HEADER SIGNALING PROTEIN 07-DEC-11 3UZA TITLE THERMOSTABILISED ADENOSINE A2A RECEPTOR IN COMPLEX WITH 6-(2,6- TITLE 2 DIMETHYLPYRIDIN-4-YL)-5-PHENYL-1,2,4-TRIAZIN-3-AMINE COMPND MOL_ID: 1; COMPND 2 MOLECULE: ADENOSINE RECEPTOR A2A; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: RESIDUES 1-317; COMPND 5 ENGINEERED: YES; COMPND 6 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: ADORA2A; SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS KEYWDS 7TM, GPCR, SIGNALING PROTEIN, G-PROTEIN, MEMBRANE PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR M.CONGREVE,S.P.ANDREWS,A.S.DORE,K.HOLLENSTEIN,E.HURRELL,C.J.LANGMEAD, AUTHOR 2 J.S.MASON,I.W.NG,B.TEHAN,A.ZHUKOV,M.WEIR,F.H.MARSHALL REVDAT 1 21-MAR-12 3UZA 0 JRNL AUTH M.CONGREVE,S.P.ANDREWS,A.S.DORE,K.HOLLENSTEIN,E.HURRELL, JRNL AUTH 2 C.J.LANGMEAD,J.S.MASON,I.W.NG,B.TEHAN,A.ZHUKOV,M.WEIR, JRNL AUTH 3 F.H.MARSHALL JRNL TITL DISCOVERY OF 1,2,4-TRIAZINE DERIVATIVES AS ADENOSINE A(2A) JRNL TITL 2 ANTAGONISTS USING STRUCTURE BASED DRUG DESIGN JRNL REF J.MED.CHEM. V. 55 1898 2012 JRNL REFN ISSN 0022-2623 JRNL PMID 22220592 JRNL DOI 10.1021/JM201376W REMARK 2 REMARK 2 RESOLUTION. 3.27 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.4_84) 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 : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.27 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.77 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.510 REMARK 3 COMPLETENESS FOR RANGE (%) : 91.6 REMARK 3 NUMBER OF REFLECTIONS : 11401 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.295 REMARK 3 R VALUE (WORKING SET) : 0.293 REMARK 3 FREE R VALUE : 0.335 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.810 REMARK 3 FREE R VALUE TEST SET COUNT : 548 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 19.7738 - 5.1716 0.92 2815 136 0.2638 0.3074 REMARK 3 2 5.1716 - 4.1170 0.93 2736 136 0.2607 0.2966 REMARK 3 3 4.1170 - 3.6002 0.94 2703 158 0.3316 0.3934 REMARK 3 4 3.6002 - 3.2726 0.88 2599 118 0.3950 0.4260 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.11 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : 0.22 REMARK 3 B_SOL : 60.16 REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.460 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 42.610 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 94.40 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 154.90 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -72.30920 REMARK 3 B22 (A**2) : 7.05460 REMARK 3 B33 (A**2) : 45.66940 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 : 0.002 2333 REMARK 3 ANGLE : 0.466 3180 REMARK 3 CHIRALITY : 0.031 377 REMARK 3 PLANARITY : 0.002 390 REMARK 3 DIHEDRAL : 11.809 789 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 15 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: chain A and resid 7:33 REMARK 3 ORIGIN FOR THE GROUP (A): 29.8601 19.8787 41.9416 REMARK 3 T TENSOR REMARK 3 T11: 0.7974 T22: 1.0542 REMARK 3 T33: 2.2534 T12: -0.0532 REMARK 3 T13: -0.1911 T23: 0.0891 REMARK 3 L TENSOR REMARK 3 L11: 0.5730 L22: 0.6937 REMARK 3 L33: 3.3859 L12: -0.4859 REMARK 3 L13: -1.2981 L23: 0.7333 REMARK 3 S TENSOR REMARK 3 S11: 1.5321 S12: -0.4203 S13: -1.1429 REMARK 3 S21: 0.9976 S22: 0.2253 S23: -0.0887 REMARK 3 S31: 0.5770 S32: -0.1862 S33: 0.0000 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: chain A and resid 34:40 REMARK 3 ORIGIN FOR THE GROUP (A): 11.6918 21.2280 29.8354 REMARK 3 T TENSOR REMARK 3 T11: 1.0264 T22: 1.4670 REMARK 3 T33: 2.7036 T12: 0.0609 REMARK 3 T13: 0.0490 T23: 0.3644 REMARK 3 L TENSOR REMARK 3 L11: 0.0286 L22: 0.0225 REMARK 3 L33: 0.0438 L12: 0.0231 REMARK 3 L13: 0.0268 L23: 0.0321 REMARK 3 S TENSOR REMARK 3 S11: 0.4098 S12: 1.6802 S13: -0.2703 REMARK 3 S21: -1.7773 S22: -0.0295 S23: 0.7118 REMARK 3 S31: 0.7285 S32: 1.2415 S33: 0.0000 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: chain A and resid 41:68 REMARK 3 ORIGIN FOR THE GROUP (A): 33.5546 17.7564 33.5287 REMARK 3 T TENSOR REMARK 3 T11: 0.8403 T22: 0.9101 REMARK 3 T33: 2.3669 T12: 0.0610 REMARK 3 T13: -0.3570 T23: 0.4226 REMARK 3 L TENSOR REMARK 3 L11: 0.5788 L22: 0.7159 REMARK 3 L33: 0.9007 L12: 0.2259 REMARK 3 L13: -0.6952 L23: -0.0923 REMARK 3 S TENSOR REMARK 3 S11: 0.0076 S12: 1.1804 S13: 0.8842 REMARK 3 S21: 0.3159 S22: -0.6586 S23: -1.0298 REMARK 3 S31: -0.0511 S32: 0.1067 S33: -0.0000 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: chain A and resid 69:76 REMARK 3 ORIGIN FOR THE GROUP (A): 51.8895 7.6703 31.7134 REMARK 3 T TENSOR REMARK 3 T11: 0.7163 T22: 1.0993 REMARK 3 T33: 3.3229 T12: 0.3037 REMARK 3 T13: -0.0733 T23: 0.1859 REMARK 3 L TENSOR REMARK 3 L11: 0.1244 L22: 0.4084 REMARK 3 L33: 0.1322 L12: -0.0854 REMARK 3 L13: 0.0067 L23: -0.2117 REMARK 3 S TENSOR REMARK 3 S11: -0.0765 S12: -0.1589 S13: 0.3099 REMARK 3 S21: -1.2246 S22: 0.1678 S23: -0.4967 REMARK 3 S31: -0.8882 S32: 1.0536 S33: 0.0001 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: chain A and resid 77:104 REMARK 3 ORIGIN FOR THE GROUP (A): 32.8243 21.6182 23.9034 REMARK 3 T TENSOR REMARK 3 T11: 1.0013 T22: 0.8443 REMARK 3 T33: 1.0992 T12: 0.3537 REMARK 3 T13: -0.2194 T23: 0.4823 REMARK 3 L TENSOR REMARK 3 L11: 0.2977 L22: 0.4311 REMARK 3 L33: 1.0082 L12: 0.1865 REMARK 3 L13: 0.0356 L23: 0.5991 REMARK 3 S TENSOR REMARK 3 S11: 1.4228 S12: 0.9274 S13: -0.4301 REMARK 3 S21: -1.5677 S22: -0.1297 S23: -0.1154 REMARK 3 S31: 1.3687 S32: -0.1525 S33: -0.0000 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: chain A and resid 105:118 REMARK 3 ORIGIN FOR THE GROUP (A): 12.8547 27.1731 14.2424 REMARK 3 T TENSOR REMARK 3 T11: 1.0868 T22: 1.9058 REMARK 3 T33: 3.5319 T12: -0.0266 REMARK 3 T13: -0.1959 T23: 0.4545 REMARK 3 L TENSOR REMARK 3 L11: 0.1467 L22: 0.1825 REMARK 3 L33: 0.2377 L12: -0.1602 REMARK 3 L13: -0.1924 L23: 0.2112 REMARK 3 S TENSOR REMARK 3 S11: -0.2507 S12: 2.0818 S13: -0.5415 REMARK 3 S21: -2.1820 S22: -0.1503 S23: 0.2694 REMARK 3 S31: 0.5972 S32: 0.9899 S33: 0.0000 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: chain A and resid 119:141 REMARK 3 ORIGIN FOR THE GROUP (A): 32.8881 14.6050 19.5265 REMARK 3 T TENSOR REMARK 3 T11: 1.2026 T22: 1.4771 REMARK 3 T33: 2.1403 T12: 0.0390 REMARK 3 T13: -0.2414 T23: -0.1281 REMARK 3 L TENSOR REMARK 3 L11: 0.1248 L22: 0.6509 REMARK 3 L33: 0.8149 L12: 0.1442 REMARK 3 L13: -0.1095 L23: 0.4713 REMARK 3 S TENSOR REMARK 3 S11: 0.4854 S12: 2.2377 S13: -0.3539 REMARK 3 S21: -1.7063 S22: 0.0087 S23: -0.7588 REMARK 3 S31: 0.5235 S32: 0.6693 S33: -0.0000 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: chain A and resid 142:149 REMARK 3 ORIGIN FOR THE GROUP (A): 56.5427 13.9557 21.6676 REMARK 3 T TENSOR REMARK 3 T11: 1.3244 T22: 1.3539 REMARK 3 T33: 3.6434 T12: -0.2437 REMARK 3 T13: 0.1519 T23: 0.1364 REMARK 3 L TENSOR REMARK 3 L11: 0.0151 L22: 0.2613 REMARK 3 L33: 0.1510 L12: 0.0474 REMARK 3 L13: 0.0175 L23: 0.1771 REMARK 3 S TENSOR REMARK 3 S11: -2.5638 S12: 0.1327 S13: -0.4075 REMARK 3 S21: -1.5054 S22: -0.0311 S23: 0.4975 REMARK 3 S31: 2.5504 S32: 0.7844 S33: -0.0002 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: chain A and resid 158:175 REMARK 3 ORIGIN FOR THE GROUP (A): 55.8040 13.4600 29.5073 REMARK 3 T TENSOR REMARK 3 T11: 0.9651 T22: 1.4727 REMARK 3 T33: 3.1046 T12: 0.0355 REMARK 3 T13: -0.2268 T23: -0.1799 REMARK 3 L TENSOR REMARK 3 L11: 0.4984 L22: 0.6921 REMARK 3 L33: 1.0769 L12: -0.1780 REMARK 3 L13: -0.2810 L23: 0.8597 REMARK 3 S TENSOR REMARK 3 S11: 1.4255 S12: 1.7188 S13: -0.1189 REMARK 3 S21: -0.8874 S22: 0.4692 S23: -0.8777 REMARK 3 S31: 1.1928 S32: 2.1782 S33: 0.0000 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: chain A and resid 176:211 REMARK 3 ORIGIN FOR THE GROUP (A): 30.3864 34.6141 17.7844 REMARK 3 T TENSOR REMARK 3 T11: 0.8917 T22: 1.3173 REMARK 3 T33: 1.6806 T12: 0.2854 REMARK 3 T13: -0.1635 T23: 0.1918 REMARK 3 L TENSOR REMARK 3 L11: 0.7746 L22: 0.9038 REMARK 3 L33: 1.8450 L12: 0.8354 REMARK 3 L13: 0.4427 L23: 0.2486 REMARK 3 S TENSOR REMARK 3 S11: 0.0479 S12: -0.6906 S13: 0.7535 REMARK 3 S21: 0.0033 S22: -0.2091 S23: 0.4172 REMARK 3 S31: 0.2613 S32: -0.2197 S33: 0.0000 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: chain A and resid 212:220 REMARK 3 ORIGIN FOR THE GROUP (A): 2.2237 45.7382 18.7634 REMARK 3 T TENSOR REMARK 3 T11: 1.1082 T22: 1.6025 REMARK 3 T33: 3.4713 T12: -0.0152 REMARK 3 T13: -0.4406 T23: 0.5201 REMARK 3 L TENSOR REMARK 3 L11: 0.0410 L22: 0.0034 REMARK 3 L33: 0.1100 L12: -0.0084 REMARK 3 L13: -0.0677 L23: 0.0167 REMARK 3 S TENSOR REMARK 3 S11: -0.7367 S12: 1.3159 S13: 0.4136 REMARK 3 S21: -0.6100 S22: 1.4132 S23: -0.2355 REMARK 3 S31: -0.7138 S32: 1.0698 S33: 0.0000 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: chain A and resid 221:258 REMARK 3 ORIGIN FOR THE GROUP (A): 31.4883 33.9806 26.7093 REMARK 3 T TENSOR REMARK 3 T11: 0.8441 T22: 0.6548 REMARK 3 T33: 1.7843 T12: 0.0149 REMARK 3 T13: -0.0433 T23: -0.1770 REMARK 3 L TENSOR REMARK 3 L11: 0.4526 L22: 1.8293 REMARK 3 L33: 2.3894 L12: -0.0272 REMARK 3 L13: 0.9206 L23: -1.1423 REMARK 3 S TENSOR REMARK 3 S11: 1.5304 S12: 0.9797 S13: 1.9018 REMARK 3 S21: -1.1397 S22: -0.4916 S23: -0.4669 REMARK 3 S31: 0.1125 S32: -0.4865 S33: 0.0001 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: chain A and resid 259:267 REMARK 3 ORIGIN FOR THE GROUP (A): 58.3201 32.6214 30.1614 REMARK 3 T TENSOR REMARK 3 T11: 0.9364 T22: 1.1418 REMARK 3 T33: 2.7737 T12: 0.1130 REMARK 3 T13: -0.1816 T23: -0.0347 REMARK 3 L TENSOR REMARK 3 L11: 0.3572 L22: 0.4196 REMARK 3 L33: 0.6487 L12: 0.2018 REMARK 3 L13: 0.0750 L23: 0.4769 REMARK 3 S TENSOR REMARK 3 S11: 1.5342 S12: 2.2205 S13: -0.4853 REMARK 3 S21: -0.0984 S22: -1.7001 S23: 1.2596 REMARK 3 S31: -1.0689 S32: -0.4521 S33: 0.0011 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: chain A and resid 268:292 REMARK 3 ORIGIN FOR THE GROUP (A): 34.4680 29.2297 37.1336 REMARK 3 T TENSOR REMARK 3 T11: 1.0619 T22: 0.1901 REMARK 3 T33: -0.6292 T12: -0.1317 REMARK 3 T13: 0.1912 T23: -1.2089 REMARK 3 L TENSOR REMARK 3 L11: 0.3439 L22: 0.1461 REMARK 3 L33: 1.6867 L12: -0.0656 REMARK 3 L13: 0.2472 L23: 0.5952 REMARK 3 S TENSOR REMARK 3 S11: 0.0402 S12: -0.5240 S13: 0.2477 REMARK 3 S21: 0.1374 S22: -0.1282 S23: -0.2133 REMARK 3 S31: -0.3508 S32: -0.6276 S33: 0.5979 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: chain A and resid 293:305 REMARK 3 ORIGIN FOR THE GROUP (A): 13.5317 25.8910 42.3899 REMARK 3 T TENSOR REMARK 3 T11: 1.1135 T22: 1.8098 REMARK 3 T33: 2.0674 T12: 0.0320 REMARK 3 T13: -0.0760 T23: -0.1646 REMARK 3 L TENSOR REMARK 3 L11: 0.1563 L22: 0.3944 REMARK 3 L33: 0.0408 L12: 0.2101 REMARK 3 L13: 0.0870 L23: 0.1107 REMARK 3 S TENSOR REMARK 3 S11: 0.3952 S12: -0.8974 S13: 0.2206 REMARK 3 S21: 0.0266 S22: -0.1258 S23: 1.8021 REMARK 3 S31: -1.7608 S32: -3.0972 S33: -0.0000 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 3UZA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-DEC-11. REMARK 100 THE RCSB ID CODE IS RCSB069396. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 12-MAY-10 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 8.0 REMARK 200 NUMBER OF CRYSTALS USED : 2 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : DIAMOND REMARK 200 BEAMLINE : I24 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9777 REMARK 200 MONOCHROMATOR : ACCEL FIXED EXIT DOUBLE CRYSTAL REMARK 200 SI (111) REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : SCALA REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 11568 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.273 REMARK 200 RESOLUTION RANGE LOW (A) : 49.400 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 93.6 REMARK 200 DATA REDUNDANCY : 6.100 REMARK 200 R MERGE (I) : 0.11000 REMARK 200 R SYM (I) : NULL REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.3000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.27 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.46 REMARK 200 COMPLETENESS FOR SHELL (%) : 88.2 REMARK 200 DATA REDUNDANCY IN SHELL : 6.10 REMARK 200 R MERGE FOR SHELL (I) : 0.96000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.600 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: 3PWH REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 77.20 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 5.40 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 32-42% PEG1000, 0.25M MGCL2, 0.3% NG, REMARK 280 0.1%(W/V) 1-BUTANOL, 0.05% CYMAL-6, 0.1M TRIS-HCL, PH 8.0, VAPOR REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 277K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z REMARK 290 3555 -X,Y,-Z REMARK 290 4555 X,-Y,-Z REMARK 290 5555 X+1/2,Y+1/2,Z+1/2 REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2 REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2 REMARK 290 8555 X+1/2,-Y+1/2,-Z+1/2 REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 3 -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 0.00000 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 55.90700 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 55.94800 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 62.92050 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 55.90700 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 55.94800 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 62.92050 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 55.90700 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 55.94800 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 62.92050 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 55.90700 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 55.94800 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 62.92050 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: A REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 MET A 1 REMARK 465 PRO A 2 REMARK 465 ILE A 3 REMARK 465 MET A 4 REMARK 465 GLY A 5 REMARK 465 SER A 6 REMARK 465 LYS A 150 REMARK 465 GLU A 151 REMARK 465 GLY A 152 REMARK 465 LYS A 153 REMARK 465 ASN A 154 REMARK 465 HIS A 155 REMARK 465 SER A 156 REMARK 465 GLN A 157 REMARK 465 HIS A 306 REMARK 465 VAL A 307 REMARK 465 LEU A 308 REMARK 465 ARG A 309 REMARK 465 GLN A 310 REMARK 465 GLN A 311 REMARK 465 GLU A 312 REMARK 465 PRO A 313 REMARK 465 PHE A 314 REMARK 465 LYS A 315 REMARK 465 ALA A 316 REMARK 465 ALA A 317 REMARK 465 ALA A 318 REMARK 465 ALA A 319 REMARK 465 HIS A 320 REMARK 465 HIS A 321 REMARK 465 HIS A 322 REMARK 465 HIS A 323 REMARK 465 HIS A 324 REMARK 465 HIS A 325 REMARK 465 HIS A 326 REMARK 465 HIS A 327 REMARK 465 HIS A 328 REMARK 465 HIS A 329 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 LEU A 58 -56.42 -130.12 REMARK 500 ALA A 165 105.73 -54.51 REMARK 500 VAL A 178 -61.87 -103.32 REMARK 500 PHE A 182 -74.24 -76.79 REMARK 500 VAL A 186 -57.54 -125.38 REMARK 500 PRO A 215 20.22 -72.39 REMARK 500 PRO A 217 -71.94 -57.57 REMARK 500 SER A 263 112.66 -38.45 REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE T4G A 330 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 3UZC RELATED DB: PDB REMARK 900 THE SAME PROTEIN COMPLEXED WITH COMPOUND 4E REMARK 900 RELATED ID: 3PWH RELATED DB: PDB REMARK 900 THE SAME PROTEIN COMPLEXED WITH ZM241385 REMARK 900 RELATED ID: 3REY RELATED DB: PDB REMARK 900 THE SAME PROTEIN COMPLEXED WITH XAC REMARK 900 RELATED ID: 3RFM RELATED DB: PDB REMARK 900 THE SAME PROTEIN COMPLEXED WITH CAFFEINE DBREF 3UZA A 1 317 UNP P29274 AA2AR_HUMAN 1 317 SEQADV 3UZA LEU A 54 UNP P29274 ALA 54 ENGINEERED MUTATION SEQADV 3UZA ALA A 88 UNP P29274 THR 88 ENGINEERED MUTATION SEQADV 3UZA ALA A 107 UNP P29274 ARG 107 ENGINEERED MUTATION SEQADV 3UZA ALA A 122 UNP P29274 LYS 122 ENGINEERED MUTATION SEQADV 3UZA ALA A 202 UNP P29274 LEU 202 ENGINEERED MUTATION SEQADV 3UZA ALA A 235 UNP P29274 LEU 235 ENGINEERED MUTATION SEQADV 3UZA ALA A 239 UNP P29274 VAL 239 ENGINEERED MUTATION SEQADV 3UZA ALA A 277 UNP P29274 SER 277 ENGINEERED MUTATION SEQADV 3UZA ALA A 318 UNP P29274 EXPRESSION TAG SEQADV 3UZA ALA A 319 UNP P29274 EXPRESSION TAG SEQADV 3UZA HIS A 320 UNP P29274 EXPRESSION TAG SEQADV 3UZA HIS A 321 UNP P29274 EXPRESSION TAG SEQADV 3UZA HIS A 322 UNP P29274 EXPRESSION TAG SEQADV 3UZA HIS A 323 UNP P29274 EXPRESSION TAG SEQADV 3UZA HIS A 324 UNP P29274 EXPRESSION TAG SEQADV 3UZA HIS A 325 UNP P29274 EXPRESSION TAG SEQADV 3UZA HIS A 326 UNP P29274 EXPRESSION TAG SEQADV 3UZA HIS A 327 UNP P29274 EXPRESSION TAG SEQADV 3UZA HIS A 328 UNP P29274 EXPRESSION TAG SEQADV 3UZA HIS A 329 UNP P29274 EXPRESSION TAG SEQRES 1 A 329 MET PRO ILE MET GLY SER SER VAL TYR ILE THR VAL GLU SEQRES 2 A 329 LEU ALA ILE ALA VAL LEU ALA ILE LEU GLY ASN VAL LEU SEQRES 3 A 329 VAL CYS TRP ALA VAL TRP LEU ASN SER ASN LEU GLN ASN SEQRES 4 A 329 VAL THR ASN TYR PHE VAL VAL SER LEU ALA ALA ALA ASP SEQRES 5 A 329 ILE LEU VAL GLY VAL LEU ALA ILE PRO PHE ALA ILE THR SEQRES 6 A 329 ILE SER THR GLY PHE CYS ALA ALA CYS HIS GLY CYS LEU SEQRES 7 A 329 PHE ILE ALA CYS PHE VAL LEU VAL LEU ALA GLN SER SER SEQRES 8 A 329 ILE PHE SER LEU LEU ALA ILE ALA ILE ASP ARG TYR ILE SEQRES 9 A 329 ALA ILE ALA ILE PRO LEU ARG TYR ASN GLY LEU VAL THR SEQRES 10 A 329 GLY THR ARG ALA ALA GLY ILE ILE ALA ILE CYS TRP VAL SEQRES 11 A 329 LEU SER PHE ALA ILE GLY LEU THR PRO MET LEU GLY TRP SEQRES 12 A 329 ASN ASN CYS GLY GLN PRO LYS GLU GLY LYS ASN HIS SER SEQRES 13 A 329 GLN GLY CYS GLY GLU GLY GLN VAL ALA CYS LEU PHE GLU SEQRES 14 A 329 ASP VAL VAL PRO MET ASN TYR MET VAL TYR PHE ASN PHE SEQRES 15 A 329 PHE ALA CYS VAL LEU VAL PRO LEU LEU LEU MET LEU GLY SEQRES 16 A 329 VAL TYR LEU ARG ILE PHE ALA ALA ALA ARG ARG GLN LEU SEQRES 17 A 329 LYS GLN MET GLU SER GLN PRO LEU PRO GLY GLU ARG ALA SEQRES 18 A 329 ARG SER THR LEU GLN LYS GLU VAL HIS ALA ALA LYS SER SEQRES 19 A 329 ALA ALA ILE ILE ALA GLY LEU PHE ALA LEU CYS TRP LEU SEQRES 20 A 329 PRO LEU HIS ILE ILE ASN CYS PHE THR PHE PHE CYS PRO SEQRES 21 A 329 ASP CYS SER HIS ALA PRO LEU TRP LEU MET TYR LEU ALA SEQRES 22 A 329 ILE VAL LEU ALA HIS THR ASN SER VAL VAL ASN PRO PHE SEQRES 23 A 329 ILE TYR ALA TYR ARG ILE ARG GLU PHE ARG GLN THR PHE SEQRES 24 A 329 ARG LYS ILE ILE ARG SER HIS VAL LEU ARG GLN GLN GLU SEQRES 25 A 329 PRO PHE LYS ALA ALA ALA ALA HIS HIS HIS HIS HIS HIS SEQRES 26 A 329 HIS HIS HIS HIS HET T4G A 330 21 HETNAM T4G 6-(2,6-DIMETHYLPYRIDIN-4-YL)-5-PHENYL-1,2,4-TRIAZIN-3- HETNAM 2 T4G AMINE FORMUL 2 T4G C16 H15 N5 HELIX 1 1 SER A 7 ASN A 34 1 28 HELIX 2 2 THR A 41 LEU A 58 1 18 HELIX 3 3 LEU A 58 GLY A 69 1 12 HELIX 4 4 ALA A 73 ILE A 108 1 36 HELIX 5 5 ILE A 108 VAL A 116 1 9 HELIX 6 6 THR A 117 LEU A 137 1 21 HELIX 7 7 THR A 138 GLY A 142 5 5 HELIX 8 8 LEU A 167 VAL A 172 1 6 HELIX 9 9 PRO A 173 TYR A 179 1 7 HELIX 10 10 VAL A 186 MET A 211 1 26 HELIX 11 11 GLU A 212 GLN A 214 5 3 HELIX 12 12 GLY A 218 CYS A 259 1 42 HELIX 13 13 PRO A 266 ILE A 292 1 27 HELIX 14 14 ILE A 292 SER A 305 1 14 SHEET 1 A 2 PHE A 70 ALA A 72 0 SHEET 2 A 2 VAL A 164 CYS A 166 -1 O CYS A 166 N PHE A 70 SSBOND 1 CYS A 71 CYS A 159 1555 1555 2.03 SSBOND 2 CYS A 74 CYS A 146 1555 1555 2.03 SSBOND 3 CYS A 77 CYS A 166 1555 1555 2.03 SSBOND 4 CYS A 259 CYS A 262 1555 1555 2.03 SITE 1 AC1 6 PHE A 168 MET A 177 LEU A 249 HIS A 250 SITE 2 AC1 6 ASN A 253 ILE A 274 CRYST1 111.814 111.896 125.841 90.00 90.00 90.00 I 2 2 2 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 0.008943 0.000000 0.000000 0.00000 SCALE2 0.000000 0.008937 0.000000 0.00000 SCALE3 0.000000 0.000000 0.007947 0.00000 ATOM 1 N SER A 7 49.301 21.838 50.629 1.00169.86 N ANISOU 1 N SER A 7 15601 20792 28145 -464 -4587 -5521 N ATOM 2 CA SER A 7 48.035 21.114 50.581 1.00173.12 C ANISOU 2 CA SER A 7 16240 20787 28750 -445 -4791 -4843 C ATOM 3 C SER A 7 46.846 22.064 50.487 1.00168.45 C ANISOU 3 C SER A 7 15802 20115 28087 -724 -3978 -4481 C ATOM 4 O SER A 7 45.742 21.731 50.916 1.00165.42 O ANISOU 4 O SER A 7 15654 19491 27708 -851 -3998 -3870 O ATOM 5 CB SER A 7 47.882 20.213 51.809 1.00177.90 C ANISOU 5 CB SER A 7 17086 21295 29213 -491 -5376 -4420 C ATOM 6 OG SER A 7 48.881 19.208 51.840 1.00180.47 O ANISOU 6 OG SER A 7 17300 21651 29619 -173 -6176 -4692 O ATOM 7 N VAL A 8 47.074 23.246 49.925 1.00164.96 N ANISOU 7 N VAL A 8 15234 19875 27567 -813 -3254 -4861 N ATOM 8 CA VAL A 8 46.009 24.233 49.774 1.00157.72 C ANISOU 8 CA VAL A 8 14464 18905 26555 -1038 -2430 -4561 C ATOM 9 C VAL A 8 45.407 24.177 48.376 1.00160.03 C ANISOU 9 C VAL A 8 14647 18975 27184 -808 -2280 -4521 C ATOM 10 O VAL A 8 44.183 24.206 48.217 1.00161.66 O ANISOU 10 O VAL A 8 14994 18978 27451 -868 -2035 -4014 O ATOM 11 CB VAL A 8 46.504 25.660 50.056 1.00149.22 C ANISOU 11 CB VAL A 8 13385 18166 25146 -1298 -1623 -4955 C ATOM 12 CG1 VAL A 8 45.388 26.664 49.812 1.00141.13 C ANISOU 12 CG1 VAL A 8 12532 17065 24026 -1476 -760 -4639 C ATOM 13 CG2 VAL A 8 47.018 25.764 51.485 1.00152.00 C ANISOU 13 CG2 VAL A 8 13853 18759 25140 -1553 -1734 -4971 C ATOM 14 N TYR A 9 46.268 24.105 47.364 1.00161.96 N ANISOU 14 N TYR A 9 14628 19275 27634 -543 -2422 -5062 N ATOM 15 CA TYR A 9 45.807 23.927 45.994 1.00165.22 C ANISOU 15 CA TYR A 9 14915 19477 28384 -281 -2378 -5063 C ATOM 16 C TYR A 9 44.939 22.680 45.945 1.00168.47 C ANISOU 16 C TYR A 9 15416 19547 29049 -157 -3009 -4517 C ATOM 17 O TYR A 9 43.915 22.645 45.265 1.00167.97 O ANISOU 17 O TYR A 9 15380 19286 29155 -102 -2816 -4193 O ATOM 18 CB TYR A 9 46.987 23.760 45.038 1.00175.01 C ANISOU 18 CB TYR A 9 15859 20811 29825 12 -2634 -5720 C ATOM 19 CG TYR A 9 48.075 24.805 45.179 1.00188.33 C ANISOU 19 CG TYR A 9 17432 22861 31263 -118 -2156 -6338 C ATOM 20 CD1 TYR A 9 47.898 26.091 44.681 1.00190.62 C ANISOU 20 CD1 TYR A 9 17741 23258 31426 -240 -1254 -6533 C ATOM 21 CD2 TYR A 9 49.288 24.499 45.786 1.00189.15 C ANISOU 21 CD2 TYR A 9 17411 23209 31248 -110 -2600 -6743 C ATOM 22 CE1 TYR A 9 48.889 27.050 44.797 1.00190.76 C ANISOU 22 CE1 TYR A 9 17672 23595 31212 -389 -788 -7115 C ATOM 23 CE2 TYR A 9 50.286 25.448 45.906 1.00186.23 C ANISOU 23 CE2 TYR A 9 16917 23196 30646 -255 -2158 -7335 C ATOM 24 CZ TYR A 9 50.081 26.723 45.410 1.00186.63 C ANISOU 24 CZ TYR A 9 17003 23326 30581 -411 -1245 -7522 C ATOM 25 OH TYR A 9 51.073 27.671 45.529 1.00184.02 O ANISOU 25 OH TYR A 9 16567 23339 30012 -587 -779 -8125 O ATOM 26 N ILE A 10 45.359 21.659 46.685 1.00172.13 N ANISOU 26 N ILE A 10 15932 19951 29520 -116 -3754 -4426 N ATOM 27 CA ILE A 10 44.616 20.411 46.777 1.00172.85 C ANISOU 27 CA ILE A 10 16151 19703 29821 -29 -4385 -3917 C ATOM 28 C ILE A 10 43.253 20.642 47.419 1.00166.99 C ANISOU 28 C ILE A 10 15664 18843 28940 -322 -4025 -3264 C ATOM 29 O ILE A 10 42.238 20.144 46.938 1.00165.36 O ANISOU 29 O ILE A 10 15506 18381 28942 -281 -4116 -2864 O ATOM 30 CB ILE A 10 45.391 19.360 47.595 1.00180.60 C ANISOU 30 CB ILE A 10 17192 20661 30769 64 -5198 -3949 C ATOM 31 CG1 ILE A 10 46.798 19.174 47.020 1.00182.23 C ANISOU 31 CG1 ILE A 10 17126 21036 31076 360 -5544 -4620 C ATOM 32 CG2 ILE A 10 44.635 18.040 47.625 1.00182.68 C ANISOU 32 CG2 ILE A 10 17620 20533 31257 156 -5836 -3439 C ATOM 33 CD1 ILE A 10 47.658 18.207 47.805 1.00186.20 C ANISOU 33 CD1 ILE A 10 17670 21570 31509 498 -6322 -4703 C ATOM 34 N THR A 11 43.239 21.405 48.507 1.00165.43 N ANISOU 34 N THR A 11 15623 18851 28381 -623 -3611 -3169 N ATOM 35 CA THR A 11 42.000 21.701 49.219 1.00162.16 C ANISOU 35 CA THR A 11 15458 18361 27794 -915 -3235 -2562 C ATOM 36 C THR A 11 41.033 22.496 48.345 1.00154.12 C ANISOU 36 C THR A 11 14400 17321 26838 -930 -2536 -2419 C ATOM 37 O THR A 11 39.854 22.157 48.245 1.00148.36 O ANISOU 37 O THR A 11 13767 16398 26205 -982 -2523 -1908 O ATOM 38 CB THR A 11 42.267 22.481 50.521 1.00163.46 C ANISOU 38 CB THR A 11 15790 18779 27539 -1230 -2869 -2550 C ATOM 39 OG1 THR A 11 43.086 21.692 51.393 1.00169.83 O ANISOU 39 OG1 THR A 11 16646 19617 28265 -1201 -3542 -2634 O ATOM 40 CG2 THR A 11 40.961 22.810 51.225 1.00160.58 C ANISOU 40 CG2 THR A 11 15682 18335 26996 -1522 -2456 -1917 C ATOM 41 N VAL A 12 41.537 23.552 47.715 1.00148.37 N ANISOU 41 N VAL A 12 13532 16800 26040 -880 -1949 -2878 N ATOM 42 CA VAL A 12 40.715 24.395 46.855 1.00136.46 C ANISOU 42 CA VAL A 12 11997 15296 24557 -852 -1239 -2791 C ATOM 43 C VAL A 12 40.173 23.617 45.661 1.00131.56 C ANISOU 43 C VAL A 12 11225 14439 24322 -567 -1578 -2681 C ATOM 44 O VAL A 12 38.993 23.716 45.331 1.00127.81 O ANISOU 44 O VAL A 12 10800 13871 23891 -588 -1298 -2268 O ATOM 45 CB VAL A 12 41.500 25.619 46.350 1.00130.26 C ANISOU 45 CB VAL A 12 11107 14755 23631 -825 -576 -3365 C ATOM 46 CG1 VAL A 12 40.664 26.420 45.364 1.00124.71 C ANISOU 46 CG1 VAL A 12 10388 14032 22962 -730 126 -3279 C ATOM 47 CG2 VAL A 12 41.934 26.489 47.516 1.00131.32 C ANISOU 47 CG2 VAL A 12 11404 15133 23359 -1146 -150 -3465 C ATOM 48 N GLU A 13 41.041 22.847 45.015 1.00135.99 N ANISOU 48 N GLU A 13 11596 14922 25152 -298 -2178 -3060 N ATOM 49 CA GLU A 13 40.636 22.027 43.877 1.00136.34 C ANISOU 49 CA GLU A 13 11493 14735 25573 -22 -2564 -2998 C ATOM 50 C GLU A 13 39.521 21.056 44.257 1.00132.35 C ANISOU 50 C GLU A 13 11134 13980 25174 -119 -2973 -2368 C ATOM 51 O GLU A 13 38.585 20.837 43.486 1.00134.54 O ANISOU 51 O GLU A 13 11356 14126 25637 -33 -2912 -2116 O ATOM 52 CB GLU A 13 41.834 21.264 43.307 1.00141.56 C ANISOU 52 CB GLU A 13 11959 15348 26480 268 -3214 -3495 C ATOM 53 CG GLU A 13 42.776 22.124 42.485 1.00141.16 C ANISOU 53 CG GLU A 13 11703 15503 26429 430 -2811 -4134 C ATOM 54 CD GLU A 13 42.127 22.647 41.221 1.00144.54 C ANISOU 54 CD GLU A 13 12022 15889 27007 596 -2318 -4154 C ATOM 55 OE1 GLU A 13 41.319 21.910 40.620 1.00152.17 O ANISOU 55 OE1 GLU A 13 12957 16634 28225 728 -2615 -3845 O ATOM 56 OE2 GLU A 13 42.430 23.789 40.821 1.00140.76 O ANISOU 56 OE2 GLU A 13 11495 15600 26388 597 -1631 -4488 O ATOM 57 N LEU A 14 39.625 20.482 45.451 1.00129.71 N ANISOU 57 N LEU A 14 10987 13590 24707 -304 -3380 -2123 N ATOM 58 CA LEU A 14 38.602 19.573 45.956 1.00133.27 C ANISOU 58 CA LEU A 14 11616 13798 25222 -443 -3748 -1521 C ATOM 59 C LEU A 14 37.286 20.311 46.196 1.00128.93 C ANISOU 59 C LEU A 14 11180 13312 24496 -684 -3083 -1047 C ATOM 60 O LEU A 14 36.222 19.842 45.797 1.00118.52 O ANISOU 60 O LEU A 14 9862 11837 23335 -692 -3151 -664 O ATOM 61 CB LEU A 14 39.077 18.883 47.240 1.00135.98 C ANISOU 61 CB LEU A 14 12163 14082 25421 -579 -4281 -1385 C ATOM 62 CG LEU A 14 39.786 17.530 47.106 1.00137.28 C ANISOU 62 CG LEU A 14 12312 14022 25826 -345 -5188 -1524 C ATOM 63 CD1 LEU A 14 40.888 17.566 46.057 1.00137.50 C ANISOU 63 CD1 LEU A 14 12066 14131 26048 -8 -5340 -2156 C ATOM 64 CD2 LEU A 14 40.336 17.073 48.452 1.00137.42 C ANISOU 64 CD2 LEU A 14 12545 14047 25622 -463 -5598 -1427 C ATOM 65 N ALA A 15 37.367 21.468 46.846 1.00129.80 N ANISOU 65 N ALA A 15 11383 13667 24270 -879 -2434 -1086 N ATOM 66 CA ALA A 15 36.194 22.302 47.076 1.00125.66 C ANISOU 66 CA ALA A 15 10971 13236 23539 -1083 -1731 -674 C ATOM 67 C ALA A 15 35.452 22.554 45.767 1.00127.15 C ANISOU 67 C ALA A 15 10982 13412 23918 -880 -1406 -656 C ATOM 68 O ALA A 15 34.226 22.474 45.713 1.00138.50 O ANISOU 68 O ALA A 15 12461 14803 25359 -966 -1237 -187 O ATOM 69 CB ALA A 15 36.598 23.617 47.722 1.00112.08 C ANISOU 69 CB ALA A 15 9353 11787 21446 -1259 -1030 -858 C ATOM 70 N ILE A 16 36.204 22.862 44.715 1.00125.50 N ANISOU 70 N ILE A 16 10568 13261 23854 -606 -1317 -1175 N ATOM 71 CA ILE A 16 35.622 23.090 43.396 1.00131.81 C ANISOU 71 CA ILE A 16 11188 14057 24837 -367 -1035 -1216 C ATOM 72 C ILE A 16 34.933 21.831 42.877 1.00139.29 C ANISOU 72 C ILE A 16 12049 14763 26112 -269 -1663 -928 C ATOM 73 O ILE A 16 33.796 21.882 42.407 1.00144.19 O ANISOU 73 O ILE A 16 12626 15384 26774 -258 -1425 -595 O ATOM 74 CB ILE A 16 36.689 23.538 42.378 1.00139.27 C ANISOU 74 CB ILE A 16 11937 15083 25897 -82 -905 -1863 C ATOM 75 CG1 ILE A 16 37.321 24.862 42.809 1.00136.93 C ANISOU 75 CG1 ILE A 16 11731 15031 25267 -202 -201 -2172 C ATOM 76 CG2 ILE A 16 36.084 23.668 40.990 1.00102.09 C ANISOU 76 CG2 ILE A 16 7046 10352 21391 194 -677 -1895 C ATOM 77 CD1 ILE A 16 38.389 25.368 41.859 1.00136.22 C ANISOU 77 CD1 ILE A 16 11464 15031 25263 41 -17 -2825 C ATOM 78 N ALA A 17 35.628 20.703 42.974 1.00140.17 N ANISOU 78 N ALA A 17 12142 14679 26437 -198 -2458 -1063 N ATOM 79 CA ALA A 17 35.104 19.423 42.508 1.00142.91 C ANISOU 79 CA ALA A 17 12438 14763 27100 -115 -3105 -833 C ATOM 80 C ALA A 17 33.704 19.146 43.048 1.00142.23 C ANISOU 80 C ALA A 17 12490 14613 26939 -378 -3030 -191 C ATOM 81 O ALA A 17 32.805 18.768 42.297 1.00139.25 O ANISOU 81 O ALA A 17 12000 14164 26742 -315 -3071 17 O ATOM 82 CB ALA A 17 36.053 18.295 42.887 1.00145.80 C ANISOU 82 CB ALA A 17 12859 14923 27615 -54 -3935 -1000 C ATOM 83 N VAL A 18 33.530 19.329 44.353 1.00143.09 N ANISOU 83 N VAL A 18 12831 14761 26774 -676 -2923 110 N ATOM 84 CA VAL A 18 32.240 19.115 44.998 1.00142.27 C ANISOU 84 CA VAL A 18 12875 14614 26566 -956 -2824 721 C ATOM 85 C VAL A 18 31.146 19.968 44.358 1.00138.11 C ANISOU 85 C VAL A 18 12230 14285 25962 -937 -2127 912 C ATOM 86 O VAL A 18 30.083 19.460 43.999 1.00135.43 O ANISOU 86 O VAL A 18 11830 13881 25748 -981 -2221 1256 O ATOM 87 CB VAL A 18 32.311 19.420 46.506 1.00142.87 C ANISOU 87 CB VAL A 18 13222 14750 26313 -1266 -2694 965 C ATOM 88 CG1 VAL A 18 30.937 19.294 47.139 1.00146.75 C ANISOU 88 CG1 VAL A 18 13857 15218 26682 -1557 -2522 1595 C ATOM 89 CG2 VAL A 18 33.306 18.493 47.189 1.00142.18 C ANISOU 89 CG2 VAL A 18 13266 14476 26282 -1268 -3418 825 C ATOM 90 N LEU A 19 31.418 21.261 44.210 1.00133.25 N ANISOU 90 N LEU A 19 11585 13918 25128 -867 -1423 678 N ATOM 91 CA LEU A 19 30.446 22.191 43.642 1.00134.95 C ANISOU 91 CA LEU A 19 11718 14343 25216 -809 -695 843 C ATOM 92 C LEU A 19 30.098 21.851 42.195 1.00133.32 C ANISOU 92 C LEU A 19 11245 14106 25304 -509 -808 712 C ATOM 93 O LEU A 19 28.925 21.822 41.824 1.00131.88 O ANISOU 93 O LEU A 19 10982 13995 25132 -517 -619 1054 O ATOM 94 CB LEU A 19 30.949 23.634 43.745 1.00137.70 C ANISOU 94 CB LEU A 19 12126 14927 25267 -772 79 565 C ATOM 95 CG LEU A 19 30.794 24.359 45.088 1.00140.87 C ANISOU 95 CG LEU A 19 12791 15451 25283 -1088 512 819 C ATOM 96 CD1 LEU A 19 31.468 23.603 46.221 1.00141.28 C ANISOU 96 CD1 LEU A 19 13003 15356 25323 -1308 -89 848 C ATOM 97 CD2 LEU A 19 31.340 25.780 44.990 1.00137.96 C ANISOU 97 CD2 LEU A 19 12475 15296 24646 -1024 1294 477 C ATOM 98 N ALA A 20 31.119 21.592 41.385 1.00133.30 N ANISOU 98 N ALA A 20 11098 14017 25532 -242 -1118 209 N ATOM 99 CA ALA A 20 30.911 21.214 39.991 1.00132.26 C ANISOU 99 CA ALA A 20 10716 13841 25695 59 -1278 40 C ATOM 100 C ALA A 20 29.973 20.016 39.880 1.00130.19 C ANISOU 100 C ALA A 20 10408 13407 25651 -39 -1819 431 C ATOM 101 O ALA A 20 29.076 19.990 39.036 1.00133.26 O ANISOU 101 O ALA A 20 10626 13872 26133 75 -1670 571 O ATOM 102 CB ALA A 20 32.239 20.915 39.317 1.00133.70 C ANISOU 102 CB ALA A 20 10780 13913 26105 321 -1662 -540 C ATOM 103 N ILE A 21 30.188 19.022 40.735 1.00127.76 N ANISOU 103 N ILE A 21 10260 12871 25413 -252 -2439 599 N ATOM 104 CA ILE A 21 29.341 17.838 40.748 1.00134.02 C ANISOU 104 CA ILE A 21 11059 13465 26397 -396 -2959 972 C ATOM 105 C ILE A 21 27.927 18.189 41.206 1.00137.89 C ANISOU 105 C ILE A 21 11593 14119 26680 -649 -2519 1512 C ATOM 106 O ILE A 21 26.957 17.958 40.485 1.00140.97 O ANISOU 106 O ILE A 21 11813 14570 27180 -611 -2471 1694 O ATOM 107 CB ILE A 21 29.926 16.734 41.649 1.00138.39 C ANISOU 107 CB ILE A 21 11830 13721 27033 -562 -3686 1040 C ATOM 108 CG1 ILE A 21 31.303 16.301 41.137 1.00134.96 C ANISOU 108 CG1 ILE A 21 11329 13138 26811 -279 -4166 506 C ATOM 109 CG2 ILE A 21 28.987 15.541 41.702 1.00115.30 C ANISOU 109 CG2 ILE A 21 8954 10573 24283 -749 -4164 1445 C ATOM 110 CD1 ILE A 21 31.966 15.228 41.984 1.00129.92 C ANISOU 110 CD1 ILE A 21 10911 12219 26233 -379 -4884 541 C ATOM 111 N LEU A 22 27.818 18.759 42.402 1.00139.48 N ANISOU 111 N LEU A 22 12012 14414 26571 -903 -2192 1756 N ATOM 112 CA LEU A 22 26.521 19.132 42.962 1.00135.26 C ANISOU 112 CA LEU A 22 11539 14046 25808 -1154 -1758 2276 C ATOM 113 C LEU A 22 25.723 20.032 42.020 1.00126.94 C ANISOU 113 C LEU A 22 10266 13291 24674 -956 -1104 2292 C ATOM 114 O LEU A 22 24.558 19.761 41.725 1.00128.58 O ANISOU 114 O LEU A 22 10356 13587 24911 -1024 -1053 2624 O ATOM 115 CB LEU A 22 26.697 19.826 44.315 1.00129.36 C ANISOU 115 CB LEU A 22 11057 13382 24711 -1403 -1410 2451 C ATOM 116 CG LEU A 22 27.251 18.976 45.459 1.00125.40 C ANISOU 116 CG LEU A 22 10808 12624 24214 -1641 -1996 2556 C ATOM 117 CD1 LEU A 22 27.401 19.810 46.719 1.00117.94 C ANISOU 117 CD1 LEU A 22 10102 11812 22898 -1865 -1570 2704 C ATOM 118 CD2 LEU A 22 26.349 17.778 45.710 1.00127.33 C ANISOU 118 CD2 LEU A 22 11111 12660 24609 -1867 -2490 2989 C ATOM 119 N GLY A 23 26.357 21.103 41.554 1.00121.04 N ANISOU 119 N GLY A 23 9470 12709 23812 -707 -598 1925 N ATOM 120 CA GLY A 23 25.697 22.082 40.710 1.00120.21 C ANISOU 120 CA GLY A 23 9204 12890 23580 -480 90 1919 C ATOM 121 C GLY A 23 25.078 21.514 39.446 1.00124.72 C ANISOU 121 C GLY A 23 9489 13482 24417 -259 -127 1897 C ATOM 122 O GLY A 23 23.859 21.557 39.274 1.00127.03 O ANISOU 122 O GLY A 23 9675 13955 24634 -306 101 2256 O ATOM 123 N ASN A 24 25.914 20.989 38.555 1.00131.05 N ANISOU 123 N ASN A 24 10155 14118 25521 -14 -561 1469 N ATOM 124 CA ASN A 24 25.428 20.454 37.288 1.00133.14 C ANISOU 124 CA ASN A 24 10144 14395 26046 217 -781 1395 C ATOM 125 C ASN A 24 24.538 19.221 37.453 1.00134.95 C ANISOU 125 C ASN A 24 10327 14495 26452 -30 -1337 1768 C ATOM 126 O ASN A 24 23.592 19.033 36.689 1.00135.38 O ANISOU 126 O ASN A 24 10164 14695 26580 49 -1285 1909 O ATOM 127 CB ASN A 24 26.590 20.151 36.340 1.00135.07 C ANISOU 127 CB ASN A 24 10273 14473 26574 528 -1136 840 C ATOM 128 CG ASN A 24 27.424 21.381 36.019 1.00135.34 C ANISOU 128 CG ASN A 24 10328 14649 26446 779 -549 438 C ATOM 129 OD1 ASN A 24 27.008 22.248 35.249 1.00138.36 O ANISOU 129 OD1 ASN A 24 10594 15263 26712 1025 40 377 O ATOM 130 ND2 ASN A 24 28.612 21.456 36.605 1.00131.07 N ANISOU 130 ND2 ASN A 24 9940 13976 25886 721 -701 152 N ATOM 131 N VAL A 25 24.840 18.383 38.442 1.00133.27 N ANISOU 131 N VAL A 25 10324 14017 26296 -329 -1860 1919 N ATOM 132 CA VAL A 25 23.985 17.236 38.733 1.00132.03 C ANISOU 132 CA VAL A 25 10181 13712 26273 -614 -2345 2297 C ATOM 133 C VAL A 25 22.591 17.731 39.096 1.00133.69 C ANISOU 133 C VAL A 25 10351 14217 26229 -812 -1834 2775 C ATOM 134 O VAL A 25 21.583 17.174 38.659 1.00140.85 O ANISOU 134 O VAL A 25 11089 15193 27235 -894 -1963 3002 O ATOM 135 CB VAL A 25 24.533 16.372 39.886 1.00135.18 C ANISOU 135 CB VAL A 25 10874 13779 26710 -904 -2908 2416 C ATOM 136 CG1 VAL A 25 23.401 15.598 40.550 1.00134.78 C ANISOU 136 CG1 VAL A 25 10913 13657 26638 -1290 -3116 2936 C ATOM 137 CG2 VAL A 25 25.617 15.428 39.384 1.00142.62 C ANISOU 137 CG2 VAL A 25 11818 14396 27977 -727 -3607 2025 C ATOM 138 N LEU A 26 22.546 18.788 39.899 1.00129.85 N ANISOU 138 N LEU A 26 10017 13917 25404 -890 -1244 2917 N ATOM 139 CA LEU A 26 21.291 19.428 40.262 1.00125.05 C ANISOU 139 CA LEU A 26 9379 13623 24510 -1033 -673 3352 C ATOM 140 C LEU A 26 20.584 19.943 39.015 1.00124.10 C ANISOU 140 C LEU A 26 8947 13818 24387 -717 -272 3283 C ATOM 141 O LEU A 26 19.383 19.737 38.845 1.00133.27 O ANISOU 141 O LEU A 26 9949 15180 25508 -816 -186 3609 O ATOM 142 CB LEU A 26 21.548 20.576 41.234 1.00118.61 C ANISOU 142 CB LEU A 26 8797 12940 23330 -1110 -75 