Browse entries in the PDBbind-CN Database
HEADER OXIDOREDUCTASE 22-OCT-18 6IM9 TITLE MDM2 BOUND CUEO-PM2 SENSOR COMPND MOL_ID: 1; COMPND 2 MOLECULE: BLUE COPPER OXIDASE CUEO,PM2 PEPTIDE,BLUE COPPER OXIDASE COMPND 3 CUEO; COMPND 4 CHAIN: A; COMPND 5 SYNONYM: COPPER EFFLUX OXIDASE; COMPND 6 ENGINEERED: YES; COMPND 7 MUTATION: YES; COMPND 8 OTHER_DETAILS: CHIMERA PROTEIN CUEO-PM2 MULTICOPPER OXIDASE; COMPND 9 MOL_ID: 2; COMPND 10 MOLECULE: E3 UBIQUITIN-PROTEIN LIGASE MDM2; COMPND 11 CHAIN: B; COMPND 12 SYNONYM: DOUBLE MINUTE 2 PROTEIN,HDM2,ONCOPROTEIN MDM2,RING-TYPE E3 COMPND 13 UBIQUITIN TRANSFERASE MDM2,P53-BINDING PROTEIN MDM2; COMPND 14 EC: 2.3.2.27; COMPND 15 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI (STRAIN K12), SYNTHETIC SOURCE 3 CONSTRUCT; SOURCE 4 ORGANISM_TAXID: 83333, 32630; SOURCE 5 STRAIN: K12; SOURCE 6 GENE: CUEO, YACK, B0123, JW0119; SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 11 ORGANISM_COMMON: HUMAN; SOURCE 12 ORGANISM_TAXID: 9606; SOURCE 13 GENE: MDM2; SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 15 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS MULTICOPPER OXIDASE, LACCASE, MDM2, OXIDOREDUCTASE EXPDTA X-RAY DIFFRACTION AUTHOR J.WONGSANTICHON,R.ROBINSON,F.GHADESSY REVDAT 2 07-AUG-19 6IM9 1 JRNL REVDAT 1 20-MAR-19 6IM9 0 JRNL AUTH B.SANA,S.M.Q.CHEE,J.WONGSANTICHON,S.RAGHAVAN,R.C.ROBINSON, JRNL AUTH 2 F.J.GHADESSY JRNL TITL DEVELOPMENT AND STRUCTURAL CHARACTERIZATION OF AN ENGINEERED JRNL TITL 2 MULTI-COPPER OXIDASE REPORTER OF PROTEIN-PROTEIN JRNL TITL 3 INTERACTIONS. JRNL REF J.BIOL.CHEM. V. 294 7002 2019 JRNL REFN ESSN 1083-351X JRNL PMID 30770473 JRNL DOI 10.1074/JBC.RA118.007141 REMARK 2 REMARK 2 RESOLUTION. 3.30 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.13_2998 REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : GEOSTD + MONOMER LIBRARY REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.30 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.92 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.380 REMARK 3 COMPLETENESS FOR RANGE (%) : 92.1 REMARK 3 NUMBER OF REFLECTIONS : 14161 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.180 REMARK 3 R VALUE (WORKING SET) : 0.177 REMARK 3 FREE R VALUE : 0.249 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990 REMARK 3 FREE R VALUE TEST SET COUNT : 707 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 28.9200 - 5.6300 0.99 3057 154 0.1754 0.2667 REMARK 3 2 5.6300 - 4.4700 1.00 2956 152 0.1545 0.1943 REMARK 3 3 4.4700 - 3.9100 1.00 2877 156 0.1581 0.2255 REMARK 3 4 3.9100 - 3.5500 0.99 2837 144 0.2060 0.2885 REMARK 3 5 3.5500 - 3.3000 0.61 1727 101 0.2495 0.3779 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.11 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.447 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.483 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 66.85 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 70.27 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.011 4604 REMARK 3 ANGLE : 1.215 6248 REMARK 3 CHIRALITY : 0.061 690 REMARK 3 PLANARITY : 0.009 809 REMARK 3 DIHEDRAL : 7.800 2756 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 11 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 31 THROUGH 342 ) REMARK 3 ORIGIN FOR THE GROUP (A): 25.4481 -24.2417 9.7156 REMARK 3 T TENSOR REMARK 3 T11: 0.8031 T22: 0.3556 REMARK 3 T33: 0.4410 T12: -0.5693 REMARK 3 T13: 0.2049 T23: 0.0049 REMARK 3 L TENSOR REMARK 3 L11: 1.0939 L22: 1.8462 REMARK 3 L33: 1.1475 L12: 0.4416 REMARK 3 L13: 0.4333 L23: -0.3052 REMARK 3 S TENSOR REMARK 3 S11: -0.0283 S12: -0.1622 S13: -0.1439 REMARK 3 S21: 0.5016 S22: 0.1163 S23: 0.1887 REMARK 3 S31: 0.2076 S32: -0.4997 S33: -0.0906 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 343 THROUGH 444 ) REMARK 3 ORIGIN FOR THE GROUP (A): 38.6145 -8.7026 28.0426 REMARK 3 T TENSOR REMARK 3 T11: 1.2174 T22: 0.5090 REMARK 3 T33: 0.5444 T12: -0.1555 REMARK 3 T13: 0.1356 T23: -0.1345 REMARK 3 L TENSOR REMARK 3 L11: 1.8016 L22: 1.1275 REMARK 3 L33: 1.9039 L12: 0.1822 REMARK 3 L13: 1.7370 L23: -0.2723 REMARK 3 S TENSOR REMARK 3 S11: 0.1677 S12: -0.1498 S13: -0.1983 REMARK 3 S21: 0.4210 S22: -0.0247 S23: 0.0279 REMARK 3 S31: 0.2435 S32: -0.1642 S33: -0.1053 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 445 THROUGH 520 ) REMARK 3 ORIGIN FOR THE GROUP (A): 26.2806 -6.5650 16.9786 REMARK 3 T TENSOR REMARK 3 T11: 0.8739 T22: 0.4887 REMARK 3 T33: 0.3698 T12: -0.1978 REMARK 3 T13: 0.1569 T23: -0.0789 REMARK 3 L TENSOR REMARK 3 L11: 1.0217 L22: 1.8168 REMARK 3 L33: 1.9007 L12: 0.1091 REMARK 3 L13: 0.6400 L23: -0.6135 REMARK 3 S TENSOR REMARK 3 S11: -0.1399 S12: -0.3548 S13: 0.1249 REMARK 3 S21: 0.4913 S22: 0.0714 S23: 0.4136 REMARK 3 S31: -0.1982 S32: -0.4551 S33: 0.0506 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 25 THROUGH 31 ) REMARK 3 ORIGIN FOR THE GROUP (A): 49.9391 -3.4941 59.0886 REMARK 3 T TENSOR REMARK 3 T11: 0.8937 T22: 0.3561 REMARK 3 T33: 0.3750 T12: 0.1377 REMARK 3 T13: 0.0404 T23: -0.0797 REMARK 3 L TENSOR REMARK 3 L11: 7.7490 L22: 5.9515 REMARK 3 L33: 0.2350 L12: -4.5837 REMARK 3 L13: -1.0124 L23: 0.0224 REMARK 3 S TENSOR REMARK 3 S11: -0.0183 S12: -0.0053 S13: 0.4910 REMARK 3 S21: 0.1462 S22: -0.0600 S23: 0.0181 REMARK 3 S31: -0.1507 S32: 0.0683 S33: 0.0556 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 32 THROUGH 39 ) REMARK 3 ORIGIN FOR THE GROUP (A): 62.3224 -3.1987 56.8047 REMARK 3 T TENSOR REMARK 3 T11: 0.7384 T22: 0.4823 REMARK 3 T33: 0.4894 T12: 0.0740 REMARK 3 T13: -0.0709 T23: -0.0409 REMARK 3 L TENSOR REMARK 3 L11: 6.3385 L22: 2.1060 REMARK 3 L33: 2.3239 L12: 1.2892 REMARK 3 L13: 2.4538 L23: -1.0710 REMARK 3 S TENSOR REMARK 3 S11: 0.0053 S12: -0.0559 S13: -0.0694 REMARK 3 S21: 0.0466 S22: -0.0940 S23: -0.5512 REMARK 3 S31: 0.0017 S32: 0.6101 S33: 0.0800 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 40 THROUGH 49 ) REMARK 3 ORIGIN FOR THE GROUP (A): 57.0062 3.1419 56.1177 REMARK 3 T TENSOR REMARK 3 T11: 0.9286 T22: 0.5460 REMARK 3 T33: 0.5488 T12: 0.1066 REMARK 3 T13: -0.0593 T23: -0.1630 REMARK 3 L TENSOR REMARK 3 L11: 4.5516 L22: 1.1239 REMARK 3 L33: 1.1028 L12: -1.8396 REMARK 3 L13: -1.9573 L23: 0.4767 REMARK 3 S TENSOR REMARK 3 S11: 0.1283 S12: -0.3105 S13: 0.5746 REMARK 3 S21: 0.2821 S22: -0.0412 S23: -0.3274 REMARK 3 S31: -0.7002 S32: 0.4759 S33: -0.0808 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 50 THROUGH 63 ) REMARK 3 ORIGIN FOR THE GROUP (A): 56.4482 -1.6957 47.3183 REMARK 3 T TENSOR REMARK 3 T11: 0.9671 T22: 0.4340 REMARK 3 T33: 0.3214 T12: 0.0731 REMARK 3 T13: -0.0371 T23: -0.0447 REMARK 3 L TENSOR REMARK 3 L11: 7.8459 L22: 2.9661 REMARK 3 L33: 3.5534 L12: -0.5836 REMARK 3 L13: -2.0921 L23: 0.3611 REMARK 3 S TENSOR REMARK 3 S11: -0.0187 S12: -0.1327 S13: 0.1986 REMARK 3 S21: -0.0092 S22: 0.0016 S23: -0.2071 REMARK 3 S31: -0.1567 S32: 0.2232 S33: -0.0365 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 64 THROUGH 73 ) REMARK 3 ORIGIN FOR THE GROUP (A): 63.7335 -9.7490 36.0440 REMARK 3 T TENSOR REMARK 3 T11: 1.0029 T22: 0.8044 REMARK 3 T33: 0.8856 T12: 0.1374 REMARK 3 T13: 0.2185 T23: 0.0010 REMARK 3 L TENSOR REMARK 3 L11: 0.2731 L22: 0.3245 REMARK 3 L33: 3.7599 L12: -0.2957 REMARK 3 L13: -1.0122 L23: 1.1044 REMARK 3 S TENSOR REMARK 3 S11: -0.0698 S12: 0.4744 S13: -0.3556 REMARK 3 S21: -0.3763 S22: 0.1804 S23: -0.3998 REMARK 3 S31: 0.0941 S32: 0.4980 S33: -0.1451 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 74 THROUGH 86 ) REMARK 3 ORIGIN FOR THE GROUP (A): 65.3427 -12.5704 47.6957 REMARK 3 T TENSOR REMARK 3 T11: 1.0871 T22: 0.7083 REMARK 3 T33: 0.7544 T12: 0.3667 REMARK 3 T13: 0.0588 T23: -0.1408 REMARK 3 L TENSOR REMARK 3 L11: 3.2132 L22: 0.6030 REMARK 3 L33: 5.4234 L12: 1.3720 REMARK 3 L13: 3.8012 L23: 1.4963 REMARK 3 S TENSOR REMARK 3 S11: -0.0025 S12: 0.1942 S13: -0.3456 REMARK 3 S21: -0.1288 S22: 0.0949 S23: -0.6429 REMARK 3 S31: 0.3191 S32: 0.9795 S33: -0.1062 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 87 THROUGH 95 ) REMARK 3 ORIGIN FOR THE GROUP (A): 58.5549 -16.3491 43.7590 REMARK 3 T TENSOR REMARK 3 T11: 0.9802 T22: 0.4533 REMARK 3 T33: 0.7960 T12: 0.3309 REMARK 3 T13: 0.1966 T23: -0.2928 REMARK 3 L TENSOR REMARK 3 L11: 4.6251 L22: 2.7343 REMARK 3 L33: 3.0659 L12: -1.7073 REMARK 3 L13: 2.7407 L23: -1.0280 REMARK 3 S TENSOR REMARK 3 S11: -0.1337 S12: -0.0898 S13: -0.3811 REMARK 3 S21: 0.3204 S22: 0.0971 S23: -0.1048 REMARK 3 S31: 0.4397 S32: 0.1228 S33: 0.0273 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 96 THROUGH 111 ) REMARK 3 ORIGIN FOR THE GROUP (A): 51.0685 -12.1581 53.7487 REMARK 3 T TENSOR REMARK 3 T11: 1.0394 T22: 0.2806 REMARK 3 T33: 0.5288 T12: 0.2825 REMARK 3 T13: -0.0614 T23: -0.1221 REMARK 3 L TENSOR REMARK 3 L11: 0.3449 L22: 0.4479 REMARK 3 L33: 2.4981 L12: -0.0173 REMARK 3 L13: 0.1495 L23: -0.0959 REMARK 3 S TENSOR REMARK 3 S11: -0.0456 S12: 0.1179 S13: -0.3367 REMARK 3 S21: -0.1705 S22: -0.0335 S23: 0.1202 REMARK 3 S31: 0.2788 S32: 0.0776 S33: 0.0720 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 6IM9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-NOV-18. REMARK 100 THE DEPOSITION ID IS D_1300009411. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 14-OCT-15 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : NSRRC REMARK 200 BEAMLINE : BL13B1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15209 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.300 REMARK 200 RESOLUTION RANGE LOW (A) : 30.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.7 REMARK 200 DATA REDUNDANCY : 5.100 REMARK 200 R MERGE (I) : 0.04600 REMARK 200 R SYM (I) : NULL REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.1000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.30 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.38 REMARK 200 COMPLETENESS FOR SHELL (%) : 85.8 REMARK 200 DATA REDUNDANCY IN SHELL : 3.40 REMARK 200 R MERGE FOR SHELL (I) : 0.28200 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: MOLREP REMARK 200 STARTING MODEL: 1KV7 AND 5WTS REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 64.70 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.48 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 4M SODIUM FORMATE, VAPOR DIFFUSION, REMARK 280 SITTING DROP, TEMPERATURE 289K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z+2/3 REMARK 290 3555 -X+Y,-X,Z+1/3 REMARK 290 4555 Y,X,-Z REMARK 290 5555 X-Y,-Y,-Z+1/3 REMARK 290 6555 -X,-X+Y,-Z+2/3 REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 160.11400 REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 80.05700 REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 80.05700 REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 160.11400 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 1570 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 23140 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 ALA A 29 REMARK 465 GLU A 30 REMARK 465 SER A 521 REMARK 465 SER A 522 REMARK 465 SER A 523 REMARK 465 VAL A 524 REMARK 465 ASP A 525 REMARK 465 LYS A 526 REMARK 465 LEU A 527 REMARK 465 ALA A 528 REMARK 465 ALA A 529 REMARK 465 ALA A 530 REMARK 465 LEU A 531 REMARK 465 GLU A 532 REMARK 465 HIS A 533 REMARK 465 HIS A 534 REMARK 465 HIS A 535 REMARK 465 HIS A 536 REMARK 465 HIS A 537 REMARK 465 GLY B 4 REMARK 465 PRO B 5 REMARK 465 MET B 6 REMARK 465 SER B 7 REMARK 465 VAL B 8 REMARK 465 PRO B 9 REMARK 465 THR B 10 REMARK 465 ASP B 11 REMARK 465 GLY B 12 REMARK 465 ALA B 13 REMARK 465 VAL B 14 REMARK 465 THR B 15 REMARK 465 THR B 16 REMARK 465 SER B 17 REMARK 465 GLN B 18 REMARK 465 ILE B 19 REMARK 465 PRO B 20 REMARK 465 ALA B 21 REMARK 465 SER B 22 REMARK 465 GLU B 23 REMARK 465 GLN B 24 REMARK 465 GLN B 112 REMARK 465 GLN B 113 REMARK 465 GLU B 114 REMARK 465 SER B 115 REMARK 465 SER B 116 REMARK 465 ASP B 117 REMARK 465 SER B 118 REMARK 465 GLY B 119 REMARK 465 THR B 120 REMARK 465 SER B 121 REMARK 465 VAL B 122 REMARK 465 SER B 123 REMARK 465 GLU B 124 REMARK 465 ASN B 125 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 OH TYR A 221 OD2 ASP A 294 2.04 REMARK 500 OH TYR B 60 OD2 ASP B 80 2.12 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 ASP A 43 -158.29 -98.45 REMARK 500 ASN A 46 72.98 -62.69 REMARK 500 ILE A 52 78.79 -100.08 REMARK 500 ASN A 70 44.21 37.97 REMARK 500 LEU A 74 -12.63 69.94 REMARK 500 GLN A 93 41.03 -93.88 REMARK 500 ILE A 178 -70.76 -111.23 REMARK 500 LEU A 200 56.77 -98.58 REMARK 500 ASN A 288 -70.66 -128.29 REMARK 500 ASN A 290 6.56 -66.62 REMARK 500 LYS A 291 108.92 -58.99 REMARK 500 PHE A 293 147.24 -171.01 REMARK 500 SER A 301 64.88 -69.73 REMARK 500 ALA A 323 30.77 -76.02 REMARK 500 SER A 327 -19.11 -148.53 REMARK 500 HIS A 381 -132.95 -160.23 REMARK 500 ASN A 397 58.64 -96.95 REMARK 500 MET A 440 33.20 -98.44 REMARK 500 ASN A 478 -152.81 -133.31 REMARK 500 MET A 511 143.30 -178.63 REMARK 500 LYS B 45 178.18 -56.51 REMARK 500 THR B 47 103.66 -173.62 REMARK 500 LYS B 70 -70.19 -88.87 REMARK 500 REMARK 500 REMARK: NULL DBREF 6IM9 A 29 384 UNP P36649 CUEO_ECOLI 29 384 DBREF 6IM9 A 385 395 PDB 6IM9 6IM9 385 395 DBREF 6IM9 A 396 516 UNP P36649 CUEO_ECOLI 396 516 DBREF 6IM9 B 6 125 UNP Q00987 MDM2_HUMAN 6 125 SEQADV 6IM9 ILE A 358 UNP P36649 MET 358 ENGINEERED MUTATION SEQADV 6IM9 LYS A 517 UNP P36649 EXPRESSION TAG SEQADV 6IM9 ASP A 518 UNP P36649 EXPRESSION TAG SEQADV 6IM9 PRO A 519 UNP P36649 EXPRESSION TAG SEQADV 6IM9 ASN A 520 UNP P36649 EXPRESSION TAG SEQADV 6IM9 SER A 521 UNP P36649 EXPRESSION TAG SEQADV 6IM9 SER A 522 UNP P36649 EXPRESSION TAG SEQADV 6IM9 SER A 523 UNP P36649 EXPRESSION TAG SEQADV 6IM9 VAL A 524 UNP P36649 EXPRESSION TAG SEQADV 6IM9 ASP A 525 UNP P36649 EXPRESSION TAG SEQADV 6IM9 LYS A 526 UNP P36649 EXPRESSION TAG SEQADV 6IM9 LEU A 527 UNP P36649 EXPRESSION TAG SEQADV 6IM9 ALA A 528 UNP P36649 EXPRESSION TAG SEQADV 6IM9 ALA A 529 UNP P36649 EXPRESSION TAG SEQADV 6IM9 ALA A 530 UNP P36649 EXPRESSION TAG SEQADV 6IM9 LEU A 531 UNP P36649 EXPRESSION TAG SEQADV 6IM9 GLU A 532 UNP P36649 EXPRESSION TAG SEQADV 6IM9 HIS A 533 UNP P36649 EXPRESSION TAG SEQADV 6IM9 HIS A 534 UNP P36649 EXPRESSION TAG SEQADV 6IM9 HIS A 535 UNP P36649 EXPRESSION TAG SEQADV 6IM9 HIS A 536 UNP P36649 EXPRESSION TAG SEQADV 6IM9 HIS A 537 UNP P36649 EXPRESSION TAG SEQADV 6IM9 GLY B 4 UNP Q00987 EXPRESSION TAG SEQADV 6IM9 PRO B 5 UNP Q00987 EXPRESSION TAG SEQRES 1 A 509 ALA GLU ARG PRO THR LEU PRO ILE PRO ASP LEU LEU THR SEQRES 2 A 509 THR ASP ALA ARG ASN ARG ILE GLN LEU THR ILE GLY ALA SEQRES 3 A 509 GLY GLN SER THR PHE GLY GLY LYS THR ALA THR THR TRP SEQRES 4 A 509 GLY TYR ASN GLY ASN LEU LEU GLY PRO ALA VAL LYS LEU SEQRES 5 A 509 GLN ARG GLY LYS ALA VAL THR VAL ASP ILE TYR ASN GLN SEQRES 6 A 509 LEU THR GLU GLU THR THR LEU HIS TRP HIS GLY LEU GLU SEQRES 7 A 509 VAL PRO GLY GLU VAL ASP GLY GLY PRO GLN GLY ILE ILE SEQRES 8 A 509 PRO PRO GLY GLY LYS ARG SER VAL THR LEU ASN VAL ASP SEQRES 9 A 509 GLN PRO ALA ALA THR CYS TRP PHE HIS PRO HIS GLN HIS SEQRES 10 A 509 GLY LYS THR GLY ARG GLN VAL ALA MET GLY LEU ALA GLY SEQRES 11 A 509 LEU VAL VAL ILE GLU ASP ASP GLU ILE LEU LYS LEU MET SEQRES 12 A 509 LEU PRO LYS GLN TRP GLY ILE ASP ASP VAL PRO VAL ILE SEQRES 13 A 509 VAL GLN ASP LYS LYS PHE SER ALA ASP GLY GLN ILE ASP SEQRES 14 A 509 TYR GLN LEU ASP VAL MET THR ALA ALA VAL GLY TRP PHE SEQRES 15 A 509 GLY ASP THR LEU LEU THR ASN GLY ALA ILE TYR PRO GLN SEQRES 16 A 509 HIS ALA ALA PRO ARG GLY TRP LEU ARG LEU ARG LEU LEU SEQRES 17 A 509 ASN GLY CYS ASN ALA ARG SER LEU ASN PHE ALA THR SER SEQRES 18 A 509 ASP ASN ARG PRO LEU TYR VAL ILE ALA SER ASP GLY GLY SEQRES 19 A 509 LEU LEU PRO GLU PRO VAL LYS VAL SER GLU LEU PRO VAL SEQRES 20 A 509 LEU MET GLY GLU ARG PHE GLU VAL LEU VAL GLU VAL ASN SEQRES 21 A 509 ASP ASN LYS PRO PHE ASP LEU VAL THR LEU PRO VAL SER SEQRES 22 A 509 GLN MET GLY MET ALA ILE ALA PRO PHE ASP LYS PRO HIS SEQRES 23 A 509 PRO VAL MET ARG ILE GLN PRO ILE ALA ILE SER ALA SER SEQRES 24 A 509 GLY ALA LEU PRO ASP THR LEU SER SER LEU PRO ALA LEU SEQRES 25 A 509 PRO SER LEU GLU GLY LEU THR VAL ARG LYS LEU GLN LEU SEQRES 26 A 509 SER MET ASP PRO ILE LEU ASP MET MET GLY MET GLN MET SEQRES 27 A 509 LEU MET GLU LYS TYR GLY ASP GLN