40.32 O ANISOU 1665 O TYR A 258 6550 4529 4240 -393 -1175 -223 O ATOM 1666 CB TYR A 258 14.896 -23.927 -1.245 1.00 41.48 C ANISOU 1666 CB TYR A 258 7107 4709 3944 -867 -873 -115 C ATOM 1667 CG TYR A 258 16.267 -24.092 -1.865 1.00 43.89 C ANISOU 1667 CG TYR A 258 7469 5103 4104 -1124 -636 -132 C ATOM 1668 CD1 TYR A 258 17.167 -23.033 -1.901 1.00 46.23 C ANISOU 1668 CD1 TYR A 258 7968 5321 4275 -1308 -544 -42 C ATOM 1669 CD2 TYR A 258 16.663 -25.306 -2.411 1.00 43.55 C ANISOU 1669 CD2 TYR A 258 7265 5215 4068 -1193 -496 -259 C ATOM 1670 CE1 TYR A 258 18.421 -23.179 -2.464 1.00 47.07 C ANISOU 1670 CE1 TYR A 258 8092 5519 4273 -1561 -315 -83 C ATOM 1671 CE2 TYR A 258 17.917 -25.461 -2.976 1.00 45.39 C ANISOU 1671 CE2 TYR A 258 7519 5534 4191 -1426 -266 -300 C ATOM 1672 CZ TYR A 258 18.791 -24.394 -3.000 1.00 46.90 C ANISOU 1672 CZ TYR A 258 7891 5665 4264 -1613 -175 -214 C ATOM 1673 OH TYR A 258 20.039 -24.541 -3.560 1.00 47.62 O ANISOU 1673 OH TYR A 258 7973 5851 4268 -1863 62 -281 O ATOM 1674 N LEU A 259 13.414 -22.952 1.710 1.00 39.04 N ANISOU 1674 N LEU A 259 6572 4224 4039 -472 -1114 -84 N ATOM 1675 CA LEU A 259 12.165 -22.591 2.373 1.00 38.19 C ANISOU 1675 CA LEU A 259 6397 4022 4092 -242 -1304 -105 C ATOM 1676 C LEU A 259 11.824 -21.114 2.204 1.00 40.48 C ANISOU 1676 C LEU A 259 6984 4098 4300 -185 -1465 -12 C ATOM 1677 O LEU A 259 12.702 -20.282 1.976 1.00 41.42 O ANISOU 1677 O LEU A 259 7346 4131 4260 -349 -1394 79 O ATOM 1678 CB LEU A 259 12.238 -22.927 3.863 1.00 34.49 C ANISOU 1678 CB LEU A 259 5681 3608 3817 -199 -1217 -161 C ATOM 1679 CG LEU A 259 12.520 -24.384 4.232 1.00 31.75 C ANISOU 1679 CG LEU A 259 5038 3422 3605 -238 -1065 -258 C ATOM 1680 CD1 LEU A 259 12.614 -24.540 5.738 1.00 26.81 C ANISOU 1680 CD1 LEU A 259 4202 2820 3164 -203 -967 -275 C ATOM 1681 CD2 LEU A 259 11.447 -25.298 3.661 1.00 32.48 C ANISOU 1681 CD2 LEU A 259 4981 3565 3795 -116 -1152 -352 C ATOM 1682 N LEU A 260 10.538 -20.799 2.320 1.00 40.48 N ANISOU 1682 N LEU A 260 6948 4002 4429 42 -1671 -62 N ATOM 1683 CA LEU A 260 10.076 -19.418 2.315 1.00 42.10 C ANISOU 1683 CA LEU A 260 7398 3985 4613 133 -1837 -29 C ATOM 1684 C LEU A 260 9.471 -19.078 3.668 1.00 43.47 C ANISOU 1684 C LEU A 260 7408 4123 4985 293 -1885 -114 C ATOM 1685 O LEU A 260 8.645 -19.827 4.190 1.00 44.27 O ANISOU 1685 O LEU A 260 7211 4324 5285 438 -1906 -227 O ATOM 1686 CB LEU A 260 9.031 -19.203 1.222 1.00 44.37 C ANISOU 1686 CB LEU A 260 7781 4194 4883 266 -2049 -59 C ATOM 1687 CG LEU A 260 8.380 -17.817 1.217 1.00 47.33 C ANISOU 1687 CG LEU A 260 8364 4362 5257 388 -2244 -74 C ATOM 1688 CD1 LEU A 260 9.355 -16.768 0.702 1.00 47.89 C ANISOU 1688 CD1 LEU A 260 8811 4290 5095 191 -2208 43 C ATOM 1689 CD2 LEU A 260 7.091 -17.811 0.407 1.00 50.20 C ANISOU 1689 CD2 LEU A 260 8706 4692 5676 576 -2473 -144 C ATOM 1690 N TYR A 261 9.877 -17.948 4.237 1.00 44.39 N ANISOU 1690 N TYR A 261 7701 4125 5040 244 -1881 -82 N ATOM 1691 CA TYR A 261 9.360 -17.550 5.540 1.00 44.40 C ANISOU 1691 CA TYR A 261 7522 4153 5196 372 -1893 -159 C ATOM 1692 C TYR A 261 8.476 -16.305 5.502 1.00 46.47 C ANISOU 1692 C TYR A 261 7887 4292 5478 523 -2061 -203 C ATOM 1693 O TYR A 261 8.870 -15.252 4.999 1.00 46.30 O ANISOU 1693 O TYR A 261 8167 4136 5288 451 -2111 -128 O ATOM 1694 CB TYR A 261 10.494 -17.363 6.555 1.00 44.19 C ANISOU 1694 CB TYR A 261 7486 4178 5124 213 -1687 -80 C ATOM 1695 CG TYR A 261 10.008 -16.869 7.900 1.00 45.86 C ANISOU 1695 CG TYR A 261 7511 4404 5510 323 -1632 -144 C ATOM 1696 CD1 TYR A 261 9.384 -17.731 8.793 1.00 45.93 C ANISOU 1696 CD1 TYR A 261 7184 4525 5744 421 -1561 -252 C ATOM 1697 CD2 TYR A 261 10.166 -15.541 8.273 1.00 47.71 C ANISOU 1697 CD2 TYR A 261 7913 4533 5680 310 -1636 -113 C ATOM 1698 CE1 TYR A 261 8.934 -17.284 10.021 1.00 47.26 C ANISOU 1698 CE1 TYR A 261 7200 4705 6053 489 -1487 -327 C ATOM 1699 CE2 TYR A 261 9.719 -15.085 9.498 1.00 48.88 C ANISOU 1699 CE2 TYR A 261 7906 4680 5986 398 -1574 -184 C ATOM 1700 CZ TYR A 261 9.104 -15.960 10.368 1.00 49.78 C ANISOU 1700 CZ TYR A 261 7696 4910 6308 482 -1496 -293 C ATOM 1701 OH TYR A 261 8.658 -15.511 11.590 1.00 52.28 O ANISOU 1701 OH TYR A 261 7875 5226 6762 542 -1415 -380 O ATOM 1702 N ARG A 262 7.269 -16.459 6.035 1.00 48.50 N ANISOU 1702 N ARG A 262 7881 4599 5949 722 -2136 -336 N ATOM 1703 CA ARG A 262 6.361 -15.356 6.300 1.00 51.98 C ANISOU 1703 CA ARG A 262 8340 4944 6465 884 -2270 -400 C ATOM 1704 C ARG A 262 6.090 -15.426 7.802 1.00 53.19 C ANISOU 1704 C ARG A 262 8206 5191 6811 934 -2125 -479 C ATOM 1705 O ARG A 262 6.159 -16.512 8.374 1.00 52.40 O ANISOU 1705 O ARG A 262 7853 5238 6817 895 -1984 -524 O ATOM 1706 CB ARG A 262 5.078 -15.518 5.474 1.00 53.33 C ANISOU 1706 CB ARG A 262 8442 5095 6724 1058 -2477 -512 C ATOM 1707 CG ARG A 262 5.278 -15.304 3.972 1.00 54.24 C ANISOU 1707 CG ARG A 262 8873 5087 6648 1015 -2620 -424 C ATOM 1708 CD ARG A 262 3.965 -15.395 3.200 1.00 56.26 C ANISOU 1708 CD ARG A 262 9057 5320 6999 1203 -2835 -529 C ATOM 1709 NE ARG A 262 3.785 -16.687 2.537 1.00 54.80 N ANISOU 1709 NE ARG A 262 8728 5253 6840 1180 -2805 -558 N ATOM 1710 CZ ARG A 262 2.619 -17.144 2.088 1.00 56.40 C ANISOU 1710 CZ ARG A 262 8754 5510 7167 1327 -2933 -679 C ATOM 1711 NH1 ARG A 262 1.518 -16.420 2.237 1.00 58.73 N ANISOU 1711 NH1 ARG A 262 8986 5749 7581 1513 -3107 -791 N ATOM 1712 NH2 ARG A 262 2.551 -18.330 1.498 1.00 54.50 N ANISOU 1712 NH2 ARG A 262 8387 5390 6933 1286 -2882 -691 N ATOM 1713 N PRO A 263 5.800 -14.276 8.445 1.00 55.55 N ANISOU 1713 N PRO A 263 8555 5395 7158 1010 -2144 -499 N ATOM 1714 CA PRO A 263 5.746 -14.170 9.915 1.00 54.24 C ANISOU 1714 CA PRO A 263 8183 5285 7143 1015 -1965 -563 C ATOM 1715 C PRO A 263 5.116 -15.374 10.626 1.00 50.72 C ANISOU 1715 C PRO A 263 7362 5022 6889 1043 -1850 -694 C ATOM 1716 O PRO A 263 3.909 -15.606 10.509 1.00 52.58 O ANISOU 1716 O PRO A 263 7405 5308 7266 1178 -1947 -837 O ATOM 1717 CB PRO A 263 4.885 -12.925 10.138 1.00 57.02 C ANISOU 1717 CB PRO A 263 8584 5504 7579 1179 -2088 -638 C ATOM 1718 CG PRO A 263 5.172 -12.072 8.955 1.00 58.81 C ANISOU 1718 CG PRO A 263 9168 5561 7614 1178 -2276 -529 C ATOM 1719 CD PRO A 263 5.413 -13.008 7.793 1.00 58.78 C ANISOU 1719 CD PRO A 263 9224 5619 7492 1107 -2344 -479 C ATOM 1720 N GLY A 264 5.943 -16.131 11.343 1.00 44.41 N ANISOU 1720 N GLY A 264 6470 4318 6085 899 -1641 -652 N ATOM 1721 CA GLY A 264 5.500 -17.332 12.031 1.00 42.64 C ANISOU 1721 CA GLY A 264 5929 4260 6014 886 -1509 -759 C ATOM 1722 C GLY A 264 5.042 -18.464 11.126 1.00 43.08 C ANISOU 1722 C GLY A 264 5860 4409 6098 909 -1591 -802 C ATOM 1723 O GLY A 264 4.181 -19.254 11.515 1.00 44.12 O ANISOU 1723 O GLY A 264 5722 4662 6378 935 -1537 -938 O ATOM 1724 N HIS A 265 5.614 -18.555 9.926 1.00 41.73 N ANISOU 1724 N HIS A 265 5899 4181 5777 876 -1704 -698 N ATOM 1725 CA HIS A 265 5.226 -19.609 8.987 1.00 40.72 C ANISOU 1725 CA HIS A 265 5685 4121 5665 890 -1778 -750 C ATOM 1726 C HIS A 265 6.273 -19.924 7.912 1.00 37.23 C ANISOU 1726 C HIS A 265 5482 3626 5038 789 -1815 -613 C ATOM 1727 O HIS A 265 6.885 -19.023 7.339 1.00 37.35 O ANISOU 1727 O HIS A 265 5803 3514 4875 742 -1890 -497 O ATOM 1728 CB HIS A 265 3.894 -19.266 8.319 1.00 43.75 C ANISOU 1728 CB HIS A 265 6036 4471 6116 1042 -1968 -878 C ATOM 1729 CG HIS A 265 3.339 -20.380 7.489 1.00 46.49 C ANISOU 1729 CG HIS A 265 6266 4890 6509 1055 -1999 -960 C ATOM 1730 ND1 HIS A 265 3.040 -21.617 8.016 1.00 46.73 N ANISOU 1730 ND1 HIS A 265 6020 5066 6669 998 -1837 -1055 N ATOM 1731 CD2 HIS A 265 3.040 -20.449 6.171 1.00 49.91 C ANISOU 1731 CD2 HIS A 265 6833 5262 6868 1110 -2153 -950 C ATOM 1732 CE1 HIS A 265 2.576 -22.400 7.060 1.00 47.74 C ANISOU 1732 CE1 HIS A 265 6109 5222 6807 1023 -1883 -1104 C ATOM 1733 NE2 HIS A 265 2.564 -21.715 5.930 1.00 50.40 N ANISOU 1733 NE2 HIS A 265 6681 5444 7023 1096 -2078 -1038 N ATOM 1734 N TYR A 266 6.456 -21.213 7.635 1.00 33.57 N ANISOU 1734 N TYR A 266 4882 3258 4617 738 -1745 -634 N ATOM 1735 CA TYR A 266 7.395 -21.662 6.610 1.00 31.24 C ANISOU 1735 CA TYR A 266 4764 2955 4151 625 -1740 -508 C ATOM 1736 C TYR A 266 6.700 -22.471 5.516 1.00 30.35 C ANISOU 1736 C TYR A 266 4569 2911 4053 667 -1787 -564 C ATOM 1737 O TYR A 266 5.822 -23.289 5.797 1.00 28.44 O ANISOU 1737 O TYR A 266 4057 2765 3984 733 -1743 -697 O ATOM 1738 CB TYR A 266 8.505 -22.516 7.229 1.00 27.07 C ANISOU 1738 CB TYR A 266 4122 2559 3604 433 -1499 -466 C ATOM 1739 CG TYR A 266 9.411 -21.783 8.192 1.00 25.99 C ANISOU 1739 CG TYR A 266 4077 2376 3423 328 -1361 -387 C ATOM 1740 CD1 TYR A 266 9.052 -21.618 9.524 1.00 25.10 C ANISOU 1740 CD1 TYR A 266 3804 2269 3463 379 -1280 -452 C ATOM 1741 CD2 TYR A 266 10.634 -21.273 7.774 1.00 24.75 C ANISOU 1741 CD2 TYR A 266 4162 2181 3061 156 -1302 -263 C ATOM 1742 CE1 TYR A 266 9.880 -20.958 10.409 1.00 25.10 C ANISOU 1742 CE1 TYR A 266 3884 2245 3407 271 -1157 -385 C ATOM 1743 CE2 TYR A 266 11.469 -20.612 8.653 1.00 24.76 C ANISOU 1743 CE2 TYR A 266 4232 2153 3023 45 -1180 -207 C ATOM 1744 CZ TYR A 266 11.086 -20.457 9.970 1.00 26.84 C ANISOU 1744 CZ TYR A 266 4334 2428 3436 109 -1116 -264 C ATOM 1745 OH TYR A 266 11.912 -19.799 10.851 1.00 30.07 O ANISOU 1745 OH TYR A 266 4800 2836 3791 -9 -993 -211 O ATOM 1746 N ASP A 267 7.105 -22.241 4.270 1.00 29.26 N ANISOU 1746 N ASP A 267 4675 2725 3716 603 -1858 -464 N ATOM 1747 CA ASP A 267 6.627 -23.030 3.138 1.00 29.25 C ANISOU 1747 CA ASP A 267 4626 2804 3685 609 -1903 -500 C ATOM 1748 C ASP A 267 7.809 -23.604 2.362 1.00 30.48 C ANISOU 1748 C ASP A 267 4899 3043 3638 400 -1779 -407 C ATOM 1749 O ASP A 267 8.936 -23.129 2.495 1.00 31.53 O ANISOU 1749 O ASP A 267 5207 3142 3631 256 -1685 -304 O ATOM 1750 CB ASP A 267 5.752 -22.181 2.211 1.00 31.25 C ANISOU 1750 CB ASP A 267 5059 2926 3887 735 -2131 -509 C ATOM 1751 CG ASP A 267 4.397 -21.863 2.814 1.00 33.60 C ANISOU 1751 CG ASP A 267 5172 3196 4400 929 -2235 -670 C ATOM 1752 OD1 ASP A 267 3.838 -22.730 3.517 1.00 33.13 O ANISOU 1752 OD1 ASP A 267 4803 3259 4525 959 -2129 -799 O ATOM 1753 OD2 ASP A 267 3.890 -20.746 2.583 1.00 37.22 O ANISOU 1753 OD2 ASP A 267 5793 3515 4832 1031 -2409 -678 O ATOM 1754 N ILE A 268 7.546 -24.625 1.551 1.00 30.55 N ANISOU 1754 N ILE A 268 4805 3168 3634 368 -1762 -466 N ATOM 1755 CA ILE A 268 8.590 -25.257 0.750 1.00 30.10 C ANISOU 1755 CA ILE A 268 4836 3203 3397 169 -1630 -429 C ATOM 1756 C ILE A 268 8.743 -24.569 -0.604 1.00 33.79 C ANISOU 1756 C ILE A 268 5618 3597 3625 108 -1740 -340 C ATOM 1757 O ILE A 268 7.757 -24.325 -1.300 1.00 35.88 O ANISOU 1757 O ILE A 268 5935 3813 3885 226 -1928 -359 O ATOM 1758 CB ILE A 268 8.295 -26.755 0.513 1.00 28.73 C ANISOU 1758 CB ILE A 268 4413 3181 3320 142 -1540 -556 C ATOM 1759 CG1 ILE A 268 7.972 -27.459 1.832 1.00 27.40 C ANISOU 1759 CG1 ILE A 268 3943 3060 3406 203 -1430 -639 C ATOM 1760 CG2 ILE A 268 9.467 -27.433 -0.184 1.00 25.88 C ANISOU 1760 CG2 ILE A 268 4123 2909 2802 -63 -1377 -559 C ATOM 1761 CD1 ILE A 268 7.642 -28.929 1.674 1.00 25.71 C ANISOU 1761 CD1 ILE A 268 3506 2959 3305 170 -1326 -755 C ATOM 1762 N LEU A 269 9.984 -24.252 -0.964 1.00 34.29 N ANISOU 1762 N LEU A 269 5885 3652 3492 -87 -1611 -251 N ATOM 1763 CA LEU A 269 10.300 -23.711 -2.282 1.00 36.83 C ANISOU 1763 CA LEU A 269 6510 3915 3569 -201 -1658 -168 C ATOM 1764 C LEU A 269 11.004 -24.773 -3.110 1.00 37.48 C ANISOU 1764 C LEU A 269 6546 4161 3533 -379 -1491 -232 C ATOM 1765 O LEU A 269 11.784 -25.562 -2.579 1.00 35.95 O ANISOU 1765 O LEU A 269 6176 4081 3404 -471 -1290 -300 O ATOM 1766 CB LEU A 269 11.235 -22.506 -2.166 1.00 37.69 C ANISOU 1766 CB LEU A 269 6898 3883 3538 -332 -1599 -36 C ATOM 1767 CG LEU A 269 10.770 -21.227 -1.469 1.00 39.20 C ANISOU 1767 CG LEU A 269 7223 3869 3801 -200 -1748 26 C ATOM 1768 CD1 LEU A 269 11.971 -20.306 -1.259 1.00 39.59 C ANISOU 1768 CD1 LEU A 269 7502 3822 3717 -400 -1610 125 C ATOM 1769 CD2 LEU A 269 9.647 -20.519 -2.227 1.00 41.14 C ANISOU 1769 CD2 LEU A 269 7643 3961 4028 -43 -2016 38 C ATOM 1770 N TYR A 270 10.744 -24.782 -4.412 1.00 40.33 N ANISOU 1770 N TYR A 270 7070 4526 3726 -426 -1576 -224 N ATOM 1771 CA TYR A 270 11.480 -25.643 -5.330 1.00 40.71 C ANISOU 1771 CA TYR A 270 7123 4713 3632 -613 -1409 -293 C ATOM 1772 C TYR A 270 12.129 -24.790 -6.407 1.00 43.21 C ANISOU 1772 C TYR A 270 7791 4946 3682 -792 -1392 -180 C ATOM 1773 O TYR A 270 11.515 -23.856 -6.914 1.00 44.65 O ANISOU 1773 O TYR A 270 8209 4980 3774 -731 -1596 -82 O ATOM 1774 CB TYR A 270 10.549 -26.645 -6.008 1.00 39.65 C ANISOU 1774 CB TYR A 270 6845 4691 3532 -539 -1504 -419 C ATOM 1775 CG TYR A 270 9.863 -27.627 -5.092 1.00 37.43 C ANISOU 1775 CG TYR A 270 6216 4491 3517 -404 -1500 -551 C ATOM 1776 CD1 TYR A 270 10.414 -28.877 -4.839 1.00 36.32 C ANISOU 1776 CD1 TYR A 270 5860 4472 3469 -489 -1297 -690 C ATOM 1777 CD2 TYR A 270 8.647 -27.316 -4.502 1.00 38.21 C ANISOU 1777 CD2 TYR A 270 6204 4526 3790 -196 -1689 -549 C ATOM 1778 CE1 TYR A 270 9.781 -29.781 -4.012 1.00 34.36 C ANISOU 1778 CE1 TYR A 270 5320 4267 3468 -393 -1281 -799 C ATOM 1779 CE2 TYR A 270 8.006 -28.213 -3.673 1.00 37.14 C ANISOU 1779 CE2 TYR A 270 5755 4456 3902 -101 -1657 -667 C ATOM 1780 CZ TYR A 270 8.576 -29.443 -3.432 1.00 34.79 C ANISOU 1780 CZ TYR A 270 5273 4265 3679 -209 -1451 -778 C ATOM 1781 OH TYR A 270 7.937 -30.336 -2.605 1.00 35.05 O ANISOU 1781 OH TYR A 270 5025 4333 3961 -131 -1404 -875 O ATOM 1782 N LYS A 271 13.363 -25.111 -6.771 1.00 45.45 N ANISOU 1782 N LYS A 271 8108 5310 3851 -1019 -1147 -206 N ATOM 1783 CA LYS A 271 14.009 -24.395 -7.862 1.00 52.47 C ANISOU 1783 CA LYS A 271 9320 6128 4487 -1230 -1099 -120 C ATOM 1784 C LYS A 271 13.359 -24.751 -9.194 1.00 58.10 C ANISOU 1784 C LYS A 271 10151 6879 5047 -1238 -1224 -152 C ATOM 1785 O LYS A 271 13.299 -25.918 -9.579 1.00 59.41 O ANISOU 1785 O LYS A 271 10137 7205 5232 -1250 -1147 -292 O ATOM 1786 CB LYS A 271 15.509 -24.684 -7.896 1.00 54.41 C ANISOU 1786 CB LYS A 271 9529 6468 4675 -1485 -782 -167 C ATOM 1787 CG LYS A 271 16.276 -24.020 -6.771 1.00 56.17 C ANISOU 1787 CG LYS A 271 9718 6635 4989 -1532 -671 -109 C ATOM 1788 CD LYS A 271 17.613 -23.494 -7.259 1.00 60.80 C ANISOU 1788 CD LYS A 271 10467 7211 5422 -1837 -450 -89 C ATOM 1789 CE LYS A 271 18.222 -22.531 -6.253 1.00 61.90 C ANISOU 1789 CE LYS A 271 10642 7255 5624 -1892 -397 -16 C ATOM 1790 NZ LYS A 271 17.337 -21.358 -6.005 1.00 63.68 N ANISOU 1790 NZ LYS A 271 11099 7253 5842 -1751 -651 115 N ATOM 1791 OXT LYS A 271 12.870 -23.880 -9.914 1.00 61.57 O ANISOU 1791 OXT LYS A 271 10875 7179 5340 -1232 -1412 -45 O TER 1792 LYS A 271 ATOM 1793 N GLY B -1 36.001 3.692 15.337 1.00 64.94 N ANISOU 1793 N GLY B -1 11050 6601 7023 -1193 -501 685 N ATOM 1794 CA GLY B -1 36.921 2.589 15.138 1.00 63.73 C ANISOU 1794 CA GLY B -1 10812 6592 6810 -1401 116 523 C ATOM 1795 C GLY B -1 38.272 2.826 15.784 1.00 61.84 C ANISOU 1795 C GLY B -1 10365 6380 6751 -1439 470 419 C ATOM 1796 O GLY B -1 39.144 3.472 15.205 1.00 66.96 O ANISOU 1796 O GLY B -1 11168 7092 7183 -1817 601 362 O ATOM 1797 N SER B 0 38.443 2.301 16.993 1.00 54.43 N ANISOU 1797 N SER B 0 9005 5446 6231 -1012 578 324 N ATOM 1798 CA SER B 0 39.709 2.405 17.707 1.00 50.78 C ANISOU 1798 CA SER B 0 8236 5005 6052 -944 839 155 C ATOM 1799 C SER B 0 40.137 1.036 18.219 1.00 46.95 C ANISOU 1799 C SER B 0 7340 4586 5911 -710 1102 -131 C ATOM 1800 O SER B 0 41.318 0.795 18.468 1.00 47.56 O ANISOU 1800 O SER B 0 7140 4665 6266 -725 1353 -408 O ATOM 1801 CB SER B 0 39.595 3.392 18.870 1.00 48.85 C ANISOU 1801 CB SER B 0 7899 4637 6026 -607 509 335 C ATOM 1802 OG SER B 0 40.810 3.470 19.594 1.00 49.08 O ANISOU 1802 OG SER B 0 7638 4660 6348 -520 717 176 O ATOM 1803 N MET B 1 39.165 0.144 18.379 1.00 41.82 N ANISOU 1803 N MET B 1 6658 3954 5278 -501 988 -91 N ATOM 1804 CA MET B 1 39.441 -1.229 18.782 1.00 37.76 C ANISOU 1804 CA MET B 1 5859 3435 5052 -320 1126 -323 C ATOM 1805 C MET B 1 38.629 -2.207 17.941 1.00 36.82 C ANISOU 1805 C MET B 1 5846 3403 4739 -429 1198 -367 C ATOM 1806 O MET B 1 37.762 -1.803 17.165 1.00 34.77 O ANISOU 1806 O MET B 1 5877 3197 4136 -600 1099 -199 O ATOM 1807 CB MET B 1 39.153 -1.432 20.271 1.00 34.89 C ANISOU 1807 CB MET B 1 5352 2961 4944 60 866 -216 C ATOM 1808 CG MET B 1 37.679 -1.459 20.635 1.00 32.88 C ANISOU 1808 CG MET B 1 5224 2756 4513 176 638 -21 C ATOM 1809 SD MET B 1 37.435 -1.779 22.393 1.00 39.76 S ANISOU 1809 SD MET B 1 5874 3701 5531 378 362 20 S ATOM 1810 CE MET B 1 35.665 -2.045 22.461 1.00 28.90 C ANISOU 1810 CE MET B 1 4628 2397 3956 381 305 60 C ATOM 1811 N GLN B 2 38.909 -3.496 18.100 1.00 38.33 N ANISOU 1811 N GLN B 2 5820 3563 5181 -320 1302 -601 N ATOM 1812 CA GLN B 2 38.288 -4.517 17.267 1.00 38.36 C ANISOU 1812 CA GLN B 2 5888 3647 5039 -431 1405 -694 C ATOM 1813 C GLN B 2 37.443 -5.502 18.071 1.00 34.28 C ANISOU 1813 C GLN B 2 5339 3053 4633 -164 1184 -604 C ATOM 1814 O GLN B 2 37.891 -6.034 19.085 1.00 35.18 O ANISOU 1814 O GLN B 2 5303 3006 5057 41 1037 -658 O ATOM 1815 CB GLN B 2 39.362 -5.265 16.476 1.00 43.79 C ANISOU 1815 CB GLN B 2 6352 4374 5911 -640 1754 -1151 C ATOM 1816 CG GLN B 2 38.825 -6.307 15.514 1.00 46.23 C ANISOU 1816 CG GLN B 2 6713 4782 6072 -794 1900 -1298 C ATOM 1817 CD GLN B 2 39.877 -6.769 14.527 1.00 52.07 C ANISOU 1817 CD GLN B 2 7183 5667 6934 -1114 2241 -1739 C ATOM 1818 OE1 GLN B 2 39.965 -6.254 13.412 1.00 56.32 O ANISOU 1818 OE1 GLN B 2 7930 6371 7099 -1585 2503 -1796 O ATOM 1819 NE2 GLN B 2 40.685 -7.741 14.933 1.00 53.36 N ANISOU 1819 NE2 GLN B 2 6887 5774 7613 -900 2129 -2003 N ATOM 1820 N ILE B 3 36.216 -5.732 17.613 1.00 32.70 N ANISOU 1820 N ILE B 3 5317 2949 4157 -214 1123 -470 N ATOM 1821 CA ILE B 3 35.336 -6.732 18.215 1.00 30.62 C ANISOU 1821 CA ILE B 3 5053 2656 3925 -76 983 -429 C ATOM 1822 C ILE B 3 34.744 -7.630 17.135 1.00 30.79 C ANISOU 1822 C ILE B 3 5147 2766 3785 -214 1104 -525 C ATOM 1823 O ILE B 3 34.819 -7.319 15.947 1.00 31.93 O ANISOU 1823 O ILE B 3 5398 3010 3725 -434 1261 -576 O ATOM 1824 CB ILE B 3 34.180 -6.089 19.012 1.00 28.63 C ANISOU 1824 CB ILE B 3 4878 2459 3541 17 770 -235 C ATOM 1825 CG1 ILE B 3 33.245 -5.321 18.076 1.00 28.91 C ANISOU 1825 CG1 ILE B 3 5052 2599 3333 -74 696 -164 C ATOM 1826 CG2 ILE B 3 34.717 -5.188 20.115 1.00 26.77 C ANISOU 1826 CG2 ILE B 3 4574 2150 3447 136 656 -154 C ATOM 1827 CD1 ILE B 3 32.027 -4.752 18.770 1.00 29.35 C ANISOU 1827 CD1 ILE B 3 5066 2705 3382 37 467 -138 C ATOM 1828 N PHE B 4 34.150 -8.743 17.549 1.00 31.12 N ANISOU 1828 N PHE B 4 5184 2764 3876 -141 1020 -542 N ATOM 1829 CA PHE B 4 33.578 -9.692 16.601 1.00 34.85 C ANISOU 1829 CA PHE B 4 5708 3307 4226 -248 1121 -642 C ATOM 1830 C PHE B 4 32.108 -9.956 16.898 1.00 35.63 C ANISOU 1830 C PHE B 4 5914 3486 4138 -235 988 -519 C ATOM 1831 O PHE B 4 31.726 -10.157 18.051 1.00 37.51 O ANISOU 1831 O PHE B 4 6157 3677 4416 -180 856 -454 O ATOM 1832 CB PHE B 4 34.361 -11.006 16.627 1.00 36.36 C ANISOU 1832 CB PHE B 4 5756 3339 4722 -207 1147 -886 C ATOM 1833 CG PHE B 4 35.848 -10.829 16.504 1.00 39.15 C ANISOU 1833 CG PHE B 4 5848 3644 5384 -191 1218 -1110 C ATOM 1834 CD1 PHE B 4 36.435 -10.608 15.269 1.00 41.39 C ANISOU 1834 CD1 PHE B 4 6029 4092 5606 -418 1525 -1340 C ATOM 1835 CD2 PHE B 4 36.660 -10.886 17.625 1.00 40.32 C ANISOU 1835 CD2 PHE B 4 5855 3618 5846 -3 946 -1100 C ATOM 1836 CE1 PHE B 4 37.804 -10.446 15.155 1.00 43.13 C ANISOU 1836 CE1 PHE B 4 5945 4323 6118 -461 1624 -1608 C ATOM 1837 CE2 PHE B 4 38.028 -10.725 17.518 1.00 41.76 C ANISOU 1837 CE2 PHE B 4 5754 3788 6324 24 973 -1335 C ATOM 1838 CZ PHE B 4 38.601 -10.504 16.281 1.00 42.93 C ANISOU 1838 CZ PHE B 4 5728 4121 6462 -207 1343 -1618 C ATOM 1839 N VAL B 5 31.280 -9.959 15.859 1.00 33.17 N ANISOU 1839 N VAL B 5 5699 3294 3609 -338 1025 -526 N ATOM 1840 CA VAL B 5 29.861 -10.254 16.038 1.00 31.04 C ANISOU 1840 CA VAL B 5 5460 3107 3225 -330 912 -512 C ATOM 1841 C VAL B 5 29.498 -11.624 15.457 1.00 33.11 C ANISOU 1841 C VAL B 5 5755 3383 3445 -407 1005 -614 C ATOM 1842 O VAL B 5 29.790 -11.918 14.295 1.00 33.03 O ANISOU 1842 O VAL B 5 5797 3396 3358 -506 1128 -689 O ATOM 1843 CB VAL B 5 28.969 -9.147 15.438 1.00 29.78 C ANISOU 1843 CB VAL B 5 5372 3011 2930 -336 735 -471 C ATOM 1844 CG1 VAL B 5 27.508 -9.494 15.612 1.00 25.64 C ANISOU 1844 CG1 VAL B 5 4778 2574 2391 -315 622 -588 C ATOM 1845 CG2 VAL B 5 29.276 -7.810 16.099 1.00 25.07 C ANISOU 1845 CG2 VAL B 5 4733 2371 2421 -241 589 -389 C ATOM 1846 N LYS B 6 28.868 -12.462 16.276 1.00 34.88 N ANISOU 1846 N LYS B 6 5973 3595 3684 -421 956 -634 N ATOM 1847 CA LYS B 6 28.542 -13.835 15.887 1.00 36.34 C ANISOU 1847 CA LYS B 6 6207 3752 3847 -499 1001 -718 C ATOM 1848 C LYS B 6 27.057 -14.018 15.573 1.00 34.16 C ANISOU 1848 C LYS B 6 5907 3648 3425 -569 971 -752 C ATOM 1849 O LYS B 6 26.196 -13.592 16.348 1.00 33.98 O ANISOU 1849 O LYS B 6 5817 3725 3369 -605 914 -786 O ATOM 1850 CB LYS B 6 28.933 -14.809 16.999 1.00 41.57 C ANISOU 1850 CB LYS B 6 6947 4221 4628 -539 884 -694 C ATOM 1851 CG LYS B 6 30.087 -15.734 16.642 1.00 47.34 C ANISOU 1851 CG LYS B 6 7643 4718 5628 -469 834 -806 C ATOM 1852 CD LYS B 6 29.920 -16.327 15.247 1.00 51.78 C ANISOU 1852 CD LYS B 6 8122 5386 6168 -493 993 -960 C ATOM 1853 CE LYS B 6 29.062 -17.591 15.228 1.00 54.20 C ANISOU 1853 CE LYS B 6 8534 5659 6401 -585 912 -971 C ATOM 1854 NZ LYS B 6 29.864 -18.840 15.054 1.00 58.04 N ANISOU 1854 NZ LYS B 6 8946 5907 7201 -523 757 -1131 N ATOM 1855 N THR B 7 26.763 -14.666 14.447 1.00 33.57 N ANISOU 1855 N THR B 7 5831 3616 3310 -601 1007 -791 N ATOM 1856 CA THR B 7 25.383 -14.980 14.081 1.00 34.30 C ANISOU 1856 CA THR B 7 5872 3835 3326 -646 950 -853 C ATOM 1857 C THR B 7 25.109 -16.473 14.226 1.00 35.20 C ANISOU 1857 C THR B 7 6008 3919 3448 -745 992 -882 C ATOM 1858 O THR B 7 26.033 -17.281 14.323 1.00 36.93 O ANISOU 1858 O THR B 7 6316 3980 3736 -756 1025 -884 O ATOM 1859 CB THR B 7 25.039 -14.530 12.644 1.00 35.42 C ANISOU 1859 CB THR B 7 6087 4014 3357 -644 897 -875 C ATOM 1860 OG1 THR B 7 25.828 -15.265 11.700 1.00 36.64 O ANISOU 1860 OG1 THR B 7 6290 4134 3498 -713 1023 -863 O ATOM 1861 CG2 THR B 7 25.299 -13.041 12.473 1.00 36.21 C ANISOU 1861 CG2 THR B 7 6310 4067 3380 -611 783 -841 C ATOM 1862 N LEU B 8 23.831 -16.832 14.226 1.00 33.06 N ANISOU 1862 N LEU B 8 5293 3281 3987 -1290 415 94 N ATOM 1863 CA LEU B 8 23.420 -18.213 14.442 1.00 31.48 C ANISOU 1863 CA LEU B 8 5037 2979 3946 -1297 383 101 C ATOM 1864 C LEU B 8 23.813 -19.154 13.302 1.00 35.54 C ANISOU 1864 C LEU B 8 5794 3311 4400 -1540 556 -149 C ATOM 1865 O LEU B 8 23.861 -20.365 13.492 1.00 37.50 O ANISOU 1865 O LEU B 8 6002 3425 4822 -1527 614 -213 O ATOM 1866 CB LEU B 8 21.914 -18.280 14.703 1.00 29.25 C ANISOU 1866 CB LEU B 8 4713 2805 3596 -1315 83 388 C ATOM 1867 CG LEU B 8 21.494 -17.915 16.128 1.00 26.71 C ANISOU 1867 CG LEU B 8 4098 2615 3435 -1008 -69 646 C ATOM 1868 CD1 LEU B 8 20.010 -17.609 16.191 1.00 25.82 C ANISOU 1868 CD1 LEU B 8 3979 2648 3184 -1041 -357 953 C ATOM 1869 CD2 LEU B 8 21.853 -19.043 17.087 1.00 26.38 C ANISOU 1869 CD2 LEU B 8 3832 2476 3714 -813 5 624 C ATOM 1870 N THR B 9 24.098 -18.602 12.126 1.00 37.66 N ANISOU 1870 N THR B 9 6310 3579 4420 -1737 643 -288 N ATOM 1871 CA THR B 9 24.498 -19.426 10.986 1.00 39.76 C ANISOU 1871 CA THR B 9 6766 3752 4588 -1868 794 -509 C ATOM 1872 C THR B 9 25.933 -19.924 11.135 1.00 39.77 C ANISOU 1872 C THR B 9 6693 3640 4779 -1741 1096 -722 C ATOM 1873 O THR B 9 26.334 -20.895 10.494 1.00 41.82 O ANISOU 1873 O THR B 9 7055 3799 5036 -1790 1241 -874 O ATOM 1874 CB THR B 9 24.379 -18.663 9.650 1.00 42.35 C ANISOU 1874 CB THR B 9 7350 4168 4574 -2055 798 -561 C ATOM 1875 OG1 THR B 9 25.306 -17.571 9.632 1.00 41.63 O ANISOU 1875 OG1 THR B 9 7244 4125 4449 -1993 951 -623 O ATOM 1876 CG2 THR B 9 22.969 -18.133 9.458 1.00 43.01 C ANISOU 1876 CG2 THR B 9 7504 4387 4451 -2176 503 -340 C ATOM 1877 N GLY B 10 26.700 -19.251 11.986 1.00 37.82 N ANISOU 1877 N GLY B 10 6263 3418 4690 -1572 1190 -716 N ATOM 1878 CA GLY B 10 28.099 -19.582 12.181 1.00 37.90 C ANISOU 1878 CA GLY B 10 6165 3358 4879 -1438 1471 -890 C ATOM 1879 C GLY B 10 29.013 -18.506 11.628 1.00 39.63 C ANISOU 1879 C GLY B 10 6440 3647 4970 -1469 1624 -979 C ATOM 1880 O GLY B 10 30.237 -18.607 11.713 1.00 40.53 O ANISOU 1880 O GLY B 10 6454 3733 5213 -1376 1858 -1099 O ATOM 1881 N LYS B 11 28.410 -17.465 11.063 1.00 40.01 N ANISOU 1881 N LYS B 11 6638 3795 4768 -1601 1490 -900 N ATOM 1882 CA LYS B 11 29.159 -16.361 10.476 1.00 41.34 C ANISOU 1882 CA LYS B 11 6879 4030 4798 -1648 1620 -962 C ATOM 1883 C LYS B 11 29.755 -15.437 11.536 1.00 41.32 C ANISOU 1883 C LYS B 11 6666 4070 4963 -1492 1637 -922 C ATOM 1884 O LYS B 11 29.078 -15.054 12.489 1.00 40.05 O ANISOU 1884 O LYS B 11 6388 3953 4878 -1404 1443 -759 O ATOM 1885 CB LYS B 11 28.263 -15.557 9.533 1.00 41.54 C ANISOU 1885 CB LYS B 11 7138 4148 4498 -1832 1472 -877 C ATOM 1886 CG LYS B 11 28.934 -14.337 8.934 1.00 44.42 C ANISOU 1886 CG LYS B 11 7585 4578 4716 -1888 1597 -911 C ATOM 1887 CD LYS B 11 28.035 -13.653 7.924 1.00 46.90 C ANISOU 1887 CD LYS B 11 8141 4975 4703 -2072 1471 -821 C ATOM 1888 CE LYS B 11 28.798 -12.599 7.145 1.00 48.77 C ANISOU 1888 CE LYS B 11 8469 5238 4824 -2154 1640 -848 C ATOM 1889 NZ LYS B 11 27.988 -12.052 6.024 1.00 50.72 N ANISOU 1889 NZ LYS B 11 8915 5520 4837 -2318 1507 -755 N ATOM 1890 N THR B 12 31.024 -15.082 11.358 1.00 42.39 N ANISOU 1890 N THR B 12 6743 4203 5159 -1459 1865 -1042 N ATOM 1891 CA THR B 12 31.699 -14.145 12.249 1.00 41.26 C ANISOU 1891 CA THR B 12 6412 4103 5161 -1332 1890 -1024 C ATOM 1892 C THR B 12 31.950 -12.813 11.547 1.00 40.30 C ANISOU 1892 C THR B 12 6425 4057 4831 -1452 1921 -1020 C ATOM 1893 O THR B 12 32.614 -12.760 10.512 1.00 43.83 O ANISOU 1893 O THR B 12 6977 4490 5185 -1572 2099 -1097 O ATOM 1894 CB THR B 12 33.037 -14.716 12.765 1.00 43.67 C ANISOU 1894 CB THR B 12 6483 4368 5743 -1190 2107 -1128 C ATOM 1895 OG1 THR B 12 32.781 -15.838 13.618 1.00 46.08 O ANISOU 1895 OG1 THR B 12 6631 4615 6260 -1037 2068 -1107 O ATOM 1896 CG2 THR B 12 33.804 -13.661 13.547 1.00 41.64 C ANISOU 1896 CG2 THR B 12 6035 4177 5609 -1081 2117 -1109 C ATOM 1897 N ILE B 13 31.407 -11.740 12.113 1.00 35.42 N ANISOU 1897 N ILE B 13 5796 3503 4160 -1425 1744 -892 N ATOM 1898 CA ILE B 13 31.560 -10.407 11.544 1.00 34.34 C ANISOU 1898 CA ILE B 13 5787 3434 3825 -1521 1754 -872 C ATOM 1899 C ILE B 13 32.567 -9.592 12.348 1.00 36.06 C ANISOU 1899 C ILE B 13 5811 3672 4218 -1409 1828 -895 C ATOM 1900 O ILE B 13 32.439 -9.460 13.566 1.00 36.03 O ANISOU 1900 O ILE B 13 5589 3732 4370 -1211 1681 -787 O ATOM 1901 CB ILE B 13 30.217 -9.654 11.516 1.00 30.89 C ANISOU 1901 CB ILE B 13 5476 3093 3169 -1557 1487 -667 C ATOM 1902 CG1 ILE B 13 29.152 -10.495 10.814 1.00 30.36 C ANISOU 1902 CG1 ILE B 13 5572 3018 2944 -1671 1378 -630 C ATOM 1903 CG2 ILE B 13 30.373 -8.302 10.836 1.00 30.90 C ANISOU 1903 CG2 ILE B 13 5612 3142 2987 -1622 1466 -673 C ATOM 1904 CD1 ILE B 13 27.741 -10.027 11.074 1.00 29.46 C ANISOU 1904 CD1 ILE B 13 5489 3018 2686 -1646 1080 -389 C ATOM 1905 N THR B 14 33.569 -9.051 11.663 1.00 36.13 N ANISOU 1905 N THR B 14 5853 3651 4225 -1488 1970 -994 N ATOM 1906 CA THR B 14 34.592 -8.242 12.314 1.00 37.20 C ANISOU 1906 CA THR B 14 5815 3794 4524 -1407 2012 -1026 C ATOM 1907 C THR B 14 34.254 -6.758 12.215 1.00 38.12 C ANISOU 1907 C THR B 14 6043 3980 4461 -1438 1883 -939 C ATOM 1908 O THR B 14 34.048 -6.231 11.122 1.00 40.58 O ANISOU 1908 O THR B 14 6563 4265 4591 -1576 1869 -950 O ATOM 1909 CB THR B 14 35.981 -8.485 11.695 1.00 39.47 C ANISOU 1909 CB THR B 14 6044 3996 4959 -1469 2206 -1151 C ATOM 1910 OG1 THR B 14 36.295 -9.882 11.754 1.00 40.76 O ANISOU 1910 OG1 THR B 14 6105 4102 5279 -1424 2310 -1201 O ATOM 1911 CG2 THR B 14 37.046 -7.698 12.444 1.00 38.83 C ANISOU 1911 CG2 THR B 14 5765 3945 5043 -1376 2221 -1176 C ATOM 1912 N LEU B 15 34.197 -6.088 13.361 1.00 34.59 N ANISOU 1912 N LEU B 15 5445 3612 4084 -1308 1783 -836 N ATOM 1913 CA LEU B 15 33.889 -4.665 13.398 1.00 34.42 C ANISOU 1913 CA LEU B 15 5522 3641 3914 -1323 1655 -732 C ATOM 1914 C LEU B 15 35.013 -3.865 14.037 1.00 36.37 C ANISOU 1914 C LEU B 15 5615 3890 4316 -1284 1728 -786 C ATOM 1915 O LEU B 15 35.695 -4.344 14.942 1.00 36.61 O ANISOU 1915 O LEU B 15 5402 3929 4581 -1178 1788 -833 O ATOM 1916 CB LEU B 15 32.595 -4.411 14.174 1.00 33.26 C ANISOU 1916 CB LEU B 15 5393 3575 3669 -1216 1425 -514 C ATOM 1917 CG LEU B 15 31.280 -4.911 13.581 1.00 32.65 C ANISOU 1917 CG LEU B 15 5467 3526 3411 -1248 1274 -410 C ATOM 1918 CD1 LEU B 15 30.139 -4.591 14.528 1.00 31.34 C ANISOU 1918 CD1 LEU B 15 5264 3450 3195 -1089 1028 -174 C ATOM 1919 CD2 LEU B 15 31.036 -4.291 12.216 1.00 32.49 C ANISOU 1919 CD2 LEU B 15 5656 3490 3199 -1388 1244 -450 C ATOM 1920 N GLU B 16 35.198 -2.641 13.556 1.00 38.41 N ANISOU 1920 N GLU B 16 6002 4142 4449 -1365 1709 -779 N ATOM 1921 CA GLU B 16 36.106 -1.701 14.191 1.00 39.05 C ANISOU 1921 CA GLU B 16 5970 4229 4641 -1351 1747 -805 C ATOM 1922 C GLU B 16 35.246 -0.693 14.939 1.00 35.75 C ANISOU 1922 C GLU B 16 5622 3855 4104 -1285 1559 -631 C ATOM 1923 O GLU B 16 34.378 -0.052 14.348 1.00 35.73 O ANISOU 1923 O GLU B 16 5824 3865 3888 -1309 1436 -536 O ATOM 1924 CB GLU B 16 36.975 -1.000 13.146 1.00 44.62 C ANISOU 1924 CB GLU B 16 6777 4882 5296 -1487 1873 -915 C ATOM 1925 CG GLU B 16 38.290 -0.455 13.685 1.00 50.10 C ANISOU 1925 CG GLU B 16 7292 5571 6173 -1490 1972 -993 C ATOM 1926 CD GLU B 16 39.301 -1.549 13.984 1.00 54.78 C ANISOU 1926 CD GLU B 16 7648 6147 7021 -1436 2098 -1107 C ATOM 1927 OE1 GLU B 16 39.123 -2.682 13.489 1.00 56.22 O ANISOU 1927 OE1 GLU B 16 7852 6292 7219 -1429 2152 -1149 O ATOM 1928 OE2 GLU B 16 40.278 -1.273 14.713 1.00 56.27 O ANISOU 1928 OE2 GLU B 16 7630 6354 7397 -1400 2127 -1146 O ATOM 1929 N VAL B 17 35.469 -0.568 16.243 1.00 32.16 N ANISOU 1929 N VAL B 17 4976 3430 3812 -1135 1463 -594 N ATOM 1930 CA VAL B 17 34.604 0.259 17.076 1.00 28.69 C ANISOU 1930 CA VAL B 17 4596 3032 3274 -990 1225 -425 C ATOM 1931 C VAL B 17 35.373 1.132 18.058 1.00 29.31 C ANISOU 1931 C VAL B 17 4553 3103 3478 -920 1166 -453 C ATOM 1932 O VAL B 17 36.537 0.875 18.364 1.00 29.89 O ANISOU 1932 O VAL B 17 4424 3167 3767 -938 1271 -589 O ATOM 1933 CB VAL B 17 33.611 -0.603 17.885 1.00 25.57 C ANISOU 1933 CB VAL B 17 4101 2703 2912 -771 1037 -298 C ATOM 1934 CG1 VAL B 17 32.567 -1.229 16.972 1.00 24.45 C ANISOU 1934 CG1 VAL B 17 4122 2573 2593 -846 1030 -223 C ATOM 1935 CG2 VAL B 17 34.357 -1.670 18.672 1.00 22.32 C ANISOU 1935 CG2 VAL B 17 3394 2305 2781 -644 1075 -398 C ATOM 1936 N GLU B 18 34.703 2.170 18.545 1.00 32.87 N ANISOU 1936 N GLU B 18 4781 2642 5066 -470 643 -816 N ATOM 1937 CA GLU B 18 35.219 2.985 19.632 1.00 32.28 C ANISOU 1937 CA GLU B 18 4509 2577 5177 -500 554 -793 C ATOM 1938 C GLU B 18 34.716 2.381 20.935 1.00 29.52 C ANISOU 1938 C GLU B 18 3990 2342 4884 -352 275 -771 C ATOM 1939 O GLU B 18 33.595 1.875 20.988 1.00 29.92 O ANISOU 1939 O GLU B 18 4151 2435 4784 -293 122 -719 O ATOM 1940 CB GLU B 18 34.718 4.424 19.503 1.00 34.01 C ANISOU 1940 CB GLU B 18 4958 2713 5252 -557 513 -686 C ATOM 1941 CG GLU B 18 35.089 5.112 18.198 1.00 37.48 C ANISOU 1941 CG GLU B 18 5651 3012 5576 -709 813 -635 C ATOM 1942 CD GLU B 18 36.523 5.604 18.178 1.00 42.81 C ANISOU 1942 CD GLU B 18 6145 3637 6485 -947 1050 -677 C ATOM 1943 OE1 GLU B 18 37.200 5.520 19.223 1.00 44.73 O ANISOU 1943 OE1 GLU B 18 6060 3967 6967 -971 947 -775 O ATOM 1944 OE2 GLU B 18 36.972 6.081 17.116 1.00 47.46 O ANISOU 1944 OE2 GLU B 18 6888 4173 6974 -1100 1329 -597 O ATOM 1945 N PRO B 19 35.541 2.428 21.991 1.00 28.53 N ANISOU 1945 N PRO B 19 3576 2272 4991 -314 229 -834 N ATOM 1946 CA PRO B 19 35.155 1.889 23.301 1.00 27.57 C ANISOU 1946 CA PRO B 19 3278 2259 4938 -149 -6 -808 C ATOM 1947 C PRO B 19 33.879 2.532 23.840 1.00 27.23 C ANISOU 1947 C PRO B 19 3344 2287 4716 -93 -242 -707 C ATOM 1948 O PRO B 19 33.186 1.931 24.661 1.00 28.35 O ANISOU 1948 O PRO B 19 3396 2519 4856 26 -436 -655 O ATOM 1949 CB PRO B 19 36.345 2.259 24.192 1.00 28.42 C ANISOU 1949 CB PRO B 19 3056 2415 5327 -127 -6 -953 C ATOM 1950 CG PRO B 19 37.496 2.364 23.254 1.00 29.49 C ANISOU 1950 CG PRO B 19 3135 2524 5546 -278 282 -1053 C ATOM 1951 CD PRO B 19 36.924 2.937 21.990 1.00 30.21 C ANISOU 1951 CD PRO B 19 3575 2460 5445 -444 415 -969 C ATOM 1952 N SER B 20 33.574 3.736 23.368 1.00 27.33 N ANISOU 1952 N SER B 20 3562 2233 4590 -157 -226 -687 N ATOM 1953 CA SER B 20 32.417 4.483 23.843 1.00 26.97 C ANISOU 1953 CA SER B 20 3636 2242 4370 -25 -466 -638 C ATOM 1954 C SER B 20 31.272 4.494 22.836 1.00 28.24 C ANISOU 1954 C SER B 20 4072 2447 4211 -6 -465 -552 C ATOM 1955 O SER B 20 30.333 5.279 22.970 1.00 30.78 O ANISOU 1955 O SER B 20 4538 2877 4279 149 -623 -496 O ATOM 1956 CB SER B 20 32.819 5.919 24.164 1.00 29.64 C ANISOU 1956 CB SER B 20 4063 2484 4715 -37 -479 -674 C ATOM 1957 OG SER B 20 33.235 6.599 22.993 1.00 32.90 O ANISOU 1957 OG SER B 20 4753 2668 5079 -216 -242 -656 O ATOM 1958 N ASP B 21 31.354 3.636 21.824 1.00 26.44 N ANISOU 1958 N ASP B 21 3912 2180 3955 -124 -295 -562 N ATOM 1959 CA ASP B 21 30.292 3.540 20.828 1.00 26.86 C ANISOU 1959 CA ASP B 21 4181 2348 3676 -110 -299 -517 C ATOM 1960 C ASP B 21 28.993 3.085 21.472 1.00 26.85 C ANISOU 1960 C ASP B 21 4065 2662 3475 -25 -555 -455 C ATOM 1961 O ASP B 21 28.987 2.174 22.299 1.00 27.59 O ANISOU 1961 O ASP B 21 3945 2822 3717 -67 -642 -438 O ATOM 1962 CB ASP B 21 30.674 2.564 19.713 1.00 28.71 C ANISOU 1962 CB ASP B 21 4483 2497 3928 -246 -94 -591 C ATOM 1963 CG ASP B 21 31.232 3.261 18.491 1.00 31.10 C ANISOU 1963 CG ASP B 21 5009 2663 4142 -286 156 -596 C ATOM 1964 OD1 ASP B 21 30.894 4.443 18.275 1.00 33.97 O ANISOU 1964 OD1 ASP B 21 5574 3008 4326 -209 148 -509 O ATOM 1965 OD2 ASP B 21 32.004 2.625 17.743 1.00 30.75 O ANISOU 1965 OD2 ASP B 21 4964 2534 4184 -369 366 -676 O ATOM 1966 N THR B 22 27.891 3.723 21.096 1.00 26.43 N ANISOU 1966 N THR B 22 4149 2837 