3436 C ATOM 143 CG LEU A 26 20.325 21.306 41.782 1.00119.82 C ANISOU 143 CG LEU A 26 8974 13408 23145 -1265 546 3903 C ATOM 144 CD1 LEU A 26 19.420 20.337 42.514 1.00129.31 C ANISOU 144 CD1 LEU A 26 10224 14523 24386 -1664 164 4368 C ATOM 145 CD2 LEU A 26 20.749 22.444 42.698 1.00109.34 C ANISOU 145 CD2 LEU A 26 7904 12170 21469 -1320 1122 3920 C ATOM 146 N VAL A 27 21.343 20.598 38.141 1.00114.39 N ANISOU 146 N VAL A 27 7629 12642 23194 -332 -32 2846 N ATOM 147 CA VAL A 27 20.809 21.113 36.886 1.00119.73 C ANISOU 147 CA VAL A 27 8025 13602 23866 29 346 2728 C ATOM 148 C VAL A 27 20.216 20.002 36.023 1.00126.45 C ANISOU 148 C VAL A 27 8608 14415 25022 45 -191 2752 C ATOM 149 O VAL A 27 19.183 20.187 35.381 1.00130.49 O ANISOU 149 O VAL A 27 8882 15232 25465 161 75 2913 O ATOM 150 CB VAL A 27 21.891 21.863 36.081 1.00125.03 C ANISOU 150 CB VAL A 27 8676 14262 24567 431 606 2206 C ATOM 151 CG1 VAL A 27 21.371 22.228 34.697 1.00123.61 C ANISOU 151 CG1 VAL A 27 8208 14337 24422 830 901 2068 C ATOM 152 CG2 VAL A 27 22.348 23.109 36.831 1.00131.92 C ANISOU 152 CG2 VAL A 27 9798 15229 25096 422 1261 2176 C ATOM 153 N CYS A 28 20.883 18.852 36.006 1.00128.37 N ANISOU 153 N CYS A 28 8895 14291 25588 -64 -942 2583 N ATOM 154 CA CYS A 28 20.402 17.692 35.264 1.00135.38 C ANISOU 154 CA CYS A 28 9575 15084 26779 -97 -1506 2592 C ATOM 155 C CYS A 28 19.115 17.165 35.879 1.00143.31 C ANISOU 155 C CYS A 28 10561 16193 27699 -486 -1572 3101 C ATOM 156 O CYS A 28 18.159 16.835 35.174 1.00143.89 O ANISOU 156 O CYS A 28 10369 16466 27835 -470 -1598 3213 O ATOM 157 CB CYS A 28 21.451 16.577 35.265 1.00134.63 C ANISOU 157 CB CYS A 28 9599 14537 27018 -146 -2285 2322 C ATOM 158 SG CYS A 28 22.997 16.972 34.425 1.00153.22 S ANISOU 158 SG CYS A 28 11929 16756 29533 303 -2331 1681 S ATOM 159 N TRP A 29 19.108 17.077 37.205 1.00149.86 N ANISOU 159 N TRP A 29 11671 16892 28378 -842 -1603 3396 N ATOM 160 CA TRP A 29 17.961 16.567 37.939 1.00157.91 C ANISOU 160 CA TRP A 29 12718 17976 29305 -1254 -1667 3887 C ATOM 161 C TRP A 29 16.752 17.469 37.713 1.00154.18 C ANISOU 161 C TRP A 29 12029 18005 28546 -1182 -985 4152 C ATOM 162 O TRP A 29 15.667 16.994 37.380 1.00154.94 O ANISOU 162 O TRP A 29 11906 18289 28675 -1314 -1057 4373 O ATOM 163 CB TRP A 29 18.292 16.466 39.431 1.00167.06 C ANISOU 163 CB TRP A 29 14245 18909 30320 -1602 -1757 4131 C ATOM 164 CG TRP A 29 17.252 15.756 40.242 1.00177.40 C ANISOU 164 CG TRP A 29 15632 20195 31577 -2060 -1928 4613 C ATOM 165 CD1 TRP A 29 16.077 15.233 39.789 1.00178.72 C ANISOU 165 CD1 TRP A 29 15563 20539 31804 -2207 -1994 4833 C ATOM 166 CD2 TRP A 29 17.293 15.488 41.652 1.00186.04 C ANISOU 166 CD2 TRP A 29 17063 21086 32539 -2440 -2049 4925 C ATOM 167 NE1 TRP A 29 15.382 14.661 40.827 1.00183.85 N ANISOU 167 NE1 TRP A 29 16384 21101 32371 -2670 -2134 5260 N ATOM 168 CE2 TRP A 29 16.106 14.803 41.981 1.00188.86 C ANISOU 168 CE2 TRP A 29 17380 21492 32888 -2812 -2171 5333 C ATOM 169 CE3 TRP A 29 18.216 15.763 42.666 1.00189.25 C ANISOU 169 CE3 TRP A 29 17795 21288 32823 -2504 -2061 4892 C ATOM 170 CZ2 TRP A 29 15.818 14.389 43.281 1.00195.00 C ANISOU 170 CZ2 TRP A 29 18452 22097 33544 -3236 -2296 5715 C ATOM 171 CZ3 TRP A 29 17.927 15.350 43.958 1.00194.30 C ANISOU 171 CZ3 TRP A 29 18719 21768 33337 -2910 -2198 5274 C ATOM 172 CH2 TRP A 29 16.739 14.671 44.253 1.00197.51 C ANISOU 172 CH2 TRP A 29 19098 22204 33744 -3267 -2310 5686 C ATOM 173 N ALA A 30 16.951 18.773 37.881 1.00148.20 N ANISOU 173 N ALA A 30 11337 17474 27499 -965 -316 4115 N ATOM 174 CA ALA A 30 15.888 19.749 37.679 1.00145.15 C ANISOU 174 CA ALA A 30 10781 17570 26800 -832 391 4353 C ATOM 175 C ALA A 30 15.234 19.593 36.311 1.00143.57 C ANISOU 175 C ALA A 30 10192 17639 26719 -549 392 4231 C ATOM 176 O ALA A 30 14.014 19.687 36.182 1.00145.74 O ANISOU 176 O ALA A 30 10255 18278 26842 -603 640 4530 O ATOM 177 CB ALA A 30 16.432 21.158 37.850 1.00139.24 C ANISOU 177 CB ALA A 30 10187 16958 25761 -564 1085 4221 C ATOM 178 N VAL A 31 16.054 19.365 35.292 1.00142.79 N ANISOU 178 N VAL A 31 9991 17381 26884 -239 119 3784 N ATOM 179 CA VAL A 31 15.559 19.151 33.938 1.00145.42 C ANISOU 179 CA VAL A 31 9960 17935 27357 50 60 3619 C ATOM 180 C VAL A 31 14.745 17.864 33.853 1.00153.57 C ANISOU 180 C VAL A 31 10822 18927 28601 -283 -509 3815 C ATOM 181 O VAL A 31 13.712 17.816 33.184 1.00161.80 O ANISOU 181 O VAL A 31 11548 20331 29597 -213 -382 3928 O ATOM 182 CB VAL A 31 16.714 19.077 32.922 1.00152.93 C ANISOU 182 CB VAL A 31 10870 18664 28573 423 -178 3084 C ATOM 183 CG1 VAL A 31 16.213 18.586 31.572 1.00152.25 C ANISOU 183 CG1 VAL A 31 10417 18744 28685 657 -389 2921 C ATOM 184 CG2 VAL A 31 17.394 20.436 32.792 1.00152.80 C ANISOU 184 CG2 VAL A 31 10973 18755 28328 788 474 2859 C ATOM 185 N TRP A 32 15.212 16.824 34.537 1.00157.32 N ANISOU 185 N TRP A 32 11515 18967 29294 -645 -1125 3851 N ATOM 186 CA TRP A 32 14.541 15.528 34.509 1.00163.64 C ANISOU 186 CA TRP A 32 12216 19651 30308 -1000 -1691 4016 C ATOM 187 C TRP A 32 13.177 15.591 35.183 1.00162.55 C ANISOU 187 C TRP A 32 12002 19838 29921 -1343 -1411 4508 C ATOM 188 O TRP A 32 12.225 14.955 34.732 1.00171.04 O ANISOU 188 O TRP A 32 12819 21096 31071 -1499 -1587 4628 O ATOM 189 CB TRP A 32 15.406 14.452 35.168 1.00170.85 C ANISOU 189 CB TRP A 32 13443 19995 31475 -1287 -2374 3954 C ATOM 190 CG TRP A 32 14.964 13.055 34.841 1.00174.00 C ANISOU 190 CG TRP A 32 13759 20194 32159 -1564 -3009 3991 C ATOM 191 CD1 TRP A 32 14.711 12.550 33.600 1.00171.41 C ANISOU 191 CD1 TRP A 32 13130 19947 32052 -1395 -3248 3761 C ATOM 192 CD2 TRP A 32 14.744 11.980 35.764 1.00178.51 C ANISOU 192 CD2 TRP A 32 14575 20435 32817 -2061 -3474 4263 C ATOM 193 NE1 TRP A 32 14.339 11.230 33.691 1.00173.75 N ANISOU 193 NE1 TRP A 32 13466 19983 32567 -1774 -3826 3867 N ATOM 194 CE2 TRP A 32 14.352 10.856 35.009 1.00179.79 C ANISOU 194 CE2 TRP A 32 14574 20483 33253 -2185 -3968 4177 C ATOM 195 CE3 TRP A 32 14.837 11.858 37.154 1.00181.64 C ANISOU 195 CE3 TRP A 32 15324 20614 33076 -2414 -3511 4569 C ATOM 196 CZ2 TRP A 32 14.054 9.627 35.596 1.00185.95 C ANISOU 196 CZ2 TRP A 32 15554 20925 34172 -2655 -4477 4386 C ATOM 197 CZ3 TRP A 32 14.540 10.637 37.736 1.00187.31 C ANISOU 197 CZ3 TRP A 32 16236 21002 33931 -2860 -4023 4784 C ATOM 198 CH2 TRP A 32 14.153 9.539 36.958 1.00189.23 C ANISOU 198 CH2 TRP A 32 16330 21122 34445 -2980 -4491 4691 C ATOM 199 N LEU A 33 13.090 16.352 36.270 1.00154.32 N ANISOU 199 N LEU A 33 11182 18874 28578 -1471 -977 4784 N ATOM 200 CA LEU A 33 11.829 16.530 36.979 1.00150.36 C ANISOU 200 CA LEU A 33 10623 18699 27806 -1777 -651 5260 C ATOM 201 C LEU A 33 10.900 17.482 36.228 1.00144.06 C ANISOU 201 C LEU A 33 9481 18504 26754 -1449 -22 5321 C ATOM 202 O LEU A 33 9.816 17.097 35.793 1.00144.09 O ANISOU 202 O LEU A 33 9174 18824 26748 -1550 -53 5474 O ATOM 203 CB LEU A 33 12.074 17.051 38.397 1.00144.74 C ANISOU 203 CB LEU A 33 10279 17867 26848 -2006 -386 5530 C ATOM 204 CG LEU A 33 12.906 16.172 39.334 1.00137.47 C ANISOU 204 CG LEU A 33 9731 16393 26111 -2343 -959 5537 C ATOM 205 CD1 LEU A 33 12.927 16.770 40.729 1.00134.95 C ANISOU 205 CD1 LEU A 33 9729 16052 25494 -2572 -621 5851 C ATOM 206 CD2 LEU A 33 12.372 14.746 39.371 1.00136.77 C ANISOU 206 CD2 LEU A 33 9608 16091 26267 -2742 -1582 5678 C ATOM 207 N ASN A 34 11.334 18.728 36.077 1.00138.12 N ANISOU 207 N ASN A 34 9443 13267 29769 623 809 3228 N ATOM 208 CA ASN A 34 10.505 19.752 35.458 1.00134.10 C ANISOU 208 CA ASN A 34 8977 12684 29291 343 617 3549 C ATOM 209 C ASN A 34 10.455 19.622 33.941 1.00131.60 C ANISOU 209 C ASN A 34 9012 12613 28378 483 395 3443 C ATOM 210 O ASN A 34 11.448 19.863 33.253 1.00130.07 O ANISOU 210 O ASN A 34 8873 12941 27605 611 651 3420 O ATOM 211 CB ASN A 34 10.991 21.141 35.864 1.00141.08 C ANISOU 211 CB ASN A 34 9550 13836 30219 74 1010 3945 C ATOM 212 CG ASN A 34 9.939 22.206 35.659 1.00147.78 C ANISOU 212 CG ASN A 34 10359 14456 31335 -275 806 4311 C ATOM 213 OD1 ASN A 34 9.199 22.184 34.678 1.00153.91 O ANISOU 213 OD1 ASN A 34 11398 15135 31946 -288 451 4303 O ATOM 214 ND2 ASN A 34 9.862 23.148 36.592 1.00145.95 N ANISOU 214 ND2 ASN A 34 9798 14134 31523 -560 1028 4635 N ATOM 215 N SER A 35 9.288 19.240 33.430 1.00138.44 N ANISOU 215 N SER A 35 10113 13095 29391 456 -83 3377 N ATOM 216 CA SER A 35 9.098 19.038 31.997 1.00144.99 C ANISOU 216 CA SER A 35 11295 14094 29700 586 -348 3262 C ATOM 217 C SER A 35 9.001 20.367 31.251 1.00144.40 C ANISOU 217 C SER A 35 11204 14275 29385 344 -287 3622 C ATOM 218 O SER A 35 9.003 20.403 30.020 1.00147.26 O ANISOU 218 O SER A 35 11831 14869 29253 432 -435 3575 O ATOM 219 CB SER A 35 7.854 18.183 31.731 1.00145.60 C ANISOU 219 CB SER A 35 11626 13660 30037 633 -884 3075 C ATOM 220 OG SER A 35 6.686 18.791 32.259 1.00148.48 O ANISOU 220 OG SER A 35 11862 13565 30989 311 -1096 3348 O ATOM 221 N ASN A 36 8.915 21.457 32.005 1.00141.69 N ANISOU 221 N ASN A 36 10551 13888 29396 39 -70 3982 N ATOM 222 CA ASN A 36 8.886 22.790 31.418 1.00143.39 C ANISOU 222 CA ASN A 36 10712 14355 29414 -207 32 4347 C ATOM 223 C ASN A 36 10.292 23.273 31.080 1.00146.53 C ANISOU 223 C ASN A 36 11031 15393 29250 -107 492 4387 C ATOM 224 O ASN A 36 10.473 24.357 30.526 1.00144.26 O ANISOU 224 O ASN A 36 10705 15401 28708 -276 628 4668 O ATOM 225 CB ASN A 36 8.188 23.778 32.355 1.00136.07 C ANISOU 225 CB ASN A 36 9487 13112 29102 -582 68 4722 C ATOM 226 CG ASN A 36 6.755 23.383 32.652 1.00132.28 C ANISOU 226 CG ASN A 36 9084 12000 29177 -701 -394 4706 C ATOM 227 OD1 ASN A 36 6.101 22.734 31.839 1.00134.87 O ANISOU 227 OD1 ASN A 36 9719 12159 29367 -582 -787 4518 O ATOM 228 ND2 ASN A 36 6.261 23.774 33.819 1.00119.18 N ANISOU 228 ND2 ASN A 36 7146 9989 28149 -939 -348 4904 N ATOM 229 N LEU A 37 11.282 22.452 31.420 1.00148.87 N ANISOU 229 N LEU A 37 11306 15900 29358 170 729 4102 N ATOM 230 CA LEU A 37 12.677 22.738 31.106 1.00151.15 C ANISOU 230 CA LEU A 37 11538 16798 29094 310 1162 4086 C ATOM 231 C LEU A 37 13.187 21.759 30.055 1.00151.19 C ANISOU 231 C LEU A 37 11876 17073 28497 667 1055 3718 C ATOM 232 O LEU A 37 14.280 21.925 29.517 1.00151.15 O ANISOU 232 O LEU A 37 11898 17593 27940 811 1350 3674 O ATOM 233 CB LEU A 37 13.540 22.649 32.366 1.00150.82 C ANISOU 233 CB LEU A 37 11180 16835 29289 342 1574 4067 C ATOM 234 CG LEU A 37 13.277 23.688 33.457 1.00149.08 C ANISOU 234 CG LEU A 37 10594 16436 29612 0 1771 4439 C ATOM 235 CD1 LEU A 37 13.977 23.303 34.751 1.00120.38 C ANISOU 235 CD1 LEU A 37 6687 12779 26272 73 2096 4344 C ATOM 236 CD2 LEU A 37 13.707 25.072 32.999 1.00148.53 C ANISOU 236 CD2 LEU A 37 10408 16772 29256 -210 2038 4797 C ATOM 237 N GLN A 38 12.385 20.738 29.767 1.00151.56 N ANISOU 237 N GLN A 38 12176 16755 28654 809 629 3454 N ATOM 238 CA GLN A 38 12.761 19.713 28.799 1.00154.65 C ANISOU 238 CA GLN A 38 12896 17346 28517 1153 484 3085 C ATOM 239 C GLN A 38 12.550 20.176 27.362 1.00154.92 C ANISOU 239 C GLN A 38 13193 17621 28049 1136 304 3166 C ATOM 240 O GLN A 38 11.894 19.498 26.573 1.00151.80 O ANISOU 240 O GLN A 38 13104 17048 27524 1260 -91 2970 O ATOM 241 CB GLN A 38 11.977 18.422 29.051 1.00154.70 C ANISOU 241 CB GLN A 38 13075 16864 28840 1314 94 2766 C ATOM 242 CG GLN A 38 12.222 17.795 30.410 1.00138.37 C ANISOU 242 CG GLN A 38 10783 14563 27229 1377 251 2632 C ATOM 243 CD GLN A 38 11.473 16.491 30.592 1.00154.71 C ANISOU 243 CD GLN A 38 13040 16169 29576 1549 -139 2304 C ATOM 244 OE1 GLN A 38 10.790 16.022 29.682 1.00160.32 O ANISOU 244 OE1 GLN A 38 14055 16738 30121 1634 -528 2165 O ATOM 245 NE2 GLN A 38 11.597 15.896 31.772 1.00135.50 N ANISOU 245 NE2 GLN A 38 10425 13494 27565 1603 -37 2178 N ATOM 246 N ASN A 39 13.107 21.336 27.028 1.00159.59 N ANISOU 246 N ASN A 39 13663 18616 28358 980 596 3456 N ATOM 247 CA ASN A 39 13.031 21.855 25.667 1.00169.34 C ANISOU 247 CA ASN A 39 15129 20134 29080 961 474 3549 C ATOM 248 C ASN A 39 14.264 21.460 24.859 1.00175.42 C ANISOU 248 C ASN A 39 16052 21467 29133 1264 703 3318 C ATOM 249 O ASN A 39 15.301 21.117 25.427 1.00173.10 O ANISOU 249 O ASN A 39 15617 21415 28739 1427 1048 3180 O ATOM 250 CB ASN A 39 12.855 23.377 25.676 1.00170.80 C ANISOU 250 CB ASN A 39 15113 20427 29355 608 630 4007 C ATOM 251 CG ASN A 39 13.970 24.093 26.420 1.00168.99 C ANISOU 251 CG ASN A 39 14554 20559 29095 537 1167 4184 C ATOM 252 OD1 ASN A 39 15.139 23.725 26.318 1.00172.15 O ANISOU 252 OD1 ASN A 39 14954 21371 29083 772 1467 3999 O ATOM 253 ND2 ASN A 39 13.609 25.125 27.173 1.00163.54 N ANISOU 253 ND2 ASN A 39 13580 19715 28843 210 1291 4544 N ATOM 254 N VAL A 40 14.145 21.506 23.536 1.00183.14 N ANISOU 254 N VAL A 40 17319 22649 29615 1339 508 3277 N ATOM 255 CA VAL A 40 15.243 21.118 22.657 1.00190.32 C ANISOU 255 CA VAL A 40 18406 24087 29822 1629 686 3052 C ATOM 256 C VAL A 40 16.503 21.922 22.958 1.00196.07 C ANISOU 256 C VAL A 40 18880 25323 30297 1591 1226 3224 C ATOM 257 O VAL A 40 17.619 21.433 22.787 1.00199.96 O ANISOU 257 O VAL A 40 19407 26207 30364 1851 1484 3002 O ATOM 258 CB VAL A 40 14.866 21.284 21.173 1.00195.97 C ANISOU 258 CB VAL A 40 19445 24955 30058 1657 408 3054 C ATOM 259 CG1 VAL A 40 15.968 20.738 20.281 1.00198.84 C ANISOU 259 CG1 VAL A 40 20010 25832 29709 1982 565 2782 C ATOM 260 CG2 VAL A 40 13.548 20.584 20.879 1.00202.61 C ANISOU 260 CG2 VAL A 40 20529 25278 31175 1665 -134 2917 C ATOM 261 N THR A 41 16.312 23.154 23.417 1.00152.79 N ANISOU 261 N THR A 41 13014 19717 25322 2090 -1738 3454 N ATOM 262 CA THR A 41 17.422 24.043 23.740 1.00157.74 C ANISOU 262 CA THR A 41 13567 19934 26435 2073 -1901 3849 C ATOM 263 C THR A 41 18.294 23.484 24.861 1.00150.24 C ANISOU 263 C THR A 41 12855 18515 25716 1903 -2042 3684 C ATOM 264 O THR A 41 19.522 23.482 24.763 1.00151.16 O ANISOU 264 O THR A 41 12864 18483 26086 1887 -2074 3949 O ATOM 265 CB THR A 41 16.914 25.435 24.164 1.00161.09 C ANISOU 265 CB THR A 41 13997 20091 27118 2103 -2060 4032 C ATOM 266 OG1 THR A 41 16.051 25.962 23.148 1.00164.27 O ANISOU 266 OG1 THR A 41 14183 20933 27300 2269 -1932 4183 O ATOM 267 CG2 THR A 41 18.082 26.387 24.393 1.00156.51 C ANISOU 267 CG2 THR A 41 13316 19117 27033 2085 -2211 4464 C ATOM 268 N ASN A 42 17.652 23.009 25.923 1.00141.56 N ANISOU 268 N ASN A 42 12074 17187 24525 1778 -2125 3248 N ATOM 269 CA ASN A 42 18.363 22.540 27.108 1.00139.40 C ANISOU 269 CA ASN A 42 12056 16441 24469 1611 -2280 3070 C ATOM 270 C ASN A 42 18.992 21.159 26.947 1.00140.75 C ANISOU 270 C ASN A 42 12270 16753 24454 1568 -2152 2884 C ATOM 271 O ASN A 42 19.697 20.685 27.838 1.00145.37 O ANISOU 271 O ASN A 42 13044 16979 25212 1443 -2266 2763 O ATOM 272 CB ASN A 42 17.447 22.572 28.334 1.00139.75 C ANISOU 272 CB ASN A 42 12437 16168 24491 1491 -2418 2677 C ATOM 273 CG ASN A 42 17.103 23.983 28.765 1.00148.50 C ANISOU 273 CG ASN A 42 13546 16984 25894 1501 -2586 2883 C ATOM 274 OD1 ASN A 42 17.781 24.941 28.393 1.00152.20 O ANISOU 274 OD1 ASN A 42 13802 17361 26665 1562 -2645 3324 O ATOM 275 ND2 ASN A 42 16.047 24.119 29.557 1.00151.94 N ANISOU 275 ND2 ASN A 42 14223 17262 26245 1438 -2657 2562 N ATOM 276 N TYR A 43 18.736 20.512 25.815 1.00138.32 N ANISOU 276 N TYR A 43 11792 16971 23793 1671 -1912 2861 N ATOM 277 CA TYR A 43 19.396 19.251 25.506 1.00136.23 C ANISOU 277 CA TYR A 43 11532 16871 23358 1648 -1760 2736 C ATOM 278 C TYR A 43 20.903 19.466 25.487 1.00133.34 C ANISOU 278 C TYR A 43 11026 16266 23371 1641 -1838 3112 C ATOM 279 O TYR A 43 21.665 18.627 25.963 1.00127.16 O ANISOU 279 O TYR A 43 10366 15304 22646 1557 -1848 2990 O ATOM 280 CB TYR A 43 18.917 18.706 24.160 1.00140.26 C ANISOU 280 CB TYR A 43 11839 18003 23451 1770 -1485 2721 C ATOM 281 CG TYR A 43 17.614 17.944 24.235 1.00145.33 C ANISOU 281 CG TYR A 43 12662 18907 23648 1740 -1365 2238 C ATOM 282 CD1 TYR A 43 17.598 16.557 24.203 1.00147.29 C ANISOU 282 CD1 TYR A 43 13048 19326 23589 1681 -1198 1884 C ATOM 283 CD2 TYR A 43 16.404 18.609 24.347 1.00145.49 C ANISOU 283 CD2 TYR A 43 12718 19000 23561 1769 -1413 2134 C ATOM 284 CE1 TYR A 43 16.409 15.854 24.274 1.00146.75 C ANISOU 284 CE1 TYR A 43 13147 19497 23113 1644 -1083 1435 C ATOM 285 CE2 TYR A 43 15.210 17.918 24.419 1.00143.84 C ANISOU 285 CE2 TYR A 43 12668 19036 22949 1737 -1304 1690 C ATOM 286 CZ TYR A 43 15.218 16.540 24.383 1.00145.72 C ANISOU 286 CZ TYR A 43 13042 19443 22883 1670 -1140 1338 C ATOM 287 OH TYR A 43 14.032 15.845 24.455 1.00148.39 O ANISOU 287 OH TYR A 43 13538 20024 22818 1629 -1025 889 O ATOM 288 N PHE A 44 21.320 20.604 24.941 1.00133.46 N ANISOU 288 N PHE A 44 10784 16278 23646 1731 -1891 3573 N ATOM 289 CA PHE A 44 22.729 20.973 24.896 1.00130.30 C ANISOU 289 CA PHE A 44 10227 15646 23635 1727 -1974 3966 C ATOM 290 C PHE A 44 23.224 21.391 26.277 1.00127.81 C ANISOU 290 C PHE A 44 10126 14729 23706 1579 -2248 3940 C ATOM 291 O PHE A 44 24.377 21.151 26.630 1.00132.82 O ANISOU 291 O PHE A 44 10756 15116 24595 1515 -2326 4067 O ATOM 292 CB PHE A 44 22.954 22.106 23.892 1.00134.15 C ANISOU 292 CB PHE A 44 10381 16314 24275 1866 -1940 4460 C ATOM 293 CG PHE A 44 22.548 21.762 22.483 1.00143.82 C ANISOU 293 CG PHE A 44 11374 18137 25134 2014 -1677 4529 C ATOM 294 CD1 PHE A 44 21.411 22.320 21.918 1.00150.07 C ANISOU 294 CD1 PHE A 44 12083 19230 25705 2115 -1610 4531 C ATOM 295 CD2 PHE A 44 23.302 20.879 21.725 1.00149.52 C ANISOU 295 CD2 PHE A 44 11959 19122 25730 2051 -1493 4593 C ATOM 296 CE1 PHE A 44 21.036 22.008 20.623 1.00153.69 C ANISOU 296 CE1 PHE A 44 12327 20250 25817 2245 -1374 4597 C ATOM 297 CE2 PHE A 44 22.931 20.562 20.429 1.00155.19 C ANISOU 297 CE2 PHE A 44 12470 20391 26103 2178 -1248 4653 C ATOM 298 CZ PHE A 44 21.796 21.128 19.878 1.00157.04 C ANISOU 298 CZ PHE A 44 12625 20931 26114 2272 -1193 4654 C ATOM 299 N VAL A 45 22.349 22.022 27.055 1.00123.36 N ANISOU 299 N VAL A 45 9749 13934 23187 1523 -2393 3778 N ATOM 300 CA VAL A 45 22.690 22.433 28.413 1.00127.34 C ANISOU 300 CA VAL A 45 10485 13868 24031 1371 -2654 3717 C ATOM 301 C VAL A 45 23.090 21.228 29.259 1.00126.94 C ANISOU 301 C VAL A 45 10690 13623 23920 1241 -2687 3373 C ATOM 302 O VAL A 45 24.000 21.312 30.081 1.00129.86 O ANISOU 302 O VAL A 45 11148 13585 24608 1131 -2867 3448 O ATOM 303 CB VAL A 45 21.528 23.188 29.089 1.00127.77 C ANISOU 303 CB VAL A 45 10723 13742 24082 1334 -2771 3539 C ATOM 304 CG1 VAL A 45 21.844 23.465 30.549 1.00106.27 C ANISOU 304 CG1 VAL A 45 8276 10433 21670 1158 -3030 3419 C ATOM 305 CG2 VAL A 45 21.238 24.486 28.343 1.00127.67 C ANISOU 305 CG2 VAL A 45 10461 13859 24189 1462 -2758 3921 C ATOM 306 N VAL A 46 22.411 20.106 29.045 1.00126.24 N ANISOU 306 N VAL A 46 10716 13833 23417 1253 -2511 2998 N ATOM 307 CA VAL A 46 22.754 18.867 29.734 1.00128.08 C ANISOU 307 CA VAL A 46 11184 13929 23550 1147 -2503 2665 C ATOM 308 C VAL A 46 24.135 18.381 29.302 1.00129.75 C ANISOU 308 C VAL A 46 11220 14169 23911 1172 -2447 2923 C ATOM 309 O VAL A 46 24.921 17.911 30.122 1.00130.68 O ANISOU 309 O VAL A 46 11484 13962 24206 1068 -2563 2855 O ATOM 310 CB VAL A 46 21.703 17.765 29.487 1.00126.33 C ANISOU 310 CB VAL A 46 11108 14057 22833 1161 -2295 2215 C ATOM 311 CG1 VAL A 46 22.114 16.474 30.174 1.00127.34 C ANISOU 311 CG1 VAL A 46 11479 14036 22866 1058 -2273 1889 C ATOM 312 CG2 VAL A 46 20.337 18.223 29.986 1.00122.31 C ANISOU 312 CG2 VAL A 46 10782 13503 22186 1129 -2358 1945 C ATOM 313 N SER A 47 24.419 18.497 28.008 1.00129.18 N ANISOU 313 N SER A 47 10830 14489 23763 1311 -2267 3222 N ATOM 314 CA SER A 47 25.734 18.167 27.476 1.00132.44 C ANISOU 314 CA SER A 47 11035 14950 24336 1351 -2201 3518 C ATOM 315 C SER A 47 26.796 18.983 28.207 1.00139.84 C ANISOU 315 C SER A 47 11944 15414 25775 1273 -2456 3822 C ATOM 316 O SER A 47 27.876 18.484 28.530 1.00138.59 O ANISOU 316 O SER A 47 11788 15072 25799 1222 -2502 3893 O ATOM 317 CB SER A 47 25.786 18.450 25.973 1.00134.94 C ANISOU 317 CB SER A 47 11003 15738 24528 1515 -1990 3837 C ATOM 318 OG SER A 47 27.080 18.204 25.451 1.00144.32 O ANISOU 318 OG SER A 47 11981 16960 25895 1554 -1927 4145 O ATOM 319 N LEU A 48 26.473 20.247 28.459 1.00142.24 N ANISOU 319 N LEU A 48 12219 15526 26301 1263 -2617 4001 N ATOM 320 CA LEU A 48 27.327 21.128 29.242 1.00141.93 C ANISOU 320 CA LEU A 48 12181 15014 26731 1169 -2873 4258 C ATOM 321 C LEU A 48 27.442 20.626 30.673 1.00139.19 C ANISOU 321 C LEU A 48 12172 14238 26474 998 -3063 3935 C ATOM 322 O LEU A 48 28.517 20.659 31.268 1.00133.10 O ANISOU 322 O LEU A 48 11410 13145 26018 911 -3219 4079 O ATOM 323 CB LEU A 48 26.760 22.546 29.241 1.00143.80 C ANISOU 323 CB LEU A 48 12355 15145 27139 1192 -2982 4459 C ATOM 324 CG LEU A 48 27.402 23.533 30.216 1.00147.67 C ANISOU 324 CG LEU A 48 12907 15108 28092 1067 -3261 4655 C ATOM 325 CD1 LEU A 48 28.872 23.732 29.889 1.00153.78 C ANISOU 325 CD1 LEU A 48 13438 15797 29194 1072 -3297 5064 C ATOM 326 CD2 LEU A 48 26.658 24.859 30.197 1.00146.52 C ANISOU 326 CD2 LEU A 48 12729 14882 28059 1097 -3334 4802 C ATOM 327 N ALA A 49 26.325 20.158 31.220 1.00141.13 N ANISOU 327 N ALA A 49 12697 14488 26440 949 -3049 3497 N ATOM 328 CA ALA A 49 26.303 19.642 32.580 1.00138.29 C ANISOU 328 CA ALA A 49 12683 13737 26124 788 -3216 3155 C ATOM 329 C ALA A 49 27.187 18.408 32.711 1.00128.49 C ANISOU 329 C ALA A 49 11488 12496 24837 760 -3155 3056 C ATOM 330 O ALA A 49 28.130 18.398 33.497 1.00124.10 O ANISOU 330 O ALA A 49 10999 11580 24573 659 -3336 3139 O ATOM 331 CB ALA A 49 24.877 19.336 33.011 1.00140.55 C ANISOU 331 CB ALA A 49 13240 14077 26084 756 -3177 2702 C ATOM 332 N ALA A 50 26.880 17.370 31.940 1.00125.72 N ANISOU 332 N ALA A 50 11100 12551 24117 848 -2896 2879 N ATOM 333 CA ALA A 50 27.681 16.151 31.952 1.00128.16 C ANISOU 333 CA ALA A 50 11441 12897 24356 840 -2798 2788 C ATOM 334 C ALA A 50 29.154 16.466 31.712 1.00132.76 C ANISOU 334 C ALA A 50 11774 13360 25307 859 -2870 3229 C ATOM 335 O ALA A 50 30.027 15.986 32.436 1.00129.38 O ANISOU 335 O ALA A 50 11444 12653 25059 778 -2982 3213 O ATOM 336 CB ALA A 50 27.171 15.164 30.914 1.00126.46 C ANISOU 336 CB ALA A 50 11158 13188 23704 950 -2479 2612 C ATOM 337 N ALA A 51 29.423 17.282 30.698 1.00136.49 N ANISOU 337 N ALA A 51 11922 14044 25892 967 -2805 3627 N ATOM 338 CA ALA A 51 30.793 17.654 30.358 1.00134.41 C ANISOU 338 CA ALA A 51 11392 13699 25979 994 -2855 4070 C ATOM 339 C ALA A 51 31.500 18.326 31.528 1.00133.87 C ANISOU 339 C ALA A 51 11421 13105 26337 852 -3170 4191 C ATOM 340 O ALA A 51 32.648 18.014 31.831 1.00137.49 O ANISOU 340 O ALA A 51 11829 13383 27027 809 -3247 4336 O ATOM 341 CB ALA A 51 30.811 18.561 29.134 1.00132.19 C ANISOU 341 CB ALA A 51 10770 13711 25747 1127 -2746 4464 C ATOM 342 N ASP A 52 30.806 19.251 32.182 1.00134.54 N ANISOU 342 N ASP A 52 11646 12949 26524 776 -3348 4130 N ATOM 343 CA ASP A 52 31.387 20.010 33.285 1.00137.69 C ANISOU 343 CA ASP A 52 12143 12848 27323 630 -3649 4245 C ATOM 344 C ASP A 52 31.327 19.270 34.622 1.00128.27 C ANISOU 344 C ASP A 52 11310 11322 26104 480 -3801 3864 C ATOM 345 O ASP A 52 32.077 19.589 35.543 1.00126.31 O ANISOU 345 O ASP A 52 11137 10676 26177 352 -4039 3953 O ATOM 346 CB ASP A 52 30.732 21.390 33.403 1.00150.18 C ANISOU 346 CB ASP A 52 13713 14294 29053 611 -3770 4374 C ATOM 347 CG ASP A 52 31.162 22.338 32.295 1.00159.21 C ANISOU 347 CG ASP A 52 14490 15634 30370 729 -3693 4850 C ATOM 348 OD1 ASP A 52 31.859 21.891 31.358 1.00162.26 O ANISOU 348 OD1 ASP A 52 14628 16302 30720 834 -3526 5059 O ATOM 349 OD2 ASP A 52 30.805 23.533 32.360 1.00159.68 O ANISOU 349 OD2 ASP A 52 14510 15559 30603 719 -3793 5018 O ATOM 350 N ILE A 53 30.434 18.291 34.735 1.00127.22 N ANISOU 350 N ILE A 53 11400 11351 25586 490 -3665 3439 N ATOM 351 CA ILE A 53 30.401 17.452 35.927 1.00128.73 C ANISOU 351 CA ILE A 53 11933 11259 25720 362 -3777 3069 C ATOM 352 C ILE A 53 31.663 16.609 35.968 1.00131.87 C ANISOU 352 C ILE A 53 12257 11617 26232 361 -3765 3179 C ATOM 353 O ILE A 53 32.319 16.503 37.002 1.00131.93 O ANISOU 353 O ILE A 53 12412 11251 26462 238 -3976 3151 O ATOM 354 CB ILE A 53 29.190 16.502 35.945 1.00124.76 C ANISOU 354 CB ILE A 53 11672 10971 24759 381 -3600 2589 C ATOM 355 CG1 ILE A 53 27.897 17.269 36.213 1.00124.36 C ANISOU 355 CG1 ILE A 53 11763 10878 24608 352 -3654 2413 C ATOM 356 CG2 ILE A 53 29.372 15.438 37.016 1.00121.72 C ANISOU 356 CG2 ILE A 53 11604 10337 24305 271 -3671 2243 C ATOM 357 CD1 ILE A 53 26.650 16.409 36.137 1.00123.45 C ANISOU 357 CD1 ILE A 53 11857 11009 24038 375 -3468 1955 C ATOM 358 N LEU A 54 31.997 16.017 34.827 1.00132.79 N ANISOU 358 N LEU A 54 12139 12122 26192 502 -3513 3309 N ATOM 359 CA LEU A 54 33.162 15.145 34.720 1.00127.10 C ANISOU 359 CA LEU A 54 11326 11414 25550 526 -3456 3417 C ATOM 360 C LEU A 54 34.456 15.877 35.045 1.00126.47 C ANISOU 360 C LEU A 54 11069 11041 25942 469 -3678 3820 C ATOM 361 O LEU A 54 35.480 15.249 35.300 1.00126.10 O ANISOU 361 O LEU A 54 10992 10890 26029 453 -3709 3897 O ATOM 362 CB LEU A 54 33.244 14.519 33.328 1.00124.23 C ANISOU 362 CB LEU A 54 10720 11540 24943 692 -3131 3516 C ATOM 363 CG LEU A 54 32.055 13.647 32.933 1.00122.29 C ANISOU 363 CG LEU A 54 10633 11622 24208 746 -2885 3112 C ATOM 364 CD1 LEU A 54 32.325 12.950 31.611 1.00123.57 C ANISOU 364 CD1 LEU A 54 10557 12241 24154 894 -2569 3224 C ATOM 365 CD2 LEU A 54 31.765 12.636 34.027 1.00119.64 C ANISOU 365 CD2 LEU A 54 10671 11068 23719 643 -2932 2670 C ATOM 366 N VAL A 55 34.412 17.204 35.021 1.00126.61 N ANISOU 366 N VAL A 55 10965 10931 26211 440 -3826 4081 N ATOM 367 CA VAL A 55 35.559 17.990 35.446 1.00128.89 C ANISOU 367 CA VAL A 55 11112 10904 26954 359 -4059 4438 C ATOM 368 C VAL A 55 35.883 17.648 36.894 1.00135.69 C ANISOU 368 C VAL A 55 12266 11338 27954 191 -4308 4225 C ATOM 369 O VAL A 55 36.967 17.160 37.194 1.00142.97 O ANISOU 369 O VAL A 55 13135 12136 29050 162 -4377 4337 O ATOM 370 CB VAL A 55 35.307 19.500 35.298 1.00127.54 C ANISOU 370 CB VAL A 55 10814 10632 27013 338 -4179 4704 C ATOM 371 CG1 VAL A 55 36.457 20.295 35.894 1.00128.88 C ANISOU 371 CG1 VAL A 55 10880 10434 27653 223 -4439 5028 C ATOM 372 CG2 VAL A 55 35.113 19.861 33.832 1.00126.15 C ANISOU 372 CG2 VAL A 55 10325 10881 26725 511 -3939 4962 C ATOM 373 N GLY A 56 34.931 17.888 37.786 1.00135.18 N ANISOU 373 N GLY A 56 12508 11053 27801 84 -4438 3914 N ATOM 374 CA GLY A 56 35.104 17.542 39.184 1.00133.88 C ANISOU 374 CA GLY A 56 12653 10490 27726 -79 -4667 3673 C ATOM 375 C GLY A 56 35.221 16.046 39.392 1.00132.00 C ANISOU 375 C GLY A 56 12579 10339 27237 -53 -4545 3381 C ATOM 376 O GLY A 56 35.764 15.587 40.394 1.00128.36 O ANISOU 376 O GLY A 56 12298 9585 26889 -160 -4714 3273 O ATOM 377 N VAL A 57 34.705 15.284 38.435 1.00131.09 N ANISOU 377 N VAL A 57 12402 10632 26776 90 -4244 3254 N ATOM 378 CA VAL A 57 34.719 13.829 38.515 1.00125.21 C ANISOU 378 CA VAL A 57 11813 10006 25756 128 -4081 2962 C ATOM 379 C VAL A 57 36.077 13.249 38.140 1.00126.21 C ANISOU 379 C VAL A 57 11716 10193 26044 192 -4025 3233 C ATOM 380 O VAL A 57 36.585 12.353 38.815 1.00129.19 O ANISOU 380 O VAL A 57 12252 10415 26421 150 -4068 3088 O ATOM 381 CB VAL A 57 33.635 13.208 37.603 1.00111.72 C ANISOU 381 CB VAL A 57 10124 8726 23601 249 -3765 2712 C ATOM 382 CG1 VAL A 57 33.755 11.693 37.576 1.00105.70 C ANISOU 382 CG1 VAL A 57 9493 8102 22565 294 -3568 2444 C ATOM 383 CG2 VAL A 57 32.245 13.631 38.065 1.00105.14 C ANISOU 383 CG2 VAL A 57 9540 7828 22580 183 -3815 2394 C ATOM 384 N LEU A 58 36.656 13.760 37.057 1.00122.61 N ANISOU 384 N LEU A 58 10893 9967 25725 298 -3922 3628 N ATOM 385 CA LEU A 58 37.900 13.214 36.528 1.00117.51 C ANISOU 385 CA LEU A 58 10002 9431 25214 380 -3827 3901 C ATOM 386 C LEU A 58 38.964 14.278 36.264 1.00118.45 C ANISOU 386 C LEU A 58 9799 9443 25762 370 -3977 4399 C ATOM 387 O LEU A 58 40.072 14.197 36.786 1.00123.47 O ANISOU 387 O LEU A 58 10376 9852 26685 314 -4136 4576 O ATOM 388 CB LEU A 58 37.627 12.419 35.249 1.00117.87 C ANISOU 388 CB LEU A 58 9904 9951 24928 548 -3459 3863 C ATOM 389 CG LEU A 58 36.753 11.170 35.384 1.00123.00 C ANISOU 389 CG LEU A 58 10842 10747 25145 568 -3263 3387 C ATOM 390 CD1 LEU A 58 36.533 10.519 34.024 1.00127.20 C ANISOU 390 CD1 LEU A 58 11196 11764 25372 726 -2899 3395 C ATOM 391 CD2 LEU A 58 37.380 10.187 36.353 1.00123.60 C ANISOU 391 CD2 LEU A 58 11129 10567 25268 504 -3347 3216 C ATOM 392 N ALA A 59 38.621 15.270 35.450 1.00110.58 N ANISOU 392 N ALA A 59 8593 8616 24807 427 -3923 4624 N ATOM 393 CA ALA A 59 39.565 16.322 35.080 1.00138.07 C ANISOU 393 CA ALA A 59 11756 12026 28679 426 -4034 5104 C ATOM 394 C ALA A 59 40.309 16.895 36.284 1.00137.20 C ANISOU 394 C ALA A 59 11725 11451 28956 256 -4380 5209 C ATOM 395 O ALA A 59 41.538 16.946 36.290 1.00141.23 O ANISOU 395 O ALA A 59 12034 11866 29761 243 -4462 5508 O ATOM 396 CB ALA A 59 38.862 17.428 34.307 1.00145.09 C ANISOU 396 CB ALA A 59 12495 13084 29550 482 -3974 5266 C ATOM 397 N ILE A 60 39.564 17.330 37.295 1.00133.04 N ANISOU 397 N ILE A 60 11487 10638 28425 120 -4579 4964 N ATOM 398 CA ILE A 60 40.164 17.873 38.509 1.00130.07 C ANISOU 398 CA ILE A 60 11222 9811 28388 -60 -4914 5024 C ATOM 399 C ILE A 60 41.024 16.839 39.238 1.00124.83 C ANISOU 399 C ILE A 60 10661 8992 27777 -108 -4998 4932 C ATOM 400 O ILE A 60 42.164 17.130 39.596 1.00129.24 O ANISOU 400 O ILE A 60 11078 9349 28678 -178 -5179 5203 O ATOM 401 CB ILE A 60 39.108 18.462 39.473 1.00130.73 C ANISOU 401 CB ILE A 60 11629 9622 28422 -198 -5093 4739 C ATOM 402 CG1 ILE A 60 38.414 19.672 38.841 1.00130.33 C ANISOU 402 CG1 ILE A 60 11451 9667 28402 -161 -5052 4898 C ATOM 403 CG2 ILE A 60 39.754 18.851 40.791 1.00125.24 C ANISOU 403 CG2 ILE A 60 11080 8462 28045 -395 -5432 4761 C ATOM 404 CD1 ILE A 60 37.389 20.321 39.746 1.00125.65 C ANISOU 404 CD1 ILE A 60 11158 8803 27781 -289 -5216 4643 C ATOM 405 N PRO A 61 40.477 15.636 39.479 1.00124.40 N ANISOU 405 N PRO A 61 10854 9026 27386 -74 -4868 4548 N ATOM 406 CA PRO A 61 41.305 14.566 40.043 1.00128.82 C ANISOU 406 CA PRO A 61 11494 9480 27974 -89 -4906 4476 C ATOM 407 C PRO A 61 42.608 14.366 39.267 1.00130.89 C ANISOU 407 C PRO A 61 11391 9899 28441 13 -4813 4869 C ATOM 408 O PRO A 61 43.674 14.281 39.877 1.00133.84 O ANISOU 408 O PRO A 61 11713 10050 29090 -57 -4998 5030 O ATOM 409 CB PRO A 61 40.413 13.336 39.896 1.00125.99 C ANISOU 409 CB PRO A 61 11369 9335 27165 -7 -4661 4057 C ATOM 410 CG PRO A 61 39.036 13.876 40.021 1.00122.13 C ANISOU 410 CG PRO A 61 11080 8849 26474 -49 -4660 3800 C ATOM 411 CD PRO A 61 39.059 15.238 39.390 1.00120.84 C ANISOU 411 CD PRO A 61 10651 8734 26529 -38 -4707 4147 C ATOM 412 N PHE A 62 42.515 14.286 37.942 1.00131.05 N ANISOU 412 N PHE A 62 11162 10306 28325 174 -4530 5021 N ATOM 413 CA PHE A 62 43.689 14.118 37.090 1.00129.90 C ANISOU 413 CA PHE A 62 10659 10339 28358 283 -4409 5398 C ATOM 414 C PHE A 62 44.621 15.320 37.197 1.00137.04 C ANISOU 414 C PHE A 62 11312 11040 29716 202 -4640 5823 C ATOM 415 O PHE A 62 45.823 15.167 37.394 1.00141.95 O ANISOU 415 O PHE A 62 11774 11551 30608 184 -4737 6060 O ATOM 416 CB PHE A 62 43.274 13.913 35.631 1.00123.10 C ANISOU 416 CB PHE A 62 9596 9934 27243 461 -4060 5465 C ATOM 417 CG PHE A 62 42.592 12.597 35.367 1.00113.66 C ANISOU 417 CG PHE A 62 8589 8981 25614 552 -3792 5095 C ATOM 418 CD1 PHE A 62 43.201 11.403 35.711 1.00115.38 C ANISOU 418 CD1 PHE A 62 8892 9163 25782 576 -3733 4980 C ATOM 419 CD2 PHE A 62 41.354 12.554 34.748 1.00112.44 C ANISOU 419 CD2 PHE A 62 8519 9099 25103 616 -3591 4869 C ATOM 420 CE1 PHE A 62 42.578 10.191 35.462 1.00112.08 C ANISOU 420 CE1 PHE A 62 8656 8962 24967 656 -3473 4637 C ATOM 421 CE2 PHE A 62 40.728 11.345 34.495 1.00110.98 C ANISOU 421 CE2 PHE A 62 8507 9142 24517 689 -3338 4523 C ATOM 422 CZ PHE A 62 41.341 10.163 34.853 1.00110.72 C ANISOU 422 CZ PHE A 62 8570 9059 24439 707 -3275 4404 C ATOM 423 N ALA A 63 44.054 16.514 37.057 1.00138.42 N ANISOU 423 N ALA A 63 11451 11171 29972 155 -4720 5917 N ATOM 424 CA ALA A 63 44.817 17.757 37.133 1.00145.01 C ANISOU 424 CA ALA A 63 12061 11810 31226 70 -4927 6308 C ATOM 425 C ALA A 63 45.639 17.838 38.417 1.00151.48 C ANISOU 425 C ALA A 63 12988 12221 32347 -105 -5253 6329 C ATOM 426 O ALA A 63 46.812 18.209 38.393 1.00154.54 O ANISOU 426 O ALA A 63 13128 12514 33076 -138 -5366 6676 O ATOM 427 CB ALA A 63 43.889 18.953 37.021 1.00144.25 C ANISOU 427 CB ALA A 63 12003 11675 31132 28 -4978 6317 C ATOM 428 N ILE A 64 45.010 17.499 39.537 1.00155.63 N ANISOU 428 N ILE A 64 13882 12510 32740 -219 -5403 5957 N ATOM 429 CA ILE A 64 45.689 17.492 40.827 1.00158.43 C ANISOU 429 CA ILE A 64 14380 12480 33336 -391 -5714 5931 C ATOM 430 C ILE A 64 46.796 16.443 40.847 1.00155.97 C ANISOU 430 C ILE A 64 13956 12218 33086 -331 -5677 6022 C ATOM 431 O ILE A 64 47.855 16.655 41.437 1.00162.74 O ANISOU 431 O ILE A 64 14717 12852 34266 -430 -5902 6231 O ATOM 432 CB ILE A 64 44.709 17.205 41.980 1.00164.61 C ANISOU 432 CB ILE A 64 15604 13026 33914 -511 -5848 5479 C ATOM 433 CG1 ILE A 64 43.583 18.241 42.002 1.00172.04 C ANISOU 433 CG1 ILE A 64 16666 13905 34796 -570 -5883 5380 C ATOM 434 CG2 ILE A 64 45.444 17.187 43.309 1.00161.93 C ANISOU 434 CG2 ILE A 64 15411 12296 33818 -691 -6174 5461 C ATOM 435 CD1 ILE A 64 42.477 17.910 42.980 1.00174.16 C ANISOU 435 CD1 ILE A 64 17364 13992 34815 -664 -5961 4913 C ATOM 436 N THR A 65 46.546 15.311 40.197 1.00153.43 N ANISOU 436 N THR A 65 13647 12193 32454 -169 -5388 5866 N ATOM 437 CA THR A 65 47.522 14.227 40.143 1.00162.28 C ANISOU 437 CA THR A 65 14672 13385 33601 -90 -5310 5935 C ATOM 438 C THR A 65 48.721 14.599 39.276 1.00172.15 C ANISOU 438 C THR A 65 15487 14773 35148 -13 -5252 6413 C ATOM 439 O THR A 65 49.869 14.475 39.702 1.00171.34 O ANISOU 439 O THR A 65 15258 14520 35324 -57 -5406 6620 O ATOM 440 CB THR A 65 46.896 12.928 39.602 1.00162.32 C ANISOU 440 CB THR A 65 14806 13683 33183 65 -4984 5637 C ATOM 441 OG1 THR A 65 45.837 12.505 40.470 1.00166.11 O ANISOU 441 OG1 THR A 65 15699 14022 33393 -12 -5039 5182 O ATOM 442 CG2 THR A 65 47.943 11.828 39.514 1.00162.71 C ANISOU 442 CG2 THR A 65 14747 13801 33276 156 -4887 5730 C ATOM 443 N ILE A 66 48.445 15.061 38.061 1.00179.64 N ANISOU 443 N ILE A 66 16208 16013 36036 103 -5032 6590 N ATOM 444 CA ILE A 66 49.490 15.404 37.104 1.00184.97 C ANISOU 444 CA ILE A 66 16466 16854 36959 191 -4935 7037 C ATOM 445 C ILE A 66 50.322 16.598 37.570 1.00192.70 C ANISOU 445 C ILE A 66 17273 17556 38389 45 -5233 7371 C ATOM 446 O ILE A 66 51.436 16.809 37.094 1.00192.94 O ANISOU 446 O ILE A 66 16977 17637 38695 80 -5225 7743 O ATOM 447 CB ILE A 66 48.895 15.697 35.709 1.00183.18 C ANISOU 447 CB ILE A 66 16057 17001 36543 341 -4634 7136 C ATOM 448 CG1 ILE A 66 49.992 15.720 34.641 1.00187.14 C ANISOU 448 CG1 ILE A 66 16147 17721 37236 462 -4471 7555 C ATOM 449 CG2 ILE A 66 48.118 17.005 35.722 1.00180.59 C ANISOU 449 CG2 ILE A 66 15762 16584 36269 260 -4749 7169 C ATOM 450 CD1 ILE A 66 49.472 15.963 33.240 1.00187.56 C ANISOU 450 CD1 ILE A 66 16013 18153 37098 613 -4169 7667 C ATOM 451 N SER A 67 49.780 17.374 38.505 1.00197.48 N ANISOU 451 N SER A 67 18101 17865 39068 -125 -5491 7234 N ATOM 452 CA SER A 67 50.486 18.537 39.030 1.00201.54 C ANISOU 452 CA SER A 67 18487 18092 39997 -288 -5782 7517 C ATOM 453 C SER A 67 51.815 18.118 39.645 1.00204.16 C ANISOU 453 C SER A 67 18710 18257 40605 -351 -5960 7683 C ATOM 454 O SER A 67 52.840 18.762 39.429 1.00208.17 O ANISOU 454 O SER A 67 18917 18715 41461 -389 -6054 8062 O ATOM 455 CB SER A 67 49.639 19.268 40.073 1.00201.66 