ALA MET ALA GLY MET SEQRES 28 A 509 ASP HIS SER GLN MET THR SER PHE ALA GLU TYR TRP ALA SEQRES 29 A 509 LEU LEU SER MET ASN HIS GLY GLY LYS PHE ASP PHE HIS SEQRES 30 A 509 HIS ALA ASN LYS ILE ASN GLY GLN ALA PHE ASP MET ASN SEQRES 31 A 509 LYS PRO MET PHE ALA ALA ALA LYS GLY GLN TYR GLU ARG SEQRES 32 A 509 TRP VAL ILE SER GLY VAL GLY ASP MET MET LEU HIS PRO SEQRES 33 A 509 PHE HIS ILE HIS GLY THR GLN PHE ARG ILE LEU SER GLU SEQRES 34 A 509 ASN GLY LYS PRO PRO ALA ALA HIS ARG ALA GLY TRP LYS SEQRES 35 A 509 ASP THR VAL LYS VAL GLU GLY ASN VAL SER GLU VAL LEU SEQRES 36 A 509 VAL LYS PHE ASN HIS ASP ALA PRO LYS GLU HIS ALA TYR SEQRES 37 A 509 MET ALA HIS CYS HIS LEU LEU GLU HIS GLU ASP THR GLY SEQRES 38 A 509 MET MET LEU GLY PHE THR VAL LYS ASP PRO ASN SER SER SEQRES 39 A 509 SER VAL ASP LYS LEU ALA ALA ALA LEU GLU HIS HIS HIS SEQRES 40 A 509 HIS HIS SEQRES 1 B 122 GLY PRO MET SER VAL PRO THR ASP GLY ALA VAL THR THR SEQRES 2 B 122 SER GLN ILE PRO ALA SER GLU GLN GLU THR LEU VAL ARG SEQRES 3 B 122 PRO LYS PRO LEU LEU LEU LYS LEU LEU LYS SER VAL GLY SEQRES 4 B 122 ALA GLN LYS ASP THR TYR THR MET LYS GLU VAL LEU PHE SEQRES 5 B 122 TYR LEU GLY GLN TYR ILE MET THR LYS ARG LEU TYR ASP SEQRES 6 B 122 GLU LYS GLN GLN HIS ILE VAL TYR CYS SER ASN ASP LEU SEQRES 7 B 122 LEU GLY ASP LEU PHE GLY VAL PRO SER PHE SER VAL LYS SEQRES 8 B 122 GLU HIS ARG LYS ILE TYR THR MET ILE TYR ARG ASN LEU SEQRES 9 B 122 VAL VAL VAL ASN GLN GLN GLU SER SER ASP SER GLY THR SEQRES 10 B 122 SER VAL SER GLU ASN HELIX 1 AA1 PRO A 108 GLY A 113 1 6 HELIX 2 AA2 LYS A 147 GLY A 155 1 9 HELIX 3 AA3 ASP A 164 LYS A 169 1 6 HELIX 4 AA4 MET A 203 GLY A 208 1 6 HELIX 5 AA5 ASP A 356 TYR A 371 1 16 HELIX 6 AA6 GLY A 372 ALA A 375 5 4 HELIX 7 AA7 SER A 386 ASN A 397 1 12 HELIX 8 AA8 ASP A 403 HIS A 406 5 4 HELIX 9 AA9 ALA A 463 ALA A 467 5 5 HELIX 10 AB1 LEU A 502 THR A 508 1 7 HELIX 11 AB2 LYS B 31 SER B 40 1 10 HELIX 12 AB3 MET B 50 LYS B 64 1 15 HELIX 13 AB4 ASP B 80 GLY B 87 1 8 HELIX 14 AB5 GLU B 95 ASN B 106 1 12 SHEET 1 AA1 4 LYS A 62 TYR A 69 0 SHEET 2 AA1 4 ARG A 47 PHE A 59 -1 N SER A 57 O ALA A 64 SHEET 3 AA1 4 ALA A 85 TYR A 91 1 O TYR A 91 N ILE A 52 SHEET 4 AA1 4 LYS A 124 ASN A 130 -1 O LEU A 129 N VAL A 86 SHEET 1 AA2 4 VAL A 78 GLN A 81 0 SHEET 2 AA2 4 LEU A 159 GLU A 163 1 O VAL A 161 N LEU A 80 SHEET 3 AA2 4 ALA A 136 HIS A 141 -1 N CYS A 138 O VAL A 160 SHEET 4 AA2 4 HIS A 101 HIS A 103 -1 N HIS A 101 O HIS A 141 SHEET 1 AA3 7 ALA A 219 ILE A 220 0 SHEET 2 AA3 7 THR A 213 THR A 216 -1 N THR A 216 O ALA A 219 SHEET 3 AA3 7 ASP A 180 LYS A 188 -1 N GLN A 186 O LEU A 215 SHEET 4 AA3 7 GLY A 229 ASN A 237 1 O ARG A 234 N VAL A 183 SHEET 5 AA3 7 ARG A 280 VAL A 287 -1 O VAL A 287 N GLY A 229 SHEET 6 AA3 7 LEU A 254 SER A 259 -1 N ILE A 257 O GLU A 282 SHEET 7 AA3 7 GLY A 262 VAL A 270 -1 O VAL A 268 N VAL A 256 SHEET 1 AA4 5 GLN A 223 ALA A 226 0 SHEET 2 AA4 5 HIS A 314 PRO A 321 1 O GLN A 320 N HIS A 224 SHEET 3 AA4 5 PHE A 293 THR A 297 -1 N LEU A 295 O MET A 317 SHEET 4 AA4 5 LEU A 244 THR A 248 -1 N ALA A 247 O VAL A 296 SHEET 5 AA4 5 LEU A 273 VAL A 275 -1 O VAL A 275 N LEU A 244 SHEET 1 AA5 5 ASN A 408 ILE A 410 0 SHEET 2 AA5 5 THR A 347 MET A 355 -1 N SER A 354 O LYS A 409 SHEET 3 AA5 5 GLU A 430 SER A 435 1 O SER A 435 N LEU A 351 SHEET 4 AA5 5 VAL A 479 VAL A 484 -1 O SER A 480 N ILE A 434 SHEET 5 AA5 5 ARG A 453 SER A 456 -1 N ARG A 453 O LEU A 483 SHEET 1 AA6 5 PHE A 422 ALA A 425 0 SHEET 2 AA6 5 MET A 511 LYS A 517 1 O THR A 515 N ALA A 424 SHEET 3 AA6 5 TYR A 496 CYS A 500 -1 N ALA A 498 O LEU A 512 SHEET 4 AA6 5 PHE A 445 ILE A 447 -1 N HIS A 446 O HIS A 499 SHEET 5 AA6 5 THR A 472 VAL A 473 -1 O VAL A 473 N PHE A 445 SHEET 1 AA7 3 TYR B 48 THR B 49 0 SHEET 2 AA7 3 LEU B 27 PRO B 30 -1 N VAL B 28 O TYR B 48 SHEET 3 AA7 3 LEU B 107 VAL B 109 -1 O VAL B 108 N ARG B 29 SHEET 1 AA8 2 ILE B 74 TYR B 76 0 SHEET 2 AA8 2 SER B 90 SER B 92 -1 O PHE B 91 N VAL B 75 CISPEP 1 ALA A 308 PRO A 309 0 2.15 CRYST1 83.636 83.636 240.171 90.00 90.00 120.00 P 32 2 1 6 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.011957 0.006903 0.000000 0.00000 SCALE2 0.000000 0.013806 0.000000 0.00000 SCALE3 0.000000 0.000000 0.004164 0.00000 ATOM 1 N ARG A 31 34.769 -43.371 2.963 1.00 67.67 N ANISOU 1 N ARG A 31 10691 6432 8588 -3478 623 -353 N ATOM 2 CA ARG A 31 34.278 -42.206 3.718 1.00 67.93 C ANISOU 2 CA ARG A 31 10720 6595 8495 -3465 646 -308 C ATOM 3 C ARG A 31 32.754 -42.211 3.812 1.00 66.13 C ANISOU 3 C ARG A 31 10517 6471 8138 -3549 678 -274 C ATOM 4 O ARG A 31 32.085 -42.614 2.862 1.00 71.88 O ANISOU 4 O ARG A 31 11240 7229 8843 -3602 704 -307 O ATOM 5 CB ARG A 31 34.707 -40.875 3.067 1.00 71.57 C ANISOU 5 CB ARG A 31 11118 7164 8911 -3398 693 -356 C ATOM 6 CG ARG A 31 36.197 -40.663 2.745 1.00 75.70 C ANISOU 6 CG ARG A 31 11594 7609 9559 -3316 674 -398 C ATOM 7 CD ARG A 31 37.075 -40.715 3.975 1.00 76.26 C ANISOU 7 CD ARG A 31 11677 7578 9720 -3273 603 -346 C ATOM 8 NE ARG A 31 36.363 -40.305 5.173 1.00 76.17 N ANISOU 8 NE ARG A 31 11716 7625 9600 -3298 592 -275 N ATOM 9 CZ ARG A 31 36.642 -40.763 6.385 1.00 79.83 C ANISOU 9 CZ ARG A 31 12230 7995 10106 -3305 529 -213 C ATOM 10 NH1 ARG A 31 37.599 -41.660 6.546 1.00 84.86 N ANISOU 10 NH1 ARG A 31 12866 8471 10907 -3285 463 -211 N ATOM 11 NH2 ARG A 31 35.955 -40.344 7.435 1.00 81.20 N ANISOU 11 NH2 ARG A 31 12457 8232 10163 -3336 530 -154 N ATOM 12 N PRO A 32 32.213 -41.718 4.928 1.00 60.35 N ANISOU 12 N PRO A 32 9810 5794 7325 -3564 678 -213 N ATOM 13 CA PRO A 32 30.755 -41.676 5.119 1.00 62.95 C ANISOU 13 CA PRO A 32 10151 6219 7548 -3644 710 -178 C ATOM 14 C PRO A 32 30.106 -40.549 4.351 1.00 62.64 C ANISOU 14 C PRO A 32 10052 6330 7419 -3632 768 -217 C ATOM 15 O PRO A 32 30.704 -39.493 4.152 1.00 65.23 O ANISOU 15 O PRO A 32 10345 6709 7732 -3557 786 -249 O ATOM 16 CB PRO A 32 30.620 -41.412 6.615 1.00 53.30 C ANISOU 16 CB PRO A 32 8975 4996 6280 -3651 693 -107 C ATOM 17 CG PRO A 32 31.782 -40.546 6.908 1.00 52.25 C ANISOU 17 CG PRO A 32 8829 4852 6172 -3556 679 -125 C ATOM 18 CD PRO A 32 32.915 -41.109 6.067 1.00 58.72 C ANISOU 18 CD PRO A 32 9622 5568 7121 -3509 649 -174 C ATOM 19 N THR A 33 28.858 -40.754 3.931 1.00 61.88 N ANISOU 19 N THR A 33 9942 6300 7270 -3709 792 -208 N ATOM 20 CA THR A 33 28.243 -39.758 3.057 1.00 60.53 C ANISOU 20 CA THR A 33 9709 6258 7031 -3701 836 -246 C ATOM 21 C THR A 33 27.636 -38.649 3.913 1.00 59.15 C ANISOU 21 C THR A 33 9514 6178 6784 -3686 864 -214 C ATOM 22 O THR A 33 27.050 -38.910 4.961 1.00 62.25 O ANISOU 22 O THR A 33 9935 6561 7157 -3731 862 -156 O ATOM 23 CB THR A 33 27.224 -40.380 2.084 1.00 56.67 C ANISOU 23 CB THR A 33 9204 5797 6530 -3788 841 -256 C ATOM 24 OG1 THR A 33 25.936 -40.460 2.680 1.00 55.81 O ANISOU 24 OG1 THR A 33 9084 5739 6382 -3863 848 -197 O ATOM 25 CG2 THR A 33 27.674 -41.775 1.653 1.00 58.73 C ANISOU 25 CG2 THR A 33 9512 5933 6871 -3826 806 -271 C ATOM 26 N LEU A 34 27.850 -37.413 3.496 1.00 55.96 N ANISOU 26 N LEU A 34 9064 5854 6345 -3621 890 -251 N ATOM 27 CA LEU A 34 27.560 -36.274 4.340 1.00 49.15 C ANISOU 27 CA LEU A 34 8187 5057 5430 -3588 913 -231 C ATOM 28 C LEU A 34 26.066 -36.192 4.601 1.00 49.76 C ANISOU 28 C LEU A 34 8233 5205 5469 -3662 941 -193 C ATOM 29 O LEU A 34 25.276 -36.380 3.682 1.00 57.46 O ANISOU 29 O LEU A 34 9162 6225 6444 -3710 947 -203 O ATOM 30 CB LEU A 34 28.039 -34.999 3.658 1.00 47.84 C ANISOU 30 CB LEU A 34 7972 4958 5246 -3511 930 -280 C ATOM 31 CG LEU A 34 27.571 -33.653 4.172 1.00 47.06 C ANISOU 31 CG LEU A 34 7843 4940 5098 -3479 958 -274 C ATOM 32 CD1 LEU A 34 28.465 -33.163 5.308 1.00 46.56 C ANISOU 32 CD1 LEU A 34 7827 4833 5031 -3421 945 -259 C ATOM 33 CD2 LEU A 34 27.532 -32.690 3.023 1.00 46.22 C ANISOU 33 CD2 LEU A 34 7674 4910 4978 -3444 972 -318 C ATOM 34 N PRO A 35 25.656 -35.917 5.826 1.00 49.98 N ANISOU 34 N PRO A 35 8281 5240 5468 -3675 958 -149 N ATOM 35 CA PRO A 35 24.229 -35.825 6.151 1.00 50.72 C ANISOU 35 CA PRO A 35 8332 5397 5542 -3746 995 -106 C ATOM 36 C PRO A 35 23.621 -34.513 5.699 1.00 49.93 C ANISOU 36 C PRO A 35 8148 5397 5425 -3714 1031 -129 C ATOM 37 O PRO A 35 24.242 -33.470 5.834 1.00 61.37 O ANISOU 37 O PRO A 35 9599 6865 6856 -3636 1038 -160 O ATOM 38 CB PRO A 35 24.228 -35.891 7.678 1.00 51.19 C ANISOU 38 CB PRO A 35 8454 5422 5573 -3762 1010 -56 C ATOM 39 CG PRO A 35 25.591 -36.336 8.073 1.00 50.95 C ANISOU 39 CG PRO A 35 8506 5296 5557 -3716 962 -63 C ATOM 40 CD PRO A 35 26.510 -35.911 7.014 1.00 49.87 C ANISOU 40 CD PRO A 35 8340 5160 5447 -3640 941 -126 C ATOM 41 N ILE A 36 22.384 -34.532 5.219 1.00 50.58 N ANISOU 41 N ILE A 36 8156 5541 5524 -3776 1050 -106 N ATOM 42 CA ILE A 36 21.773 -33.246 4.871 1.00 49.95 C ANISOU 42 CA ILE A 36 7989 5547 5445 -3744 1081 -116 C ATOM 43 C ILE A 36 20.575 -32.930 5.761 1.00 50.76 C ANISOU 43 C ILE A 36 8038 5690 5559 -3790 1136 -56 C ATOM 44 O ILE A 36 19.571 -33.672 5.760 1.00 52.05 O ANISOU 44 O ILE A 36 8159 5864 5752 -3878 1147 -3 O ATOM 45 CB ILE A 36 21.344 -33.172 3.398 1.00 49.92 C ANISOU 45 CB ILE A 36 7916 5591 5461 -3763 1057 -138 C ATOM 46 CG1 ILE A 36 22.448 -33.631 2.455 1.00 49.41 C ANISOU 46 CG1 ILE A 36 7904 5486 5385 -3733 1016 -194 C ATOM 47 CG2 ILE A 36 20.944 -31.754 3.059 1.00 49.16 C ANISOU 47 CG2 ILE A 36 7737 5569 5371 -3716 1077 -149 C ATOM 48 CD1 ILE A 36 23.710 -32.903 2.624 1.00 48.16 C ANISOU 48 CD1 ILE A 36 7784 5307 5207 -3636 1015 -238 C ATOM 49 N PRO A 37 20.640 -31.831 6.514 1.00 54.38 N ANISOU 49 N PRO A 37 8491 6169 6000 -3735 1177 -60 N ATOM 50 CA PRO A 37 19.516 -31.425 7.366 1.00 58.27 C ANISOU 50 CA PRO A 37 8926 6702 6511 -3772 1248 -2 C ATOM 51 C PRO A 37 18.210 -31.312 6.603 1.00 61.88 C ANISOU 51 C PRO A 37 9249 7227 7034 -3824 1267 38 C ATOM 52 O PRO A 37 18.137 -30.656 5.565 1.00 64.89 O ANISOU 52 O PRO A 37 9566 7648 7442 -3792 1241 10 O ATOM 53 CB PRO A 37 19.958 -30.060 7.888 1.00 51.68 C ANISOU 53 CB PRO A 37 8102 5879 5654 -3688 1279 -34 C ATOM 54 CG PRO A 37 21.420 -30.137 7.903 1.00 48.96 C ANISOU 54 CG PRO A 37 7862 5477 5264 -3627 1225 -87 C ATOM 55 CD PRO A 37 21.859 -31.067 6.817 1.00 48.86 C ANISOU 55 CD PRO A 37 7858 5443 5265 -3643 1164 -109 C ATOM 56 N ASP A 38 17.165 -31.930 7.150 1.00 60.85 N ANISOU 56 N ASP A 38 9075 7111 6934 -3908 1311 112 N ATOM 57 CA ASP A 38 15.849 -31.891 6.527 1.00 63.03 C ANISOU 57 CA ASP A 38 9211 7451 7288 -3966 1331 168 C ATOM 58 C ASP A 38 15.384 -30.449 6.366 1.00 58.53 C ANISOU 58 C ASP A 38 8536 6940 6762 -3907 1374 171 C ATOM 59 O ASP A 38 15.446 -29.658 7.307 1.00 57.82 O ANISOU 59 O ASP A 38 8456 6855 6658 -3861 1440 176 O ATOM 60 CB ASP A 38 14.870 -32.668 7.395 1.00 71.19 C ANISOU 60 CB ASP A 38 10212 8490 8347 -4060 1390 258 C ATOM 61 CG ASP A 38 15.516 -33.883 8.023 1.00 84.84 C ANISOU 61 CG ASP A 38 12072 10144 10019 -4103 1362 259 C ATOM 62 OD1 ASP A 38 15.772 -34.850 7.270 1.00 88.17 O ANISOU 62 OD1 ASP A 38 12529 10528 10443 -4143 1290 243 O ATOM 63 OD2 ASP A 38 15.817 -33.846 9.253 1.00 89.67 O ANISOU 63 OD2 ASP A 38 12760 10730 10582 -4094 1408 274 O ATOM 64 N LEU A 39 14.945 -30.094 5.168 1.00 57.05 N ANISOU 64 N LEU A 39 8255 6795 6629 -3909 1335 170 N ATOM 65 CA LEU A 39 14.369 -28.776 4.953 1.00 60.04 C ANISOU 65 CA LEU A 39 8516 7226 7070 -3862 1372 190 C ATOM 66 C LEU A 39 12.933 -28.760 5.450 1.00 67.66 C ANISOU 66 C LEU A 39 9342 8240 8126 -3921 1456 294 C ATOM 67 O LEU A 39 12.213 -29.747 5.325 1.00 80.20 O ANISOU 67 O LEU A 39 10888 9837 9748 -4011 1452 350 O ATOM 68 CB LEU A 39 14.446 -28.406 3.478 1.00 52.62 C ANISOU 68 CB LEU A 39 7530 6310 6155 -3848 1294 159 C ATOM 69 CG LEU A 39 14.285 -26.937 3.099 1.00 52.88 C ANISOU 69 CG LEU A 39 7476 6378 6238 -3779 1304 158 C ATOM 70 CD1 LEU A 39 15.293 -26.005 3.743 1.00 50.54 C ANISOU 70 CD1 LEU A 39 7263 6053 5887 -3684 1324 100 C ATOM 71 CD2 LEU A 39 14.413 -26.855 1.614 1.00 53.74 C ANISOU 71 CD2 LEU A 39 7563 6505 6351 -3786 1216 132 C ATOM 72 N LEU A 40 12.505 -27.647 6.028 1.00 64.09 N ANISOU 72 N LEU A 40 8814 7820 7717 -3871 1538 325 N ATOM 73 CA LEU A 40 11.293 -27.691 6.843 1.00 63.92 C ANISOU 73 CA LEU A 40 8677 7843 7764 -3918 1650 428 C ATOM 74 C LEU A 40 10.372 -26.518 6.538 1.00 72.95 C ANISOU 74 C LEU A 40 9646 9046 9024 -3883 1705 488 C ATOM 75 O LEU A 40 10.458 -25.474 7.184 1.00 75.96 O ANISOU 75 O LEU A 40 10017 9438 9405 -3814 1779 486 O ATOM 76 CB LEU A 40 11.673 -27.720 8.308 1.00 62.71 C ANISOU 76 CB LEU A 40 8627 7667 7532 -3902 1734 425 C ATOM 77 CG LEU A 40 10.756 -28.591 9.138 1.00 58.69 C ANISOU 77 CG LEU A 40 8074 7183 7042 -3989 1820 520 C ATOM 78 CD1 LEU A 40 10.870 -30.036 8.651 1.00 59.19 C ANISOU 78 CD1 LEU A 40 8192 7209 7087 -4077 1732 519 C ATOM 79 CD2 LEU A 40 11.163 -28.442 10.595 1.00 58.83 C ANISOU 79 CD2 LEU A 40 8203 7182 6968 -3967 1908 516 C ATOM 80 N THR A 41 9.463 -26.711 5.593 1.00 76.89 N ANISOU 80 N THR A 41 10005 9582 9627 -3936 1673 546 N ATOM 81 CA THR A 41 8.390 -25.749 5.423 1.00 84.65 C ANISOU 81 CA THR A 41 10793 10622 10747 -3918 1739 632 C ATOM 82 C THR A 41 7.207 -26.110 6.310 1.00 95.22 C ANISOU 82 C THR A 41 12008 12012 12160 -3972 1870 749 C ATOM 83 O THR A 41 7.164 -27.155 6.968 1.00 97.54 O ANISOU 83 O THR A 41 12367 12295 12399 -4036 1898 767 O ATOM 84 CB THR A 41 7.920 -25.675 3.979 1.00 84.76 C ANISOU 84 CB THR A 41 10700 10651 10853 -3949 1643 649 C ATOM 85 OG1 THR A 41 7.295 -26.923 3.624 1.00 88.18 O ANISOU 85 OG1 THR A 41 11101 11089 11313 -4058 1610 694 O ATOM 86 CG2 THR A 41 9.062 -25.348 3.061 1.00 84.02 C ANISOU 86 CG2 THR A 41 10727 10519 10677 -3900 1524 541 C ATOM 87 N THR A 42 6.213 -25.236 6.281 1.00102.16 N ANISOU 87 N THR A 42 12697 12948 13172 -3948 1951 837 N ATOM 88 CA THR A 42 5.027 -25.345 7.106 1.00105.16 C ANISOU 88 CA THR A 42 12925 13393 13638 -3982 2100 962 C ATOM 89 C THR A 42 4.071 -26.411 6.564 1.00109.63 C ANISOU 89 C THR A 42 13378 13975 14302 -4096 2074 1041 C ATOM 90 O THR A 42 4.233 -26.928 5.452 1.00109.24 O ANISOU 90 O THR A 42 13353 13890 14262 -4144 1939 1001 O ATOM 91 CB THR A 42 4.364 -23.964 7.198 1.00 99.22 C ANISOU 91 CB THR A 42 12012 12706 12982 -3929 2203 1015 C ATOM 92 OG1 THR A 42 3.638 -23.651 6.001 1.00 97.38 O ANISOU 92 OG1 THR A 42 11602 12485 12914 -3945 2138 1069 O ATOM 93 CG2 THR A 42 5.433 -22.944 7.357 1.00 92.10 C ANISOU 93 CG2 THR A 42 11250 11772 11973 -3847 2186 904 C ATOM 94 N ASP A 43 3.089 -26.764 7.392 1.00114.87 N ANISOU 94 N ASP A 43 13926 14693 15027 -4141 2209 1153 N ATOM 95 CA ASP A 43 2.034 -27.694 7.022 1.00121.46 C ANISOU 95 CA ASP A 43 14628 15547 15976 -4252 2211 1246 C ATOM 96 C ASP A 43 0.785 -26.901 6.609 1.00121.56 C ANISOU 96 C ASP A 43 14370 15620 16199 -4239 2284 1358 C ATOM 97 O ASP A 43 0.882 -25.727 6.221 1.00123.25 O ANISOU 97 O ASP A 43 14522 15845 16463 -4157 2278 1342 O ATOM 98 CB ASP A 43 1.779 -28.689 8.182 1.00127.55 C ANISOU 98 CB ASP A 43 15446 16333 16684 -4322 2312 1302 C ATOM 99 CG ASP A 43 1.225 -28.019 9.453 1.00131.56 C ANISOU 99 CG ASP A 43 15862 16922 17202 -4268 2514 1390 C ATOM 100 OD1 ASP A 43 0.007 -27.748 9.519 1.00134.58 O ANISOU 100 OD1 ASP A 43 16024 17384 17725 -4298 2632 1506 O ATOM 101 OD2 ASP A 43 2.005 -27.780 10.400 1.00130.81 O ANISOU 101 OD2 ASP A 43 15928 16823 16953 -4221 2565 1329 O ATOM 102 N ALA A 44 -0.390 -27.547 6.670 1.00124.06 N ANISOU 102 N ALA A 44 14521 15972 16646 -4328 2353 1472 N ATOM 103 CA ALA A 44 -1.650 -26.876 6.347 1.00115.87 C ANISOU 103 CA ALA A 44 13210 14993 15824 -4332 2440 1581 C ATOM 104 C ALA A 44 -1.863 -25.650 7.231 1.00111.78 C ANISOU 104 C ALA A 44 12614 14577 15280 -4272 2613 1611 C ATOM 105 O ALA A 44 -2.270 -24.589 6.749 1.00108.80 O ANISOU 105 O ALA A 44 12089 14238 15011 -4240 2633 1629 O ATOM 106 CB ALA A 44 -2.817 -27.856 6.485 1.00110.56 C ANISOU 106 CB ALA A 44 12385 14338 15283 -4442 2511 1694 C ATOM 107 N ARG A 45 -1.597 -25.780 8.532 1.00111.83 N ANISOU 107 N ARG A 45 12723 14630 15137 -4262 2741 1611 N ATOM 108 CA ARG A 45 -1.516 -24.638 9.435 1.00109.79 C ANISOU 108 CA ARG A 45 12463 14462 14789 -4197 2900 1593 C ATOM 109 C ARG A 45 -0.082 -24.128 9.412 1.00106.91 C ANISOU 109 C ARG A 45 12342 14023 14255 -4119 2799 1440 C ATOM 110 O ARG A 45 0.831 -24.812 9.891 1.00106.81 O ANISOU 110 O ARG A 