3056 109 -665 -406 N ATOM 1967 CA THR B 22 26.581 3.277 21.540 1.00 25.87 C ANISOU 1967 CA THR B 22 3919 3183 2727 159 -888 -353 C ATOM 1968 C THR B 22 26.285 1.938 20.881 1.00 29.81 C ANISOU 1968 C THR B 22 4382 3731 3215 -100 -830 -407 C ATOM 1969 O THR B 22 26.911 1.581 19.884 1.00 29.34 O ANISOU 1969 O THR B 22 4481 3428 3239 -216 -636 -500 O ATOM 1970 CB THR B 22 25.479 4.273 21.153 1.00 25.18 C ANISOU 1970 CB THR B 22 3947 3400 2219 403 -978 -304 C ATOM 1971 OG1 THR B 22 25.375 4.339 19.726 1.00 27.35 O ANISOU 1971 OG1 THR B 22 4489 3644 2260 387 -860 -359 O ATOM 1972 CG2 THR B 22 25.789 5.657 21.700 1.00 25.68 C ANISOU 1972 CG2 THR B 22 4137 3297 2324 653 -995 -271 C ATOM 1973 N ILE B 23 25.333 1.197 21.434 1.00 24.73 N ANISOU 1973 N ILE B 23 3302 2682 3412 -429 -107 -5 N ATOM 1974 CA ILE B 23 24.962 -0.095 20.869 1.00 27.49 C ANISOU 1974 CA ILE B 23 3662 3078 3703 -421 -182 -27 C ATOM 1975 C ILE B 23 24.372 0.053 19.466 1.00 30.73 C ANISOU 1975 C ILE B 23 4287 3406 3982 -379 -303 21 C ATOM 1976 O ILE B 23 24.662 -0.740 18.571 1.00 31.03 O ANISOU 1976 O ILE B 23 4396 3490 3905 -375 -283 18 O ATOM 1977 CB ILE B 23 23.984 -0.855 21.792 1.00 25.58 C ANISOU 1977 CB ILE B 23 3277 2942 3500 -354 -204 -105 C ATOM 1978 CG1 ILE B 23 24.596 -1.033 23.185 1.00 26.12 C ANISOU 1978 CG1 ILE B 23 3288 3108 3530 -366 -85 -122 C ATOM 1979 CG2 ILE B 23 23.621 -2.202 21.192 1.00 24.55 C ANISOU 1979 CG2 ILE B 23 3131 2856 3340 -335 -248 -142 C ATOM 1980 CD1 ILE B 23 26.000 -1.609 23.185 1.00 28.10 C ANISOU 1980 CD1 ILE B 23 3553 3397 3728 -385 -42 -100 C ATOM 1981 N GLU B 24 23.553 1.086 19.275 1.00 33.49 N ANISOU 1981 N GLU B 24 4731 3661 4334 -299 -422 52 N ATOM 1982 CA GLU B 24 22.908 1.344 17.977 1.00 38.28 C ANISOU 1982 CA GLU B 24 5563 4201 4782 -179 -572 92 C ATOM 1983 C GLU B 24 23.913 1.790 16.916 1.00 37.76 C ANISOU 1983 C GLU B 24 5779 4066 4504 -230 -430 221 C ATOM 1984 O GLU B 24 23.652 1.660 15.719 1.00 39.70 O ANISOU 1984 O GLU B 24 6257 4283 4543 -150 -514 259 O ATOM 1985 CB GLU B 24 21.781 2.374 18.114 1.00 43.68 C ANISOU 1985 CB GLU B 24 6275 4773 5548 -59 -772 72 C ATOM 1986 CG GLU B 24 22.225 3.844 18.010 1.00 50.97 C ANISOU 1986 CG GLU B 24 7391 5537 6437 -75 -720 201 C ATOM 1987 CD GLU B 24 21.702 4.689 19.162 1.00 57.10 C ANISOU 1987 CD GLU B 24 7987 6264 7445 -71 -769 135 C ATOM 1988 OE1 GLU B 24 21.236 4.105 20.165 1.00 57.39 O ANISOU 1988 OE1 GLU B 24 7754 6404 7646 -97 -775 1 O ATOM 1989 OE2 GLU B 24 21.765 5.937 19.073 1.00 60.46 O ANISOU 1989 OE2 GLU B 24 8515 6590 7867 -49 -758 202 O ATOM 1990 N ASN B 25 25.052 2.325 17.352 1.00 33.64 N ANISOU 1990 N ASN B 25 5242 3508 4031 -367 -206 268 N ATOM 1991 CA ASN B 25 26.108 2.659 16.412 1.00 32.40 C ANISOU 1991 CA ASN B 25 5323 3281 3707 -462 5 353 C ATOM 1992 C ASN B 25 26.828 1.388 15.982 1.00 30.92 C ANISOU 1992 C ASN B 25 5067 3221 3460 -530 124 279 C ATOM 1993 O ASN B 25 27.341 1.298 14.869 1.00 32.47 O ANISOU 1993 O ASN B 25 5488 3390 3457 -574 251 317 O ATOM 1994 CB ASN B 25 27.091 3.654 17.024 1.00 32.61 C ANISOU 1994 CB ASN B 25 5209 3301 3881 -542 201 338 C ATOM 1995 CG ASN B 25 27.975 4.312 15.982 1.00 37.66 C ANISOU 1995 CG ASN B 25 6051 3875 4384 -601 398 385 C ATOM 1996 OD1 ASN B 25 27.614 4.389 14.805 1.00 39.54 O ANISOU 1996 OD1 ASN B 25 6584 4046 4393 -554 364 459 O ATOM 1997 ND2 ASN B 25 29.138 4.789 16.407 1.00 39.51 N ANISOU 1997 ND2 ASN B 25 6132 4124 4757 -690 587 321 N ATOM 1998 N VAL B 26 26.857 0.405 16.878 1.00 27.90 N ANISOU 1998 N VAL B 26 4390 2965 3244 -538 85 167 N ATOM 1999 CA VAL B 26 27.385 -0.912 16.553 1.00 27.89 C ANISOU 1999 CA VAL B 26 4295 3077 3225 -574 144 79 C ATOM 2000 C VAL B 26 26.438 -1.608 15.580 1.00 30.15 C ANISOU 2000 C VAL B 26 4696 3408 3352 -458 -22 69 C ATOM 2001 O VAL B 26 26.873 -2.248 14.622 1.00 31.85 O ANISOU 2001 O VAL B 26 5006 3666 3429 -482 54 38 O ATOM 2002 CB VAL B 26 27.558 -1.784 17.815 1.00 22.52 C ANISOU 2002 CB VAL B 26 3317 2485 2753 -590 110 -21 C ATOM 2003 CG1 VAL B 26 28.053 -3.173 17.444 1.00 17.63 C ANISOU 2003 CG1 VAL B 26 2610 1957 2132 -608 142 -115 C ATOM 2004 CG2 VAL B 26 28.511 -1.119 18.795 1.00 22.37 C ANISOU 2004 CG2 VAL B 26 3152 2465 2883 -619 212 -40 C ATOM 2005 N LYS B 27 25.139 -1.471 15.831 1.00 29.47 N ANISOU 2005 N LYS B 27 4582 3309 3305 -332 -249 62 N ATOM 2006 CA LYS B 27 24.120 -2.033 14.952 1.00 29.51 C ANISOU 2006 CA LYS B 27 4670 3345 3200 -197 -450 11 C ATOM 2007 C LYS B 27 24.140 -1.352 13.588 1.00 32.55 C ANISOU 2007 C LYS B 27 5425 3646 3297 -137 -477 106 C ATOM 2008 O LYS B 27 23.817 -1.967 12.571 1.00 36.77 O ANISOU 2008 O LYS B 27 6086 4224 3662 -56 -575 60 O ATOM 2009 CB LYS B 27 22.732 -1.902 15.585 1.00 29.12 C ANISOU 2009 CB LYS B 27 4477 3277 3309 -82 -677 -63 C ATOM 2010 CG LYS B 27 22.580 -2.629 16.912 1.00 26.64 C ANISOU 2010 CG LYS B 27 3856 3029 3237 -148 -631 -154 C ATOM 2011 CD LYS B 27 21.156 -2.538 17.437 1.00 26.95 C ANISOU 2011 CD LYS B 27 3753 3044 3442 -59 -808 -267 C ATOM 2012 CE LYS B 27 20.985 -3.355 18.707 1.00 27.59 C ANISOU 2012 CE LYS B 27 3576 3211 3696 -120 -626 -301 C ATOM 2013 NZ LYS B 27 19.579 -3.334 19.199 1.00 29.11 N ANISOU 2013 NZ LYS B 27 3638 3401 4022 -42 -645 -379 N ATOM 2014 N ALA B 28 24.519 -0.078 13.574 1.00 31.75 N ANISOU 2014 N ALA B 28 5519 3413 3133 -177 -387 237 N ATOM 2015 CA ALA B 28 24.631 0.680 12.333 1.00 30.47 C ANISOU 2015 CA ALA B 28 5766 3132 2681 -139 -370 354 C ATOM 2016 C ALA B 28 25.788 0.157 11.489 1.00 33.30 C ANISOU 2016 C ALA B 28 6220 3540 2893 -273 -96 341 C ATOM 2017 O ALA B 28 25.686 0.071 10.265 1.00 38.30 O ANISOU 2017 O ALA B 28 7061 4159 3332 -211 -117 344 O ATOM 2018 CB ALA B 28 24.815 2.160 12.628 1.00 26.06 C ANISOU 2018 CB ALA B 28 5291 2424 2186 -168 -294 451 C ATOM 2019 N LYS B 29 26.887 -0.190 12.151 1.00 32.23 N ANISOU 2019 N LYS B 29 5905 3455 2885 -454 159 303 N ATOM 2020 CA LYS B 29 28.053 -0.742 11.470 1.00 33.91 C ANISOU 2020 CA LYS B 29 6121 3719 3046 -588 427 229 C ATOM 2021 C LYS B 29 27.738 -2.119 10.905 1.00 36.03 C ANISOU 2021 C LYS B 29 6350 4130 3210 -532 327 122 C ATOM 2022 O LYS B 29 28.241 -2.500 9.848 1.00 38.91 O ANISOU 2022 O LYS B 29 6816 4517 3449 -566 448 79 O ATOM 2023 CB LYS B 29 29.241 -0.829 12.428 1.00 29.79 C ANISOU 2023 CB LYS B 29 5314 3222 2782 -756 662 142 C ATOM 2024 CG LYS B 29 29.753 0.519 12.892 1.00 31.14 C ANISOU 2024 CG LYS B 29 5464 3281 3086 -796 768 179 C ATOM 2025 CD LYS B 29 30.795 0.370 13.985 1.00 31.08 C ANISOU 2025 CD LYS B 29 5108 3330 3370 -878 886 44 C ATOM 2026 CE LYS B 29 31.275 1.728 14.467 1.00 33.48 C ANISOU 2026 CE LYS B 29 5378 3551 3791 -889 963 62 C ATOM 2027 NZ LYS B 29 31.879 2.521 13.360 1.00 36.14 N ANISOU 2027 NZ LYS B 29 5968 3774 3991 -958 1163 84 N ATOM 2028 N ILE B 30 26.903 -2.864 11.622 1.00 34.73 N ANISOU 2028 N ILE B 30 5916 4056 3225 -425 92 43 N ATOM 2029 CA ILE B 30 26.474 -4.181 11.175 1.00 34.97 C ANISOU 2029 CA ILE B 30 5837 4209 3240 -350 -35 -89 C ATOM 2030 C ILE B 30 25.570 -4.041 9.952 1.00 39.84 C ANISOU 2030 C ILE B 30 6734 4807 3598 -190 -232 -66 C ATOM 2031 O ILE B 30 25.641 -4.845 9.021 1.00 40.53 O ANISOU 2031 O ILE B 30 6838 4973 3589 -163 -225 -146 O ATOM 2032 CB ILE B 30 25.741 -4.941 12.303 1.00 31.68 C ANISOU 2032 CB ILE B 30 5069 3856 3112 -288 -209 -180 C ATOM 2033 CG1 ILE B 30 26.698 -5.214 13.468 1.00 29.70 C ANISOU 2033 CG1 ILE B 30 4558 3623 3103 -419 -42 -207 C ATOM 2034 CG2 ILE B 30 25.152 -6.246 11.787 1.00 31.46 C ANISOU 2034 CG2 ILE B 30 4939 3926 3087 -205 -347 -323 C ATOM 2035 CD1 ILE B 30 26.067 -5.949 14.631 1.00 26.64 C ANISOU 2035 CD1 ILE B 30 3895 3271 2955 -380 -171 -271 C ATOM 2036 N GLN B 31 24.738 -3.002 9.952 1.00 44.25 N ANISOU 2036 N GLN B 31 7425 5253 4134 -70 -405 33 N ATOM 2037 CA GLN B 31 23.811 -2.754 8.848 1.00 51.82 C ANISOU 2037 CA GLN B 31 8563 6165 4961 110 -612 40 C ATOM 2038 C GLN B 31 24.531 -2.427 7.542 1.00 57.23 C ANISOU 2038 C GLN B 31 9568 6800 5378 60 -440 116 C ATOM 2039 O GLN B 31 24.321 -3.106 6.536 1.00 60.24 O ANISOU 2039 O GLN B 31 10012 7249 5626 128 -503 48 O ATOM 2040 CB GLN B 31 22.817 -1.640 9.187 1.00 55.28 C ANISOU 2040 CB GLN B 31 9060 6469 5475 243 -827 94 C ATOM 2041 CG GLN B 31 21.894 -1.302 8.015 1.00 60.66 C ANISOU 2041 CG GLN B 31 9955 7072 6021 433 -1046 79 C ATOM 2042 CD GLN B 31 21.088 -0.032 8.227 1.00 64.35 C ANISOU 2042 CD GLN B 31 10532 7374 6544 551 -1227 121 C ATOM 2043 OE1 GLN B 31 21.553 0.919 8.859 1.00 65.05 O ANISOU 2043 OE1 GLN B 31 10676 7375 6665 461 -1113 229 O ATOM 2044 NE2 GLN B 31 19.870 -0.011 7.692 1.00 66.43 N ANISOU 2044 NE2 GLN B 31 10813 7589 6838 755 -1510 13 N ATOM 2045 N ASP B 32 25.376 -1.396 7.545 1.00 60.29 N ANISOU 2045 N ASP B 32 10142 7062 5703 -67 -213 240 N ATOM 2046 CA ASP B 32 26.131 -1.056 6.335 1.00 66.76 C ANISOU 2046 CA ASP B 32 11260 7814 6293 -144 -7 295 C ATOM 2047 C ASP B 32 27.254 -2.061 6.029 1.00 66.90 C ANISOU 2047 C ASP B 32 11164 7953 6303 -310 263 195 C ATOM 2048 O ASP B 32 28.273 -1.703 5.435 1.00 71.55 O ANISOU 2048 O ASP B 32 11907 8474 6805 -459 546 216 O ATOM 2049 CB ASP B 32 26.653 0.399 6.352 1.00 70.25 C ANISOU 2049 CB ASP B 32 11924 8066 6702 -230 162 425 C ATOM 2050 CG ASP B 32 27.629 0.679 7.495 1.00 69.32 C ANISOU 2050 CG ASP B 32 11576 7945 6818 -415 410 413 C ATOM 2051 OD1 ASP B 32 28.722 0.072 7.530 1.00 69.09 O ANISOU 2051 OD1 ASP B 32 11407 7984 6861 -582 671 324 O ATOM 2052 OD2 ASP B 32 27.314 1.540 8.343 1.00 68.22 O ANISOU 2052 OD2 ASP B 32 11381 7730 6809 -389 340 471 O ATOM 2053 N LYS B 33 27.043 -3.318 6.421 1.00 62.27 N ANISOU 2053 N LYS B 33 10295 7534 5830 -283 173 60 N ATOM 2054 CA LYS B 33 27.997 -4.391 6.179 1.00 61.22 C ANISOU 2054 CA LYS B 33 10006 7523 5731 -414 386 -76 C ATOM 2055 C LYS B 33 27.270 -5.725 5.992 1.00 60.20 C ANISOU 2055 C LYS B 33 9690 7558 5626 -288 169 -226 C ATOM 2056 O LYS B 33 27.815 -6.662 5.405 1.00 61.44 O ANISOU 2056 O LYS B 33 9773 7818 5755 -341 281 -353 O ATOM 2057 CB LYS B 33 29.004 -4.490 7.334 1.00 57.81 C ANISOU 2057 CB LYS B 33 9312 7097 5556 -592 607 -132 C ATOM 2058 CG LYS B 33 30.221 -5.366 7.020 1.00 58.27 C ANISOU 2058 CG LYS B 33 9209 7229 5701 -746 864 -291 C ATOM 2059 CD LYS B 33 31.279 -5.306 8.124 1.00 57.99 C ANISOU 2059 CD LYS B 33 8900 7169 5964 -907 1060 -370 C ATOM 2060 CE LYS B 33 32.529 -6.084 7.705 1.00 60.47 C ANISOU 2060 CE LYS B 33 9044 7524 6408 -1049 1288 -555 C ATOM 2061 NZ LYS B 33 33.575 -6.153 8.768 1.00 60.34 N ANISOU 2061 NZ LYS B 33 8711 7483 6733 -1168 1411 -686 N ATOM 2062 N GLU B 34 26.042 -5.809 6.498 1.00 57.81 N ANISOU 2062 N GLU B 34 9279 7269 5416 -126 -135 -238 N ATOM 2063 CA GLU B 34 25.250 -7.030 6.374 1.00 56.87 C ANISOU 2063 CA GLU B 34 8936 7280 5391 -14 -341 -404 C ATOM 2064 C GLU B 34 23.859 -6.750 5.814 1.00 56.40 C ANISOU 2064 C GLU B 34 8962 7183 5284 191 -646 -397 C ATOM 2065 O GLU B 34 23.067 -7.669 5.602 1.00 57.07 O ANISOU 2065 O GLU B 34 8865 7347 5473 285 -815 -539 O ATOM 2066 CB GLU B 34 25.146 -7.741 7.725 1.00 56.50 C ANISOU 2066 CB GLU B 34 8542 7279 5647 -51 -378 -502 C ATOM 2067 CG GLU B 34 26.477 -8.238 8.258 1.00 58.41 C ANISOU 2067 CG GLU B 34 8656 7548 5988 -237 -111 -560 C ATOM 2068 CD GLU B 34 27.047 -9.372 7.431 1.00 63.11 C ANISOU 2068 CD GLU B 34 9177 8245 6556 -268 -12 -714 C ATOM 2069 OE1 GLU B 34 26.290 -10.315 7.115 1.00 64.52 