C ANISOU 455 CB SER A 67 18816 17794 40011 -470 -6027 7280 C ATOM 456 OG SER A 67 49.652 18.584 41.313 1.00203.02 O ANISOU 456 OG SER A 67 19289 17716 40133 -582 -6220 6994 O ATOM 457 N THR A 68 51.788 17.031 40.411 1.00201.60 N ANISOU 457 N THR A 68 18629 17849 40121 -361 -6003 7399 N ATOM 458 CA THR A 68 52.992 16.506 41.041 1.00203.01 C ANISOU 458 CA THR A 68 18727 17880 40526 -407 -6166 7527 C ATOM 459 C THR A 68 53.755 15.593 40.086 1.00202.49 C ANISOU 459 C THR A 68 18394 18116 40428 -210 -5896 7709 C ATOM 460 O THR A 68 54.951 15.359 40.256 1.00206.17 O ANISOU 460 O THR A 68 18660 18523 41151 -216 -5988 7949 O ATOM 461 CB THR A 68 52.662 15.735 42.334 1.00199.03 C ANISOU 461 CB THR A 68 18611 17138 39872 -504 -6339 7150 C ATOM 462 OG1 THR A 68 51.784 14.643 42.032 1.00194.63 O ANISOU 462 OG1 THR A 68 18269 16786 38895 -365 -6073 6806 O ATOM 463 CG2 THR A 68 51.991 16.652 43.347 1.00195.99 C ANISOU 463 CG2 THR A 68 18493 16430 39546 -714 -6621 6980 C ATOM 464 N GLY A 69 53.054 15.081 39.079 1.00203.59 N ANISOU 464 N GLY A 69 14730 20109 42517 1814 -1135 1180 N ATOM 465 CA GLY A 69 53.663 14.213 38.087 1.00195.62 C ANISOU 465 CA GLY A 69 13740 19166 41421 1830 -923 1236 C ATOM 466 C GLY A 69 53.802 12.781 38.565 1.00186.15 C ANISOU 466 C GLY A 69 12123 18285 40322 2093 -937 1246 C ATOM 467 O GLY A 69 54.006 12.531 39.752 1.00185.20 O ANISOU 467 O GLY A 69 11577 18446 40344 2160 -1004 1177 O ATOM 468 N PHE A 70 53.693 11.838 37.635 1.00181.42 N ANISOU 468 N PHE A 70 11647 17639 39647 2243 -875 1331 N ATOM 469 CA PHE A 70 53.806 10.422 37.966 1.00180.13 C ANISOU 469 CA PHE A 70 11116 17759 39567 2501 -882 1350 C ATOM 470 C PHE A 70 54.496 9.642 36.851 1.00179.17 C ANISOU 470 C PHE A 70 11058 17681 39338 2485 -639 1405 C ATOM 471 O PHE A 70 55.057 10.229 35.927 1.00183.34 O ANISOU 471 O PHE A 70 11858 18066 39738 2248 -440 1416 O ATOM 472 CB PHE A 70 52.428 9.823 38.262 1.00182.44 C ANISOU 472 CB PHE A 70 11466 17932 39919 2845 -1189 1414 C ATOM 473 CG PHE A 70 51.463 9.917 37.113 1.00187.65 C ANISOU 473 CG PHE A 70 12654 18195 40448 2930 -1286 1520 C ATOM 474 CD1 PHE A 70 50.688 11.051 36.930 1.00186.95 C ANISOU 474 CD1 PHE A 70 12959 17768 40307 2837 -1428 1533 C ATOM 475 CD2 PHE A 70 51.325 8.868 36.219 1.00187.82 C ANISOU 475 CD2 PHE A 70 12780 18182 40400 3103 -1239 1606 C ATOM 476 CE1 PHE A 70 49.799 11.138 35.875 1.00184.10 C ANISOU 476 CE1 PHE A 70 13083 17042 39826 2914 -1520 1632 C ATOM 477 CE2 PHE A 70 50.438 8.949 35.163 1.00183.51 C ANISOU 477 CE2 PHE A 70 12722 17272 39733 3181 -1333 1703 C ATOM 478 CZ PHE A 70 49.674 10.085 34.992 1.00182.17 C ANISOU 478 CZ PHE A 70 12937 16768 39512 3086 -1474 1717 C ATOM 479 N CYS A 71 54.453 8.317 36.945 1.00175.93 N ANISOU 479 N CYS A 71 10396 17468 38982 2741 -656 1441 N ATOM 480 CA CYS A 71 55.092 7.457 35.955 1.00177.94 C ANISOU 480 CA CYS A 71 10676 17788 39144 2756 -433 1494 C ATOM 481 C CYS A 71 54.098 6.473 35.353 1.00178.40 C ANISOU 481 C CYS A 71 10926 17692 39165 3069 -587 1598 C ATOM 482 O CYS A 71 53.506 5.664 36.066 1.00181.66 O ANISOU 482 O CYS A 71 11093 18235 39693 3342 -775 1609 O ATOM 483 CB CYS A 71 56.261 6.696 36.582 1.00180.81 C ANISOU 483 CB CYS A 71 10505 18588 39604 2740 -246 1433 C ATOM 484 SG CYS A 71 57.563 7.745 37.265 1.00235.61 S ANISOU 484 SG CYS A 71 17184 25743 46593 2368 -41 1312 S ATOM 485 N ALA A 72 53.924 6.543 34.038 1.00181.92 N ANISOU 485 N ALA A 72 11810 17860 39450 3027 -507 1675 N ATOM 486 CA ALA A 72 53.007 5.649 33.341 1.00187.61 C ANISOU 486 CA ALA A 72 12755 18409 40119 3305 -641 1778 C ATOM 487 C ALA A 72 53.286 5.633 31.843 1.00187.29 C ANISOU 487 C ALA A 72 13116 18153 39891 3201 -450 1846 C ATOM 488 O ALA A 72 54.032 6.468 31.331 1.00185.99 O ANISOU 488 O ALA A 72 13113 17920 39633 2911 -243 1819 O ATOM 489 CB ALA A 72 51.566 6.055 33.609 1.00186.80 C ANISOU 489 CB ALA A 72 12901 18028 40047 3466 -970 1817 C ATOM 490 N ALA A 73 52.683 4.676 31.143 1.00183.51 N ANISOU 490 N ALA A 73 12798 17567 39359 3441 -521 1937 N ATOM 491 CA ALA A 73 52.851 4.561 29.700 1.00178.68 C ANISOU 491 CA ALA A 73 12582 16742 38567 3377 -359 2009 C ATOM 492 C ALA A 73 52.412 5.844 29.005 1.00179.59 C ANISOU 492 C ALA A 73 13206 16473 38558 3179 -391 2031 C ATOM 493 O ALA A 73 51.817 6.723 29.626 1.00172.83 O ANISOU 493 O ALA A 73 12413 15495 37757 3134 -571 2000 O ATOM 494 CB ALA A 73 52.067 3.372 29.169 1.00173.36 C ANISOU 494 CB ALA A 73 12015 15987 37868 3694 -488 2103 C ATOM 495 N CYS A 74 52.708 5.949 27.715 1.00189.40 N ANISOU 495 N CYS A 74 14812 17523 39629 3063 -213 2084 N ATOM 496 CA CYS A 74 52.352 7.138 26.951 1.00202.53 C ANISOU 496 CA CYS A 74 16974 18817 41160 2867 -221 2110 C ATOM 497 C CYS A 74 50.838 7.264 26.801 1.00212.96 C ANISOU 497 C CYS A 74 18636 19810 42471 3068 -541 2182 C ATOM 498 O CYS A 74 50.279 8.345 26.974 1.00215.08 O ANISOU 498 O CYS A 74 19131 19856 42734 2961 -673 2170 O ATOM 499 CB CYS A 74 53.025 7.123 25.576 1.00205.68 C ANISOU 499 CB CYS A 74 17677 19094 41376 2714 48 2156 C ATOM 500 SG CYS A 74 52.928 8.693 24.688 1.00227.10 S ANISOU 500 SG CYS A 74 20944 21413 43929 2405 110 2169 S ATOM 501 N HIS A 75 50.181 6.154 26.480 1.00218.38 N ANISOU 501 N HIS A 75 19356 20466 43154 3358 -664 2258 N ATOM 502 CA HIS A 75 48.727 6.138 26.353 1.00216.74 C ANISOU 502 CA HIS A 75 19443 19963 42947 3575 -975 2333 C ATOM 503 C HIS A 75 48.055 6.578 27.650 1.00210.41 C ANISOU 503 C HIS A 75 18429 19210 42308 3651 -1227 2286 C ATOM 504 O HIS A 75 47.271 7.527 27.663 1.00213.28 O ANISOU 504 O HIS A 75 19085 19298 42653 3598 -1394 2299 O ATOM 505 CB HIS A 75 48.233 4.747 25.952 1.00221.91 C ANISOU 505 CB HIS A 75 20079 20639 43597 3886 -1061 2414 C ATOM 506 CG HIS A 75 48.479 4.409 24.512 1.00229.66 C ANISOU 506 CG HIS A 75 21416 21450 44396 3852 -891 2485 C ATOM 507 ND1 HIS A 75 49.670 3.886 24.064 1.00234.13 N ANISOU 507 ND1 HIS A 75 21827 22228 44902 3752 -589 2466 N ATOM 508 CD2 HIS A 75 47.680 4.520 23.425 1.00232.51 C ANISOU 508 CD2 HIS A 75 22281 21445 44619 3906 -982 2577 C ATOM 509 CE1 HIS A 75 49.599 3.689 22.757 1.00237.55 C ANISOU 509 CE1 HIS A 75 22658 22434 45166 3747 -498 2542 C ATOM 510 NE2 HIS A 75 48.402 4.065 22.346 1.00237.02 N ANISOU 510 NE2 HIS A 75 22994 22015 45048 3838 -734 2610 N ATOM 511 N GLY A 76 48.371 5.885 28.739 1.00181.26 N ANISOU 511 N GLY A 76 14228 15870 38773 3777 -1251 2232 N ATOM 512 CA GLY A 76 47.801 6.201 30.036 1.00174.34 C ANISOU 512 CA GLY A 76 13106 15077 38059 3863 -1479 2183 C ATOM 513 C GLY A 76 48.126 7.609 30.498 1.00188.18 C ANISOU 513 C GLY A 76 14899 16781 39820 3577 -1438 2104 C ATOM 514 O GLY A 76 47.321 8.252 31.170 1.00198.48 O ANISOU 514 O GLY A 76 16250 17965 41198 3614 -1662 2092 O ATOM 515 N CYS A 77 49.311 8.088 30.133 1.00155.38 N ANISOU 515 N CYS A 77 22051 14459 22526 6269 -4832 -632 N ATOM 516 CA CYS A 77 49.760 9.417 30.536 1.00153.82 C ANISOU 516 CA CYS A 77 21316 14584 22545 6266 -4064 -501 C ATOM 517 C CYS A 77 49.080 10.506 29.713 1.00153.17 C ANISOU 517 C CYS A 77 21101 14818 22278 6251 -3635 -230 C ATOM 518 O CYS A 77 48.681 11.541 30.246 1.00147.78 O ANISOU 518 O CYS A 77 19993 14371 21786 5982 -3231 87 O ATOM 519 CB CYS A 77 51.282 9.530 30.406 1.00152.29 C ANISOU 519 CB CYS A 77 21035 14429 22398 6734 -3630 -900 C ATOM 520 SG CYS A 77 51.984 11.083 31.010 1.00195.27 S ANISOU 520 SG CYS A 77 25815 20244 28135 6739 -2691 -786 S ATOM 521 N LEU A 78 48.953 10.267 28.412 1.00158.89 N ANISOU 521 N LEU A 78 22196 15545 22630 6544 -3725 -358 N ATOM 522 CA LEU A 78 48.306 11.220 27.518 1.00164.55 C ANISOU 522 CA LEU A 78 22847 16543 23130 6564 -3360 -121 C ATOM 523 C LEU A 78 46.828 11.394 27.856 1.00168.29 C ANISOU 523 C LEU A 78 23253 17052 23635 6066 -3657 316 C ATOM 524 O LEU A 78 46.338 12.517 27.960 1.00162.86 O ANISOU 524 O LEU A 78 22217 16640 23022 5888 -3219 629 O ATOM 525 CB LEU A 78 48.464 10.785 26.060 1.00169.63 C ANISOU 525 CB LEU A 78 23947 17148 23355 6977 -3473 -369 C ATOM 526 CG LEU A 78 49.846 10.947 25.428 1.00172.60 C ANISOU 526 CG LEU A 78 24353 17594 23633 7508 -3013 -765 C ATOM 527 CD1 LEU A 78 49.862 10.364 24.024 1.00178.09 C ANISOU 527 CD1 LEU A 78 25544 18214 23907 7867 -3237 -997 C ATOM 528 CD2 LEU A 78 50.248 12.410 25.408 1.00169.69 C ANISOU 528 CD2 LEU A 78 23529 17584 23360 7584 -2166 -636 C ATOM 529 N PHE A 79 46.121 10.281 28.024 1.00175.00 N ANISOU 529 N PHE A 79 24439 17625 24426 5843 -4401 332 N ATOM 530 CA PHE A 79 44.705 10.329 28.359 1.00175.15 C ANISOU 530 CA PHE A 79 24420 17659 24469 5359 -4741 721 C ATOM 531 C PHE A 79 44.461 11.222 29.570 1.00163.92 C ANISOU 531 C PHE A 79 22455 16407 23421 4972 -4405 1034 C ATOM 532 O PHE A 79 43.604 12.104 29.540 1.00169.62 O ANISOU 532 O PHE A 79 22934 17362 24151 4733 -4176 1377 O ATOM 533 CB PHE A 79 44.155 8.925 28.614 1.00184.23 C ANISOU 533 CB PHE A 79 25978 18454 25568 5149 -5590 656 C ATOM 534 CG PHE A 79 42.761 8.916 29.181 1.00190.94 C ANISOU 534 CG PHE A 79 26749 19302 26497 4603 -5958 1042 C ATOM 535 CD1 PHE A 79 41.663 9.118 28.361 1.00192.71 C ANISOU 535 CD1 PHE A 79 27119 19643 26458 4502 -6093 1258 C ATOM 536 CD2 PHE A 79 42.551 8.703 30.534 1.00194.51 C ANISOU 536 CD2 PHE A 79 26982 19639 27285 4189 -6169 1183 C ATOM 537 CE1 PHE A 79 40.382 9.112 28.881 1.00191.70 C ANISOU 537 CE1 PHE A 79 26910 19525 26404 3999 -6429 1601 C ATOM 538 CE2 PHE A 79 41.274 8.696 31.059 1.00193.59 C ANISOU 538 CE2 PHE A 79 26788 19529 27241 3679 -6501 1529 C ATOM 539 CZ PHE A 79 40.188 8.900 30.232 1.00192.05 C ANISOU 539 CZ PHE A 79 26730 19456 26783 3584 -6631 1735 C ATOM 540 N ILE A 80 45.226 10.985 30.630 1.00142.28 N ANISOU 540 N ILE A 80 19526 13547 20988 4918 -4380 906 N ATOM 541 CA ILE A 80 45.112 11.763 31.858 1.00131.94 C ANISOU 541 CA ILE A 80 17699 12377 20053 4560 -4068 1168 C ATOM 542 C ILE A 80 45.405 13.245 31.626 1.00139.30 C ANISOU 542 C ILE A 80 18208 13683 21037 4687 -3241 1307 C ATOM 543 O ILE A 80 44.812 14.113 32.269 1.00143.35 O ANISOU 543 O ILE A 80 18325 14390 21753 4347 -2978 1644 O ATOM 544 CB ILE A 80 46.050 11.210 32.953 1.00118.77 C ANISOU 544 CB ILE A 80 15932 10510 18686 4552 -4165 951 C ATOM 545 CG1 ILE A 80 45.563 9.836 33.415 1.00 80.05 C ANISOU 545 CG1 ILE A 80 11391 5240 13783 4308 -4997 901 C ATOM 546 CG2 ILE A 80 46.140 12.173 34.128 1.00108.59 C ANISOU 546 CG2 ILE A 80 14070 9410 17778 4261 -3707 1186 C ATOM 547 CD1 ILE A 80 46.333 9.270 34.582 1.00 86.02 C ANISOU 547 CD1 ILE A 80 12054 5786 14843 4238 -5152 733 C ATOM 548 N ALA A 81 46.308 13.529 30.694 1.00144.21 N ANISOU 548 N ALA A 81 18920 14404 21468 5173 -2834 1044 N ATOM 549 CA ALA A 81 46.733 14.899 30.428 1.00142.78 C ANISOU 549 CA ALA A 81 18367 14563 21321 5336 -2025 1129 C ATOM 550 C ALA A 81 45.820 15.618 29.438 1.00139.37 C ANISOU 550 C ALA A 81 17983 14351 20619 5332 -1854 1383 C ATOM 551 O ALA A 81 45.630 16.831 29.526 1.00133.15 O ANISOU 551 O ALA A 81 16823 13848 19922 5244 -1297 1630 O ATOM 552 CB ALA A 81 48.173 14.914 29.927 1.00146.90 C ANISOU 552 CB ALA A 81 18941 15101 21772 5853 -1631 722 C ATOM 553 N CYS A 82 45.262 14.865 28.495 1.00146.96 N ANISOU 553 N CYS A 82 19410 15179 21249 5431 -2336 1318 N ATOM 554 CA CYS A 82 44.456 15.449 27.428 1.00155.84 C ANISOU 554 CA CYS A 82 20639 16496 22075 5482 -2208 1516 C ATOM 555 C CYS A 82 42.953 15.283 27.663 1.00156.49 C ANISOU 555 C CYS A 82 20760 16555 22143 5025 -2687 1872 C ATOM 556 O CYS A 82 42.141 15.801 26.897 1.00154.20 O ANISOU 556 O CYS A 82 20521 16435 21634 5007 -2612 2082 O ATOM 557 CB CYS A 82 44.845 14.843 26.078 1.00162.56 C ANISOU 557 CB CYS A 82 21976 17257 22532 5932 -2357 1205 C ATOM 558 SG CYS A 82 46.605 14.955 25.686 1.00147.86 S ANISOU 558 SG CYS A 82 20112 15421 20648 6492 -1830 748 S ATOM 559 N PHE A 83 42.586 14.568 28.722 1.00157.31 N ANISOU 559 N PHE A 83 20839 16454 22479 4656 -3174 1938 N ATOM 560 CA PHE A 83 41.177 14.345 29.031 1.00158.33 C ANISOU 560 CA PHE A 83 20998 16550 22612 4195 -3654 2259 C ATOM 561 C PHE A 83 40.445 15.666 29.242 1.00151.90 C ANISOU 561 C PHE A 83 19751 16058 21906 3946 -3196 2654 C ATOM 562 O PHE A 83 39.290 15.817 28.842 1.00155.22 O ANISOU 562 O PHE A 83 20242 16563 22171 3745 -3405 2906 O ATOM 563 CB PHE A 83 41.021 13.453 30.265 1.00162.83 C ANISOU 563 CB PHE A 83 21559 16858 23451 3826 -4178 2262 C ATOM 564 CG PHE A 83 39.590 13.232 30.679 1.00169.00 C ANISOU 564 CG PHE A 83 22343 17609 24259 3320 -4658 2588 C ATOM 565 CD1 PHE A 83 38.815 12.265 30.057 1.00171.56 C ANISOU 565 CD1 PHE A 83 23125 17751 24310 3263 -5306 2556 C ATOM 566 CD2 PHE A 83 39.020 13.990 31.691 1.00167.87 C ANISOU 566 CD2 PHE A 83 21743 17626 24415 2896 -4462 2921 C ATOM 567 CE1 PHE A 83 37.500 12.060 30.435 1.00168.99 C ANISOU 567 CE1 PHE A 83 22797 17406 24004 2792 -5744 2846 C ATOM 568 CE2 PHE A 83 37.706 13.788 32.072 1.00164.58 C ANISOU 568 CE2 PHE A 83 21320 17191 24021 2427 -4900 3211 C ATOM 569 CZ PHE A 83 36.946 12.822 31.444 1.00165.71 C ANISOU 569 CZ PHE A 83 21919 17155 23888 2373 -5541 3171 C ATOM 570 N VAL A 84 41.123 16.618 29.874 1.00142.84 N ANISOU 570 N VAL A 84 18156 15091 21026 3963 -2575 2702 N ATOM 571 CA VAL A 84 40.543 17.931 30.128 1.00138.12 C ANISOU 571 CA VAL A 84 17122 14802 20556 3747 -2085 3063 C ATOM 572 C VAL A 84 40.197 18.639 28.822 1.00135.04 C ANISOU 572 C VAL A 84 16848 14631 19832 4004 -1785 3145 C ATOM 573 O VAL A 84 39.221 19.388 28.752 1.00130.35 O ANISOU 573 O VAL A 84 16072 14234 19220 3778 -1672 3479 O ATOM 574 CB VAL A 84 41.495 18.813 30.964 1.00139.26 C ANISOU 574 CB VAL A 84 16787 15095 21031 3776 -1431 3051 C ATOM 575 CG1 VAL A 84 42.842 18.950 30.269 1.00141.65 C ANISOU 575 CG1 VAL A 84 17186 15425 21209 4308 -989 2701 C ATOM 576 CG2 VAL A 84 40.871 20.176 31.223 1.00137.13 C ANISOU 576 CG2 VAL A 84 16072 15140 20892 3549 -928 3429 C ATOM 577 N LEU A 85 40.998 18.390 27.790 1.00138.02 N ANISOU 577 N LEU A 85 17533 14969 19940 4479 -1665 2837 N ATOM 578 CA LEU A 85 40.774 18.997 26.484 1.00137.82 C ANISOU 578 CA LEU A 85 17660 15133 19571 4764 -1383 2879 C ATOM 579 C LEU A 85 39.441 18.552 25.888 1.00135.42 C ANISOU 579 C LEU A 85 17653 14789 19013 4581 -1936 3063 C ATOM 580 O LEU A 85 38.765 19.327 25.213 1.00135.15 O ANISOU 580 O LEU A 85 17579 14970 18801 4595 -1719 3286 O ATOM 581 CB LEU A 85 41.922 18.660 25.529 1.00146.06 C ANISOU 581 CB LEU A 85 19009 16111 20374 5299 -1212 2478 C ATOM 582 CG LEU A 85 43.312 19.178 25.909 1.00140.96 C ANISOU 582 CG LEU A 85 18090 15540 19927 5548 -600 2262 C ATOM 583 CD1 LEU A 85 44.366 18.694 24.922 1.00136.02 C ANISOU 583 CD1 LEU A 85 17813 14829 19039 6064 -523 1845 C ATOM 584 CD2 LEU A 85 43.313 20.696 25.993 1.00139.13 C ANISOU 584 CD2 LEU A 85 17420 15640 19804 5519 149 2513 C ATOM 585 N VAL A 86 39.069 17.301 26.143 1.00140.07 N ANISOU 585 N VAL A 86 18540 15098 19581 4411 -2652 2967 N ATOM 586 CA VAL A 86 37.808 16.751 25.653 1.00140.96 C ANISOU 586 CA VAL A 86 18947 15147 19464 4212 -3236 3119 C ATOM 587 C VAL A 86 36.613 17.477 26.267 1.00135.29 C ANISOU 587 C VAL A 86 17883 14612 18907 3752 -3216 3547 C ATOM 588 O VAL A 86 35.716 17.927 25.553 1.00134.10 O ANISOU 588 O VAL A 86 17785 14626 18541 3722 -3217 3754 O ATOM 589 CB VAL A 86 37.699 15.242 25.949 1.00143.98 C ANISOU 589 CB VAL A 86 19698 15177 19829 4087 -4006 2926 C ATOM 590 CG1 VAL A 86 36.352 14.703 25.487 1.00146.71 C ANISOU 590 CG1 VAL A 86 20327 15469 19946 3849 -4602 3094 C ATOM 591 CG2 VAL A 86 38.839 14.490 25.283 1.00149.88 C ANISOU 591 CG2 VAL A 86 20810 15740 20399 4555 -4056 2495 C ATOM 592 N LEU A 87 36.609 17.592 27.591 1.00121.62 N ANISOU 592 N LEU A 87 15796 12857 17555 3398 -3198 3673 N ATOM 593 CA LEU A 87 35.535 18.285 28.294 1.00105.34 C ANISOU 593 CA LEU A 87 13370 10970 15686 2943 -3163 4069 C ATOM 594 C LEU A 87 35.457 19.748 27.873 1.00108.18 C ANISOU 594 C LEU A 87 13414 11673 16018 3065 -2468 4283 C ATOM 595 O LEU A 87 34.369 20.294 27.691 1.00117.00 O ANISOU 595 O LEU A 87 14424 12962 17068 2853 -2490 4583 O ATOM 596 CB LEU A 87 35.728 18.188 29.809 1.00 90.55 C ANISOU 596 CB LEU A 87 11157 9012 14238 2579 -3198 4133 C ATOM 597 CG LEU A 87 35.833 16.783 30.404 1.00 94.08 C ANISOU 597 CG LEU A 87 11878 9110 14758 2418 -3867 3939 C ATOM 598 CD1 LEU A 87 35.859 16.846 31.924 1.00 88.85 C ANISOU 598 CD1 LEU A 87 10836 8404 14517 2010 -3870 4067 C ATOM 599 CD2 LEU A 87 34.686 15.912 29.925 1.00102.12 C ANISOU 599 CD2 LEU A 87 13276 9995 15529 2227 -4568 4004 C ATOM 600 N ALA A 88 36.617 20.378 27.721 1.00108.57 N ANISOU 600 N ALA A 88 13316 11818 16115 3408 -1852 4125 N ATOM 601 CA ALA A 88 36.683 21.781 27.327 1.00110.74 C ANISOU 601 CA ALA A 88 13300 12408 16367 3551 -1146 4303 C ATOM 602 C ALA A 88 36.257 21.979 25.875 1.00119.30 C ANISOU 602 C ALA A 88 14703 13598 17028 3839 -1130 4314 C ATOM 603 O ALA A 88 35.697 23.016 25.520 1.00116.09 O ANISOU 603 O ALA A 88 14111 13443 16555 3817 -776 4574 O ATOM 604 CB ALA A 88 38.086 22.329 27.549 1.00109.79 C ANISOU 604 CB ALA A 88 12962 12350 16403 3841 -508 4102 C ATOM 605 N GLN A 89 36.528 20.982 25.039 1.00129.38 N ANISOU 605 N GLN A 89 16460 14680 18017 4111 -1516 4031 N ATOM 606 CA GLN A 89 36.165 21.051 23.629 1.00143.45 C ANISOU 606 CA GLN A 89 18586 16540 19379 4398 -1546 4011 C ATOM 607 C GLN A 89 34.683 20.756 23.438 1.00154.98 C ANISOU 607 C GLN A 89 20179 18004 20701 4087 -2087 4264 C ATOM 608 O GLN A 89 34.027 21.351 22.583 1.00154.19 O ANISOU 608 O GLN A 89 20139 18087 20357 4172 -1964 4433 O ATOM 609 CB GLN A 89 37.006 20.074 22.804 1.00150.13 C ANISOU 609 CB GLN A 89 19899 17176 19969 4803 -1765 3605 C ATOM 610 CG GLN A 89 36.718 20.112 21.310 1.00155.62 C ANISOU 610 CG GLN A 89 20967 17944 20217 5126 -1786 3557 C ATOM 611 CD GLN A 89 37.101 21.436 20.671 1.00154.64 C ANISOU 611 CD GLN A 89 20657 18107 19993 5401 -1028 3641 C ATOM 612 OE1 GLN A 89 37.756 22.274 21.292 1.00152.02 O ANISOU 612 OE1 GLN A 89 19940 17904 19915 5402 -460 3682 O ATOM 613 NE2 GLN A 89 36.697 21.626 19.421 1.00156.63 N ANISOU 613 NE2 GLN A 89 21189 18457 19867 5633 -1018 3665 N ATOM 614 N SER A 90 34.161 19.832 24.237 1.00165.77 N ANISOU 614 N SER A 90 21596 19169 22222 3726 -2688 4285 N ATOM 615 CA SER A 90 32.745 19.493 24.185 1.00165.06 C ANISOU 615 CA SER A 90 21609 19075 22030 3384 -3230 4517 C ATOM 616 C SER A 90 31.901 20.699 24.575 1.00154.74 C ANISOU 616 C SER A 90 19868 18056 20871 3106 -2894 4911 C ATOM 617 O SER A 90 30.850 20.948 23.986 1.00152.90 O ANISOU 617 O SER A 90 19708 17952 20435 3021 -3051 5115 O ATOM 618 CB SER A 90 32.439 18.313 25.109 1.00167.31 C ANISOU 618 CB SER A 90 21993 19086 22492 3024 -3891 4460 C ATOM 619 OG SER A 90 31.064 17.972 25.063 1.00169.48 O ANISOU 619 OG SER A 90 22368 19362 22667 2680 -4417 4675 O ATOM 620 N SER A 91 32.369 21.446 25.570 1.00137.10 N ANISOU 620 N SER A 91 17179 15922 18991 2969 -2433 5012 N ATOM 621 CA SER A 91 31.681 22.654 26.004 1.00122.32 C ANISOU 621 CA SER A 91 14863 14326 17288 2719 -2056 5375 C ATOM 622 C SER A 91 31.603 23.673 24.869 1.00119.48 C ANISOU 622 C SER A 91 14524 14215 16657 3043 -1576 5471 C ATOM 623 O SER A 91 30.612 24.388 24.738 1.00121.48 O ANISOU 623 O SER A 91 14614 14672 16872 2871 -1512 5771 O ATOM 624 CB SER A 91 32.376 23.261 27.224 1.00114.22 C ANISOU 624 CB SER A 91 13364 13353 16681 2568 -1602 5423 C ATOM 625 OG SER A 91 32.362 22.361 28.318 1.00110.77 O ANISOU 625 OG SER A 91 12894 12694 16499 2237 -2054 5364 O ATOM 626 N ILE A 92 32.649 23.729 24.050 1.00121.41 N ANISOU 626 N ILE A 92 14976 14444 16711 3513 -1246 5211 N ATOM 627 CA ILE A 92 32.688 24.640 22.908 1.00129.46 C ANISOU 627 CA ILE A 92 16060 15680 17447 3855 -783 5268 C ATOM 628 C ILE A 92 31.507 24.405 21.972 1.00134.06 C ANISOU 628 C ILE A 92 16943 16303 17690 3833 -1209 5400 C ATOM 629 O ILE A 92 30.774 25.336 21.635 1.00133.94 O ANISOU 629 O ILE A 92 16775 16520 17595 3789 -974 5673 O ATOM 630 CB ILE A 92 34.000 24.494 22.110 1.00140.54 C ANISOU 630 CB ILE A 92 17719 17019 18663 4364 -468 4917 C ATOM 631 CG1 ILE A 92 35.194 24.939 22.955 1.00143.54 C ANISOU 631 CG1 ILE A 92 17761 17412 19366 4419 62 4801 C ATOM 632 CG2 ILE A 92 33.935 25.309 20.828 1.00140.73 C ANISOU 632 CG2 ILE A 92 17881 17246 18345 4708 -75 4971 C ATOM 633 CD1 ILE A 92 35.204 26.421 23.249 1.00140.96 C ANISOU 633 CD1 ILE A 92 16983 17370 19206 4372 765 5061 C ATOM 634 N PHE A 93 31.333 23.156 21.553 1.00138.56 N ANISOU 634 N PHE A 93 17942 16644 18058 3868 -1837 5200 N ATOM 635 CA PHE A 93 30.227 22.780 20.683 1.00141.68 C ANISOU 635 CA PHE A 93 18652 17052 18126 3838 -2308 5293 C ATOM 636 C PHE A 93 28.880 23.105 21.324 1.00125.96 C ANISOU 636 C PHE A 93 16390 15186 16285 3365 -2543 5651 C ATOM 637 O PHE A 93 28.007 23.687 20.684 1.00120.08 O ANISOU 637 O PHE A 93 15649 14630 15344 3366 -2510 5866 O ATOM 638 CB PHE A 93 30.301 21.291 20.349 1.00151.84 C ANISOU 638 CB PHE A 93 20414 18044 19234 3895 -2978 5008 C ATOM 639 CG PHE A 93 31.534 20.897 19.581 1.00154.19 C ANISOU 639 CG PHE A 93 21026 18220 19338 4378 -2806 4642 C ATOM 640 CD1 PHE A 93 31.637 21.166 18.225 1.00156.13 C ANISOU 640 CD1 PHE A 93 21558 18564 19201 4772 -2626 4564 C ATOM 641 CD2 PHE A 93 32.583 20.244 20.210 1.00151.55 C ANISOU 641 CD2 PHE A 93 20707 17675 19201 4437 -2835 4368 C ATOM 642 CE1 PHE A 93 32.766 20.801 17.514 1.00156.27 C ANISOU 642 CE1 PHE A 93 21862 18477 19038 5210 -2467 4219 C ATOM 643 CE2 PHE A 93 33.715 19.876 19.503 1.00154.06 C ANISOU 643 CE2 PHE A 93 21306 17887 19341 4883 -2682 4019 C ATOM 644 CZ PHE A 93 33.805 20.155 18.154 1.00157.06 C ANISOU 644 CZ PHE A 93 21963 18372 19341 5266 -2495 3943 C ATOM 645 N SER A 94 28.718 22.717 22.586 1.00115.06 N ANISOU 645 N SER A 94 14776 13696 15245 2965 -2787 5709 N ATOM 646 CA SER A 94 27.495 22.999 23.329 1.00107.31 C ANISOU 646 CA SER A 94 13504 12827 14444 2484 -3005 6036 C ATOM 647 C SER A 94 27.199 24.495 23.341 1.00109.53 C ANISOU 647 C SER A 94 13383 13426 14806 2477 -2394 6333 C ATOM 648 O SER A 94 26.102 24.923 22.987 1.00109.00 O ANISOU 648 O SER A 94 13274 13529 14612 2346 -2500 6576 O ATOM 649 CB SER A 94 27.607 22.481 24.763 1.00 98.47 C ANISOU 649 CB SER A 94 12152 11549 13715 2086 -3232 6034 C ATOM 650 OG SER A 94 27.849 21.086 24.786 1.00103.24 O ANISOU 650 OG SER A 94 13133 11845 14246 2078 -3815 5767 O ATOM 651 N LEU A 95 28.186 25.284 23.752 1.00112.60 N ANISOU 651 N LEU A 95 13479 13897 15406 2621 -1757 6307 N ATOM 652 CA LEU A 95 28.045 26.734 23.799 1.00107.46 C ANISOU 652 CA LEU A 95 12444 13538 14849 2636 -1123 6570 C ATOM 653 C LEU A 95 27.712 27.312 22.425 1.00107.23 C ANISOU 653 C LEU A 95 12636 13676 14429 2969 -936 6633 C ATOM 654 O LEU A 95 26.878 28.211 22.309 1.00 98.38 O ANISOU 654 O LEU A 95 11307 12781 13289 2859 -759 6924 O ATOM 655 CB LEU A 95 29.322 27.378 24.345 1.00101.18 C ANISOU 655 CB LEU A 95 11362 12775 14305 2793 -468 6472 C ATOM 656 CG LEU A 95 29.701 27.079 25.797 1.00104.69 C ANISOU 656 CG LEU A 95 11498 13103 15177 2464 -519 6451 C ATOM 657 CD1 LEU A 95 31.047 27.700 26.138 1.00111.15 C ANISOU 657 CD1 LEU A 95 12085 13960 16187 2693 146 6315 C ATOM 658 CD2 LEU A 95 28.631 27.582 26.741 1.00105.26 C ANISOU 658 CD2 LEU A 95 11169 13312 15512 1977 -596 6796 C ATOM 659 N LEU A 96 28.365 26.793 21.388 1.00113.01 N ANISOU 659 N LEU A 96 13792 14296 14849 3377 -978 6357 N ATOM 660 CA LEU A 96 28.130 27.256 20.024 1.00119.29 C ANISOU 660 CA LEU A 96 14844 15231 15249 3720 -816 6385 C ATOM 661 C LEU A 96 26.725 26.895 19.557 1.00120.09 C ANISOU 661 C LEU A 96 15130 15366 15131 3532 -1384 6554 C ATOM 662 O LEU A 96 26.007 27.735 19.016 1.00119.02 O ANISOU 662 O LEU A 96 14925 15450 14846 3567 -1203 6788 O ATOM 663 CB LEU A 96 29.166 26.666 19.065 1.00122.66 C ANISOU 663 CB LEU A 96 15696 15511 15397 4181 -779 6026 C ATOM 664 CG LEU A 96 28.994 27.024 17.587 1.00121.52 C ANISOU 664 CG LEU A 96 15873 15487 14814 4559 -645 6018 C ATOM 665 CD1 LEU A 96 29.088 28.527 17.390 1.00112.49 C ANISOU 665 CD1 LEU A 96 14435 14619 13687 4688 80 6238 C ATOM 666 CD2 LEU A 96 30.023 26.306 16.728 1.00123.78 C ANISOU 666 CD2 LEU A 96 16582 15606 14844 4981 -666 5638 C ATOM 667 N ALA A 97 26.344 25.640 19.771 1.00119.71 N ANISOU 667 N ALA A 97 15321 15100 15062 3333 -2072 6431 N ATOM 668 CA ALA A 97 25.015 25.167 19.405 1.00116.69 C ANISOU 668 CA ALA A 97 15121 14731 14486 3121 -2665 6566 C ATOM 669 C ALA A 97 23.935 26.038 20.035 1.00113.31 C ANISOU 669 C ALA A 97 14273 14530 14249 2752 -2582 6940 C ATOM 670 O ALA A 97 23.000 26.465 19.358 1.00113.99 O ANISOU 670 O ALA A 97 14409 14788 14115 2764 -2654 7126 O ATOM 671 CB ALA A 97 24.837 23.716 19.817 1.00110.78 C ANISOU 671 CB ALA A 97 14620 13701 13768 2892 -3382 6386 C ATOM 672 N ILE A 98 24.069 26.294 21.332 1.00105.29 N ANISOU 672 N ILE A 98 12844 13517 13643 2428 -2435 7044 N ATOM 673 CA ILE A 98 23.128 27.149 22.047 1.00 94.45 C ANISOU 673 CA ILE A 98 11033 12359 12494 2065 -2319 7390 C ATOM 674 C ILE A 98 23.020 28.515 21.378 1.00 98.51 C ANISOU 674 C ILE A 98 11393 13154 12883 2310 -1728 7588 C ATOM 675 O ILE A 98 21.922 29.030 21.175 1.00100.73 O ANISOU 675 O ILE A 98 11566 13620 13086 2165 -1813 7842 O ATOM 676 CB ILE A 98 23.544 27.341 23.515 1.00 80.55 C ANISOU 676 CB ILE A 98 8839 10565 11201 1747 -2120 7446 C ATOM 677 CG1 ILE A 98 23.512 26.006 24.263 1.00 80.71 C ANISOU 677 CG1 ILE A 98 8996 10312 11358 1451 -2741 7285 C ATOM 678 CG2 ILE A 98 22.637 28.353 24.198 1.00 69.32 C ANISOU 678 CG2 ILE A 98 6945 9388 10004 1408 -1920 7804 C ATOM 679 CD1 ILE A 98 23.940 26.108 25.711 1.00 82.59 C ANISOU 679 CD1 ILE A 98 8835 10499 12047 1136 -2583 7325 C ATOM 680 N ALA A 99 24.164 29.099 21.040 1.00109.57 N ANISOU 680 N ALA A 99 12786 14583 14262 2680 -1129 7467 N ATOM 681 CA ALA A 99 24.191 30.389 20.361 1.00121.61 C ANISOU 681 CA ALA A 99 14198 16354 15652 2946 -532 7631 C ATOM 682 C ALA A 99 23.429 30.321 19.042 1.00130.89 C ANISOU 682 C ALA A 99 15739 17605 16390 3158 -783 7669 C ATOM 683 O ALA A 99 22.620 31.198 18.737 1.00133.78 O ANISOU 683 O ALA A 99 15962 18193 16675 3130 -627 7932 O ATOM 684 CB ALA A 99 25.626 30.837 20.129 1.00125.78 C ANISOU 684 CB ALA A 99 14733 16867 16191 3327 96 7439 C ATOM 685 N ILE A 100 23.698 29.278 18.264 1.00138.89 N ANISOU 685 N ILE A 100 17221 18430 17119 3374 -1173 7402 N ATOM 686 CA ILE A 100 22.990 29.051 17.013 1.00149.58 C ANISOU 686 CA ILE A 100 18958 19829 18046 3568 -1481 7407 C ATOM 687 C ILE A 100 21.492 28.934 17.280 1.00151.79 C ANISOU 687 C ILE A 100 19133 20200 18340 3180 -1977 7655 C ATOM 688 O ILE A 100 20.681 29.593 16.631 1.00152.75 O ANISOU 688 O ILE A 100 19255 20521 18263 3241 -1923 7857 O ATOM 689 CB ILE A 100 23.470 27.762 16.320 1.00155.41 C ANISOU 689 CB ILE A 100 20206 20318 18524 3789 -1917 7065 C ATOM 690 CG1 ILE A 100 24.979 27.811 16.066 1.00150.68 C ANISOU 690 CG1 ILE A 100 19714 19625 17912 4172 -1449 6792 C ATOM 691 CG2 ILE A 100 22.711 27.545 15.020 1.00162.69 C ANISOU 691 CG2 ILE A 100 21518 21295 19001 3983 -2234 7075 C ATOM 692 CD1 ILE A 100 25.540 26.538 15.466 1.00149.74 C ANISOU 692 CD1 ILE A 100 20075 19253 17568 4391 -1858 6437 C ATOM 693 N ASP A 101 21.140 28.091 18.246 1.00150.21 N ANISOU 693 N ASP A 101 18844 19854 18376 2782 -2459 7632 N ATOM 694 CA ASP A 101 19.752 27.867 18.624 1.00146.58 C ANISOU 694 CA ASP A 101 18273 19463 17959 2368 -2965 7841 C ATOM 695 C ASP A 101 19.045 29.177 18.953 1.00137.18 C ANISOU 695 C ASP A 101 16647 18562 16914 2214 -2589 8188 C ATOM 696 O ASP A 101 18.030 29.513 18.345 1.00139.87 O ANISOU 696 O ASP A 101 17032 19069 17044 2205 -2741 8363 O ATOM 697 CB ASP A 101 19.681 26.916 19.817 1.00149.93 C ANISOU 697 CB ASP A 101 18593 19687 18686 1945 -3410 7770 C ATOM 698 CG ASP A 101 18.261 26.664 20.276 1.00157.49 C ANISOU 698 CG ASP A 101 19421 20715 19704 1488 -3931 7977 C ATOM 699 OD1 ASP A 101 17.444 26.179 19.463 1.00165.97 O ANISOU 699 OD1 ASP A 101 20797 21799 20467 1514 -4383 7969 O ATOM 700 OD2 ASP A 101 17.963 26.948 21.454 1.00155.31 O ANISOU 700 OD2 ASP A 101 18736 20489 19785 1097 -3888 8141 O ATOM 701 N ARG A 102 19.585 29.910 19.920 1.00130.16 N ANISOU 701 N ARG A 102 15337 17732 16385 2095 -2102 8283 N ATOM 702 CA ARG A 102 19.007 31.185 20.329 1.00127.99 C ANISOU 702 CA ARG A 102 14622 17724 16284 1944 -1704 8606 C ATOM 703 C ARG A 102 18.854 32.144 19.155 1.00130.47 C ANISOU 703 C ARG A 102 15047 18242 16285 2321 -1328 8718 C ATOM 704 O ARG A 102 17.917 32.938 19.114 1.00133.87 O ANISOU 704 O ARG A 102 15264 18892 16709 2204 -1257 8989 O ATOM 705 CB ARG A 102 19.850 31.832 21.430 1.00131.05 C ANISOU 705 CB ARG A 102 14586 18128 17080 1839 -1163 8645 C ATOM 706 CG ARG A 102 19.760 31.130 22.785 1.00140.48 C ANISOU 706 CG ARG A 102 15556 19180 18642 1379 -1500 8625 C ATOM 707 CD ARG A 102 18.321 31.087 23.291 1.00155.05 C ANISOU 707 CD ARG A 102 17200 21136 20578 927 -1937 8867 C ATOM 708 NE ARG A 102 17.546 30.010 22.677 1.00169.66 N ANISOU 708 NE ARG A 102 19441 22878 22143 869 -2644 8772 N ATOM 709 CZ ARG A 102 16.231 29.869 22.802 1.00174.01 C ANISOU 709 CZ ARG A 102 19921 23529 22667 543 -3088 8947 C ATOM 710 NH1 ARG A 102 15.532 30.744 23.511 1.00169.26 N ANISOU 710 NH1 ARG A 102 18848 23145 22320 231 -2876 9185 N ATOM 711 NH2 ARG A 102 15.613 28.855 22.211 1.00179.72 N ANISOU 711 NH2 ARG A 102 21021 24144 23121 509 -3717 8836 N ATOM 712 N TYR A 103 19.779 32.073 18.205 1.00133.23 N ANISOU 712 N TYR A 103 15731 18517 16373 2772 -1086 8508 N ATOM 713 CA TYR A 103 19.705 32.915 17.017 1.00138.35 C ANISOU 713 CA TYR A 103 16537 19337 16692 3154 -738 8591 C ATOM 714 C TYR A 103 18.594 32.459 16.078 1.00146.68 C ANISOU 714 C TYR A 103 17913 20433 17385 3179 -1280 8634 C ATOM 715 O TYR A 103 17.817 33.274 15.582 1.00142.29 O ANISOU 715 O TYR A 103 17289 20092 16684 3232 -1161 8862 O ATOM 716 CB TYR A 103 21.040 32.930 16.272 1.00135.43 C ANISOU 716 CB TYR A 103 16442 18873 16141 3622 -327 8336 C ATOM 717 CG TYR A 103 20.984 33.677 14.958 1.00134.93 C ANISOU 717 CG TYR A 103 16606 18964 15697 4028 -15 8395 C ATOM 718 CD1 TYR A 103 21.066 35.064 14.919 1.00130.89 C ANISOU 718 CD1 TYR A 103 15824 18668 15241 4140 627 8613 C ATOM 719 CD2 TYR A 103 20.844 32.997 13.755 1.00138.37 C ANISOU 719 CD2 TYR A 103 17536 19326 15713 4297 -362 8233 C ATOM 720 CE1 TYR A 103 21.012 35.750 13.720 1.00133.34 C ANISOU 720 CE1 TYR A 103 16355 19112 15195 4508 911 8671 C ATOM 721 CE2 TYR A 103 20.790 33.676 12.551 1.00140.45 C ANISOU 721 CE2 TYR A 103 18017 19727 15620 4666 -81 8288 C ATOM 722 CZ TYR A 103 20.875 35.052 12.541 1.00137.83 C ANISOU 722 CZ TYR A 103 17416 19606 15349 4769 555 8509 C ATOM 723 OH TYR A 103 20.823 35.732 11.347 1.00138.78 O ANISOU 723 OH TYR A 103 17764 19857 15109 5134 836 8567 O ATOM 724 N ILE A 104 18.532 31.154 15.835 1.00162.67 N ANISOU 724 N ILE A 104 20292 22251 19264 3146 -1876 8411 N ATOM 725 CA ILE A 104 17.533 30.580 14.939 1.00169.55 C ANISOU 725 CA ILE A 104 21500 23138 19784 3168 -2434 8415 C ATOM 726 C ILE A 104 16.114 31.000 15.316 1.00158.95 C ANISOU 726 C ILE A 104 19878 21993 18522 2814 -2676 8719 C ATOM 727 O ILE A 104 15.325 31.390 14.457 1.00159.89 O ANISOU 727 O ILE A 104 20117 22274 18359 2942 -2752 8850 O ATOM 728 CB ILE A 104 17.618 29.042 14.920 1.00180.17 C ANISOU 728 CB ILE A 104 23199 24212 21045 3079 -3084 8142 C ATOM 729 CG1 ILE A 104 18.981 28.587 14.391 1.00184.62 C ANISOU 729 CG1 ILE A 104 24083 24586 21478 3471 -2879 7823 C ATOM 730 CG2 ILE A 104 16.492 28.457 14.080 1.00185.69 C ANISOU 730 CG2 ILE A 104 24213 24940 21403 3053 -3681 8163 C ATOM 731 CD1 ILE A 104 19.177 27.087 14.421 1.00188.48 C ANISOU 731 CD1 ILE A 104 24916 24792 21905 3400 -3484 7541 C ATOM 732 N ALA A 105 15.795 30.913 16.603 1.00215.05 N ANISOU 732 N ALA A 105 15188 25271 41252 -570 -1146 6391 N ATOM 733 CA ALA A 105 14.472 31.277 17.097 1.00195.09 C ANISOU 733 CA ALA A 105 12616 22329 39182 -761 -1670 6449 C ATOM 734 C ALA A 105 14.133 32.728 16.769 1.00194.89 C ANISOU 734 C ALA A 105 12598 22476 38975 -1056 -1971 6912 C ATOM 735 O ALA A 105 13.064 33.021 16.237 1.00201.81 O ANISOU 735 O ALA A 105 13689 23230 39758 -1225 -2436 6872 O ATOM 736 CB ALA A 105 14.385 31.037 18.596 1.00178.53 C ANISOU 736 CB ALA A 105 10142 19837 37854 -698 -1610 6492 C ATOM 737 N ILE A 106 15.051 33.631 17.093 1.00189.59 N ANISOU 737 N ILE A 106 11690 22089 38256 -1116 -1702 7350 N ATOM 738 CA ILE A 106 14.838 35.056 16.868 1.00183.92 C ANISOU 738 CA ILE A 106 10947 21547 37387 -1392 -1943 7825 C ATOM 739 C ILE A 106 14.792 35.398 15.380 1.00192.44 C ANISOU 739 C ILE A 106 12410 22992 37716 -1480 -2059 7811 C ATOM 740 O ILE A 106 13.936 36.166 14.938 1.00190.56 O ANISOU 740 O ILE A 106 12314 22728 37364 -1704 -2487 7973 O ATOM 741 CB ILE A 106 15.926 35.898 17.560 1.00173.88 C ANISOU 741 CB ILE A 106 9326 20512 36227 -1419 -1584 8285 C ATOM 742 CG1 ILE A 106 15.936 35.614 19.064 1.00168.03 C ANISOU 742 CG1 ILE A 106 8196 19402 36244 -1340 -1488 8317 C ATOM 743 CG2 ILE A 106 15.706 37.377 17.295 1.00169.57 C ANISOU 743 CG2 ILE A 106 8765 20154 35510 -1707 -1830 8775 C ATOM 744 CD1 ILE A 106 16.957 36.420 19.832 1.00170.08 C ANISOU 744 CD1 ILE A 106 8092 19863 36667 -1365 -1149 8761 C ATOM 745 N ALA A 107 15.712 34.823 14.612 1.00197.92 N ANISOU 745 N ALA A 107 13274 24027 37899 -1300 -1677 7615 N ATOM 746 CA ALA A 107 15.775 35.073 13.177 1.00202.02 C ANISOU 746 CA ALA A 107 14162 24917 37679 -1358 -1738 7582 C ATOM 747 C ALA A 107 14.614 34.409 12.444 1.00204.91 C ANISOU 747 C ALA A 107 14878 25065 37915 -1366 -2149 7171 C ATOM 748 O ALA A 107 13.931 35.045 11.641 1.00206.20 O ANISOU 748 O ALA A 107 15275 25313 37758 -1552 -2513 7268 O ATOM 749 CB ALA A 107 17.104 34.597 12.612 1.00202.43 C ANISOU 749 CB ALA A 107 14284 25382 37247 -1153 -1199 7476 C ATOM 750 N ILE A 108 14.397 33.128 12.724 1.00204.63 N ANISOU 750 N ILE A 108 14875 24748 38128 -1162 -2088 6712 N ATOM 751 CA ILE A 108 13.318 32.379 12.092 1.00206.37 C ANISOU 751 CA ILE A 108 15413 24737 38261 -1148 -2452 6282 C ATOM 752 C ILE A 108 12.537 31.574 13.125 1.00199.59 C ANISOU 752 C ILE A 108 14399 23337 38100 -1074 -2620 6011 C ATOM 753 O ILE A 108 12.832 30.401 13.353 1.00205.43 O ANISOU 753 O ILE A 108 15136 23949 38967 -839 -2369 5633 O ATOM 754 CB ILE A 108 13.855 31.415 11.021 1.00212.90 C ANISOU 754 CB ILE A 108 16552 25825 38514 -943 -2190 5883 C ATOM 755 CG1 ILE A 108 14.947 32.092 10.189 1.00215.50 C ANISOU 755 CG1 ILE A 108 16968 26713 38201 -962 -1877 6155 C ATOM 756 CG2 ILE A 108 12.718 30.924 10.136 1.00214.88 C ANISOU 756 CG2 ILE A 108 17173 25923 38548 -982 -2616 5514 C ATOM 757 CD1 ILE A 108 15.538 31.192 9.121 1.00220.56 C ANISOU 757 CD1 ILE A 108 17911 27635 38256 -762 -1601 5785 C ATOM 758 N PRO A 109 11.537 32.208 13.757 1.00183.93 N ANISOU 758 N PRO A 109 12283 21031 36571 -1275 -3045 6205 N ATOM 759 CA PRO A 109 10.714 31.559 14.785 1.00176.44 C ANISOU 759 CA PRO A 109 11174 19549 36316 -1232 -3243 5986 C ATOM 760 C PRO A 109 9.830 30.461 14.202 1.00184.97 C ANISOU 760 C PRO A 109 12564 20391 37324 -1142 -3487 5445 C ATOM 761 O PRO A 109 9.588 29.452 14.863 1.00184.46 O ANISOU 761 O PRO A 109 12418 19979 37691 -986 -3434 5115 O ATOM 762 CB PRO A 109 9.848 32.706 15.314 1.00164.74 C ANISOU 762 CB PRO A 109 9540 17870 35185 -1509 -3677 6370 C ATOM 763 CG PRO A 109 9.800 33.686 14.192 1.00166.59 C ANISOU 763 CG PRO A 109 10011 18477 34811 -1695 -3853 6619 C ATOM 764 CD PRO A 109 11.134 33.604 13.523 1.00175.00 C ANISOU 764 CD PRO A 109 11150 20029 35313 -1557 -3361 6654 C ATOM 765 N LEU A 110 