45 12546 13946 14090 -4117 2747 1369 O ATOM 111 CB ARG A 45 -1.917 -25.043 10.847 1.00110.56 C ANISOU 111 CB ARG A 45 12571 14643 14793 -4229 3094 1652 C ATOM 112 CG ARG A 45 -2.884 -26.201 10.915 1.00115.85 C ANISOU 112 CG ARG A 45 13113 15328 15578 -4328 3132 1780 C ATOM 113 CD ARG A 45 -3.070 -26.614 12.357 1.00121.52 C ANISOU 113 CD ARG A 45 13886 16119 16165 -4356 3313 1825 C ATOM 114 NE ARG A 45 -3.761 -25.586 13.126 1.00127.81 N ANISOU 114 NE ARG A 45 14540 17067 16956 -4316 3539 1870 N ATOM 115 CZ ARG A 45 -3.560 -25.370 14.423 1.00132.04 C ANISOU 115 CZ ARG A 45 15187 17673 17309 -4295 3710 1839 C ATOM 116 NH1 ARG A 45 -4.225 -24.410 15.059 1.00135.01 N ANISOU 116 NH1 ARG A 45 15426 18196 17677 -4251 3927 1864 N ATOM 117 NH2 ARG A 45 -2.684 -26.112 15.085 1.00132.62 N ANISOU 117 NH2 ARG A 45 15513 17670 17206 -4315 3666 1776 N ATOM 118 N ASN A 46 0.131 -22.930 8.858 1.00105.81 N ANISOU 118 N ASN A 46 12165 13889 14150 -4057 2771 1390 N ATOM 119 CA ASN A 46 1.500 -22.456 8.668 1.00102.03 C ANISOU 119 CA ASN A 46 11906 13327 13535 -3987 2659 1248 C ATOM 120 C ASN A 46 2.211 -22.299 10.005 1.00 96.85 C ANISOU 120 C ASN A 46 11443 12675 12679 -3956 2774 1168 C ATOM 121 O ASN A 46 2.440 -21.184 10.482 1.00 98.33 O ANISOU 121 O ASN A 46 11666 12891 12804 -3904 2877 1104 O ATOM 122 CB ASN A 46 1.547 -21.149 7.875 1.00102.70 C ANISOU 122 CB ASN A 46 11909 13415 13697 -3935 2620 1217 C ATOM 123 CG ASN A 46 0.559 -20.131 8.381 1.00104.06 C ANISOU 123 CG ASN A 46 11885 13707 13946 -3930 2815 1280 C ATOM 124 OD1 ASN A 46 0.155 -20.163 9.542 1.00106.96 O ANISOU 124 OD1 ASN A 46 12242 14156 14244 -3937 3004 1302 O ATOM 125 ND2 ASN A 46 0.187 -19.194 7.521 1.00101.90 N ANISOU 125 ND2 ASN A 46 11458 13450 13810 -3914 2778 1301 N ATOM 126 N ARG A 47 2.560 -23.423 10.619 1.00 92.13 N ANISOU 126 N ARG A 47 10980 12041 11984 -3994 2761 1164 N ATOM 127 CA ARG A 47 3.357 -23.384 11.830 1.00 90.86 C ANISOU 127 CA ARG A 47 11031 11862 11631 -3972 2842 1081 C ATOM 128 C ARG A 47 4.286 -24.590 11.852 1.00 86.22 C ANISOU 128 C ARG A 47 10631 11174 10954 -3995 2699 1036 C ATOM 129 O ARG A 47 3.869 -25.712 11.552 1.00 85.58 O ANISOU 129 O ARG A 47 10497 11082 10940 -4058 2641 1109 O ATOM 130 CB ARG A 47 2.459 -23.298 13.070 1.00 97.48 C ANISOU 130 CB ARG A 47 11797 12811 12432 -4004 3081 1151 C ATOM 131 CG ARG A 47 1.393 -24.372 13.171 1.00103.08 C ANISOU 131 CG ARG A 47 12354 13576 13235 -4089 3127 1295 C ATOM 132 CD ARG A 47 0.138 -23.850 13.889 1.00106.34 C ANISOU 132 CD ARG A 47 12569 14139 13697 -4102 3370 1392 C ATOM 133 NE ARG A 47 0.419 -22.802 14.871 1.00106.86 N ANISOU 133 NE ARG A 47 12729 14252 13621 -4040 3543 1302 N ATOM 134 CZ ARG A 47 0.879 -23.027 16.099 1.00107.64 C ANISOU 134 CZ ARG A 47 13020 14345 13535 -4044 3648 1251 C ATOM 135 NH1 ARG A 47 1.073 -24.269 16.508 1.00111.27 N ANISOU 135 NH1 ARG A 47 13581 14763 13934 -4112 3595 1294 N ATOM 136 NH2 ARG A 47 1.110 -22.018 16.930 1.00104.70 N ANISOU 136 NH2 ARG A 47 12740 14002 13039 -3983 3811 1157 N ATOM 137 N ILE A 48 5.559 -24.326 12.144 1.00 82.68 N ANISOU 137 N ILE A 48 10399 10649 10368 -3944 2637 912 N ATOM 138 CA ILE A 48 6.620 -25.324 12.183 1.00 78.15 C ANISOU 138 CA ILE A 48 10012 9978 9704 -3950 2501 852 C ATOM 139 C ILE A 48 6.754 -25.795 13.621 1.00 75.93 C ANISOU 139 C ILE A 48 9864 9702 9285 -3992 2618 856 C ATOM 140 O ILE A 48 6.626 -25.000 14.561 1.00 74.49 O ANISOU 140 O ILE A 48 9720 9564 9020 -3978 2774 834 O ATOM 141 CB ILE A 48 7.948 -24.737 11.637 1.00 73.76 C ANISOU 141 CB ILE A 48 9597 9337 9090 -3870 2366 724 C ATOM 142 CG1 ILE A 48 7.772 -24.184 10.216 1.00 68.07 C ANISOU 142 CG1 ILE A 48 8745 8619 8499 -3831 2261 726 C ATOM 143 CG2 ILE A 48 9.100 -25.755 11.656 1.00 71.77 C ANISOU 143 CG2 ILE A 48 9525 8992 8752 -3868 2230 661 C ATOM 144 CD1 ILE A 48 7.688 -22.690 10.167 1.00 64.94 C ANISOU 144 CD1 ILE A 48 8302 8254 8119 -3779 2331 693 C ATOM 145 N GLN A 49 6.988 -27.092 13.796 1.00 78.17 N ANISOU 145 N GLN A 49 10222 9939 9539 -4047 2547 882 N ATOM 146 CA GLN A 49 7.095 -27.709 15.112 1.00 85.64 C ANISOU 146 CA GLN A 49 11297 10883 10359 -4102 2639 901 C ATOM 147 C GLN A 49 8.527 -28.164 15.352 1.00 81.15 C ANISOU 147 C GLN A 49 10959 10203 9671 -4083 2512 801 C ATOM 148 O GLN A 49 9.086 -28.921 14.554 1.00 81.00 O ANISOU 148 O GLN A 49 10971 10116 9688 -4083 2354 775 O ATOM 149 CB GLN A 49 6.131 -28.886 15.241 1.00100.81 C ANISOU 149 CB GLN A 49 13112 12842 12348 -4197 2675 1029 C ATOM 150 CG GLN A 49 6.491 -29.847 16.370 1.00113.18 C ANISOU 150 CG GLN A 49 14842 14373 13787 -4264 2704 1046 C ATOM 151 CD GLN A 49 5.871 -31.241 16.196 1.00120.45 C ANISOU 151 CD GLN A 49 15696 15287 14783 -4362 2668 1150 C ATOM 152 OE1 GLN A 49 4.978 -31.445 15.363 1.00120.22 O ANISOU 152 OE1 GLN A 49 15489 15296 14892 -4402 2658 1216 O ATOM 153 NE2 GLN A 49 6.359 -32.208 16.976 1.00124.08 N ANISOU 153 NE2 GLN A 49 16318 15693 15134 -4431 2649 1153 N ATOM 154 N LEU A 50 9.109 -27.718 16.460 1.00 79.84 N ANISOU 154 N LEU A 50 10959 10019 9358 -4074 2591 743 N ATOM 155 CA LEU A 50 10.498 -28.008 16.796 1.00 77.26 C ANISOU 155 CA LEU A 50 10852 9586 8916 -4056 2481 650 C ATOM 156 C LEU A 50 10.547 -28.578 18.198 1.00 74.49 C ANISOU 156 C LEU A 50 10645 9228 8429 -4128 2573 681 C ATOM 157 O LEU A 50 10.139 -27.908 19.151 1.00 75.87 O ANISOU 157 O LEU A 50 10852 9455 8520 -4140 2739 686 O ATOM 158 CB LEU A 50 11.378 -26.754 16.744 1.00 75.24 C ANISOU 158 CB LEU A 50 10692 9292 8604 -3972 2465 533 C ATOM 159 CG LEU A 50 11.702 -25.995 15.466 1.00 68.46 C ANISOU 159 CG LEU A 50 9750 8421 7842 -3890 2360 476 C ATOM 160 CD1 LEU A 50 12.767 -24.966 15.791 1.00 60.93 C ANISOU 160 CD1 LEU A 50 8951 7408 6792 -3829 2350 362 C ATOM 161 CD2 LEU A 50 12.142 -26.950 14.367 1.00 69.57 C ANISOU 161 CD2 LEU A 50 9859 8514 8061 -3878 2181 479 C ATOM 162 N THR A 51 11.082 -29.782 18.337 1.00 72.27 N ANISOU 162 N THR A 51 10460 8878 8119 -4176 2469 698 N ATOM 163 CA THR A 51 11.203 -30.407 19.645 1.00 75.22 C ANISOU 163 CA THR A 51 10986 9234 8362 -4253 2534 734 C ATOM 164 C THR A 51 12.674 -30.521 20.015 1.00 70.83 C ANISOU 164 C THR A 51 10652 8565 7695 -4231 2417 642 C ATOM 165 O THR A 51 13.492 -30.956 19.194 1.00 66.37 O ANISOU 165 O THR A 51 10104 7930 7184 -4190 2254 598 O ATOM 166 CB THR A 51 10.536 -31.779 19.662 1.00 76.86 C ANISOU 166 CB THR A 51 11126 9453 8623 -4345 2523 848 C ATOM 167 OG1 THR A 51 11.454 -32.753 19.157 1.00 80.27 O ANISOU 167 OG1 THR A 51 11640 9782 9075 -4346 2342 819 O ATOM 168 CG2 THR A 51 9.292 -31.760 18.784 1.00 73.88 C ANISOU 168 CG2 THR A 51 10503 9162 8407 -4351 2566 928 C ATOM 169 N ILE A 52 12.997 -30.149 21.260 1.00 71.41 N ANISOU 169 N ILE A 52 10896 8623 7612 -4258 2506 618 N ATOM 170 CA ILE A 52 14.373 -30.015 21.744 1.00 69.88 C ANISOU 170 CA ILE A 52 10923 8325 7304 -4238 2411 532 C ATOM 171 C ILE A 52 14.790 -31.241 22.555 1.00 66.41 C ANISOU 171 C ILE A 52 10630 7823 6779 -4325 2358 585 C ATOM 172 O ILE A 52 14.840 -31.188 23.787 1.00 67.91 O ANISOU 172 O ILE A 52 10975 8005 6823 -4384 2443 600 O ATOM 173 CB ILE A 52 14.532 -28.740 22.599 1.00 65.80 C ANISOU 173 CB ILE A 52 10526 7814 6661 -4216 2534 464 C ATOM 174 CG1 ILE A 52 14.077 -27.501 21.821 1.00 64.98 C ANISOU 174 CG1 ILE A 52 10275 7768 6646 -4134 2595 417 C ATOM 175 CG2 ILE A 52 15.972 -28.570 23.055 1.00 64.62 C ANISOU 175 CG2 ILE A 52 10603 7550 6400 -4199 2423 379 C ATOM 176 CD1 ILE A 52 14.219 -26.188 22.600 1.00 68.20 C ANISOU 176 CD1 ILE A 52 10803 8174 6937 -4107 2724 342 C ATOM 177 N GLY A 53 15.143 -32.341 21.887 1.00 68.35 N ANISOU 177 N GLY A 53 10843 8017 7108 -4333 2215 611 N ATOM 178 CA GLY A 53 15.369 -33.594 22.572 1.00 70.26 C ANISOU 178 CA GLY A 53 11198 8205 7294 -4423 2168 679 C ATOM 179 C GLY A 53 16.838 -33.935 22.773 1.00 71.85 C ANISOU 179 C GLY A 53 11580 8287 7432 -4403 2017 624 C ATOM 180 O GLY A 53 17.734 -33.249 22.299 1.00 75.18 O ANISOU 180 O GLY A 53 12032 8670 7864 -4314 1939 532 O ATOM 181 N ALA A 54 17.063 -35.023 23.512 1.00 72.03 N ANISOU 181 N ALA A 54 11722 8254 7392 -4490 1977 691 N ATOM 182 CA ALA A 54 18.361 -35.663 23.652 1.00 69.89 C ANISOU 182 CA ALA A 54 11598 7866 7089 -4482 1820 670 C ATOM 183 C ALA A 54 18.294 -37.032 23.004 1.00 73.89 C ANISOU 183 C ALA A 54 12031 8333 7711 -4510 1724 731 C ATOM 184 O ALA A 54 17.287 -37.400 22.392 1.00 80.18 O ANISOU 184 O ALA A 54 12678 9188 8597 -4543 1772 774 O ATOM 185 CB ALA A 54 18.775 -35.752 25.114 1.00 68.97 C ANISOU 185 CB ALA A 54 11709 7702 6796 -4565 1841 698 C ATOM 186 N GLY A 55 19.373 -37.780 23.109 1.00 72.77 N ANISOU 186 N GLY A 55 12003 8084 7560 -4507 1589 730 N ATOM 187 CA GLY A 55 19.444 -39.066 22.445 1.00 69.81 C ANISOU 187 CA GLY A 55 11606 7654 7265 -4558 1496 762 C ATOM 188 C GLY A 55 20.885 -39.402 22.138 1.00 66.37 C ANISOU 188 C GLY A 55 11263 7109 6846 -4498 1344 712 C ATOM 189 O GLY A 55 21.805 -38.845 22.730 1.00 65.56 O ANISOU 189 O GLY A 55 11268 6965 6678 -4446 1304 681 O ATOM 190 N GLN A 56 21.087 -40.306 21.193 1.00 66.24 N ANISOU 190 N GLN A 56 11200 7045 6924 -4504 1260 707 N ATOM 191 CA GLN A 56 22.422 -40.841 21.015 1.00 74.61 C ANISOU 191 CA GLN A 56 12347 7991 8011 -4459 1123 685 C ATOM 192 C GLN A 56 22.926 -40.663 19.590 1.00 72.57 C ANISOU 192 C GLN A 56 11990 7730 7852 -4367 1069 598 C ATOM 193 O GLN A 56 22.177 -40.750 18.611 1.00 69.28 O ANISOU 193 O GLN A 56 11452 7370 7502 -4376 1103 578 O ATOM 194 CB GLN A 56 22.476 -42.314 21.420 1.00 85.38 C ANISOU 194 CB GLN A 56 13791 9260 9389 -4557 1055 774 C ATOM 195 CG GLN A 56 23.795 -42.653 22.094 1.00 93.37 C ANISOU 195 CG GLN A 56 14951 10153 10374 -4532 940 791 C ATOM 196 CD GLN A 56 23.638 -43.611 23.246 1.00102.01 C ANISOU 196 CD GLN A 56 16172 11182 11404 -4647 916 902 C ATOM 197 OE1 GLN A 56 22.594 -44.267 23.380 1.00108.01 O ANISOU 197 OE1 GLN A 56 16903 11972 12164 -4750 974 971 O ATOM 198 NE2 GLN A 56 24.648 -43.651 24.132 1.00101.78 N ANISOU 198 NE2 GLN A 56 16286 11066 11318 -4634 832 928 N ATOM 199 N SER A 57 24.222 -40.402 19.495 1.00 74.00 N ANISOU 199 N SER A 57 12226 7846 8044 -4280 984 551 N ATOM 200 CA SER A 57 24.909 -40.346 18.221 1.00 73.04 C ANISOU 200 CA SER A 57 12030 7706 8016 -4192 927 478 C ATOM 201 C SER A 57 26.226 -41.084 18.387 1.00 72.13 C ANISOU 201 C SER A 57 12002 7460 7946 -4163 809 494 C ATOM 202 O SER A 57 26.636 -41.403 19.505 1.00 76.56 O ANISOU 202 O SER A 57 12681 7953 8454 -4200 767 553 O ATOM 203 CB SER A 57 25.108 -38.898 17.766 1.00 72.49 C ANISOU 203 CB SER A 57 11895 7715 7932 -4092 968 394 C ATOM 204 OG SER A 57 23.863 -38.208 17.754 1.00 71.92 O ANISOU 204 OG SER A 57 11744 7753 7828 -4121 1078 390 O ATOM 205 N THR A 58 26.866 -41.404 17.268 1.00 67.38 N ANISOU 205 N THR A 58 11339 6816 7448 -4103 754 445 N ATOM 206 CA THR A 58 28.064 -42.229 17.284 1.00 68.80 C ANISOU 206 CA THR A 58 11575 6859 7708 -4074 646 462 C ATOM 207 C THR A 58 29.183 -41.554 16.529 1.00 67.95 C ANISOU 207 C THR A 58 11414 6738 7666 -3953 611 387 C ATOM 208 O THR A 58 29.050 -41.281 15.334 1.00 69.70 O ANISOU 208 O THR A 58 11534 7011 7937 -3910 642 322 O ATOM 209 CB THR A 58 27.855 -43.587 16.638 1.00 72.46 C ANISOU 209 CB THR A 58 12019 7247 8268 -4128 609 486 C ATOM 210 OG1 THR A 58 26.875 -44.336 17.369 1.00 77.23 O ANISOU 210 OG1 THR A 58 12674 7848 8820 -4250 631 568 O ATOM 211 CG2 THR A 58 29.193 -44.322 16.609 1.00 71.25 C ANISOU 211 CG2 THR A 58 11909 6941 8221 -4080 500 493 C ATOM 212 N PHE A 59 30.305 -41.361 17.202 1.00 69.42 N ANISOU 212 N PHE A 59 11669 6849 7859 -3905 540 402 N ATOM 213 CA PHE A 59 31.464 -40.734 16.591 1.00 70.45 C ANISOU 213 CA PHE A 59 11746 6957 8064 -3794 501 343 C ATOM 214 C PHE A 59 32.615 -41.724 16.621 1.00 77.48 C ANISOU 214 C PHE A 59 12664 7690 9085 -3771 394 370 C ATOM 215 O PHE A 59 33.058 -42.138 17.702 1.00 86.34 O ANISOU 215 O PHE A 59 13889 8725 10192 -3801 324 437 O ATOM 216 CB PHE A 59 31.800 -39.436 17.312 1.00 65.78 C ANISOU 216 CB PHE A 59 11193 6419 7381 -3749 512 331 C ATOM 217 CG PHE A 59 30.601 -38.588 17.566 1.00 62.01 C ANISOU 217 CG PHE A 59 10709 6071 6780 -3786 616 316 C ATOM 218 CD1 PHE A 59 29.958 -37.963 16.516 1.00 59.43 C ANISOU 218 CD1 PHE A 59 10270 5848 6462 -3756 691 252 C ATOM 219 CD2 PHE A 59 30.102 -38.433 18.853 1.00 63.94 C ANISOU 219 CD2 PHE A 59 11059 6328 6907 -3853 640 368 C ATOM 220 CE1 PHE A 59 28.833 -37.196 16.738 1.00 62.81 C ANISOU 220 CE1 PHE A 59 10678 6384 6803 -3788 786 240 C ATOM 221 CE2 PHE A 59 28.978 -37.659 19.091 1.00 64.78 C ANISOU 221 CE2 PHE A 59 11148 6546 6921 -3886 747 352 C ATOM 222 CZ PHE A 59 28.337 -37.044 18.033 1.00 65.00 C ANISOU 222 CZ PHE A 59 11051 6670 6977 -3851 819 289 C ATOM 223 N GLY A 60 33.074 -42.111 15.432 1.00 78.21 N ANISOU 223 N GLY A 60 12667 7742 9309 -3721 382 318 N ATOM 224 CA GLY A 60 34.100 -43.117 15.285 1.00 80.83 C ANISOU 224 CA GLY A 60 13002 7912 9796 -3696 292 331 C ATOM 225 C GLY A 60 33.788 -44.317 16.140 1.00 79.95 C ANISOU 225 C GLY A 60 12990 7704 9683 -3787 242 415 C ATOM 226 O GLY A 60 34.571 -44.679 17.021 1.00 80.50 O ANISOU 226 O GLY A 60 13136 7663 9788 -3785 154 470 O ATOM 227 N GLY A 61 32.614 -44.897 15.935 1.00 80.70 N ANISOU 227 N GLY A 61 13090 7843 9729 -3874 292 434 N ATOM 228 CA GLY A 61 32.266 -46.103 16.647 1.00 84.28 C ANISOU 228 CA GLY A 61 13632 8202 10186 -3969 246 517 C ATOM 229 C GLY A 61 32.127 -46.003 18.156 1.00 87.93 C ANISOU 229 C GLY A 61 14221 8662 10528 -4030 219 604 C ATOM 230 O GLY A 61 31.920 -47.035 18.807 1.00 96.51 O ANISOU 230 O GLY A 61 15392 9660 11617 -4113 171 683 O ATOM 231 N LYS A 62 32.233 -44.821 18.753 1.00 82.30 N ANISOU 231 N LYS A 62 13532 8035 9704 -3998 246 595 N ATOM 232 CA LYS A 62 31.980 -44.707 20.184 1.00 82.68 C ANISOU 232 CA LYS A 62 13710 8088 9615 -4068 232 674 C ATOM 233 C LYS A 62 30.686 -43.932 20.374 1.00 80.21 C ANISOU 233 C LYS A 62 13385 7935 9157 -4121 355 663 C ATOM 234 O LYS A 62 30.464 -42.910 19.712 1.00 79.53 O ANISOU 234 O LYS A 62 13210 7956 9053 -4060 427 587 O ATOM 235 CB LYS A 62 33.149 -44.047 20.926 1.00 80.70 C ANISOU 235 CB LYS A 62 13523 7788 9350 -4004 154 682 C ATOM 236 CG LYS A 62 34.510 -44.690 20.637 1.00 76.65 C ANISOU 236 CG LYS A 62 12991 7117 9015 -3935 36 683 C ATOM 237 CD LYS A 62 35.585 -44.266 21.618 1.00 75.19 C ANISOU 237 CD LYS A 62 12894 6864 8812 -3900 -63 720 C ATOM 238 CE LYS A 62 35.190 -44.644 23.043 1.00 82.33 C ANISOU 238 CE LYS A 62 13966 7744 9572 -4007 -103 820 C ATOM 239 NZ LYS A 62 36.248 -44.309 24.060 1.00 87.86 N ANISOU 239 NZ LYS A 62 14771 8368 10245 -3985 -219 866 N ATOM 240 N THR A 63 29.821 -44.434 21.250 1.00 80.77 N ANISOU 240 N THR A 63 13539 8017 9135 -4234 382 740 N ATOM 241 CA THR A 63 28.488 -43.873 21.396 1.00 79.48 C ANISOU 241 CA THR A 63 13345 7991 8862 -4294 508 736 C ATOM 242 C THR A 63 28.515 -42.747 22.422 1.00 81.08 C ANISOU 242 C THR A 63 13626 8256 8927 -4286 547 736 C ATOM 243 O THR A 63 29.067 -42.897 23.520 1.00 81.65 O ANISOU 243 O THR A 63 13830 8258 8934 -4315 482 794 O ATOM 244 CB THR A 63 27.465 -44.946 21.780 1.00 82.58 C ANISOU 244 CB THR A 63 13772 8372 9232 -4425 533 820 C ATOM 245 OG1 THR A 63 26.156 -44.461 21.462 1.00 80.07 O ANISOU 245 OG1 THR A 63 13365 8190 8868 -4465 661 801 O ATOM 246 CG2 THR A 63 27.540 -45.348 23.295 1.00 88.37 C ANISOU 246 CG2 THR A 63 14670 9048 9860 -4513 495 922 C ATOM 247 N ALA A 64 27.944 -41.610 22.040 1.00 79.04 N ANISOU 247 N ALA A 64 13285 8120 8626 -4246 649 668 N ATOM 248 CA ALA A 64 27.884 -40.436 22.884 1.00 79.17 C ANISOU 248 CA ALA A 64 13362 8198 8520 -4232 702 652 C ATOM 249 C ALA A 64 26.448 -39.948 22.964 1.00 73.36 C ANISOU 249 C ALA A 64 12568 7585 7719 -4287 848 647 C ATOM 250 O ALA A 64 25.621 -40.191 22.078 1.00 62.51 O ANISOU 250 O ALA A 64 11073 6269 6410 -4302 904 631 O ATOM 251 CB ALA A 64 28.791 -39.317 22.365 1.00 60.36 C ANISOU 251 CB ALA A 64 10936 5832 6167 -4109 676 567 C ATOM 252 N THR A 65 26.167 -39.261 24.062 1.00 71.66 N ANISOU 252 N THR A 65 12443 7405 7378 -4318 908 666 N ATOM 253 CA THR A 65 24.880 -38.624 24.279 1.00 72.45 C ANISOU 253 CA THR A 65 12505 7619 7405 -4372 1061 659 C ATOM 254 C THR A 65 24.918 -37.241 23.662 1.00 69.35 C ANISOU 254 C THR A 65 12026 7299 7025 -4272 