O ANISOU 2069 OE1 GLU B 34 9222 8507 6785 -158 -193 -843 O ATOM 2070 OE2 GLU B 34 28.249 -9.321 7.093 1.00 65.30 O ANISOU 2070 OE2 GLU B 34 9497 8515 6797 -410 255 -722 O ATOM 2071 N GLY B 35 23.568 -5.476 5.576 1.00 59.44 N ANISOU 2071 N GLY B 35 10174 6389 6022 -1250 -1638 -34 N ATOM 2072 CA GLY B 35 22.288 -5.073 5.024 1.00 59.08 C ANISOU 2072 CA GLY B 35 10071 6437 5940 -1131 -2000 -37 C ATOM 2073 C GLY B 35 21.122 -5.376 5.945 1.00 56.72 C ANISOU 2073 C GLY B 35 9273 6371 5907 -1142 -2164 -123 C ATOM 2074 O GLY B 35 19.980 -5.471 5.499 1.00 61.43 O ANISOU 2074 O GLY B 35 9725 7111 6506 -1089 -2427 -168 O ATOM 2075 N ILE B 36 21.411 -5.525 7.234 1.00 50.30 N ANISOU 2075 N ILE B 36 8183 5607 5322 -1205 -1983 -150 N ATOM 2076 CA ILE B 36 20.387 -5.848 8.220 1.00 47.65 C ANISOU 2076 CA ILE B 36 7369 5493 5243 -1221 -2064 -217 C ATOM 2077 C ILE B 36 19.959 -4.612 9.000 1.00 45.76 C ANISOU 2077 C ILE B 36 6917 5330 5139 -1026 -2192 -177 C ATOM 2078 O ILE B 36 20.759 -4.039 9.740 1.00 44.14 O ANISOU 2078 O ILE B 36 6711 5027 5035 -946 -1952 -125 O ATOM 2079 CB ILE B 36 20.887 -6.901 9.227 1.00 45.12 C ANISOU 2079 CB ILE B 36 6866 5187 5091 -1363 -1751 -265 C ATOM 2080 CG1 ILE B 36 21.431 -8.131 8.497 1.00 45.97 C ANISOU 2080 CG1 ILE B 36 7214 5202 5051 -1484 -1597 -288 C ATOM 2081 CG2 ILE B 36 19.772 -7.287 10.190 1.00 44.12 C ANISOU 2081 CG2 ILE B 36 6282 5283 5200 -1393 -1804 -328 C ATOM 2082 CD1 ILE B 36 22.038 -9.167 9.419 1.00 43.61 C ANISOU 2082 CD1 ILE B 36 6804 4899 4867 -1545 -1286 -320 C ATOM 2083 N PRO B 37 18.696 -4.191 8.825 1.00 46.18 N ANISOU 2083 N PRO B 37 6748 5576 5222 -881 -2483 -191 N ATOM 2084 CA PRO B 37 18.099 -3.084 9.579 1.00 46.90 C ANISOU 2084 CA PRO B 37 6591 5783 5447 -623 -2603 -154 C ATOM 2085 C PRO B 37 18.337 -3.231 11.080 1.00 45.03 C ANISOU 2085 C PRO B 37 6031 5601 5475 -639 -2336 -167 C ATOM 2086 O PRO B 37 18.054 -4.295 11.632 1.00 44.05 O ANISOU 2086 O PRO B 37 5650 5603 5485 -837 -2252 -238 O ATOM 2087 CB PRO B 37 16.602 -3.230 9.295 1.00 49.30 C ANISOU 2087 CB PRO B 37 6560 6382 5788 -543 -2832 -216 C ATOM 2088 CG PRO B 37 16.491 -4.080 8.066 1.00 51.11 C ANISOU 2088 CG PRO B 37 6992 6586 5841 -713 -2911 -268 C ATOM 2089 CD PRO B 37 17.841 -4.620 7.706 1.00 48.73 C ANISOU 2089 CD PRO B 37 7100 6002 5414 -895 -2691 -239 C ATOM 2090 N PRO B 38 18.856 -2.177 11.729 1.00 42.84 N ANISOU 2090 N PRO B 38 5803 5213 5260 -434 -2206 -102 N ATOM 2091 CA PRO B 38 19.136 -2.169 13.170 1.00 40.23 C ANISOU 2091 CA PRO B 38 5216 4917 5154 -396 -1971 -118 C ATOM 2092 C PRO B 38 17.929 -2.567 14.025 1.00 43.28 C ANISOU 2092 C PRO B 38 5118 5603 5724 -356 -2047 -170 C ATOM 2093 O PRO B 38 18.109 -3.142 15.101 1.00 43.61 O ANISOU 2093 O PRO B 38 4951 5693 5925 -431 -1823 -202 O ATOM 2094 CB PRO B 38 19.525 -0.714 13.436 1.00 37.62 C ANISOU 2094 CB PRO B 38 5051 4431 4810 -131 -1964 -46 C ATOM 2095 CG PRO B 38 20.117 -0.257 12.149 1.00 37.51 C ANISOU 2095 CG PRO B 38 5492 4198 4563 -161 -2023 22 C ATOM 2096 CD PRO B 38 19.304 -0.934 11.077 1.00 41.80 C ANISOU 2096 CD PRO B 38 6045 4874 4963 -244 -2268 -9 C ATOM 2097 N ASP B 39 16.720 -2.274 13.554 1.00 45.67 N ANISOU 2097 N ASP B 39 5240 6115 5997 -232 -2350 -180 N ATOM 2098 CA ASP B 39 15.516 -2.643 14.291 1.00 49.78 C ANISOU 2098 CA ASP B 39 5274 6968 6674 -207 -2344 -222 C ATOM 2099 C ASP B 39 15.235 -4.150 14.257 1.00 50.06 C ANISOU 2099 C ASP B 39 5152 7114 6754 -567 -2230 -296 C ATOM 2100 O ASP B 39 14.356 -4.640 14.971 1.00 50.16 O ANISOU 2100 O ASP B 39 4788 7386 6885 -619 -2136 -329 O ATOM 2101 CB ASP B 39 14.302 -1.847 13.799 1.00 56.35 C ANISOU 2101 CB ASP B 39 5962 8029 7418 49 -2568 -202 C ATOM 2102 CG ASP B 39 14.368 -1.533 12.317 1.00 60.65 C ANISOU 2102 CG ASP B 39 6859 8454 7733 74 -2809 -193 C ATOM 2103 OD1 ASP B 39 15.051 -0.554 11.949 1.00 61.03 O ANISOU 2103 OD1 ASP B 39 7283 8247 7658 262 -2861 -127 O ATOM 2104 OD2 ASP B 39 13.731 -2.256 11.523 1.00 62.90 O ANISOU 2104 OD2 ASP B 39 7065 8889 7944 -93 -2934 -251 O ATOM 2105 N GLN B 40 15.988 -4.880 13.435 1.00 49.55 N ANISOU 2105 N GLN B 40 5416 6844 6568 -806 -2206 -320 N ATOM 2106 CA GLN B 40 15.895 -6.337 13.401 1.00 51.14 C ANISOU 2106 CA GLN B 40 5577 7065 6788 -1116 -2053 -401 C ATOM 2107 C GLN B 40 16.984 -6.982 14.255 1.00 47.78 C ANISOU 2107 C GLN B 40 5272 6450 6431 -1235 -1727 -394 C ATOM 2108 O GLN B 40 16.876 -8.147 14.636 1.00 48.68 O ANISOU 2108 O GLN B 40 5323 6567 6605 -1417 -1541 -454 O ATOM 2109 CB GLN B 40 16.005 -6.858 11.965 1.00 55.72 C ANISOU 2109 CB GLN B 40 6469 7536 7165 -1253 -2189 -441 C ATOM 2110 CG GLN B 40 14.836 -6.494 11.066 1.00 63.33 C ANISOU 2110 CG GLN B 40 7303 8713 8045 -1164 -2505 -480 C ATOM 2111 CD GLN B 40 14.961 -7.100 9.679 1.00 67.81 C ANISOU 2111 CD GLN B 40 8193 9162 8410 -1295 -2630 -527 C ATOM 2112 OE1 GLN B 40 15.885 -7.868 9.403 1.00 67.16 O ANISOU 2112 OE1 GLN B 40 8420 8847 8250 -1452 -2460 -526 O ATOM 2113 NE2 GLN B 40 14.030 -6.756 8.798 1.00 71.98 N ANISOU 2113 NE2 GLN B 40 8652 9862 8834 -1200 -2920 -567 N ATOM 2114 N GLN B 41 18.034 -6.220 14.547 1.00 43.94 N ANISOU 2114 N GLN B 41 4978 5782 5935 -1111 -1662 -331 N ATOM 2115 CA GLN B 41 19.187 -6.745 15.271 1.00 39.54 C ANISOU 2115 CA GLN B 41 4558 5054 5410 -1185 -1353 -337 C ATOM 2116 C GLN B 41 18.962 -6.801 16.777 1.00 38.64 C ANISOU 2116 C GLN B 41 4135 5049 5498 -1098 -1170 -338 C ATOM 2117 O GLN B 41 18.501 -5.835 17.385 1.00 39.02 O ANISOU 2117 O GLN B 41 3974 5209 5642 -852 -1222 -306 O ATOM 2118 CB GLN B 41 20.431 -5.902 14.985 1.00 36.30 C ANISOU 2118 CB GLN B 41 4466 4428 4899 -1050 -1265 -291 C ATOM 2119 CG GLN B 41 20.781 -5.762 13.517 1.00 36.91 C ANISOU 2119 CG GLN B 41 4897 4375 4752 -1112 -1400 -268 C ATOM 2120 CD GLN B 41 22.051 -4.963 13.306 1.00 35.25 C ANISOU 2120 CD GLN B 41 4975 3960 4457 -1017 -1249 -212 C ATOM 2121 OE1 GLN B 41 22.969 -5.012 14.125 1.00 30.45 O ANISOU 2121 OE1 GLN B 41 4351 3284 3933 -1000 -1003 -225 O ATOM 2122 NE2 GLN B 41 22.108 -4.213 12.211 1.00 38.03 N ANISOU 2122 NE2 GLN B 41 5591 4218 4640 -957 -1397 -152 N ATOM 2123 N LYS B 42 19.296 -7.940 17.372 1.00 37.87 N ANISOU 2123 N LYS B 42 4061 4906 5420 -1239 -913 -379 N ATOM 2124 CA LYS B 42 19.332 -8.063 18.823 1.00 37.93 C ANISOU 2124 CA LYS B 42 3867 4966 5578 -1160 -706 -371 C ATOM 2125 C LYS B 42 20.708 -8.568 19.242 1.00 32.01 C ANISOU 2125 C LYS B 42 3390 4007 4766 -1157 -454 -388 C ATOM 2126 O LYS B 42 21.114 -9.671 18.877 1.00 33.30 O ANISOU 2126 O LYS B 42 3771 4040 4839 -1238 -360 -388 O ATOM 2127 CB LYS B 42 18.223 -8.991 19.327 1.00 43.24 C ANISOU 2127 CB LYS B 42 4301 5768 6361 -1262 -640 -380 C ATOM 2128 CG LYS B 42 18.203 -9.168 20.838 1.00 46.48 C ANISOU 2128 CG LYS B 42 4574 6257 6827 -1177 -408 -299 C ATOM 2129 CD LYS B 42 16.803 -9.485 21.347 1.00 52.69 C ANISOU 2129 CD LYS B 42 5035 7256 7730 -1224 -418 -226 C ATOM 2130 CE LYS B 42 16.228 -10.726 20.687 1.00 57.96 C ANISOU 2130 CE LYS B 42 5749 7812 8460 -1482 -463 -261 C ATOM 2131 NZ LYS B 42 14.845 -11.017 21.160 1.00 63.17 N ANISOU 2131 NZ LYS B 42 6063 8655 9282 -1547 -457 -223 N ATOM 2132 N LEU B 43 21.427 -7.744 19.997 1.00 25.49 N ANISOU 2132 N LEU B 43 2563 3131 3991 -920 -352 -389 N ATOM 2133 CA LEU B 43 22.797 -8.055 20.383 1.00 23.95 C ANISOU 2133 CA LEU B 43 2584 2777 3739 -878 -140 -428 C ATOM 2134 C LEU B 43 22.893 -8.529 21.828 1.00 23.79 C ANISOU 2134 C LEU B 43 2456 2788 3797 -763 74 -451 C ATOM 2135 O LEU B 43 22.298 -7.938 22.729 1.00 24.46 O ANISOU 2135 O LEU B 43 2314 2982 3999 -589 74 -433 O ATOM 2136 CB LEU B 43 23.703 -6.839 20.164 1.00 23.30 C ANISOU 2136 CB LEU B 43 2616 2600 3638 -718 -180 -419 C ATOM 2137 CG LEU B 43 23.950 -6.442 18.707 1.00 22.36 C ANISOU 2137 CG LEU B 43 2711 2397 3389 -822 -325 -386 C ATOM 2138 CD1 LEU B 43 24.684 -5.114 18.623 1.00 19.75 C ANISOU 2138 CD1 LEU B 43 2474 1967 3064 -682 -351 -360 C ATOM 2139 CD2 LEU B 43 24.726 -7.532 17.981 1.00 20.90 C ANISOU 2139 CD2 LEU B 43 2751 2136 3055 -928 -211 -391 C ATOM 2140 N LEU B 44 23.650 -9.600 22.040 1.00 23.26 N ANISOU 2140 N LEU B 44 2601 2638 3597 -778 240 -458 N ATOM 2141 CA LEU B 44 23.851 -10.142 23.376 1.00 22.76 C ANISOU 2141 CA LEU B 44 2501 2567 3579 -669 456 -500 C ATOM 2142 C LEU B 44 25.325 -10.131 23.758 1.00 19.49 C ANISOU 2142 C LEU B 44 2253 2056 3097 -507 587 -568 C ATOM 2143 O LEU B 44 26.196 -10.377 22.926 1.00 19.47 O ANISOU 2143 O LEU B 44 2431 2032 2937 -520 561 -548 O ATOM 2144 CB LEU B 44 23.320 -11.575 23.462 1.00 25.99 C ANISOU 2144 CB LEU B 44 3005 2971 3899 -818 540 -468 C ATOM 2145 CG LEU B 44 21.876 -11.847 23.036 1.00 31.78 C ANISOU 2145 CG LEU B 44 3573 3815 4688 -1020 407 -397 C ATOM 2146 CD1 LEU B 44 21.515 -13.294 23.318 1.00 33.34 C ANISOU 2146 CD1 LEU B 44 3889 3963 4818 -1158 522 -376 C ATOM 2147 CD2 LEU B 44 20.909 -10.911 23.736 1.00 33.28 C ANISOU 2147 CD2 LEU B 44 3408 4184 5054 -930 376 -371 C ATOM 2148 N PHE B 45 25.594 -9.834 25.024 1.00 22.71 N ANISOU 2148 N PHE B 45 3480 2892 2255 -942 -443 -377 N ATOM 2149 CA PHE B 45 26.923 -10.007 25.594 1.00 23.08 C ANISOU 2149 CA PHE B 45 3633 2856 2282 -837 -330 -380 C ATOM 2150 C PHE B 45 26.773 -10.593 26.989 1.00 24.40 C ANISOU 2150 C PHE B 45 3742 3124 2404 -940 -281 -364 C ATOM 2151 O PHE B 45 26.087 -10.018 27.835 1.00 26.55 O ANISOU 2151 O PHE B 45 3812 3567 2709 -958 -297 -406 O ATOM 2152 CB PHE B 45 27.682 -8.681 25.655 1.00 22.02 C ANISOU 2152 CB PHE B 45 3388 2769 2211 -670 -339 -414 C ATOM 2153 CG PHE B 45 29.062 -8.802 26.236 1.00 18.79 C ANISOU 2153 CG PHE B 45 3066 2348 1724 -649 -276 -341 C ATOM 2154 CD1 PHE B 45 30.127 -9.209 25.449 1.00 17.64 C ANISOU 2154 CD1 PHE B 45 3142 2031 1527 -575 -214 -241 C ATOM 2155 CD2 PHE B 45 29.296 -8.510 27.570 1.00 18.08 C ANISOU 2155 CD2 PHE B 45 2848 2438 1584 -720 -259 -319 C ATOM 2156 CE1 PHE B 45 31.398 -9.324 25.981 1.00 18.28 C ANISOU 2156 CE1 PHE B 45 3154 2169 1624 -478 -122 2 C ATOM 2157 CE2 PHE B 45 30.565 -8.624 28.108 1.00 19.03 C ANISOU 2157 CE2 PHE B 45 2959 2655 1616 -747 -240 -126 C ATOM 2158 CZ PHE B 45 31.618 -9.031 27.311 1.00 18.27 C ANISOU 2158 CZ PHE B 45 2943 2425 1573 -590 -171 87 C ATOM 2159 N ALA B 46 27.419 -11.733 27.219 1.00 24.02 N ANISOU 2159 N ALA B 46 3912 2950 2262 -1026 -184 -294 N ATOM 2160 CA ALA B 46 27.260 -12.491 28.457 1.00 23.48 C ANISOU 2160 CA ALA B 46 3737 2993 2190 -1096 -112 -191 C ATOM 2161 C ALA B 46 25.786 -12.786 28.726 1.00 25.99 C ANISOU 2161 C ALA B 46 3966 3416 2493 -1293 -204 -269 C ATOM 2162 O ALA B 46 25.301 -12.627 29.847 1.00 25.38 O ANISOU 2162 O ALA B 46 3672 3551 2419 -1332 -202 -259 O ATOM 2163 CB ALA B 46 27.895 -11.761 29.631 1.00 21.74 C ANISOU 2163 CB ALA B 46 3290 3019 1950 -1050 -113 -122 C ATOM 2164 N ARG B 47 25.086 -13.197 27.671 1.00 27.20 N ANISOU 2164 N ARG B 47 4252 3446 2638 -1373 -252 -279 N ATOM 2165 CA ARG B 47 23.673 -13.572 27.735 1.00 29.05 C ANISOU 2165 CA ARG B 47 4366 3807 2866 -1542 -344 -234 C ATOM 2166 C ARG B 47 22.744 -12.435 28.164 1.00 28.49 C ANISOU 2166 C ARG B 47 3937 3997 2889 -1497 -436 -228 C ATOM 2167 O ARG B 47 21.610 -12.675 28.575 1.00 30.85 O ANISOU 2167 O ARG B 47 4055 4465 3202 -1639 -492 -137 O ATOM 2168 CB ARG B 47 23.471 -14.799 28.629 1.00 31.08 C ANISOU 2168 CB ARG B 47 4694 4044 3069 -1720 -274 -179 C ATOM 2169 CG ARG B 47 24.335 -15.989 28.247 1.00 34.41 