9.362 30.657 12.974 1.00193.79 N ANISOU 765 N LEU A 110 14034 21698 37900 -1239 -3746 5354 N ATOM 766 CA LEU A 110 8.473 29.695 12.332 1.00200.53 C ANISOU 766 CA LEU A 110 15199 22347 38646 -1174 -4010 4851 C ATOM 767 C LEU A 110 9.193 28.395 11.975 1.00205.28 C ANISOU 767 C LEU A 110 15931 23045 39019 -885 -3604 4414 C ATOM 768 O LEU A 110 8.697 27.304 12.259 1.00203.43 O ANISOU 768 O LEU A 110 15741 22473 39081 -749 -3655 3990 O ATOM 769 CB LEU A 110 7.819 30.311 11.090 1.00206.49 C ANISOU 769 CB LEU A 110 16294 23304 38856 -1356 -4390 4892 C ATOM 770 CG LEU A 110 6.867 31.488 11.332 1.00202.64 C ANISOU 770 CG LEU A 110 15737 22672 38587 -1645 -4876 5251 C ATOM 771 CD1 LEU A 110 6.358 32.052 10.013 1.00205.47 C ANISOU 771 CD1 LEU A 110 16451 23282 38336 -1798 -5199 5280 C ATOM 772 CD2 LEU A 110 5.703 31.078 12.224 1.00196.64 C ANISOU 772 CD2 LEU A 110 14858 21352 38504 -1685 -5235 5065 C ATOM 773 N ARG A 111 10.364 28.513 11.359 1.00210.35 N ANISOU 773 N ARG A 111 16635 24149 39140 -794 -3199 4516 N ATOM 774 CA ARG A 111 11.150 27.341 10.988 1.00214.83 C ANISOU 774 CA ARG A 111 17322 24850 39452 -520 -2783 4130 C ATOM 775 C ARG A 111 11.947 26.802 12.171 1.00210.11 C ANISOU 775 C ARG A 111 16384 24114 39335 -330 -2361 4125 C ATOM 776 O ARG A 111 12.592 25.758 12.071 1.00212.32 O ANISOU 776 O ARG A 111 16716 24447 39511 -86 -2000 3799 O ATOM 777 CB ARG A 111 12.086 27.663 9.823 1.00221.64 C ANISOU 777 CB ARG A 111 18397 26268 39550 -495 -2516 4231 C ATOM 778 CG ARG A 111 11.367 28.084 8.551 1.00228.12 C ANISOU 778 CG ARG A 111 19586 27254 39835 -653 -2899 4193 C ATOM 779 CD ARG A 111 10.540 26.944 7.984 1.00234.29 C ANISOU 779 CD ARG A 111 20665 27807 40546 -550 -3117 3636 C ATOM 780 NE ARG A 111 11.348 25.747 7.772 1.00240.62 N ANISOU 780 NE ARG A 111 21544 28708 41172 -270 -2682 3259 N ATOM 781 CZ ARG A 111 12.149 25.561 6.727 1.00248.80 C ANISOU 781 CZ ARG A 111 22808 30169 41554 -169 -2404 3172 C ATOM 782 NH1 ARG A 111 12.255 26.498 5.795 1.00252.61 N ANISOU 782 NH1 ARG A 111 23466 31018 41494 -325 -2513 3438 N ATOM 783 NH2 ARG A 111 12.848 24.440 6.615 1.00251.99 N ANISOU 783 NH2 ARG A 111 23266 30632 41847 88 -2015 2821 N ATOM 784 N TYR A 112 11.901 27.517 13.291 1.00203.55 N ANISOU 784 N TYR A 112 15206 23106 39028 -440 -2406 4488 N ATOM 785 CA TYR A 112 12.589 27.073 14.497 1.00197.73 C ANISOU 785 CA TYR A 112 14125 22211 38792 -272 -2037 4507 C ATOM 786 C TYR A 112 12.131 25.674 14.887 1.00193.45 C ANISOU 786 C TYR A 112 13625 21272 38605 -71 -2031 3991 C ATOM 787 O TYR A 112 12.945 24.770 15.056 1.00192.99 O ANISOU 787 O TYR A 112 13525 21267 38535 175 -1609 3759 O ATOM 788 CB TYR A 112 12.353 28.049 15.652 1.00193.54 C ANISOU 788 CB TYR A 112 13233 21482 38822 -444 -2183 4948 C ATOM 789 CG TYR A 112 12.917 27.578 16.976 1.00189.94 C ANISOU 789 CG TYR A 112 12415 20807 38947 -278 -1853 4956 C ATOM 790 CD1 TYR A 112 12.134 26.858 17.869 1.00184.03 C ANISOU 790 CD1 TYR A 112 11554 19550 38820 -218 -2025 4705 C ATOM 791 CD2 TYR A 112 14.233 27.852 17.332 1.00189.15 C ANISOU 791 CD2 TYR A 112 12086 21010 38773 -180 -1368 5212 C ATOM 792 CE1 TYR A 112 12.643 26.425 19.080 1.00179.66 C ANISOU 792 CE1 TYR A 112 10672 18794 38795 -61 -1724 4712 C ATOM 793 CE2 TYR A 112 14.751 27.423 18.543 1.00183.22 C ANISOU 793 CE2 TYR A 112 11003 20062 38550 -23 -1068 5218 C ATOM 794 CZ TYR A 112 13.951 26.709 19.412 1.00177.07 C ANISOU 794 CZ TYR A 112 10122 18776 38380 38 -1248 4968 C ATOM 795 OH TYR A 112 14.461 26.279 20.616 1.00165.29 O ANISOU 795 OH TYR A 112 8304 17087 37411 199 -949 4974 O ATOM 796 N ASN A 113 10.822 25.497 15.018 1.00190.91 N ANISOU 796 N ASN A 113 13391 20553 38594 -177 -2500 3810 N ATOM 797 CA ASN A 113 10.267 24.204 15.398 1.00189.28 C ANISOU 797 CA ASN A 113 13229 19937 38750 -7 -2539 3321 C ATOM 798 C ASN A 113 10.449 23.147 14.312 1.00191.05 C ANISOU 798 C ASN A 113 13806 20320 38466 173 -2398 2848 C ATOM 799 O ASN A 113 10.497 21.951 14.601 1.00186.87 O ANISOU 799 O ASN A 113 13291 19571 38140 389 -2221 2445 O ATOM 800 CB ASN A 113 8.790 24.344 15.765 1.00189.30 C ANISOU 800 CB ASN A 113 13245 19487 39194 -183 -3096 3257 C ATOM 801 CG ASN A 113 8.557 25.384 16.843 1.00186.94 C ANISOU 801 CG ASN A 113 12602 19016 39410 -366 -3254 3718 C ATOM 802 OD1 ASN A 113 8.627 25.086 18.035 1.00185.27 O ANISOU 802 OD1 ASN A 113 12097 18503 39793 -284 -3132 3733 O ATOM 803 ND2 ASN A 113 8.280 26.616 16.427 1.00187.54 N ANISOU 803 ND2 ASN A 113 12714 19284 39258 -613 -3527 4099 N ATOM 804 N GLY A 114 10.556 23.596 13.066 1.00196.50 N ANISOU 804 N GLY A 114 14778 21390 38491 86 -2473 2902 N ATOM 805 CA GLY A 114 10.739 22.693 11.944 1.00203.10 C ANISOU 805 CA GLY A 114 15962 22414 38791 240 -2353 2481 C ATOM 806 C GLY A 114 12.167 22.205 11.791 1.00205.41 C ANISOU 806 C GLY A 114 16218 23049 38779 472 -1761 2434 C ATOM 807 O GLY A 114 12.405 21.112 11.277 1.00207.04 O ANISOU 807 O GLY A 114 16625 23290 38752 675 -1566 2009 O ATOM 808 N LEU A 115 13.118 23.020 12.237 1.00204.79 N ANISOU 808 N LEU A 115 15882 23224 38703 442 -1475 2869 N ATOM 809 CA LEU A 115 14.530 22.675 12.119 1.00209.64 C ANISOU 809 CA LEU A 115 16439 24191 39026 649 -905 2871 C ATOM 810 C LEU A 115 15.116 22.226 13.456 1.00208.48 C ANISOU 810 C LEU A 115 15926 23828 39459 816 -566 2893 C ATOM 811 O LEU A 115 15.788 21.199 13.536 1.00211.86 O ANISOU 811 O LEU A 115 16359 24275 39862 1069 -187 2594 O ATOM 812 CB LEU A 115 15.323 23.853 11.547 1.00209.87 C ANISOU 812 CB LEU A 115 16462 24718 38563 518 -767 3322 C ATOM 813 CG LEU A 115 14.796 24.423 10.227 1.00211.96 C ANISOU 813 CG LEU A 115 17077 25224 38233 342 -1096 3353 C ATOM 814 CD1 LEU A 115 15.770 25.441 9.649 1.00213.00 C ANISOU 814 CD1 LEU A 115 17205 25877 37847 258 -865 3763 C ATOM 815 CD2 LEU A 115 14.521 23.311 9.223 1.00216.23 C ANISOU 815 CD2 LEU A 115 17991 25780 38389 488 -1121 2825 C ATOM 816 N VAL A 116 14.856 23.003 14.502 1.00202.57 N ANISOU 816 N VAL A 116 14864 22874 39230 675 -705 3250 N ATOM 817 CA VAL A 116 15.291 22.645 15.846 1.00194.53 C ANISOU 817 CA VAL A 116 13484 21613 38815 815 -434 3290 C ATOM 818 C VAL A 116 14.416 21.519 16.389 1.00193.31 C ANISOU 818 C VAL A 116 13354 20947 39149 929 -603 2851 C ATOM 819 O VAL A 116 13.396 21.765 17.032 1.00188.44 O ANISOU 819 O VAL A 116 12636 19943 39021 790 -985 2903 O ATOM 820 CB VAL A 116 15.233 23.855 16.803 1.00182.02 C ANISOU 820 CB VAL A 116 11556 19957 37647 618 -553 3812 C ATOM 821 CG1 VAL A 116 15.682 23.456 18.202 1.00173.92 C ANISOU 821 CG1 VAL A 116 10157 18676 37248 772 -271 3843 C ATOM 822 CG2 VAL A 116 16.085 24.996 16.270 1.00177.04 C ANISOU 822 CG2 VAL A 116 10899 19828 36538 497 -389 4253 C ATOM 823 N THR A 117 14.820 20.282 16.118 1.00198.68 N ANISOU 823 N THR A 117 14173 21627 39691 1184 -315 2417 N ATOM 824 CA THR A 117 14.073 19.115 16.570 1.00198.40 C ANISOU 824 CA THR A 117 14180 21125 40078 1317 -429 1966 C ATOM 825 C THR A 117 14.793 18.439 17.733 1.00205.81 C ANISOU 825 C THR A 117 14816 21892 41491 1547 -18 1906 C ATOM 826 O THR A 117 16.023 18.401 17.777 1.00209.08 O ANISOU 826 O THR A 117 15118 22621 41703 1694 448 2015 O ATOM 827 CB THR A 117 13.876 18.094 15.433 1.00196.58 C ANISOU 827 CB THR A 117 14344 20965 39383 1445 -434 1466 C ATOM 828 OG1 THR A 117 15.086 17.352 15.232 1.00204.24 O ANISOU 828 OG1 THR A 117 15328 22200 40073 1705 101 1298 O ATOM 829 CG2 THR A 117 13.499 18.804 14.140 1.00191.82 C ANISOU 829 CG2 THR A 117 14047 20662 38173 1249 -729 1559 C ATOM 830 N GLY A 118 14.021 17.910 18.676 1.00211.56 N ANISOU 830 N GLY A 118 15412 22119 42852 1579 -192 1732 N ATOM 831 CA GLY A 118 14.580 17.229 19.829 1.00215.08 C ANISOU 831 CA GLY A 118 15575 22351 43794 1796 161 1654 C ATOM 832 C GLY A 118 15.433 16.041 19.429 1.00228.70 C ANISOU 832 C GLY A 118 17435 24230 45229 2094 608 1270 C ATOM 833 O GLY A 118 16.245 15.554 20.217 1.00227.39 O ANISOU 833 O GLY A 118 17044 24033 45322 2299 1011 1251 O ATOM 834 N THR A 119 15.245 15.572 18.199 1.00180.50 N ANISOU 834 N THR A 119 21388 21213 25982 -1149 -7399 133 N ATOM 835 CA THR A 119 16.024 14.456 17.677 1.00187.72 C ANISOU 835 CA THR A 119 22375 22218 26731 -943 -7275 -369 C ATOM 836 C THR A 119 17.378 14.932 17.165 1.00188.84 C ANISOU 836 C THR A 119 22391 22620 26741 -806 -6745 -265 C ATOM 837 O THR A 119 18.414 14.355 17.496 1.00189.99 O ANISOU 837 O THR A 119 22412 22640 27136 -703 -6552 -523 O ATOM 838 CB THR A 119 15.282 13.728 16.540 1.00196.48 C ANISOU 838 CB THR A 119 23786 23607 27259 -835 -7493 -691 C ATOM 839 OG1 THR A 119 14.004 13.276 17.008 1.00197.04 O ANISOU 839 OG1 THR A 119 23974 23443 27449 -969 -7988 -799 O ATOM 840 CG2 THR A 119 16.092 12.533 16.057 1.00200.40 C ANISOU 840 CG2 THR A 119 24357 24173 27613 -624 -7372 -1224 C ATOM 841 N ARG A 120 17.364 15.986 16.354 1.00181.54 N ANISOU 841 N ARG A 120 21501 22058 25419 -805 -6511 110 N ATOM 842 CA ARG A 120 18.598 16.557 15.824 1.00175.78 C ANISOU 842 CA ARG A 120 20658 21597 24534 -694 -5993 249 C ATOM 843 C ARG A 120 19.506 17.021 16.957 1.00169.99 C ANISOU 843 C ARG A 120 19614 20575 24400 -772 -5762 450 C ATOM 844 O ARG A 120 20.729 16.951 16.854 1.00173.35 O ANISOU 844 O ARG A 120 19904 21078 24882 -656 -5387 352 O ATOM 845 CB ARG A 120 18.297 17.726 14.883 1.00172.34 C ANISOU 845 CB ARG A 120 20317 21558 23606 -716 -5814 677 C ATOM 846 CG ARG A 120 17.641 17.323 13.572 1.00172.85 C ANISOU 846 CG ARG A 120 20685 21985 23004 -602 -5946 477 C ATOM 847 CD ARG A 120 17.443 18.529 12.667 1.00171.76 C ANISOU 847 CD ARG A 120 20635 22233 22392 -618 -5739 918 C ATOM 848 NE ARG A 120 16.833 18.164 11.392 1.00173.32 N ANISOU 848 NE ARG A 120 21128 22787 21938 -506 -5860 733 N ATOM 849 CZ ARG A 120 16.570 19.028 10.416 1.00173.06 C ANISOU 849 CZ ARG A 120 21234 23127 21395 -490 -5721 1039 C ATOM 850 NH1 ARG A 120 16.014 18.607 9.288 1.00178.00 N ANISOU 850 NH1 ARG A 120 22130 24060 21442 -384 -5852 836 N ATOM 851 NH2 ARG A 120 16.865 20.313 10.565 1.00168.07 N ANISOU 851 NH2 ARG A 120 20475 22559 20824 -580 -5451 1546 N ATOM 852 N ALA A 121 18.896 17.496 18.038 1.00159.66 N ANISOU 852 N ALA A 121 18192 18936 23537 -972 -5989 728 N ATOM 853 CA ALA A 121 19.642 17.928 19.213 1.00148.98 C ANISOU 853 CA ALA A 121 16548 17272 22787 -1067 -5818 925 C ATOM 854 C ALA A 121 20.510 16.792 19.736 1.00147.97 C ANISOU 854 C ALA A 121 16323 16905 22995 -951 -5787 460 C ATOM 855 O ALA A 121 21.722 16.947 19.901 1.00154.13 O ANISOU 855 O ALA A 121 16910 17700 23952 -876 -5416 465 O ATOM 856 CB ALA A 121 18.698 18.421 20.293 1.00142.02 C ANISOU 856 CB ALA A 121 15596 16045 22321 -1298 -6140 1225 C ATOM 857 N ALA A 122 19.885 15.649 19.994 1.00144.71 N ANISOU 857 N ALA A 122 16047 16272 22666 -934 -6177 56 N ATOM 858 CA ALA A 122 20.603 14.479 20.483 1.00150.79 C ANISOU 858 CA ALA A 122 16757 16796 23738 -818 -6196 -415 C ATOM 859 C ALA A 122 21.663 14.024 19.483 1.00161.44 C ANISOU 859 C ALA A 122 18139 18475 24726 -580 -5842 -708 C ATOM 860 O ALA A 122 22.760 13.622 19.869 1.00164.50 O ANISOU 860 O ALA A 122 18362 18746 25394 -479 -5623 -907 O ATOM 861 CB ALA A 122 19.627 13.343 20.779 1.00150.70 C ANISOU 861 CB ALA A 122 16934 16532 23793 -844 -6689 -797 C ATOM 862 N GLY A 123 21.330 14.096 18.198 1.00163.91 N ANISOU 862 N GLY A 123 18663 19201 24415 -490 -5789 -734 N ATOM 863 CA GLY A 123 22.256 13.716 17.146 1.00164.78 C ANISOU 863 CA GLY A 123 18826 19659 24126 -270 -5453 -997 C ATOM 864 C GLY A 123 23.491 14.594 17.114 1.00159.07 C ANISOU 864 C GLY A 123 17869 19089 23483 -237 -4940 -726 C ATOM 865 O GLY A 123 24.614 14.095 17.067 1.00159.38 O ANISOU 865 O GLY A 123 17797 19149 23611 -86 -4674 -997 O ATOM 866 N ILE A 124 23.281 15.907 17.135 1.00155.70 N ANISOU 866 N ILE A 124 17366 18770 23021 -378 -4801 -194 N ATOM 867 CA ILE A 124 24.382 16.863 17.128 1.00153.14 C ANISOU 867 CA ILE A 124 16821 18591 22772 -375 -4313 113 C ATOM 868 C ILE A 124 25.278 16.688 18.353 1.00146.99 C ANISOU 868 C ILE A 124 15753 17448 22649 -399 -4209 55 C ATOM 869 O ILE A 124 26.503 16.644 18.233 1.00149.29 O ANISOU 869 O ILE A 124 15887 17839 22996 -280 -3831 -53 O ATOM 870 CB ILE A 124 23.869 18.316 17.072 1.00159.62 C ANISOU 870 CB ILE A 124 17621 19538 23490 -548 -4232 716 C ATOM 871 CG1 ILE A 124 23.058 18.548 15.794 1.00171.08 C ANISOU 871 CG1 ILE A 124 19357 21379 24264 -511 -4303 787 C ATOM 872 CG2 ILE A 124 25.031 19.294 17.148 1.00122.51 C ANISOU 872 CG2 ILE A 124 12683 14961 18906 -558 -3725 1029 C ATOM 873 CD1 ILE A 124 22.371 19.901 15.738 1.00176.29 C ANISOU 873 CD1 ILE A 124 20034 22143 24806 -679 -4298 1362 C ATOM 874 N ILE A 125 24.661 16.592 19.528 1.00139.75 N ANISOU 874 N ILE A 125 14766 16110 22223 -553 -4547 126 N ATOM 875 CA ILE A 125 25.398 16.395 20.773 1.00136.18 C ANISOU 875 CA ILE A 125 14053 15273 22415 -589 -4503 72 C ATOM 876 C ILE A 125 26.363 15.219 20.658 1.00140.04 C ANISOU 876 C ILE A 125 14513 15736 22959 -373 -4393 -462 C ATOM 877 O ILE A 125 27.548 15.341 20.969 1.00142.79 O ANISOU 877 O ILE A 125 14635 16063 23558 -306 -4060 -479 O ATOM 878 CB ILE A 125 24.445 16.152 21.961 1.00128.19 C ANISOU 878 CB ILE A 125 13038 13800 21868 -766 -4962 106 C ATOM 879 CG1 ILE A 125 23.592 17.394 22.225 1.00128.25 C ANISOU 879 CG1 ILE A 125 13029 13800 21901 -987 -5045 662 C ATOM 880 CG2 ILE A 125 25.230 15.777 23.209 1.00118.89 C ANISOU 880 CG2 ILE A 125 11618 12219 21336 -779 -4937 -19 C ATOM 881 CD1 ILE A 125 22.548 17.198 23.306 1.00125.17 C ANISOU 881 CD1 ILE A 125 12655 12985 21919 -1171 -5506 707 C ATOM 882 N ALA A 126 25.846 14.081 20.206 1.00138.36 N ANISOU 882 N ALA A 126 14533 15528 22511 -265 -4676 -900 N ATOM 883 CA ALA A 126 26.658 12.885 20.016 1.00137.13 C ANISOU 883 CA ALA A 126 14386 15354 22361 -50 -4607 -1436 C ATOM 884 C ALA A 126 27.863 13.164 19.125 1.00137.12 C ANISOU 884 C ALA A 126 14298 15740 22060 117 -4097 -1465 C ATOM 885 O ALA A 126 28.991 12.807 19.462 1.00138.87 O ANISOU 885 O ALA A 126 14333 15881 22550 232 -3863 -1669 O ATOM 886 CB ALA A 126 25.817 11.764 19.434 1.00139.18 C ANISOU 886 CB ALA A 126 14946 15643 22293 35 -4963 -1854 C ATOM 887 N ILE A 127 27.614 13.800 17.985 1.00138.64 N ANISOU 887 N ILE A 127 14629 16353 21693 130 -3928 -1266 N ATOM 888 CA ILE A 127 28.676 14.137 17.046 1.00145.47 C ANISOU 888 CA ILE A 127 15438 17617 22218 273 -3438 -1269 C ATOM 889 C ILE A 127 29.717 15.039 17.700 1.00144.47 C ANISOU 889 C ILE A 127 14987 17430 22474 212 -3056 -957 C ATOM 890 O ILE A 127 30.921 14.823 17.554 1.00145.62 O ANISOU 890 O ILE A 127 14980 17675 22673 354 -2710 -1148 O ATOM 891 CB ILE A 127 28.121 14.842 15.796 1.00150.21 C ANISOU 891 CB ILE A 127 16247 18656 22169 260 -3337 -1024 C ATOM 892 CG1 ILE A 127 27.126 13.937 15.069 1.00156.04 C ANISOU 892 CG1 ILE A 127 17307 19486 22494 330 -3698 -1350 C ATOM 893 CG2 ILE A 127 29.255 15.250 14.868 1.00138.80 C ANISOU 893 CG2 ILE A 127 14735 17613 20389 392 -2807 -1007 C ATOM 894 CD1 ILE A 127 26.532 14.559 13.825 1.00162.29 C ANISOU 894 CD1 ILE A 127 18323 20705 22634 326 -3631 -1135 C ATOM 895 N CYS A 128 29.245 16.051 18.421 1.00140.36 N ANISOU 895 N CYS A 128 14361 16748 22220 -1 -3121 -479 N ATOM 896 CA CYS A 128 30.131 16.980 19.107 1.00136.86 C ANISOU 896 CA CYS A 128 13614 16229 22157 -86 -2784 -145 C ATOM 897 C CYS A 128 31.097 16.243 20.027 1.00139.87 C ANISOU 897 C CYS A 128 13769 16305 23072 -1 -2735 -457 C ATOM 898 O CYS A 128 32.288 16.545 20.054 1.00145.09 O ANISOU 898 O CYS A 128 14210 17066 23854 67 -2331 -438 O ATOM 899 CB CYS A 128 29.322 18.006 19.898 1.00130.83 C ANISOU 899 CB CYS A 128 12790 15259 21660 -336 -2955 368 C ATOM 900 SG CYS A 128 28.339 19.119 18.865 1.00158.56 S ANISOU 900 SG CYS A 128 16523 19147 24576 -442 -2940 820 S ATOM 901 N TRP A 129 30.581 15.271 20.772 1.00140.00 N ANISOU 901 N TRP A 129 13843 15950 23401 -3 -3149 -750 N ATOM 902 CA TRP A 129 31.408 14.481 21.676 1.00143.70 C ANISOU 902 CA TRP A 129 14125 16098 24377 84 -3155 -1071 C ATOM 903 C TRP A 129 32.438 13.641 20.926 1.00143.92 C ANISOU 903 C TRP A 129 14154 16349 24179 343 -2897 -1531 C ATOM 904 O TRP A 129 33.598 13.566 21.328 1.00145.97 O ANISOU 904 O TRP A 129 14173 16549 24738 429 -2623 -1637 O ATOM 905 CB TRP A 129 30.533 13.591 22.560 1.00147.59 C ANISOU 905 CB TRP A 129 14722 16152 25202 22 -3674 -1293 C ATOM 906 CG TRP A 129 29.858 14.339 23.667 1.00144.99 C ANISOU 906 CG TRP A 129 14294 15498 25299 -227 -3885 -881 C ATOM 907 CD1 TRP A 129 28.586 14.824 23.672 1.00137.78 C ANISOU 907 CD1 TRP A 129 13535 14555 24261 -405 -4173 -596 C ATOM 908 CD2 TRP A 129 30.427 14.691 24.934 1.00147.53 C ANISOU 908 CD2 TRP A 129 14334 15478 26241 -326 -3822 -712 C ATOM 909 NE1 TRP A 129 28.324 15.456 24.865 1.00134.18 N ANISOU 909 NE1 TRP A 129 12913 13758 24311 -610 -4290 -259 N ATOM 910 CE2 TRP A 129 29.439 15.387 25.656 1.00141.72 C ANISOU 910 CE2 TRP A 129 13604 14516 25728 -568 -4079 -321 C ATOM 911 CE3 TRP A 129 31.675 14.483 25.526 1.00145.22 C ANISOU 911 CE3 TRP A 129 13786 15052 26338 -232 -3577 -856 C ATOM 912 CZ2 TRP A 129 29.662 15.878 26.942 1.00143.64 C ANISOU 912 CZ2 TRP A 129 13610 14403 26563 -722 -4093 -70 C ATOM 913 CZ3 TRP A 129 31.894 14.970 26.799 1.00140.91 C ANISOU 913 CZ3 TRP A 129 13006 14157 26378 -382 -3596 -607 C ATOM 914 CH2 TRP A 129 30.894 15.658 27.493 1.00143.52 C ANISOU 914 CH2 TRP A 129 13352 14265 26914 -626 -3851 -218 C ATOM 915 N VAL A 130 32.007 13.008 19.839 1.00142.98 N ANISOU 915 N VAL A 130 14305 16488 23534 466 -2988 -1809 N ATOM 916 CA VAL A 130 32.908 12.225 19.002 1.00146.62 C ANISOU 916 CA VAL A 130 14796 17197 23716 713 -2744 -2245 C ATOM 917 C VAL A 130 34.041 13.104 18.482 1.00151.46 C ANISOU 917 C VAL A 130 15214 18147 24187 759 -2188 -2035 C ATOM 918 O VAL A 130 35.209 12.720 18.526 1.00153.07 O ANISOU 918 O VAL A 130 15244 18379 24539 912 -1913 -2290 O ATOM 919 CB VAL A 130 32.162 11.588 17.814 1.00147.78 C ANISOU 919 CB VAL A 130 15281 17612 23256 812 -2914 -2504 C ATOM 920 CG1 VAL A 130 33.139 10.891 16.880 1.00152.99 C ANISOU 920 CG1 VAL A 130 15965 18563 23599 1062 -2615 -2920 C ATOM 921 CG2 VAL A 130 31.103 10.613 18.316 1.00144.66 C ANISOU 921 CG2 VAL A 130 15078 16883 23003 777 -3455 -2766 C ATOM 922 N LEU A 131 33.686 14.291 18.000 1.00152.74 N ANISOU 922 N LEU A 131 15407 18562 24066 624 -2026 -1569 N ATOM 923 CA LEU A 131 34.669 15.251 17.512 1.00154.49 C ANISOU 923 CA LEU A 131 15457 19104 24137 636 -1498 -1315 C ATOM 924 C LEU A 131 35.533 15.767 18.655 1.00154.24 C ANISOU 924 C LEU A 131 15075 18821 24707 558 -1304 -1125 C ATOM 925 O LEU A 131 36.729 15.999 18.482 1.00160.67 O ANISOU 925 O LEU A 131 15687 19801 25556 646 -878 -1162 O ATOM 926 CB LEU A 131 33.974 16.419 16.811 1.00154.76 C ANISOU 926 CB LEU A 131 15627 19428 23747 493 -1414 -837 C ATOM 927 CG LEU A 131 33.130 16.078 15.583 1.00160.83 C ANISOU 927 CG LEU A 131 16742 20497 23870 561 -1568 -969 C ATOM 928 CD1 LEU A 131 32.399 17.310 15.066 1.00162.91 C ANISOU 928 CD1 LEU A 131 17121 20991 23784 402 -1516 -451 C ATOM 929 CD2 LEU A 131 34.000 15.475 14.496 1.00146.04 C ANISOU 929 CD2 LEU A 131 14928 18969 21592 788 -1258 -1352 C ATOM 930 N SER A 132 34.920 15.942 19.822 1.00147.12 N ANISOU 930 N SER A 132 14103 17519 24276 389 -1616 -925 N ATOM 931 CA SER A 132 35.636 16.407 21.005 1.00143.23 C ANISOU 931 CA SER A 132 13288 16747 24387 299 -1482 -739 C ATOM 932 C SER A 132 36.759 15.453 21.398 1.00140.39 C ANISOU 932 C SER A 132 12752 16248 24342 489 -1373 -1194 C ATOM 933 O SER A 132 37.856 15.887 21.749 1.00139.59 O ANISOU 933 O SER A 132 12372 16164 24503 506 -1021 -1113 O ATOM 934 CB SER A 132 34.673 16.591 22.180 1.00137.80 C ANISOU 934 CB SER A 132 12592 15630 24136 94 -1895 -504 C ATOM 935 OG SER A 132 33.750 17.636 21.929 1.00135.75 O ANISOU 935 OG SER A 132 12442 15489 23647 -94 -1952 -28 O ATOM 936 N PHE A 133 36.481 14.155 21.344 1.00139.43 N ANISOU 936 N PHE A 133 12793 15987 24196 632 -1678 -1674 N ATOM 937 CA PHE A 133 37.486 13.150 21.672 1.00144.46 C ANISOU 937 CA PHE A 133 13295 16488 25107 832 -1608 -2143 C ATOM 938 C PHE A 133 38.614 13.134 20.645 1.00151.34 C ANISOU 938 C PHE A 133 14096 17776 25630 1022 -1134 -2329 C ATOM 939 O PHE A 133 39.789 13.157 21.005 1.00155.94 O ANISOU 939 O PHE A 133 14411 18340 26499 1106 -837 -2420 O ATOM 940 CB PHE A 133 36.849 11.763 21.790 1.00147.51 C ANISOU 940 CB PHE A 133 13906 16635 25507 936 -2054 -2611 C ATOM 941 CG PHE A 133 36.286 11.465 23.155 1.00145.19 C ANISOU 941 CG PHE A 133 13570 15821 25776 808 -2461 -2584 C ATOM 942 CD1 PHE A 133 37.105 10.988 24.167 1.00142.40 C ANISOU 942 CD1 PHE A 133 12994 15144 25968 874 -2455 -2782 C ATOM 943 CD2 PHE A 133 34.937 11.649 23.424 1.00145.71 C ANISOU 943 CD2 PHE A 133 13823 15720 25821 622 -2852 -2370 C ATOM 944 CE1 PHE A 133 36.594 10.709 25.421 1.00135.97 C ANISOU 944 CE1 PHE A 133 12152 13847 25664 753 -2826 -2760 C ATOM 945 CE2 PHE A 133 34.421 11.370 24.676 1.00141.41 C ANISOU 945 CE2 PHE A 133 13245 14696 25790 497 -3219 -2353 C ATOM 946 CZ PHE A 133 35.252 10.900 25.675 1.00135.01 C ANISOU 946 CZ PHE A 133 12220 13563 25516 561 -3205 -2545 C ATOM 947 N ALA A 134 38.250 13.084 19.368 1.00151.89 N ANISOU 947 N ALA A 134 14408 18223 25081 1090 -1066 -2394 N ATOM 948 CA ALA A 134 39.233 13.125 18.291 1.00155.02 C ANISOU 948 CA ALA A 134 14767 19045 25087 1256 -611 -2551 C ATOM 949 C ALA A 134 40.192 14.291 18.495 1.00155.93 C ANISOU 949 C ALA A 134 14584 19295 25369 1174 -144 -2187 C ATOM 950 O ALA A 134 41.403 14.100 18.605 1.00160.16 O ANISOU 950 O ALA A 134 14888 19875 26088 1303 167 -2388 O ATOM 951 CB ALA A 134 38.546 13.229 16.944 1.00155.86 C ANISOU 951 CB ALA A 134 15181 19540 24500 1277 -603 -2525 C ATOM 952 N ILE A 135 39.640 15.498 18.543 1.00151.64 N ANISOU 952 N ILE A 135 14044 18815 24756 960 -99 -1655 N ATOM 953 CA ILE A 135 40.434 16.695 18.776 1.00151.89 C ANISOU 953 CA ILE A 135 13807 18958 24944 851 324 -1262 C ATOM 954 C ILE A 135 41.158 16.628 20.119 1.00153.02 C ANISOU 954 C ILE A 135 13628 18731 25783 825 332 -1282 C ATOM 955 O ILE A 135 42.385 16.564 20.166 1.00157.93 O ANISOU 955 O ILE A 135 14011 19436 26558 938 681 -1443 O ATOM 956 CB ILE A 135 39.563 17.967 18.734 1.00145.93 C ANISOU 956 CB ILE A 135 13134 18271 24042 611 298 -675 C ATOM 957 CG1 ILE A 135 38.986 18.172 17.331 1.00147.88 C ANISOU 957 CG1 ILE A 135 13681 18932 23573 641 361 -622 C ATOM 958 CG2 ILE A 135 40.374 19.177 19.160 1.00145.25 C ANISOU 958 CG2 ILE A 135 12756 18234 24200 482 706 -267 C ATOM 959 CD1 ILE A 135 38.175 19.441 17.184 1.00145.17 C ANISOU 959 CD1 ILE A 135 13429 18689 23038 423 361 -51 C ATOM 960 N GLY A 136 40.390 16.636 21.204 1.00148.94 N ANISOU 960 N GLY A 136 13104 17804 25681 677 -55 -1124 N ATOM 961 CA GLY A 136 40.943 16.635 22.548 1.00150.40 C ANISOU 961 CA GLY A 136 13001 17608 26536 626 -89 -1098 C ATOM 962 C GLY A 136 42.041 15.614 22.783 1.00159.12 C ANISOU 962 C GLY A 136 13944 18625 27889 852 9 -1600 C ATOM 963 O GLY A 136 42.925 15.824 23.615 1.00159.12 O ANISOU 963 O GLY A 136 13645 18461 28355 844 181 -1566 O ATOM 964 N LEU A 137 41.985 14.504 22.053 1.00166.73 N ANISOU 964 N LEU A 137 15106 19699 28543 1056 -104 -2071 N ATOM 965 CA LEU A 137 42.971 13.439 22.206 1.00170.13 C ANISOU 965 CA LEU A 137 15415 20052 29176 1291 -37 -2584 C ATOM 966 C LEU A 137 43.817 13.241 20.948 1.00172.55 C ANISOU 966 C LEU A 137 15736 20815 29010 1489 367 -2844 C ATOM 967 O LEU A 137 44.309 12.143 20.686 1.00171.69 O ANISOU 967 O LEU A 137 15657 20713 28864 1714 347 -3344 O ATOM 968 CB LEU A 137 42.289 12.126 22.602 1.00172.01 C ANISOU 968 CB LEU A 137 15852 19956 29546 1381 -538 -2987 C ATOM 969 CG LEU A 137 41.569 12.094 23.953 1.00125.49 C ANISOU 969 CG LEU A 137 9934 13562 24183 1213 -955 -2830 C ATOM 970 CD1 LEU A 137 40.972 10.720 24.208 1.00124.92 C ANISOU 970 CD1 LEU A 137 10080 13199 24187 1322 -1414 -3278 C ATOM 971 CD2 LEU A 137 42.512 12.482 25.080 1.00122.62 C ANISOU 971 CD2 LEU A 137 9212 12959 24417 1173 -786 -2710 C ATOM 972 N THR A 138 43.984 14.309 20.173 1.00172.41 N ANISOU 972 N THR A 138 15702 21174 28631 1403 735 -2503 N ATOM 973 CA THR A 138 44.830 14.269 18.982 1.00173.03 C ANISOU 973 CA THR A 138 15779 21703 28260 1566 1164 -2700 C ATOM 974 C THR A 138 46.301 14.002 19.318 1.00178.15 C ANISOU 974 C THR A 138 16101 22352 29234 1719 1499 -2963 C ATOM 975 O THR A 138 46.993 13.314 18.571 1.00182.86 O ANISOU 975 O THR A 138 16712 23177 29588 1934 1694 -3368 O ATOM 976 CB THR A 138 44.712 15.564 18.149 1.00169.02 C ANISOU 976 CB THR A 138 15317 21582 27320 1421 1502 -2240 C ATOM 977 OG1 THR A 138 43.357 15.737 17.716 1.00166.81 O ANISOU 977 OG1 THR A 138 15357 21336 26688 1308 1191 -2038 O ATOM 978 CG2 THR A 138 45.621 15.505 16.931 1.00171.42 C ANISOU 978 CG2 THR A 138 15619 22346 27166 1586 1956 -2457 C ATOM 979 N PRO A 139 46.791 14.555 20.441 1.00174.85 N ANISOU 979 N PRO A 139 15383 21684 29366 1610 1570 -2736 N ATOM 980 CA PRO A 139 48.163 14.239 20.853 1.00174.27 C ANISOU 980 CA PRO A 139 14990 21579 29644 1761 1848 -3006 C ATOM 981 C PRO A 139 48.375 12.738 21.031 1.00172.65 C ANISOU 981 C PRO A 139 14840 21173 29585 2003 1592 -3600 C ATOM 982 O PRO A 139 49.507 12.268 20.949 1.00172.28 O ANISOU 982 O PRO A 139 14601 21212 29645 2194 1845 -3936 O ATOM 983 CB PRO A 139 48.292 14.951 22.201 1.00169.05 C ANISOU 983 CB PRO A 139 14063 20581 29587 1577 1804 -2657 C ATOM 984 CG PRO A 139 47.348 16.091 22.110 1.00167.90 C ANISOU 984 CG PRO A 139 14039 20494 29262 1319 1763 -2102 C ATOM 985 CD PRO A 139 46.184 15.588 21.299 1.00171.22 C ANISOU 985 CD PRO A 139 14852 21006 29200 1342 1452 -2203 C ATOM 986 N MET A 140 47.297 12.001 21.275 1.00176.45 N ANISOU 986 N MET A 140 15581 21390 30073 1995 1096 -3727 N ATOM 987 CA MET A 140 47.383 10.554 21.428 1.00179.83 C ANISOU 987 CA MET A 140 16101 21611 30615 2216 821 -4285 C ATOM 988 C MET A 140 47.457 9.863 20.071 1.00186.06 C ANISOU 988 C MET A 140 17113 22762 30818 2414 933 -4655 C ATOM 989 O MET A 140 47.818 8.690 19.980 1.00184.44 O ANISOU 989 O MET A 140 16953 22484 30642 2637 831 -5160 O ATOM 990 CB MET A 140 46.192 10.023 22.228 1.00174.64 C ANISOU 990 CB MET A 140 15643 20522 30192 2120 249 -4284 C ATOM 991 CG MET A 140 46.105 10.576 23.640 1.00167.06 C ANISOU 991 CG MET A 140 14473 19162 29840 1935 102 -3963 C ATOM 992 SD MET A 140 44.951 9.660 24.678 1.00149.46 S ANISOU 992 SD MET A 140 12449 16379 27960 1876 -561 -4105 S ATOM 993 CE MET A 140 45.645 8.012 24.578 1.00133.56 C ANISOU 993 CE MET A 140 10476 14262 26009 2207 -660 -4828 C ATOM 994 N LEU A 141 47.114 10.600 19.019 1.00190.47 N ANISOU 994 N LEU A 141 17815 23709 30844 2330 1144 -4400 N ATOM 995 CA LEU A 141 47.171 10.068 17.663 1.00194.34 C ANISOU 995 CA LEU A 141 18523 24577 30740 2499 1281 -4707 C ATOM 996 C LEU A 141 48.617 9.972 17.186 1.00194.23 C ANISOU 996 C LEU A 141 18276 24842 30681 2685 1768 -4966 C ATOM 997 O LEU A 141 48.892 9.431 16.115 1.00196.11 O ANISOU 997 O LEU A 141 18649 25386 30479 2857 1925 -5287 O ATOM 998 CB LEU A 141 46.354 10.941 16.707 1.00196.20 C ANISOU 998 CB LEU A 141 18987 25139 30422 2344 1356 -4332 C ATOM 999 CG LEU A 141 44.880 11.153 17.064 1.00189.98 C ANISOU 999 CG LEU A 141 18432 24127 29623 2149 900 -4042 C ATOM 1000 CD1 LEU A 141 44.217 12.120 16.091 1.00191.46 C ANISOU 1000 CD1 LEU A 141 18812 24670 29264 2007 1032 -3653 C ATOM 1001 CD2 LEU A 141 44.135 9.827 17.099 1.00187.87 C ANISOU 1001 CD2 LEU A 141 18423 23636 29322 2266 429 -4464 C ATOM 1002 N GLY A 142 49.536 10.500 17.989 1.00212.37 N ANISOU 1002 N GLY A 142 22405 15961 42324 -6708 2464 -2210 N ATOM 1003 CA GLY A 142 50.951 10.466 17.663 1.00212.01 C ANISOU 1003 CA GLY A 142 22447 16196 41911 -6217 2838 -1577 C ATOM 1004 C GLY A 142 51.638 11.797 17.900 1.00204.40 C ANISOU 1004 C GLY A 142 20658 15889 41117 -5987 1839 -1211 C ATOM 1005 O GLY A 142 52.851 11.854 18.094 1.00206.06 O ANISOU 1005 O GLY A 142 20735 16438 41121 -5370 2126 -636 O ATOM 1006 N TRP A 143 50.855 12.870 17.883 1.00199.51 N ANISOU 1006 N TRP A 143 19482 15446 40876 -6486 660 -1551 N ATOM 1007 CA TRP A 143 51.377 14.217 18.069 1.00196.35 C ANISOU 1007 CA TRP A 143 18271 15659 40673 -6354 -401 -1265 C ATOM 1008 C TRP A 143 51.701 14.479 19.537 1.00191.48 C ANISOU 1008 C TRP A 143 17006 15425 40323 -5600 -419 -1005 C ATOM 1009 O TRP A 143 50.974 15.203 20.218 1.00190.50 O ANISOU 1009 O TRP A 143 16278 15473 40629 -5720 -1203 -1278 O ATOM 1010 CB TRP A 143 50.354 15.244 17.576 1.00197.44 C ANISOU 1010 CB TRP A 143 18048 15831 41140 -7162 -1647 -1750 C ATOM 1011 CG TRP A 143 50.917 16.613 17.346 1.00201.02 C ANISOU 1011 CG TRP A 143 17821 16853 41704 -7199 -2756 -1474 C ATOM 1012 CD1 TRP A 143 51.551 17.406 18.259 1.00202.03 C ANISOU 1012 CD1 TRP A 143 17190 17540 42034 -6623 -3220 -1097 C ATOM 1013 CD2 TRP A 143 50.879 17.360 16.124 1.00204.62 C ANISOU 1013 CD2 TRP A 143 18292 17374 42081 -7854 -3554 -1560 C ATOM 1014 NE1 TRP A 143 51.921 18.594 17.677 1.00204.16 N ANISOU 1014 NE1 TRP A 143 17004 18218 42351 -6877 -4248 -939 N ATOM 1015 CE2 TRP A 143 51.520 18.591 16.367 1.00205.83 C ANISOU 1015 CE2 TRP A 143 17678 18137 42392 -7631 -4473 -1217 C ATOM 1016 CE3 TRP A 143 50.370 17.104 14.846 1.00206.03 C ANISOU 1016 CE3 TRP A 143 19063 17153 42067 -8607 -3577 -1891 C ATOM 1017 CZ2 TRP A 143 51.665 19.565 15.380 1.00205.30 C ANISOU 1017 CZ2 TRP A 143 17421 18288 42295 -8134 -5405 -1197 C ATOM 1018 CZ3 TRP A 143 50.515 18.072 13.867 1.00206.45 C ANISOU 1018 CZ3 TRP A 143 18928 17423 42091 -9106 -4504 -1870 C ATOM 1019 CH2 TRP A 143 51.157 19.288 14.139 1.00205.92 C ANISOU 1019 CH2 TRP A 143 18093 17964 42182 -8868 -5406 -1525 C ATOM 1020 N ASN A 144 52.793 13.895 20.022 1.00188.69 N ANISOU 1020 N ASN A 144 16774 15204 39715 -4822 441 -479 N ATOM 1021 CA ASN A 144 53.176 14.051 21.423 1.00182.00 C ANISOU 1021 CA ASN A 144 15360 14706 39087 -4056 527 -200 C ATOM 1022 C ASN A 144 54.687 14.109 21.643 1.00183.83 C ANISOU 1022 C ASN A 144 15439 15352 39056 -3295 891 514 C ATOM 1023 O ASN A 144 55.467 13.843 20.730 1.00186.27 O ANISOU 1023 O ASN A 144 16174 15625 38975 -3315 1256 802 O ATOM 1024 CB ASN A 144 52.562 12.936 22.274 1.00177.91 C ANISOU 1024 CB ASN A 144 15185 13780 38633 -3805 1448 -449 C ATOM 1025 CG ASN A 144 53.039 11.557 21.861 1.00178.43 C ANISOU 1025 CG ASN A 144 16130 13426 38240 -3587 2780 -289 C ATOM 1026 OD1 ASN A 144 54.238 11.273 21.873 1.00182.61 O ANISOU 1026 OD1 ASN A 144 16773 14146 38463 -3008 3350 258 O ATOM 1027 ND2 ASN A 144 52.101 10.687 21.502 1.00176.26 N ANISOU 1027 ND2 ASN A 144 16479 12574 37916 -4046 3288 -769 N ATOM 1028 N ASN A 145 55.091 14.457 22.861 1.00180.45 N ANISOU 1028 N ASN A 145 14400 15317 38846 -2625 791 794 N ATOM 1029 CA ASN A 145 56.506 14.532 23.212 1.00178.46 C ANISOU 1029 CA ASN A 145 13943 15481 38381 -1850 1125 1471 C ATOM 1030 C ASN A 145 56.908 13.473 24.235 1.00178.51 C ANISOU 1030 C ASN A 145 14176 15366 38284 -1074 2272 1703 C ATOM 1031 O ASN A 145 57.597 13.770 25.212 1.00161.86 O ANISOU 1031 O ASN A 145 11557 13665 36278 -375 2268 2095 O ATOM 1032 CB ASN A 145 56.858 15.925 23.737 1.00174.78 C ANISOU 1032 CB ASN A 145 12529 15655 38225 -1652 9 1702 C ATOM 1033 CG ASN A 145 56.782 16.992 22.663 1.00178.25 C ANISOU 1033 CG ASN A 145 12749 16288 38691 -2306 -1065 1615 C ATOM 1034 OD1 ASN A 145 56.817 16.692 21.470 1.00181.06 O ANISOU 1034 OD1 ASN A 145 13669 16377 38751 -2777 -890 1539 O ATOM 1035 ND2 ASN A 145 56.683 18.247 23.084 1.00152.64 N ANISOU 1035 ND2 ASN A 145 8683 13512 35800 -2336 -2185 1629 N ATOM 1036 N CYS A 146 56.471 12.238 24.008 1.00178.32 N ANISOU 1036 N CYS A 146 14919 14777 38057 -1200 3250 1458 N ATOM 1037 CA CYS A 146 56.794 11.134 24.906 1.00179.73 C ANISOU 1037 CA CYS A 146 15397 14780 38113 -509 4404 1645 C ATOM 1038 C CYS A 146 58.235 10.671 24.726 1.00185.14 C ANISOU 1038 C CYS A 146 16347 15625 38374 121 5178 2281 C ATOM 1039 O CYS A 146 58.535 9.885 23.828 1.00188.41 O ANISOU 1039 O CYS A 146 17478 15711 38398 -33 5885 2335 O ATOM 1040 CB CYS A 146 55.841 9.958 24.676 1.00182.40 C ANISOU 1040 CB CYS A 146 16489 14449 38365 -877 5196 1164 C ATOM 1041 SG CYS A 146 54.108 10.306 25.060 1.00247.64 S ANISOU 1041 SG CYS A 146 24491 22472 47131 -1533 4469 402 S ATOM 1042 N GLY A 147 59.123 11.164 25.582 1.00184.36 N ANISOU 1042 N GLY A 147 15664 16031 38355 830 5037 2759 N ATOM 1043 CA GLY A 147 60.517 10.762 25.549 1.00185.03 C ANISOU 1043 CA GLY A 147 15930 16307 38067 1496 5754 3382 C ATOM 1044 C GLY A 147 61.388 11.645 24.677 1.00189.65 C ANISOU 1044 C GLY A 147 16284 17284 38491 1378 5115 3735 C ATOM 1045 O GLY A 147 62.412 11.198 24.155 1.00197.84 O ANISOU 1045 O GLY A 147 17701 18339 39133 1667 5738 4150 O ATOM 1046 N GLN A 148 60.979 12.901 24.517 1.00187.14 N ANISOU 1046 N GLN A 148 15345 17279 38480 949 3869 3567 N ATOM 1047 CA GLN A 148 61.765 13.875 23.766 1.00191.10 C ANISOU 1047 CA GLN A 148 15533 18200 38877 832 3137 3892 C ATOM 1048 C GLN A 148 62.855 14.475 24.646 1.00190.04 C ANISOU 1048 C GLN A 148 14736 18661 38809 1626 2956 4463 C ATOM 1049 O GLN A 148 62.583 14.939 25.747 1.00181.36 O ANISOU 1049 O GLN A 148 13029 17814 38067 1929 2559 4430 O ATOM 1050 CB GLN A 148 60.874 14.983 23.198 1.00189.04 C ANISOU 1050 CB GLN A 148 14889 18026 38913 28 1862 3473 C ATOM 1051 CG GLN A 148 59.910 14.512 22.125 1.00193.32 C ANISOU 1051 CG GLN A 148 16082 18019 39352 -812 1943 2947 C ATOM 1052 CD GLN A 148 60.613 13.797 20.985 1.00199.16 C ANISOU 1052 CD GLN A 148 17568 18517 39587 -907 2674 3168 C ATOM 1053 OE1 GLN A 148 61.688 14.208 20.548 1.00202.77 O ANISOU 1053 OE1 GLN A 148 17908 19312 39825 -680 2552 3634 O ATOM 1054 NE2 GLN A 148 60.001 12.725 20.493 1.00200.38 N ANISOU 1054 NE2 GLN A 148 18494 18084 39557 -1249 3435 2830 N ATOM 1055 N PRO A 149 64.097 14.474 24.148 1.00194.01 N ANISOU 1055 N PRO A 149 15357 19392 38967 1958 3240 4987 N ATOM 1056 CA PRO A 149 65.306 14.886 24.858 1.00191.99 C ANISOU 1056 CA PRO A 149 14592 19671 38686 2757 3244 5592 C ATOM 1057 C PRO A 149 65.088 16.028 25.837 1.00187.39 C ANISOU 1057 C PRO A 149 13068 19570 38562 2935 2243 5592 C ATOM 1058 O PRO A 149 64.966 15.746 27.029 1.00187.64 O ANISOU 1058 O PRO A 149 12864 19643 38786 3451 2559 5616 O ATOM 1059 CB PRO A 149 66.240 15.286 23.713 1.00194.02 C ANISOU 1059 CB PRO A 149 14973 20128 38619 2606 3038 5938 C ATOM 1060 CG PRO A 149 65.905 14.285 22.657 1.00197.95 C ANISOU 1060 CG PRO A 149 16382 20047 38782 2126 3763 5687 C ATOM 1061 CD PRO A 149 64.403 14.105 22.756 1.00196.47 C ANISOU 1061 CD PRO A 149 16321 19450 38878 1526 3538 5016 C ATOM 1062 N GLY A 158 64.859 7.224 36.649 1.00223.57 N ANISOU 1062 N GLY A 158 17973 25254 41721 3839 -5800 -7392 N ATOM 1063 CA GLY A 158 63.642 7.984 36.861 1.00215.19 C ANISOU 1063 CA GLY A 158 17151 23732 40879 3197 -5541 -6618 C ATOM 1064 C GLY A 158 62.426 7.099 37.054 1.00206.16 C ANISOU 1064 C GLY A 158 16756 21840 39737 3233 -6240 -6316 C ATOM 1065 O GLY A 158 62.085 6.735 38.180 1.00197.56 O ANISOU 1065 O GLY A 158 15942 20201 38921 3144 -6676 -6236 O ATOM 1066 N CYS A 159 61.771 6.751 35.951 1.00205.55 N ANISOU 1066 N CYS A 159 17008 21742 39352 3364 -6343 -6154 N ATOM 1067 CA CYS A 159 60.580 5.912 36.000 1.00205.71 C ANISOU 1067 CA CYS A 159 17739 21079 39343 3400 -6982 -5871 C ATOM 1068 C CYS A 159 60.847 4.540 35.388 1.00208.86 C ANISOU 1068 C CYS A 159 18451 21519 39387 4103 -7641 -6398 C ATOM 1069 O CYS A 159 60.033 3.624 35.514 1.00210.17 O ANISOU 1069 O CYS A 159 19216 21123 39517 4245 -8281 -6305 O ATOM 