1114 560 C ATOM 255 O THR A 65 25.797 -36.440 23.994 1.00 69.92 O ANISOU 255 O THR A 65 12190 7342 7033 -4226 1073 512 O ATOM 256 CB THR A 65 24.565 -38.507 25.770 1.00 75.15 C ANISOU 256 CB THR A 65 13038 7959 7557 -4493 1117 710 C ATOM 257 OG1 THR A 65 24.494 -39.815 26.355 1.00 79.78 O ANISOU 257 OG1 THR A 65 13706 8478 8128 -4594 1064 812 O ATOM 258 CG2 THR A 65 23.241 -37.773 25.973 1.00 76.63 C ANISOU 258 CG2 THR A 65 13168 8266 7682 -4538 1295 700 C ATOM 259 N THR A 66 23.978 -36.969 22.760 1.00 71.98 N ANISOU 259 N THR A 66 12186 7721 7441 -4244 1197 534 N ATOM 260 CA THR A 66 23.906 -35.699 22.054 1.00 59.64 C ANISOU 260 CA THR A 66 10525 6229 5907 -4152 1246 446 C ATOM 261 C THR A 66 22.472 -35.192 22.092 1.00 62.78 C ANISOU 261 C THR A 66 10833 6732 6287 -4197 1396 455 C ATOM 262 O THR A 66 21.548 -35.925 22.446 1.00 66.00 O ANISOU 262 O THR A 66 11224 7166 6688 -4290 1457 531 O ATOM 263 CB THR A 66 24.365 -35.839 20.609 1.00 58.22 C ANISOU 263 CB THR A 66 10234 6044 5842 -4081 1176 388 C ATOM 264 OG1 THR A 66 23.304 -36.415 19.834 1.00 58.77 O ANISOU 264 OG1 THR A 66 10182 6167 5981 -4129 1224 408 O ATOM 265 CG2 THR A 66 25.614 -36.719 20.516 1.00 58.11 C ANISOU 265 CG2 THR A 66 10293 5919 5865 -4063 1040 402 C ATOM 266 N TRP A 67 22.294 -33.915 21.757 1.00 59.38 N ANISOU 266 N TRP A 67 10347 6362 5853 -4134 1460 385 N ATOM 267 CA TRP A 67 20.983 -33.274 21.717 1.00 67.64 C ANISOU 267 CA TRP A 67 11291 7509 6901 -4160 1606 390 C ATOM 268 C TRP A 67 20.623 -32.910 20.284 1.00 67.31 C ANISOU 268 C TRP A 67 11046 7524 7005 -4073 1596 353 C ATOM 269 O TRP A 67 21.403 -33.133 19.365 1.00 74.25 O ANISOU 269 O TRP A 67 11903 8366 7942 -4021 1491 307 O ATOM 270 CB TRP A 67 20.950 -32.027 22.596 1.00 67.97 C ANISOU 270 CB TRP A 67 11445 7570 6812 -4170 1705 343 C ATOM 271 CG TRP A 67 21.187 -32.263 24.075 1.00 73.00 C ANISOU 271 CG TRP A 67 12299 8156 7281 -4266 1732 378 C ATOM 272 CD1 TRP A 67 21.425 -33.457 24.709 1.00 72.35 C ANISOU 272 CD1 TRP A 67 12318 8016 7154 -4346 1671 454 C ATOM 273 CD2 TRP A 67 21.195 -31.264 25.097 1.00 72.83 C ANISOU 273 CD2 TRP A 67 12431 8134 7109 -4295 1826 341 C ATOM 274 NE1 TRP A 67 21.591 -33.246 26.051 1.00 69.38 N ANISOU 274 NE1 TRP A 67 12148 7607 6605 -4424 1715 469 N ATOM 275 CE2 TRP A 67 21.460 -31.907 26.311 1.00 69.75 C ANISOU 275 CE2 TRP A 67 12235 7687 6581 -4393 1813 397 C ATOM 276 CE3 TRP A 67 21.010 -29.882 25.097 1.00 75.43 C ANISOU 276 CE3 TRP A 67 12759 8496 7405 -4249 1921 266 C ATOM 277 CZ2 TRP A 67 21.549 -31.214 27.510 1.00 72.87 C ANISOU 277 CZ2 TRP A 67 12827 8061 6800 -4446 1890 377 C ATOM 278 CZ3 TRP A 67 21.095 -29.202 26.289 1.00 74.87 C ANISOU 278 CZ3 TRP A 67 12883 8399 7165 -4298 2004 242 C ATOM 279 CH2 TRP A 67 21.359 -29.868 27.476 1.00 74.12 C ANISOU 279 CH2 TRP A 67 12983 8250 6927 -4396 1989 296 C ATOM 280 N GLY A 68 19.443 -32.329 20.093 1.00 64.41 N ANISOU 280 N GLY A 68 10559 7247 6667 -4086 1715 365 N ATOM 281 CA GLY A 68 19.061 -31.919 18.752 1.00 68.00 C ANISOU 281 CA GLY A 68 10842 7754 7239 -4024 1703 330 C ATOM 282 C GLY A 68 17.663 -31.341 18.671 1.00 72.68 C ANISOU 282 C GLY A 68 11287 8447 7880 -4038 1836 372 C ATOM 283 O GLY A 68 16.793 -31.626 19.503 1.00 78.23 O ANISOU 283 O GLY A 68 11997 9189 8536 -4123 1946 442 O ATOM 284 N TYR A 69 17.459 -30.535 17.621 1.00 73.12 N ANISOU 284 N TYR A 69 11219 8547 8016 -3971 1831 324 N ATOM 285 CA TYR A 69 16.138 -30.055 17.229 1.00 67.05 C ANISOU 285 CA TYR A 69 10275 7872 7328 -3978 1934 370 C ATOM 286 C TYR A 69 15.522 -31.052 16.252 1.00 71.47 C ANISOU 286 C TYR A 69 10727 8454 7976 -4039 1887 410 C ATOM 287 O TYR A 69 16.148 -31.408 15.244 1.00 66.43 O ANISOU 287 O TYR A 69 10093 7779 7369 -4019 1772 357 O ATOM 288 CB TYR A 69 16.232 -28.660 16.616 1.00 62.55 C ANISOU 288 CB TYR A 69 9638 7331 6796 -3886 1945 304 C ATOM 289 CG TYR A 69 16.795 -27.635 17.580 1.00 62.54 C ANISOU 289 CG TYR A 69 9790 7302 6670 -3873 2010 239 C ATOM 290 CD1 TYR A 69 18.163 -27.487 17.760 1.00 60.73 C ANISOU 290 CD1 TYR A 69 9711 6990 6372 -3831 1912 167 C ATOM 291 CD2 TYR A 69 15.960 -26.826 18.322 1.00 65.88 C ANISOU 291 CD2 TYR A 69 10206 7781 7044 -3904 2176 253 C ATOM 292 CE1 TYR A 69 18.680 -26.545 18.625 1.00 62.87 C ANISOU 292 CE1 TYR A 69 10133 7226 6528 -3827 1965 108 C ATOM 293 CE2 TYR A 69 16.469 -25.894 19.204 1.00 70.16 C ANISOU 293 CE2 TYR A 69 10906 8288 7465 -3896 2241 186 C ATOM 294 CZ TYR A 69 17.829 -25.755 19.355 1.00 71.13 C ANISOU 294 CZ TYR A 69 11188 8318 7518 -3862 2129 113 C ATOM 295 OH TYR A 69 18.319 -24.813 20.239 1.00 77.84 O ANISOU 295 OH TYR A 69 12207 9123 8245 -3863 2191 49 O ATOM 296 N ASN A 70 14.305 -31.513 16.568 1.00 76.93 N ANISOU 296 N ASN A 70 11324 9205 8702 -4117 1981 507 N ATOM 297 CA ASN A 70 13.664 -32.612 15.855 1.00 61.78 C ANISOU 297 CA ASN A 70 9320 7297 6856 -4199 1941 561 C ATOM 298 C ASN A 70 14.670 -33.677 15.474 1.00 61.13 C ANISOU 298 C ASN A 70 9357 7124 6746 -4221 1802 518 C ATOM 299 O ASN A 70 14.653 -34.162 14.344 1.00 72.97 O ANISOU 299 O ASN A 70 10802 8615 8309 -4233 1722 499 O ATOM 300 CB ASN A 70 12.956 -32.111 14.609 1.00 61.38 C ANISOU 300 CB ASN A 70 9094 7308 6922 -4173 1934 558 C ATOM 301 CG ASN A 70 11.943 -31.057 14.925 1.00 65.89 C ANISOU 301 CG ASN A 70 9529 7969 7540 -4144 2072 610 C ATOM 302 OD1 ASN A 70 11.486 -30.929 16.066 1.00 63.44 O ANISOU 302 OD1 ASN A 70 9230 7692 7182 -4165 2195 671 O ATOM 303 ND2 ASN A 70 11.591 -30.273 13.922 1.00 66.23 N ANISOU 303 ND2 ASN A 70 9440 8053 7672 -4092 2057 592 N ATOM 304 N GLY A 71 15.555 -34.040 16.389 1.00 61.10 N ANISOU 304 N GLY A 71 9516 7049 6649 -4227 1774 507 N ATOM 305 CA GLY A 71 16.542 -35.026 16.012 1.00 60.55 C ANISOU 305 CA GLY A 71 9548 6892 6566 -4238 1646 474 C ATOM 306 C GLY A 71 17.385 -35.463 17.183 1.00 76.41 C ANISOU 306 C GLY A 71 11730 8824 8478 -4257 1622 487 C ATOM 307 O GLY A 71 17.259 -34.953 18.297 1.00 61.48 O ANISOU 307 O GLY A 71 9896 6948 6516 -4261 1702 513 O ATOM 308 N ASN A 72 18.216 -36.471 16.904 1.00 72.54 N ANISOU 308 N ASN A 72 11322 8248 7989 -4273 1510 476 N ATOM 309 CA ASN A 72 19.348 -36.826 17.743 1.00 73.07 C ANISOU 309 CA ASN A 72 11555 8226 7984 -4265 1446 473 C ATOM 310 C ASN A 72 20.414 -35.757 17.770 1.00 69.27 C ANISOU 310 C ASN A 72 11128 7726 7466 -4156 1414 391 C ATOM 311 O ASN A 72 21.183 -35.698 18.733 1.00 66.49 O ANISOU 311 O ASN A 72 10907 7316 7038 -4148 1388 397 O ATOM 312 CB ASN A 72 19.993 -38.105 17.236 1.00 76.84 C ANISOU 312 CB ASN A 72 12080 8615 8500 -4294 1333 480 C ATOM 313 CG ASN A 72 19.561 -39.294 18.009 1.00 87.68 C ANISOU 313 CG ASN A 72 13515 9946 9853 -4409 1336 577 C ATOM 314 OD1 ASN A 72 18.749 -39.189 18.940 1.00 89.85 O ANISOU 314 OD1 ASN A 72 13794 10266 10079 -4473 1429 644 O ATOM 315 ND2 ASN A 72 20.121 -40.449 17.663 1.00 93.06 N ANISOU 315 ND2 ASN A 72 14247 10537 10573 -4438 1237 591 N ATOM 316 N LEU A 73 20.502 -34.947 16.715 1.00 78.92 N ANISOU 316 N LEU A 73 12255 8990 8740 -4076 1405 320 N ATOM 317 CA LEU A 73 21.643 -34.063 16.515 1.00 78.66 C ANISOU 317 CA LEU A 73 12266 8932 8690 -3972 1354 242 C ATOM 318 C LEU A 73 21.238 -32.893 15.626 1.00 70.51 C ANISOU 318 C LEU A 73 11111 7977 7703 -3905 1394 186 C ATOM 319 O LEU A 73 20.527 -33.088 14.637 1.00 68.01 O ANISOU 319 O LEU A 73 10677 7707 7455 -3921 1401 188 O ATOM 320 CB LEU A 73 22.816 -34.839 15.907 1.00 55.05 C ANISOU 320 CB LEU A 73 9323 5862 5730 -3942 1236 216 C ATOM 321 CG LEU A 73 24.176 -34.168 15.981 1.00 53.69 C ANISOU 321 CG LEU A 73 9219 5645 5536 -3848 1174 163 C ATOM 322 CD1 LEU A 73 24.243 -33.407 17.261 1.00 53.91 C ANISOU 322 CD1 LEU A 73 9337 5669 5476 -3848 1217 175 C ATOM 323 CD2 LEU A 73 25.290 -35.197 15.910 1.00 53.79 C ANISOU 323 CD2 LEU A 73 9303 5558 5576 -3843 1071 176 C ATOM 324 N LEU A 74 21.610 -31.682 16.046 1.00 53.70 N ANISOU 324 N LEU A 74 9012 5858 5535 -3838 1422 146 N ATOM 325 CA LEU A 74 21.831 -30.531 15.185 1.00 52.22 C ANISOU 325 CA LEU A 74 8750 5708 5384 -3750 1416 78 C ATOM 326 C LEU A 74 20.619 -29.889 14.519 1.00 64.55 C ANISOU 326 C LEU A 74 10160 7356 7010 -3750 1490 84 C ATOM 327 O LEU A 74 20.778 -28.809 13.958 1.00 70.21 O ANISOU 327 O LEU A 74 10824 8100 7752 -3678 1490 36 O ATOM 328 CB LEU A 74 22.840 -30.895 14.081 1.00 53.21 C ANISOU 328 CB LEU A 74 8870 5800 5548 -3700 1312 32 C ATOM 329 CG LEU A 74 24.353 -30.635 14.222 1.00 50.04 C ANISOU 329 CG LEU A 74 8560 5333 5118 -3629 1234 -8 C ATOM 330 CD1 LEU A 74 25.032 -30.563 12.876 1.00 48.89 C ANISOU 330 CD1 LEU A 74 8353 5194 5030 -3566 1173 -57 C ATOM 331 CD2 LEU A 74 24.695 -29.416 15.058 1.00 49.52 C ANISOU 331 CD2 LEU A 74 8554 5264 4995 -3582 1262 -30 C ATOM 332 N GLY A 75 19.433 -30.490 14.504 1.00 63.38 N ANISOU 332 N GLY A 75 9930 7252 6899 -3827 1547 148 N ATOM 333 CA GLY A 75 18.280 -29.806 13.927 1.00 59.56 C ANISOU 333 CA GLY A 75 9291 6851 6489 -3823 1617 167 C ATOM 334 C GLY A 75 18.213 -29.628 12.418 1.00 53.05 C ANISOU 334 C GLY A 75 8360 6056 5739 -3791 1556 131 C ATOM 335 O GLY A 75 19.082 -30.047 11.646 1.00 52.16 O ANISOU 335 O GLY A 75 8287 5907 5624 -3766 1462 84 O ATOM 336 N PRO A 76 17.155 -28.946 11.963 1.00 53.37 N ANISOU 336 N PRO A 76 8258 6168 5852 -3788 1615 160 N ATOM 337 CA PRO A 76 16.859 -28.899 10.517 1.00 52.91 C ANISOU 337 CA PRO A 76 8090 6145 5868 -3781 1559 145 C ATOM 338 C PRO A 76 16.971 -27.519 9.893 1.00 51.73 C ANISOU 338 C PRO A 76 7876 6025 5753 -3698 1557 104 C ATOM 339 O PRO A 76 17.195 -26.545 10.600 1.00 51.45 O ANISOU 339 O PRO A 76 7871 5984 5693 -3645 1606 88 O ATOM 340 CB PRO A 76 15.378 -29.348 10.482 1.00 54.61 C ANISOU 340 CB PRO A 76 8173 6420 6157 -3864 1625 238 C ATOM 341 CG PRO A 76 14.861 -28.720 11.751 1.00 55.42 C ANISOU 341 CG PRO A 76 8268 6547 6240 -3859 1748 284 C ATOM 342 CD PRO A 76 15.979 -28.505 12.727 1.00 54.67 C ANISOU 342 CD PRO A 76 8340 6390 6043 -3817 1742 232 C ATOM 343 N ALA A 77 16.749 -27.415 8.597 1.00 51.34 N ANISOU 343 N ALA A 77 7739 6007 5762 -3692 1502 93 N ATOM 344 CA ALA A 77 16.746 -26.137 7.912 1.00 50.40 C ANISOU 344 CA ALA A 77 7547 5918 5686 -3624 1494 67 C ATOM 345 C ALA A 77 15.316 -25.652 7.735 1.00 51.47 C ANISOU 345 C ALA A 77 7515 6119 5921 -3652 1562 145 C ATOM 346 O ALA A 77 14.503 -26.318 7.096 1.00 54.99 O ANISOU 346 O ALA A 77 7871 6597 6425 -3717 1547 194 O ATOM 347 CB ALA A 77 17.448 -26.252 6.569 1.00 53.61 C ANISOU 347 CB ALA A 77 7965 6318 6087 -3600 1392 12 C ATOM 348 N VAL A 78 15.024 -24.487 8.283 1.00 52.08 N ANISOU 348 N VAL A 78 7547 6214 6026 -3602 1637 160 N ATOM 349 CA VAL A 78 13.674 -23.962 8.332 1.00 55.61 C ANISOU 349 CA VAL A 78 7828 6725 6576 -3618 1725 248 C ATOM 350 C VAL A 78 13.512 -23.037 7.136 1.00 59.27 C ANISOU 350 C VAL A 78 8187 7212 7122 -3577 1671 244 C ATOM 351 O VAL A 78 13.960 -21.893 7.174 1.00 64.13 O ANISOU 351 O VAL A 78 8817 7813 7738 -3504 1674 209 O ATOM 352 CB VAL A 78 13.427 -23.212 9.638 1.00 53.07 C ANISOU 352 CB VAL A 78 7517 6412 6236 -3585 1852 274 C ATOM 353 CG1 VAL A 78 11.992 -22.767 9.687 1.00 54.64 C ANISOU 353 CG1 VAL A 78 7534 6689 6538 -3612 1964 371 C ATOM 354 CG2 VAL A 78 13.816 -24.056 10.827 1.00 53.60 C ANISOU 354 CG2 VAL A 78 7722 6445 6200 -3623 1890 268 C ATOM 355 N LYS A 79 12.877 -23.510 6.068 1.00 59.37 N ANISOU 355 N LYS A 79 8098 7257 7204 -3628 1617 281 N ATOM 356 CA LYS A 79 12.636 -22.632 4.926 1.00 59.51 C ANISOU 356 CA LYS A 79 8012 7297 7303 -3598 1564 289 C ATOM 357 C LYS A 79 11.619 -21.573 5.332 1.00 62.79 C ANISOU 357 C LYS A 79 8273 7754 7831 -3571 1664 372 C ATOM 358 O LYS A 79 10.469 -21.894 5.648 1.00 70.01 O ANISOU 358 O LYS A 79 9061 8715 8825 -3620 1743 465 O ATOM 359 CB LYS A 79 12.154 -23.416 3.703 1.00 59.05 C ANISOU 359 CB LYS A 79 7888 7261 7286 -3669 1482 313 C ATOM 360 CG LYS A 79 12.392 -22.688 2.365 1.00 59.95 C ANISOU 360 CG LYS A 79 7965 7382 7432 -3640 1390 288 C ATOM 361 CD LYS A 79 11.669 -23.308 1.151 1.00 67.87 C ANISOU 361 CD LYS A 79 8882 8414 8490 -3718 1319 328 C ATOM 362 CE LYS A 79 10.259 -22.706 0.950 1.00 77.09 C ANISOU 362 CE LYS A 79 9841 9627 9822 -3742 1362 437 C ATOM 363 NZ LYS A 79 9.461 -23.178 -0.255 1.00 79.28 N ANISOU 363 NZ LYS A 79 10020 9931 10172 -3824 1288 483 N ATOM 364 N LEU A 80 12.048 -20.315 5.357 1.00 59.34 N ANISOU 364 N LEU A 80 7844 7301 7404 -3494 1669 343 N ATOM 365 CA LEU A 80 11.151 -19.178 5.505 1.00 64.70 C ANISOU 365 CA LEU A 80 8384 8021 8178 -3486 1761 404 C ATOM 366 C LEU A 80 11.054 -18.415 4.196 1.00 72.25 C ANISOU 366 C LEU A 80 9243 8978 9231 -3461 1666 419 C ATOM 367 O LEU A 80 11.932 -18.495 3.336 1.00 74.60 O ANISOU 367 O LEU A 80 9618 9240 9488 -3433 1543 360 O ATOM 368 CB LEU A 80 11.602 -18.216 6.609 1.00 62.82 C ANISOU 368 CB LEU A 80 8254 7766 7851 -3463 1872 339 C ATOM 369 CG LEU A 80 11.774 -18.784 8.013 1.00 63.90 C ANISOU 369 CG LEU A 80 8514 7894 7873 -3489 1978 314 C ATOM 370 CD1 LEU A 80 11.814 -17.659 9.014 1.00 53.97 C ANISOU 370 CD1 LEU A 80 7324 6631 6552 -3482 2125 264 C ATOM 371 CD2 LEU A 80 10.669 -19.795 8.344 1.00 55.12 C ANISOU 371 CD2 LEU A 80 7295 6841 6805 -3558 2049 409 C ATOM 372 N GLN A 81 9.974 -17.653 4.068 1.00 76.40 N ANISOU 372 N GLN A 81 9608 9554 9868 -3495 1740 490 N ATOM 373 CA GLN A 81 9.680 -16.894 2.862 1.00 75.26 C ANISOU 373 CA GLN A 81 9348 9411 9835 -3489 1657 523 C ATOM 374 C GLN A 81 9.426 -15.463 3.296 1.00 76.34 C ANISOU 374 C GLN A 81 9439 9562 10003 -3483 1759 521 C ATOM 375 O GLN A 81 8.577 -15.225 4.157 1.00 85.29 O ANISOU 375 O GLN A 81 10490 10749 11166 -3518 1917 561 O ATOM 376 CB GLN A 81 8.471 -17.485 2.129 1.00 79.73 C ANISOU 376 CB GLN A 81 9733 10021 10540 -3552 1636 626 C ATOM 377 CG GLN A 81 8.309 -16.985 0.715 1.00 86.07 C ANISOU 377 CG GLN A 81 10448 10812 11444 -3552 1516 649 C ATOM 378 CD GLN A 81 8.945 -17.927 -0.303 1.00 86.52 C ANISOU 378 CD GLN A 81 10605 10841 11429 -3565 1376 594 C ATOM 379 OE1 GLN A 81 8.997 -19.148 -0.082 1.00 89.41 O ANISOU 379 OE1 GLN A 81 11042 11216 11714 -3620 1378 572 O ATOM 380 NE2 GLN A 81 9.445 -17.364 -1.421 1.00 80.25 N ANISOU 380 NE2 GLN A 81 9839 10028 10626 -3552 1267 558 N ATOM 381 N ARG A 82 10.175 -14.523 2.734 1.00 74.08 N ANISOU 381 N ARG A 82 9209 9229 9708 -3438 1680 470 N ATOM 382 CA ARG A 82 10.115 -13.145 3.198 1.00 77.41 C ANISOU 382 CA ARG A 82 9622 9644 10147 -3432 1776 448 C ATOM 383 C ARG A 82 8.706 -12.584 3.108 1.00 86.00 C ANISOU 383 C ARG A 82 10489 10800 11388 -3487 1875 543 C ATOM 384 O ARG A 82 7.985 -12.827 2.137 1.00 89.29 O ANISOU 384 O ARG A 82 10750 11245 11931 -3520 1795 628 O ATOM 385 CB ARG A 82 11.047 -12.277 2.372 1.00 75.68 C ANISOU 385 CB ARG A 82 9472 9362 9922 -3385 1648 401 C ATOM 386 CG ARG A 82 11.029 -10.821 2.769 1.00 76.20 C ANISOU 386 CG ARG A 82 9539 9401 10014 -3386 1735 373 C ATOM 387 CD ARG A 82 11.954 -10.027 1.891 1.00 74.55 C ANISOU 387 CD ARG A 82 9394 9126 9805 -3344 1592 340 C ATOM 388 NE ARG A 82 12.356 -8.786 2.521 1.00 76.40 N ANISOU 388 NE ARG A 82 9712 9301 10016 -3335 1671 277 N ATOM 389 CZ ARG A 82 13.365 -8.047 2.087 1.00 80.06 C ANISOU 389 CZ ARG A 82 10275 9693 10450 -3293 1567 232 C ATOM 390 NH1 ARG A 82 14.057 -8.435 1.021 1.00 79.65 N ANISOU 390 NH1 ARG A 82 10241 9636 10385 -3252 1395 242 N ATOM 391 NH2 ARG A 82 13.679 -6.924 2.715 1.00 81.31 N ANISOU 391 NH2 ARG A 82 10518 9782 10594 -3293 1646 174 N ATOM 392 N GLY A 83 8.317 -11.832 4.139 1.00 92.33 N ANISOU 392 N GLY A 83 11275 11625 12181 -3497 2062 521 N ATOM 393 CA GLY A 83 7.047 -11.119 4.160 1.00 94.21 C ANISOU 393 CA GLY A 83 11292 11935 12568 -3538 2189 595 C ATOM 394 C GLY A 83 5.856 -11.984 4.517 1.00 93.68 C ANISOU 394 C GLY A 83 11060 11968 12565 -3584 2289 692 C ATOM 395 O GLY A 83 4.766 -11.488 4.830 1.00 95.99 O ANISOU 395 O GLY A 83 11162 12343 12968 -3610 2443 747 O ATOM 396 N LYS A 84 6.062 -13.290 4.447 1.00 90.08 N ANISOU 396 N LYS A 84 10670 11506 12052 -3592 2204 710 N ATOM 397 CA LYS A 84 5.066 -14.282 4.806 1.00 85.81 C ANISOU 397 CA LYS A 84 10004 11042 11558 -3639 2280 801 C ATOM 398 C LYS A 84 5.463 -14.881 6.150 1.00 82.38 C ANISOU 398 C LYS A 84 9731 10611 10959 -3628 2403 742 C ATOM 399 O LYS A 84 6.550 -15.451 6.291 1.00 79.84 O ANISOU 399 O LYS A 84 9614 10216 10506 -3601 2311 665 O ATOM 400 CB