C ANISOU 2169 CG ARG B 47 5537 4115 3422 -1792 -92 -165 C ATOM 2170 CD ARG B 47 23.901 -17.238 28.993 1.00 38.69 C ANISOU 2170 CD ARG B 47 6144 4602 3954 -1963 1 -74 C ATOM 2171 NE ARG B 47 22.582 -17.690 28.563 1.00 41.68 N ANISOU 2171 NE ARG B 47 6533 5081 4225 -2164 -144 -76 N ATOM 2172 CZ ARG B 47 21.822 -18.538 29.247 1.00 43.63 C ANISOU 2172 CZ ARG B 47 6728 5394 4454 -2331 -158 0 C ATOM 2173 NH1 ARG B 47 22.243 -19.025 30.407 1.00 40.73 N ANISOU 2173 NH1 ARG B 47 6271 5014 4191 -2285 -20 86 N ATOM 2174 NH2 ARG B 47 20.635 -18.893 28.775 1.00 47.94 N ANISOU 2174 NH2 ARG B 47 7284 6052 4880 -2552 -309 49 N ATOM 2175 N LYS B 48 23.223 -11.200 28.063 1.00 28.77 N ANISOU 2175 N LYS B 48 3884 4059 2989 -1323 -426 -305 N ATOM 2176 CA LYS B 48 22.391 -10.037 28.355 1.00 32.49 C ANISOU 2176 CA LYS B 48 4059 4734 3552 -1314 -443 -306 C ATOM 2177 C LYS B 48 22.228 -9.176 27.107 1.00 32.32 C ANISOU 2177 C LYS B 48 3982 4698 3601 -1258 -552 -253 C ATOM 2178 O LYS B 48 23.195 -8.923 26.390 1.00 31.19 O ANISOU 2178 O LYS B 48 4035 4389 3425 -1152 -563 -333 O ATOM 2179 CB LYS B 48 22.992 -9.209 29.493 1.00 33.65 C ANISOU 2179 CB LYS B 48 4179 4895 3713 -1138 -239 -428 C ATOM 2180 CG LYS B 48 22.160 -7.992 29.873 1.00 39.18 C ANISOU 2180 CG LYS B 48 4664 5664 4560 -987 -57 -414 C ATOM 2181 CD LYS B 48 22.882 -7.101 30.872 1.00 44.04 C ANISOU 2181 CD LYS B 48 5417 6220 5098 -913 175 -603 C ATOM 2182 CE LYS B 48 23.030 -7.779 32.224 1.00 49.14 C ANISOU 2182 CE LYS B 48 6118 6983 5570 -1069 257 -645 C ATOM 2183 NZ LYS B 48 23.754 -6.914 33.200 1.00 51.00 N ANISOU 2183 NZ LYS B 48 6549 7201 5629 -1137 451 -822 N ATOM 2184 N GLN B 49 21.002 -8.732 26.846 1.00 34.70 N ANISOU 2184 N GLN B 49 3970 5185 4030 -1284 -602 -39 N ATOM 2185 CA GLN B 49 20.733 -7.901 25.678 1.00 35.70 C ANISOU 2185 CA GLN B 49 3958 5362 4243 -1247 -717 115 C ATOM 2186 C GLN B 49 21.287 -6.493 25.851 1.00 32.19 C ANISOU 2186 C GLN B 49 3468 4796 3966 -901 -501 21 C ATOM 2187 O GLN B 49 21.093 -5.860 26.888 1.00 32.97 O ANISOU 2187 O GLN B 49 3470 4868 4188 -708 -221 -25 O ATOM 2188 CB GLN B 49 19.234 -7.848 25.368 1.00 40.42 C ANISOU 2188 CB GLN B 49 4139 6260 4958 -1386 -834 516 C ATOM 2189 CG GLN B 49 18.897 -6.995 24.151 1.00 43.67 C ANISOU 2189 CG GLN B 49 4327 6799 5469 -1374 -975 793 C ATOM 2190 CD GLN B 49 17.431 -7.052 23.772 1.00 48.12 C ANISOU 2190 CD GLN B 49 4539 7643 6101 -1484 -1066 1275 C ATOM 2191 OE1 GLN B 49 16.658 -7.819 24.346 1.00 50.82 O ANISOU 2191 OE1 GLN B 49 4819 8095 6393 -1618 -1072 1391 O ATOM 2192 NE2 GLN B 49 17.040 -6.238 22.798 1.00 49.57 N ANISOU 2192 NE2 GLN B 49 4513 7942 6381 -1422 -1129 1592 N ATOM 2193 N LEU B 50 21.980 -6.010 24.827 1.00 29.66 N ANISOU 2193 N LEU B 50 3270 4377 3622 -856 -602 -18 N ATOM 2194 CA LEU B 50 22.553 -4.672 24.855 1.00 27.83 C ANISOU 2194 CA LEU B 50 3033 4004 3536 -573 -417 -100 C ATOM 2195 C LEU B 50 21.506 -3.645 24.427 1.00 32.04 C ANISOU 2195 C LEU B 50 3185 4641 4347 -405 -324 218 C ATOM 2196 O LEU B 50 20.784 -3.852 23.451 1.00 31.95 O ANISOU 2196 O LEU B 50 2947 4839 4355 -553 -557 528 O ATOM 2197 CB LEU B 50 23.786 -4.609 23.952 1.00 24.81 C ANISOU 2197 CB LEU B 50 2918 3479 3028 -578 -551 -234 C ATOM 2198 CG LEU B 50 24.796 -5.744 24.157 1.00 24.04 C ANISOU 2198 CG LEU B 50 3145 3282 2707 -707 -604 -405 C ATOM 2199 CD1 LEU B 50 26.018 -5.564 23.267 1.00 23.45 C ANISOU 2199 CD1 LEU B 50 3279 3058 2571 -620 -637 -459 C ATOM 2200 CD2 LEU B 50 25.204 -5.856 25.619 1.00 23.33 C ANISOU 2200 CD2 LEU B 50 3097 3179 2589 -669 -429 -533 C ATOM 2201 N GLU B 51 21.423 -2.543 25.164 1.00 36.43 N ANISOU 2201 N GLU B 51 3688 5049 5107 -124 48 180 N ATOM 2202 CA GLU B 51 20.375 -1.553 24.940 1.00 42.79 C ANISOU 2202 CA GLU B 51 4108 5896 6256 127 284 554 C ATOM 2203 C GLU B 51 20.852 -0.331 24.170 1.00 46.39 C ANISOU 2203 C GLU B 51 4570 6178 6878 343 381 599 C ATOM 2204 O GLU B 51 21.969 0.140 24.368 1.00 46.10 O ANISOU 2204 O GLU B 51 4889 5892 6735 378 465 252 O ATOM 2205 CB GLU B 51 19.778 -1.099 26.270 1.00 46.28 C ANISOU 2205 CB GLU B 51 4517 6211 6856 337 783 531 C ATOM 2206 CG GLU B 51 18.956 -2.153 26.976 1.00 50.64 C ANISOU 2206 CG GLU B 51 4911 6988 7340 182 734 641 C ATOM 2207 CD GLU B 51 18.209 -1.588 28.163 1.00 57.88 C ANISOU 2207 CD GLU B 51 5754 7785 8452 436 1297 701 C ATOM 2208 OE1 GLU B 51 18.480 -0.427 28.537 1.00 60.26 O ANISOU 2208 OE1 GLU B 51 6258 7760 8879 688 1759 557 O ATOM 2209 OE2 GLU B 51 17.346 -2.301 28.719 1.00 60.28 O ANISOU 2209 OE2 GLU B 51 5838 8295 8773 370 1315 891 O ATOM 2210 N ASP B 52 19.987 0.184 23.301 1.00 51.04 N ANISOU 2210 N ASP B 52 4729 6934 7731 463 359 1089 N ATOM 2211 CA ASP B 52 20.263 1.420 22.582 1.00 53.91 C ANISOU 2211 CA ASP B 52 5021 7138 8323 714 504 1230 C ATOM 2212 C ASP B 52 20.409 2.568 23.572 1.00 56.24 C ANISOU 2212 C ASP B 52 5516 7015 8839 1054 1128 1044 C ATOM 2213 O ASP B 52 19.569 2.748 24.455 1.00 60.31 O ANISOU 2213 O ASP B 52 5911 7461 9544 1236 1550 1174 O ATOM 2214 CB ASP B 52 19.138 1.732 21.593 1.00 58.53 C ANISOU 2214 CB ASP B 52 5047 8031 9159 765 395 1906 C ATOM 2215 CG ASP B 52 18.974 0.658 20.536 1.00 58.41 C ANISOU 2215 CG ASP B 52 4978 8404 8812 298 -210 2054 C ATOM 2216 OD1 ASP B 52 19.996 0.097 20.088 1.00 53.49 O ANISOU 2216 OD1 ASP B 52 4678 7750 7894 70 -516 1706 O ATOM 2217 OD2 ASP B 52 17.820 0.375 20.151 1.00 64.08 O ANISOU 2217 OD2 ASP B 52 5470 9386 9493 127 -327 2484 O ATOM 2218 N GLY B 53 21.478 3.341 23.424 1.00 53.58 N ANISOU 2218 N GLY B 53 5525 6381 8451 1107 1213 741 N ATOM 2219 CA GLY B 53 21.735 4.461 24.309 1.00 54.35 C ANISOU 2219 CA GLY B 53 5962 6034 8654 1299 1791 500 C ATOM 2220 C GLY B 53 22.920 4.199 25.214 1.00 49.90 C ANISOU 2220 C GLY B 53 5952 5306 7700 1024 1763 -80 C ATOM 2221 O GLY B 53 23.621 5.124 25.625 1.00 52.95 O ANISOU 2221 O GLY B 53 6737 5412 7969 949 1961 -326 O ATOM 2222 N ARG B 54 23.143 2.927 25.524 1.00 43.62 N ANISOU 2222 N ARG B 54 5186 4780 6608 749 1391 -219 N ATOM 2223 CA ARG B 54 24.266 2.522 26.357 1.00 40.29 C ANISOU 2223 CA ARG B 54 5187 4317 5804 449 1286 -635 C ATOM 2224 C ARG B 54 25.488 2.248 25.486 1.00 37.12 C ANISOU 2224 C ARG B 54 4872 4002 5228 306 849 -699 C ATOM 2225 O ARG B 54 25.356 1.873 24.322 1.00 37.87 O ANISOU 2225 O ARG B 54 4729 4259 5402 360 547 -480 O ATOM 2226 CB ARG B 54 23.898 1.278 27.166 1.00 40.53 C ANISOU 2226 CB ARG B 54 5175 4577 5649 270 1166 -680 C ATOM 2227 CG ARG B 54 22.664 1.458 28.041 1.00 45.38 C ANISOU 2227 CG ARG B 54 5676 5134 6431 421 1610 -579 C ATOM 2228 CD ARG B 54 23.043 1.660 29.497 1.00 48.45 C ANISOU 2228 CD ARG B 54 6503 5354 6554 232 1945 -939 C ATOM 2229 NE ARG B 54 23.464 0.409 30.121 1.00 48.83 N ANISOU 2229 NE ARG B 54 6602 5670 6281 -75 1615 -1059 N ATOM 2230 CZ ARG B 54 24.138 0.331 31.264 1.00 51.08 C ANISOU 2230 CZ ARG B 54 7230 5951 6228 -377 1663 -1305 C ATOM 2231 NH1 ARG B 54 24.480 1.437 31.912 1.00 54.13 N ANISOU 2231 NH1 ARG B 54 7903 6121 6543 -472 1850 -1362 N ATOM 2232 NH2 ARG B 54 24.478 -0.853 31.754 1.00 49.31 N ANISOU 2232 NH2 ARG B 54 6976 5994 5766 -614 1383 -1328 N ATOM 2233 N THR B 55 26.675 2.440 26.050 1.00 34.36 N ANISOU 2233 N THR B 55 4869 3566 4621 90 828 -962 N ATOM 2234 CA THR B 55 27.911 2.248 25.301 1.00 30.20 C ANISOU 2234 CA THR B 55 4404 3116 3956 -11 481 -960 C ATOM 2235 C THR B 55 28.522 0.874 25.561 1.00 30.59 C ANISOU 2235 C THR B 55 4461 3402 3758 -205 187 -960 C ATOM 2236 O THR B 55 28.111 0.166 26.482 1.00 32.74 O ANISOU 2236 O THR B 55 4738 3775 3927 -317 239 -1010 O ATOM 2237 CB THR B 55 28.952 3.326 25.649 1.00 29.73 C ANISOU 2237 CB THR B 55 4580 2944 3774 -133 534 -1033 C ATOM 2238 OG1 THR B 55 29.407 3.137 26.995 1.00 31.19 O ANISOU 2238 OG1 THR B 55 4898 3247 3704 -393 544 -1083 O ATOM 2239 CG2 THR B 55 28.347 4.713 25.510 1.00 32.48 C ANISOU 2239 CG2 THR B 55 4972 3018 4350 45 889 -1019 C ATOM 2240 N LEU B 56 29.504 0.504 24.745 1.00 28.09 N ANISOU 2240 N LEU B 56 4148 3154 3372 -217 -72 -870 N ATOM 2241 CA LEU B 56 30.212 -0.760 24.914 1.00 25.13 C ANISOU 2241 CA LEU B 56 3692 2978 2879 -277 -241 -738 C ATOM 2242 C LEU B 56 30.932 -0.814 26.259 1.00 28.64 C ANISOU 2242 C LEU B 56 4186 3515 3182 -429 -199 -698 C ATOM 2243 O LEU B 56 31.039 -1.875 26.875 1.00 28.94 O ANISOU 2243 O LEU B 56 4186 3669 3140 -500 -228 -615 O ATOM 2244 CB LEU B 56 31.219 -0.968 23.780 1.00 21.30 C ANISOU 2244 CB LEU B 56 3188 2514 2392 -222 -340 -580 C ATOM 2245 CG LEU B 56 30.674 -1.151 22.362 1.00 20.57 C ANISOU 2245 CG LEU B 56 3089 2353 2373 -98 -444 -518 C ATOM 2246 CD1 LEU B 56 31.814 -1.202 21.355 1.00 17.53 C ANISOU 2246 CD1 LEU B 56 2756 1938 1967 -17 -506 -383 C ATOM 2247 CD2 LEU B 56 29.822 -2.407 22.269 1.00 21.49 C ANISOU 2247 CD2 LEU B 56 3185 2531 2447 -155 -480 -499 C ATOM 2248 N SER B 57 31.423 0.336 26.710 1.00 33.40 N ANISOU 2248 N SER B 57 4474 4086 4129 -1206 -399 162 N ATOM 2249 CA SER B 57 32.152 0.411 27.971 1.00 35.19 C ANISOU 2249 CA SER B 57 4483 4503 4385 -1267 -521 143 C ATOM 2250 C SER B 57 31.226 0.245 29.173 1.00 34.74 C ANISOU 2250 C SER B 57 4373 4669 4157 -1145 -676 101 C ATOM 2251 O SER B 57 31.668 -0.133 30.257 1.00 37.02 O ANISOU 2251 O SER B 57 4450 5182 4433 -1158 -773 139 O ATOM 2252 CB SER B 57 32.930 1.726 28.069 1.00 38.54 C ANISOU 2252 CB SER B 57 4972 4819 4853 -1442 -568 23 C ATOM 2253 OG SER B 57 32.083 2.842 27.858 1.00 40.78 O ANISOU 2253 OG SER B 57 5544 4925 5026 -1409 -635 -109 O ATOM 2254 N ASP B 58 29.941 0.526 28.975 1.00 32.61 N ANISOU 2254 N ASP B 58 4284 4366 3741 -1025 -701 22 N ATOM 2255 CA ASP B 58 28.949 0.347 30.030 1.00 30.76 C ANISOU 2255 CA ASP B 58 3985 4384 3318 -913 -819 -32 C ATOM 2256 C ASP B 58 28.763 -1.131 30.359 1.00 27.56 C ANISOU 2256 C ASP B 58 3401 4153 2918 -869 -770 158 C ATOM 2257 O ASP B 58 28.384 -1.485 31.475 1.00 27.15 O ANISOU 2257 O ASP B 58 3241 4278 2796 -766 -775 169 O ATOM 2258 CB ASP B 58 27.606 0.963 29.627 1.00 32.50 C ANISOU 2258 CB ASP B 58 4397 4522 3428 -738 -807 -171 C ATOM 2259 CG ASP B 58 27.637 2.479 29.624 1.00 34.92 C ANISOU 2259 CG ASP B 58 4868 4666 3733 -714 -878 -365 C ATOM 2260 OD1 ASP B 58 28.431 3.060 30.392 1.00 38.28 O ANISOU 2260 OD1 ASP B 58 5223 5125 4197 -794 -948 -439 O ATOM 2261 OD2 ASP B 58 26.862 3.089 28.858 1.00 33.06 O ANISOU 2261 OD2 ASP B 58 4824 4267 3470 -606 -862 -438 O ATOM 2262 N TYR B 59 29.032 -1.987 29.379 1.00 25.36 N ANISOU 2262 N TYR B 59 3126 3728 2780 -886 -643 294 N ATOM 2263 CA TYR B 59 28.897 -3.428 29.558 1.00 22.63 C ANISOU 2263 CA TYR B 59 2648 3472 2478 -857 -606 478 C ATOM 2264 C TYR B 59 30.251 -4.098 29.752 1.00 23.09 C ANISOU 2264 C TYR B 59 2522 3524 2727 -904 -593 619 C ATOM 2265 O TYR B 59 30.357 -5.324 29.685 1.00 20.16 O ANISOU 2265 O TYR B 59 2066 3138 2457 -868 -555 780 O ATOM 2266 CB TYR B 59 28.180 -4.052 28.360 1.00 21.53 C ANISOU 2266 CB TYR B 59 2634 3170 2377 -808 -476 503 C ATOM 2267 CG TYR B 59 26.745 -3.608 28.202 1.00 23.36 C ANISOU 2267 CG TYR B 59 3002 3456 2417 -736 -504 379 C ATOM 2268 CD1 TYR B 59 25.737 -4.162 28.980 1.00 25.48 C ANISOU 2268 CD1 TYR B 59 3188 3927 2565 -689 -534 398 C ATOM 2269 CD2 TYR B 59 26.397 -2.641 27.269 1.00 24.01 C ANISOU 2269 CD2 TYR B 59 3286 3374 2462 -695 -478 239 C ATOM 2270 CE1 TYR B 59 24.422 -3.761 28.838 1.00 26.36 C ANISOU 2270 CE1 TYR B 59 3368 4047 2599 -556 -495 241 