1070 CB CYS A 159 59.416 6.593 35.276 1.00203.44 C ANISOU 1070 CB CYS A 159 17653 20638 39008 2943 -6619 -5194 C ATOM 1071 SG CYS A 159 58.991 8.235 35.908 1.00199.32 S ANISOU 1071 SG CYS A 159 16799 20044 38889 2096 -5828 -4521 S ATOM 1072 N GLY A 160 61.992 4.405 34.728 1.00205.57 N ANISOU 1072 N GLY A 160 17626 21770 38711 4538 -7476 -6959 N ATOM 1073 CA GLY A 160 62.360 3.156 34.087 1.00211.00 C ANISOU 1073 CA GLY A 160 18548 22574 39047 5225 -8049 -7500 C ATOM 1074 C GLY A 160 61.800 3.046 32.682 1.00213.01 C ANISOU 1074 C GLY A 160 19002 22996 38937 5321 -7954 -7332 C ATOM 1075 O GLY A 160 60.910 3.804 32.298 1.00208.88 O ANISOU 1075 O GLY A 160 18565 22351 38450 4850 -7565 -6738 O ATOM 1076 N GLU A 161 62.325 2.098 31.912 1.00217.36 N ANISOU 1076 N GLU A 161 19627 23829 39133 5941 -8313 -7863 N ATOM 1077 CA GLU A 161 61.866 1.887 30.544 1.00209.21 C ANISOU 1077 CA GLU A 161 18787 22981 37723 6101 -8271 -7772 C ATOM 1078 C GLU A 161 60.390 1.505 30.514 1.00188.26 C ANISOU 1078 C GLU A 161 16797 19635 35096 5890 -8665 -7249 C ATOM 1079 O GLU A 161 59.906 0.790 31.392 1.00172.82 O ANISOU 1079 O GLU A 161 15275 17062 33325 5924 -9266 -7221 O ATOM 1080 CB GLU A 161 62.712 0.816 29.846 1.00217.47 C ANISOU 1080 CB GLU A 161 19823 24402 38402 6840 -8672 -8480 C ATOM 1081 CG GLU A 161 62.675 -0.549 30.515 1.00218.31 C ANISOU 1081 CG GLU A 161 20397 24020 38532 7290 -9568 -8839 C ATOM 1082 CD GLU A 161 63.515 -1.579 29.783 1.00226.26 C ANISOU 1082 CD GLU A 161 21383 25415 39169 8021 -9944 -9538 C ATOM 1083 OE1 GLU A 161 63.435 -2.775 30.135 1.00228.40 O ANISOU 1083 OE1 GLU A 161 22085 25302 39397 8439 -10694 -9839 O ATOM 1084 OE2 GLU A 161 64.255 -1.192 28.853 1.00231.45 O ANISOU 1084 OE2 GLU A 161 21601 26762 39578 8178 -9484 -9788 O ATOM 1085 N GLY A 162 59.680 1.987 29.500 1.00193.44 N ANISOU 1085 N GLY A 162 17534 20400 35566 5671 -8319 -6842 N ATOM 1086 CA GLY A 162 58.255 1.745 29.383 1.00201.18 C ANISOU 1086 CA GLY A 162 19100 20775 36564 5432 -8616 -6321 C ATOM 1087 C GLY A 162 57.447 2.895 29.951 1.00206.68 C ANISOU 1087 C GLY A 162 19757 21173 37598 4703 -8153 -5623 C ATOM 1088 O GLY A 162 56.609 3.477 29.263 1.00205.83 O ANISOU 1088 O GLY A 162 19754 21043 37408 4383 -7828 -5130 O ATOM 1089 N GLN A 163 57.702 3.222 31.214 1.00208.59 N ANISOU 1089 N GLN A 163 19847 21188 38219 4446 -8127 -5586 N ATOM 1090 CA GLN A 163 57.022 4.333 31.868 1.00204.87 C ANISOU 1090 CA GLN A 163 19302 20439 38100 3750 -7683 -4954 C ATOM 1091 C GLN A 163 57.727 5.654 31.587 1.00196.84 C ANISOU 1091 C GLN A 163 17627 20043 37120 3452 -6799 -4866 C ATOM 1092 O GLN A 163 58.954 5.712 31.510 1.00192.61 O ANISOU 1092 O GLN A 163 16626 20053 36502 3734 -6595 -5367 O ATOM 1093 CB GLN A 163 56.931 4.098 33.376 1.00207.25 C ANISOU 1093 CB GLN A 163 19754 20191 38799 3588 -8054 -4934 C ATOM 1094 CG GLN A 163 56.080 2.904 33.765 1.00207.69 C ANISOU 1094 CG GLN A 163 20499 19544 38868 3776 -8885 -4922 C ATOM 1095 CD GLN A 163 55.961 2.743 35.267 1.00206.47 C ANISOU 1095 CD GLN A 163 20498 18841 39111 3579 -9211 -4865 C ATOM 1096 OE1 GLN A 163 56.636 3.433 36.031 1.00209.02 O ANISOU 1096 OE1 GLN A 163 20389 19344 39685 3372 -8861 -4913 O ATOM 1097 NE2 GLN A 163 55.100 1.829 35.698 1.00202.17 N ANISOU 1097 NE2 GLN A 163 20571 17623 38622 3641 -9880 -4766 N ATOM 1098 N VAL A 164 56.941 6.714 31.435 1.00193.95 N ANISOU 1098 N VAL A 164 17227 19587 36877 2879 -6276 -4230 N ATOM 1099 CA VAL A 164 57.476 8.040 31.153 1.00192.48 C ANISOU 1099 CA VAL A 164 16458 19940 36736 2535 -5402 -4068 C ATOM 1100 C VAL A 164 56.991 9.047 32.187 1.00185.41 C ANISOU 1100 C VAL A 164 15461 18704 36282 1872 -5050 -3540 C ATOM 1101 O VAL A 164 55.835 9.011 32.603 1.00183.94 O ANISOU 1101 O VAL A 164 15704 17910 36273 1554 -5292 -3062 O ATOM 1102 CB VAL A 164 57.053 8.529 29.755 1.00193.83 C ANISOU 1102 CB VAL A 164 16625 20445 36579 2470 -4966 -3786 C ATOM 1103 CG1 VAL A 164 57.542 9.949 29.516 1.00193.64 C ANISOU 1103 CG1 VAL A 164 16027 20929 36619 2070 -4041 -3572 C ATOM 1104 CG2 VAL A 164 57.574 7.586 28.679 1.00200.94 C ANISOU 1104 CG2 VAL A 164 17592 21728 37030 3121 -5269 -4315 C ATOM 1105 N ALA A 165 57.883 9.939 32.605 1.00183.88 N ANISOU 1105 N ALA A 165 14693 18906 36267 1665 -4478 -3641 N ATOM 1106 CA ALA A 165 57.522 11.010 33.524 1.00176.24 C ANISOU 1106 CA ALA A 165 13557 17695 35711 1023 -4052 -3153 C ATOM 1107 C ALA A 165 56.347 11.798 32.961 1.00167.64 C ANISOU 1107 C ALA A 165 12664 16417 34613 543 -3677 -2443 C ATOM 1108 O ALA A 165 56.506 12.578 32.019 1.00165.30 O ANISOU 1108 O ALA A 165 12091 16591 34123 429 -3059 -2300 O ATOM 1109 CB ALA A 165 58.713 11.926 33.761 1.00179.32 C ANISOU 1109 CB ALA A 165 13251 18663 36218 896 -3391 -3387 C ATOM 1110 N CYS A 166 55.168 11.589 33.539 1.00164.60 N ANISOU 1110 N CYS A 166 12764 15344 34435 266 -4053 -2004 N ATOM 1111 CA CYS A 166 53.953 12.222 33.044 1.00162.41 C ANISOU 1111 CA CYS A 166 12733 14825 34151 -164 -3791 -1334 C ATOM 1112 C CYS A 166 53.849 13.672 33.498 1.00157.12 C ANISOU 1112 C CYS A 166 11697 14211 33788 -810 -3045 -853 C ATOM 1113 O CYS A 166 53.199 13.976 34.496 1.00155.23 O ANISOU 1113 O CYS A 166 11603 13464 33913 -1234 -3114 -480 O ATOM 1114 CB CYS A 166 52.715 11.437 33.487 1.00157.48 C ANISOU 1114 CB CYS A 166 12764 13439 33632 -220 -4479 -1061 C ATOM 1115 SG CYS A 166 51.184 11.939 32.669 1.00190.41 S ANISOU 1115 SG CYS A 166 17312 17330 37703 -608 -4296 -330 S ATOM 1116 N LEU A 167 54.492 14.563 32.750 1.00157.00 N ANISOU 1116 N LEU A 167 11214 14818 33623 -882 -2325 -866 N ATOM 1117 CA LEU A 167 54.422 15.992 33.022 1.00160.33 C ANISOU 1117 CA LEU A 167 11274 15350 34294 -1484 -1552 -410 C ATOM 1118 C LEU A 167 53.810 16.697 31.820 1.00168.69 C ANISOU 1118 C LEU A 167 12375 16618 35101 -1671 -1058 29 C ATOM 1119 O LEU A 167 54.350 16.639 30.717 1.00176.25 O ANISOU 1119 O LEU A 167 13173 18106 35689 -1350 -839 -227 O ATOM 1120 CB LEU A 167 55.814 16.549 33.317 1.00163.11 C ANISOU 1120 CB LEU A 167 10979 16265 34730 -1455 -1059 -816 C ATOM 1121 CG LEU A 167 56.627 15.769 34.351 1.00170.90 C ANISOU 1121 CG LEU A 167 11874 17168 35891 -1152 -1550 -1368 C ATOM 1122 CD1 LEU A 167 57.995 16.402 34.555 1.00177.34 C ANISOU 1122 CD1 LEU A 167 12017 18588 36777 -1141 -1004 -1763 C ATOM 1123 CD2 LEU A 167 55.873 15.669 35.670 1.00164.31 C ANISOU 1123 CD2 LEU A 167 11333 15627 35470 -1489 -1925 -1058 C ATOM 1124 N PHE A 168 52.681 17.361 32.045 1.00163.45 N ANISOU 1124 N PHE A 168 11931 15536 34637 -2187 -888 686 N ATOM 1125 CA PHE A 168 51.900 17.957 30.965 1.00165.80 C ANISOU 1125 CA PHE A 168 12362 15926 34707 -2372 -511 1159 C ATOM 1126 C PHE A 168 52.743 18.696 29.926 1.00166.87 C ANISOU 1126 C PHE A 168 12044 16801 34560 -2295 211 1030 C ATOM 1127 O PHE A 168 52.613 18.450 28.728 1.00169.75 O ANISOU 1127 O PHE A 168 12540 17429 34527 -2014 225 990 O ATOM 1128 CB PHE A 168 50.825 18.886 31.531 1.00173.40 C ANISOU 1128 CB PHE A 168 13450 16435 36001 -3027 -235 1872 C ATOM 1129 CG PHE A 168 49.910 19.457 30.487 1.00185.13 C ANISOU 1129 CG PHE A 168 15125 17948 37267 -3219 91 2385 C ATOM 1130 CD1 PHE A 168 49.123 18.625 29.708 1.00186.89 C ANISOU 1130 CD1 PHE A 168 15832 17983 37194 -2924 -406 2423 C ATOM 1131 CD2 PHE A 168 49.833 20.824 30.286 1.00188.74 C ANISOU 1131 CD2 PHE A 168 15282 18619 37811 -3690 893 2828 C ATOM 1132 CE1 PHE A 168 48.281 19.146 28.744 1.00184.40 C ANISOU 1132 CE1 PHE A 168 15692 17703 36670 -3086 -116 2886 C ATOM 1133 CE2 PHE A 168 48.991 21.350 29.325 1.00188.70 C ANISOU 1133 CE2 PHE A 168 15463 18639 37595 -3852 1187 3301 C ATOM 1134 CZ PHE A 168 48.214 20.511 28.553 1.00185.61 C ANISOU 1134 CZ PHE A 168 15549 18069 36906 -3546 679 3329 C ATOM 1135 N GLU A 169 53.604 19.597 30.387 1.00163.79 N ANISOU 1135 N GLU A 169 11121 16741 34372 -2548 811 959 N ATOM 1136 CA GLU A 169 54.411 20.409 29.480 1.00160.95 C ANISOU 1136 CA GLU A 169 10305 17070 33778 -2540 1563 863 C ATOM 1137 C GLU A 169 55.445 19.580 28.723 1.00156.44 C ANISOU 1137 C GLU A 169 9589 17020 32831 -1903 1371 177 C ATOM 1138 O GLU A 169 55.833 19.927 27.607 1.00153.03 O ANISOU 1138 O GLU A 169 8970 17108 32065 -1769 1818 108 O ATOM 1139 CB GLU A 169 55.096 21.554 30.233 1.00168.05 C ANISOU 1139 CB GLU A 169 10663 18176 35010 -2978 2240 931 C ATOM 1140 CG GLU A 169 56.172 21.115 31.217 1.00180.29 C ANISOU 1140 CG GLU A 169 11903 19826 36773 -2781 2012 358 C ATOM 1141 CD GLU A 169 55.603 20.541 32.500 1.00183.42 C ANISOU 1141 CD GLU A 169 12610 19553 37528 -2888 1374 439 C ATOM 1142 OE1 GLU A 169 54.384 20.679 32.729 1.00176.42 O ANISOU 1142 OE1 GLU A 169 12118 18129 36784 -3215 1216 990 O ATOM 1143 OE2 GLU A 169 56.379 19.955 33.284 1.00191.13 O ANISOU 1143 OE2 GLU A 169 13436 20544 38641 -2645 1034 -52 O ATOM 1144 N ASP A 170 55.881 18.481 29.330 1.00158.40 N ANISOU 1144 N ASP A 170 9933 17122 33131 -1509 703 -328 N ATOM 1145 CA ASP A 170 56.917 17.638 28.740 1.00170.98 C ANISOU 1145 CA ASP A 170 11376 19189 34400 -888 473 -1023 C ATOM 1146 C ASP A 170 56.351 16.549 27.831 1.00177.00 C ANISOU 1146 C ASP A 170 12632 19835 34786 -428 -119 -1127 C ATOM 1147 O ASP A 170 57.045 16.053 26.945 1.00189.16 O ANISOU 1147 O ASP A 170 14064 21845 35964 46 -157 -1582 O ATOM 1148 CB ASP A 170 57.783 17.004 29.833 1.00172.84 C ANISOU 1148 CB ASP A 170 11433 19373 34864 -657 69 -1564 C ATOM 1149 CG ASP A 170 58.614 18.025 30.587 1.00173.63 C ANISOU 1149 CG ASP A 170 10955 19743 35275 -1013 689 -1608 C ATOM 1150 OD1 ASP A 170 58.617 19.208 30.187 1.00172.25 O ANISOU 1150 OD1 ASP A 170 10493 19845 35111 -1409 1459 -1263 O ATOM 1151 OD2 ASP A 170 59.268 17.640 31.580 1.00175.13 O ANISOU 1151 OD2 ASP A 170 10981 19867 35693 -893 406 -1992 O ATOM 1152 N VAL A 171 55.092 16.181 28.053 1.00168.66 N ANISOU 1152 N VAL A 171 12110 18157 33818 -571 -578 -714 N ATOM 1153 CA VAL A 171 54.474 15.095 27.297 1.00173.70 C ANISOU 1153 CA VAL A 171 13249 18617 34133 -154 -1196 -805 C ATOM 1154 C VAL A 171 53.444 15.590 26.284 1.00175.87 C ANISOU 1154 C VAL A 171 13777 18855 34190 -360 -927 -257 C ATOM 1155 O VAL A 171 52.950 14.815 25.465 1.00177.35 O ANISOU 1155 O VAL A 171 14338 18984 34062 -23 -1336 -315 O ATOM 1156 CB VAL A 171 53.805 14.066 28.228 1.00174.03 C ANISOU 1156 CB VAL A 171 13773 17963 34386 -66 -2039 -829 C ATOM 1157 CG1 VAL A 171 54.833 13.458 29.171 1.00179.31 C ANISOU 1157 CG1 VAL A 171 14233 18671 35228 211 -2369 -1409 C ATOM 1158 CG2 VAL A 171 52.675 14.713 29.010 1.00169.24 C ANISOU 1158 CG2 VAL A 171 13384 16773 34147 -672 -1963 -165 C ATOM 1159 N VAL A 172 53.122 16.878 26.343 1.00172.86 N ANISOU 1159 N VAL A 172 13193 18509 33976 -908 -244 268 N ATOM 1160 CA VAL A 172 52.154 17.463 25.421 1.00166.01 C ANISOU 1160 CA VAL A 172 12542 17616 32917 -1135 65 817 C ATOM 1161 C VAL A 172 52.766 18.601 24.612 1.00166.83 C ANISOU 1161 C VAL A 172 12197 18347 32846 -1290 954 914 C ATOM 1162 O VAL A 172 53.208 19.602 25.175 1.00171.61 O ANISOU 1162 O VAL A 172 12402 19086 33715 -1683 1534 1055 O ATOM 1163 CB VAL A 172 50.901 17.976 26.159 1.00164.00 C ANISOU 1163 CB VAL A 172 12574 16728 33011 -1689 35 1479 C ATOM 1164 CG1 VAL A 172 49.942 18.639 25.180 1.00166.90 C ANISOU 1164 CG1 VAL A 172 13135 17106 33171 -1917 390 2039 C ATOM 1165 CG2 VAL A 172 50.213 16.836 26.894 1.00162.20 C ANISOU 1165 CG2 VAL A 172 12831 15860 32935 -1545 -843 1406 C ATOM 1166 N PRO A 173 52.789 18.446 23.280 1.00165.44 N ANISOU 1166 N PRO A 173 12090 18552 32217 -983 1067 837 N ATOM 1167 CA PRO A 173 53.367 19.422 22.349 1.00173.29 C ANISOU 1167 CA PRO A 173 12704 20165 32973 -1066 1884 898 C ATOM 1168 C PRO A 173 52.738 20.805 22.481 1.00171.45 C ANISOU 1168 C PRO A 173 12383 19816 32942 -1702 2559 1585 C ATOM 1169 O PRO A 173 51.522 20.919 22.626 1.00164.32 O ANISOU 1169 O PRO A 173 11864 18418 32150 -1972 2375 2103 O ATOM 1170 CB PRO A 173 53.037 18.830 20.977 1.00173.89 C ANISOU 1170 CB PRO A 173 13074 20446 32549 -650 1683 826 C ATOM 1171 CG PRO A 173 52.884 17.379 21.221 1.00171.07 C ANISOU 1171 CG PRO A 173 13077 19777 32144 -194 770 433 C ATOM 1172 CD PRO A 173 52.272 17.259 22.579 1.00162.59 C ANISOU 1172 CD PRO A 173 12196 18048 31535 -511 387 659 C ATOM 1173 N MET A 174 53.566 21.842 22.425 1.00181.13 N ANISOU 1173 N MET A 174 13106 21499 34215 -1934 3337 1576 N ATOM 1174 CA MET A 174 53.084 23.215 22.519 1.00181.99 C ANISOU 1174 CA MET A 174 13093 21549 34507 -2532 4043 2201 C ATOM 1175 C MET A 174 52.440 23.668 21.211 1.00190.84 C ANISOU 1175 C MET A 174 14413 22848 35250 -2546 4383 2592 C ATOM 1176 O MET A 174 51.417 24.353 21.220 1.00193.82 O ANISOU 1176 O MET A 174 15002 22906 35733 -2950 4583 3214 O ATOM 1177 CB MET A 174 54.225 24.158 22.902 1.00179.82 C ANISOU 1177 CB MET A 174 12208 21709 34407 -2771 4768 2034 C ATOM 1178 CG MET A 174 54.772 23.925 24.299 1.00176.20 C ANISOU 1178 CG MET A 174 11531 21043 34375 -2858 4518 1744 C ATOM 1179 SD MET A 174 53.527 24.193 25.575 1.00298.15 S ANISOU 1179 SD MET A 174 27291 35670 50323 -3395 4240 2345 S ATOM 1180 CE MET A 174 53.144 25.922 25.315 1.00138.97 C ANISOU 1180 CE MET A 174 6916 15623 30264 -4045 5234 3033 C ATOM 1181 N ASN A 175 53.040 23.279 20.089 1.00195.46 N ANISOU 1181 N ASN A 175 14932 23944 35390 -2097 4443 2221 N ATOM 1182 CA ASN A 175 52.502 23.611 18.773 1.00198.08 C ANISOU 1182 CA ASN A 175 15460 24487 35316 -2041 4732 2532 C ATOM 1183 C ASN A 175 51.045 23.177 18.626 1.00198.71 C ANISOU 1183 C ASN A 175 16124 24014 35361 -2072 4200 2966 C ATOM 1184 O ASN A 175 50.261 23.817 17.926 1.00195.06 O ANISOU 1184 O ASN A 175 15844 23530 34739 -2272 4520 3470 O ATOM 1185 CB ASN A 175 53.361 22.995 17.664 1.00197.52 C ANISOU 1185 CB ASN A 175 15278 25000 34771 -1477 4710 1983 C ATOM 1186 CG ASN A 175 53.519 21.492 17.812 1.00194.71 C ANISOU 1186 CG ASN A 175 15149 24504 34330 -937 3826 1440 C ATOM 1187 OD1 ASN A 175 53.119 20.910 18.818 1.00188.68 O ANISOU 1187 OD1 ASN A 175 14584 23229 33877 -981 3248 1425 O ATOM 1188 ND2 ASN A 175 54.110 20.857 16.805 1.00199.21 N ANISOU 1188 ND2 ASN A 175 15693 25527 34472 -424 3721 989 N ATOM 1189 N TYR A 176 50.691 22.088 19.299 1.00151.35 N ANISOU 1189 N TYR A 176 17296 20538 19672 4653 -1826 4009 N ATOM 1190 CA TYR A 176 49.321 21.597 19.289 1.00148.47 C ANISOU 1190 CA TYR A 176 17102 20035 19274 4525 -1822 4028 C ATOM 1191 C TYR A 176 48.426 22.446 20.181 1.00139.76 C ANISOU 1191 C TYR A 176 15838 19009 18257 4315 -1789 3872 C ATOM 1192 O TYR A 176 47.295 22.759 19.818 1.00139.64 O ANISOU 1192 O TYR A 176 15827 18879 18353 4189 -1759 3830 O ATOM 1193 CB TYR A 176 49.271 20.140 19.748 1.00158.60 C ANISOU 1193 CB TYR A 176 18658 21299 20303 4588 -1880 4147 C ATOM 1194 CG TYR A 176 47.870 19.637 19.998 1.00170.50 C ANISOU 1194 CG TYR A 176 20329 22710 21743 4421 -1879 4154 C ATOM 1195 CD1 TYR A 176 47.166 18.961 19.010 1.00176.10 C ANISOU 1195 CD1 TYR A 176 21259 23214 22438 4426 -1880 4258 C ATOM 1196 CD2 TYR A 176 47.248 19.842 21.223 1.00176.37 C ANISOU 1196 CD2 TYR A 176 21004 23578 22430 4247 -1874 4052 C ATOM 1197 CE1 TYR A 176 45.883 18.503 19.236 1.00178.90 C ANISOU 1197 CE1 TYR A 176 21756 23495 22723 4261 -1880 4264 C ATOM 1198 CE2 TYR A 176 45.967 19.390 21.456 1.00180.03 C ANISOU 1198 CE2 TYR A 176 21604 23975 22825 4083 -1867 4051 C ATOM 1199 CZ TYR A 176 45.289 18.721 20.462 1.00179.88 C ANISOU 1199 CZ TYR A 176 21798 23757 22792 4090 -1872 4159 C ATOM 1200 OH TYR A 176 44.011 18.271 20.701 1.00179.27 O ANISOU 1200 OH TYR A 176 21849 23628 22638 3913 -1867 4157 O ATOM 1201 N MET A 177 48.937 22.806 21.355 1.00134.25 N ANISOU 1201 N MET A 177 14995 18511 17504 4279 -1796 3782 N ATOM 1202 CA MET A 177 48.166 23.565 22.335 1.00132.11 C ANISOU 1202 CA MET A 177 14570 18334 17290 4082 -1759 3620 C ATOM 1203 C MET A 177 47.941 25.011 21.905 1.00131.66 C ANISOU 1203 C MET A 177 14275 18249 17500 4007 -1707 3485 C ATOM 1204 O MET A 177 47.082 25.703 22.453 1.00130.11 O ANISOU 1204 O MET A 177 13959 18080 17397 3848 -1668 3342 O ATOM 1205 CB MET A 177 48.864 23.534 23.696 1.00135.30 C ANISOU 1205 CB MET A 177 14896 18963 17548 4063 -1784 3568 C ATOM 1206 CG MET A 177 48.877 22.162 24.358 1.00137.38 C ANISOU 1206 CG MET A 177 15399 19259 17541 4091 -1847 3682 C ATOM 1207 SD MET A 177 47.213 21.577 24.708 1.00149.63 S ANISOU 1207 SD MET A 177 17122 20725 19007 3888 -1828 3665 S ATOM 1208 CE MET A 177 46.546 22.986 25.591 1.00210.10 C ANISOU 1208 CE MET A 177 24485 28520 26822 3669 -1749 3421 C ATOM 1209 N VAL A 178 48.715 25.464 20.926 1.00132.97 N ANISOU 1209 N VAL A 178 14376 18360 17786 4120 -1707 3526 N ATOM 1210 CA VAL A 178 48.644 26.849 20.479 1.00133.77 C ANISOU 1210 CA VAL A 178 14267 18428 18134 4055 -1673 3410 C ATOM 1211 C VAL A 178 47.887 26.996 19.161 1.00141.26 C ANISOU 1211 C VAL A 178 15287 19149 19238 4047 -1666 3460 C ATOM 1212 O VAL A 178 46.853 27.660 19.099 1.00140.68 O ANISOU 1212 O VAL A 178 15140 18993 19319 3922 -1646 3364 O ATOM 1213 CB VAL A 178 50.053 27.461 20.339 1.00123.75 C ANISOU 1213 CB VAL A 178 12845 17273 16901 4149 -1679 3403 C ATOM 1214 CG1 VAL A 178 49.972 28.840 19.713 1.00117.77 C ANISOU 1214 CG1 VAL A 178 11908 16447 16393 4079 -1654 3305 C ATOM 1215 CG2 VAL A 178 50.738 27.524 21.694 1.00121.11 C ANISOU 1215 CG2 VAL A 178 12404 17173 16440 4130 -1688 3333 C ATOM 1216 N TYR A 179 48.410 26.372 18.111 1.00150.32 N ANISOU 1216 N TYR A 179 16574 20198 20343 4181 -1686 3608 N ATOM 1217 CA TYR A 179 47.814 26.470 16.782 1.00161.12 C ANISOU 1217 CA TYR A 179 18023 21352 21842 4174 -1685 3673 C ATOM 1218 C TYR A 179 46.517 25.674 16.669 1.00162.57 C ANISOU 1218 C TYR A 179 18394 21406 21970 4104 -1691 3724 C ATOM 1219 O TYR A 179 45.435 26.245 16.534 1.00160.08 O ANISOU 1219 O TYR A 179 18020 21003 21802 3979 -1680 3650 O ATOM 1220 CB TYR A 179 48.805 25.996 15.718 1.00168.23 C ANISOU 1220 CB TYR A 179 19023 22202 22694 4332 -1696 3809 C ATOM 1221 CG TYR A 179 50.040 26.858 15.606 1.00175.32 C ANISOU 1221 CG TYR A 179 19729 23219 23666 4385 -1687 3763 C ATOM 1222 CD1 TYR A 179 50.157 27.809 14.600 1.00177.60 C ANISOU 1222 CD1 TYR A 179 19924 23414 24142 4349 -1679 3746 C ATOM 1223 CD2 TYR A 179 51.088 26.724 16.507 1.00180.21 C ANISOU 1223 CD2 TYR A 179 20262 24049 24162 4460 -1693 3739 C ATOM 1224 CE1 TYR A 179 51.286 28.601 14.494 1.00181.18 C ANISOU 1224 CE1 TYR A 179 20206 23984 24649 4377 -1672 3704 C ATOM 1225 CE2 TYR A 179 52.219 27.510 16.408 1.00183.07 C ANISOU 1225 CE2 TYR A 179 20441 24535 24582 4496 -1685 3697 C ATOM 1226 CZ TYR A 179 52.313 28.446 15.401 1.00183.47 C ANISOU 1226 CZ TYR A 179 20405 24494 24813 4450 -1671 3678 C ATOM 1227 OH TYR A 179 53.438 29.232 15.302 1.00184.45 O ANISOU 1227 OH TYR A 179 20351 24749 24983 4466 -1664 3636 O ATOM 1228 N PHE A 180 46.637 24.352 16.723 1.00163.21 N ANISOU 1228 N PHE A 180 18702 21476 21836 4185 -1712 3850 N ATOM 1229 CA PHE A 180 45.494 23.464 16.549 1.00160.00 C ANISOU 1229 CA PHE A 180 18506 20944 21343 4118 -1722 3921 C ATOM 1230 C PHE A 180 44.445 23.632 17.646 1.00151.89 C ANISOU 1230 C PHE A 180 17413 19996 20303 3948 -1706 3802 C ATOM 1231 O PHE A 180 43.260 23.785 17.360 1.00152.73 O ANISOU 1231 O PHE A 180 17530 20003 20498 3830 -1696 3773 O ATOM 1232 CB PHE A 180 45.962 22.008 16.488 1.00166.33 C ANISOU 1232 CB PHE A 180 19575 21724 21900 4245 -1755 4076 C ATOM 1233 CG PHE A 180 44.849 21.017 16.310 1.00173.77 C ANISOU 1233 CG PHE A 180 20761 22537 22727 4169 -1770 4160 C ATOM 1234 CD1 PHE A 180 44.438 20.636 15.043 1.00176.33 C ANISOU 1234 CD1 PHE A 180 21249 22664 23086 4189 -1775 4268 C ATOM 1235 CD2 PHE A 180 44.219 20.458 17.408 1.00178.60 C ANISOU 1235 CD2 PHE A 180 21445 23230 23183 4062 -1781 4133 C ATOM 1236 CE1 PHE A 180 43.413 19.722 14.876 1.00178.56 C ANISOU 1236 CE1 PHE A 180 21759 22832 23253 4106 -1791 4348 C ATOM 1237 CE2 PHE A 180 43.194 19.545 17.249 1.00181.38 C ANISOU 1237 CE2 PHE A 180 22026 23473 23417 3974 -1796 4211 C ATOM 1238 CZ PHE A 180 42.790 19.176 15.982 1.00180.92 C ANISOU 1238 CZ PHE A 180 22127 23218 23397 3997 -1802 4320 C ATOM 1239 N ASN A 181 44.887 23.608 18.898 1.00144.67 N ANISOU 1239 N ASN A 181 16424 19269 19275 3933 -1704 3731 N ATOM 1240 CA ASN A 181 43.974 23.628 20.035 1.00138.83 C ANISOU 1240 CA ASN A 181 15640 18629 18479 3767 -1684 3619 C ATOM 1241 C ASN A 181 43.344 24.997 20.311 1.00139.00 C ANISOU 1241 C ASN A 181 15398 18685 18731 3639 -1639 3428 C ATOM 1242 O ASN A 181 42.123 25.133 20.311 1.00144.59 O ANISOU 1242 O ASN A 181 16092 19339 19509 3511 -1618 3364 O ATOM 1243 CB ASN A 181 44.670 23.101 21.291 1.00138.03 C ANISOU 1243 CB ASN A 181 15565 18717 18163 3783 -1704 3614 C ATOM 1244 CG ASN A 181 43.718 22.941 22.460 1.00136.85 C ANISOU 1244 CG ASN A 181 15411 18675 17912 3597 -1683 3514 C ATOM 1245 OD1 ASN A 181 43.573 23.843 23.286 1.00136.63 O ANISOU 1245 OD1 ASN A 181 15169 18779 17966 3492 -1643 3346 O ATOM 1246 ND2 ASN A 181 43.065 21.788 22.538 1.00135.62 N ANISOU 1246 ND2 ASN A 181 15496 18465 17569 3547 -1708 3614 N ATOM 1247 N PHE A 182 44.179 26.003 20.550 1.00138.37 N ANISOU 1247 N PHE A 182 15110 18697 18766 3673 -1627 3332 N ATOM 1248 CA PHE A 182 43.686 27.331 20.894 1.00138.63 C ANISOU 1248 CA PHE A 182 14898 18762 19012 3562 -1588 3140 C ATOM 1249 C PHE A 182 43.159 28.103 19.691 1.00137.34 C ANISOU 1249 C PHE A 182 14675 18408 19101 3561 -1593 3133 C ATOM 1250 O PHE A 182 41.951 28.269 19.530 1.00137.56 O ANISOU 1250 O PHE A 182 14688 18350 19228 3465 -1582 3078 O ATOM 1251 CB PHE A 182 44.763 28.147 21.610 1.00142.58 C ANISOU 1251 CB PHE A 182 15210 19426 19538 3583 -1578 3040 C ATOM 1252 CG PHE A 182 44.354 29.567 21.893 1.00143.74 C ANISOU 1252 CG PHE A 182 15116 19586 19913 3482 -1542 2841 C ATOM 1253 CD1 PHE A 182 43.202 29.839 22.612 1.00143.31 C ANISOU 1253 CD1 PHE A 182 14986 19565 19902 3339 -1502 2692 C ATOM 1254 CD2 PHE A 182 45.130 30.629 21.456 1.00143.86 C ANISOU 1254 CD2 PHE A 182 14982 19583 20094 3526 -1549 2797 C ATOM 1255 CE1 PHE A 182 42.823 31.143 22.877 1.00143.11 C ANISOU 1255 CE1 PHE A 182 14742 19543 20092 3260 -1471 2498 C ATOM 1256 CE2 PHE A 182 44.757 31.936 21.719 1.00143.70 C ANISOU 1256 CE2 PHE A 182 14758 19557 20284 3435 -1525 2612 C ATOM 1257 CZ PHE A 182 43.600 32.193 22.431 1.00142.33 C ANISOU 1257 CZ PHE A 182 14512 19405 20161 3311 -1486 2460 C ATOM 1258 N PHE A 183 44.074 28.584 18.857 1.00140.77 N ANISOU 1258 N PHE A 183 15071 18783 19634 3662 -1614 3188 N ATOM 1259 CA PHE A 183 43.712 29.423 17.719 1.00147.47 C ANISOU 1259 CA PHE A 183 15859 19453 20722 3654 -1630 3183 C ATOM 1260 C PHE A 183 42.544 28.876 16.901 1.00146.76 C ANISOU 1260 C PHE A 183 15915 19185 20662 3617 -1647 3266 C ATOM 1261 O PHE A 183 41.643 29.624 16.523 1.00147.09 O ANISOU 1261 O PHE A 183 15864 19118 20906 3542 -1655 3190 O ATOM 1262 CB PHE A 183 44.923 29.658 16.809 1.00153.30 C ANISOU 1262 CB PHE A 183 16602 20152 21493 3769 -1653 3278 C ATOM 1263 CG PHE A 183 45.889 30.684 17.334 1.00159.13 C ANISOU 1263 CG PHE A 183 17138 21023 22301 3769 -1642 3167 C ATOM 1264 CD1 PHE A 183 45.524 32.018 17.414 1.00163.41 C ANISOU 1264 CD1 PHE A 183 17493 21528 23068 3679 -1640 3015 C ATOM 1265 CD2 PHE A 183 47.166 30.320 17.732 1.00158.96 C ANISOU 1265 CD2 PHE A 183 17114 21161 22121 3861 -1640 3214 C ATOM 1266 CE1 PHE A 183 46.408 32.966 17.890 1.00164.64 C ANISOU 1266 CE1 PHE A 183 17475 21800 23279 3666 -1633 2913 C ATOM 1267 CE2 PHE A 183 48.053 31.265 18.207 1.00160.10 C ANISOU 1267 CE2 PHE A 183 17072 21437 22322 3848 -1632 3114 C ATOM 1268 CZ PHE A 183 47.673 32.588 18.286 1.00162.63 C ANISOU 1268 CZ PHE A 183 17219 21716 22857 3743 -1627 2964 C ATOM 1269 N ALA A 184 42.561 27.574 16.636 1.00143.06 N ANISOU 1269 N ALA A 184 15677 18686 19992 3669 -1659 3422 N ATOM 1270 CA ALA A 184 41.562 26.965 15.763 1.00139.17 C ANISOU 1270 CA ALA A 184 15351 18023 19505 3635 -1679 3524 C ATOM 1271 C ALA A 184 40.345 26.412 16.508 1.00136.10 C ANISOU 1271 C ALA A 184 15010 17677 19026 3510 -1662 3476 C ATOM 1272 O ALA A 184 39.205 26.755 16.186 1.00135.60 O ANISOU 1272 O ALA A 184 14899 17524 19099 3416 -1666 3427 O ATOM 1273 CB ALA A 184 42.200 25.885 14.900 1.00139.04 C ANISOU 1273 CB ALA A 184 15576 17920 19331 3754 -1702 3722 C ATOM 1274 N CYS A 185 40.589 25.556 17.496 1.00132.75 N ANISOU 1274 N CYS A 185 14680 17393 18368 3505 -1648 3490 N ATOM 1275 CA CYS A 185 39.507 24.865 18.196 1.00127.45 C ANISOU 1275 CA CYS A 185 14090 16773 17562 3374 -1633 3464 C ATOM 1276 C CYS A 185 38.851 25.690 19.302 1.00132.37 C ANISOU 1276 C CYS A 185 14484 17540 18272 3240 -1587 3249 C ATOM 1277 O CYS A 185 37.816 25.299 19.839 1.00138.01 O ANISOU 1277 O CYS A 185 15225 18304 18910 3107 -1565 3199 O ATOM 1278 CB CYS A 185 40.002 23.537 18.776 1.00124.01 C ANISOU 1278 CB CYS A 185 13882 16415 16822 3412 -1649 3581 C ATOM 1279 SG CYS A 185 40.526 22.316 17.551 1.00165.43 S ANISOU 1279 SG CYS A 185 19444 21483 21929 3558 -1699 3827 S ATOM 1280 N VAL A 186 39.450 26.827 19.640 1.00137.66 N ANISOU 1280 N VAL A 186 14931 18279 19096 3266 -1569 3118 N ATOM 1281 CA VAL A 186 38.917 27.681 20.699 1.00144.64 C ANISOU 1281 CA VAL A 186 15591 19297 20069 3149 -1520 2898 C ATOM 1282 C VAL A 186 38.681 29.116 20.231 1.00146.17 C ANISOU 1282 C VAL A 186 15559 19404 20576 3150 -1518 2765 C ATOM 1283 O VAL A 186 37.563 29.626 20.318 1.00143.24 O ANISOU 1283 O VAL A 186 15069 19006 20349 3058 -1499 2638 O ATOM 1284 CB VAL A 186 39.838 27.695 21.940 1.00152.34 C ANISOU 1284 CB VAL A 186 16507 20481 20895 3148 -1496 2828 C ATOM 1285 CG1 VAL A 186 39.327 28.692 22.972 1.00101.13 C ANISOU 1285 CG1 VAL A 186 9782 14126 14519 3025 -1438 2586 C ATOM 1286 CG2 VAL A 186 39.940 26.301 22.541 1.00100.72 C ANISOU 1286 CG2 VAL A 186 10192 14031 14047 3127 -1509 2944 C ATOM 1287 N LEU A 187 39.735 29.762 19.741 1.00147.77 N ANISOU 1287 N LEU A 187 15703 19562 20879 3253 -1542 2791 N ATOM 1288 CA LEU A 187 39.644 31.152 19.304 1.00148.48 C ANISOU 1288 CA LEU A 187 15599 19561 21257 3253 -1554 2674 C ATOM 1289 C LEU A 187 38.645 31.333 18.165 1.00144.85 C ANISOU 1289 C LEU A 187 15166 18893 20978 3240 -1594 2720 C ATOM 1290 O LEU A 187 37.807 32.234 18.205 1.00142.74 O ANISOU 1290 O LEU A 187 14737 18575 20922 3182 -1594 2574 O ATOM 1291 CB LEU A 187 41.019 31.685 18.894 1.00151.41 C ANISOU 1291 CB LEU A 187 15935 19924 21670 3353 -1578 2722 C ATOM 1292 CG LEU A 187 41.064 33.148 18.443 1.00154.52 C ANISOU 1292 CG LEU A 187 16147 20217 22345 3346 -1601 2611 C ATOM 1293 CD1 LEU A 187 40.494 34.058 19.518 1.00156.14 C ANISOU 1293 CD1 LEU A 187 16147 20515 22664 3252 -1559 2372 C ATOM 1294 CD2 LEU A 187 42.482 33.568 18.076 1.00154.55 C ANISOU 1294 CD2 LEU A 187 16131 20240 22351 3425 -1621 2669 C ATOM 1295 N VAL A 188 38.736 30.472 17.155 1.00144.06 N ANISOU 1295 N VAL A 188 15271 18671 20792 3297 -1632 2920 N ATOM 1296 CA VAL A 188 37.830 30.537 16.012 1.00145.43 C ANISOU 1296 CA VAL A 188 15496 18647 21114 3279 -1678 2990 C ATOM 1297 C VAL A 188 36.363 30.390 16.424 1.00144.35 C ANISOU 1297 C VAL A 188 15312 18528 21008 3164 -1660 2897 C ATOM 1298 O VAL A 188 35.529 31.216 16.050 1.00142.68 O ANISOU 1298 O VAL A 188 14966 18217 21029 3128 -1686 2808 O ATOM 1299 CB VAL A 188 38.185 29.487 14.935 1.00147.16 C ANISOU 1299 CB VAL A 188 15970 18749 21195 3348 -1713 3224 C ATOM 1300 CG1 VAL A 188 37.105 29.433 13.865 1.00149.22 C ANISOU 1300 CG1 VAL A 188 16296 18822 21578 3301 -1760 3296 C ATOM 1301 CG2 VAL A 188 39.540 29.798 14.317 1.00146.29 C ANISOU 1301 CG2 VAL A 188 15876 18605 21102 3458 -1732 3303 C ATOM 1302 N PRO A 189 36.039 29.335 17.191 1.00142.11 N ANISOU 1302 N PRO A 189 15137 18372 20486 3104 -1620 2917 N ATOM 1303 CA PRO A 189 34.656 29.180 17.656 1.00134.27 C ANISOU 1303 CA PRO A 189 14087 17427 19502 2977 -1593 2817 C ATOM 1304 C PRO A 189 34.179 30.407 18.425 1.00126.72 C ANISOU 1304 C PRO A 189 12847 16552 18750 2923 -1557 2566 C ATOM 1305 O PRO A 189 33.099 30.917 18.143 1.00128.86 O ANISOU 1305 O PRO A 189 12999 16755 19207 2875 -1569 2478 O ATOM 1306 CB PRO A 189 34.736 27.968 18.587 1.00136.57 C ANISOU 1306 CB PRO A 189 14532 17881 19478 2918 -1552 2863 C ATOM 1307 CG PRO A 189 35.896 27.189 18.084 1.00140.50 C ANISOU 1307 CG PRO A 189 15247 18327 19811 3035 -1585 3061 C ATOM 1308 CD PRO A 189 36.889 28.207 17.612 1.00142.24 C ANISOU 1308 CD PRO A 189 15344 18487 20213 3147 -1605 3039 C ATOM 1309 N LEU A 190 34.978 30.873 19.380 1.00120.25 N ANISOU 1309 N LEU A 190 11919 15874 17896 2936 -1515 2449 N ATOM 1310 CA LEU A 190 34.624 32.053 20.162 1.00116.83 C ANISOU 1310 CA LEU A 190 11226 15519 17646 2888 -1474 2199 C ATOM 1311 C LEU A 190 34.399 33.270 19.272 1.00119.56 C ANISOU 1311 C LEU A 190 11434 15676 18317 2945 -1530 2144 C ATOM 1312 O LEU A 190 33.626 34.162 19.615 1.00124.34 O ANISOU 1312 O LEU A 190 11840 16284 19120 2905 -1514 1948 O ATOM 1313 CB LEU A 190 35.702 32.352 21.204 1.00116.59 C ANISOU 1313 CB LEU A 190 11129 15655 17517 2897 -1430 2111 C ATOM 1314 CG LEU A 190 35.780 31.395 22.394 1.00119.49 C ANISOU 1314 CG LEU A 190 11576 16237 17587 2812 -1372 2101 C ATOM 1315 CD1 LEU A 190 37.029 31.666 23.218 1.00123.70 C ANISOU 1315 CD1 LEU A 190 12065 16912 18023 2841 -1351 2058 C ATOM 1316 CD2 LEU A 190 34.529 31.505 23.253 1.00103.09 C ANISOU 1316 CD2 LEU A 190 9370 14280 15521 2669 -1306 1908 C ATOM 1317 N LEU A 191 35.080 33.305 18.132 1.00119.90 N ANISOU 1317 N LEU A 191 11587 15556 18414 3037 -1599 2313 N ATOM 1318 CA LEU A 191 34.901 34.388 17.172 1.00123.09 C ANISOU 1318 CA LEU A 191 11897 15761 19109 3081 -1670 2293 C ATOM 1319 C LEU A 191 33.624 34.178 16.369 1.00125.40 C ANISOU 1319 C LEU A 191 12218 15916 19513 3048 -1718 2343 C ATOM 1320 O LEU A 191 32.978 35.137 15.947 1.00127.51 O ANISOU 1320 O LEU A 191 12347 16057 20046 3053 -1769 2251 O ATOM 1321 CB LEU A 191 36.108 34.490 16.239 1.00124.99 C ANISOU 1321 CB LEU A 191 12249 15891 19350 3171 -1724 2457 C ATOM 1322 CG LEU A 191 37.416 34.939 16.893 1.00128.84 C ANISOU 1322 CG LEU A 191 12675 16500 19778 3207 -1692 2401 C ATOM 1323 CD1 LEU A 191 38.564 34.885 15.896 1.00134.60 C ANISOU 1323 CD1 LEU A 191 13523 17138 20481 3288 -1740 2576 C ATOM 1324 CD2 LEU A 191 37.272 36.336 17.480 1.00125.32 C ANISOU 1324 CD2 LEU A 191 11998 16065 19554 3178 -1686 2171 C ATOM 1325 N LEU A 192 33.266 32.915 16.162 1.00126.27 N ANISOU 1325 N LEU A 192 12512 16049 19417 3014 -1709 2491 N ATOM 1326 CA LEU A 192 32.016 32.573 15.495 1.00128.87 C ANISOU 1326 CA LEU A 192 12876 16278 19811 2961 -1748 2543 C ATOM 1327 C LEU A 192 30.841 32.824 16.431 1.00127.55 C ANISOU 1327 C LEU A 192 12520 16241 19703 2869 -1695 2332 C ATOM 1328 O LEU A 192 29.860 33.463 16.052 1.00122.42 O ANISOU 1328 O LEU A 192 11732 15501 19280 2856 -1737 2249 O ATOM 1329 CB LEU A 192 32.027 31.111 15.043 1.00131.00 C ANISOU 1329 CB LEU A 192 13417 16539 19819 2940 -1750 2763 C ATOM 1330 CG LEU A 192 33.043 30.737 13.962 1.00129.19 C ANISOU 1330 CG LEU A 192 13389 16169 19527 3031 -1800 2979 C ATOM 1331 CD1 LEU A 192 33.076 29.231 13.748 1.00127.70 C ANISOU 1331 CD1 LEU A 192 13472 15995 19054 3012 -1789 3167 C ATOM 1332 CD2 LEU A 192 32.735 31.463 12.661 1.00125.46 C ANISOU 1332 CD2 LEU A 192 12893 15474 19302 3057 -1892 3040 C ATOM 1333 N MET A 193 30.951 32.318 17.656 1.00130.77 N ANISOU 1333 N MET A 193 12919 16864 19903 2805 -1606 2245 N ATOM 1334 CA MET A 193 29.924 32.523 18.668 1.00136.25 C ANISOU 1334 CA MET A 193 13430 17717 20621 2703 -1538 2028 C ATOM 1335 C MET A 193 29.646 34.007 18.859 1.00139.22 C ANISOU 1335 C MET A 193 13535 18052 21310 2741 -1544 1801 C ATOM 1336 O MET A 193 28.510 34.457 18.721 1.00148.57 O ANISOU 1336 O MET A 193 14568 19202 22679 2715 -1558 1686 O ATOM 1337 CB MET A 193 30.345 31.896 19.997 1.00102.82 C ANISOU 1337 CB MET A 193 9232 13721 16114 2627 -1445 1966 C ATOM 1338 CG MET A 193 30.616 30.402 19.921 1.00126.62 C ANISOU 1338 CG MET A 193 12526 16776 18807 2589 -1445 2180 C ATOM 1339 SD MET A 193 30.942 29.697 21.545 1.00115.16 S ANISOU 1339 SD MET A 193 11110 15603 17041 2478 -1352 2097 S ATOM 1340 CE MET A 193 29.468 30.207 22.417 1.00199.25 C ANISOU 1340 CE MET A 193 21506 26409 27790 2327 -1273 1822 C ATOM 1341 N LEU A 194 30.692 34.762 19.178 1.00135.13 N ANISOU 1341 N LEU A 194 12958 17537 20848 2806 -1537 1737 N ATOM 1342 CA LEU A 194 30.567 36.204 19.340 1.00134.94 C ANISOU 1342 CA LEU A 194 12704 17452 21116 2849 -1551 1528 C ATOM 1343 C LEU A 194 29.910 36.819 18.110 1.00134.86 C ANISOU 1343 C LEU A 194 12654 17201 21384 2908 -1660 1575 C ATOM 1344 O LEU A 194 29.074 37.714 18.224 1.00137.77 O ANISOU 1344 O LEU A 194 12823 17527 21996 2917 -1674 1390 O ATOM 1345 CB LEU A 194 31.936 36.839 19.579 1.00138.25 C ANISOU 1345 CB LEU A 194 13118 17872 21538 2909 -1551 1514 C ATOM 1346 CG LEU A 194 31.950 38.360 19.740 1.00142.27 C ANISOU 1346 CG LEU A 194 13418 18301 22336 2950 -1572 1307 C ATOM 1347 CD1 LEU A 194 31.078 38.776 20.911 1.00143.47 C ANISOU 1347 CD1 LEU A 194 13361 18608 22542 2883 -1484 1028 C ATOM 1348 CD2 LEU A 194 33.374 38.872 19.917 1.00143.42 C ANISOU 1348 CD2 LEU A 194 13588 18457 22449 2992 -1575 1322 C ATOM 1349 N GLY A 195 30.290 36.327 16.935 1.00129.09 N ANISOU 1349 N GLY A 195 12118 16314 20616 2950 -1738 1820 N ATOM 1350 CA GLY A 195 29.718 36.800 15.688 1.00124.55 C ANISOU 1350 CA GLY A 195 11540 15506 20277 2993 -1853 1899 C ATOM 1351 C GLY A 195 28.233 36.507 15.592 1.00120.30 C ANISOU 1351 C GLY A 195 10926 14978 19804 2935 -1862 1852 C ATOM 1352 O GLY A 195 27.466 37.308 15.058 1.00120.05 O ANISOU 1352 O GLY A 195 10763 14806 20043 2967 -1941 1783 O ATOM 1353 N VAL A 196 27.829 35.350 16.106 1.00117.81 N ANISOU 1353 N VAL A 196 10696 14831 19236 2846 -1787 1891 N ATOM 1354 CA VAL A 196 26.424 34.964 16.113 1.00117.75 C ANISOU 1354 CA VAL A 196 10617 14875 19250 2766 -1782 1844 C ATOM 1355 C VAL A 196 25.601 35.934 16.956 1.00118.14 C ANISOU 1355 C VAL A 196 10366 15017 19506 2758 -1739 1545 C ATOM 1356 O VAL A 196 24.602 36.477 16.488 1.00106.71 O ANISOU 1356 O VAL A 196 8774 13476 18294 2778 -1802 1475 O ATOM 1357 CB VAL A 196 26.231 33.530 16.643 1.00117.64 C ANISOU 1357 CB VAL A 196 10762 15042 18892 2650 -1702 1932 C ATOM 1358 CG1 VAL A 196 24.754 33.236 16.853 1.00122.26 C ANISOU 1358 CG1 VAL A 196 11232 15726 19495 2546 -1680 1839 C ATOM 1359 CG2 VAL A 196 26.852 32.522 15.688 1.00102.42 C ANISOU 1359 CG2 VAL A 196 9136 12999 16778 2665 -1754 2226 C ATOM 1360 N TYR A 197 26.030 36.152 18.195 1.00120.22 N ANISOU 1360 N TYR A 197 10535 15462 19682 2732 -1635 1367 N ATOM 1361 CA TYR A 197 25.334 37.067 19.093 1.00125.66 C ANISOU 1361 CA TYR A 197 10943 16255 20549 2723 -1576 1063 C ATOM 1362 C TYR A 197 25.211 38.461 18.485 1.00129.56 C ANISOU 1362 C TYR A 197 11280 16533 21414 2845 -1675 965 C ATOM 1363 O TYR A 197 24.255 39.184 18.760 1.00130.32 O ANISOU 1363 O TYR A 197 11147 16640 21728 2862 -1672 750 O ATOM 1364 CB TYR A 197 26.045 37.143 20.447 1.00128.39 C ANISOU 1364 CB TYR A 197 11241 16808 20733 2677 -1456 908 C ATOM 1365 CG TYR A 197 26.038 35.847 21.225 1.00130.12 C ANISOU 1365 CG TYR A 197 11590 17257 20593 2543 -1360 966 C ATOM 1366 CD1 TYR A 197 24.909 35.442 21.923 1.00127.39 C ANISOU 1366 CD1 TYR A 197 11133 17101 20169 2419 -1280 825 C ATOM 1367 CD2 TYR A 197 27.162 35.035 21.270 1.00138.46 C ANISOU 1367 CD2 TYR A 197 12880 18342 21387 2537 -1354 1158 C ATOM 1368 CE1 TYR A 197 24.895 34.258 22.639 1.00129.20 C ANISOU 1368 CE1 TYR A 197 11496 17534 20058 2278 -1201 883 C ATOM 1369 CE2 TYR A 197 27.161 33.849 21.982 1.00142.89 C ANISOU 