LYS A 84 4.967 -15.335 3.701 1.00 83.90 C ANISOU 400 CB LYS A 84 9722 10774 11384 -3666 2098 859 C ATOM 401 CG LYS A 84 4.736 -14.717 2.300 1.00 85.36 C ANISOU 401 CG LYS A 84 9786 10934 11714 -3675 1960 898 C ATOM 402 CD LYS A 84 3.582 -13.675 2.345 1.00 93.03 C ANISOU 402 CD LYS A 84 10516 11980 12852 -3708 2076 980 C ATOM 403 CE LYS A 84 2.861 -13.480 0.987 1.00 92.89 C ANISOU 403 CE LYS A 84 10308 11952 13033 -3751 1950 1062 C ATOM 404 NZ LYS A 84 1.550 -12.744 1.096 1.00 90.64 N ANISOU 404 NZ LYS A 84 9740 11757 12942 -3793 2070 1164 N ATOM 405 N ALA A 85 4.606 -14.707 7.140 1.00 80.66 N ANISOU 405 N ALA A 85 9421 10478 10749 -3646 2617 773 N ATOM 406 CA ALA A 85 4.961 -15.069 8.498 1.00 78.86 C ANISOU 406 CA ALA A 85 9355 10249 10357 -3634 2758 708 C ATOM 407 C ALA A 85 4.591 -16.517 8.787 1.00 80.82 C ANISOU 407 C ALA A 85 9592 10530 10587 -3682 2742 784 C ATOM 408 O ALA A 85 3.774 -17.127 8.091 1.00 81.99 O ANISOU 408 O ALA A 85 9565 10719 10868 -3727 2679 895 O ATOM 409 CB ALA A 85 4.273 -14.139 9.490 1.00 75.03 C ANISOU 409 CB ALA A 85 8799 9838 9870 -3616 3025 685 C ATOM 410 N VAL A 86 5.227 -17.068 9.827 1.00 83.05 N ANISOU 410 N VAL A 86 10070 10780 10705 -3677 2795 720 N ATOM 411 CA VAL A 86 4.956 -18.434 10.272 1.00 87.98 C ANISOU 411 CA VAL A 86 10708 11424 11294 -3727 2794 783 C ATOM 412 C VAL A 86 5.142 -18.542 11.781 1.00 90.78 C ANISOU 412 C VAL A 86 11211 11793 11489 -3728 2968 734 C ATOM 413 O VAL A 86 5.862 -17.761 12.400 1.00 90.23 O ANISOU 413 O VAL A 86 11302 11677 11306 -3685 3035 624 O ATOM 414 CB VAL A 86 5.844 -19.482 9.559 1.00 85.67 C ANISOU 414 CB VAL A 86 10537 11040 10975 -3731 2570 760 C ATOM 415 CG1 VAL A 86 5.314 -19.748 8.175 1.00 86.66 C ANISOU 415 CG1 VAL A 86 10495 11169 11264 -3752 2431 836 C ATOM 416 CG2 VAL A 86 7.262 -18.985 9.481 1.00 84.15 C ANISOU 416 CG2 VAL A 86 10553 10750 10671 -3670 2472 628 C ATOM 417 N THR A 87 4.498 -19.546 12.371 1.00 95.04 N ANISOU 417 N THR A 87 11704 12388 12018 -3783 3039 819 N ATOM 418 CA THR A 87 4.511 -19.750 13.811 1.00 95.88 C ANISOU 418 CA THR A 87 11933 12521 11975 -3795 3213 794 C ATOM 419 C THR A 87 5.314 -20.991 14.173 1.00 94.65 C ANISOU 419 C THR A 87 11964 12287 11711 -3832 3098 778 C ATOM 420 O THR A 87 5.293 -22.000 13.469 1.00 96.39 O ANISOU 420 O THR A 87 12142 12481 12003 -3869 2949 836 O ATOM 421 CB THR A 87 3.090 -19.859 14.357 1.00100.95 C ANISOU 421 CB THR A 87 12370 13304 12684 -3831 3417 910 C ATOM 422 OG1 THR A 87 2.282 -18.849 13.741 1.00102.39 O ANISOU 422 OG1 THR A 87 12330 13561 13014 -3801 3486 943 O ATOM 423 CG2 THR A 87 3.077 -19.656 15.865 1.00103.79 C ANISOU 423 CG2 THR A 87 12856 13702 12877 -3821 3640 863 C ATOM 424 N VAL A 88 6.040 -20.901 15.270 1.00 90.19 N ANISOU 424 N VAL A 88 11615 11679 10975 -3822 3170 694 N ATOM 425 CA VAL A 88 6.967 -21.935 15.673 1.00 88.95 C ANISOU 425 CA VAL A 88 11655 11436 10706 -3852 3057 662 C ATOM 426 C VAL A 88 6.617 -22.311 17.100 1.00 88.18 C ANISOU 426 C VAL A 88 11639 11384 10482 -3898 3235 690 C ATOM 427 O VAL A 88 6.681 -21.463 18.003 1.00 89.10 O ANISOU 427 O VAL A 88 11849 11516 10491 -3869 3397 626 O ATOM 428 CB VAL A 88 8.423 -21.468 15.559 1.00 90.03 C ANISOU 428 CB VAL A 88 12002 11453 10751 -3800 2931 527 C ATOM 429 CG1 VAL A 88 9.380 -22.637 15.745 1.00 91.30 C ANISOU 429 CG1 VAL A 88 12330 11529 10832 -3828 2786 505 C ATOM 430 CG2 VAL A 88 8.650 -20.792 14.210 1.00 86.60 C ANISOU 430 CG2 VAL A 88 11473 10994 10435 -3746 2799 500 C ATOM 431 N ASP A 89 6.180 -23.552 17.288 1.00 86.57 N ANISOU 431 N ASP A 89 11394 11204 10293 -3969 3217 788 N ATOM 432 CA ASP A 89 6.025 -24.129 18.609 1.00 86.23 C ANISOU 432 CA ASP A 89 11459 11187 10116 -4024 3348 820 C ATOM 433 C ASP A 89 7.331 -24.807 18.954 1.00 81.37 C ANISOU 433 C ASP A 89 11093 10447 9378 -4042 3203 747 C ATOM 434 O ASP A 89 7.851 -25.604 18.169 1.00 78.84 O ANISOU 434 O ASP A 89 10782 10056 9117 -4052 3011 749 O ATOM 435 CB ASP A 89 4.884 -25.137 18.643 1.00 93.79 C ANISOU 435 CB ASP A 89 12244 12231 11161 -4102 3403 972 C ATOM 436 CG ASP A 89 3.618 -24.588 18.051 1.00100.65 C ANISOU 436 CG ASP A 89 12834 13217 12192 -4088 3504 1058 C ATOM 437 OD1 ASP A 89 3.201 -23.476 18.444 1.00103.47 O ANISOU 437 OD1 ASP A 89 13137 13650 12529 -4038 3678 1028 O ATOM 438 OD2 ASP A 89 3.068 -25.253 17.149 1.00102.14 O ANISOU 438 OD2 ASP A 89 12860 13415 12534 -4126 3404 1150 O ATOM 439 N ILE A 90 7.867 -24.469 20.112 1.00 78.55 N ANISOU 439 N ILE A 90 10935 10060 8849 -4041 3296 680 N ATOM 440 CA ILE A 90 9.139 -24.987 20.577 1.00 76.34 C ANISOU 440 CA ILE A 90 10901 9661 8444 -4059 3171 611 C ATOM 441 C ILE A 90 8.855 -25.781 21.840 1.00 75.08 C ANISOU 441 C ILE A 90 10841 9528 8159 -4141 3279 676 C ATOM 442 O ILE A 90 8.316 -25.234 22.816 1.00 78.09 O ANISOU 442 O ILE A 90 11250 9977 8442 -4145 3483 682 O ATOM 443 CB ILE A 90 10.149 -23.855 20.828 1.00 75.48 C ANISOU 443 CB ILE A 90 10969 9472 8236 -3995 3163 474 C ATOM 444 CG1 ILE A 90 10.275 -22.947 19.596 1.00 66.41 C ANISOU 444 CG1 ILE A 90 9702 8314 7216 -3917 3084 422 C ATOM 445 CG2 ILE A 90 11.501 -24.407 21.267 1.00 71.94 C ANISOU 445 CG2 ILE A 90 10763 8899 7670 -4016 3020 411 C ATOM 446 CD1 ILE A 90 10.748 -21.548 19.930 1.00 66.00 C ANISOU 446 CD1 ILE A 90 9762 8224 7089 -3857 3164 311 C ATOM 447 N TYR A 91 9.192 -27.067 21.806 1.00 73.39 N ANISOU 447 N TYR A 91 10678 9260 7947 -4204 3150 725 N ATOM 448 CA TYR A 91 8.935 -28.006 22.884 1.00 78.23 C ANISOU 448 CA TYR A 91 11378 9889 8456 -4296 3222 803 C ATOM 449 C TYR A 91 10.253 -28.533 23.426 1.00 75.86 C ANISOU 449 C TYR A 91 11335 9461 8027 -4323 3089 741 C ATOM 450 O TYR A 91 11.083 -29.020 22.655 1.00 74.66 O ANISOU 450 O TYR A 91 11212 9221 7936 -4304 2894 703 O ATOM 451 CB TYR A 91 8.077 -29.171 22.391 1.00 85.56 C ANISOU 451 CB TYR A 91 12133 10864 9512 -4364 3191 934 C ATOM 452 CG TYR A 91 6.732 -28.782 21.808 1.00 94.17 C ANISOU 452 CG TYR A 91 12952 12078 10749 -4349 3306 1017 C ATOM 453 CD1 TYR A 91 5.629 -28.531 22.641 1.00 99.03 C ANISOU 453 CD1 TYR A 91 13477 12822 11329 -4378 3538 1100 C ATOM 454 CD2 TYR A 91 6.551 -28.682 20.428 1.00 96.53 C ANISOU 454 CD2 TYR A 91 13082 12372 11223 -4308 3187 1018 C ATOM 455 CE1 TYR A 91 4.387 -28.187 22.110 1.00101.51 C ANISOU 455 CE1 TYR A 91 13525 13255 11790 -4366 3646 1185 C ATOM 456 CE2 TYR A 91 5.308 -28.336 19.884 1.00 99.16 C ANISOU 456 CE2 TYR A 91 13161 12815 11700 -4302 3284 1104 C ATOM 457 CZ TYR A 91 4.232 -28.089 20.729 1.00101.38 C ANISOU 457 CZ TYR A 91 13342 13222 11954 -4331 3512 1189 C ATOM 458 OH TYR A 91 3.006 -27.744 20.194 1.00101.54 O ANISOU 458 OH TYR A 91 13096 13354 12129 -4324 3609 1281 O ATOM 459 N ASN A 92 10.419 -28.488 24.751 1.00 76.46 N ANISOU 459 N ASN A 92 11593 9531 7926 -4368 3196 738 N ATOM 460 CA ASN A 92 11.708 -28.716 25.413 1.00 73.23 C ANISOU 460 CA ASN A 92 11450 9000 7376 -4390 3087 670 C ATOM 461 C ASN A 92 11.765 -30.025 26.210 1.00 74.73 C ANISOU 461 C ASN A 92 11748 9163 7484 -4499 3059 759 C ATOM 462 O ASN A 92 11.498 -30.027 27.406 1.00 78.59 O ANISOU 462 O ASN A 92 12356 9683 7823 -4556 3194 794 O ATOM 463 CB ASN A 92 12.001 -27.524 26.304 1.00 74.09 C ANISOU 463 CB ASN A 92 11720 9100 7331 -4356 3212 584 C ATOM 464 CG ASN A 92 13.238 -27.719 27.142 1.00 77.82 C ANISOU 464 CG ASN A 92 12478 9449 7642 -4392 3115 528 C ATOM 465 OD1 ASN A 92 14.116 -28.515 26.797 1.00 79.39 O ANISOU 465 OD1 ASN A 92 12740 9555 7869 -4411 2922 525 O ATOM 466 ND2 ASN A 92 13.337 -26.961 28.236 1.00 78.56 N ANISOU 466 ND2 ASN A 92 12747 9538 7565 -4397 3247 482 N ATOM 467 N GLN A 93 12.177 -31.124 25.576 1.00 83.75 N ANISOU 467 N GLN A 93 12868 10240 8714 -4526 2883 792 N ATOM 468 CA GLN A 93 12.274 -32.431 26.248 1.00 82.51 C ANISOU 468 CA GLN A 93 12813 10044 8494 -4632 2838 879 C ATOM 469 C GLN A 93 13.657 -32.741 26.815 1.00 76.20 C ANISOU 469 C GLN A 93 12267 9112 7572 -4651 2697 822 C ATOM 470 O GLN A 93 14.134 -33.887 26.735 1.00 74.09 O ANISOU 470 O GLN A 93 12053 8771 7326 -4701 2561 865 O ATOM 471 CB GLN A 93 11.823 -33.537 25.302 1.00 77.70 C ANISOU 471 CB GLN A 93 12035 9438 8051 -4660 2744 958 C ATOM 472 CG GLN A 93 10.311 -33.548 25.054 1.00 84.83 C ANISOU 472 CG GLN A 93 12705 10472 9054 -4685 2895 1059 C ATOM 473 CD GLN A 93 9.777 -32.262 24.428 1.00 92.63 C ANISOU 473 CD GLN A 93 13532 11542 10119 -4590 2986 1010 C ATOM 474 OE1 GLN A 93 10.449 -31.231 24.416 1.00 95.68 O ANISOU 474 OE1 GLN A 93 14003 11898 10454 -4514 2977 899 O ATOM 475 NE2 GLN A 93 8.558 -32.328 23.887 1.00 99.96 N ANISOU 475 NE2 GLN A 93 14227 12572 11182 -4600 3071 1097 N ATOM 476 N LEU A 94 14.307 -31.747 27.416 1.00 79.18 N ANISOU 476 N LEU A 94 12808 9455 7824 -4615 2728 732 N ATOM 477 CA LEU A 94 15.486 -31.953 28.242 1.00 84.85 C ANISOU 477 CA LEU A 94 13787 10058 8395 -4652 2626 697 C ATOM 478 C LEU A 94 15.081 -31.941 29.716 1.00 92.12 C ANISOU 478 C LEU A 94 14868 11011 9123 -4740 2777 750 C ATOM 479 O LEU A 94 14.046 -31.387 30.111 1.00 92.06 O ANISOU 479 O LEU A 94 14784 11115 9079 -4742 2981 777 O ATOM 480 CB LEU A 94 16.542 -30.874 27.976 1.00 71.69 C ANISOU 480 CB LEU A 94 12217 8318 6704 -4562 2548 566 C ATOM 481 CG LEU A 94 17.020 -30.614 26.534 1.00 70.98 C ANISOU 481 CG LEU A 94 11980 8204 6783 -4458 2415 498 C ATOM 482 CD1 LEU A 94 17.680 -29.254 26.432 1.00 67.53 C ANISOU 482 CD1 LEU A 94 11618 7733 6309 -4378 2414 381 C ATOM 483 CD2 LEU A 94 17.972 -31.695 25.996 1.00 67.61 C ANISOU 483 CD2 LEU A 94 11578 7688 6424 -4456 2207 510 C ATOM 484 N THR A 95 15.906 -32.581 30.541 1.00 92.99 N ANISOU 484 N THR A 95 15201 11026 9106 -4813 2678 770 N ATOM 485 CA THR A 95 15.702 -32.413 31.969 1.00 89.36 C ANISOU 485 CA THR A 95 14932 10583 8437 -4890 2808 802 C ATOM 486 C THR A 95 15.963 -30.967 32.392 1.00 91.80 C ANISOU 486 C THR A 95 15356 10888 8635 -4826 2903 692 C ATOM 487 O THR A 95 15.444 -30.527 33.420 1.00 93.69 O ANISOU 487 O THR A 95 15696 11184 8719 -4859 3078 706 O ATOM 488 CB THR A 95 16.593 -33.391 32.741 1.00 87.61 C ANISOU 488 CB THR A 95 14936 10249 8102 -4984 2659 850 C ATOM 489 OG1 THR A 95 17.869 -32.788 32.981 1.00 95.27 O ANISOU 489 OG1 THR A 95 16109 11102 8986 -4950 2534 754 O ATOM 490 CG2 THR A 95 16.806 -34.675 31.937 1.00 82.74 C ANISOU 490 CG2 THR A 95 14212 9586 7638 -5005 2493 913 C ATOM 491 N GLU A 96 16.722 -30.202 31.606 1.00 92.58 N ANISOU 491 N GLU A 96 15441 10925 8811 -4732 2800 583 N ATOM 492 CA GLU A 96 17.082 -28.839 31.970 1.00 91.13 C ANISOU 492 CA GLU A 96 15383 10713 8527 -4675 2868 475 C ATOM 493 C GLU A 96 16.503 -27.834 30.981 1.00 87.26 C ANISOU 493 C GLU A 96 14680 10297 8178 -4567 2958 413 C ATOM 494 O GLU A 96 16.060 -28.181 29.890 1.00 83.96 O ANISOU 494 O GLU A 96 14027 9931 7942 -4531 2921 442 O ATOM 495 CB GLU A 96 18.599 -28.680 32.043 1.00 90.96 C ANISOU 495 CB GLU A 96 15570 10540 8451 -4666 2665 402 C ATOM 496 CG GLU A 96 19.305 -28.828 30.733 1.00 88.33 C ANISOU 496 CG GLU A 96 15104 10160 8298 -4591 2482 360 C ATOM 497 CD GLU A 96 20.687 -28.193 30.784 1.00 88.97 C ANISOU 497 CD GLU A 96 15366 10118 8322 -4553 2334 268 C ATOM 498 OE1 GLU A 96 20.793 -26.936 30.846 1.00 85.04 O ANISOU 498 OE1 GLU A 96 14925 9607 7780 -4501 2404 180 O ATOM 499 OE2 GLU A 96 21.669 -28.970 30.776 1.00 90.95 O ANISOU 499 OE2 GLU A 96 15701 10282 8573 -4575 2146 291 O ATOM 500 N GLU A 97 16.532 -26.568 31.381 1.00 92.55 N ANISOU 500 N GLU A 97 15444 10963 8758 -4517 3073 327 N ATOM 501 CA GLU A 97 15.954 -25.470 30.623 1.00 96.20 C ANISOU 501 CA GLU A 97 15733 11492 9328 -4418 3182 266 C ATOM 502 C GLU A 97 16.919 -24.975 29.546 1.00 98.48 C ANISOU 502 C GLU A 97 15993 11693 9734 -4344 3004 178 C ATOM 503 O GLU A 97 18.128 -25.234 29.584 1.00 98.85 O ANISOU 503 O GLU A 97 16195 11622 9744 -4360 2820 145 O ATOM 504 CB GLU A 97 15.602 -24.327 31.565 1.00 97.86 C ANISOU 504 CB GLU A 97 16073 11728 9381 -4391 3388 209 C ATOM 505 CG GLU A 97 16.811 -23.859 32.318 1.00100.59 C ANISOU 505 CG GLU A 97 16727 11930 9562 -4408 3295 130 C ATOM 506 CD GLU A 97 16.465 -23.151 33.583 1.00107.73 C ANISOU 506 CD GLU A 97 17819 12854 10260 -4412 3489 102 C ATOM 507 OE1 GLU A 97 17.133 -23.429 34.602 1.00109.95 O ANISOU 507 OE1 GLU A 97 18362 13050 10363 -4483 3429 107 O ATOM 508 OE2 GLU A 97 15.525 -22.331 33.559 1.00111.01 O ANISOU 508 OE2 GLU A 97 18119 13372 10689 -4341 3700 75 O ATOM 509 N THR A 98 16.369 -24.220 28.592 1.00 96.92 N ANISOU 509 N THR A 98 15591 11557 9675 -4262 3065 144 N ATOM 510 CA THR A 98 17.106 -23.776 27.414 1.00 88.14 C ANISOU 510 CA THR A 98 14405 10388 8695 -4188 2910 75 C ATOM 511 C THR A 98 16.342 -22.653 26.714 1.00 85.16 C ANISOU 511 C THR A 98 13853 10085 8421 -4106 3036 35 C ATOM 512 O THR A 98 15.156 -22.427 26.974 1.00 83.94 O ANISOU 512 O THR A 98 13582 10041 8271 -4102 3231 77 O ATOM 513 CB THR A 98 17.338 -24.940 26.450 1.00 83.36 C ANISOU 513 CB THR A 98 13656 9784 8235 -4193 2732 131 C ATOM 514 OG1 THR A 98 18.367 -24.596 25.514 1.00 82.88 O ANISOU 514 OG1 THR A 98 13586 9650 8256 -4124 2560 59 O ATOM 515 CG2 THR A 98 16.052 -25.269 25.707 1.00 81.23 C ANISOU 515 CG2 THR A 98 13111 9639 8113 -4182 2816 207 C ATOM 516 N THR A 99 17.042 -21.955 25.814 1.00 81.56 N ANISOU 516 N THR A 99 13370 9570 8050 -4038 2923 -40 N ATOM 517 CA THR A 99 16.468 -20.902 24.981 1.00 73.84 C ANISOU 517 CA THR A 99 12223 8645 7187 -3960 3003 -78 C ATOM 518 C THR A 99 16.577 -21.282 23.513 1.00 67.35 C ANISOU 518 C THR A 99 11191 7844 6554 -3917 2843 -57 C ATOM 519 O THR A 99 17.035 -22.383 23.153 1.00 63.29 O ANISOU 519 O THR A 99 10656 7310 6082 -3940 2687 -16 O ATOM 520 CB THR A 99 17.167 -19.572 25.212 1.00 73.33 C ANISOU 520 CB THR A 99 12327 8490 7046 -3916 3025 -187 C ATOM 521 OG1 THR A 99 17.548 -19.498 26.586 1.00 79.04 O ANISOU 521 OG1 THR A 99 13317 9148 7568 -3965 3088 -211 O ATOM 522 CG2 THR A 99 16.217 -18.417 24.906 1.00 74.58 C ANISOU 522 CG2 THR A 99 12352 8719 7266 -3851 3209 -214 C ATOM 523 N LEU A 100 16.135 -20.347 22.664 1.00 64.71 N ANISOU 523 N LEU A 100 10704 7552 6332 -3852 2888 -85 N ATOM 524 CA LEU A 100 16.213 -20.530 21.218 1.00 66.50 C ANISOU 524 CA LEU A 100 10736 7799 6730 -3804 2741 -70 C ATOM 525 C LEU A 100 16.370 -19.163 20.560 1.00 66.19 C ANISOU 525 C LEU A 100 10660 7741 6750 -3733 2754 -142 C ATOM 526 O LEU A 100 15.377 -18.444 20.397 1.00 66.85 O ANISOU 526 O LEU A 100 10614 7896 6891 -3712 2902 -129 O ATOM 527 CB LEU A 100 14.986 -21.259 20.705 1.00 65.80 C ANISOU 527 CB LEU A 100 10414 7826 6762 -3823 2788 34 C ATOM 528 CG LEU A 100 15.219 -21.821 19.315 1.00 63.01 C ANISOU 528 CG LEU A 100 9906 7476 6558 -3788 2603 59 C ATOM 529 CD1 LEU A 100 14.601 -23.174 19.189 1.00 60.20 C ANISOU 529 CD1 LEU A 100 9446 7172 6256 -3841 2575 160 C ATOM 530 CD2 LEU A 100 14.593 -20.878 18.329 1.00 63.11 C ANISOU 530 CD2 LEU A 100 9736 7545 6699 -3732 2636 56 C ATOM 531 N HIS A 101 17.612 -18.833 20.170 1.00 64.35 N ANISOU 531 N HIS A 101 10530 7415 6505 -3697 2599 -210 N ATOM 532 CA HIS A 101 17.959 -17.567 19.525 1.00 65.34 C ANISOU 532 CA HIS A 101 10641 7504 6679 -3635 2581 -276 C ATOM 533 C HIS A 101 18.004 -17.759 18.018 1.00 60.54 C ANISOU 533 C HIS A 101 9829 6939 6236 -3581 2434 -248 C ATOM 534 O HIS A 101 18.675 -18.678 17.529 1.00 60.60 O ANISOU 534 O HIS A 101 9820 6935 6271 -3568 2272 -229 O ATOM 535 CB HIS A 101 19.308 -17.030 20.032 1.00 66.93 C ANISOU 535 CB HIS A 101 11082 7583 6763 -3628 2501 -359 C ATOM 536 CG HIS A 101 19.908 -15.927 19.198 1.00 65.70 C ANISOU 536 CG HIS A 101 10908 7385 6670 -3564 2427 -415 C ATOM 537 ND1 HIS A 101 19.169 -14.882 18.681 1.00 66.44 N ANISOU 537 ND1 HIS A 101 10887 7510 6847 -3533 2531 -427 N ATOM 538 CD2 HIS A 101 21.197 -15.666 18.866 1.00 63.98 C ANISOU 538 CD2 HIS A 101 10777 7096 6437 -3524 2266 -457 C ATOM 539 CE1 HIS A 101 19.967 -14.052 18.031 1.00 63.94 C ANISOU 539 CE1 HIS A 101 10590 7137 6565 -3484 2428 -473 C ATOM 540 NE2 HIS A 101 21.204 -14.503 18.133 1.00 63.28 N ANISOU 540 NE2 HIS A 101 10624 6998 6422 -3474 2268 -490 N ATOM 541 N TRP A 102 17.278 -16.891 17.299 1.00 60.77 N ANISOU 541 N TRP A 102 9704 7016 6370 -3547 2497 -243 N ATOM 542 CA TRP A 102 17.244 -16.863 15.833 1.00 60.36 C ANISOU 542 CA TRP A 102 9464 7002 6468 -3496 2366 -215 C ATOM 543 C TRP