C ATOM 2271 CE2 TYR B 59 25.085 -2.234 27.119 1.00 26.08 C ANISOU 2271 CE2 TYR B 59 3651 3697 2560 -588 -522 114 C ATOM 2272 CZ TYR B 59 24.102 -2.797 27.905 1.00 27.91 C ANISOU 2272 CZ TYR B 59 3735 4105 2766 -480 -500 100 C ATOM 2273 OH TYR B 59 22.795 -2.394 27.758 1.00 30.53 O ANISOU 2273 OH TYR B 59 4106 4451 3044 -302 -497 -42 O ATOM 2274 N ASN B 60 31.279 -3.287 29.988 1.00 24.46 N ANISOU 2274 N ASN B 60 2631 3702 2960 -983 -635 547 N ATOM 2275 CA ASN B 60 32.644 -3.778 30.165 1.00 26.18 C ANISOU 2275 CA ASN B 60 2636 3950 3361 -1021 -634 645 C ATOM 2276 C ASN B 60 33.142 -4.589 28.971 1.00 25.88 C ANISOU 2276 C ASN B 60 2584 3718 3529 -994 -464 717 C ATOM 2277 O ASN B 60 33.875 -5.565 29.127 1.00 25.49 O ANISOU 2277 O ASN B 60 2353 3698 3632 -940 -464 841 O ATOM 2278 CB ASN B 60 32.769 -4.587 31.459 1.00 26.45 C ANISOU 2278 CB ASN B 60 2500 4211 3339 -956 -765 788 C ATOM 2279 CG ASN B 60 32.484 -3.755 32.691 1.00 26.21 C ANISOU 2279 CG ASN B 60 2511 4348 3100 -934 -856 661 C ATOM 2280 OD1 ASN B 60 32.893 -2.597 32.778 1.00 25.50 O ANISOU 2280 OD1 ASN B 60 2445 4248 2998 -1002 -891 489 O ATOM 2281 ND2 ASN B 60 31.773 -4.337 33.649 1.00 26.08 N ANISOU 2281 ND2 ASN B 60 2506 4463 2939 -853 -873 732 N ATOM 2282 N ILE B 61 32.729 -4.172 27.778 1.00 25.24 N ANISOU 2282 N ILE B 61 2700 3447 3443 -1015 -328 628 N ATOM 2283 CA ILE B 61 33.147 -4.817 26.542 1.00 24.82 C ANISOU 2283 CA ILE B 61 2652 3231 3545 -997 -148 652 C ATOM 2284 C ILE B 61 34.463 -4.224 26.058 1.00 27.71 C ANISOU 2284 C ILE B 61 2920 3568 4039 -1116 -59 594 C ATOM 2285 O ILE B 61 34.523 -3.054 25.679 1.00 29.35 O ANISOU 2285 O ILE B 61 3273 3705 4175 -1219 -26 487 O ATOM 2286 CB ILE B 61 32.089 -4.642 25.442 1.00 24.09 C ANISOU 2286 CB ILE B 61 2816 2985 3352 -974 -46 587 C ATOM 2287 CG1 ILE B 61 30.759 -5.258 25.885 1.00 21.86 C ANISOU 2287 CG1 ILE B 61 2597 2764 2947 -879 -124 628 C ATOM 2288 CG2 ILE B 61 32.573 -5.254 24.135 1.00 24.01 C ANISOU 2288 CG2 ILE B 61 2815 2838 3468 -951 148 571 C ATOM 2289 CD1 ILE B 61 29.621 -5.014 24.922 1.00 19.91 C ANISOU 2289 CD1 ILE B 61 2575 2415 2575 -846 -61 544 C ATOM 2290 N HIS B 62 35.515 -5.035 26.076 1.00 28.34 N ANISOU 2290 N HIS B 62 2761 3702 4305 -1077 -18 651 N ATOM 2291 CA HIS B 62 36.842 -4.571 25.693 1.00 30.91 C ANISOU 2291 CA HIS B 62 2946 4061 4739 -1172 77 567 C ATOM 2292 C HIS B 62 37.232 -5.104 24.318 1.00 33.18 C ANISOU 2292 C HIS B 62 3235 4247 5126 -1155 301 529 C ATOM 2293 O HIS B 62 36.420 -5.725 23.634 1.00 31.31 O ANISOU 2293 O HIS B 62 3144 3889 4864 -1067 374 549 O ATOM 2294 CB HIS B 62 37.873 -4.986 26.744 1.00 32.94 C ANISOU 2294 CB HIS B 62 2889 4511 5115 -1134 -53 619 C ATOM 2295 CG HIS B 62 37.491 -4.605 28.141 1.00 35.61 C ANISOU 2295 CG HIS B 62 3220 4993 5318 -1135 -277 652 C ATOM 2296 ND1 HIS B 62 37.216 -3.306 28.510 1.00 36.62 N ANISOU 2296 ND1 HIS B 62 3484 5132 5299 -1264 -343 537 N ATOM 2297 CD2 HIS B 62 37.338 -5.354 29.260 1.00 37.51 C ANISOU 2297 CD2 HIS B 62 3345 5373 5533 -1016 -449 781 C ATOM 2298 CE1 HIS B 62 36.909 -3.270 29.794 1.00 37.61 C ANISOU 2298 CE1 HIS B 62 3564 5423 5304 -1219 -534 564 C ATOM 2299 NE2 HIS B 62 36.976 -4.499 30.273 1.00 38.05 N ANISOU 2299 NE2 HIS B 62 3480 5567 5411 -1073 -594 720 N ATOM 2300 N LYS B 63 38.473 -4.855 23.913 1.00 37.18 N ANISOU 2300 N LYS B 63 3572 4832 5722 -1247 409 455 N ATOM 2301 CA LYS B 63 38.941 -5.284 22.600 1.00 39.54 C ANISOU 2301 CA LYS B 63 3850 5105 6069 -1243 617 409 C ATOM 2302 C LYS B 63 38.912 -6.805 22.444 1.00 39.17 C ANISOU 2302 C LYS B 63 3649 5008 6227 -1023 661 453 C ATOM 2303 O LYS B 63 39.055 -7.542 23.420 1.00 37.74 O ANISOU 2303 O LYS B 63 3276 4871 6191 -892 514 552 O ATOM 2304 CB LYS B 63 40.341 -4.733 22.311 1.00 42.37 C ANISOU 2304 CB LYS B 63 4009 5627 6464 -1390 693 354 C ATOM 2305 CG LYS B 63 41.353 -4.957 23.423 1.00 44.36 C ANISOU 2305 CG LYS B 63 3922 6068 6864 -1366 583 329 C ATOM 2306 CD LYS B 63 42.699 -4.346 23.064 1.00 47.71 C ANISOU 2306 CD LYS B 63 4146 6683 7298 -1533 650 299 C ATOM 2307 CE LYS B 63 43.672 -4.417 24.230 1.00 50.80 C ANISOU 2307 CE LYS B 63 4226 7286 7788 -1521 526 207 C ATOM 2308 NZ LYS B 63 43.916 -5.817 24.674 1.00 52.26 N ANISOU 2308 NZ LYS B 63 4154 7520 8182 -1230 451 256 N ATOM 2309 N GLU B 64 38.708 -7.253 21.207 1.00 39.90 N ANISOU 2309 N GLU B 64 3841 5002 6317 -981 848 385 N ATOM 2310 CA GLU B 64 38.651 -8.675 20.861 1.00 41.09 C ANISOU 2310 CA GLU B 64 3891 5061 6659 -774 915 376 C ATOM 2311 C GLU B 64 37.499 -9.428 21.534 1.00 38.27 C ANISOU 2311 C GLU B 64 3686 4572 6282 -637 741 488 C ATOM 2312 O GLU B 64 37.512 -10.657 21.599 1.00 40.86 O ANISOU 2312 O GLU B 64 3943 4808 6774 -454 713 512 O ATOM 2313 CB GLU B 64 39.989 -9.374 21.148 1.00 45.48 C ANISOU 2313 CB GLU B 64 4075 5742 7465 -647 919 346 C ATOM 2314 CG GLU B 64 41.228 -8.586 20.734 1.00 49.12 C ANISOU 2314 CG GLU B 64 4345 6408 7910 -802 1046 237 C ATOM 2315 CD GLU B 64 41.315 -8.346 19.237 1.00 51.59 C ANISOU 2315 CD GLU B 64 4791 6722 8089 -888 1290 107 C ATOM 2316 OE1 GLU B 64 40.767 -9.159 18.464 1.00 52.07 O ANISOU 2316 OE1 GLU B 64 4940 6648 8196 -767 1414 44 O ATOM 2317 OE2 GLU B 64 41.937 -7.341 18.835 1.00 53.93 O ANISOU 2317 OE2 GLU B 64 5104 7156 8231 -1082 1347 82 O ATOM 2318 N SER B 65 36.506 -8.693 22.029 1.00 34.55 N ANISOU 2318 N SER B 65 3423 4091 5614 -731 627 550 N ATOM 2319 CA SER B 65 35.328 -9.311 22.637 1.00 30.72 C ANISOU 2319 CA SER B 65 3074 3528 5070 -645 486 649 C ATOM 2320 C SER B 65 34.397 -9.884 21.582 1.00 30.03 C ANISOU 2320 C SER B 65 3190 3285 4937 -603 598 579 C ATOM 2321 O SER B 65 34.506 -9.563 20.396 1.00 30.47 O ANISOU 2321 O SER B 65 3330 3308 4939 -652 771 456 O ATOM 2322 CB SER B 65 34.554 -8.304 23.492 1.00 27.70 C ANISOU 2322 CB SER B 65 2816 3230 4478 -746 338 697 C ATOM 2323 OG SER B 65 35.334 -7.827 24.572 1.00 30.39 O ANISOU 2323 OG SER B 65 2974 3728 4846 -788 208 747 O ATOM 2324 N PHE B 66 33.471 -10.725 22.027 1.00 32.09 N ANISOU 2324 N PHE B 66 3222 3844 5125 -1140 432 -511 N ATOM 2325 CA PHE B 66 32.497 -11.332 21.133 1.00 31.15 C ANISOU 2325 CA PHE B 66 3341 3684 4809 -1073 598 -472 C ATOM 2326 C PHE B 66 31.079 -10.856 21.469 1.00 25.68 C ANISOU 2326 C PHE B 66 2955 2924 3877 -1069 483 -372 C ATOM 2327 O PHE B 66 30.613 -11.025 22.601 1.00 25.35 O ANISOU 2327 O PHE B 66 2974 2863 3794 -1013 300 -368 O ATOM 2328 CB PHE B 66 32.582 -12.864 21.216 1.00 36.72 C ANISOU 2328 CB PHE B 66 4025 4372 5553 -841 558 -519 C ATOM 2329 CG PHE B 66 33.870 -13.445 20.680 1.00 43.99 C ANISOU 2329 CG PHE B 66 4630 5368 6717 -726 712 -653 C ATOM 2330 CD1 PHE B 66 33.932 -13.955 19.389 1.00 46.02 C ANISOU 2330 CD1 PHE B 66 4944 5634 6909 -702 1027 -729 C ATOM 2331 CD2 PHE B 66 35.013 -13.498 21.471 1.00 48.78 C ANISOU 2331 CD2 PHE B 66 4874 6046 7615 -628 535 -723 C ATOM 2332 CE1 PHE B 66 35.109 -14.498 18.892 1.00 49.68 C ANISOU 2332 CE1 PHE B 66 5085 6191 7601 -553 1233 -900 C ATOM 2333 CE2 PHE B 66 36.193 -14.040 20.980 1.00 52.41 C ANISOU 2333 CE2 PHE B 66 4944 6616 8352 -468 687 -877 C ATOM 2334 CZ PHE B 66 36.240 -14.541 19.689 1.00 52.86 C ANISOU 2334 CZ PHE B 66 5039 6697 8349 -415 1072 -980 C ATOM 2335 N LEU B 67 30.408 -10.235 20.500 1.00 23.31 N ANISOU 2335 N LEU B 67 2838 2610 3408 -1087 564 -295 N ATOM 2336 CA LEU B 67 28.985 -9.964 20.639 1.00 21.87 C ANISOU 2336 CA LEU B 67 2843 2398 3068 -1036 477 -235 C ATOM 2337 C LEU B 67 28.239 -11.044 19.871 1.00 22.82 C ANISOU 2337 C LEU B 67 3052 2549 3069 -1005 534 -208 C ATOM 2338 O LEU B 67 28.771 -11.611 18.917 1.00 24.50 O ANISOU 2338 O LEU B 67 3284 2757 3267 -1035 672 -235 O ATOM 2339 CB LEU B 67 28.624 -8.580 20.099 1.00 20.34 C ANISOU 2339 CB LEU B 67 2798 2118 2811 -1089 462 -181 C ATOM 2340 CG LEU B 67 29.403 -7.398 20.672 1.00 24.27 C ANISOU 2340 CG LEU B 67 3288 2534 3399 -1169 395 -201 C ATOM 2341 CD1 LEU B 67 28.772 -6.074 20.259 1.00 24.21 C ANISOU 2341 CD1 LEU B 67 3536 2353 3309 -1207 338 -152 C ATOM 2342 CD2 LEU B 67 29.510 -7.497 22.187 1.00 24.65 C ANISOU 2342 CD2 LEU B 67 3264 2585 3516 -1136 264 -281 C ATOM 2343 N TYR B 68 27.014 -11.336 20.288 1.00 20.97 N ANISOU 2343 N TYR B 68 2877 2350 2739 -981 447 -174 N ATOM 2344 CA TYR B 68 26.227 -12.367 19.627 1.00 21.50 C ANISOU 2344 CA TYR B 68 3035 2452 2682 -999 446 -137 C ATOM 2345 C TYR B 68 24.936 -11.783 19.069 1.00 22.67 C ANISOU 2345 C TYR B 68 3247 2634 2732 -1048 380 -69 C ATOM 2346 O TYR B 68 24.208 -11.075 19.765 1.00 21.53 O ANISOU 2346 O TYR B 68 3024 2543 2615 -1008 315 -69 O ATOM 2347 CB TYR B 68 25.966 -13.536 20.581 1.00 19.35 C ANISOU 2347 CB TYR B 68 2761 2208 2384 -1006 384 -143 C ATOM 2348 CG TYR B 68 27.243 -14.235 20.990 1.00 21.16 C ANISOU 2348 CG TYR B 68 2971 2334 2735 -980 404 -209 C ATOM 2349 CD1 TYR B 68 27.777 -15.254 20.214 1.00 21.51 C ANISOU 2349 CD1 TYR B 68 3102 2283 2787 -943 475 -255 C ATOM 2350 CD2 TYR B 68 27.930 -13.857 22.137 1.00 24.06 C ANISOU 2350 CD2 TYR B 68 3228 2704 3211 -918 308 -240 C ATOM 2351 CE1 TYR B 68 28.953 -15.888 20.575 1.00 22.77 C ANISOU 2351 CE1 TYR B 68 3181 2363 3107 -792 453 -336 C ATOM 2352 CE2 TYR B 68 29.105 -14.486 22.508 1.00 22.68 C ANISOU 2352 CE2 TYR B 68 2975 2459 3184 -813 238 -293 C ATOM 2353 CZ TYR B 68 29.611 -15.500 21.723 1.00 22.67 C ANISOU 2353 CZ TYR B 68 3001 2374 3236 -723 311 -344 C ATOM 2354 OH TYR B 68 30.779 -16.127 22.089 1.00 23.70 O ANISOU 2354 OH TYR B 68 3006 2437 3564 -540 218 -420 O ATOM 2355 N LEU B 69 24.670 -12.074 17.801 1.00 23.38 N ANISOU 2355 N LEU B 69 3481 2697 2705 -1107 378 -28 N ATOM 2356 CA LEU B 69 23.564 -11.451 17.088 1.00 24.10 C ANISOU 2356 CA LEU B 69 3666 2783 2709 -1190 252 63 C ATOM 2357 C LEU B 69 22.441 -12.430 16.782 1.00 26.38 C ANISOU 2357 C LEU B 69 3948 3183 2892 -1280 127 106 C ATOM 2358 O LEU B 69 22.643 -13.427 16.091 1.00 26.14 O ANISOU 2358 O LEU B 69 4078 3115 2740 -1350 151 88 O ATOM 2359 CB LEU B 69 24.067 -10.834 15.783 1.00 25.57 C ANISOU 2359 CB LEU B 69 4093 2837 2784 -1244 283 105 C ATOM 2360 CG LEU B 69 23.017 -10.254 14.834 1.00 26.01 C ANISOU 2360 CG LEU B 69 4342 2835 2706 -1298 59 230 C ATOM 2361 CD1 LEU B 69 22.289 -9.088 15.483 1.00 25.09 C ANISOU 2361 CD1 LEU B 69 4083 2719 2730 -1087 -127 252 C ATOM 2362 CD2 LEU B 69 23.664 -9.825 13.529 1.00 27.59 C ANISOU 2362 CD2 LEU B 69 4868 2897 2717 -1406 120 266 C ATOM 2363 N VAL B 70 21.254 -12.143 17.302 1.00 28.73 N ANISOU 2363 N VAL B 70 4025 3646 3245 -1215 -14 130 N ATOM 2364 CA VAL B 70 20.071 -12.898 16.917 1.00 31.70 C ANISOU 2364 CA VAL B 70 4330 4173 3544 -1355 -171 185 C ATOM 2365 C VAL B 70 19.049 -11.954 16.273 1.00 34.96 C ANISOU 2365 C VAL B 70 4641 4650 3993 -1246 -419 250 C ATOM 2366 O VAL B 70 18.806 -10.852 16.765 1.00 35.90 O ANISOU 2366 O VAL B 70 4597 4790 4253 -1004 -450 220 O ATOM 2367 CB VAL B 70 19.475 -13.719 18.102 1.00 48.13 C ANISOU 2367 CB VAL B 70 6174 6459 5654 -1446 -113 154 C ATOM 2368 CG1 VAL B 70 20.591 -14.400 18.893 1.00 45.74 C ANISOU 2368 CG1 VAL B 70 6013 6029 5335 -1424 56 97 C ATOM 2369 CG2 VAL B 70 18.638 -12.847 19.023 1.00 50.40 C ANISOU 2369 CG2 VAL B 70 6104 6969 6078 -1270 -105 108 C ATOM 2370 N LEU B 71 18.493 -12.370 15.141 1.00 38.74 N ANISOU 2370 N LEU B 71 5265 5121 4335 -1405 -630 334 N ATOM 2371 CA LEU B 71 17.528 -11.546 14.422 1.00 42.56 C ANISOU 2371 CA LEU B 71 5681 5641 4849 -1293 -960 418 C ATOM 2372 C LEU B 71 16.129 -11.769 14.987 1.00 47.94 C ANISOU 2372 C LEU B 71 5853 6667 5695 -1266 -1114 403 C ATOM 2373 O LEU B 71 15.816 -12.856 15.473 1.00 48.63 O ANISOU 2373 O LEU B 71 5784 6937 5757 -1504 -1015 378 O ATOM 2374 CB LEU B 71 17.568 -11.851 12.924 1.00 43.29 C ANISOU 2374 CB LEU B 71 6200 5567 4680 -1502 -1164 520 C ATOM 2375 CG LEU B 71 18.928 -11.632 12.254 1.00 42.43 C ANISOU 2375 CG LEU B 71 6577 5167 4377 -1570 -944 518 C ATOM 2376 CD1 LEU B 71 18.866 -11.954 10.769 1.00 46.21 C ANISOU 2376 CD1 LEU B 71 7531 5500 4528 -1804 -1118 602 C ATOM 2377 CD2 LEU B 71 19.416 -10.207 12.476 1.00 42.62 C ANISOU 2377 CD2 LEU B 71 6641 5045 4508 -1347 -908 538 C ATOM 2378 N ARG B 72 15.293 -10.737 14.930 1.00 53.05 N ANISOU 2378 N ARG B 72 6240 7401 6516 -980 -1352 414 N ATOM 2379 CA ARG B 72 13.977 -10.798 15.556 1.00 60.39 C ANISOU 2379 CA ARG B 72 6559 8722 7663 -892 -1438 357 C ATOM 2380 C ARG B 72 12.963 -11.595 14.741 1.00 67.62 C ANISOU 2380 C ARG B 72 7311 9846 8535 -1174 -1771 452 C ATOM 2381 O ARG B 72 12.117 -12.292 15.303 1.00 70.82 O ANISOU 2381 O ARG B 72 7259 10616 9035 -1362 -1720 412 O ATOM 2382 CB ARG B 72 13.437 -9.391 15.825 1.00 64.48 C ANISOU 2382 CB ARG B 72 6814 9255 8430 -398 -1577 292 C ATOM 2383 CG ARG B 72 14.265 -8.573 16.804 1.00 62.89 C ANISOU 2383 CG ARG B 72 6736 8877 8281 -140 -1266 167 C ATOM 2384 CD ARG B 72 13.461 -7.398 17.344 1.00 68.46 C ANISOU 2384 CD ARG B 72 7087 9668 9254 361 -1352 36 C ATOM 2385 NE ARG B 72 14.306 -6.356 17.922 1.00 69.41 N ANISOU 2385 NE ARG B 72 7521 9470 9382 619 -1196 -55 N ATOM 2386 CZ ARG B 72 14.683 -6.312 19.196 1.00 70.06 C ANISOU 2386 CZ ARG B 72 7527 9623 9470 660 -829 -221 C ATOM 2387 NH1 ARG B 72 14.296 -7.259 20.039 1.00 71.11 N ANISOU 2387 NH1 ARG B 72 7304 10133 9584 458 -554 -301 N ATOM 2388 NH2 ARG B 72 15.452 -5.321 19.627 1.00 69.33 N ANISOU 2388 NH2 ARG B 72 7767 9205 9369 858 -758 -298 N ATOM 2389 N LEU B 73 13.046 -11.492 13.419 1.00 70.35 N ANISOU 2389 N LEU B 73 8058 9962 8709 -1252 -2115 582 N ATOM 2390 CA LEU B 73 12.066 -12.131 12.550 1.00 75.13 C ANISOU 2390 CA LEU B 73 8587 10698 9260 -1477 -2457 657 C ATOM 2391 C LEU B 73 12.737 -12.992 11.486 1.00 74.01 C ANISOU 2391 C LEU B 73 9119 10240 8763 -1803 -2421 728 C ATOM 2392 O LEU B 73 13.442 -13.950 11.803 1.00 70.99 O ANISOU 2392 O LEU B 73 8963 9770 8239 -2029 -2089 682 O ATOM 2393 CB LEU B 73 11.179 -11.073 11.891 1.00 80.76 C ANISOU 2393 CB LEU B 73 9118 11432 10135 -1135 -2918 714 C ATOM 2394 CG LEU B 73 9.979 -11.556 11.076 1.00 87.22 C ANISOU 2394 CG LEU B 73 9760 12411 10968 -1253 -3233 737 C ATOM 2395 CD1 LEU B 73 8.970 -12.269 11.963 1.00 90.27 C ANISOU 2395 CD1 LEU B 73 9464 13241 11593 -1361 -3071 597 C ATOM 2396 CD2 LEU B 73 9.327 -10.383 10.366 1.00 92.10 C ANISOU 2396 CD2 LEU B 73 10317 12972 11704 -861 -3697 802 C TER 2397 LEU B 73 HETATM 2398 O HOH A 301 2.440 -27.410 9.747 1.00 27.62 O HETATM 2399 O HOH A 302 20.059 -46.234 -6.723 1.00 21.65 O HETATM 2400 O HOH A 303 4.141 -45.726 -3.828 1.00 34.95 O HETATM 2401 O HOH A 304 -2.097 -29.277 13.375 1.00 33.58 O HETATM 2402 O HOH A 305 18.636 -33.763 28.153 1.00 25.66 O HETATM 2403 O HOH A 306 20.573 -49.417 4.341 1.00 34.06 O HETATM 2404 O HOH A 307 1.207 -31.731 -6.786 1.00 32.17 O HETATM 2405 O HOH A 308 26.789 -19.393 3.243 1.00 53.79 O HETATM 2406 O HOH A 309 7.964 -46.049 -7.878 1.00 34.07 O HETATM 2407 O HOH A 310 3.092 -22.212 11.491 1.00 33.27 O HETATM 2408 O HOH A 311 6.165 -46.260 15.139 1.00 39.03 O HETATM 2409 O HOH A 312 21.036 -15.682 11.651 1.00 53.70 O HETATM 2410 O HOH A 313 17.360 -32.170 0.318 1.00 30.27 O HETATM 2411 O HOH A 314 -2.773 -36.390 0.442 1.00 27.03 O HETATM 2412 O HOH A 315 28.248 -20.646 26.879 1.00 32.81 O HETATM 2413 O HOH A 316 22.457 -34.801 19.925 1.00 29.40 O HETATM 2414 O HOH A 317 17.585 -47.417 -5.211 1.00 38.76 O HETATM 2415 O HOH A 318 28.261 -15.151 26.288 1.00 44.56 O HETATM 2416 O HOH A 319 19.267 -45.682 17.594 1.00 35.88 O HETATM 2417 O HOH A 320 21.786 -36.483 7.108 1.00 41.04 O HETATM 2418 O HOH A 321 20.472 -36.211 4.154 1.00 35.14 O HETATM 2419 O HOH A 322 4.923 -20.209 17.869 1.00 26.01 O HETATM 2420 O HOH A 323 13.022 -47.195 16.886 1.00 42.92 O HETATM 2421 O HOH A 324 -3.806 -37.752 2.436 1.00 34.29 O HETATM 2422 O HOH A 325 0.957 -43.263 2.204 1.00 21.50 O HETATM 2423 O HOH A 326 16.368 -16.657 28.401 1.00 34.51 O HETATM 2424 O HOH A 327 12.164 -31.398 -2.418 1.00 33.52 O HETATM 2425 O HOH A 328 13.480 -41.840 -8.168 1.00 27.53 O HETATM 2426 O HOH A 329 5.648 -18.893 4.115 1.00 53.77 O HETATM 2427 O HOH A 330 15.800 -34.642 28.210 1.00 48.46 O HETATM 2428 O HOH A 331 14.518 -46.827 7.532 1.00 32.65 O HETATM 2429 O HOH A 332 30.229 -31.627 21.136 1.00 41.37 O HETATM 2430 O HOH A 333 25.872 -43.510 1.982 1.00 47.66 O HETATM 2431 O HOH A 334 9.863 -22.690 -6.478 1.00 41.39 O HETATM 2432 O HOH A 335 18.996 -49.488 -4.058 1.00 45.52 O HETATM 2433 O HOH A 336 8.214 -24.862 13.172 1.00 43.74 O HETATM 2434 O HOH A 337 19.915 -35.061 18.572 1.00 38.50 O HETATM 2435 O HOH A 338 29.310 -26.350 22.534 1.00 37.20 O HETATM 2436 O HOH A 339 23.654 -41.836 -5.221 1.00 35.17 O HETATM 2437 O HOH A 340 25.478 -45.754 -0.188 1.00 36.33 O HETATM 2438 O HOH A 341 3.050 -24.546 22.180 1.00 28.52 O HETATM 2439 O HOH A 342 10.706 -36.719 25.576 1.00 42.29 O HETATM 2440 O HOH A 343 12.597 -37.933 27.331 1.00 40.87 O HETATM 2441 O HOH A 344 2.069 -22.602 21.176 1.00 41.04 O HETATM 2442 O HOH A 345 27.905 -25.861 18.033 1.00 33.30 O HETATM 2443 O HOH A 346 28.988 -27.934 24.507 1.00 43.37 O HETATM 2444 O HOH A 347 26.300 -24.829 15.728 1.00 42.65 O HETATM 2445 O HOH A 348 27.248 -17.267 27.408 1.00 44.00 O HETATM 2446 O HOH A 349 23.708 -15.521 1.401 1.00 48.62 O HETATM 2447 O HOH A 350 0.077 -30.914 16.690 1.00 38.36 O HETATM 2448 O HOH A 351 18.302 -46.555 22.152 1.00 34.58 O HETATM 2449 O HOH A 352 11.894 -49.156 9.649 1.00 30.40 O HETATM 2450 O HOH A 353 15.319 -30.780 -0.494 1.00 37.03 O HETATM 2451 O HOH A 354 4.063 -24.180 25.035 1.00 40.19 O HETATM 2452 O HOH A 355 12.877 -36.201 -10.605 1.00 47.81 O HETATM 2453 O HOH A 356 15.605 -16.689 19.517 1.00 44.04 O HETATM 2454 O HOH A 357 29.784 -22.393 8.556 1.00 47.87 O HETATM 2455 O HOH A 358 6.594 -5.385 5.425 1.00 44.69 O HETATM 2456 O HOH B 101 25.893 -13.648 25.197 1.00 19.58 O HETATM 2457 O HOH B 102 19.984 -5.361 21.057 1.00 40.56 O HETATM 2458 O HOH B 103 33.644 -9.421 8.561 1.00 40.11 O HETATM 2459 O HOH B 104 35.320 -7.516 27.727 1.00 31.98 O HETATM 2460 O HOH B 105 21.686 -20.668 32.718 1.00 34.82 O HETATM 2461 O HOH B 106 29.942 -13.234 26.353 1.00 30.16 O HETATM 2462 O HOH B 107 19.236 -14.579 14.166 1.00 44.61 O HETATM 2463 O HOH B 108 13.143 -8.581 21.614 1.00 49.66 O HETATM 2464 O HOH B 109 18.900 -9.348 28.748 1.00 33.46 O HETATM 2465 O HOH B 110 33.704 3.667 15.221 1.00 43.59 O HETATM 2466 O HOH B 111 35.041 -12.374 10.777 1.00 46.57 O HETATM 2467 O HOH B 112 41.622 -4.464 19.299 1.00 31.88 O HETATM 2468 O HOH B 113 28.530 5.797 19.018 1.00 43.90 O HETATM 2469 O HOH B 114 31.077 3.540 30.655 1.00 26.43 O HETATM 2470 O HOH B 115 35.237 -0.515 26.259 1.00 36.63 O HETATM 2471 O HOH B 116 38.443 -12.286 23.539 1.00 49.80 O HETATM 2472 O HOH B 117 41.880 -1.768 16.433 1.00 54.35 O HETATM 2473 O HOH B 118 23.788 -14.968 9.140 1.00 49.75 O HETATM 2474 O HOH B 119 29.061 7.103 21.018 1.00 31.96 O HETATM 2475 O HOH B 120 11.453 -12.651 17.419 1.00 25.94 O HETATM 2476 O HOH B 121 37.211 -14.179 11.624 1.00 39.87 O HETATM 2477 O HOH B 122 18.271 -7.602 5.126 1.00 32.79 O HETATM 2478 O HOH B 123 42.161 5.429 19.611 1.00 35.00 O HETATM 2479 O HOH B 124 30.518 -9.118 6.805 1.00 52.39 O HETATM 2480 O HOH B 125 32.201 -15.277 24.563 1.00 40.47 O HETATM 2481 O HOH B 126 43.793 -6.517 20.815 1.00 48.90 O MASTER 433 0 0 14 11 0 0 6 2479 2 0 24 END
Display Options:
Goto PDB code:
3D presentation of molecule is powered by
3Dmol
, which supports all modern browsers and mobile devices via WebGL.
Hold mouse button:
left to rotate,middle to shift,right to zoom
Related entries of code: 4i6l
Entries with 90% protein sequence similarity cutoff in PDBbind
PDB Code
Check Database
Protein Sequence Similarity
1cmx
RCSB PDB
PDBbind
76aa, >1CMX_2|Chains... at 100%
1xd3
RCSB PDB
PDBbind
75aa, >1XD3_2|Chains... at 100%
2hd5
RCSB PDB
PDBbind
76aa, >2HD5_2|Chain... at 100%
2xbb
RCSB PDB
PDBbind
76aa, >2XBB_2|Chains... at 100%
2y5b
RCSB PDB
PDBbind
152aa, >2Y5B_2|Chains... at 99%
3dvg
RCSB PDB
PDBbind
79aa, >3DVG_4|Chain... at 94%
3dvn
RCSB PDB
PDBbind
79aa, >3DVN_4|Chains... at 94%
3kw5
RCSB PDB
PDBbind
75aa, >3KW5_2|Chain... at 100%
3olm
RCSB PDB
PDBbind
79aa, >3OLM_2|Chain... at 92%
3rul
RCSB PDB
PDBbind
79aa, >3RUL_1|Chains... at 94%
3znz
RCSB PDB
PDBbind
152aa, >3ZNZ_2|Chain... at 100%
4m0w
RCSB PDB
PDBbind
76aa, >4M0W_2|Chain... at 100%
5e6j
RCSB PDB
PDBbind
76aa, >5E6J_2|Chains... at 97%
5gvi
RCSB PDB
PDBbind
72aa, >5GVI_3|Chain... at 100%
5l6h
RCSB PDB
PDBbind
76aa, >5L6H_2|Chains... at 96%
5l6i
RCSB PDB
PDBbind
76aa, >5L6I_2|Chains... at 96%
5l6j
RCSB PDB
PDBbind
76aa, >5L6J_2|Chains... at 96%
5lrw
RCSB PDB
PDBbind
76aa, >5LRW_2|Chains... at 98%
5ohp
RCSB PDB
PDBbind
76aa, >5OHP_2|Chains... at 100%
5ydr
RCSB PDB
PDBbind
75aa, >5YDR_1|Chains... at 97%
5yij
RCSB PDB
PDBbind
78aa, >5YIJ_2|Chains... at 97%
6isu
RCSB PDB
PDBbind
76aa, >6ISU_3|Chain... at 100%
Complexes with the same small molecule ligand
PDB Code
Check Database
Ligand Name
1otr
RCSB PDB
PDBbind
ubiquitin
1p3q
RCSB PDB
PDBbind
ubiquitin
1q0w
RCSB PDB
PDBbind
ubiquitin
1s1q
RCSB PDB
PDBbind
Ubiquitin
1wr1
RCSB PDB
PDBbind
ubiquitin
1wr6
RCSB PDB
PDBbind
ubiquitin
1wrd
RCSB PDB
PDBbind
ubiquitin
1yx5
RCSB PDB
PDBbind
Ubiquitin
1yx6
RCSB PDB
PDBbind
Ubiquitin
2c7m
RCSB PDB
PDBbind
ubiquitin
2c7n
RCSB PDB
PDBbind
ubiquitin
2den
RCSB PDB
PDBbind
Ubiquitin
2dx5
RCSB PDB
PDBbind
Ubiquitin
2fuh
RCSB PDB
PDBbind
Ubiquitin
2g45
RCSB PDB
PDBbind
ubiquitin
2hd5
RCSB PDB
PDBbind
ubiquitin
2hth
RCSB PDB
PDBbind
ubiquitin
2jt4
RCSB PDB
PDBbind
Ubiquitin
2k6d
RCSB PDB
PDBbind
ubiquitin
2kwu
RCSB PDB
PDBbind
Ubiquitin
2kwv
RCSB PDB
PDBbind
Ubiquitin
2lvo
RCSB PDB
PDBbind
ubiquitin
2mbb
RCSB PDB
PDBbind
Ubiquitin
2mcn
RCSB PDB
PDBbind
Ubiquitin
2mj5
RCSB PDB
PDBbind
Ubiquitin
2mur
RCSB PDB
PDBbind
Ubiquitin
2oob
RCSB PDB
PDBbind
ubiquitin
2qho
RCSB PDB
PDBbind
ubiquitin
2xbb
RCSB PDB
PDBbind
UBIQUITIN
3olm
RCSB PDB
PDBbind
Ubiquitin
4hcn
RCSB PDB
PDBbind
ubiquitin
4k1r
RCSB PDB
PDBbind
Ubiquitin
4m0w
RCSB PDB
PDBbind
ubiquitin
4msm
RCSB PDB
PDBbind
Ubiquitin
Entry Information
PDB ID
4i6l
Complex Type
Protein-Protein
PDBbind Subset
general set
Protein Name
Ubiquitin thioesterase OTUB1
Ligand Name
Ubiquitin
EC.Number
E.C.3.4.19.12
Resolution
2.49(Å)
Affinity (Kd/Ki/IC50)
Kd=20nM
Release Year
2013
Protein/NA Sequence
Check fasta file
Primary Reference
(2013) Science Vol. 339: pp. 590-595
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):
Q96FW1
P0CG48
Entrez Gene ID
NCBI Entrez Gene ID:
55611
7316
ASD
Information of known allosteric effects of PDB entries
This site has been visited
times since Nov 2007.
Copyright ©2007-2024 涓婃捣鐩堣禌鎬濅俊鎭鎶鏈夐檺鍏徃 缃戠珯澶囨鍙凤細
娌狪CP澶2021015625鍙-3
娌叕缃戝畨澶囷細
姝ｅ湪鐢宠涓
Technical Support锛堟妧鏈敮鎸侊級:
yingsaisi@foxmail.com
times since Nov 2007. 
娌叕缃戝畨澶囷細姝ｅ湪鐢宠涓