1369 CE2 TYR A 197 13577 19097 21620 2416 -1282 1218 C ATOM 1370 CZ TYR A 197 26.024 33.465 22.665 1.00137.05 C ANISOU 1370 CZ TYR A 197 12739 18535 20799 2279 -1208 1084 C ATOM 1371 OH TYR A 197 26.019 32.287 23.376 1.00138.77 O ANISOU 1371 OH TYR A 197 13109 18939 20680 2142 -1145 1148 O ATOM 1372 N LEU A 198 26.185 38.833 17.661 1.00130.99 N ANISOU 1372 N LEU A 198 11588 16518 21663 2929 -1765 1119 N ATOM 1373 CA LEU A 198 26.164 40.124 16.983 1.00134.45 C ANISOU 1373 CA LEU A 198 11921 16725 22438 3034 -1879 1060 C ATOM 1374 C LEU A 198 24.917 40.268 16.119 1.00135.80 C ANISOU 1374 C LEU A 198 12019 16758 22822 3057 -1980 1083 C ATOM 1375 O LEU A 198 24.250 41.303 16.143 1.00133.27 O ANISOU 1375 O LEU A 198 11494 16351 22790 3121 -2030 898 O ATOM 1376 CB LEU A 198 27.417 40.301 16.125 1.00131.88 C ANISOU 1376 CB LEU A 198 11781 16224 22102 3090 -1960 1264 C ATOM 1377 CG LEU A 198 28.738 40.457 16.878 1.00129.74 C ANISOU 1377 CG LEU A 198 11550 16059 21685 3089 -1886 1227 C ATOM 1378 CD1 LEU A 198 29.911 40.474 15.908 1.00129.83 C ANISOU 1378 CD1 LEU A 198 11751 15915 21663 3133 -1966 1452 C ATOM 1379 CD2 LEU A 198 28.721 41.716 17.729 1.00127.24 C ANISOU 1379 CD2 LEU A 198 11016 15765 21566 3118 -1857 944 C ATOM 1380 N ARG A 199 24.606 39.224 15.358 1.00139.90 N ANISOU 1380 N ARG A 199 12705 17253 23196 3006 -2015 1308 N ATOM 1381 CA ARG A 199 23.428 39.228 14.500 1.00150.25 C ANISOU 1381 CA ARG A 199 13963 18449 24678 3010 -2116 1358 C ATOM 1382 C ARG A 199 22.154 39.054 15.323 1.00149.20 C ANISOU 1382 C ARG A 199 13617 18515 24555 2949 -2035 1151 C ATOM 1383 O ARG A 199 21.113 39.626 15.003 1.00142.93 O ANISOU 1383 O ARG A 199 12645 17650 24012 2990 -2107 1051 O ATOM 1384 CB ARG A 199 23.528 38.121 13.448 1.00156.60 C ANISOU 1384 CB ARG A 199 15028 19174 25300 2959 -2171 1666 C ATOM 1385 CG ARG A 199 24.827 38.119 12.655 1.00159.73 C ANISOU 1385 CG ARG A 199 15647 19408 25637 3004 -2230 1876 C ATOM 1386 CD ARG A 199 25.071 39.452 11.965 1.00168.03 C ANISOU 1386 CD ARG A 199 16623 20219 27003 3102 -2359 1845 C ATOM 1387 NE ARG A 199 26.237 39.404 11.085 1.00173.75 N ANISOU 1387 NE ARG A 199 17563 20793 27662 3124 -2419 2060 N ATOM 1388 CZ ARG A 199 27.481 39.672 11.470 1.00172.67 C ANISOU 1388 CZ ARG A 199 17475 20690 27442 3150 -2370 2047 C ATOM 1389 NH1 ARG A 199 27.734 40.011 12.727 1.00173.19 N ANISOU 1389 NH1 ARG A 199 17400 20926 27478 3155 -2265 1835 N ATOM 1390 NH2 ARG A 199 28.476 39.602 10.596 1.00169.56 N ANISOU 1390 NH2 ARG A 199 17267 20168 26990 3164 -2426 2242 N ATOM 1391 N ILE A 200 22.249 38.260 16.385 1.00147.80 N ANISOU 1391 N ILE A 200 13459 18594 24103 2849 -1889 1087 N ATOM 1392 CA ILE A 200 21.116 38.003 17.266 1.00141.56 C ANISOU 1392 CA ILE A 200 12479 18033 23275 2761 -1791 887 C ATOM 1393 C ILE A 200 20.487 39.294 17.775 1.00151.01 C ANISOU 1393 C ILE A 200 13363 19229 24785 2842 -1787 579 C ATOM 1394 O ILE A 200 19.318 39.569 17.515 1.00157.41 O ANISOU 1394 O ILE A 200 13995 20027 25786 2859 -1832 485 O ATOM 1395 CB ILE A 200 21.528 37.145 18.479 1.00131.25 C ANISOU 1395 CB ILE A 200 11242 16999 21627 2638 -1633 839 C ATOM 1396 CG1 ILE A 200 21.894 35.727 18.039 1.00128.81 C ANISOU 1396 CG1 ILE A 200 11235 16709 20997 2549 -1636 1128 C ATOM 1397 CG2 ILE A 200 20.415 37.105 19.506 1.00126.32 C ANISOU 1397 CG2 ILE A 200 10387 16622 20986 2542 -1522 584 C ATOM 1398 CD1 ILE A 200 22.189 34.785 19.188 1.00129.10 C ANISOU 1398 CD1 ILE A 200 11360 17005 20688 2418 -1500 1100 C ATOM 1399 N PHE A 201 21.271 40.083 18.502 1.00155.76 N ANISOU 1399 N PHE A 201 13897 19845 25439 2895 -1736 419 N ATOM 1400 CA PHE A 201 20.763 41.288 19.150 1.00163.26 C ANISOU 1400 CA PHE A 201 14562 20811 26660 2968 -1711 100 C ATOM 1401 C PHE A 201 20.487 42.426 18.169 1.00162.33 C ANISOU 1401 C PHE A 201 14357 20399 26923 3120 -1878 90 C ATOM 1402 O PHE A 201 19.544 43.193 18.353 1.00163.46 O ANISOU 1402 O PHE A 201 14254 20530 27323 3186 -1897 -134 O ATOM 1403 CB PHE A 201 21.728 41.746 20.246 1.00171.87 C ANISOU 1403 CB PHE A 201 15630 22007 27668 2961 -1604 -61 C ATOM 1404 CG PHE A 201 21.902 40.746 21.360 1.00176.04 C ANISOU 1404 CG PHE A 201 16210 22836 27840 2808 -1442 -94 C ATOM 1405 CD1 PHE A 201 20.967 40.658 22.381 1.00176.86 C ANISOU 1405 CD1 PHE A 201 16110 23185 27905 2720 -1317 -344 C ATOM 1406 CD2 PHE A 201 22.999 39.898 21.388 1.00175.59 C ANISOU 1406 CD2 PHE A 201 16407 22821 27490 2750 -1418 123 C ATOM 1407 CE1 PHE A 201 21.123 39.744 23.406 1.00177.49 C ANISOU 1407 CE1 PHE A 201 16251 23539 27648 2562 -1176 -368 C ATOM 1408 CE2 PHE A 201 23.159 38.983 22.411 1.00175.76 C ANISOU 1408 CE2 PHE A 201 16488 23105 27186 2609 -1286 101 C ATOM 1409 CZ PHE A 201 22.220 38.905 23.419 1.00177.50 C ANISOU 1409 CZ PHE A 201 16519 23563 27361 2507 -1168 -140 C ATOM 1410 N ALA A 202 21.313 42.536 17.134 1.00162.48 N ANISOU 1410 N ALA A 202 14579 20183 26975 3173 -2002 330 N ATOM 1411 CA ALA A 202 21.112 43.552 16.108 1.00164.53 C ANISOU 1411 CA ALA A 202 14796 20145 27572 3299 -2180 359 C ATOM 1412 C ALA A 202 19.744 43.384 15.460 1.00160.60 C ANISOU 1412 C ALA A 202 14188 19606 27226 3311 -2266 378 C ATOM 1413 O ALA A 202 18.987 44.347 15.324 1.00162.34 O ANISOU 1413 O ALA A 202 14204 19714 27764 3414 -2350 211 O ATOM 1414 CB ALA A 202 22.212 43.480 15.062 1.00166.86 C ANISOU 1414 CB ALA A 202 15355 20227 27817 3316 -2287 644 C ATOM 1415 N ALA A 203 19.434 42.153 15.064 1.00156.88 N ANISOU 1415 N ALA A 203 13856 19226 26527 3205 -2249 581 N ATOM 1416 CA ALA A 203 18.154 41.845 14.437 1.00155.85 C ANISOU 1416 CA ALA A 203 13637 19083 26497 3190 -2326 624 C ATOM 1417 C ALA A 203 17.013 41.876 15.450 1.00154.52 C ANISOU 1417 C ALA A 203 13181 19162 26367 3160 -2214 338 C ATOM 1418 O ALA A 203 15.906 42.305 15.133 1.00159.77 O ANISOU 1418 O ALA A 203 13647 19787 27273 3217 -2293 240 O ATOM 1419 CB ALA A 203 18.215 40.489 13.748 1.00154.14 C ANISOU 1419 CB ALA A 203 13674 18894 25999 3070 -2334 926 C ATOM 1420 N ALA A 204 17.290 41.416 16.666 1.00151.64 N ANISOU 1420 N ALA A 204 12796 19060 25762 3066 -2033 204 N ATOM 1421 CA ALA A 204 16.291 41.401 17.727 1.00152.30 C ANISOU 1421 CA ALA A 204 12614 19410 25842 3011 -1903 -80 C ATOM 1422 C ALA A 204 15.716 42.793 17.964 1.00160.03 C ANISOU 1422 C ALA A 204 13294 20307 27204 3164 -1945 -375 C ATOM 1423 O ALA A 204 14.503 42.959 18.098 1.00167.53 O ANISOU 1423 O ALA A 204 13999 21353 28303 3180 -1942 -545 O ATOM 1424 CB ALA A 204 16.886 40.843 19.008 1.00149.62 C ANISOU 1424 CB ALA A 204 12322 19336 25192 2888 -1712 -178 C ATOM 1425 N ARG A 205 16.594 43.789 18.022 1.00159.61 N ANISOU 1425 N ARG A 205 13262 20077 27305 3277 -1986 -439 N ATOM 1426 CA ARG A 205 16.172 45.171 18.218 1.00162.99 C ANISOU 1426 CA ARG A 205 13441 20386 28102 3435 -2039 -712 C ATOM 1427 C ARG A 205 15.455 45.706 16.981 1.00164.34 C ANISOU 1427 C ARG A 205 13558 20293 28591 3560 -2251 -619 C ATOM 1428 O ARG A 205 14.634 46.617 17.075 1.00163.05 O ANISOU 1428 O ARG A 205 13141 20071 28738 3686 -2305 -848 O ATOM 1429 CB ARG A 205 17.366 46.061 18.574 1.00162.86 C ANISOU 1429 CB ARG A 205 13495 20240 28144 3504 -2035 -784 C ATOM 1430 CG ARG A 205 17.758 46.029 20.052 1.00166.79 C ANISOU 1430 CG ARG A 205 13914 21002 28456 3424 -1828 -1022 C ATOM 1431 CD ARG A 205 17.985 44.607 20.540 1.00171.63 C ANISOU 1431 CD ARG A 205 14673 21886 28654 3236 -1689 -886 C ATOM 1432 NE ARG A 205 18.409 44.556 21.937 1.00178.60 N ANISOU 1432 NE ARG A 205 15499 23017 29343 3146 -1504 -1094 N ATOM 1433 CZ ARG A 205 19.677 44.511 22.332 1.00182.48 C ANISOU 1433 CZ ARG A 205 16161 23517 29657 3108 -1457 -1025 C ATOM 1434 NH1 ARG A 205 20.654 44.513 21.435 1.00179.46 N ANISOU 1434 NH1 ARG A 205 16007 22915 29265 3155 -1575 -762 N ATOM 1435 NH2 ARG A 205 19.971 44.464 23.624 1.00185.26 N ANISOU 1435 NH2 ARG A 205 16449 24105 29835 3016 -1293 -1222 N ATOM 1436 N ARG A 206 15.771 45.134 15.823 1.00165.61 N ANISOU 1436 N ARG A 206 13959 20292 28672 3527 -2374 -284 N ATOM 1437 CA ARG A 206 15.078 45.477 14.586 1.00171.09 C ANISOU 1437 CA ARG A 206 14631 20749 29627 3614 -2582 -156 C ATOM 1438 C ARG A 206 13.635 45.000 14.663 1.00172.59 C ANISOU 1438 C ARG A 206 14607 21122 29848 3577 -2562 -244 C ATOM 1439 O ARG A 206 12.717 45.684 14.214 1.00176.03 O ANISOU 1439 O ARG A 206 14847 21442 30595 3694 -2691 -335 O ATOM 1440 CB ARG A 206 15.771 44.837 13.381 1.00175.44 C ANISOU 1440 CB ARG A 206 15505 21121 30034 3555 -2695 227 C ATOM 1441 CG ARG A 206 17.205 45.292 13.158 1.00183.72 C ANISOU 1441 CG ARG A 206 16767 21986 31053 3585 -2729 337 C ATOM 1442 CD ARG A 206 17.871 44.485 12.052 1.00189.18 C ANISOU 1442 CD ARG A 206 17772 22553 31553 3507 -2807 704 C ATOM 1443 NE ARG A 206 19.290 44.804 11.918 1.00192.60 N ANISOU 1443 NE ARG A 206 18404 22861 31915 3518 -2814 805 N ATOM 1444 CZ ARG A 206 20.123 44.177 11.093 1.00195.08 C ANISOU 1444 CZ ARG A 206 18994 23082 32044 3456 -2855 1095 C ATOM 1445 NH1 ARG A 206 19.680 43.192 10.323 1.00194.66 N ANISOU 1445 NH1 ARG A 206 19070 23035 31858 3378 -2893 1317 N ATOM 1446 NH2 ARG A 206 21.400 44.534 11.037 1.00197.27 N ANISOU 1446 NH2 ARG A 206 19419 23267 32266 3468 -2855 1159 N ATOM 1447 N GLN A 207 13.446 43.814 15.234 1.00169.50 N ANISOU 1447 N GLN A 207 14256 21020 29127 3409 -2404 -213 N ATOM 1448 CA GLN A 207 12.115 43.253 15.427 1.00167.16 C ANISOU 1448 CA GLN A 207 13761 20948 28806 3335 -2357 -303 C ATOM 1449 C GLN A 207 11.267 44.197 16.266 1.00174.42 C ANISOU 1449 C GLN A 207 14308 21976 29988 3443 -2303 -689 C ATOM 1450 O GLN A 207 10.117 44.480 15.930 1.00182.84 O ANISOU 1450 O GLN A 207 15147 23044 31279 3510 -2386 -780 O ATOM 1451 CB GLN A 207 12.201 41.886 16.110 1.00161.19 C ANISOU 1451 CB GLN A 207 13125 20496 27625 3121 -2176 -237 C ATOM 1452 CG GLN A 207 12.997 40.850 15.333 1.00157.33 C ANISOU 1452 CG GLN A 207 13006 19916 26856 3015 -2217 134 C ATOM 1453 CD GLN A 207 12.347 40.478 14.018 1.00160.26 C ANISOU 1453 CD GLN A 207 13454 20138 27301 3005 -2384 376 C ATOM 1454 OE1 GLN A 207 11.130 40.566 13.869 1.00172.04 O ANISOU 1454 OE1 GLN A 207 14724 21700 28941 3010 -2428 282 O ATOM 1455 NE2 GLN A 207 13.157 40.046 13.059 1.00147.89 N ANISOU 1455 NE2 GLN A 207 12197 18371 25622 2984 -2476 688 N ATOM 1456 N LEU A 208 11.847 44.682 17.358 1.00177.38 N ANISOU 1456 N LEU A 208 14618 22445 30332 3462 -2165 -920 N ATOM 1457 CA LEU A 208 11.156 45.603 18.250 1.00186.78 C ANISOU 1457 CA LEU A 208 15468 23743 31756 3564 -2092 -1311 C ATOM 1458 C LEU A 208 10.801 46.908 17.545 1.00198.72 C ANISOU 1458 C LEU A 208 16838 24948 33718 3795 -2291 -1395 C ATOM 1459 O LEU A 208 9.779 47.521 17.845 1.00203.16 O ANISOU 1459 O LEU A 208 17089 25571 34531 3901 -2294 -1663 O ATOM 1460 CB LEU A 208 12.006 45.888 19.490 1.00187.19 C ANISOU 1460 CB LEU A 208 15525 23925 31674 3530 -1916 -1514 C ATOM 1461 CG LEU A 208 12.295 44.695 20.404 1.00186.17 C ANISOU 1461 CG LEU A 208 15500 24124 31111 3305 -1711 -1488 C ATOM 1462 CD1 LEU A 208 13.238 45.092 21.530 1.00184.69 C ANISOU 1462 CD1 LEU A 208 15336 24024 30816 3284 -1567 -1667 C ATOM 1463 CD2 LEU A 208 11.002 44.125 20.963 1.00188.46 C ANISOU 1463 CD2 LEU A 208 15550 24733 31322 3196 -1595 -1661 C ATOM 1464 N LYS A 209 11.649 47.325 16.609 1.00205.83 N ANISOU 1464 N LYS A 209 17969 25522 34716 3871 -2458 -1167 N ATOM 1465 CA LYS A 209 11.415 48.555 15.857 1.00215.17 C ANISOU 1465 CA LYS A 209 19067 26376 36311 4078 -2671 -1208 C ATOM 1466 C LYS A 209 10.273 48.386 14.860 1.00219.61 C ANISOU 1466 C LYS A 209 19528 26865 37048 4121 -2839 -1093 C ATOM 1467 O LYS A 209 9.464 49.295 14.666 1.00220.25 O ANISOU 1467 O LYS A 209 19374 26825 37484 4291 -2960 -1266 O ATOM 1468 CB LYS A 209 12.685 49.002 15.130 1.00215.96 C ANISOU 1468 CB LYS A 209 19461 26160 36434 4115 -2801 -983 C ATOM 1469 CG LYS A 209 12.504 50.282 14.328 1.00221.09 C ANISOU 1469 CG LYS A 209 20058 26449 37496 4312 -3037 -1007 C ATOM 1470 CD LYS A 209 13.783 50.686 13.611 1.00223.68 C ANISOU 1470 CD LYS A 209 20688 26484 37818 4317 -3159 -778 C ATOM 1471 CE LYS A 209 13.578 51.955 12.799 1.00230.46 C ANISOU 1471 CE LYS A 209 21513 26974 39079 4497 -3408 -793 C ATOM 1472 NZ LYS A 209 14.812 52.388 12.089 1.00232.45 N ANISOU 1472 NZ LYS A 209 22056 26943 39320 4484 -3530 -575 N ATOM 1473 N GLN A 210 10.215 47.220 14.225 1.00221.61 N ANISOU 1473 N GLN A 210 19962 27187 37051 3967 -2850 -800 N ATOM 1474 CA GLN A 210 9.125 46.909 13.310 1.00224.38 C ANISOU 1474 CA GLN A 210 20229 27506 37518 3972 -2995 -673 C ATOM 1475 C GLN A 210 7.820 46.803 14.086 1.00223.91 C ANISOU 1475 C GLN A 210 19809 27748 37517 3971 -2885 -961 C ATOM 1476 O GLN A 210 6.771 47.253 13.623 1.00230.01 O ANISOU 1476 O GLN A 210 20357 28463 38573 4085 -3020 -1035 O ATOM 1477 CB GLN A 210 9.401 45.606 12.558 1.00226.84 C ANISOU 1477 CB GLN A 210 20832 27848 37507 3785 -3006 -306 C ATOM 1478 CG GLN A 210 10.645 45.650 11.683 1.00229.13 C ANISOU 1478 CG GLN A 210 21474 27850 37734 3780 -3118 -10 C ATOM 1479 CD GLN A 210 10.837 44.381 10.879 1.00229.54 C ANISOU 1479 CD GLN A 210 21806 27921 37489 3609 -3136 341 C ATOM 1480 OE1 GLN A 210 9.963 43.514 10.848 1.00230.62 O ANISOU 1480 OE1 GLN A 210 21879 28253 37492 3498 -3096 382 O ATOM 1481 NE2 GLN A 210 11.984 44.266 10.220 1.00227.31 N ANISOU 1481 NE2 GLN A 210 21834 27438 37095 3583 -3195 590 N ATOM 1482 N MET A 211 7.893 46.204 15.271 1.00218.46 N ANISOU 1482 N MET A 211 19063 27387 36556 3837 -2642 -1125 N ATOM 1483 CA MET A 211 6.738 46.109 16.152 1.00219.30 C ANISOU 1483 CA MET A 211 18823 27816 36686 3814 -2505 -1429 C ATOM 1484 C MET A 211 6.506 47.443 16.853 1.00225.97 C ANISOU 1484 C MET A 211 19380 28615 37864 4018 -2488 -1810 C ATOM 1485 O MET A 211 5.509 47.629 17.548 1.00229.11 O ANISOU 1485 O MET A 211 19445 29245 38362 4048 -2393 -2111 O ATOM 1486 CB MET A 211 6.932 44.990 17.177 1.00215.36 C ANISOU 1486 CB MET A 211 18388 27681 35759 3578 -2255 -1463 C ATOM 1487 CG MET A 211 7.121 43.614 16.558 1.00212.76 C ANISOU 1487 CG MET A 211 18347 27406 35084 3372 -2263 -1103 C ATOM 1488 SD MET A 211 7.104 42.293 17.783 1.00150.13 S ANISOU 1488 SD MET A 211 10459 19915 26668 3091 -1988 -1164 S ATOM 1489 CE MET A 211 8.404 42.841 18.883 1.00174.86 C ANISOU 1489 CE MET A 211 13676 23044 29719 3124 -1844 -1332 C ATOM 1490 N GLU A 212 7.439 48.369 16.661 1.00262.84 N ANISOU 1490 N GLU A 212 23258 30014 46594 -2086 -3790 4052 N ATOM 1491 CA GLU A 212 7.317 49.713 17.211 1.00264.40 C ANISOU 1491 CA GLU A 212 23640 29878 46941 -2117 -3837 4364 C ATOM 1492 C GLU A 212 6.497 50.576 16.259 1.00258.50 C ANISOU 1492 C GLU A 212 23112 29057 46050 -2532 -3893 4931 C ATOM 1493 O GLU A 212 5.934 51.597 16.653 1.00256.05 O ANISOU 1493 O GLU A 212 23014 28393 45881 -2505 -3978 5343 O ATOM 1494 CB GLU A 212 8.703 50.323 17.429 1.00274.24 C ANISOU 1494 CB GLU A 212 24750 31302 48147 -2325 -3704 3980 C ATOM 1495 CG GLU A 212 8.702 51.695 18.080 1.00282.07 C ANISOU 1495 CG GLU A 212 25913 31960 49302 -2340 -3742 4247 C ATOM 1496 CD GLU A 212 10.106 52.224 18.310 1.00291.53 C ANISOU 1496 CD GLU A 212 26961 33349 50459 -2532 -3605 3836 C ATOM 1497 OE1 GLU A 212 11.073 51.491 18.015 1.00294.16 O ANISOU 1497 OE1 GLU A 212 27055 34066 50648 -2626 -3484 3335 O ATOM 1498 OE2 GLU A 212 10.242 53.371 18.786 1.00295.58 O ANISOU 1498 OE2 GLU A 212 27596 33628 51083 -2588 -3619 4012 O ATOM 1499 N SER A 213 6.433 50.150 15.001 1.00254.86 N ANISOU 1499 N SER A 213 22596 28932 45306 -2915 -3844 4949 N ATOM 1500 CA SER A 213 5.664 50.854 13.983 1.00255.59 C ANISOU 1500 CA SER A 213 22880 29000 45233 -3331 -3890 5466 C ATOM 1501 C SER A 213 4.481 50.011 13.522 1.00252.79 C ANISOU 1501 C SER A 213 22599 28604 44847 -3196 -3990 5739 C ATOM 1502 O SER A 213 4.105 50.042 12.350 1.00256.36 O ANISOU 1502 O SER A 213 23099 29244 45062 -3593 -3983 5969 O ATOM 1503 CB SER A 213 6.553 51.205 12.788 1.00264.67 C ANISOU 1503 CB SER A 213 23925 30581 46058 -3956 -3749 5308 C ATOM 1504 OG SER A 213 7.662 51.992 13.188 1.00271.05 O ANISOU 1504 OG SER A 213 24662 31436 46888 -4094 -3653 5053 O ATOM 1505 N GLN A 214 3.900 49.255 14.449 1.00246.84 N ANISOU 1505 N GLN A 214 21853 27604 44332 -2635 -4084 5710 N ATOM 1506 CA GLN A 214 2.757 48.404 14.139 1.00241.31 C ANISOU 1506 CA GLN A 214 21221 26837 43630 -2449 -4186 5954 C ATOM 1507 C GLN A 214 1.453 49.046 14.605 1.00245.27 C ANISOU 1507 C GLN A 214 22001 26855 44333 -2230 -4350 6545 C ATOM 1508 O GLN A 214 1.379 49.579 15.712 1.00242.65 O ANISOU 1508 O GLN A 214 21757 26176 44262 -1905 -4408 6614 O ATOM 1509 CB GLN A 214 2.927 47.023 14.777 1.00229.95 C ANISOU 1509 CB GLN A 214 19599 25467 42304 -1974 -4181 5528 C ATOM 1510 CG GLN A 214 2.992 47.046 16.294 1.00219.93 C ANISOU 1510 CG GLN A 214 18340 23852 41371 -1418 -4236 5400 C ATOM 1511 CD GLN A 214 3.267 45.679 16.890 1.00212.92 C ANISOU 1511 CD GLN A 214 17255 23064 40580 -974 -4218 4943 C ATOM 1512 OE1 GLN A 214 3.359 44.682 16.173 1.00212.26 O ANISOU 1512 OE1 GLN A 214 17032 23300 40316 -1068 -4168 4732 O ATOM 1513 NE2 GLN A 214 3.400 45.626 18.210 1.00208.27 N ANISOU 1513 NE2 GLN A 214 16655 22202 40277 -485 -4257 4787 N ATOM 1514 N PRO A 215 0.421 48.999 13.749 1.00249.77 N ANISOU 1514 N PRO A 215 22712 27408 44782 -2411 -4424 6973 N ATOM 1515 CA PRO A 215 -0.898 49.578 14.034 1.00249.07 C ANISOU 1515 CA PRO A 215 22894 26886 44854 -2245 -4582 7567 C ATOM 1516 C PRO A 215 -1.684 48.777 15.069 1.00246.21 C ANISOU 1516 C PRO A 215 22567 26213 44769 -1611 -4701 7594 C ATOM 1517 O PRO A 215 -2.907 48.905 15.137 1.00242.29 O ANISOU 1517 O PRO A 215 22271 25416 44373 -1456 -4835 8065 O ATOM 1518 CB PRO A 215 -1.613 49.508 12.676 1.00249.64 C ANISOU 1518 CB PRO A 215 23050 27133 44669 -2650 -4602 7910 C ATOM 1519 CG PRO A 215 -0.528 49.296 11.664 1.00253.55 C ANISOU 1519 CG PRO A 215 23345 28133 44859 -3126 -4442 7539 C ATOM 1520 CD PRO A 215 0.508 48.491 12.372 1.00253.73 C ANISOU 1520 CD PRO A 215 23123 28321 44960 -2844 -4354 6923 C ATOM 1521 N LEU A 216 -0.993 47.965 15.862 1.00248.71 N ANISOU 1521 N LEU A 216 22692 26600 45206 -1251 -4652 7097 N ATOM 1522 CA LEU A 216 -1.652 47.141 16.872 1.00246.28 C ANISOU 1522 CA LEU A 216 22397 26017 45159 -638 -4756 7074 C ATOM 1523 C LEU A 216 -0.743 46.859 18.066 1.00242.05 C ANISOU 1523 C LEU A 216 21704 25436 44826 -252 -4705 6591 C ATOM 1524 O LEU A 216 0.478 46.830 17.927 1.00245.40 O ANISOU 1524 O LEU A 216 21940 26167 45135 -451 -4569 6150 O ATOM 1525 CB LEU A 216 -2.153 45.832 16.251 1.00247.79 C ANISOU 1525 CB LEU A 216 22502 26418 45229 -566 -4770 6999 C ATOM 1526 CG LEU A 216 -1.182 45.011 15.395 1.00251.27 C ANISOU 1526 CG LEU A 216 22689 27382 45401 -856 -4623 6518 C ATOM 1527 CD1 LEU A 216 -0.119 44.333 16.247 1.00250.53 C ANISOU 1527 CD1 LEU A 216 22365 27408 45416 -543 -4537 5913 C ATOM 1528 CD2 LEU A 216 -1.946 43.976 14.583 1.00252.25 C ANISOU 1528 CD2 LEU A 216 22797 27667 45381 -875 -4659 6615 C ATOM 1529 N PRO A 217 -1.343 46.662 19.250 1.00230.72 N ANISOU 1529 N PRO A 217 20351 23616 43696 303 -4816 6679 N ATOM 1530 CA PRO A 217 -0.590 46.345 20.468 1.00226.31 C ANISOU 1530 CA PRO A 217 19656 22978 43355 725 -4782 6244 C ATOM 1531 C PRO A 217 0.253 45.083 20.301 1.00222.48 C ANISOU 1531 C PRO A 217 18892 22884 42757 793 -4672 5658 C ATOM 1532 O PRO A 217 1.477 45.171 20.210 1.00231.09 O ANISOU 1532 O PRO A 217 19806 24255 43744 590 -4539 5239 O ATOM 1533 CB PRO A 217 -1.692 46.107 21.504 1.00221.15 C ANISOU 1533 CB PRO A 217 19152 21867 43007 1295 -4940 6516 C ATOM 1534 CG PRO A 217 -2.854 46.889 21.006 1.00218.51 C ANISOU 1534 CG PRO A 217 19080 21292 42651 1108 -5051 7156 C ATOM 1535 CD PRO A 217 -2.786 46.794 19.510 1.00222.18 C ANISOU 1535 CD PRO A 217 19506 22138 42774 557 -4982 7217 C ATOM 1536 N GLY A 218 -0.401 43.927 20.261 1.00212.54 N ANISOU 1536 N GLY A 218 17596 21641 41520 1074 -4727 5634 N ATOM 1537 CA GLY A 218 0.289 42.661 20.088 1.00207.90 C ANISOU 1537 CA GLY A 218 16753 21411 40828 1159 -4632 5104 C ATOM 1538 C GLY A 218 1.417 42.464 21.082 1.00209.86 C ANISOU 1538 C GLY A 218 16819 21701 41218 1431 -4551 4577 C ATOM 1539 O GLY A 218 2.559 42.218 20.696 1.00215.10 O ANISOU 1539 O GLY A 218 17275 22740 41711 1191 -4410 4132 O ATOM 1540 N GLU A 219 1.097 42.575 22.367 1.00201.76 N ANISOU 1540 N GLU A 219 15868 20287 40503 1933 -4639 4627 N ATOM 1541 CA GLU A 219 2.093 42.412 23.419 1.00195.45 C ANISOU 1541 CA GLU A 219 14910 19483 39867 2236 -4574 4151 C ATOM 1542 C GLU A 219 2.499 40.952 23.585 1.00196.60 C ANISOU 1542 C GLU A 219 14827 19871 40002 2523 -4520 3657 C ATOM 1543 O GLU A 219 3.443 40.641 24.310 1.00196.43 O ANISOU 1543 O GLU A 219 14633 19930 40071 2738 -4445 3190 O ATOM 1544 CB GLU A 219 1.579 42.981 24.743 1.00187.23 C ANISOU 1544 CB GLU A 219 14029 17943 39166 2690 -4690 4374 C ATOM 1545 CG GLU A 219 1.372 44.487 24.718 1.00184.89 C ANISOU 1545 CG GLU A 219 13940 17411 38900 2424 -4728 4796 C ATOM 1546 CD GLU A 219 2.635 45.237 24.340 1.00181.02 C ANISOU 1546 CD GLU A 219 13341 17193 38246 1984 -4586 4534 C ATOM 1547 OE1 GLU A 219 2.545 46.192 23.541 1.00182.04 O ANISOU 1547 OE1 GLU A 219 13588 17365 38216 1516 -4573 4843 O ATOM 1548 OE2 GLU A 219 3.719 44.864 24.834 1.00176.94 O ANISOU 1548 OE2 GLU A 219 12619 16851 37757 2106 -4487 4018 O ATOM 1549 N ARG A 220 1.781 40.061 22.910 1.00197.28 N ANISOU 1549 N ARG A 220 14911 20070 39975 2524 -4557 3762 N ATOM 1550 CA ARG A 220 2.128 38.646 22.906 1.00198.43 C ANISOU 1550 CA ARG A 220 14841 20477 40076 2745 -4501 3312 C ATOM 1551 C ARG A 220 3.437 38.429 22.160 1.00195.00 C ANISOU 1551 C ARG A 220 14174 20538 39381 2345 -4329 2840 C ATOM 1552 O ARG A 220 4.282 37.641 22.582 1.00193.46 O ANISOU 1552 O ARG A 220 13764 20534 39209 2549 -4246 2322 O ATOM 1553 CB ARG A 220 1.012 37.821 22.265 1.00202.60 C ANISOU 1553 CB ARG A 220 15436 21013 40528 2794 -4582 3574 C ATOM 1554 CG ARG A 220 -0.132 37.493 23.208 1.00202.81 C ANISOU 1554 CG ARG A 220 15610 20606 40841 3350 -4737 3847 C ATOM 1555 CD ARG A 220 0.254 36.381 24.169 1.00205.34 C ANISOU 1555 CD ARG A 220 15757 20930 41335 3873 -4720 3383 C ATOM 1556 NE ARG A 220 -0.777 36.140 25.174 1.00205.98 N ANISOU 1556 NE ARG A 220 15978 20575 41709 4423 -4866 3631 N ATOM 1557 CZ ARG A 220 -0.709 36.570 26.429 1.00205.90 C ANISOU 1557 CZ ARG A 220 16022 20231 41982 4807 -4917 3616 C ATOM 1558 NH1 ARG A 220 0.346 37.256 26.839 1.00206.21 N ANISOU 1558 NH1 ARG A 220 15983 20320 42047 4706 -4832 3361 N ATOM 1559 NH2 ARG A 220 -1.693 36.306 27.278 1.00204.02 N ANISOU 1559 NH2 ARG A 220 15912 19607 41998 5296 -5052 3852 N ATOM 1560 N ALA A 221 3.598 39.140 21.049 1.00177.95 N ANISOU 1560 N ALA A 221 16607 23988 27017 2456 -3658 5985 N ATOM 1561 CA ALA A 221 4.818 39.059 20.258 1.00179.31 C ANISOU 1561 CA ALA A 221 17244 23797 27089 2632 -3493 5913 C ATOM 1562 C ALA A 221 5.989 39.689 21.002 1.00178.43 C ANISOU 1562 C ALA A 221 17081 23192 27522 2612 -2874 5423 C ATOM 1563 O ALA A 221 7.068 39.105 21.082 1.00124.97 O ANISOU 1563 O ALA A 221 10646 16233 20604 2445 -2936 5058 O ATOM 1564 CB ALA A 221 4.621 39.732 18.909 1.00187.86 C ANISOU 1564 CB ALA A 221 18428 24783 28167 3137 -3282 6491 C ATOM 1565 N ARG A 222 5.772 40.885 21.541 1.00175.95 N ANISOU 1565 N ARG A 222 16352 22666 27835 2786 -2285 5423 N ATOM 1566 CA ARG A 222 6.811 41.588 22.286 1.00172.36 C ANISOU 1566 CA ARG A 222 15825 21725 27940 2765 -1685 4985 C ATOM 1567 C ARG A 222 7.275 40.788 23.500 1.00167.56 C ANISOU 1567 C ARG A 222 15244 21153 27270 2253 -1923 4373 C ATOM 1568 O ARG A 222 8.468 40.542 23.667 1.00169.23 O ANISOU 1568 O ARG A 222 15711 21065 27525 2128 -1806 4002 O ATOM 1569 CB ARG A 222 6.331 42.974 22.722 1.00173.71 C ANISOU 1569 CB ARG A 222 15547 21694 28759 3024 -1076 5102 C ATOM 1570 CG ARG A 222 6.514 44.067 21.677 1.00179.13 C ANISOU 1570 CG ARG A 222 16263 22067 29730 3547 -573 5533 C ATOM 1571 CD ARG A 222 6.455 45.441 22.330 1.00184.80 C ANISOU 1571 CD ARG A 222 16614 22436 31164 3744 106 5470 C ATOM 1572 NE ARG A 222 6.802 46.525 21.414 1.00192.10 N ANISOU 1572 NE ARG A 222 17593 22990 32407 4213 626 5823 N ATOM 1573 CZ ARG A 222 5.916 47.336 20.845 1.00200.38 C ANISOU 1573 CZ ARG A 222 18430 24097 33610 4598 805 6315 C ATOM 1574 NH1 ARG A 222 4.621 47.191 21.094 1.00202.91 N ANISOU 1574 NH1 ARG A 222 18449 24845 33801 4578 514 6524 N ATOM 1575 NH2 ARG A 222 6.326 48.296 20.028 1.00203.71 N ANISOU 1575 NH2 ARG A 222 18931 24152 34316 5001 1275 6609 N ATOM 1576 N SER A 223 6.329 40.388 24.344 1.00164.65 N ANISOU 1576 N SER A 223 14601 21157 26800 1958 -2257 4280 N ATOM 1577 CA SER A 223 6.646 39.612 25.538 1.00162.44 C ANISOU 1577 CA SER A 223 14329 20948 26442 1451 -2518 3716 C ATOM 1578 C SER A 223 7.458 38.367 25.194 1.00160.66 C ANISOU 1578 C SER A 223 14595 20766 25682 1206 -3013 3498 C ATOM 1579 O SER A 223 8.477 38.085 25.826 1.00163.47 O ANISOU 1579 O SER A 223 15101 20867 26143 964 -2930 3003 O ATOM 1580 CB SER A 223 5.367 39.223 26.281 1.00166.07 C ANISOU 1580 CB SER A 223 14454 21897 26747 1184 -2906 3755 C ATOM 1581 OG SER A 223 5.661 38.465 27.440 1.00164.66 O ANISOU 1581 OG SER A 223 14292 21791 26482 683 -3168 3214 O ATOM 1582 N THR A 224 7.005 37.630 24.184 1.00158.19 N ANISOU 1582 N THR A 224 14544 20767 24792 1279 -3532 3873 N ATOM 1583 CA THR A 224 7.713 36.442 23.720 1.00151.01 C ANISOU 1583 CA THR A 224 14148 19908 23323 1105 -4024 3720 C ATOM 1584 C THR A 224 9.112 36.798 23.223 1.00138.73 C ANISOU 1584 C THR A 224 12880 17869 21962 1340 -3574 3578 C ATOM 1585 O THR A 224 10.098 36.164 23.604 1.00120.77 O ANISOU 1585 O THR A 224 10861 15443 19584 1101 -3677 3142 O ATOM 1586 CB THR A 224 6.942 35.733 22.588 1.00150.87 C ANISOU 1586 CB THR A 224 14384 20273 22666 1213 -4616 4219 C ATOM 1587 OG1 THR A 224 5.665 35.299 23.074 1.00139.92 O ANISOU 1587 OG1 THR A 224 12732 19366 21066 946 -5092 4352 O ATOM 1588 CG2 THR A 224 7.724 34.528 22.082 1.00155.72 C ANISOU 1588 CG2 THR A 224 15576 20901 22690 1069 -5106 4052 C ATOM 1589 N LEU A 225 9.188 37.815 22.370 1.00140.23 N ANISOU 1589 N LEU A 225 13018 17827 22437 1809 -3078 3961 N ATOM 1590 CA LEU A 225 10.458 38.271 21.819 1.00132.26 C ANISOU 1590 CA LEU A 225 12242 16370 21641 2068 -2603 3901 C ATOM 1591 C LEU A 225 11.430 38.638 22.933 1.00127.28 C ANISOU 1591 C LEU A 225 11473 15367 21520 1852 -2184 3351 C ATOM 1592 O LEU A 225 12.582 38.205 22.930 1.00126.86 O ANISOU 1592 O LEU A 225 11705 15100 21398 1759 -2161 3048 O ATOM 1593 CB LEU A 225 10.231 39.468 20.889 1.00133.66 C ANISOU 1593 CB LEU A 225 12295 16358 22130 2583 -2092 4409 C ATOM 1594 CG LEU A 225 11.402 39.997 20.055 1.00130.44 C ANISOU 1594 CG LEU A 225 12135 15534 21893 2920 -1611 4495 C ATOM 1595 CD1 LEU A 225 12.374 40.810 20.899 1.00131.20 C ANISOU 1595 CD1 LEU A 225 12039 15167 22644 2859 -992 4102 C ATOM 1596 CD2 LEU A 225 12.119 38.853 19.357 1.00127.59 C ANISOU 1596 CD2 LEU A 225 12297 15256 20926 2872 -2031 4432 C ATOM 1597 N GLN A 226 10.959 39.438 23.885 1.00131.07 N ANISOU 1597 N GLN A 226 11522 15771 22508 1777 -1855 3230 N ATOM 1598 CA GLN A 226 11.787 39.869 25.006 1.00135.89 C ANISOU 1598 CA GLN A 226 11986 16016 23632 1563 -1453 2720 C ATOM 1599 C GLN A 226 12.300 38.683 25.819 1.00136.37 C ANISOU 1599 C GLN A 226 12236 16185 23393 1071 -1912 2194 C ATOM 1600 O GLN A 226 13.433 38.697 26.301 1.00141.61 O ANISOU 1600 O GLN A 226 12997 16515 24294 928 -1684 1794 O ATOM 1601 CB GLN A 226 11.021 40.835 25.914 1.00143.53 C ANISOU 1601 CB GLN A 226 12480 16938 25117 1559 -1100 2691 C ATOM 1602 CG GLN A 226 10.651 42.160 25.259 1.00152.46 C ANISOU 1602 CG GLN A 226 13406 17869 26653 2048 -554 3146 C ATOM 1603 CD GLN A 226 10.160 43.187 26.264 1.00158.68 C ANISOU 1603 CD GLN A 226 13768 18502 28020 2054 -119 3026 C ATOM 1604 OE1 GLN A 226 10.579 43.187 27.422 1.00158.69 O ANISOU 1604 OE1 GLN A 226 13676 18336 28282 1740 -8 2538 O ATOM 1605 NE2 GLN A 226 9.271 44.070 25.825 1.00165.25 N ANISOU 1605 NE2 GLN A 226 14355 19382 29049 2420 129 3470 N ATOM 1606 N LYS A 227 11.463 37.661 25.970 1.00136.04 N ANISOU 1606 N LYS A 227 12245 16609 22835 807 -2570 2208 N ATOM 1607 CA LYS A 227 11.844 36.464 26.714 1.00144.30 C ANISOU 1607 CA LYS A 227 13489 17794 23544 328 -3075 1735 C ATOM 1608 C LYS A 227 12.836 35.609 25.927 1.00147.74 C ANISOU 1608 C LYS A 227 14428 18160 23547 364 -3333 1675 C ATOM 1609 O LYS A 227 13.741 35.003 26.504 1.00142.62 O ANISOU 1609 O LYS A 227 13960 17375 22853 79 -3449 1213 O ATOM 1610 CB LYS A 227 10.608 35.643 27.088 1.00150.19 C ANISOU 1610 CB LYS A 227 14138 19070 23859 28 -3715 1802 C ATOM 1611 CG LYS A 227 9.693 36.322 28.097 1.00161.17 C ANISOU 1611 CG LYS A 227 15028 20562 25649 -84 -3502 1759 C ATOM 1612 CD LYS A 227 8.486 35.451 28.444 1.00169.52 C ANISOU 1612 CD LYS A 227 15980 22176 26252 -398 -4157 1848 C ATOM 1613 CE LYS A 227 7.550 36.157 29.421 1.00170.66 C ANISOU 1613 CE LYS A 227 15607 22445 26791 -471 -3911 1833 C ATOM 1614 NZ LYS A 227 6.355 35.338 29.769 1.00164.37 N ANISOU 1614 NZ LYS A 227 14669 22215 25568 -781 -4532 1949 N ATOM 1615 N GLU A 228 12.658 35.562 24.610 1.00152.21 N ANISOU 1615 N GLU A 228 15225 18820 23789 725 -3422 2147 N ATOM 1616 CA GLU A 228 13.607 34.885 23.735 1.00150.40 C ANISOU 1616 CA GLU A 228 15481 18498 23165 850 -3585 2146 C ATOM 1617 C GLU A 228 14.961 35.581 23.815 1.00145.50 C ANISOU 1617 C GLU A 228 14867 17380 23037 996 -2949 1921 C ATOM 1618 O GLU A 228 16.006 34.930 23.878 1.00146.51 O ANISOU 1618 O GLU A 228 15284 17377 23006 872 -3052 1603 O ATOM 1619 CB GLU A 228 13.099 34.878 22.291 1.00160.25 C ANISOU 1619 CB GLU A 228 16950 19914 24024 1251 -3726 2735 C ATOM 1620 CG GLU A 228 11.906 33.965 22.056 1.00168.49 C ANISOU 1620 CG GLU A 228 18097 21458 24461 1088 -4465 2969 C ATOM 1621 CD GLU A 228 12.275 32.496 22.112 1.00172.64 C ANISOU 1621 CD GLU A 228 19073 22167 24355 774 -5144 2685 C ATOM 1622 OE1 GLU A 228 13.476 32.179 21.982 1.00173.52 O ANISOU 1622 OE1 GLU A 228 19488 22026 24417 804 -5036 2412 O ATOM 1623 OE2 GLU A 228 11.364 31.657 22.275 1.00173.60 O ANISOU 1623 OE2 GLU A 228 19248 22687 24023 501 -5793 2745 O ATOM 1624 N VAL A 229 14.932 36.910 23.818 1.00139.49 N ANISOU 1624 N VAL A 229 13782 16342 22876 1256 -2299 2097 N ATOM 1625 CA VAL A 229 16.145 37.705 23.966 1.00139.40 C ANISOU 1625 CA VAL A 229 13722 15843 23400 1373 -1666 1912 C ATOM 1626 C VAL A 229 16.771 37.485 25.340 1.00138.20 C ANISOU 1626 C VAL A 229 13458 15525 23529 933 -1645 1303 C ATOM 1627 O VAL A 229 17.992 37.393 25.466 1.00140.02 O ANISOU 1627 O VAL A 229 13834 15467 23900 878 -1452 1024 O ATOM 1628 CB VAL A 229 15.868 39.207 23.766 1.00143.86 C ANISOU 1628 CB VAL A 229 13956 16146 24560 1717 -1005 2230 C ATOM 1629 CG1 VAL A 229 17.079 40.031 24.177 1.00145.37 C ANISOU 1629 CG1 VAL A 229 14055 15825 25353 1739 -382 1977 C ATOM 1630 CG2 VAL A 229 15.488 39.488 22.321 1.00148.70 C ANISOU 1630 CG2 VAL A 229 14718 16849 24932 2182 -957 2827 C ATOM 1631 N HIS A 230 15.931 37.393 26.367 1.00137.09 N ANISOU 1631 N HIS A 230 13054 15572 23462 619 -1848 1107 N ATOM 1632 CA HIS A 230 16.409 37.165 27.727 1.00134.93 C ANISOU 1632 CA HIS A 230 12673 15163 23432 176 -1864 530 C ATOM 1633 C HIS A 230 17.169 35.846 27.818 1.00130.35 C ANISOU 1633 C HIS A 230 12467 14677 22384 -110 -2364 185 C ATOM 1634 O HIS A 230 18.151 35.737 28.549 1.00125.74 O ANISOU 1634 O HIS A 230 11912 13828 22035 -348 -2239 -256 O ATOM 1635 CB HIS A 230 15.244 37.176 28.721 1.00135.29 C ANISOU 1635 CB HIS A 230 12399 15470 23535 -99 -2062 426 C ATOM 1636 CG HIS A 230 15.662 37.009 30.146 1.00132.72 C ANISOU 1636 CG HIS A 230 11955 15000 23470 -549 -2060 -154 C ATOM 1637 ND1 HIS A 230 15.858 38.081 31.000 1.00131.89 N ANISOU 1637 ND1 HIS A 230 11549 14543 24020 -573 -1505 -349 N ATOM 1638 CD2 HIS A 230 15.927 35.904 30.880 1.00128.21 C ANISOU 1638 CD2 HIS A 230 11546 14574 22593 -997 -2551 -587 C ATOM 1639 CE1 HIS A 230 16.219 37.641 32.184 1.00124.85 C ANISOU 1639 CE1 HIS A 230 10639 13592 23208 -1016 -1654 -870 C ATOM 1640 NE2 HIS A 230 16.275 36.315 32.141 1.00122.65 N ANISOU 1640 NE2 HIS A 230 10632 13614 22356 -1284 -2288 -1026 N ATOM 1641 N ALA A 231 16.711 34.848 27.069 1.00129.88 N ANISOU 1641 N ALA A 231 12704 14986 21658 -82 -2941 394 N ATOM 1642 CA ALA A 231 17.383 33.556 27.025 1.00125.73 C ANISOU 1642 CA ALA A 231 12586 14562 20625 -304 -3452 109 C ATOM 1643 C ALA A 231 18.686 33.659 26.238 1.00126.47 C ANISOU 1643 C ALA A 231 12948 14346 20760 -14 -3134 135 C ATOM 1644 O ALA A 231 19.712 33.110 26.641 1.00125.15 O ANISOU 1644 O ALA A 231 12957 14025 20570 -209 -3203 -261 O ATOM 1645 CB ALA A 231 16.473 32.504 26.414 1.00125.87 C ANISOU 1645 CB ALA A 231 12868 15047 19910 -343 -4166 355 C ATOM 1646 N ALA A 232 18.638 34.364 25.111 1.00127.79 N ANISOU 1646 N ALA A 232 13137 14431 20987 456 -2785 613 N ATOM 1647 CA ALA A 232 19.819 34.562 24.280 1.00125.07 C ANISOU 1647 CA ALA A 232 13019 13810 20694 774 -2431 704 C ATOM 1648 C ALA A 232 20.885 35.359 25.026 1.00125.45 C ANISOU 1648 C ALA A 232 12835 13411 21421 690 -1841 389 C ATOM 1649 O ALA A 232 22.079 35.115 24.863 1.00119.57 O ANISOU 1649 O ALA A 232 12279 12463 20690 724 -1709 215 O ATOM 1650 CB ALA A 232 19.442 35.261 22.982 1.00122.47 C ANISOU 1650 CB ALA A 232 12721 13483 20329 1280 -2152 1301 C ATOM 1651 N LYS A 233 20.447 36.314 25.840 1.00128.39 N ANISOU 1651 N LYS A 233 12801 13631 22351 586 -1492 326 N ATOM 1652 CA LYS A 233 21.365 37.114 26.640 1.00124.07 C ANISOU 1652 CA LYS A 233 12030 12647 22467 469 -958 23 C ATOM 1653 C LYS A 233 22.031 36.251 27.704 1.00118.18 C ANISOU 1653 C LYS A 233 11367 11871 21663 0 -1265 -560 C ATOM 1654 O LYS A 233 23.248 36.297 27.879 1.00119.99 O ANISOU 1654 O LYS A 233 11657 11804 22127 -49 -1024 -796 O ATOM 1655 CB LYS A 233 20.637 38.292 27.291 1.00127.32 C ANISOU 1655 CB LYS A 233 12024 12914 23440 466 -560 86 C ATOM 1656 CG LYS A 233 21.531 39.165 28.159 1.00131.03 C ANISOU 1656 CG LYS A 233 12278 12906 24601 329 -23 -223 C ATOM 1657 CD LYS A 233 20.818 40.434 28.608 1.00141.39 C ANISOU 1657 CD LYS A 233 13226 14043 26454 424 418 -90 C ATOM 1658 CE LYS A 233 21.761 41.353 29.378 1.00147.61 C ANISOU 1658 CE LYS A 233 13845 14315 27925 310 960 -363 C ATOM 1659 NZ LYS A 233 21.129 42.655 29.733 1.00153.87 N ANISOU 1659 NZ LYS A 233 14327 14890 29248 452 1423 -213 N ATOM 1660 N SER A 234 21.226 35.462 28.408 1.00117.07 N ANISOU 1660 N SER A 234 11225 12047 21210 -348 -1805 -779 N ATOM 1661 CA SER A 234 21.746 34.537 29.406 1.00117.35 C ANISOU 1661 CA SER A 234 11369 12098 21122 -811 -2177 -1325 C ATOM 1662 C SER A 234 22.760 33.594 28.770 1.00117.45 C ANISOU 1662 C SER A 234 11787 12119 20721 -746 -2423 -1410 C ATOM 1663 O SER A 234 23.811 33.315 29.348 1.00121.19 O ANISOU 1663 O SER A 234 12320 12374 21353 -961 -2380 -1803 O ATOM 1664 CB SER A 234 20.609 33.732 30.037 1.00119.87 C ANISOU 1664 CB SER A 234 11670 12824 21052 -1155 -2788 -1455 C ATOM 1665 OG SER A 234 19.654 34.586 30.641 1.00121.35 O ANISOU 1665 OG SER A 234 11471 13027 21608 -1198 -2553 -1374 O ATOM 1666 N ALA A 235 22.437 33.107 27.576 1.00113.61 N ANISOU 1666 N ALA A 235 11587 11882 19699 -441 -2682 -1034 N ATOM 1667 CA ALA A 235 23.331 32.222 26.840 1.00109.21 C ANISOU 1667 CA ALA A 235 11450 11350 18694 -308 -2908 -1063 C ATOM 1668 C ALA A 235 24.652 32.921 26.549 1.00112.38 C ANISOU 1668 C ALA A 235 11808 11350 19541 -75 -2290 -1063 C ATOM 1669 O ALA A 235 25.718 32.310 26.622 1.00115.24 O ANISOU 1669 O ALA A 235 12377 11611 19798 -147 -2367 -1333 O ATOM 1670 CB ALA A 235 