A 102 18.379 -15.965 15.349 1.00 60.37 C ANISOU 543 C TRP A 102 9545 6927 6464 -3439 2256 -286 C ATOM 544 O TRP A 102 18.213 -14.777 15.066 1.00 62.60 O ANISOU 544 O TRP A 102 9805 7196 6784 -3415 2308 -316 O ATOM 545 CB TRP A 102 15.876 -16.405 15.330 1.00 63.45 C ANISOU 545 CB TRP A 102 9648 7485 6976 -3497 2482 -159 C ATOM 546 CG TRP A 102 14.746 -17.282 15.838 1.00 68.51 C ANISOU 546 CG TRP A 102 10196 8211 7623 -3551 2596 -76 C ATOM 547 CD1 TRP A 102 13.999 -17.095 16.976 1.00 74.05 C ANISOU 547 CD1 TRP A 102 10940 8949 8248 -3587 2804 -67 C ATOM 548 CD2 TRP A 102 14.253 -18.487 15.236 1.00 66.37 C ANISOU 548 CD2 TRP A 102 9780 8000 7435 -3574 2513 12 C ATOM 549 NE1 TRP A 102 13.076 -18.109 17.114 1.00 73.69 N ANISOU 549 NE1 TRP A 102 10772 8991 8237 -3632 2850 29 N ATOM 550 CE2 TRP A 102 13.207 -18.973 16.059 1.00 70.33 C ANISOU 550 CE2 TRP A 102 10234 8574 7912 -3630 2671 80 C ATOM 551 CE3 TRP A 102 14.591 -19.202 14.089 1.00 62.37 C ANISOU 551 CE3 TRP A 102 9188 7493 7017 -3550 2329 41 C ATOM 552 CZ2 TRP A 102 12.504 -20.145 15.767 1.00 69.36 C ANISOU 552 CZ2 TRP A 102 9980 8514 7858 -3671 2639 179 C ATOM 553 CZ3 TRP A 102 13.893 -20.364 13.804 1.00 65.41 C ANISOU 553 CZ3 TRP A 102 9456 7932 7464 -3590 2304 129 C ATOM 554 CH2 TRP A 102 12.865 -20.824 14.643 1.00 67.87 C ANISOU 554 CH2 TRP A 102 9723 8308 7757 -3653 2453 199 C ATOM 555 N HIS A 103 19.564 -16.563 15.290 1.00 58.71 N ANISOU 555 N HIS A 103 9430 6669 6209 -3416 2104 -306 N ATOM 556 CA HIS A 103 20.803 -15.869 14.987 1.00 57.73 C ANISOU 556 CA HIS A 103 9394 6478 6063 -3361 1991 -362 C ATOM 557 C HIS A 103 20.769 -15.376 13.549 1.00 61.40 C ANISOU 557 C HIS A 103 9685 6982 6663 -3295 1900 -344 C ATOM 558 O HIS A 103 20.779 -16.183 12.601 1.00 61.85 O ANISOU 558 O HIS A 103 9612 7088 6801 -3264 1795 -299 O ATOM 559 CB HIS A 103 21.970 -16.819 15.213 1.00 53.73 C ANISOU 559 CB HIS A 103 8985 5935 5496 -3347 1859 -363 C ATOM 560 CG HIS A 103 23.297 -16.156 15.158 1.00 52.29 C ANISOU 560 CG HIS A 103 8905 5688 5274 -3293 1756 -407 C ATOM 561 ND1 HIS A 103 24.316 -16.470 16.028 1.00 53.18 N ANISOU 561 ND1 HIS A 103 9193 5736 5275 -3305 1705 -425 N ATOM 562 CD2 HIS A 103 23.768 -15.177 14.352 1.00 51.69 C ANISOU 562 CD2 HIS A 103 8776 5604 5258 -3228 1692 -425 C ATOM 563 CE1 HIS A 103 25.367 -15.723 15.746 1.00 54.79 C ANISOU 563 CE1 HIS A 103 9436 5903 5481 -3244 1612 -447 C ATOM 564 NE2 HIS A 103 25.062 -14.930 14.733 1.00 52.86 N ANISOU 564 NE2 HIS A 103 9055 5691 5338 -3197 1605 -448 N ATOM 565 N GLY A 104 20.733 -14.054 13.396 1.00 60.61 N ANISOU 565 N GLY A 104 9596 6851 6582 -3278 1943 -378 N ATOM 566 CA GLY A 104 20.686 -13.425 12.097 1.00 46.42 C ANISOU 566 CA GLY A 104 7650 5083 4906 -3225 1860 -358 C ATOM 567 C GLY A 104 19.353 -12.843 11.659 1.00 47.46 C ANISOU 567 C GLY A 104 7628 5266 5139 -3249 1965 -321 C ATOM 568 O GLY A 104 19.276 -12.342 10.540 1.00 46.75 O ANISOU 568 O GLY A 104 7412 5198 5152 -3213 1886 -295 O ATOM 569 N LEU A 105 18.311 -12.861 12.497 1.00 57.97 N ANISOU 569 N LEU A 105 8959 6621 6447 -3307 2144 -312 N ATOM 570 CA LEU A 105 16.969 -12.453 12.084 1.00 58.40 C ANISOU 570 CA LEU A 105 8831 6744 6612 -3327 2254 -259 C ATOM 571 C LEU A 105 16.594 -11.046 12.562 1.00 66.67 C ANISOU 571 C LEU A 105 9928 7746 7658 -3336 2420 -306 C ATOM 572 O LEU A 105 16.970 -10.606 13.656 1.00 71.58 O ANISOU 572 O LEU A 105 10745 8293 8160 -3351 2531 -376 O ATOM 573 CB LEU A 105 15.931 -13.446 12.599 1.00 52.91 C ANISOU 573 CB LEU A 105 8058 6130 5916 -3375 2360 -198 C ATOM 574 CG LEU A 105 15.518 -14.558 11.654 1.00 51.49 C ANISOU 574 CG LEU A 105 7709 6024 5829 -3375 2240 -113 C ATOM 575 CD1 LEU A 105 16.676 -15.447 11.433 1.00 53.51 C ANISOU 575 CD1 LEU A 105 8059 6239 6032 -3347 2072 -136 C ATOM 576 CD2 LEU A 105 14.405 -15.346 12.269 1.00 62.43 C ANISOU 576 CD2 LEU A 105 9017 7485 7217 -3429 2367 -47 C ATOM 577 N GLU A 106 15.806 -10.355 11.731 1.00 71.28 N ANISOU 577 N GLU A 106 10334 8370 8378 -3329 2446 -265 N ATOM 578 CA GLU A 106 15.311 -9.011 12.029 1.00 73.26 C ANISOU 578 CA GLU A 106 10593 8579 8663 -3334 2619 -303 C ATOM 579 C GLU A 106 13.884 -9.138 12.539 1.00 74.44 C ANISOU 579 C GLU A 106 10607 8823 8854 -3358 2844 -261 C ATOM 580 O GLU A 106 12.922 -9.063 11.773 1.00 77.67 O ANISOU 580 O GLU A 106 10787 9315 9408 -3362 2855 -186 O ATOM 581 CB GLU A 106 15.394 -8.117 10.803 1.00 75.68 C ANISOU 581 CB GLU A 106 10787 8864 9104 -3311 2503 -281 C ATOM 582 CG GLU A 106 16.822 -7.889 10.355 1.00 77.55 C ANISOU 582 CG GLU A 106 11152 9018 9296 -3272 2297 -320 C ATOM 583 CD GLU A 106 16.929 -6.672 9.501 1.00 79.59 C ANISOU 583 CD GLU A 106 11355 9223 9661 -3255 2233 -317 C ATOM 584 OE1 GLU A 106 15.881 -6.301 8.928 1.00 83.41 O ANISOU 584 OE1 GLU A 106 11656 9756 10278 -3275 2290 -262 O ATOM 585 OE2 GLU A 106 18.032 -6.078 9.434 1.00 77.29 O ANISOU 585 OE2 GLU A 106 11197 8840 9328 -3223 2124 -363 O ATOM 586 N VAL A 107 13.764 -9.331 13.850 1.00 75.67 N ANISOU 586 N VAL A 107 10902 8970 8877 -3370 3021 -304 N ATOM 587 CA VAL A 107 12.510 -9.662 14.519 1.00 74.57 C ANISOU 587 CA VAL A 107 10650 8938 8744 -3379 3238 -263 C ATOM 588 C VAL A 107 12.538 -9.055 15.918 1.00 80.39 C ANISOU 588 C VAL A 107 11590 9622 9331 -3360 3481 -354 C ATOM 589 O VAL A 107 13.622 -8.943 16.510 1.00 81.08 O ANISOU 589 O VAL A 107 11933 9597 9275 -3366 3428 -427 O ATOM 590 CB VAL A 107 12.299 -11.182 14.568 1.00 66.35 C ANISOU 590 CB VAL A 107 9548 7981 7682 -3414 3144 -183 C ATOM 591 CG1 VAL A 107 11.744 -11.666 13.267 1.00 58.30 C ANISOU 591 CG1 VAL A 107 8284 7041 6826 -3423 2997 -81 C ATOM 592 CG2 VAL A 107 13.608 -11.886 14.863 1.00 57.24 C ANISOU 592 CG2 VAL A 107 8607 6743 6400 -3426 2975 -225 C ATOM 593 N PRO A 108 11.393 -8.637 16.475 1.00 86.36 N ANISOU 593 N PRO A 108 12243 10458 10111 -3326 3747 -354 N ATOM 594 CA PRO A 108 11.393 -7.997 17.801 1.00 85.57 C ANISOU 594 CA PRO A 108 12348 10313 9853 -3278 3996 -452 C ATOM 595 C PRO A 108 12.033 -8.846 18.898 1.00 84.81 C ANISOU 595 C PRO A 108 12489 10186 9550 -3314 3964 -472 C ATOM 596 O PRO A 108 12.046 -10.076 18.845 1.00 80.25 O ANISOU 596 O PRO A 108 11861 9664 8965 -3369 3833 -396 O ATOM 597 CB PRO A 108 9.904 -7.768 18.069 1.00 88.76 C ANISOU 597 CB PRO A 108 12526 10855 10343 -3221 4261 -424 C ATOM 598 CG PRO A 108 9.330 -7.555 16.699 1.00 87.97 C ANISOU 598 CG PRO A 108 12135 10809 10482 -3232 4167 -346 C ATOM 599 CD PRO A 108 10.100 -8.458 15.784 1.00 86.42 C ANISOU 599 CD PRO A 108 11938 10587 10310 -3309 3835 -277 C ATOM 600 N GLY A 109 12.579 -8.159 19.908 1.00 88.97 N ANISOU 600 N GLY A 109 13289 10613 9904 -3280 4085 -576 N ATOM 601 CA GLY A 109 13.199 -8.842 21.032 1.00 89.46 C ANISOU 601 CA GLY A 109 13596 10633 9761 -3316 4059 -598 C ATOM 602 C GLY A 109 12.263 -9.804 21.708 1.00 87.75 C ANISOU 602 C GLY A 109 13278 10553 9509 -3331 4174 -529 C ATOM 603 O GLY A 109 12.711 -10.674 22.462 1.00 84.80 O ANISOU 603 O GLY A 109 13057 10163 9002 -3385 4109 -512 O ATOM 604 N GLU A 110 10.965 -9.651 21.450 1.00 92.76 N ANISOU 604 N GLU A 110 13652 11323 10270 -3286 4345 -483 N ATOM 605 CA GLU A 110 9.951 -10.608 21.865 1.00100.81 C ANISOU 605 CA GLU A 110 14514 12491 11296 -3310 4438 -390 C ATOM 606 C GLU A 110 10.333 -12.038 21.488 1.00101.30 C ANISOU 606 C GLU A 110 14543 12566 11379 -3411 4195 -291 C ATOM 607 O GLU A 110 10.454 -12.909 22.356 1.00100.07 O ANISOU 607 O GLU A 110 14506 12424 11093 -3459 4196 -263 O ATOM 608 CB GLU A 110 8.621 -10.208 21.225 1.00109.87 C ANISOU 608 CB GLU A 110 15335 13772 12639 -3258 4587 -339 C ATOM 609 CG GLU A 110 7.371 -10.505 22.052 1.00118.47 C ANISOU 609 CG GLU A 110 16294 15015 13704 -3225 4833 -295 C ATOM 610 CD GLU A 110 6.094 -10.133 21.301 1.00122.99 C ANISOU 610 CD GLU A 110 16515 15717 14500 -3178 4953 -234 C ATOM 611 OE1 GLU A 110 5.222 -9.447 21.889 1.00124.46 O ANISOU 611 OE1 GLU A 110 16618 15980 14692 -3076 5229 -280 O ATOM 612 OE2 GLU A 110 5.988 -10.502 20.103 1.00123.40 O ANISOU 612 OE2 GLU A 110 16374 15789 14723 -3235 4764 -144 O ATOM 613 N VAL A 111 10.544 -12.292 20.188 1.00101.80 N ANISOU 613 N VAL A 111 14455 12623 11602 -3437 3984 -239 N ATOM 614 CA VAL A 111 10.654 -13.666 19.687 1.00 96.91 C ANISOU 614 CA VAL A 111 13750 12037 11032 -3505 3780 -141 C ATOM 615 C VAL A 111 11.879 -14.370 20.265 1.00 95.46 C ANISOU 615 C VAL A 111 13824 11748 10699 -3551 3630 -176 C ATOM 616 O VAL A 111 11.825 -15.558 20.611 1.00 91.50 O ANISOU 616 O VAL A 111 13330 11279 10156 -3606 3575 -111 O ATOM 617 CB VAL A 111 10.656 -13.683 18.144 1.00 89.36 C ANISOU 617 CB VAL A 111 12596 11092 10267 -3503 3588 -92 C ATOM 618 CG1 VAL A 111 11.582 -12.654 17.591 1.00 84.26 C ANISOU 618 CG1 VAL A 111 12049 10330 9635 -3467 3495 -181 C ATOM 619 CG2 VAL A 111 11.063 -15.034 17.644 1.00 87.09 C ANISOU 619 CG2 VAL A 111 12286 10802 10002 -3553 3363 -23 C ATOM 620 N ASP A 112 13.001 -13.658 20.368 1.00 94.43 N ANISOU 620 N ASP A 112 13904 11486 10491 -3532 3560 -275 N ATOM 621 CA ASP A 112 14.143 -14.186 21.103 1.00 93.50 C ANISOU 621 CA ASP A 112 14044 11265 10219 -3574 3447 -314 C ATOM 622 C ASP A 112 13.750 -14.543 22.534 1.00 94.81 C ANISOU 622 C ASP A 112 14345 11460 10219 -3602 3620 -307 C ATOM 623 O ASP A 112 14.073 -15.629 23.033 1.00 95.46 O ANISOU 623 O ASP A 112 14510 11535 10226 -3663 3537 -265 O ATOM 624 CB ASP A 112 15.270 -13.160 21.107 1.00 91.87 C ANISOU 624 CB ASP A 112 14042 10916 9950 -3548 3384 -418 C ATOM 625 CG ASP A 112 16.281 -13.418 20.042 1.00 84.98 C ANISOU 625 CG ASP A 112 13141 9984 9162 -3547 3120 -419 C ATOM 626 OD1 ASP A 112 16.836 -14.531 20.033 1.00 81.32 O ANISOU 626 OD1 ASP A 112 12706 9514 8678 -3580 2966 -385 O ATOM 627 OD2 ASP A 112 16.554 -12.493 19.253 1.00 85.31 O ANISOU 627 OD2 ASP A 112 13142 9986 9286 -3507 3074 -456 O ATOM 628 N GLY A 113 13.063 -13.629 23.215 1.00 97.36 N ANISOU 628 N GLY A 113 14695 11817 10480 -3552 3865 -351 N ATOM 629 CA GLY A 113 12.594 -13.889 24.558 1.00105.80 C ANISOU 629 CA GLY A 113 15880 12934 11386 -3563 4048 -346 C ATOM 630 C GLY A 113 13.357 -13.139 25.629 1.00110.68 C ANISOU 630 C GLY A 113 16819 13433 11800 -3541 4112 -452 C ATOM 631 O GLY A 113 12.761 -12.400 26.416 1.00114.82 O ANISOU 631 O GLY A 113 17402 13994 12230 -3475 4344 -505 O ATOM 632 N GLY A 114 14.676 -13.323 25.668 1.00113.76 N ANISOU 632 N GLY A 114 17418 13683 12121 -3589 3904 -486 N ATOM 633 CA GLY A 114 15.518 -12.691 26.658 1.00114.58 C ANISOU 633 CA GLY A 114 17847 13659 12030 -3583 3921 -575 C ATOM 634 C GLY A 114 15.129 -13.101 28.060 1.00117.01 C ANISOU 634 C GLY A 114 18301 14009 12149 -3604 4066 -562 C ATOM 635 O GLY A 114 14.891 -14.285 28.347 1.00117.13 O ANISOU 635 O GLY A 114 18264 14088 12151 -3676 4028 -474 O ATOM 636 N PRO A 115 15.052 -12.122 28.964 1.00118.58 N ANISOU 636 N PRO A 115 18690 14173 12194 -3535 4234 -651 N ATOM 637 CA PRO A 115 14.486 -12.389 30.297 1.00120.23 C ANISOU 637 CA PRO A 115 19012 14448 12221 -3534 4409 -643 C ATOM 638 C PRO A 115 13.050 -12.897 30.201 1.00123.44 C ANISOU 638 C PRO A 115 19131 15050 12720 -3518 4595 -562 C ATOM 639 O PRO A 115 12.202 -12.304 29.529 1.00122.67 O ANISOU 639 O PRO A 115 18804 15039 12766 -3437 4726 -572 O ATOM 640 CB PRO A 115 14.574 -11.029 30.998 1.00113.77 C ANISOU 640 CB PRO A 115 18403 13563 11260 -3423 4557 -773 C ATOM 641 CG PRO A 115 15.664 -10.289 30.266 1.00107.63 C ANISOU 641 CG PRO A 115 17732 12628 10536 -3413 4377 -837 C ATOM 642 CD PRO A 115 15.581 -10.750 28.844 1.00112.23 C ANISOU 642 CD PRO A 115 18033 13253 11357 -3454 4251 -765 C ATOM 643 N GLN A 116 12.784 -14.000 30.899 1.00125.79 N ANISOU 643 N GLN A 116 19445 15415 12935 -3600 4603 -475 N ATOM 644 CA GLN A 116 11.570 -14.806 30.718 1.00127.36 C ANISOU 644 CA GLN A 116 19367 15791 13235 -3622 4714 -363 C ATOM 645 C GLN A 116 11.270 -15.003 29.227 1.00120.86 C ANISOU 645 C GLN A 116 18243 15010 12669 -3622 4606 -307 C ATOM 646 O GLN A 116 10.145 -14.818 28.752 1.00122.24 O ANISOU 646 O GLN A 116 18151 15318 12976 -3572 4750 -267 O ATOM 647 CB GLN A 116 10.367 -14.211 31.469 1.00129.77 C ANISOU 647 CB GLN A 116 19604 16234 13469 -3532 5031 -388 C ATOM 648 CG GLN A 116 10.221 -14.657 32.952 1.00131.62 C ANISOU 648 CG GLN A 116 20038 16506 13465 -3571 5151 -372 C ATOM 649 CD GLN A 116 9.390 -15.930 33.144 1.00127.80 C ANISOU 649 CD GLN A 116 19382 16168 13009 -3661 5196 -224 C ATOM 650 OE1 GLN A 116 8.555 -16.276 32.301 1.00126.30 O ANISOU 650 OE1 GLN A 116 18887 16091 13011 -3661 5221 -141 O ATOM 651 NE2 GLN A 116 9.586 -16.604 34.284 1.00126.05 N ANISOU 651 NE2 GLN A 116 19360 15944 12589 -3740 5210 -186 N ATOM 652 N GLY A 117 12.325 -15.363 28.486 1.00112.66 N ANISOU 652 N GLY A 117 17252 13854 11698 -3675 4342 -305 N ATOM 653 CA GLY A 117 12.206 -16.025 27.199 1.00104.21 C ANISOU 653 CA GLY A 117 15936 12820 10838 -3705 4178 -228 C ATOM 654 C GLY A 117 12.663 -17.470 27.305 1.00 96.93 C ANISOU 654 C GLY A 117 15053 11877 9897 -3808 3998 -144 C ATOM 655 O GLY A 117 12.991 -18.123 26.310 1.00 91.15 O ANISOU 655 O GLY A 117 14202 11128 9304 -3835 3801 -101 O ATOM 656 N ILE A 118 12.667 -17.977 28.531 1.00 92.73 N ANISOU 656 N ILE A 118 14694 11350 9188 -3861 4070 -121 N ATOM 657 CA ILE A 118 13.229 -19.281 28.861 1.00 88.35 C ANISOU 657 CA ILE A 118 14236 10752 8579 -3962 3910 -53 C ATOM 658 C ILE A 118 12.131 -20.323 28.779 1.00 90.12 C ANISOU 658 C ILE A 118 14243 11118 8880 -4009 3976 77 C ATOM 659 O ILE A 118 11.041 -20.125 29.321 1.00 98.07 O ANISOU 659 O ILE A 118 15163 12251 9850 -3991 4203 113 O ATOM 660 CB ILE A 118 13.838 -19.260 30.268 1.00 81.29 C ANISOU 660 CB ILE A 118 13661 9781 7445 -4005 3944 -90 C ATOM 661 CG1 ILE A 118 14.884 -18.150 30.336 1.00 77.68 C ANISOU 661 CG1 ILE A 118 13419 9179 6916 -3958 3879 -214 C ATOM 662 CG2 ILE A 118 14.389 -20.640 30.642 1.00 76.45 C ANISOU 662 CG2 ILE A 118 13145 9123 6778 -4115 3781 -11 C ATOM 663 CD1 ILE A 118 15.232 -17.722 31.722 1.00 77.30 C ANISOU 663 CD1 ILE A 118 13673 9069 6628 -3969 3969 -266 C ATOM 664 N ILE A 119 12.418 -21.444 28.128 1.00 87.39 N ANISOU 664 N ILE A 119 13815 10752 8637 -4066 3783 148 N ATOM 665 CA ILE A 119 11.474 -22.552 28.029 1.00 86.99 C ANISOU 665 CA ILE A 119 13580 10813 8660 -4124 3817 279 C ATOM 666 C ILE A 119 11.811 -23.563 29.123 1.00 89.05 C ANISOU 666 C ILE A 119 14033 11040 8761 -4223 3792 333 C ATOM 667 O ILE A 119 12.920 -24.128 29.106 1.00 84.36 O ANISOU 667 O ILE A 119 13595 10324 8135 -4264 3590 313 O ATOM 668 CB ILE A 119 11.512 -23.206 26.646 1.00 84.27 C ANISOU 668 CB ILE A 119 13031 10464 8522 -4123 3627 326 C ATOM 669 CG1 ILE A 119 11.260 -22.154 25.566 1.00 79.60 C ANISOU 669 CG1 ILE A 119 12270 9898 8078 -4031 3637 273 C ATOM 670 CG2 ILE A 119 10.483 -24.326 26.574 1.00 87.80 C ANISOU 670 CG2 ILE A 119 13297 11020 9045 -4187 3669 467 C ATOM 671 CD1 ILE A 119 12.087 -22.358 24.317 1.00 75.14 C ANISOU 671 CD1 ILE A 119 11656 9250 7644 -4007 3393 243 C ATOM 672 N PRO A 120 10.909 -23.812 30.078 1.00 94.64 N ANISOU 672 N PRO A 120 14737 11854 9367 -4262 3988 404 N ATOM 673 CA PRO A 120 11.210 -24.753 31.176 1.00 91.64 C ANISOU 673 CA PRO A 120 14554 11443 8823 -4364 3970 462 C ATOM 674 C PRO A 120 10.879 -26.178 30.772 1.00 87.10 C ANISOU 674 C PRO A 120 13843 10898 8354 -4447 3867 590 C ATOM 675 O PRO A 120 9.977 -26.390 29.946 1.00 88.05 O ANISOU 675 O PRO A 120 13697 11113 8643 -4430 3901 658 O ATOM 676 CB PRO A 120 10.302 -24.261 32.307 1.00 93.09 C ANISOU 676 CB PRO A 120 14772 11743 8853 -4356 4250 476 C ATOM 677 CG PRO A 120 9.124 -23.660 31.579 1.00 93.66 C ANISOU 677 CG PRO A 120 14548 11955 9084 -4276 4408 495 C ATOM 678 CD PRO A 120 9.604 -23.142 30.262 1.00 93.14 C ANISOU 678 CD PRO A 120 14374 11820 9195 -4208 4251 427 C ATOM 679 N PRO A 121 11.579 -27.172 31.329 1.00 85.72 N ANISOU 679 N PRO A 121 13847 10638 8086 -4539 3737 629 N ATOM 680 CA PRO A 121 11.522 -28.527 30.763 1.00 81.73 C ANISOU 680 CA PRO A 121 13233 10120 7700 -4607 3591 730 C ATOM 681 C PRO A 121 10.094 -29.035 30.609 1.00109.00 C ANISOU 681 C PRO A 121 16443 13725 11249 -4638 3738 857 C ATOM 682 O PRO A 121 9.222 -28.769 31.434 1.00107.40 O ANISOU 682 O PRO A 121 16222 13634 10950 -4653 3958 904 O ATOM 683 CB PRO A 121 12.327 -29.361 31.764 1.00 82.54 C ANISOU 683 CB PRO A 121 13597 10128 7638 -4706 3496 757 C ATOM 684 CG PRO A 121 13.264 -28.389 32.381 1.00 82.05 C ANISOU 684 CG PRO A 121 13779 9975 7423 -4669 3485 639 C ATOM 685 CD PRO A 121 12.516 -27.089 32.462 1.00 82.90 C ANISOU 685 CD PRO A 121 13806 10178 7513 -4583 3703 580 C ATOM 686 N GLY A 122 9.852 -29.757 29.519 1.00108.11 N ANISOU 686 N GLY A 122 16137 13614 11326 -4644 3616 914 N ATOM 687 CA GLY A 122 8.508 -30.086 29.099 1.00113.98 C ANISOU 687 CA GLY A 122 16615 14490 12202 -4660 3732 1028 C ATOM 688 C GLY A 122 7.706 -28.933 28.533 1.00116.96 C ANISOU 688 C GLY A 122 16788 14974 12679 -4563 3873 997 C ATOM 689 O GLY A 122 6.593 -29.164 28.043 1.00119.44 O ANISOU 689 O GLY A 122 16856 15395 13128 -4572 3952 1095 O ATOM 690 N GLY A 123 8.239 -27.696 28.560 1.00112.28 N ANISOU 690 N GLY A 123 16286 14346 12029 -4475 3901 867 N ATOM 691 CA GLY A 123 7.447 -26.519 28.265 1.00106.40 C ANISOU 691 CA GLY A 123 15376 13705 11347 -4385 4071 835 C ATOM 692 C GLY A 123 7.177 -26.293 26.788 1.00 97.80 C ANISOU 692 C GLY A 123 14049 12628 10483 -4328 3968 836 C ATOM 693 O GLY A 123 7.767 -26.912 25.902 1.00 96.24 O ANISOU 693 O GLY A 123 13835 12344 10388 -4340 3750 834 O ATOM 694 N LYS A 124 6.235 -25.387 26.536 1.00 91.74 N ANISOU 694 N LYS A 124 13092 11975 9790 -4263 4137 840 N ATOM 695 CA LYS A 124 5.956 -24.875 25.207 1.00 91.42 C ANISOU 695 CA LYS A 124 12838 11951 9948 -4199 4064 829 C ATOM 696 C LYS A 124 6.316 -23.400 25.165 1.00 97.48 C ANISOU 696 C LYS A 124 13664 12693 10679 -4098 4134 695 C ATOM 697 O LYS A 124 6.235 -22.698 26.175 1.00105.26 O ANISOU 697 O LYS A 124 14768 13708 11518 -4067 4320 638 O ATOM 698 CB LYS A 124 4.476 -25.046 24.818 1.00 91.53 C ANISOU 698 CB LYS A 124 12547 12118 10112 -4212 4193 962 C ATOM 699 CG LYS A 124 4.190 -24.991 23.308 1.00 90.31 C ANISOU 699 CG LYS A 124 12166 11964 10184 -4183 4052 992 C ATOM 700 CD LYS A 124 2.756 -24.511 22.981 1.00 94.48 C ANISOU 700 CD LYS A 124 12395 12650 10854 -4160 4225 1083 C ATOM 701 CE LYS A 124 2.254 -25.090 21.650 1.00 93.47 C ANISOU 701 CE LYS A 124 12039 12527 10948 -4188 4070 1181 C ATOM 702 NZ LYS A 124 0.967 -24.516 21.137 1.00 91.53 N ANISOU 702 NZ LYS A 124 11491 12419 10869 -4162 4200 1266 N ATOM 703 N ARG A 125 6.749 -22.944 23.997 1.00 95.37 N ANISOU 703 N ARG A 125 13327 12366 10541 -4046 3982 640 N ATOM 704 CA ARG A 125 6.729 -21.522 23.688 1.00 94.19 C ANISOU 704 CA ARG A 125 13143 12222 10422 -3951 4066 544 C ATOM 705 C ARG A 125 6.289 -21.418 22.237 1.00 97.37 C ANISOU 705 C ARG A 125 13295 12655 11046 -3926 3957 589 C ATOM 706 O ARG A 125 6.545 -22.325 21.443 1.00100.34 O ANISOU 706 O ARG A 125 13622 12988 11513 -3966 3758 641 O ATOM 707 CB ARG A 125 8.103 -20.877 23.961 1.00 92.61 C ANISOU 707 CB ARG A 125 13216 11874 10097 -3915 3977 400 C ATOM 708 CG ARG A 125 8.165 -19.334 24.020 1.00 98.47 C ANISOU 708 CG ARG A 125 13995 12603 10816 -3822 4107 284 C ATOM 709 CD ARG A 125 9.551 -18.861 24.545 1.00104.54 C ANISOU 709 CD ARG A 125 15075 13216 11430 -3809 4025 157 C ATOM 710 NE ARG A 125 10.320 -18.103 23.541 1.00109.65 N ANISOU 710 NE ARG A 125 15727 13769 12167 -3758 3878 76 N ATOM 711 CZ ARG A 125 11.659 -18.114 23.418 1.00111.03 C ANISOU 711 CZ ARG A 125 16097 13803 12287 -3766 3690 4 C ATOM 712 NH1 ARG A 125 12.420 -18.838 24.233 1.00112.56 N ANISOU 712 NH1 ARG A 125 16504 13925 12340 -3825 3616 -1 N ATOM 713 NH2 ARG A 125 12.250 -17.403 22.461 1.00108.24 N ANISOU 713 NH2 ARG A 125 15720 13382 12024 -3719 3571 -57 N ATOM 714 N SER A 126 5.564 -20.361 21.897 1.00 99.06 N ANISOU 714 N SER A 126 13344 12947 11348 -3860 4093 575 N ATOM 715 CA SER A 126 5.164 -20.153 20.510 1.00 99.10 C ANISOU 715 CA SER A 126 13119 12975 11559 -3839 3984 618 C ATOM 716 C SER A 126 5.537 -18.744 20.086 1.00 98.22 C ANISOU 716 C SER A 126 13026 12819 11475 -3753 4005 503 C ATOM 717 O SER A 126 5.297 -17.787 20.828 1.00100.33 O ANISOU 717 O SER A 126 13338 13116 11666 -3697 4216 434 O ATOM 718 CB SER A 126 3.662 -20.386 20.294 1.00105.99 C ANISOU 718 CB SER A 126 13695 14005 12571 -3861 4113 757 C ATOM 719 OG SER A 126 3.401 -21.726 19.907 1.00108.33 O ANISOU 719 OG SER A 126 13911 14308 12940 -3943 3981 878 O ATOM 720 N VAL A 127 6.145 -18.626 18.897 1.00 93.97 N ANISOU 720 N VAL A 127 12462 12203 11040 -3739 3791 479 N ATOM 721 CA VAL A 127 6.531 -17.329 18.342 1.00 85.52 C ANISOU 721 CA VAL A 127 11399 11081 10014 -3668 3784 382 C ATOM 722 C VAL A 127 6.036 -17.240 16.908 1.00 81.35 C ANISOU 722 C VAL A 127 10629 10589 9692 -3666 3659 453 C ATOM 723 O VAL A 127 5.780 -18.249 16.254 1.00 80.35 O ANISOU 723 O VAL A 127 10395 10484 9652 -3714 3518 550 O ATOM 724 CB VAL A 127 8.057 -17.084 18.368 1.00 76.89 C ANISOU 724 CB VAL A 127 10571 9832 8811 -3651 3632 262 C ATOM 725 CG1 VAL A 127 8.631 -17.226 19.770 1.00 73.02 C ANISOU 725 CG1 VAL A 127 10340 9290 8113 -3666 3726 198 C ATOM 726 CG2 VAL A 127 8.744 -18.043 17.441 1.00 75.40 C ANISOU 726 CG2 VAL A 127 10386 9583 8680 -3682 3362 294 C ATOM 727 N THR A 128 5.907 -16.013 16.412 1.00 82.02 N ANISOU 727 N THR A 128 10636 10671 9855 -3609 3710 402 N ATOM 728 CA THR A 128 5.687 -15.788 14.989 1.00 84.97 C ANISOU 728 CA THR A 128 10824 11052 10410 -3607 3556 452 C ATOM 729 C THR A 128 6.861 -15.023 14.404 1.00 84.31 C ANISOU 729 C THR A 128 10885 10842 10306 -3567 3412 345 C ATOM 730 O THR A 128 7.379 -14.080 15.012 1.00 83.72 O ANISOU 730 O THR A 128 10963 10706 10141 -3524 3520 235 O ATOM 731 CB THR A 128 4.399 -15.025 14.686 1.00 89.24 C ANISOU 731 CB THR A 128 11092 11709 11107 -3586 3716 512 C ATOM 732 OG1 THR A 128 4.239 -13.966 15.639 1.00 94.24 O ANISOU 732 OG1 THR A 128 11784 12355 11669 -3522 3971 415 O ATOM 733 CG2 THR A 128 3.182 -15.960 14.688 1.00 92.71 C ANISOU 733 CG2 THR A 128 11309 12278 11636 -3642 3764 664 C ATOM 734 N LEU A 129 7.259 -15.441 13.208 1.00 87.38 N ANISOU 734 N LEU A 129 11227 11192 10780 -3579 3174 381 N ATOM 735 CA LEU A 129 8.388 -14.889 12.468 1.00 82.74 C ANISOU 735 CA LEU A 129 10754 10498 10187 -3544 3002 301 C ATOM 736 C LEU A 129 7.812 -14.348 11.167 1.00 84.63 C ANISOU 736 C LEU A 129 10777 10772 10605 -3538 2921 364 C ATOM 737 O LEU A 129 7.468 -15.126 10.268 1.00 85.06 O ANISOU 737 O LEU A 129 10705 10858 10756 -3566 2778 454 O ATOM 738 CB LEU A 129 9.446 -15.963 12.213 1.00 74.52 C ANISOU 738 CB LEU A 129 9858 9384 9074 -3552 2792 284 C ATOM 739 CG LEU A 129 10.046 -16.654 13.444 1.00 68.48 C ANISOU 739 CG LEU A 129 9301 8578 8142 -3571 2840 237 C ATOM 740 CD1 LEU A 129 11.048 -17.708 13.055 1.00 61.32 C ANISOU 740 CD1 LEU A 129 8500 7603 7194 -3574 2631 224 C ATOM 741 CD2 LEU A 129 10.683 -15.652 14.356 1.00 69.78 C ANISOU 741 CD2 LEU A 129 9656 8674 8182 -3543 2956 125 C ATOM 742 N ASN A 130 7.613 -13.034 11.101 1.00 89.92 N ANISOU 742 N ASN A 130 11400 11437 11329 -3508 3026 320 N ATOM 743 CA ASN A 130 7.267 -12.394 9.841 1.00 93.97 C ANISOU 743 CA ASN A 130 11737 11961 12007 -3506 2924 369 C ATOM 744 C ASN A 130 8.568 -11.919 9.213 1.00 93.66 C ANISOU 744 C ASN A 130 11859 11804 11924 -3475 2742 290 C ATOM 745 O ASN A 130 9.174 -10.940 9.668 1.00 94.54 O ANISOU 745 O ASN A 130 12107 11840 11974 -3444 2817 190 O ATOM 746 CB ASN A 130 6.276 -11.249 10.022 1.00100.73 C ANISOU 746 CB ASN A 130 12422 12877 12976 -3491 3135 372 C ATOM 747 CG ASN A 130 5.623 -10.853 8.703 1.00107.62 C ANISOU 747 CG ASN A 130 13056 13788 14048 -3513 3021 464 C ATOM 748 OD1 ASN A 130 6.129 -11.182 7.620 1.00107.85 O ANISOU 748 OD1 ASN A 130 13098 13772 14108 -3528 2779 500 O ATOM 749 ND2 ASN A 130 4.488 -10.167 8.784 1.00110.69 N ANISOU 749 ND2 ASN A 130 13220 14260 14576 -3510 3198 502 N ATOM 750 N VAL A 131 9.005 -12.619 8.176 1.00 87.21 N ANISOU 750 N VAL A 131 11030 10967 11137 -3478 2513 331 N ATOM 751 CA VAL A 131 10.360 -12.444 7.682 1.00 82.59 C ANISOU 751 CA VAL A 131 10611 10284 10484 -3436 2339 256 C ATOM 752 C VAL A 131 10.424 -11.143 6.907 1.00 80.54 C ANISOU 752 C VAL A 131 10293 9990 10317 -3420 2299 246 C ATOM 753 O VAL A 131 9.652 -10.935 5.970 1.00 87.47 O ANISOU 753 O VAL A 131 10980 10915 11339 -3442 2247 331 O ATOM 754 CB VAL A 131 10.774 -13.625 6.803 1.00 80.36 C ANISOU 754 CB VAL A 131 10329 9998 10206 -3430 2137 294 C ATOM 755 CG1 VAL A 131 12.270 -13.676 6.720 1.00 80.37 C ANISOU 755 CG1 VAL A 131 10527 9913 10097 -3378 2010 202 C ATOM 756 CG2 VAL A 131 10.193 -14.918 7.355 1.00 80.30 C ANISOU 756 CG2 VAL A 131 10292 10044 10175 -3471 2189 348 C ATOM 757 N ASP A 132 11.336 -10.264 7.289 1.00 76.37 N ANISOU 757 N ASP A 132 9930 9373 9714 -3389 2317 149 N ATOM 758 CA ASP A 132 11.544 -9.050 6.504 1.00 80.17 C ANISOU 758 CA ASP A 132 10377 9804 10282 -3376 2252 139 C ATOM 759 C ASP A 132 13.044 -8.760 6.470 1.00 85.17 C ANISOU 759 C ASP A 132 11219 10333 10807 -3330 2127 53 C ATOM 760 O ASP A 132 13.556 -8.010 7.311 1.00 92.90 O ANISOU 760 O ASP A 132 12352 11233 11712 -3320 2228 -34 O ATOM 761 CB ASP A 132 10.756 -7.876 7.061 1.00 85.82 C ANISOU 761 CB ASP A 132 11023 10515 11072 -3393 2473 117 C ATOM 762 CG ASP A 132 10.814 -6.661 6.146 1.00 89.70 C ANISOU 762 CG ASP A 132 11445 10949 11687 -3394 2396 125 C ATOM 763 OD1 ASP A 132 11.002 -6.858 4.922 1.00 91.12 O ANISOU 763 OD1 ASP A 132 11551 11141 11928 -3396 2178 192 O ATOM 764 OD2 ASP A 132 10.705 -5.516 6.643 1.00 89.73 O ANISOU 764 OD2 ASP A 132 11480 10885 11728 -3390 2556 61 O ATOM 765 N GLN A 133 13.735 -9.361 5.487 1.00 74.48 N ANISOU 765 N GLN A 133 9870 8981 9450 -3298 1916 78 N ATOM 766 CA GLN A 133 15.161 -9.169 5.238 1.00 65.45 C ANISOU 766 CA GLN A 133 8881 7764 8225 -3241 1779 14 C ATOM 767 C GLN A 133 15.526 -10.032 4.038 1.00 65.61 C ANISOU 767 C GLN A 133 8841 7819 8268 -3207 1595 59 C ATOM 768 O GLN A 133 14.837 -11.031 3.785 1.00 66.43 O ANISOU 768 O GLN A 133 8849 7985 8405 -3232 1592 115 O ATOM 769 CB GLN A 133 16.008 -9.563 6.443 1.00 60.06 C ANISOU 769 CB GLN A 133 8396 7033 7390 -3226 1836 -71 C ATOM 770 CG GLN A 133 16.038 -11.039 6.714 1.00 58.39 C ANISOU 770 CG GLN A 133 8199 6869 7118 -3228 1816 -56 C ATOM 771 CD GLN A 133 16.061 -11.330 8.193 1.00 62.90 C ANISOU 771 CD GLN A 133 8906 7418 7573 -3256 1964 -108 C ATOM 772 OE1 GLN A 133 15.011 -11.457 8.843 1.00 68.78 O ANISOU 772 OE1 GLN A 133 9592 8209 8332 -3303 2124 -81 O ATOM 773 NE2 GLN A 133 17.254 -11.382 8.750 1.00 60.57 N ANISOU 773 NE2 GLN A 133 8794 7055 7165 -3228 1920 -180 N ATOM 774 N PRO A 134 16.593 -9.712 3.297 1.00 60.28 N ANISOU 774 N PRO A 134 8224 7104 7575 -3152 1454 34 N ATOM 775 CA PRO A 134 16.833 -10.399 2.027 1.00 58.60 C ANISOU 775 CA PRO A 134 7946 6927 7394 -3121 1310 73 C ATOM 776 C PRO A 134 17.186 -11.856 2.259 1.00 56.64 C ANISOU 776 C PRO A 134 7749 6702 7068 -3106 1294 53 C ATOM 777 O PRO A 134 17.594 -12.260 3.353 1.00 57.56 O ANISOU 777 O PRO A 134 7978 6799 7093 -3104 1359 4 O ATOM 778 CB PRO A 134 18.021 -9.647 1.426 1.00 60.05 C ANISOU 778 CB PRO A 134 8199 7061 7555 -3061 1200 39 C ATOM 779 CG PRO A 134 18.342 -8.531 2.391 1.00 56.33 C ANISOU 779 CG PRO A 134 7827 6522 7053 -3065 1274 -11 C ATOM 780 CD PRO A 134 17.758 -8.901 3.684 1.00 56.46 C ANISOU 780 CD PRO A 134 7888 6542 7020 -3109 1429 -37 C ATOM 781 N ALA A 135 17.035 -12.643 1.194 1.00 53.36 N ANISOU 781 N ALA A 135 7261 6323 6689 -3101 1206 91 N ATOM 782 CA ALA A 135 17.319 -14.066 1.277 1.00 53.72 C ANISOU 782 CA ALA A 135 7381 6395 6636 -3136 1202 52 C ATOM 783 C ALA A 135 18.695 -14.280 1.882 1.00 56.41 C ANISOU 783 C ALA A 135 7888 6696 6849 -3097 1192 -33 C ATOM 784 O ALA A 135 19.644 -13.562 1.559 1.00 62.34 O ANISOU 784 O ALA A 135 8697 7419 7572 -3054 1138 -69 O ATOM 785 CB ALA A 135 17.235 -14.702 -0.104 1.00 53.05 C ANISOU 785 CB ALA A 135 7266 6352 6539 -3183 1118 57 C ATOM 786 N ALA A 136 18.791 -15.247 2.786 1.00 52.05 N ANISOU 786 N ALA A 136 7408 6140 6230 -3116 1243 -57 N ATOM 787 CA ALA A 136 19.960 -15.312 3.646 1.00 47.45 C ANISOU 787 CA ALA A 136 6971 5509 5548 -3079 1248 -122 C ATOM 788 C ALA A 136 19.984 -16.671 4.323 1.00 51.59 C ANISOU 788 C ALA A 136 7562 6037 6002 -3120 1281 -137 C ATOM 789 O ALA A 136 18.981 -17.391 4.337 1.00 53.33 O ANISOU 789 O ALA A 136 7712 6293 6258 -3174 1319 -93 O ATOM 790 CB ALA A 136 19.933 -14.179 4.662 1.00 42.41 C ANISOU 790 CB ALA A 136 6352 4825 4938 -3036 1307 -117 C ATOM 791 N THR A 137 21.146 -17.031 4.872 1.00 47.87 N ANISOU 791 N THR A 137 7223 5526 5439 -3097 1262 -192 N ATOM 792 CA THR A 137 21.304 -18.317 5.560 1.00 42.72 C ANISOU 792 CA THR A 137 6646 4864 4720 -3135 1284 -204 C ATOM 793 C THR A 137 21.679 -18.043 7.008 1.00 42.72 C ANISOU 793 C THR A 137 6746 4814 4672 -3115 1337 -219 C ATOM 794 O THR A 137 22.852 -17.859 7.345 1.00 41.98 O ANISOU 794 O THR A 137 6756 4677 4519 -3076 1299 -259 O ATOM 795 CB THR A 137 22.327 -19.220 4.893 1.00 42.20 C ANISOU 795 CB THR A 137 6646 4795 4593 -3137 1213 -243 C ATOM 796 OG1 THR A 137 21.965 -19.427 3.525 1.00 56.65 O ANISOU 796 OG1 THR A 137 8396 6671 6456 -3161 1168 -232 O ATOM 797 CG2 THR A 137 22.362 -20.565 5.574 1.00 42.80 C ANISOU 797 CG2 THR A 137 6787 4854 4619 -3183 1232 -243 C ATOM 798 N CYS A 138 20.667 -18.025 7.865 1.00 52.89 N ANISOU 798 N CYS A 138 8001 6110 5985 -3145 1428 -178 N ATOM 799 CA CYS A 138 20.846 -17.773 9.282 1.00 50.58 C ANISOU 799 CA CYS A 138 7823 5774 5622 -3154 1503 -197 C ATOM 800 C CYS A 138 20.744 -19.095 10.021 1.00 49.18 C ANISOU 800 C CYS A 138 7700 5592 5393 -3201 1525 -178 C ATOM 801 O CYS A 138 20.536 -20.140 9.419 1.00 48.76 O ANISOU 801 O CYS A 138 7604 5566 5355 -3237 1488 -161 O ATOM 802 CB CYS A 138 19.815 -16.757 9.774 1.00 48.25 C ANISOU 802 CB CYS A 138 7505 5493 5337 -3200 1635 -193 C ATOM 803 SG CYS A 138 19.749 -15.267 8.784 1.00 46.63 S ANISOU 803 SG CYS A 138 7211 5290 5215 -3156 1605 -198 S ATOM 804 N TRP A 139 20.853 -19.060 11.343 1.00 50.92 N ANISOU 804 N TRP A 139 8058 5776 5514 -3247 1606 -202 N ATOM 805 CA TRP A 139 20.753 -20.318 12.072 1.00 50.82 C ANISOU 805 CA TRP A 139 8102 5756 5452 -3300 1622 -176 C ATOM 806 C TRP A 139 20.096 -20.046 13.412 1.00 53.44 C ANISOU 806 C TRP A 139 8527 6080 5697 -3376 1770 -177 C ATOM 807 O TRP A 139 19.779 -18.905 13.735 1.00 58.24 O ANISOU 807 O TRP A 139 9158 6683 6286 -3381 1862 -207 O ATOM 808 CB TRP A 139 22.124 -20.978 12.184 1.00 45.43 C ANISOU 808 CB TRP A 139 7520 5019 4722 -3262 1514 -199 C ATOM 809 CG TRP A 139 23.135 -20.193 12.906 1.00 45.05 C ANISOU 809 CG TRP A 139 7620 4911 4586 -3242 1505 -251 C ATOM 810 CD1 TRP A 139 23.557 -18.930 12.625 1.00 44.34 C ANISOU 810 CD1 TRP A 139 7538 4806 4501 -3194 1494 -289 C ATOM 811 CD2 TRP A 139 23.924 -20.642 13.999 1.00 45.40 C ANISOU 811 CD2 TRP A 139 7829 4895 4526 -3270 1493 -262 C ATOM 812 NE1 TRP A 139 24.535 -18.549 13.505 1.00 44.26 N ANISOU 812 NE1 TRP A 139 7691 4731 4395 -3192 1478 -325 N ATOM 813 CE2 TRP A 139 24.779 -19.589 14.359 1.00 48.36 C ANISOU 813 CE2 TRP A 139 8309 5222 4843 -3239 1475 -308 C ATOM 814 CE3 TRP A 139 23.982 -21.834 14.724 1.00 46.19 C ANISOU 814 CE3 TRP A 139 8001 4973 4575 -3324 1490 -232 C ATOM 815 CZ2 TRP A 139 25.673 -19.693 15.406 1.00 45.21 C ANISOU 815 CZ2 TRP A 139 8085 4756 4336 -3260 1451 -322 C ATOM 816 CZ3 TRP A 139 24.864 -21.932 15.759 1.00 46.48 C ANISOU 816 CZ3 TRP A 139 8211 4943 4506 -3345 1466 -246 C ATOM 817 CH2 TRP A 139 25.698 -20.877 16.090 1.00 46.00 C ANISOU 817 CH2 TRP A 139 8252 4837 4387 -3314 1445 -290 C ATOM 818 N PHE A 140 19.844 -21.102 14.181 1.00 53.29 N ANISOU 818 N PHE A 140 8561 6060 5628 -3437 1804 -143 N ATOM 819 CA PHE A 140 19.329 -20.909 15.531 1.00 50.83 C ANISOU 819 CA PHE A 140 8359 5739 5214 -3510 1950 -143 C ATOM 820 C PHE A 140 20.059 -21.807 16.521 1.00 51.39 C ANISOU 820 C PHE A 140 8600 5753 5175 -3552 1916 -144 C ATOM 821 O PHE A 140 20.493 -22.914 16.191 1.00 50.68 O ANISOU 821 O PHE A 140 8492 5652 5112 -3547 1812 -115 O ATOM 822 CB PHE A 140 17.799 -21.115 15.626 1.00 52.51 C ANISOU 822 CB PHE A 140 8437 6035 5481 -3564 2082 -72 C ATOM 823 CG PHE A 140 17.297 -22.398 15.043 1.00 52.69 C ANISOU 823 CG PHE A 140 8335 6101 5584 -3586 2022 4 C ATOM 824 CD1 PHE A 140 17.308 -23.561 15.777 1.00 53.60 C ANISOU 824 CD1 PHE A 140 8523 6201 5640 -3647 2024 44 C ATOM 825 CD2 PHE A 140 16.750 -22.425 13.769 1.00 66.49 