22.678 31.764 25.548 1.00108.94 C ANISOU 1670 CB ALA A 235 11722 11621 18049 27 -3224 -602 C ATOM 1671 N ALA A 236 24.572 34.205 26.216 1.00111.18 N ANISOU 1671 N ALA A 236 11384 10975 19886 205 -1682 -746 N ATOM 1672 CA ALA A 236 25.762 35.001 25.948 1.00107.02 C ANISOU 1672 CA ALA A 236 10772 10059 19833 417 -1060 -698 C ATOM 1673 C ALA A 236 26.636 35.097 27.193 1.00111.84 C ANISOU 1673 C ALA A 236 11205 10378 20912 27 -909 -1210 C ATOM 1674 O ALA A 236 27.860 35.003 27.111 1.00120.10 O ANISOU 1674 O ALA A 236 12334 11213 22086 56 -711 -1347 O ATOM 1675 CB ALA A 236 25.373 36.388 25.463 1.00107.12 C ANISOU 1675 CB ALA A 236 10514 9886 20300 745 -476 -268 C ATOM 1676 N ILE A 237 25.997 35.284 28.344 1.00110.61 N ANISOU 1676 N ILE A 237 10804 10217 21005 -336 -1005 -1483 N ATOM 1677 CA ILE A 237 26.711 35.376 29.611 1.00112.19 C ANISOU 1677 CA ILE A 237 10843 10144 21641 -742 -900 -1982 C ATOM 1678 C ILE A 237 27.386 34.054 29.958 1.00111.17 C ANISOU 1678 C ILE A 237 10996 10135 21107 -1022 -1406 -2386 C ATOM 1679 O ILE A 237 28.421 34.031 30.622 1.00105.65 O ANISOU 1679 O ILE A 237 10255 9173 20714 -1243 -1272 -2734 O ATOM 1680 CB ILE A 237 25.766 35.777 30.760 1.00110.64 C ANISOU 1680 CB ILE A 237 10358 9959 21722 -1063 -941 -2184 C ATOM 1681 CG1 ILE A 237 25.012 37.062 30.411 1.00107.07 C ANISOU 1681 CG1 ILE A 237 9636 9404 21640 -761 -466 -1777 C ATOM 1682 CG2 ILE A 237 26.544 35.950 32.057 1.00109.40 C ANISOU 1682 CG2 ILE A 237 10051 9479 22039 -1473 -800 -2691 C ATOM 1683 CD1 ILE A 237 24.089 37.540 31.508 1.00100.02 C ANISOU 1683 CD1 ILE A 237 8452 8513 21039 -1023 -448 -1952 C ATOM 1684 N ILE A 238 26.795 32.953 29.505 1.00113.63 N ANISOU 1684 N ILE A 238 11607 10840 20728 -1014 -2002 -2330 N ATOM 1685 CA ILE A 238 27.355 31.630 29.754 1.00119.04 C ANISOU 1685 CA ILE A 238 12610 11662 20959 -1253 -2536 -2690 C ATOM 1686 C ILE A 238 28.639 31.419 28.955 1.00124.21 C ANISOU 1686 C ILE A 238 13488 12170 21537 -964 -2340 -2624 C ATOM 1687 O ILE A 238 29.646 30.954 29.489 1.00120.63 O ANISOU 1687 O ILE A 238 13102 11571 21162 -1171 -2399 -2995 O ATOM 1688 CB ILE A 238 26.348 30.513 29.415 1.00117.17 C ANISOU 1688 CB ILE A 238 12667 11879 19973 -1308 -3249 -2614 C ATOM 1689 CG1 ILE A 238 25.078 30.672 30.250 1.00123.86 C ANISOU 1689 CG1 ILE A 238 13268 12907 20887 -1615 -3458 -2678 C ATOM 1690 CG2 ILE A 238 26.966 29.145 29.655 1.00114.17 C ANISOU 1690 CG2 ILE A 238 12649 11614 19116 -1542 -3808 -2990 C ATOM 1691 CD1 ILE A 238 24.021 29.629 29.958 1.00132.49 C ANISOU 1691 CD1 ILE A 238 14612 14456 21273 -1705 -4165 -2573 C ATOM 1692 N ALA A 239 28.595 31.766 27.672 1.00128.27 N ANISOU 1692 N ALA A 239 14112 12728 21896 -479 -2101 -2142 N ATOM 1693 CA ALA A 239 29.758 31.634 26.803 1.00125.22 C ANISOU 1693 CA ALA A 239 13929 12227 21422 -147 -1866 -2015 C ATOM 1694 C ALA A 239 30.812 32.677 27.150 1.00128.39 C ANISOU 1694 C ALA A 239 14015 12207 22561 -138 -1195 -2070 C ATOM 1695 O ALA A 239 32.012 32.413 27.068 1.00130.82 O ANISOU 1695 O ALA A 239 14408 12371 22926 -97 -1066 -2208 O ATOM 1696 CB ALA A 239 29.347 31.765 25.350 1.00124.06 C ANISOU 1696 CB ALA A 239 13985 12246 20906 362 -1789 -1468 C ATOM 1697 N GLY A 240 30.355 33.863 27.536 1.00128.16 N ANISOU 1697 N GLY A 240 13625 11979 23093 -173 -774 -1951 N ATOM 1698 CA GLY A 240 31.252 34.934 27.925 1.00128.21 C ANISOU 1698 CA GLY A 240 13328 11562 23824 -198 -152 -1990 C ATOM 1699 C GLY A 240 32.164 34.518 29.061 1.00125.69 C ANISOU 1699 C GLY A 240 12955 11060 23741 -626 -261 -2523 C ATOM 1700 O GLY A 240 33.363 34.795 29.039 1.00124.52 O ANISOU 1700 O GLY A 240 12741 10652 23920 -588 83 -2570 O ATOM 1701 N LEU A 241 31.593 33.848 30.056 1.00128.01 N ANISOU 1701 N LEU A 241 13271 11496 23869 -1043 -747 -2913 N ATOM 1702 CA LEU A 241 32.364 33.378 31.200 1.00127.06 C ANISOU 1702 CA LEU A 241 13120 11220 23935 -1486 -916 -3443 C ATOM 1703 C LEU A 241 33.320 32.257 30.811 1.00122.41 C ANISOU 1703 C LEU A 241 12846 10743 22922 -1431 -1215 -3589 C ATOM 1704 O LEU A 241 34.259 31.952 31.544 1.00129.26 O ANISOU 1704 O LEU A 241 13686 11434 23992 -1706 -1252 -3963 O ATOM 1705 CB LEU A 241 31.438 32.904 32.321 1.00134.23 C ANISOU 1705 CB LEU A 241 13994 12284 24723 -1938 -1385 -3804 C ATOM 1706 CG LEU A 241 30.588 33.972 33.010 1.00138.37 C ANISOU 1706 CG LEU A 241 14184 12667 25723 -2070 -1098 -3774 C ATOM 1707 CD1 LEU A 241 29.714 33.341 34.082 1.00140.62 C ANISOU 1707 CD1 LEU A 241 14465 13159 25807 -2514 -1606 -4136 C ATOM 1708 CD2 LEU A 241 31.467 35.059 33.602 1.00129.12 C ANISOU 1708 CD2 LEU A 241 12735 11014 25310 -2167 -519 -3882 C ATOM 1709 N PHE A 242 33.078 31.639 29.660 1.00111.92 N ANISOU 1709 N PHE A 242 11827 9701 20996 -1068 -1436 -3294 N ATOM 1710 CA PHE A 242 33.948 30.570 29.188 1.00106.97 C ANISOU 1710 CA PHE A 242 11537 9189 19916 -950 -1712 -3402 C ATOM 1711 C PHE A 242 35.287 31.129 28.717 1.00108.91 C ANISOU 1711 C PHE A 242 11677 9165 20539 -691 -1147 -3260 C ATOM 1712 O PHE A 242 36.341 30.776 29.249 1.00100.27 O ANISOU 1712 O PHE A 242 10568 7924 19607 -876 -1155 -3576 O ATOM 1713 CB PHE A 242 33.280 29.772 28.068 1.00104.30 C ANISOU 1713 CB PHE A 242 11595 9222 18812 -622 -2111 -3114 C ATOM 1714 CG PHE A 242 34.064 28.565 27.638 1.00108.43 C ANISOU 1714 CG PHE A 242 12521 9883 18796 -509 -2472 -3260 C ATOM 1715 CD1 PHE A 242 33.839 27.331 28.224 1.00111.95 C ANISOU 1715 CD1 PHE A 242 13236 10527 18773 -831 -3160 -3645 C ATOM 1716 CD2 PHE A 242 35.031 28.665 26.652 1.00114.33 C ANISOU 1716 CD2 PHE A 242 13382 10560 19499 -74 -2120 -3008 C ATOM 1717 CE1 PHE A 242 34.561 26.219 27.833 1.00115.66 C ANISOU 1717 CE1 PHE A 242 14099 11108 18738 -709 -3499 -3786 C ATOM 1718 CE2 PHE A 242 35.756 27.558 26.257 1.00119.78 C ANISOU 1718 CE2 PHE A 242 14450 11377 19683 61 -2437 -3143 C ATOM 1719 CZ PHE A 242 35.521 26.333 26.847 1.00117.64 C ANISOU 1719 CZ PHE A 242 14462 11289 18947 -250 -3131 -3537 C ATOM 1720 N ALA A 243 35.238 32.004 27.718 1.00113.17 N ANISOU 1720 N ALA A 243 12133 9645 21220 -266 -662 -2770 N ATOM 1721 CA ALA A 243 36.440 32.658 27.220 1.00111.11 C ANISOU 1721 CA ALA A 243 11736 9133 21346 -9 -79 -2571 C ATOM 1722 C ALA A 243 37.150 33.385 28.354 1.00116.32 C ANISOU 1722 C ALA A 243 12026 9414 22754 -381 251 -2856 C ATOM 1723 O ALA A 243 38.376 33.389 28.432 1.00131.21 O ANISOU 1723 O ALA A 243 13843 11124 24889 -388 478 -2947 O ATOM 1724 CB ALA A 243 36.091 33.627 26.103 1.00111.17 C ANISOU 1724 CB ALA A 243 11674 9117 21450 445 394 -2000 C ATOM 1725 N LEU A 244 36.367 33.989 29.240 1.00108.70 N ANISOU 1725 N LEU A 244 10832 8330 22139 -690 266 -2993 N ATOM 1726 CA LEU A 244 36.913 34.756 30.353 1.00112.80 C ANISOU 1726 CA LEU A 244 11023 8466 23371 -1055 570 -3256 C ATOM 1727 C LEU A 244 37.696 33.874 31.325 1.00123.36 C ANISOU 1727 C LEU A 244 12419 9759 24693 -1462 220 -3783 C ATOM 1728 O LEU A 244 38.578 34.354 32.037 1.00125.98 O ANISOU 1728 O LEU A 244 12529 9764 25576 -1703 490 -3975 O ATOM 1729 CB LEU A 244 35.790 35.487 31.094 1.00109.97 C ANISOU 1729 CB LEU A 244 10457 8024 23301 -1279 606 -3307 C ATOM 1730 CG LEU A 244 36.206 36.437 32.218 1.00106.77 C ANISOU 1730 CG LEU A 244 9730 7191 23647 -1628 954 -3540 C ATOM 1731 CD1 LEU A 244 37.142 37.514 31.690 1.00112.59 C ANISOU 1731 CD1 LEU A 244 10273 7595 24910 -1390 1607 -3218 C ATOM 1732 CD2 LEU A 244 34.983 37.059 32.871 1.00101.96 C ANISOU 1732 CD2 LEU A 244 8965 6551 23222 -1793 954 -3578 C ATOM 1733 N CYS A 245 37.371 32.586 31.356 1.00131.38 N ANISOU 1733 N CYS A 245 13745 11097 25078 -1546 -396 -4009 N ATOM 1734 CA CYS A 245 38.009 31.664 32.292 1.00139.70 C ANISOU 1734 CA CYS A 245 14886 12132 26062 -1940 -794 -4522 C ATOM 1735 C CYS A 245 39.047 30.767 31.623 1.00143.16 C ANISOU 1735 C CYS A 245 15575 12687 26132 -1704 -921 -4523 C ATOM 1736 O CYS A 245 39.716 29.982 32.291 1.00144.81 O ANISOU 1736 O CYS A 245 15868 12876 26279 -1979 -1229 -4922 O ATOM 1737 CB CYS A 245 36.960 30.805 33.003 1.00139.48 C ANISOU 1737 CB CYS A 245 15027 12356 25614 -2281 -1440 -4844 C ATOM 1738 SG CYS A 245 35.874 31.720 34.120 1.00152.50 S ANISOU 1738 SG CYS A 245 16363 13857 27724 -2656 -1338 -4976 S ATOM 1739 N TRP A 246 39.178 30.882 30.306 1.00144.33 N ANISOU 1739 N TRP A 246 15849 12958 26031 -1186 -684 -4076 N ATOM 1740 CA TRP A 246 40.112 30.042 29.561 1.00140.19 C ANISOU 1740 CA TRP A 246 15588 12569 25110 -892 -778 -4037 C ATOM 1741 C TRP A 246 41.171 30.849 28.816 1.00136.23 C ANISOU 1741 C TRP A 246 14894 11876 24991 -539 -118 -3681 C ATOM 1742 O TRP A 246 42.293 30.383 28.634 1.00136.80 O ANISOU 1742 O TRP A 246 15025 11935 25019 -432 -71 -3751 O ATOM 1743 CB TRP A 246 39.357 29.128 28.593 1.00141.51 C ANISOU 1743 CB TRP A 246 16191 13121 24456 -572 -1213 -3857 C ATOM 1744 CG TRP A 246 38.630 28.009 29.279 1.00143.85 C ANISOU 1744 CG TRP A 246 16747 13638 24273 -921 -1953 -4249 C ATOM 1745 CD1 TRP A 246 37.379 28.053 29.813 1.00149.45 C ANISOU 1745 CD1 TRP A 246 17423 14452 24907 -1194 -2250 -4330 C ATOM 1746 CD2 TRP A 246 39.118 26.681 29.510 1.00146.23 C ANISOU 1746 CD2 TRP A 246 17376 14083 24102 -1035 -2490 -4604 C ATOM 1747 NE1 TRP A 246 37.053 26.835 30.358 1.00152.59 N ANISOU 1747 NE1 TRP A 246 18106 15057 24814 -1489 -2944 -4704 N ATOM 1748 CE2 TRP A 246 38.104 25.974 30.186 1.00150.88 C ANISOU 1748 CE2 TRP A 246 18127 14856 24344 -1400 -3112 -4885 C ATOM 1749 CE3 TRP A 246 40.312 26.021 29.209 1.00144.32 C ANISOU 1749 CE3 TRP A 246 17305 13835 23695 -857 -2506 -4704 C ATOM 1750 CZ2 TRP A 246 38.247 24.640 30.565 1.00150.14 C ANISOU 1750 CZ2 TRP A 246 18377 14925 23744 -1603 -3759 -5263 C ATOM 1751 CZ3 TRP A 246 40.452 24.701 29.585 1.00143.17 C ANISOU 1751 CZ3 TRP A 246 17502 13847 23049 -1036 -3139 -5086 C ATOM 1752 CH2 TRP A 246 39.427 24.023 30.256 1.00146.65 C ANISOU 1752 CH2 TRP A 246 18116 14454 23150 -1413 -3765 -5364 C ATOM 1753 N LEU A 247 40.814 32.054 28.385 1.00132.02 N ANISOU 1753 N LEU A 247 14130 11201 24830 -355 386 -3291 N ATOM 1754 CA LEU A 247 41.762 32.922 27.691 1.00135.95 C ANISOU 1754 CA LEU A 247 14423 11506 25727 -45 1034 -2921 C ATOM 1755 C LEU A 247 43.059 33.120 28.471 1.00139.39 C ANISOU 1755 C LEU A 247 14595 11654 26712 -321 1258 -3169 C ATOM 1756 O LEU A 247 44.140 32.909 27.926 1.00140.58 O ANISOU 1756 O LEU A 247 14759 11817 26837 -82 1462 -3046 O ATOM 1757 CB LEU A 247 41.129 34.269 27.341 1.00131.57 C ANISOU 1757 CB LEU A 247 13631 10786 25573 99 1518 -2521 C ATOM 1758 CG LEU A 247 40.153 34.275 26.165 1.00128.60 C ANISOU 1758 CG LEU A 247 13484 10673 24706 533 1484 -2097 C ATOM 1759 CD1 LEU A 247 39.718 35.705 25.851 1.00129.33 C ANISOU 1759 CD1 LEU A 247 13304 10551 25286 677 2028 -1698 C ATOM 1760 CD2 LEU A 247 40.771 33.629 24.950 1.00129.52 C ANISOU 1760 CD2 LEU A 247 13889 11008 24314 1005 1501 -1841 C ATOM 1761 N PRO A 248 42.958 33.500 29.756 1.00139.64 N ANISOU 1761 N PRO A 248 14393 11435 27228 -827 1208 -3517 N ATOM 1762 CA PRO A 248 44.172 33.718 30.550 1.00138.14 C ANISOU 1762 CA PRO A 248 13951 10951 27584 -1127 1399 -3753 C ATOM 1763 C PRO A 248 45.146 32.547 30.440 1.00142.30 C ANISOU 1763 C PRO A 248 14668 11644 27756 -1070 1115 -3960 C ATOM 1764 O PRO A 248 46.360 32.746 30.333 1.00151.38 O ANISOU 1764 O PRO A 248 15644 12652 29222 -1008 1435 -3884 O ATOM 1765 CB PRO A 248 43.637 33.820 31.978 1.00132.47 C ANISOU 1765 CB PRO A 248 13120 10056 27158 -1694 1132 -4203 C ATOM 1766 CG PRO A 248 42.253 34.349 31.813 1.00136.49 C ANISOU 1766 CG PRO A 248 13645 10635 27578 -1622 1137 -4022 C ATOM 1767 CD PRO A 248 41.733 33.743 30.541 1.00138.90 C ANISOU 1767 CD PRO A 248 14259 11319 27197 -1143 975 -3704 C ATOM 1768 N LEU A 249 44.606 31.335 30.452 1.00135.37 N ANISOU 1768 N LEU A 249 14147 11068 26218 -1084 513 -4206 N ATOM 1769 CA LEU A 249 45.424 30.134 30.377 1.00130.29 C ANISOU 1769 CA LEU A 249 13738 10593 25175 -1025 176 -4435 C ATOM 1770 C LEU A 249 46.127 30.009 29.028 1.00126.06 C ANISOU 1770 C LEU A 249 13320 10211 24364 -440 478 -4024 C ATOM 1771 O LEU A 249 47.326 29.724 28.959 1.00117.34 O ANISOU 1771 O LEU A 249 12155 9071 23359 -355 611 -4063 O ATOM 1772 CB LEU A 249 44.558 28.910 30.660 1.00126.36 C ANISOU 1772 CB LEU A 249 13627 10377 24007 -1171 -557 -4765 C ATOM 1773 CG LEU A 249 45.283 27.630 31.057 1.00116.77 C ANISOU 1773 CG LEU A 249 12644 9270 22453 -1301 -1032 -5167 C ATOM 1774 CD1 LEU A 249 46.474 27.961 31.927 1.00120.52 C ANISOU 1774 CD1 LEU A 249 12787 9441 23564 -1611 -798 -5397 C ATOM 1775 CD2 LEU A 249 44.312 26.714 31.778 1.00105.39 C ANISOU 1775 CD2 LEU A 249 11472 7996 20574 -1654 -1737 -5563 C ATOM 1776 N HIS A 250 45.370 30.231 27.960 1.00133.57 N ANISOU 1776 N HIS A 250 14439 11341 24971 -33 590 -3622 N ATOM 1777 CA HIS A 250 45.922 30.218 26.617 1.00134.51 C ANISOU 1777 CA HIS A 250 14683 11604 24821 546 915 -3189 C ATOM 1778 C HIS A 250 46.826 31.426 26.421 1.00131.03 C ANISOU 1778 C HIS A 250 13822 10892 25073 637 1638 -2868 C ATOM 1779 O HIS A 250 47.872 31.329 25.786 1.00132.75 O ANISOU 1779 O HIS A 250 14013 11149 25279 947 1927 -2671 O ATOM 1780 CB HIS A 250 44.803 30.209 25.570 1.00140.97 C ANISOU 1780 CB HIS A 250 15789 12659 25114 923 836 -2837 C ATOM 1781 CG HIS A 250 43.943 28.983 25.610 1.00136.88 C ANISOU 1781 CG HIS A 250 15718 12433 23860 873 115 -3090 C ATOM 1782 ND1 HIS A 250 44.249 27.833 24.910 1.00137.26 N ANISOU 1782 ND1 HIS A 250 16195 12741 23215 1195 -211 -3109 N ATOM 1783 CD2 HIS A 250 42.777 28.730 26.251 1.00132.66 C ANISOU 1783 CD2 HIS A 250 15274 11971 23161 543 -347 -3319 C ATOM 1784 CE1 HIS A 250 43.316 26.925 25.129 1.00133.76 C ANISOU 1784 CE1 HIS A 250 16099 12504 22219 1044 -862 -3342 C ATOM 1785 NE2 HIS A 250 42.410 27.444 25.940 1.00133.22 N ANISOU 1785 NE2 HIS A 250 15818 12338 22461 643 -954 -3467 N ATOM 1786 N ILE A 251 46.404 32.566 26.958 1.00129.43 N ANISOU 1786 N ILE A 251 13298 10417 25462 373 1926 -2804 N ATOM 1787 CA ILE A 251 47.192 33.791 26.901 1.00132.51 C ANISOU 1787 CA ILE A 251 13283 10505 26561 385 2583 -2516 C ATOM 1788 C ILE A 251 48.580 33.546 27.470 1.00134.66 C ANISOU 1788 C ILE A 251 13358 10640 27167 187 2662 -2734 C ATOM 1789 O ILE A 251 49.580 33.961 26.890 1.00134.36 O ANISOU 1789 O ILE A 251 13137 10545 27370 430 3125 -2423 O ATOM 1790 CB ILE A 251 46.525 34.935 27.689 1.00128.76 C ANISOU 1790 CB ILE A 251 12525 9717 26683 26 2771 -2543 C ATOM 1791 CG1 ILE A 251 45.374 35.535 26.884 1.00127.09 C ANISOU 1791 CG1 ILE A 251 12403 9593 26292 327 2916 -2157 C ATOM 1792 CG2 ILE A 251 47.541 36.017 28.023 1.00131.63 C ANISOU 1792 CG2 ILE A 251 12472 9708 27834 -130 3323 -2408 C ATOM 1793 CD1 ILE A 251 44.685 36.692 27.575 1.00126.05 C ANISOU 1793 CD1 ILE A 251 12009 9161 26725 39 3128 -2152 C ATOM 1794 N ILE A 252 48.631 32.873 28.614 1.00135.52 N ANISOU 1794 N ILE A 252 13497 10702 27294 -262 2205 -3259 N ATOM 1795 CA ILE A 252 49.897 32.491 29.223 1.00133.69 C ANISOU 1795 CA ILE A 252 13109 10362 27325 -475 2187 -3513 C ATOM 1796 C ILE A 252 50.731 31.652 28.265 1.00134.14 C ANISOU 1796 C ILE A 252 13359 10696 26914 -8 2197 -3357 C ATOM 1797 O ILE A 252 51.903 31.940 28.052 1.00143.27 O ANISOU 1797 O ILE A 252 14270 11766 28399 103 2584 -3179 O ATOM 1798 CB ILE A 252 49.681 31.712 30.539 1.00132.34 C ANISOU 1798 CB ILE A 252 13027 10149 27108 -1003 1598 -4124 C ATOM 1799 CG1 ILE A 252 49.250 32.664 31.657 1.00134.17 C ANISOU 1799 CG1 ILE A 252 12979 10028 27971 -1512 1693 -4300 C ATOM 1800 CG2 ILE A 252 50.943 30.968 30.941 1.00129.72 C ANISOU 1800 CG2 ILE A 252 12651 9813 26824 -1113 1461 -4384 C ATOM 1801 CD1 ILE A 252 49.120 32.006 33.010 1.00132.18 C ANISOU 1801 CD1 ILE A 252 12780 9698 27742 -2061 1167 -4891 C ATOM 1802 N ASN A 253 50.123 30.621 27.688 1.00131.17 N ANISOU 1802 N ASN A 253 13423 10650 25765 267 1772 -3413 N ATOM 1803 CA ASN A 253 50.838 29.723 26.790 1.00135.67 C ANISOU 1803 CA ASN A 253 14248 11493 25810 732 1727 -3300 C ATOM 1804 C ASN A 253 51.289 30.426 25.506 1.00140.62 C ANISOU 1804 C ASN A 253 14774 12171 26485 1268 2351 -2706 C ATOM 1805 O ASN A 253 52.361 30.157 24.987 1.00150.43 O ANISOU 1805 O ASN A 253 15979 13503 27675 1566 2581 -2559 O ATOM 1806 CB ASN A 253 49.966 28.521 26.423 1.00144.12 C ANISOU 1806 CB ASN A 253 15858 12883 26017 906 1114 -3470 C ATOM 1807 CG ASN A 253 49.697 27.622 27.581 1.00147.48 C ANISOU 1807 CG ASN A 253 16430 13309 26299 431 468 -4050 C ATOM 1808 OD1 ASN A 253 50.393 27.669 28.581 1.00151.10 O ANISOU 1808 OD1 ASN A 253 16630 13563 27219 36 452 -4353 O ATOM 1809 ND2 ASN A 253 48.680 26.784 27.453 1.00144.26 N ANISOU 1809 ND2 ASN A 253 16445 13129 25239 454 -87 -4201 N ATOM 1810 N CYS A 254 50.448 31.312 24.988 1.00140.28 N ANISOU 1810 N CYS A 254 14692 12082 26527 1397 2619 -2360 N ATOM 1811 CA CYS A 254 50.782 32.132 23.835 1.00144.92 C ANISOU 1811 CA CYS A 254 15158 12679 27226 1853 3233 -1782 C ATOM 1812 C CYS A 254 52.076 32.891 24.092 1.00149.01 C ANISOU 1812 C CYS A 254 15208 12960 28451 1744 3761 -1641 C ATOM 1813 O CYS A 254 52.893 33.037 23.193 1.00152.20 O ANISOU 1813 O CYS A 254 15545 13459 28825 2149 4175 -1269 O ATOM 1814 CB CYS A 254 49.636 33.103 23.543 1.00143.32 C ANISOU 1814 CB CYS A 254 14918 12384 27154 1872 3414 -1500 C ATOM 1815 SG CYS A 254 48.114 32.302 22.953 1.00164.90 S ANISOU 1815 SG CYS A 254 18192 15439 29025 2098 2864 -1518 S ATOM 1816 N PHE A 255 52.274 33.347 25.326 1.00146.56 N ANISOU 1816 N PHE A 255 14581 12345 28761 1190 3735 -1937 N ATOM 1817 CA PHE A 255 53.509 34.027 25.706 1.00144.61 C ANISOU 1817 CA PHE A 255 13886 11849 29208 1009 4169 -1840 C ATOM 1818 C PHE A 255 54.680 33.050 25.685 1.00137.75 C ANISOU 1818 C PHE A 255 13045 11151 28141 1129 4051 -1992 C ATOM 1819 O PHE A 255 55.694 33.306 25.044 1.00140.28 O ANISOU 1819 O PHE A 255 13170 11515 28616 1417 4495 -1649 O ATOM 1820 CB PHE A 255 53.381 34.640 27.104 1.00145.92 C ANISOU 1820 CB PHE A 255 13771 11643 30030 361 4085 -2172 C ATOM 1821 CG PHE A 255 52.661 35.963 27.136 1.00153.80 C ANISOU 1821 CG PHE A 255 14585 12375 31476 248 4425 -1919 C ATOM 1822 CD1 PHE A 255 51.693 36.270 26.193 1.00159.65 C ANISOU 1822 CD1 PHE A 255 15522 13258 31880 618 4537 -1584 C ATOM 1823 CD2 PHE A 255 52.952 36.899 28.118 1.00155.36 C ANISOU 1823 CD2 PHE A 255 14430 12170 32430 -229 4619 -2018 C ATOM 1824 CE1 PHE A 255 51.036 37.488 26.223 1.00159.27 C ANISOU 1824 CE1 PHE A 255 15308 12962 32247 531 4847 -1351 C ATOM 1825 CE2 PHE A 255 52.298 38.115 28.150 1.00156.46 C ANISOU 1825 CE2 PHE A 255 14426 12051 32973 -314 4927 -1791 C ATOM 1826 CZ PHE A 255 51.342 38.410 27.205 1.00156.43 C ANISOU 1826 CZ PHE A 255 14605 12197 32633 72 5045 -1459 C ATOM 1827 N THR A 256 54.523 31.928 26.384 1.00127.02 N ANISOU 1827 N THR A 256 11932 9897 26434 914 3449 -2499 N ATOM 1828 CA THR A 256 55.574 30.929 26.508 1.00126.79 C ANISOU 1828 CA THR A 256 11950 10013 26212 987 3262 -2713 C ATOM 1829 C THR A 256 56.029 30.394 25.156 1.00137.31 C ANISOU 1829 C THR A 256 13510 11677 26985 1663 3448 -2367 C ATOM 1830 O THR A 256 57.219 30.228 24.924 1.00151.31 O ANISOU 1830 O THR A 256 15104 13509 28877 1847 3699 -2249 O ATOM 1831 CB THR A 256 55.117 29.757 27.397 1.00112.48 C ANISOU 1831 CB THR A 256 10449 8277 24013 673 2524 -3311 C ATOM 1832 OG1 THR A 256 54.777 30.241 28.705 1.00104.07 O ANISOU 1832 OG1 THR A 256 9162 6900 23479 36 2365 -3646 O ATOM 1833 CG2 THR A 256 56.216 28.715 27.510 1.00107.53 C ANISOU 1833 CG2 THR A 256 9884 7794 23180 772 2324 -3531 C ATOM 1834 N PHE A 257 55.084 30.149 24.257 1.00129.13 N ANISOU 1834 N PHE A 257 12863 10856 25343 2038 3337 -2189 N ATOM 1835 CA PHE A 257 55.408 29.596 22.944 1.00131.58 C ANISOU 1835 CA PHE A 257 13464 11482 25047 2699 3477 -1873 C ATOM 1836 C PHE A 257 55.980 30.636 21.988 1.00143.01 C ANISOU 1836 C PHE A 257 14620 12903 26813 3057 4220 -1268 C ATOM 1837 O PHE A 257 57.121 30.521 21.563 1.00150.97 O ANISOU 1837 O PHE A 257 15475 14006 27879 3331 4542 -1077 O ATOM 1838 CB PHE A 257 54.168 28.950 22.317 1.00128.10 C ANISOU 1838 CB PHE A 257 13575 11272 23826 2958 3059 -1890 C ATOM 1839 CG PHE A 257 54.393 28.416 20.927 1.00131.29 C ANISOU 1839 CG PHE A 257 14335 11983 23566 3648 3191 -1555 C ATOM 1840 CD1 PHE A 257 54.748 27.091 20.726 1.00109.09 C ANISOU 1840 CD1 PHE A 257 11924 9412 20114 3901 2788 -1795 C ATOM 1841 CD2 PHE A 257 54.248 29.240 19.819 1.00113.39 C ANISOU 1841 CD2 PHE A 257 12024 9755 21305 4051 3713 -999 C ATOM 1842 CE1 PHE A 257 54.961 26.603 19.448 1.00122.38 C ANISOU 1842 CE1 PHE A 257 13965 11366 21170 4554 2914 -1491 C ATOM 1843 CE2 PHE A 257 54.461 28.756 18.546 1.00116.49 C ANISOU 1843 CE2 PHE A 257 12761 10424 21077 4688 3841 -691 C ATOM 1844 CZ PHE A 257 54.818 27.438 18.361 1.00115.96 C ANISOU 1844 CZ PHE A 257 13099 10591 20369 4945 3446 -939 C ATOM 1845 N PHE A 258 55.176 31.631 21.628 1.00145.19 N ANISOU 1845 N PHE A 258 14827 13063 27274 3067 4487 -957 N ATOM 1846 CA PHE A 258 55.601 32.648 20.670 1.00152.55 C ANISOU 1846 CA PHE A 258 15518 13968 28475 3407 5175 -362 C ATOM 1847 C PHE A 258 56.777 33.465 21.186 1.00151.34 C ANISOU 1847 C PHE A 258 14799 13571 29132 3142 5638 -243 C ATOM 1848 O PHE A 258 57.519 34.052 20.403 1.00154.45 O ANISOU 1848 O PHE A 258 14972 13998 29715 3451 6199 227 O ATOM 1849 CB PHE A 258 54.436 33.574 20.321 1.00157.18 C ANISOU 1849 CB PHE A 258 16139 14441 29140 3408 5318 -96 C ATOM 1850 CG PHE A 258 53.351 32.909 19.520 1.00158.79 C ANISOU 1850 CG PHE A 258 16879 14912 28542 3768 4974 -55 C ATOM 1851 CD1 PHE A 258 52.221 32.392 20.140 1.00157.85 C ANISOU 1851 CD1 PHE A 258 17028 14806 28140 3486 4379 -441 C ATOM 1852 CD2 PHE A 258 53.464 32.798 18.144 1.00162.79 C ANISOU 1852 CD2 PHE A 258 17626 15658 28569 4381 5240 381 C ATOM 1853 CE1 PHE A 258 51.232 31.786 19.401 1.00160.74 C ANISOU 1853 CE1 PHE A 258 17881 15416 27777 3796 4045 -380 C ATOM 1854 CE2 PHE A 258 52.473 32.188 17.402 1.00164.69 C ANISOU 1854 CE2 PHE A 258 18378 16129 28067 4701 4904 429 C ATOM 1855 CZ PHE A 258 51.359 31.683 18.033 1.00164.91 C ANISOU 1855 CZ PHE A 258 18659 16165 27836 4400 4299 52 C ATOM 1856 N CYS A 259 56.942 33.493 22.504 1.00175.49 N ANISOU 1856 N CYS A 259 13646 21232 31799 5759 -3334 -1095 N ATOM 1857 CA CYS A 259 58.039 34.220 23.119 1.00170.88 C ANISOU 1857 CA CYS A 259 13655 20326 30946 5255 -2998 -402 C ATOM 1858 C CYS A 259 58.800 33.313 24.082 1.00165.29 C ANISOU 1858 C CYS A 259 13027 19232 30545 4499 -2977 -435 C ATOM 1859 O CYS A 259 58.530 33.307 25.285 1.00161.92 O ANISOU 1859 O CYS A 259 12819 18182 30521 3881 -2721 -423 O ATOM 1860 CB CYS A 259 57.512 35.458 23.846 1.00167.16 C ANISOU 1860 CB CYS A 259 13640 19365 30507 5053 -2563 -24 C ATOM 1861 SG CYS A 259 58.766 36.724 24.178 1.00239.00 S ANISOU 1861 SG CYS A 259 23474 28249 39086 4713 -2157 907 S ATOM 1862 N PRO A 260 59.751 32.532 23.546 1.00160.49 N ANISOU 1862 N PRO A 260 12234 18998 29748 4551 -3255 -485 N ATOM 1863 CA PRO A 260 60.603 31.656 24.356 1.00157.61 C ANISOU 1863 CA PRO A 260 11943 18322 29619 3871 -3266 -491 C ATOM 1864 C PRO A 260 61.428 32.496 25.311 1.00157.05 C ANISOU 1864 C PRO A 260 12517 17744 29410 3243 -2840 182 C ATOM 1865 O PRO A 260 61.828 32.031 26.379 1.00154.20 O ANISOU 1865 O PRO A 260 12335 16891 29363 2541 -2713 218 O ATOM 1866 CB PRO A 260 61.518 30.997 23.320 1.00158.84 C ANISOU 1866 CB PRO A 260 11825 19097 29429 4220 -3626 -556 C ATOM 1867 CG PRO A 260 60.795 31.130 22.022 1.00160.36 C ANISOU 1867 CG PRO A 260 11622 19911 29398 5086 -3891 -843 C ATOM 1868 CD PRO A 260 60.060 32.431 22.110 1.00159.23 C ANISOU 1868 CD PRO A 260 11773 19592 29135 5277 -3583 -550 C ATOM 1869 N ASP A 261 61.669 33.740 24.910 1.00159.73 N ANISOU 1869 N ASP A 261 13205 18209 29275 3507 -2622 713 N ATOM 1870 CA ASP A 261 62.405 34.693 25.723 1.00162.59 C ANISOU 1870 CA ASP A 261 14197 18124 29454 2980 -2198 1387 C ATOM 1871 C ASP A 261 61.538 35.159 26.886 1.00159.22 C ANISOU 1871 C ASP A 261 14019 17031 29448 2539 -1856 1397 C ATOM 1872 O ASP A 261 61.993 35.213 28.029 1.00154.50 O ANISOU 1872 O ASP A 261 13786 15873 29043 1819 -1584 1657 O ATOM 1873 CB ASP A 261 62.841 35.889 24.872 1.00171.85 C ANISOU 1873 CB ASP A 261 15646 19661 29990 3446 -2082 1922 C ATOM 1874 CG ASP A 261 63.806 36.804 25.600 1.00177.13 C ANISOU 1874 CG ASP A 261 16956 19940 30404 2913 -1676 2642 C ATOM 1875 OD1 ASP A 261 63.565 37.097 26.791 1.00177.32 O ANISOU 1875 OD1 ASP A 261 17296 19327 30750 2325 -1355 2782 O ATOM 1876 OD2 ASP A 261 64.804 37.231 24.981 1.00180.00 O ANISOU 1876 OD2 ASP A 261 17507 20638 30246 3079 -1676 3064 O ATOM 1877 N CYS A 262 60.286 35.490 26.581 1.00161.84 N ANISOU 1877 N CYS A 262 14143 17432 29918 2980 -1875 1105 N ATOM 1878 CA CYS A 262 59.335 35.955 27.588 1.00156.40 C ANISOU 1878 CA CYS A 262 13642 16154 29627 2640 -1567 1065 C ATOM 1879 C CYS A 262 59.321 35.050 28.816 1.00153.57 C ANISOU 1879 C CYS A 262 13277 15244 29828 1886 -1512 809 C ATOM 1880 O CYS A 262 59.091 33.846 28.706 1.00162.44 O ANISOU 1880 O CYS A 262 13954 16501 31265 1900 -1829 256 O ATOM 1881 CB CYS A 262 57.925 36.051 26.998 1.00153.48 C ANISOU 1881 CB CYS A 262 12889 16013 29415 3256 -1712 598 C ATOM 1882 SG CYS A 262 57.711 37.377 25.786 1.00151.18 S ANISOU 1882 SG CYS A 262 12708 16216 28518 4082 -1678 951 S ATOM 1883 N SER A 263 59.565 35.645 29.981 1.00141.66 N ANISOU 1883 N SER A 263 12270 13117 28437 1231 -1109 1214 N ATOM 1884 CA SER A 263 59.604 34.910 31.240 1.00137.63 C ANISOU 1884 CA SER A 263 11831 12029 28435 459 -1007 1046 C ATOM 1885 C SER A 263 58.533 33.826 31.289 1.00138.38 C ANISOU 1885 C SER A 263 11391 12128 29058 549 -1276 284 C ATOM 1886 O SER A 263 57.338 34.121 31.311 1.00127.63 O ANISOU 1886 O SER A 263 9885 10686 27921 784 -1222 8 O ATOM 1887 CB SER A 263 59.439 35.865 32.422 1.00142.91 C ANISOU 1887 CB SER A 263 13034 12028 29237 -104 -521 1459 C ATOM 1888 OG SER A 263 58.174 36.497 32.392 1.00161.45 O ANISOU 1888 OG SER A 263 15318 14291 31736 204 -401 1287 O ATOM 1889 N HIS A 264 58.968 32.570 31.287 1.00136.03 N ANISOU 1889 N HIS A 264 10798 11936 28952 370 -1570 -60 N ATOM 1890 CA HIS A 264 58.042 31.449 31.384 1.00137.73 C ANISOU 1890 CA HIS A 264 10514 12138 29681 397 -1832 -787 C ATOM 1891 C HIS A 264 57.174 31.619 32.622 1.00143.15 C ANISOU 1891 C HIS A 264 11373 12153 30864 -135 -1530 -901 C ATOM 1892 O HIS A 264 57.685 31.824 33.723 1.00138.42 O ANISOU 1892 O HIS A 264 11202 11006 30385 -837 -1232 -559 O ATOM 1893 CB HIS A 264 58.794 30.117 31.439 1.00133.47 C ANISOU 1893 CB HIS A 264 9738 11684 29291 125 -2131 -1051 C ATOM 1894 CG HIS A 264 59.609 29.829 30.218 1.00137.07 C ANISOU 1894 CG HIS A 264 9973 12811 29296 645 -2455 -1007 C ATOM 1895 ND1 HIS A 264 59.047 29.650 28.970 1.00140.44 N ANISOU 1895 ND1 HIS A 264 9936 13860 29565 1436 -2777 -1368 N ATOM 1896 CD2 HIS A 264 60.943 29.672 30.053 1.00122.38 C ANISOU 1896 CD2 HIS A 264 8283 11102 27112 484 -2512 -657 C ATOM 1897 CE1 HIS A 264 60.000 29.406 28.091 1.00127.85 C ANISOU 1897 CE1 HIS A 264 8242 12770 27565 1737 -3012 -1236 C ATOM 1898 NE2 HIS A 264 61.162 29.413 28.722 1.00124.74 N ANISOU 1898 NE2 HIS A 264 8226 12105 27064 1171 -2857 -808 N ATOM 1899 N ALA A 265 55.861 31.545 32.434 1.00150.00 N ANISOU 1899 N ALA A 265 11907 13072 32014 204 -1606 -1381 N ATOM 1900 CA ALA A 265 54.917 31.755 33.526 1.00145.99 C ANISOU 1900 CA ALA A 265 11529 11967 31972 -233 -1324 -1526 C ATOM 1901 C ALA A 265 55.303 30.964 34.770 1.00136.81 C ANISOU 1901 C ALA A 265 10514 10241 31225 -1084 -1231 -1593 C ATOM 1902 O ALA A 265 55.531 29.755 34.697 1.00128.40 O ANISOU 1902 O ALA A 265 9127 9294 30366 -1186 -1533 -1985 O ATOM 1903 CB ALA A 265 53.512 31.395 33.084 1.00149.52 C ANISOU 1903 CB ALA A 265 11472 12615 32725 243 -1525 -2177 C ATOM 1904 N PRO A 266 55.385 31.652 35.918 1.00134.11 N ANISOU 1904 N PRO A 266 10668 9284 31005 -1700 -810 -1207 N ATOM 1905 CA PRO A 266 55.707 31.014 37.198 1.00132.76 C ANISOU 1905 CA PRO A 266 10691 8520 31233 -2549 -676 -1232 C ATOM 1906 C PRO A 266 54.715 29.904 37.513 1.00145.80 C ANISOU 1906 C PRO A 266 11898 10045 33455 -2657 -876 -1962 C ATOM 1907 O PRO A 266 53.614 29.897 36.963 1.00156.69 O ANISOU 1907 O PRO A 266 12911 11667 34958 -2151 -1005 -2388 O ATOM 1908 CB PRO A 266 55.559 32.154 38.212 1.00122.68 C ANISOU 1908 CB PRO A 266 9959 6662 29991 -3012 -177 -765 C ATOM 1909 CG PRO A 266 54.829 33.242 37.493 1.00122.66 C ANISOU 1909 CG PRO A 266 9946 6927 29732 -2373 -83 -661 C ATOM 1910 CD PRO A 266 55.184 33.102 36.060 1.00128.70 C ANISOU 1910 CD PRO A 266 10400 8430 30072 -1621 -435 -711 C ATOM 1911 N LEU A 267 55.100 28.976 38.381 1.00153.60 N ANISOU 1911 N LEU A 267 12919 10659 34782 -3307 -905 -2108 N ATOM 1912 CA LEU A 267 54.224 27.866 38.734 1.00168.33 C ANISOU 1912 CA LEU A 267 14382 12379 37196 -3464 -1094 -2795 C ATOM 1913 C LEU A 267 52.997 28.344 39.505 1.00175.34 C ANISOU 1913 C LEU A 267 15341 12819 38461 -3669 -807 -2969 C ATOM 1914 O LEU A 267 51.883 27.884 39.255 1.00172.15 O ANISOU 1914 O LEU A 267 14512 12537 38363 -3382 -971 -3551 O ATOM 1915 CB LEU A 267 54.986 26.809 39.535 1.00170.85 C ANISOU 1915 CB LEU A 267 14770 12370 37775 -4148 -1174 -2863 C ATOM 1916 CG LEU A 267 56.100 26.089 38.774 1.00176.81 C ANISOU 1916 CG LEU A 267 15360 13578 38242 -3948 -1519 -2826 C ATOM 1917 CD1 LEU A 267 56.784 25.059 39.662 1.00180.23 C ANISOU 1917 CD1 LEU A 267 15878 13631 38970 -4659 -1581 -2904 C ATOM 1918 CD2 LEU A 267 55.551 25.433 37.515 1.00173.48 C ANISOU 1918 CD2 LEU A 267 14323 13808 37784 -3186 -1953 -3373 C ATOM 1919 N TRP A 268 53.203 29.273 40.433 1.00124.91 N ANISOU 1919 N TRP A 268 19644 14931 12886 -2247 1555 -4948 N ATOM 1920 CA TRP A 268 52.108 29.792 41.247 1.00130.90 C ANISOU 1920 CA TRP A 268 20423 15727 13585 -2196 1530 -5006 C ATOM 1921 C TRP A 268 51.063 30.499 40.389 1.00126.94 C ANISOU 1921 C TRP A 268 19975 15175 13084 -2159 1560 -4975 C ATOM 1922 O TRP A 268 49.863 30.328 40.595 1.00127.84 O ANISOU 1922 O TRP A 268 20084 15331 13157 -2116 1546 -4960 O ATOM 1923 CB TRP A 268 52.636 30.743 42.324 1.00140.38 C ANISOU 1923 CB TRP A 268 21636 16944 14757 -2188 1504 -5150 C ATOM 1924 CG TRP A 268 53.145 32.042 41.782 1.00149.63 C ANISOU 1924 CG TRP A 268 22869 18031 15954 -2202 1539 -5212 C ATOM 1925 CD1 TRP A 268 54.418 32.321 41.380 1.00153.63 C ANISOU 1925 CD1 TRP A 268 23377 18493 16505 -2262 1567 -5241 C ATOM 1926 CD2 TRP A 268 52.388 33.242 41.580 1.00152.18 C ANISOU 1926 CD2 TRP A 268 23270 18301 16252 -2157 1549 -5259 C ATOM 1927 NE1 TRP A 268 54.502 33.621 40.941 1.00155.90 N ANISOU 1927 NE1 TRP A 268 23746 18697 16793 -2269 1601 -5300 N ATOM 1928 CE2 TRP A 268 53.269 34.208 41.053 1.00155.19 C ANISOU 1928 CE2 TRP A 268 23711 18594 16659 -2200 1587 -5309 C ATOM 1929 CE3 TRP A 268 51.051 33.593 41.792 1.00150.19 C ANISOU 1929 CE3 TRP A 268 23045 18069 15951 -2083 1528 -5270 C ATOM 1930 CZ2 TRP A 268 52.856 35.501 40.737 1.00154.51 C ANISOU 1930 CZ2 TRP A 268 23730 18427 16550 -2168 1602 -5363 C ATOM 1931 CZ3 TRP A 268 50.644 34.876 41.478 1.00150.56 C ANISOU 1931 CZ3 TRP A 268 23185 18043 15977 -2040 1537 -5328 C ATOM 1932 CH2 TRP A 268 51.543 35.815 40.957 1.00152.01 C ANISOU 1932 CH2 TRP A 268 23446 18127 16186 -2081 1573 -5371 C ATOM 1933 N LEU A 269 51.525 31.297 39.431 1.00124.00 N ANISOU 1933 N LEU A 269 19653 14713 12750 -2176 1602 -4973 N ATOM 1934 CA LEU A 269 50.624 32.000 38.526 1.00120.09 C ANISOU 1934 CA LEU A 269 19221 14155 12251 -2134 1628 -4943 C ATOM 1935 C LEU A 269 49.953 31.011 37.584 1.00117.46 C ANISOU 1935 C LEU A 269 18858 13829 11944 -2134 1647 -4809 C ATOM 1936 O LEU A 269 48.774 31.150 37.257 1.00122.81 O ANISOU 1936 O LEU A 269 19553 14511 12597 -2081 1646 -4785 O ATOM 1937 CB LEU A 269 51.380 33.057 37.722 1.00120.33 C ANISOU 1937 CB LEU A 269 19329 14080 12310 -2164 1672 -4971 C ATOM 1938 CG LEU A 269 50.551 33.846 36.708 1.00119.20 C ANISOU 1938 CG LEU A 269 19275 13856 12160 -2118 1698 -4941 C ATOM 1939 CD1 LEU A 269 49.448 34.623 37.409 1.00116.92 C ANISOU 1939 CD1 LEU A 269 19031 13587 11806 -2028 1656 -5023 C ATOM 1940 CD2 LEU A 269 51.435 34.780 35.897 1.00124.78 C ANISOU 1940 CD2 LEU A 269 20069 14452 12890 -2166 1747 -4964 C ATOM 1941 N MET A 270 50.716 30.014 37.146 1.00110.09 N ANISOU 1941 N MET A 270 17876 12899 11054 -2188 1662 -4730 N ATOM 1942 CA MET A 270 50.181 28.970 36.283 1.00108.76 C ANISOU 1942 CA MET A 270 17677 12736 10910 -2193 1678 -4603 C ATOM 1943 C MET A 270 49.031 28.253 36.986 1.00116.00 C ANISOU 1943 C MET A 270 18562 13737 11778 -2164 1646 -4589 C ATOM 1944 O MET A 270 47.994 27.981 36.381 1.00110.10 O ANISOU 1944 O MET A 270 17812 12994 11026 -2141 1660 -4527 O ATOM 1945 CB MET A 270 51.275 27.971 35.908 1.00103.67 C ANISOU 1945 CB MET A 270 16987 12092 10312 -2249 1686 -4538 C ATOM 1946 CG MET A 270 50.823 26.909 34.924 1.00105.54 C ANISOU 1946 CG MET A 270 17200 12325 10577 -2257 1704 -4405 C ATOM 1947 SD MET A 270 50.421 27.593 33.304 1.00147.99 S ANISOU 1947 SD MET A 270 22622 17614 15995 -2247 1761 -4340 S ATOM 1948 CE MET A 270 52.043 28.123 32.755 1.00145.68 C ANISOU 1948 CE MET A 270 22339 17261 15751 -2303 1794 -4373 C ATOM 1949 N TYR A 271 49.225 27.951 38.267 1.00126.95 N ANISOU 1949 N TYR A 271 19921 15190 13123 -2168 1606 -4653 N ATOM 1950 CA TYR A 271 48.181 27.346 39.087 1.00133.42 C ANISOU 1950 CA TYR A 271 20715 16095 13883 -2151 1578 -4660 C ATOM 1951 C TYR A 271 46.888 28.137 38.987 1.00121.98 C ANISOU 1951 C TYR A 271 19285 14661 12399 -2092 1581 -4700 C ATOM 1952 O TYR A 271 45.855 27.604 38.596 1.00122.94 O ANISOU 1952 O TYR A 271 19388 14816 12508 -2083 1591 -4645 O ATOM 1953 CB TYR A 271 48.617 27.277 40.550 1.00154.41 C ANISOU 1953 CB TYR A 271 23357 18817 16494 -2156 1534 -4751 C ATOM 1954 CG TYR A 271 49.292 25.983 40.943 1.00173.13 C ANISOU 1954 CG TYR A 271 25704 21217 18862 -2200 1513 -4701 C ATOM 1955 CD1 TYR A 271 48.546 24.912 41.421 1.00183.73 C ANISOU 1955 CD1 TYR A 271 27036 22621 20153 -2215 1498 -4658 C ATOM 1956 CD2 TYR A 271 50.671 25.833 40.851 1.00180.12 C ANISOU 1956 CD2 TYR A 271 26582 22068 19788 -2225 1506 -4704 C ATOM 1957 CE1 TYR A 271 49.147 23.724 41.792 1.00190.01 C ANISOU 1957 CE1 TYR A 271 27832 23431 20934 -2249 1473 -4613 C ATOM 1958 CE2 TYR A 271 51.283 24.648 41.217 1.00185.69 C ANISOU 1958 CE2 TYR A 271 27273 22797 20482 -2250 1476 -4665 C ATOM 1959 CZ TYR A 271 50.516 23.598 41.687 1.00191.32 C ANISOU 1959 CZ TYR A 271 27994 23560 21141 -2259 1457 -4616 C ATOM 1960 OH TYR A 271 51.125 22.419 42.051 1.00195.75 O ANISOU 1960 OH TYR A 271 28563 24132 21681 -2277 1422 -4577 O ATOM 1961 N LEU A 272 46.956 29.415 39.345 1.00110.04 N ANISOU 1961 N LEU A 272 17812 13127 10871 -2048 1569 -4804 N ATOM 1962 CA LEU A 272 45.790 30.289 39.326 1.00101.12 C ANISOU 1962 CA LEU A 272 16709 12011 9700 -1973 1559 -4864 C ATOM 1963 C LEU A 272 45.057 30.209 37.993 1.00101.18 C ANISOU 1963 C LEU A 272 16732 11978 9736 -1951 1591 -4777 C ATOM 1964 O LEU A 272 43.844 30.001 37.955 1.00104.58 O ANISOU 1964 O LEU A 272 17136 12469 10131 -1912 1583 -4776 O ATOM 1965 CB LEU A 272 46.204 31.731 39.630 1.00104.48 C ANISOU 1965 CB LEU A 272 17202 12382 10113 -1931 1546 -4975 C ATOM 1966 CG LEU A 272 45.103 32.775 39.837 1.00114.43 C ANISOU 1966 CG LEU A 272 18504 13658 11317 -1833 1519 -5065 C ATOM 1967 CD1 LEU A 272 45.612 33.927 40.693 1.00114.59 C ANISOU 1967 CD1 LEU A 272 18577 13656 11306 -1804 1490 -5196 C ATOM 1968 CD2 LEU A 272 44.556 33.288 38.510 1.00118.50 C ANISOU 1968 CD2 LEU A 272 19079 14093 11850 -1787 1544 -5016 C ATOM 1969 N ALA A 273 45.799 30.366 36.901 1.00104.62 N ANISOU 1969 N ALA A 273 17204 12316 10231 -1979 1628 -4710 N ATOM 1970 CA ALA A 273 45.218 30.282 35.566 1.00107.87 C ANISOU 1970 CA ALA A 273 17632 12681 10673 -1961 1659 -4622 C ATOM 1971 C ALA A 273 44.581 28.917 35.334 1.00108.39 C ANISOU 1971 C ALA A 273 17627 12812 10744 -1992 1667 -4529 C ATOM 1972 O ALA A 273 43.475 28.816 34.801 1.00109.62 O ANISOU 1972 O ALA A 273 17771 12992 10887 -1954 1672 -4503 O ATOM 1973 CB ALA A 273 46.273 30.562 34.511 1.00111.21 C ANISOU 1973 CB ALA A 273 18101 12998 11157 -2001 1700 -4566 C ATOM 1974 N ILE A 274 45.295 27.871 35.735 1.00109.17 N ANISOU 1974 N ILE A 274 17683 12937 10857 -2060 1666 -4483 N ATOM 1975 CA ILE A 274 44.793 26.509 35.630 1.00109.61 C ANISOU 1975 CA ILE A 274 17690 13047 10910 -2099 1672 -4398 C ATOM 1976 C ILE A 274 43.508 26.345 36.437 1.00105.12 C ANISOU 1976 C ILE A 274 17090 12580 10271 -2075 1650 -4456 C ATOM 1977 O ILE A 274 42.521 25.791 35.948 1.00105.95 O ANISOU 1977 O ILE A 274 17168 12722 10367 -2077 1666 -4409 O ATOM 1978 CB ILE A 274 45.842 25.489 36.120 1.00112.52 C ANISOU 1978 CB ILE A 274 18039 13424 11290 -2164 1661 -4360 C ATOM 1979 CG1 ILE A 274 47.043 25.463 35.171 1.00116.90 C ANISOU 1979 CG1 ILE A 274 18606 13895 11915 -2191 1685 -4297 C ATOM 1980 CG2 ILE A 274 45.226 24.102 36.241 1.00101.80 C ANISOU 1980 CG2 ILE A 274 16651 12121 9905 -2205 1660 -4288 C ATOM 1981 CD1 ILE A 274 48.159 24.548 35.627 1.00117.79 C ANISOU 1981 CD1 ILE A 274 18700 14017 12037 -2237 1665 -4275 C ATOM 1982 N VAL A 275 43.528 26.837 37.672 1.00103.38 N ANISOU 1982 N VAL A 275 16869 12411 9997 -2055 1616 -4564 N ATOM 1983 CA VAL A 275 42.378 26.747 38.565 1.00104.09 C ANISOU 1983 CA VAL A 275 16924 12613 10011 -2034 1594 -4638 C ATOM 1984 C VAL A 275 41.161 27.476 37.999 1.00111.02 C ANISOU 1984 C VAL A 275 17800 13513 10871 -1958 1597 -4677 C ATOM 1985 O VAL A 275 40.040 26.969 38.062 1.00115.88 O ANISOU 1985 O VAL A 275 18368 14216 11444 -1959 1600 -4682 O ATOM 1986 CB VAL A 275 42.706 27.318 39.959 1.00 99.39 C ANISOU 1986 CB VAL A 275 16332 12066 9365 -2016 1554 -4757 C ATOM 1987 CG1 VAL A 275 41.468 27.315 40.844 1.00 88.85 C ANISOU 1987 CG1 VAL A 275 14956 10857 7945 -1989 1533 -4844 C ATOM 1988 CG2 VAL A 275 43.828 26.525 40.605 1.00105.55 C ANISOU 1988 CG2 VAL A 275 17111 12839 10153 -2083 1544 -4729 C ATOM 1989 N LEU A 276 41.386 28.665 37.448 1.00113.28 N ANISOU 1989 N LEU A 276 18140 13719 11181 -1892 1594 -4709 N ATOM 1990 CA LEU A 276 40.303 29.469 36.890 1.00116.71 C ANISOU 1990 CA LEU A 276 18590 14162 11593 -1799 1586 -4754 C ATOM 1991 C LEU A 276 39.495 28.685 35.861 1.00125.98 C ANISOU 1991 C LEU A 276 19725 15354 12787 -1813 1616 -4664 C ATOM 1992 O LEU A 276 38.274 28.820 35.780 1.00130.28 O ANISOU 1992 O LEU A 276 20237 15976 13288 -1756 1605 -4713 O ATOM 1993 CB LEU A 276 40.853 30.751 36.261 1.00112.28 C ANISOU 1993 CB LEU A 276 18123 13481 11059 -1740 1585 -4778 C ATOM 1994 CG LEU A 276 39.802 31.731 35.738 1.00109.35 C ANISOU 1994 CG LEU A 276 17792 13103 10651 -1623 1565 -4838 C ATOM 1995 CD1 LEU A 276 38.861 32.138 36.857 1.00109.93 C ANISOU 1995 CD1 LEU A 276 17832 13297 10640 -1550 1517 -4972 C ATOM 1996 CD2 LEU A 276 40.453 32.956 35.112 1.00110.72 C ANISOU 1996 CD2 LEU A 276 18085 13139 10843 -1577 1568 -4853 C ATOM 1997 N ALA A 277 40.183 27.859 35.080 1.00128.40 N ANISOU 1997 N ALA A 277 20031 15596 13158 -1886 1652 -4540 N ATOM 1998 CA ALA A 277 39.529 27.047 34.062 1.00129.57 C ANISOU 1998 CA ALA A 277 20145 15754 13333 -1908 1682 -4447 C ATOM 1999 C ALA A 277 38.584 26.030 34.691 1.00129.01 C ANISOU 1999 C ALA A 277 20002 15809 13209 -1954 1682 -4459 C ATOM 2000 O ALA A 277 37.485 25.796 34.186 1.00127.87 O ANISOU 2000 O ALA A 277 19817 15721 13047 -1935 1693 -4458 O ATOM 2001 CB ALA A 277 40.564 26.346 33.195 1.00132.37 C ANISOU 2001 CB ALA A 277 20514 16018 13762 -1977 1716 -4318 C ATOM 2002 N HIS A 278 39.020 25.426 35.792 1.00131.51 N ANISOU 2002 N HIS A 278 20305 16169 13493 -2018 1672 -4476 N ATOM 2003 CA HIS A 278 38.200 24.457 36.506 1.00132.50 C ANISOU 2003 CA HIS A 278 20378 16412 13554 -2077 1675 -4494 C ATOM 2004 C HIS A 278 36.980 25.134 37.119 1.00125.40 C ANISOU 2004 C HIS A 278 19437 15633 12578 -2011 1652 -4627 C ATOM 2005 O HIS A 278 35.953 24.496 37.346 1.00126.19 O ANISOU 2005 O HIS A 278 19480 15844 12622 -2048 1664 -4651 O ATOM 2006 CB HIS A 278 39.010 23.769 37.606 1.00137.73 C ANISOU 2006 CB HIS A 278 21055 17087 14189 -2150 1663 -4491 C ATOM 2007 CG HIS A 278 40.284 23.148 37.125 1.00139.41 C ANISOU 2007 CG HIS A 278 21307 17195 14467 -2199 1674 -4380 C ATOM 2008 ND1 HIS A 278 40.312 21.996 36.368 1.00137.71 N ANISOU 2008 ND1 HIS A 278 21093 16950 14281 -2262 1703 -4263 N ATOM 2009 CD2 HIS A 278 41.576 23.507 37.311 1.00143.83 C ANISOU 2009 CD2 HIS A 278 21903 17682 15065 -2193 1658 -4378 C ATOM 2010 CE1 HIS A 278 41.566 21.680 36.098 1.00139.50 C ANISOU 2010 CE1 HIS A 278 21354 17092 14559 -2283 1700 -4194 C ATOM 2011 NE2 HIS A 278 42.353 22.580 36.659 1.00144.48 N ANISOU 2011 NE2 HIS A 278 22001 17699 15195 -2245 1674 -4264 N ATOM 2012 N THR A 279 37.102 26.430 37.386 1.00120.24 N ANISOU 2012 N THR A 279 18812 14960 11915 -1916 1619 -4719 N ATOM 2013 CA THR A 279 36.037 27.193 38.029 1.00125.68 C ANISOU 2013 CA THR A 279 19465 15763 12525 -1832 1585 -4859 C ATOM 2014 C THR A 279 34.810 27.357 37.132 1.00128.78 C ANISOU 2014 C THR A 279 19819 16206 12905 -1769 1592 -4876 C ATOM 2015 O THR A 279 33.677 27.378 37.614 1.00129.53 O ANISOU 2015 O THR A 279 19847 16444 12923 -1739 1578 -4974 O ATOM 2016 CB THR A 279 36.536 28.588 38.462 1.00130.07 C ANISOU 2016 CB THR A 279 20080 16267 13075 -1736 1544 -4952 C ATOM 2017 OG1 THR A 279 37.661 28.444 39.338 1.00135.38 O ANISOU 2017 OG1 THR A 279 20778 16906 13756 -1794 1536 -4950 O ATOM 2018 CG2 THR A 279 35.437 29.358 39.178 1.00131.38 C ANISOU 2018 CG2 THR A 279 20209 16559 13151 -1638 1502 -5105 C ATOM 2019 N ASN A 280 35.044 27.471 35.829 1.00128.65 N ANISOU 2019 N ASN A 280 19841 16081 12961 -1747 1612 -4784 N ATOM 2020 CA ASN A 280 33.971 27.704 34.866 1.00126.52 C ANISOU 2020 CA ASN A 280 19544 15843 12684 -1674 1614 -4797 C ATOM 2021 C ASN A 280 32.834 26.693 34.978 1.00131.99 C ANISOU 2021 C ASN A 280 20138 16685 13329 -1733 1635 -4811 C ATOM 2022 O ASN A 280 31.659 27.048 34.858 1.00143.17 O ANISOU 2022 O ASN A 280 21499 18209 14690 -1656 1618 -4903 O ATOM 2023 CB ASN A 280 34.532 27.709 33.443 1.00122.84 C ANISOU 2023 CB ASN A 280 19133 15234 12307 -1672 1641 -4672 C ATOM 2024 CG ASN A 280 33.523 28.190 32.417 1.00120.42 C ANISOU 2024 CG ASN A 280 18818 14942 11993 -1571 1633 -4694 C ATOM 2025 OD1 ASN A 280 32.388 28.520 32.752 1.00130.46 O ANISOU 2025 OD1 ASN A 280 20038 16337 13192 -1496 1605 -4807 O ATOM 2026 ND2 ASN A 280 33.937 28.232 31.159 1.00111.71 N ANISOU 2026 ND2 ASN A 280 17765 13721 10960 -1565 1656 -4590 N ATOM 2027 N SER A 281 33.188 25.435 35.212 1.00126.39 N ANISOU 2027 N SER A 281 19407 15981 12632 -1869 1672 -4727 N ATOM 2028 CA SER A 281 32.197 24.373 35.347 1.00120.89 C ANISOU 2028 CA SER A 281 18631 15417 11885 -1953 1701 -4735 C ATOM 2029 C SER A 281 31.154 24.683 36.418 1.00120.45 C ANISOU 2029 C SER A 281 18504 15543 11718 -1923 1677 -4894 C ATOM 2030 O SER A 281 30.027 24.197 36.355 1.00126.41 O ANISOU 2030 O SER A 281 19178 16436 12417 -1952 1695 -4942 O ATOM 2031 CB SER A 281 32.883 23.042 35.662 1.00116.05 C ANISOU 2031 CB SER A 281 18039 14770 11286 -2102 1736 -4630 C ATOM 2032 OG SER A 281 33.876 22.733 34.696 1.00111.07 O ANISOU 2032 OG SER A 281 17465 13984 10750 -2124 1755 -4491 O ATOM 2033 N VAL A 282 31.535 25.502 37.393 1.00117.87 N ANISOU 2033 N VAL A 282 18203 15226 11358 -1866 1636 -4981 N ATOM 2034 CA VAL A 282 30.680 25.785 38.546 1.00126.72 C ANISOU 2034 CA VAL A 282 19256 16523 12368 -1841 1610 -5134 C ATOM 2035 C VAL A 282 29.741 26.979 38.353 1.00134.96 C ANISOU 2035 C VAL A 282 20265 17648 13366 -1676 1565 -5268 C ATOM 2036 O VAL A 282 28.638 26.999 38.901 1.00136.32 O ANISOU 2036 O VAL A 282 20346 18006 13441 -1654 1554 -5392 O ATOM 2037 CB VAL A 282 31.525 26.023 39.817 1.00122.33 C ANISOU 2037 CB VAL A 282 18739 15953 11787 -1861 1585 -5173 C ATOM 2038 CG1 VAL A 282 30.670 26.590 40.940 1.00127.07 C ANISOU 2038 CG1 VAL A 282 19274 16732 12276 -1802 1549 -5345 C ATOM 2039 CG2 VAL A 282 32.200 24.730 40.251 1.00117.14 C ANISOU 2039 CG2 VAL A 282 18104 15266 11138 -2019 1622 -5073 C ATOM 2040 N VAL A 283 30.178 27.975 37.588 1.00138.98 N ANISOU 2040 N VAL A 283 20850 18021 13933 -1559 1538 -5247 N ATOM 2041 CA VAL A 283 29.416 29.215 37.449 1.00139.72 C ANISOU 2041 CA VAL A 283 20943 18167 13976 -1384 1484 -5375 C ATOM 2042 C VAL A 283 28.063 28.995 36.781 1.00140.98 C ANISOU 2042 C VAL A 283 21012 18463 14092 -1337 1489 -5425 C ATOM 2043 O VAL A 283 27.133 29.778 36.973 1.00145.43 O ANISOU 2043 O VAL A 283 21534 19147 14575 -1202 1442 -5568 O ATOM 2044 CB VAL A 283 30.198 30.274 36.648 1.00140.87 C ANISOU 2044 CB VAL A 283 21215 18119 14190 -1281 1460 -5329 C ATOM 2045 CG1 VAL A 283 31.538 30.557 37.304 1.00140.14 C ANISOU 2045 CG1 VAL A 283 21205 17905 14136 -1326 1456 -5295 C ATOM 2046 CG2 VAL A 283 30.380 29.822 35.207 1.00138.28 C ANISOU 2046 CG2 VAL A 283 20914 17677 13947 -1312 1500 -5189 C ATOM 2047 N ASN A 284 27.957 27.928 35.998 1.00135.10 N ANISOU 2047 N ASN A 284 20234 17703 13395 -1446 1543 -5315 N ATOM 2048 CA ASN A 284 26.722 27.647 35.276 1.00132.44 C ANISOU 2048 CA ASN A 284 19807 17491 13023 -1414 1553 -5356 C ATOM 2049 C ASN A 284 25.514 27.410 36.193 1.00127.41 C ANISOU 2049 C ASN A 284 19039 17111 12260 -1425 1547 -5511 C ATOM 2050 O ASN A 284 24.553 28.178 36.146 1.00127.18 O ANISOU 2050 O ASN A 284 18957 17209 12158 -1280 1503 -5648 O ATOM 2051 CB ASN A 284 26.916 26.498 34.279 1.00131.10 C ANISOU 2051 CB ASN A 284 19631 17247 12932 -1540 1614 -5203 C ATOM 2052 CG ASN A 284 28.028 26.773 33.282 1.00134.98 C ANISOU 2052 CG ASN A 284 20238 17509 13539 -1519 1620 -5060 C ATOM 2053 OD1 ASN A 284 28.429 27.918 33.083 1.00133.34 O ANISOU 2053 OD1 ASN A 284 20113 17203 13347 -1394 1579 -5083 O ATOM 2054 ND2 ASN A 284 28.532 25.718 32.651 1.00138.64 N ANISOU 2054 ND2 ASN A 284 20712 17890 14075 -1645 1672 -4914 N ATOM 2055 N PRO A 285 25.563 26.366 37.042 1.00127.91 N ANISOU 2055 N PRO A 285 19056 17257 12288 -1594 1590 -5497 N ATOM 2056 CA PRO A 285 24.424 26.118 37.929 1.00124.86 C ANISOU 2056 CA PRO A 285 18544 17127 11770 -1622 1591 -5648 C ATOM 2057 C PRO A 285 23.904 27.377 38.607 1.00120.61 C ANISOU 2057 C PRO A 285 17975 16706 11145 -1447 1521 -5824 C ATOM 2058 O PRO A 285 22.693 27.529 38.753 1.00132.19 O ANISOU 2058 O PRO A 285 19325 18391 12509 -1388 1506 -5966 O ATOM 2059 CB PRO A 285 25.013 25.192 38.984 1.00129.49 C ANISOU 2059 CB PRO A 285 19147 17719 12335 -1801 1629 -5601 C ATOM 2060 CG PRO A 285 26.121 24.489 38.302 1.00133.02 C ANISOU 2060 CG PRO A 285 19693 17947 12901 -1898 1667 -5410 C ATOM 2061 CD PRO A 285 26.675 25.430 37.303 1.00132.05 C ANISOU 2061 CD PRO A 285 19647 17651 12874 -1756 1634 -5354 C ATOM 2062 N PHE A 286 24.805 28.262 39.020 1.00105.18 N ANISOU 2062 N PHE A 286 16121 14617 9225 -1364 1477 -5821 N ATOM 2063 CA PHE A 286 24.394 29.475 39.717 1.00107.72 C ANISOU 2063 CA PHE A 286 16431 15035 9463 -1194 1406 -5987 C ATOM 2064 C PHE A 286 23.844 30.527 38.756 1.00107.68 C ANISOU 2064 C PHE A 286 16451 15006 9456 -988 1353 -6045 C ATOM 2065 O PHE A 286 22.978 31.318 39.127 1.00106.81 O ANISOU 2065 O PHE A 286 16286 15053 9245 -836 1296 -6211 O ATOM 2066 CB PHE A 286 25.542 30.064 40.546 1.00113.11 C ANISOU 2066 CB PHE A 286 17216 15585 10176 -1182 1377 -5974 C ATOM 2067 CG PHE A 286 26.050 29.151 41.631 1.00121.66 C ANISOU 2067 CG PHE A 286 18278 16706 11241 -1358 1415 -5940 C ATOM 2068 CD1 PHE A 286 27.065 28.246 41.368 1.00126.90 C ANISOU 2068 CD1 PHE A 286 19008 17211 11997 -1509 1466 -5771 C ATOM 2069 CD2 PHE A 286 25.528 29.209 42.915 1.00123.02 C ANISOU 2069 CD2 PHE A 286 18370 17073 11298 -1365 1397 -6080 C ATOM 2070 CE1 PHE A 286 27.542 27.408 42.358 1.00129.71 C ANISOU 2070 CE1 PHE A 286 19360 17594 12328 -1658 1495 -5741 C ATOM 2071 CE2 PHE A 286 26.004 28.372 43.912 1.00125.18 C ANISOU 2071 CE2 PHE A 286 18639 17376 11548 -1525 1430 -6048 C ATOM 2072 CZ PHE A 286 27.012 27.471 43.630 1.00128.93 C ANISOU 2072 CZ PHE A 286 19191 17683 12114 -1669 1478 -5877 C ATOM 2073 N ILE A 287 24.350 30.539 37.526 1.00111.32 N ANISOU 2073 N ILE A 287 16999 15276 10021 -976 1368 -5912 N ATOM 2074 CA ILE A 287 23.864 31.476 36.518 1.00117.39 C ANISOU 2074 CA ILE A 287 17810 16005 10787 -786 1320 -5951 C ATOM 2075 C ILE A 287 22.447 31.111 36.072 1.00121.24 C ANISOU 2075 C ILE A 287 18158 16709 11200 -745 1323 -6042 C ATOM 2076 O ILE A 287 21.673 31.978 35.675 1.00127.96 O ANISOU 2076 O ILE A 287 19001 17628 11988 -553 1265 -6153 O ATOM 2077 CB ILE A 287 24.808 31.558 35.291 1.00107.21 C ANISOU 2077 CB ILE A 287 16654 14456 9625 -796 1341 -5780 C ATOM 2078 CG1 ILE A 287 24.566 32.847 34.503 1.00109.40 C ANISOU 2078 CG1 ILE A 287 17029 14651 9886 -579 1277 -5831 C ATOM 2079 CG2 ILE A 287 24.640 30.351 34.388 1.00106.10 C ANISOU 2079 CG2 ILE A 287 16454 14313 9546 -929 1408 -5658 C ATOM 2080 CD1 ILE A 287 25.355 32.916 33.207 1.00110.53 C ANISOU 2080 CD1 ILE A 287 17294 14562 10139 -590 1301 -5671 C ATOM 2081 N TYR A 288 22.106 29.829 36.145 1.00111.49 N ANISOU 2081 N TYR A 288 16814 15584 9961 -925 1391 -6001 N ATOM 2082 CA TYR A 288 20.754 29.399 35.813 1.00 98.56 C ANISOU 2082 CA TYR A 288 15028 14177 8243 -913 1402 -6098 C ATOM 2083 C TYR A 288 19.767 29.795 36.907 1.00100.02 C ANISOU 2083 C TYR A 288 15091 14636 8274 -838 1363 -6308 C ATOM 2084 O TYR A 288 18.688 30.313 36.623 1.00 95.39 O ANISOU 2084 O TYR A 288 14422 14221 7600 -684 1320 -6448 O ATOM 2085 CB TYR A 288 20.709 27.891 35.582 1.00 95.00 C ANISOU 2085 CB TYR A 288 14511 13758 7827 -1143 1490 -5992 C ATOM 2086 CG TYR A 288 21.622 27.410 34.479 1.00101.19 C ANISOU 2086 CG TYR A 288 15398 14294 8754 -1217 1529 -5790 C ATOM 2087 CD1 TYR A 288 21.459 27.858 33.174 1.00106.82 C ANISOU 2087 CD1 TYR A 288 16149 14916 9521 -1094 1508 -5749 C ATOM 2088 CD2 TYR A 288 22.632 26.495 34.740 1.00107.06 C ANISOU 2088 CD2 TYR A 288 16201 14906 9572 -1403 1584 -5643 C ATOM 2089 CE1 TYR A 288 22.282 27.419 32.159 1.00109.58 C ANISOU 2089 CE1 TYR A 288 16586 15054 9995 -1162 1545 -5568 C ATOM 2090 CE2 TYR A 288 23.465 26.046 33.730 1.00112.72 C ANISOU 2090 CE2 TYR A 288 17004 15413 10412 -1463 1618 -5465 C ATOM 2091 CZ TYR A 288 23.282 26.513 32.441 1.00114.37 C ANISOU 2091 CZ TYR A 288 17241 15540 10673 -1346 1600 -5429 C ATOM 2092 OH TYR A 288 24.098 26.076 31.425 1.00118.71 O ANISOU 2092 OH TYR A 288 17869 15894 11340 -1405 1634 -5256 O ATOM 2093 N ALA A 289 20.144 29.548 38.158 1.00106.35 N ANISOU 2093 N ALA A 289 15881 15487 9039 -943 1376 -6334 N ATOM 2094 CA ALA A 289 19.309 29.919 39.294 1.00117.41 C ANISOU 2094 CA ALA A 289 17170 17149 10293 -883 1341 -6531 C ATOM 2095 C ALA A 289 19.071 31.426 39.328 1.00126.10 C ANISOU 2095 C ALA A 289 18316 18253 11343 -614 1243 -6661 C ATOM 2096 O ALA A 289 17.993 31.884 39.698 1.00134.15 O ANISOU 2096 O ALA A 289 19221 19517 12231 -488 1198 -6846 O ATOM 2097 CB ALA A 289 19.943 29.451 40.599 1.00 67.59 C ANISOU 2097 CB ALA A 289 10869 10850 3965 -1039 1369 -6516 C ATOM 2098 N TYR A 290 20.081 32.195 38.937 1.00127.77 N ANISOU 2098 N TYR A 290 18699 18197 11651 -528 1208 -6570 N ATOM 2099 CA TYR A 290 19.968 33.649 38.948 1.00128.66 C ANISOU 2099 CA TYR A 290 18893 18275 11717 -279 1115 -6681 C ATOM 2100 C TYR A 290 19.238 34.184 37.716 1.00125.96 C ANISOU 2100 C TYR A 290 18564 17934 11361 -97 1074 -6714 C ATOM 2101 O TYR A 290 18.247 34.903 37.837 1.00121.76 O ANISOU 2101 O TYR A 290 17970 17583 10709 96 1007 -6888 O ATOM 2102 CB TYR A 290 21.349 34.297 39.063 1.00129.69 C ANISOU 2102 CB TYR A 290 19211 18123 11943 -269 1096 -6579 C ATOM 2103 CG TYR A 290 21.326 35.802 38.909 1.00134.14 C ANISOU 2103 CG TYR A 290 19898 18605 12466 -21 1003 -6674 C ATOM 2104 CD1 TYR A 290 21.079 36.630 39.999 1.00137.70 C ANISOU 2104 CD1 TYR A 290 20339 19167 12814 102 937 -6837 C ATOM 2105 CD2 TYR A 290 21.551 36.397 37.673 1.00133.99 C ANISOU 2105 CD2 TYR A 290 20013 18393 12504 92 981 -6600 C ATOM 2106 CE1 TYR A 290 21.057 38.008 39.860 1.00139.71 C ANISOU 2106 CE1 TYR A 290 20722 19336 13023 333 848 -6926 C ATOM 2107 CE2 TYR A 290 21.531 37.771 37.527 1.00137.11 C ANISOU 2107 CE2 TYR A 290 20543 18701 12850 317 896 -6686 C ATOM 2108 CZ TYR A 290 21.283 38.571 38.622 1.00140.46 C ANISOU 2108 CZ TYR A 290 20964 19232 13172 438 829 -6849 C ATOM 2109 OH TYR A 290 21.262 39.940 38.477 1.00142.21 O ANISOU 2109 OH TYR A 290 21338 19358 13340 666 740 -6936 O ATOM 2110 N ARG A 291 19.735 33.832 36.535 1.00123.45 N ANISOU 2110 N ARG A 291 18326 17421 11159 -152 1113 -6550 N ATOM 2111 CA ARG A 291 19.179 34.339 35.286 1.00120.88 C ANISOU 2111 CA ARG A 291 18036 17062 10830 16 1076 -6559 C ATOM 2112 C ARG A 291 17.768 33.834 34.997 1.00118.47 C ANISOU 2112 C ARG A 291 17543 17038 10431 46 1082 -6674 C ATOM 2113 O ARG A 291 16.895 34.610 34.610 1.00122.27 O ANISOU 2113 O ARG A 291 18006 17628 10823 266 1013 -6805 O ATOM 2114 CB ARG A 291 20.107 34.001 34.120 1.00118.21 C ANISOU 2114 CB ARG A 291 17823 16453 10640 -72 1124 -6348 C ATOM 2115 CG ARG A 291 21.382 34.819 34.104 1.00118.48 C ANISOU 2115 CG ARG A 291 18059 16209 10748 -40 1102 -6258 C ATOM 2116 CD ARG A 291 21.071 36.276 33.808 1.00119.34 C ANISOU 2116 CD ARG A 291 18289 16269 10786 225 1008 -6366 C ATOM 2117 NE ARG A 291 20.337 36.423 32.554 1.00118.48 N ANISOU 2117 NE ARG A 291 18182 16171 10663 352 989 -6367 N ATOM 2118 CZ ARG A 291 19.992 37.586 32.013 1.00117.59 C ANISOU 2118 CZ ARG A 291 18187 16002 10488 590 910 -6443 C ATOM 2119 NH1 ARG A 291 20.311 38.722 32.615 1.00117.33 N ANISOU 2119 NH1 ARG A 291 18287 15894 10402 725 843 -6525 N ATOM 2120 NH2 ARG A 291 19.327 37.611 30.868 1.00115.70 N ANISOU 2120 NH2 ARG A 291 17943 15780 10236 696 896 -6439 N ATOM 2121 N ILE A 292 17.551 32.535 35.180 1.00112.32 N ANISOU 2121 N ILE A 292 16631 16379 9665 -174 1164 -6629 N ATOM 2122 CA ILE A 292 16.263 31.932 34.859 1.00110.25 C ANISOU 2122 CA ILE A 292 16187 16387 9318 -183 1184 -6728 C ATOM 2123 C ILE A 292 15.376 31.755 36.090 1.00114.01 C ANISOU 2123 C ILE A 292 16490 17187 9643 -209 1181 -6915 C ATOM 2124 O ILE A 292 15.654 30.928 36.958 1.00111.47 O ANISOU 2124 O ILE A 292 16117 16918 9318 -418 1242 -6885 O ATOM 2125 CB ILE A 292 16.436 30.575 34.157 1.00103.88 C ANISOU 2125 CB ILE A 292 15338 15527 8604 -411 1279 -6572 C ATOM 2126 CG1 ILE A 292 17.338 30.728 32.932 1.00101.23 C ANISOU 2126 CG1 ILE A 292 15165 14881 8415 -389 1284 -6387 C ATOM 2127 CG2 ILE A 292 15.083 30.005 33.764 1.00107.28 C ANISOU 2127 CG2 ILE A 292 15581 16238 8942 -418 1299 -6683 C ATOM 2128 CD1 ILE A 292 16.823 31.724 31.915 1.00100.99 C ANISOU 2128 CD1 ILE A 292 15186 14825 8360 -138 1212 -6444 C ATOM 2129 N ARG A 293 14.303 32.536 36.149 1.00178.82 N ANISOU 2129 N ARG A 293 20793 20881 26267 4205 -1987 -2448 N ATOM 2130 CA ARG A 293 13.359 32.468 37.257 1.00178.15 C ANISOU 2130 CA ARG A 293 20023 21521 26144 4370 -1646 -2458 C ATOM 2131 C ARG A 293 12.667 31.108 37.301 1.00175.62 C ANISOU 2131 C ARG A 293 18777 21879 26070 3847 -1783 -2232 C ATOM 2132 O ARG A 293 12.181 30.681 38.348 1.00177.61 O ANISOU 2132 O ARG A 293 18476 22695 26312 3679 -1497 -2197 O ATOM 2133 CB ARG A 293 12.324 33.586 37.140 1.00179.33 C ANISOU 2133 CB ARG A 293 20023 21907 26207 5303 -1566 -2599 C ATOM 2134 CG ARG A 293 12.918 34.986 37.193 1.00176.72 C ANISOU 2134 CG ARG A 293 20566 20958 25621 5870 -1395 -2832 C ATOM 2135 CD ARG A 293 11.865 36.039 36.892 1.00187.11 C ANISOU 2135 CD ARG A 293 21715 22494 26884 6789 -1384 -2955 C ATOM 2136 NE ARG A 293 11.421 35.988 35.501 1.00188.14 N ANISOU 2136 NE ARG A 293 21725 22568 27191 7012 -1842 -2874 N ATOM 2137 CZ ARG A 293 10.415 36.705 35.011 1.00187.23 C ANISOU 2137 CZ ARG A 293 21362 22685 27092 7751 -1933 -2937 C ATOM 2138 NH1 ARG A 293 9.741 37.524 35.802 1.00187.07 N ANISOU 2138 NH1 ARG A 293 21178 22975 26926 8338 -1595 -3084 N ATOM 2139 NH2 ARG A 293 10.080 36.599 33.733 1.00185.54 N ANISOU 2139 NH2 ARG A 293 21059 22395 27042 7899 -2363 -2854 N ATOM 2140 N GLU A 294 12.626 30.434 36.156 1.00170.88 N ANISOU 2140 N GLU A 294 18018 21220 25690 3591 -2222 -2079 N ATOM 2141 CA GLU A 294 12.040 29.102 36.073 1.00169.77 C ANISOU 2141 CA GLU A 294 17037 21670 25797 3062 -2396 -1855 C ATOM 2142 C GLU A 294 12.967 28.065 36.695 1.00161.09 C ANISOU 2142 C GLU A 294 16000 20472 24734 2164 -2310 -1746 C ATOM 2143 O GLU A 294 12.512 27.090 37.292 1.00133.92 O ANISOU 2143 O GLU A 294 11860 17613 21411 1729 -2231 -1607 O ATOM 2144 CB GLU A 294 11.742 28.736 34.617 1.00175.41 C ANISOU 2144 CB GLU A 294 17598 22318 26731 3076 -2902 -1731 C ATOM 2145 CG GLU A 294 11.255 27.306 34.414 1.00182.33 C ANISOU 2145 CG GLU A 294 17666 23733 27877 2473 -3125 -1489 C ATOM 2146 CD GLU A 294 9.874 27.061 35.000 1.00192.72 C ANISOU 2146 CD GLU A 294 18034 25927 29264 2721 -2972 -1438 C ATOM 2147 OE1 GLU A 294 9.457 25.885 35.065 1.00190.56 O ANISOU 2147 OE1 GLU A 294 17061 26153 29189 2211 -3082 -1248 O ATOM 2148 OE2 GLU A 294 9.207 28.042 35.392 1.00200.35 O ANISOU 2148 OE2 GLU A 294 18954 27082 30088 3424 -2742 -1588 O ATOM 2149 N PHE A 295 14.270 28.283 36.552 1.00152.47 N ANISOU 2149 N PHE A 295 15751 18638 23543 1890 -2327 -1810 N ATOM 2150 CA PHE A 295 15.263 27.365 37.099 1.00142.34 C ANISOU 2150 CA PHE A 295 14619 17175 22288 1043 -2255 -1719 C ATOM 2151 C PHE A 295 15.339 27.440 38.622 1.00137.47 C ANISOU 2151 C PHE A 295 13916 16817 21501 931 -1769 -1791 C ATOM 2152 O PHE A 295 15.259 26.419 39.303 1.00132.92 O ANISOU 2152 O PHE A 295 12830 16658 21017 347 -1672 -1657 O ATOM 2153 CB PHE A 295 16.641 27.626 36.487 1.00115.72 C ANISOU 2153 CB PHE A 295 12196 12915 18858 807 -2414 -1777 C ATOM 2154 CG PHE A 295 16.977 26.719 35.334 1.00121.21 C ANISOU 2154 CG PHE A 295 12853 13411 19792 309 -2873 -1607 C ATOM 2155 CD1 PHE A 295 17.397 25.418 35.560 1.00107.59 C ANISOU 2155 CD1 PHE A 295 10835 11818 18227 -540 -2948 -1430 C ATOM 2156 CD2 PHE A 295 16.883 27.168 34.028 1.00123.19 C ANISOU 2156 CD2 PHE A 295 13365 13336 20104 683 -3230 -1624 C ATOM 2157 CE1 PHE A 295 17.711 24.581 34.504 1.00103.85 C ANISOU 2157 CE1 PHE A 295 10325 11159 17973 -1003 -3368 -1276 C ATOM 2158 CE2 PHE A 295 17.195 26.335 32.968 1.00124.76 C ANISOU 2158 CE2 PHE A 295 13533 13351 20521 221 -3650 -1469 C ATOM 2159 CZ PHE A 295 17.610 25.041 33.207 1.00121.89 C ANISOU 2159 CZ PHE A 295 12872 13123 20316 -622 -3717 -1296 C ATOM 2160 N ARG A 296 15.495 28.651 39.151 1.00140.81 N ANISOU 2160 N ARG A 296 14841 16989 21672 1491 -1466 -2003 N ATOM 2161 CA ARG A 296 15.626 28.842 40.593 1.00144.18 C ANISOU 2161 CA ARG A 296 15268 17602 21913 1430 -992 -2091 C ATOM 2162 C ARG A 296 14.489 28.186 41.372 1.00150.26 C ANISOU 2162 C ARG A 296 15059 19264 22768 1357 -820 -1990 C ATOM 2163 O ARG A 296 14.721 27.519 42.380 1.00128.96 O ANISOU 2163 O ARG A 296 12136 16809 20052 835 -580 -1931 O ATOM 2164 CB ARG A 296 15.716 30.332 40.942 1.00128.41 C ANISOU 2164 CB ARG A 296 13861 15286 19645 2176 -713 -2339 C ATOM 2165 CG ARG A 296 14.594 31.181 40.370 1.00164.99 C ANISOU 2165 CG ARG A 296 18238 20174 24275 3030 -797 -2419 C ATOM 2166 CD ARG A 296 14.585 32.574 40.982 1.00168.99 C ANISOU 2166 CD ARG A 296 19212 20488 24508 3732 -447 -2660 C ATOM 2167 NE ARG A 296 15.864 33.257 40.812 1.00163.58 N ANISOU 2167 NE ARG A 296 19538 18958 23657 3721 -425 -2792 N ATOM 2168 CZ ARG A 296 16.128 34.474 41.280 1.00166.40 C ANISOU 2168 CZ ARG A 296 20466 18994 23765 4256 -141 -3007 C ATOM 2169 NH1 ARG A 296 17.321 35.021 41.080 1.00160.07 N ANISOU 2169 NH1 ARG A 296 20576 17417 22827 4200 -143 -3114 N ATOM 2170 NH2 ARG A 296 15.200 35.144 41.950 1.00173.40 N ANISOU 2170 NH2 ARG A 296 21010 20335 24540 4846 148 -3116 N ATOM 2171 N GLN A 297 13.263 28.376 40.897 1.00156.92 N ANISOU 2171 N GLN A 297 15324 20591 23707 1880 -945 -1969 N ATOM 2172 CA GLN A 297 12.089 27.817 41.557 1.00158.89 C ANISOU 2172 CA GLN A 297 14622 21705 24046 1880 -797 -1880 C ATOM 2173 C GLN A 297 12.120 26.292 41.543 1.00154.23 C ANISOU 2173 C GLN A 297 13465 21448 23686 1048 -975 -1641 C ATOM 2174 O GLN A 297 11.604 25.643 42.453 1.00152.28 O ANISOU 2174 O GLN A 297 12584 21803 23472 773 -760 -1563 O ATOM 2175 CB GLN A 297 10.811 28.322 40.887 1.00167.40 C ANISOU 2175 CB GLN A 297 15229 23176 25200 2607 -949 -1901 C ATOM 2176 CG GLN A 297 10.664 29.835 40.898 1.00176.84 C ANISOU 2176 CG GLN A 297 16918 24095 26178 3469 -776 -2135 C ATOM 2177 CD GLN A 297 9.359 30.294 40.284 1.00190.21 C ANISOU 2177 CD GLN A 297 18100 26213 27956 4174 -920 -2151 C ATOM 2178 OE1 GLN A 297 8.484 29.484 39.980 1.00193.40 O ANISOU 2178 OE1 GLN A 297 17724 27187 28574 4033 -1108 -1991 O ATOM 2179 NE2 GLN A 297 9.220 31.601 40.099 1.00195.50 N ANISOU 2179 NE2 GLN A 297 19210 26608 28463 4940 -836 -2345 N ATOM 2180 N THR A 298 12.720 25.727 40.500 1.00152.48 N ANISOU 2180 N THR A 298 13474 20837 23626 651 -1372 -1527 N ATOM 2181 CA THR A 298 12.834 24.279 40.376 1.00150.65 C ANISOU 2181 CA THR A 298 12761 20855 23622 -155 -1577 -1299 C ATOM 2182 C THR A 298 13.798 23.725 41.418 1.00154.99 C ANISOU 2182 C THR A 298 13544 21255 24092 -844 -1318 -1278 C ATOM 2183 O THR A 298 13.475 22.776 42.131 1.00153.14 O ANISOU 2183 O THR A 298 12691 21550 23947 -1322 -1205 -1147 O ATOM 2184 CB THR A 298 13.322 23.865 38.976 1.00139.37 C ANISOU 2184 CB THR A 298 11593 18986 22377 -405 -2065 -1195 C ATOM 2185 OG1 THR A 298 12.505 24.485 37.976 1.00145.62 O ANISOU 2185 OG1 THR A 298 12262 19844 23224 268 -2308 -1230 O ATOM 2186 CG2 THR A 298 13.255 22.356 38.816 1.00130.44 C ANISOU 2186 CG2 THR A 298 9858 18203 21501 -1185 -2289 -953 C ATOM 2187 N PHE A 299 14.982 24.325 41.499 1.00161.81 N ANISOU 2187 N PHE A 299 15304 21391 24787 -891 -1228 -1406 N ATOM 2188 CA PHE A 299 15.990 23.903 42.464 1.00166.73 C ANISOU 2188 CA PHE A 299 16242 21791 25317 -1516 -982 -1403 C ATOM 2189 C PHE A 299 15.463 24.044 43.888 1.00175.30 C ANISOU 2189 C PHE A 299 16946 23406 26254 -1409 -520 -1462 C ATOM 2190 O PHE A 299 15.658 23.161 44.724 1.00180.58 O ANISOU 2190 O PHE A 299 17307 24347 26959 -2024 -367 -1359 O ATOM 2191 CB PHE A 299 17.270 24.727 42.305 1.00166.43 C ANISOU 2191 CB PHE A 299 17262 20875 25099 -1450 -941 -1560 C ATOM 2192 CG PHE A 299 17.848 24.696 40.919 1.00168.21 C ANISOU 2192 CG PHE A 299 17939 20527 25446 -1521 -1375 -1523 C ATOM 2193 CD1 PHE A 299 18.248 23.501 40.347 1.00166.79 C ANISOU 2193 CD1 PHE A 299 17579 20298 25496 -2239 -1693 -1330 C ATOM 2194 CD2 PHE A 299 18.004 25.865 40.194 1.00172.24 C ANISOU 2194 CD2 PHE A 299 19061 20541 25839 -875 -1463 -1683 C ATOM 2195 CE1 PHE A 299 18.784 23.470 39.074 1.00165.63 C ANISOU 2195 CE1 PHE A 299 17850 19623 25460 -2310 -2088 -1299 C ATOM 2196 CE2 PHE A 299 18.540 25.841 38.921 1.00171.24 C ANISOU 2196 CE2 PHE A 299 19358 19886 25821 -944 -1859 -1650 C ATOM 2197 CZ PHE A 299 18.931 24.641 38.360 1.00167.79 C ANISOU 2197 CZ PHE A 299 18732 19408 25612 -1664 -2171 -1459 C ATOM 2198 N ARG A 300 14.799 25.164 44.154 1.00176.87 N ANISOU 2198 N ARG A 300 17172 23744 26287 -624 -300 -1631 N ATOM 2199 CA ARG A 300 14.227 25.441 45.466 1.00180.47 C ANISOU 2199 CA ARG A 300 17284 24698 26588 -422 148 -1710 C ATOM 2200 C ARG A 300 13.327 24.294 45.917 1.00179.65 C ANISOU 2200 C ARG A 300 16187 25412 26662 -811 162 -1525 C ATOM 2201 O ARG A 300 13.320 23.922 47.091 1.00178.82 O ANISOU 2201 O ARG A 300 15827 25635 26482 -1124 485 -1510 O ATOM 2202 CB ARG A 300 13.447 26.756 45.422 1.00193.19 C ANISOU 2202 CB ARG A 300 18958 26397 28048 533 296 -1898 C ATOM 2203 CG ARG A 300 12.895 27.226 46.758 1.00203.85 C ANISOU 2203 CG ARG A 300 20047 28197 29212 829 778 -2013 C ATOM 2204 CD ARG A 300 12.283 28.614 46.618 1.00213.38 C ANISOU 2204 CD ARG A 300 21446 29367 30262 1782 902 -2215 C ATOM 2205 NE ARG A 300 11.585 29.050 47.824 1.00222.57 N ANISOU 2205 NE ARG A 300 22262 31034 31269 2115 1343 -2319 N ATOM 2206 CZ ARG A 300 10.993 30.233 47.954 1.00230.77 C ANISOU 2206 CZ ARG A 300 23398 32128 32156 2925 1529 -2503 C ATOM 2207 NH1 ARG A 300 11.019 31.100 46.951 1.00232.53 N ANISOU 2207 NH1 ARG A 300 24060 31928 32361 3484 1308 -2599 N ATOM 2208 NH2 ARG A 300 10.377 30.550 49.086 1.00236.15 N ANISOU 2208 NH2 ARG A 300 23740 33283 32702 3174 1936 -2590 N ATOM 2209 N LYS A 301 12.579 23.732 44.973 1.00178.61 N ANISOU 2209 N LYS A 301 15502 25599 26765 -796 -195 -1382 N ATOM 2210 CA LYS A 301 11.717 22.590 45.249 1.00174.57 C ANISOU 2210 CA LYS A 301 14035 25847 26448 -1177 -236 -1192 C ATOM 2211 C LYS A 301 12.540 21.373 45.655 1.00173.62 C ANISOU 2211 C LYS A 301 13881 25667 26422 -2127 -262 -1034 C ATOM 2212 O LYS A 301 12.281 20.750 46.685 1.00176.47 O ANISOU 2212 O LYS A 301 13761 26513 26777 -2485 -12 -967 O ATOM 2213 CB LYS A 301 10.878 22.249 44.017 1.00163.61 C ANISOU 2213 CB LYS A 301 12153 24713 25298 -987 -657 -1072 C ATOM 2214 CG LYS A 301 10.000 21.019 44.183 1.00153.99 C ANISOU 2214 CG LYS A 301 9947 24261 24302 -1400 -743 -863 C ATOM 2215 CD LYS A 301 9.782 20.317 42.852 1.00148.17 C ANISOU 2215 CD LYS A 301 8943 23523 23833 -1586 -1245 -696 C ATOM 2216 CE LYS A 301 9.277 21.280 41.791 1.00149.99 C ANISOU 2216 CE LYS A 301 9356 23570 24062 -811 -1464 -795 C ATOM 2217 NZ LYS A 301 9.182 20.631 40.454 1.00147.46 N ANISOU 2217 NZ LYS A 301 8864 23172 23991 -1010 -1962 -639 N ATOM 2218 N ILE A 302 13.529 21.040 44.832 1.00167.95 N ANISOU 2218 N ILE A 302 13674 24348 25793 -2530 -569 -975 N ATOM 2219 CA ILE A 302 14.370 19.871 45.060 1.00163.37 C ANISOU 2219 CA ILE A 302 13100 23647 25324 -3442 -647 -820 C ATOM 2220 C ILE A 302 15.009 19.883 46.445 1.00160.33 C ANISOU 2220 C ILE A 302 12956 23211 24749 -3764 -224 -886 C ATOM 2221 O ILE A 302 14.880 18.924 47.206 1.00161.73 O ANISOU 2221 O ILE A 302 12625 23827 24998 -4319 -105 -757 O ATOM 2222 CB ILE A 302 15.483 19.762 43.998 1.00159.39 C ANISOU 2222 CB ILE A 302 13284 22378 24899 -3740 -998 -795 C ATOM 2223 CG1 ILE A 302 14.880 19.691 42.594 1.00161.93 C ANISOU 2223 CG1 ILE A 302 13368 22740 25416 -3463 -1436 -719 C ATOM 2224 CG2 ILE A 302 16.359 18.549 44.267 1.00153.06 C ANISOU 2224 CG2 ILE A 302 12485 21454 24217 -4690 -1071 -638 C ATOM 2225 CD1 ILE A 302 15.912 19.583 41.489 1.00155.80 C ANISOU 2225 CD1 ILE A 302 13240 21232 24724 -3737 -1796 -693 C ATOM 2226 N ILE A 303 15.698 20.974 46.765 1.00157.29 N ANISOU 2226 N ILE A 303 13352 22288 24121 -3415 0 -1087 N ATOM 2227 CA ILE A 303 16.400 21.094 48.038 1.00152.33 C ANISOU 2227 CA ILE A 303 13054 21530 23295 -3688 399 -1167 C ATOM 2228 C ILE A 303 15.457 20.892 49.218 1.00160.47 C ANISOU 2228 C ILE A 303 13370 23333 24269 -3628 751 -1154 C ATOM 2229 O ILE A 303 15.701 20.051 50.083 1.00159.61 O ANISOU 2229 O ILE A 303 13004 23463 24179 -4245 910 -1055 O ATOM 2230 CB ILE A 303 17.097 22.462 48.177 1.00141.79 C ANISOU 2230 CB ILE A 303 12627 19553 21694 -3173 601 -1406 C ATOM 2231 CG1 ILE A 303 18.083 22.679 47.028 1.00120.27 C ANISOU 2231 CG1 ILE A 303 10645 16036 19016 -3245 262 -1426 C ATOM 2232 CG2 ILE A 303 17.805 22.566 49.521 1.00140.67 C ANISOU 2232 CG2 ILE A 303 12807 19293 21347 -3466 1018 -1486 C ATOM 2233 CD1 ILE A 303 18.782 24.019 47.071 1.00111.06 C ANISOU 2233 CD1 ILE A 303 10385 14213 17599 -2738 431 -1657 C ATOM 2234 N ARG A 304 14.379 21.668 49.248 1.00169.38 N ANISOU 2234 N ARG A 304 14180 24848 25328 -2882 872 -1254 N ATOM 2235 CA ARG A 304 13.395 21.574 50.320 1.00180.27 C ANISOU 2235 CA ARG A 304 14871 26974 26650 -2742 1209 -1256 C ATOM 2236 C ARG A 304 12.840 20.164 50.462 1.00183.45 C ANISOU 2236 C ARG A 304 14407 28012 27283 -3353 1087 -1023 C ATOM 2237 O ARG A 304 12.823 19.599 51.556 1.00184.23 O ANISOU 2237 O ARG A 304 14189 28470 27340 -3768 1358 -972 O ATOM 2238 CB ARG A 304 12.254 22.561 50.084 1.00191.02 C ANISOU 2238 CB ARG A 304 15978 28651 27951 -1835 1273 -1382 C ATOM 2239 CG ARG A 304 12.666 24.005 50.250 1.00195.92 C ANISOU 2239 CG ARG A 304 17369 28764 28309 -1194 1496 -1629 C ATOM 2240 CD ARG A 304 11.515 24.948 49.990 1.00206.00 C ANISOU 2240 CD ARG A 304 18368 30362 29540 -305 1544 -1748 C ATOM 2241 NE ARG A 304 11.836 26.302 50.427 1.00210.14 N ANISOU 2241 NE ARG A 304 19552 30501 29791 288 1841 -1989 N ATOM 2242 CZ ARG A 304 10.997 27.329 50.360 1.00217.29 C ANISOU 2242 CZ ARG A 304 20371 31586 30602 1108 1955 -2136 C ATOM 2243 NH1 ARG A 304 11.379 28.525 50.783 1.00217.26 N ANISOU 2243 NH1 ARG A 304 21003 31198 30347 1598 2227 -2353 N ATOM 2244 NH2 ARG A 304 9.778 27.161 49.868 1.00223.75 N ANISOU 2244 NH2 ARG A 304 20470 32966 31581 1438 1794 -2068 N ATOM 2245 N SER A 305 12.380 19.604 49.348 1.00185.22 N ANISOU 2245 N SER A 305 14252 28374 27749 -3403 678 -883 N ATOM 2246 CA SER A 305 11.810 18.264 49.346 1.00186.73 C ANISOU 2246 CA SER A 305 13607 29162 28178 -3957 520 -656 C ATOM 2247 C SER A 305 12.853 17.231 48.938 1.00180.40 C ANISOU 2247 C SER A 305 13040 27974 27531 -4793 249 -499 C ATOM 2248 O SER A 305 13.607 16.735 49.774 1.00178.31 O ANISOU 2248 O SER A 305 12943 27600 27208 -5376 434 -466 O ATOM 2249 CB SER A 305 10.603 18.197 48.408 1.00192.13 C ANISOU 2249 CB SER A 305 13660 30292 29049 -3530 237 -586 C ATOM 2250 OG SER A 305 9.986 16.923 48.464 1.00193.25 O ANISOU 2250 OG SER A 305 12959 31053 29415 -4039 107 -370 O TER 2251 SER A 305 HETATM 2252 N2 T4G A 330 50.356 24.015 31.108 1.00119.01 N HETATM 2253 N1 T4G A 330 49.210 23.574 31.703 1.00119.14 N HETATM 2254 C6 T4G A 330 47.919 23.679 31.147 1.00118.66 C HETATM 2255 C5 T4G A 330 47.766 24.287 29.849 1.00118.39 C HETATM 2256 N4 T4G A 330 48.963 24.727 29.270 1.00118.44 N HETATM 2257 C3 T4G A 330 50.199 24.595 29.874 1.00118.63 C HETATM 2258 N5 T4G A 330 44.795 21.918 33.516 1.00118.48 N HETATM 2259 C10 T4G A 330 45.957 21.271 33.272 1.00119.10 C HETATM 2260 C11 T4G A 330 46.996 21.821 32.503 1.00119.22 C HETATM 2261 C7 T4G A 330 46.833 23.112 31.959 1.00118.59 C HETATM 2262 C8 T4G A 330 45.621 23.791 32.204 1.00118.23 C HETATM 2263 C9 T4G A 330 44.639 23.151 32.989 1.00118.20 C HETATM 2264 C17 T4G A 330 44.052 24.948 27.699 1.00116.86 C HETATM 2265 C18 T4G A 330 44.323 23.688 28.261 1.00117.23 C HETATM 2266 C19 T4G A 330 45.520 23.453 28.961 1.00118.03 C HETATM 2267 C14 T4G A 330 46.483 24.479 29.120 1.00118.02 C HETATM 2268 C15 T4G A 330 46.194 25.744 28.546 1.00117.19 C HETATM 2269 C16 T4G A 330 44.995 25.983 27.844 1.00116.66 C HETATM 2270 N3 T4G A 330 51.287 25.042 29.241 1.00118.47 N HETATM 2271 C13 T4G A 330 43.327 23.834 33.285 1.00117.66 C HETATM 2272 C12 T4G A 330 46.121 19.890 33.868 1.00119.60 C CONECT 484 1071 CONECT 500 1041 CONECT 520 1115 CONECT 1041 500 CONECT 1071 484 CONECT 1115 520 CONECT 1861 1882 CONECT 1882 1861 CONECT 2252 2253 2257 CONECT 2253 2252 2254 CONECT 2254 2253 2255 2261 CONECT 2255 2254 2256 2267 CONECT 2256 2255 2257 CONECT 2257 2252 2256 2270 CONECT 2258 2259 2263 CONECT 2259 2258 2260 2272 CONECT 2260 2259 2261 CONECT 2261 2254 2260 2262 CONECT 2262 2261 2263 CONECT 2263 2258 2262 2271 CONECT 2264 2265 2269 CONECT 2265 2264 2266 CONECT 2266 2265 2267 CONECT 2267 2255 2266 2268 CONECT 2268 2267 2269 CONECT 2269 2264 2268 CONECT 2270 2257 CONECT 2271 2263 CONECT 2272 2259 MASTER 521 0 1 14 2 0 2 6 2271 1 29 26 END