C ANISOU 825 CD2 PHE A 140 9899 7900 7466 -3554 1967 42 C ATOM 826 CE1 PHE A 140 16.825 -24.727 15.232 1.00 53.87 C ANISOU 826 CE1 PHE A 140 8450 6266 5753 -3674 1973 114 C ATOM 827 CE2 PHE A 140 16.258 -23.604 13.218 1.00 52.45 C ANISOU 827 CE2 PHE A 140 8018 6151 5759 -3582 1914 110 C ATOM 828 CZ PHE A 140 16.300 -24.745 13.945 1.00 53.29 C ANISOU 828 CZ PHE A 140 8199 6238 5811 -3641 1919 144 C ATOM 829 N HIS A 141 20.201 -21.306 17.742 1.00 52.22 N ANISOU 829 N HIS A 141 8877 5813 5151 -3597 2009 -178 N ATOM 830 CA HIS A 141 20.973 -22.032 18.738 1.00 56.95 C ANISOU 830 CA HIS A 141 9660 6347 5632 -3642 1967 -177 C ATOM 831 C HIS A 141 20.493 -21.627 20.129 1.00 59.61 C ANISOU 831 C HIS A 141 10152 6665 5830 -3718 2125 -186 C ATOM 832 O HIS A 141 19.957 -20.526 20.315 1.00 56.29 O ANISOU 832 O HIS A 141 9735 6258 5394 -3712 2252 -221 O ATOM 833 CB HIS A 141 22.477 -21.758 18.575 1.00 58.60 C ANISOU 833 CB HIS A 141 9973 6482 5810 -3584 1825 -228 C ATOM 834 CG HIS A 141 22.853 -20.305 18.637 1.00 68.30 C ANISOU 834 CG HIS A 141 11274 7676 7002 -3548 1854 -298 C ATOM 835 ND1 HIS A 141 22.948 -19.610 19.827 1.00 74.55 N ANISOU 835 ND1 HIS A 141 12267 8406 7651 -3600 1946 -339 N ATOM 836 CD2 HIS A 141 23.184 -19.420 17.662 1.00 73.33 C ANISOU 836 CD2 HIS A 141 11820 8322 7719 -3469 1801 -330 C ATOM 837 CE1 HIS A 141 23.318 -18.362 19.582 1.00 75.91 C ANISOU 837 CE1 HIS A 141 12473 8546 7822 -3555 1948 -396 C ATOM 838 NE2 HIS A 141 23.472 -18.221 18.276 1.00 73.84 N ANISOU 838 NE2 HIS A 141 12029 8329 7697 -3476 1859 -388 N ATOM 839 N PRO A 142 20.683 -22.489 21.126 1.00 64.19 N ANISOU 839 N PRO A 142 10871 7213 6306 -3788 2126 -154 N ATOM 840 CA PRO A 142 20.302 -22.128 22.501 1.00 69.05 C ANISOU 840 CA PRO A 142 11658 7808 6770 -3859 2276 -161 C ATOM 841 C PRO A 142 21.018 -20.865 22.945 1.00 71.67 C ANISOU 841 C PRO A 142 12167 8059 7005 -3838 2292 -249 C ATOM 842 O PRO A 142 22.212 -20.702 22.693 1.00 73.01 O ANISOU 842 O PRO A 142 12417 8159 7164 -3801 2145 -289 O ATOM 843 CB PRO A 142 20.749 -23.348 23.314 1.00 68.60 C ANISOU 843 CB PRO A 142 11734 7709 6622 -3931 2209 -111 C ATOM 844 CG PRO A 142 21.864 -23.959 22.497 1.00 63.31 C ANISOU 844 CG PRO A 142 11030 6998 6028 -3878 2004 -114 C ATOM 845 CD PRO A 142 21.423 -23.764 21.071 1.00 62.20 C ANISOU 845 CD PRO A 142 10648 6926 6058 -3800 1981 -114 C ATOM 846 N HIS A 143 20.282 -19.953 23.606 1.00 78.35 N ANISOU 846 N HIS A 143 13071 8916 7780 -3855 2479 -276 N ATOM 847 CA HIS A 143 20.889 -18.680 24.031 1.00 79.77 C ANISOU 847 CA HIS A 143 13436 9008 7867 -3836 2509 -364 C ATOM 848 C HIS A 143 20.479 -18.298 25.447 1.00 78.87 C ANISOU 848 C HIS A 143 13526 8865 7577 -3892 2685 -378 C ATOM 849 O HIS A 143 19.659 -17.399 25.641 1.00 77.66 O ANISOU 849 O HIS A 143 13348 8748 7411 -3865 2872 -404 O ATOM 850 CB HIS A 143 20.586 -17.561 23.091 1.00 74.26 C ANISOU 850 CB HIS A 143 12602 8334 7282 -3764 2550 -407 C ATOM 851 CG HIS A 143 21.470 -16.384 23.314 1.00 68.16 C ANISOU 851 CG HIS A 143 12016 7451 6432 -3743 2524 -492 C ATOM 852 ND1 HIS A 143 22.726 -16.509 23.867 1.00 64.88 N ANISOU 852 ND1 HIS A 143 11817 6932 5901 -3766 2387 -518 N ATOM 853 CD2 HIS A 143 21.281 -15.065 23.094 1.00 67.61 C ANISOU 853 CD2 HIS A 143 11958 7353 6378 -3703 2616 -550 C ATOM 854 CE1 HIS A 143 23.284 -15.318 23.957 1.00 65.29 C ANISOU 854 CE1 HIS A 143 12008 6899 5902 -3743 2386 -587 C ATOM 855 NE2 HIS A 143 22.427 -14.424 23.498 1.00 67.54 N ANISOU 855 NE2 HIS A 143 12178 7221 6263 -3706 2527 -610 N ATOM 856 N GLN A 144 21.108 -18.943 26.427 1.00 83.75 N ANISOU 856 N GLN A 144 14351 9417 8054 -3958 2622 -362 N ATOM 857 CA GLN A 144 20.923 -18.635 27.839 1.00 86.39 C ANISOU 857 CA GLN A 144 14920 9710 8193 -4011 2758 -374 C ATOM 858 C GLN A 144 22.287 -18.345 28.438 1.00 86.35 C ANISOU 858 C GLN A 144 15197 9555 8055 -4040 2611 -424 C ATOM 859 O GLN A 144 23.190 -19.185 28.354 1.00 87.53 O ANISOU 859 O GLN A 144 15388 9663 8207 -4069 2420 -395 O ATOM 860 CB GLN A 144 20.239 -19.793 28.569 1.00 90.10 C ANISOU 860 CB GLN A 144 15376 10252 8604 -4081 2826 -284 C ATOM 861 CG GLN A 144 19.677 -19.448 29.920 1.00 95.29 C ANISOU 861 CG GLN A 144 16210 10920 9076 -4115 3019 -286 C ATOM 862 CD GLN A 144 18.759 -20.539 30.445 1.00103.20 C ANISOU 862 CD GLN A 144 17132 12030 10050 -4175 3115 -184 C ATOM 863 OE1 GLN A 144 18.952 -21.724 30.153 1.00103.32 O ANISOU 863 OE1 GLN A 144 17075 12055 10128 -4223 2983 -114 O ATOM 864 NE2 GLN A 144 17.771 -20.148 31.249 1.00109.62 N ANISOU 864 NE2 GLN A 144 17961 12926 10762 -4167 3349 -175 N ATOM 865 N HIS A 145 22.438 -17.154 29.016 1.00 84.92 N ANISOU 865 N HIS A 145 15206 9296 7762 -4026 2697 -496 N ATOM 866 CA HIS A 145 23.712 -16.739 29.595 1.00 79.97 C ANISOU 866 CA HIS A 145 14863 8517 7004 -4056 2554 -542 C ATOM 867 C HIS A 145 24.122 -17.700 30.701 1.00 69.50 C ANISOU 867 C HIS A 145 13731 7147 5529 -4148 2480 -489 C ATOM 868 O HIS A 145 23.373 -17.899 31.653 1.00 68.01 O ANISOU 868 O HIS A 145 13618 6996 5225 -4186 2634 -459 O ATOM 869 CB HIS A 145 23.589 -15.312 30.129 1.00 81.45 C ANISOU 869 CB HIS A 145 15230 8630 7086 -4024 2689 -619 C ATOM 870 CG HIS A 145 24.695 -14.902 31.052 1.00 86.29 C ANISOU 870 CG HIS A 145 16181 9080 7524 -4071 2570 -653 C ATOM 871 ND1 HIS A 145 24.478 -14.118 32.165 1.00 90.73 N ANISOU 871 ND1 HIS A 145 16981 9581 7912 -4068 2701 -688 N ATOM 872 CD2 HIS A 145 26.025 -15.157 31.030 1.00 87.68 C ANISOU 872 CD2 HIS A 145 16492 9152 7671 -4109 2325 -653 C ATOM 873 CE1 HIS A 145 25.623 -13.908 32.791 1.00 91.18 C ANISOU 873 CE1 HIS A 145 17316 9482 7847 -4118 2531 -702 C ATOM 874 NE2 HIS A 145 26.578 -14.529 32.123 1.00 89.84 N ANISOU 874 NE2 HIS A 145 17091 9283 7762 -4150 2300 -682 N ATOM 875 N GLY A 146 25.309 -18.303 30.564 1.00 64.82 N ANISOU 875 N GLY A 146 13205 6487 4935 -4173 2245 -471 N ATOM 876 CA GLY A 146 25.799 -19.337 31.449 1.00 65.58 C ANISOU 876 CA GLY A 146 13459 6542 4915 -4258 2138 -409 C ATOM 877 C GLY A 146 25.766 -20.737 30.853 1.00 74.80 C ANISOU 877 C GLY A 146 14424 7793 6206 -4263 2042 -328 C ATOM 878 O GLY A 146 26.645 -21.550 31.166 1.00 64.65 O ANISOU 878 O GLY A 146 13234 6456 4874 -4302 1867 -281 O ATOM 879 N LYS A 147 24.776 -21.034 29.993 1.00 72.92 N ANISOU 879 N LYS A 147 13907 7677 6124 -4220 2146 -304 N ATOM 880 CA LYS A 147 24.562 -22.373 29.445 1.00 77.47 C ANISOU 880 CA LYS A 147 14292 8328 6816 -4226 2078 -222 C ATOM 881 C LYS A 147 24.850 -22.518 27.951 1.00 79.16 C ANISOU 881 C LYS A 147 14252 8592 7233 -4129 1970 -228 C ATOM 882 O LYS A 147 25.049 -23.651 27.497 1.00 82.81 O ANISOU 882 O LYS A 147 14600 9082 7783 -4124 1865 -166 O ATOM 883 CB LYS A 147 23.108 -22.843 29.670 1.00 85.66 C ANISOU 883 CB LYS A 147 15201 9476 7871 -4262 2272 -164 C ATOM 884 CG LYS A 147 22.663 -23.185 31.106 1.00 91.97 C ANISOU 884 CG LYS A 147 16195 10269 8483 -4360 2383 -117 C ATOM 885 CD LYS A 147 21.225 -23.754 31.098 1.00 95.38 C ANISOU 885 CD LYS A 147 16436 10840 8965 -4378 2562 -43 C ATOM 886 CE LYS A 147 20.592 -23.780 32.492 1.00104.47 C ANISOU 886 CE LYS A 147 17754 12018 9924 -4450 2730 -5 C ATOM 887 NZ LYS A 147 20.516 -22.419 33.141 1.00108.67 N ANISOU 887 NZ LYS A 147 18446 12518 10324 -4414 2871 -90 N ATOM 888 N THR A 148 24.826 -21.427 27.174 1.00 76.70 N ANISOU 888 N THR A 148 13848 8294 7001 -4050 2002 -295 N ATOM 889 CA THR A 148 25.049 -21.497 25.723 1.00 70.73 C ANISOU 889 CA THR A 148 12846 7594 6433 -3952 1908 -296 C ATOM 890 C THR A 148 26.221 -22.387 25.338 1.00 70.78 C ANISOU 890 C THR A 148 12830 7574 6488 -3918 1700 -254 C ATOM 891 O THR A 148 26.108 -23.208 24.423 1.00 72.72 O ANISOU 891 O THR A 148 12876 7878 6877 -3873 1644 -212 O ATOM 892 CB THR A 148 25.276 -20.104 25.167 1.00 60.51 C ANISOU 892 CB THR A 148 11535 6284 5172 -3882 1925 -373 C ATOM 893 OG1 THR A 148 26.021 -19.364 26.136 1.00 66.94 O ANISOU 893 OG1 THR A 148 12623 6991 5820 -3916 1904 -419 O ATOM 894 CG2 THR A 148 24.003 -19.427 24.918 1.00 58.40 C ANISOU 894 CG2 THR A 148 11151 6080 4958 -3874 2115 -395 C ATOM 895 N GLY A 149 27.358 -22.228 26.002 1.00 69.72 N ANISOU 895 N GLY A 149 12897 7352 6243 -3931 1584 -260 N ATOM 896 CA GLY A 149 28.526 -23.003 25.635 1.00 69.86 C ANISOU 896 CA GLY A 149 12872 7348 6325 -3881 1392 -207 C ATOM 897 C GLY A 149 28.246 -24.489 25.597 1.00 71.32 C ANISOU 897 C GLY A 149 12977 7556 6566 -3917 1362 -131 C ATOM 898 O GLY A 149 28.385 -25.139 24.554 1.00 71.14 O ANISOU 898 O GLY A 149 12750 7575 6703 -3846 1298 -101 O ATOM 899 N ARG A 150 27.802 -25.018 26.736 1.00 70.70 N ANISOU 899 N ARG A 150 13063 7447 6353 -4030 1417 -97 N ATOM 900 CA ARG A 150 27.569 -26.449 26.859 1.00 63.82 C ANISOU 900 CA ARG A 150 12147 6584 5516 -4080 1383 -14 C ATOM 901 C ARG A 150 26.384 -26.896 26.022 1.00 61.85 C ANISOU 901 C ARG A 150 11667 6433 5401 -4066 1488 4 C ATOM 902 O ARG A 150 26.464 -27.922 25.341 1.00 59.78 O ANISOU 902 O ARG A 150 11266 6189 5261 -4038 1414 54 O ATOM 903 CB ARG A 150 27.347 -26.805 28.317 1.00 63.22 C ANISOU 903 CB ARG A 150 12310 6457 5254 -4209 1422 23 C ATOM 904 CG ARG A 150 27.785 -28.193 28.715 1.00 69.89 C ANISOU 904 CG ARG A 150 13206 7258 6093 -4262 1302 116 C ATOM 905 CD ARG A 150 27.517 -28.415 30.220 1.00 77.63 C ANISOU 905 CD ARG A 150 14440 8189 6868 -4398 1348 154 C ATOM 906 NE ARG A 150 26.313 -27.685 30.637 1.00 79.32 N ANISOU 906 NE ARG A 150 14672 8462 7005 -4440 1564 116 N ATOM 907 CZ ARG A 150 25.080 -28.197 30.661 1.00 77.51 C ANISOU 907 CZ ARG A 150 14328 8318 6805 -4484 1710 164 C ATOM 908 NH1 ARG A 150 24.859 -29.468 30.280 1.00 74.54 N ANISOU 908 NH1 ARG A 150 13825 7968 6527 -4502 1658 246 N ATOM 909 NH2 ARG A 150 24.062 -27.421 31.049 1.00 75.57 N ANISOU 909 NH2 ARG A 150 14087 8132 6496 -4503 1913 134 N ATOM 910 N GLN A 151 25.276 -26.149 26.060 1.00 63.08 N ANISOU 910 N GLN A 151 11778 6649 5540 -4082 1658 -32 N ATOM 911 CA GLN A 151 24.087 -26.553 25.310 1.00 67.51 C ANISOU 911 CA GLN A 151 12114 7309 6228 -4073 1753 -1 C ATOM 912 C GLN A 151 24.369 -26.642 23.813 1.00 73.39 C ANISOU 912 C GLN A 151 12639 8088 7156 -3965 1661 -15 C ATOM 913 O GLN A 151 23.883 -27.558 23.136 1.00 76.81 O ANISOU 913 O GLN A 151 12916 8567 7702 -3959 1645 35 O ATOM 914 CB GLN A 151 22.940 -25.588 25.589 1.00 68.13 C ANISOU 914 CB GLN A 151 12169 7447 6269 -4092 1950 -32 C ATOM 915 CG GLN A 151 22.390 -25.683 27.001 1.00 71.88 C ANISOU 915 CG GLN A 151 12822 7914 6577 -4196 2078 1 C ATOM 916 CD GLN A 151 20.986 -25.115 27.115 1.00 76.44 C ANISOU 916 CD GLN A 151 13293 8588 7162 -4204 2297 8 C ATOM 917 OE1 GLN A 151 20.684 -24.065 26.550 1.00 75.75 O ANISOU 917 OE1 GLN A 151 13114 8531 7135 -4137 2367 -51 O ATOM 918 NE2 GLN A 151 20.120 -25.813 27.835 1.00 81.27 N ANISOU 918 NE2 GLN A 151 13907 9255 7716 -4281 2407 87 N ATOM 919 N VAL A 152 25.164 -25.706 23.278 1.00 77.39 N ANISOU 919 N VAL A 152 13139 8574 7691 -3879 1598 -79 N ATOM 920 CA VAL A 152 25.622 -25.797 21.888 1.00 69.88 C ANISOU 920 CA VAL A 152 11998 7652 6902 -3771 1499 -88 C ATOM 921 C VAL A 152 26.530 -27.007 21.701 1.00 68.24 C ANISOU 921 C VAL A 152 11783 7398 6747 -3752 1356 -34 C ATOM 922 O VAL A 152 26.317 -27.827 20.798 1.00 61.21 O ANISOU 922 O VAL A 152 10734 6538 5983 -3718 1321 -3 O ATOM 923 CB VAL A 152 26.340 -24.500 21.473 1.00 51.98 C ANISOU 923 CB VAL A 152 9737 5371 4644 -3688 1466 -155 C ATOM 924 CG1 VAL A 152 27.357 -24.784 20.412 1.00 50.22 C ANISOU 924 CG1 VAL A 152 9390 5144 4548 -3583 1324 -146 C ATOM 925 CG2 VAL A 152 25.342 -23.498 20.991 1.00 51.86 C ANISOU 925 CG2 VAL A 152 9619 5418 4668 -3671 1589 -199 C ATOM 926 N ALA A 153 27.566 -27.122 22.548 1.00 63.14 N ANISOU 926 N ALA A 153 11313 6671 6008 -3773 1268 -21 N ATOM 927 CA ALA A 153 28.510 -28.221 22.444 1.00 53.11 C ANISOU 927 CA ALA A 153 10039 5344 4797 -3751 1130 35 C ATOM 928 C ALA A 153 27.785 -29.542 22.390 1.00 54.04 C ANISOU 928 C ALA A 153 10098 5475 4961 -3810 1150 97 C ATOM 929 O ALA A 153 28.258 -30.481 21.746 1.00 58.57 O ANISOU 929 O ALA A 153 10578 6024 5653 -3768 1062 133 O ATOM 930 CB ALA A 153 29.480 -28.184 23.620 1.00 53.99 C ANISOU 930 CB ALA A 153 10372 5364 4777 -3796 1047 57 C ATOM 931 N MET A 154 26.607 -29.611 23.016 1.00 59.72 N ANISOU 931 N MET A 154 10859 6233 5599 -3906 1274 113 N ATOM 932 CA MET A 154 25.863 -30.863 23.103 1.00 64.57 C ANISOU 932 CA MET A 154 11430 6859 6244 -3978 1297 186 C ATOM 933 C MET A 154 25.314 -31.306 21.753 1.00 64.01 C ANISOU 933 C MET A 154 11130 6847 6342 -3920 1299 190 C ATOM 934 O MET A 154 25.175 -32.512 21.519 1.00 63.71 O ANISOU 934 O MET A 154 11044 6791 6371 -3947 1257 248 O ATOM 935 CB MET A 154 24.713 -30.733 24.109 1.00 66.13 C ANISOU 935 CB MET A 154 11711 7095 6319 -4091 1444 210 C ATOM 936 CG MET A 154 25.113 -30.723 25.585 1.00 63.51 C ANISOU 936 CG MET A 154 11633 6696 5803 -4182 1440 232 C ATOM 937 SD MET A 154 25.964 -32.220 26.108 1.00 63.50 S ANISOU 937 SD MET A 154 11742 6597 5787 -4236 1284 322 S ATOM 938 CE MET A 154 24.776 -33.489 25.698 1.00 62.69 C ANISOU 938 CE MET A 154 11485 6549 5784 -4293 1344 403 C ATOM 939 N GLY A 155 24.980 -30.359 20.869 1.00 66.36 N ANISOU 939 N GLY A 155 11298 7210 6707 -3846 1345 132 N ATOM 940 CA GLY A 155 24.409 -30.676 19.573 1.00 65.95 C ANISOU 940 CA GLY A 155 11041 7215 6802 -3796 1344 135 C ATOM 941 C GLY A 155 23.298 -29.748 19.114 1.00 64.24 C ANISOU 941 C GLY A 155 10707 7088 6613 -3786 1457 107 C ATOM 942 O GLY A 155 22.861 -29.836 17.966 1.00 63.43 O ANISOU 942 O GLY A 155 10454 7033 6614 -3754 1450 99 O ATOM 943 N LEU A 156 22.820 -28.863 19.981 1.00 61.34 N ANISOU 943 N LEU A 156 10424 6740 6141 -3832 1566 88 N ATOM 944 CA LEU A 156 21.796 -27.917 19.561 1.00 60.88 C ANISOU 944 CA LEU A 156 10248 6762 6123 -3816 1678 65 C ATOM 945 C LEU A 156 22.372 -26.909 18.565 1.00 66.14 C ANISOU 945 C LEU A 156 10838 7434 6856 -3708 1623 -4 C ATOM 946 O LEU A 156 23.284 -26.140 18.895 1.00 64.77 O ANISOU 946 O LEU A 156 10777 7213 6618 -3674 1590 -56 O ATOM 947 CB LEU A 156 21.214 -27.199 20.768 1.00 60.91 C ANISOU 947 CB LEU A 156 10369 6776 5998 -3885 1823 59 C ATOM 948 CG LEU A 156 20.182 -27.926 21.632 1.00 65.44 C ANISOU 948 CG LEU A 156 10960 7385 6519 -3990 1934 138 C ATOM 949 CD1 LEU A 156 19.287 -26.919 22.342 1.00 69.15 C ANISOU 949 CD1 LEU A 156 11452 7907 6914 -4021 2117 127 C ATOM 950 CD2 LEU A 156 19.348 -28.914 20.829 1.00 66.74 C ANISOU 950 CD2 LEU A 156 10938 7606 6813 -4004 1922 212 C ATOM 951 N ALA A 157 21.838 -26.940 17.343 1.00 67.13 N ANISOU 951 N ALA A 157 10778 7617 7111 -3661 1608 4 N ATOM 952 CA ALA A 157 22.108 -26.011 16.251 1.00 55.26 C ANISOU 952 CA ALA A 157 9172 6138 5686 -3567 1569 -45 C ATOM 953 C ALA A 157 20.931 -26.116 15.285 1.00 60.69 C ANISOU 953 C ALA A 157 9675 6902 6482 -3572 1607 -12 C ATOM 954 O ALA A 157 20.002 -26.882 15.523 1.00 76.16 O ANISOU 954 O ALA A 157 11591 8892 8454 -3644 1661 49 O ATOM 955 CB ALA A 157 23.423 -26.348 15.586 1.00 48.84 C ANISOU 955 CB ALA A 157 8385 5278 4892 -3508 1438 -78 C ATOM 956 N GLY A 158 20.948 -25.351 14.200 1.00 49.30 N ANISOU 956 N GLY A 158 8137 5491 5105 -3513 1580 -50 N ATOM 957 CA GLY A 158 19.875 -25.492 13.218 1.00 49.70 C ANISOU 957 CA GLY A 158 8029 5608 5244 -3536 1603 -20 C ATOM 958 C GLY A 158 19.690 -24.293 12.310 1.00 58.56 C ANISOU 958 C GLY A 158 9048 6768 6433 -3472 1601 -48 C ATOM 959 O GLY A 158 19.694 -23.162 12.794 1.00 70.30 O ANISOU 959 O GLY A 158 10546 8252 7913 -3427 1651 -61 O ATOM 960 N LEU A 159 19.504 -24.503 11.009 1.00 55.74 N ANISOU 960 N LEU A 159 8595 6443 6139 -3471 1545 -54 N ATOM 961 CA LEU A 159 19.568 -23.423 10.034 1.00 47.42 C ANISOU 961 CA LEU A 159 7462 5416 5140 -3410 1516 -82 C ATOM 962 C LEU A 159 18.199 -22.861 9.688 1.00 57.72 C ANISOU 962 C LEU A 159 8609 6784 6537 -3425 1584 -26 C ATOM 963 O LEU A 159 17.180 -23.549 9.744 1.00 67.03 O ANISOU 963 O LEU A 159 9711 8001 7755 -3490 1629 37 O ATOM 964 CB LEU A 159 20.223 -23.893 8.745 1.00 46.62 C ANISOU 964 CB LEU A 159 7353 5315 5046 -3398 1415 -119 C ATOM 965 CG LEU A 159 21.547 -24.611 8.940 1.00 46.05 C ANISOU 965 CG LEU A 159 7410 5185 4903 -3384 1350 -159 C ATOM 966 CD1 LEU A 159 21.947 -25.335 7.678 1.00 45.72 C ANISOU 966 CD1 LEU A 159 7346 5150 4874 -3390 1277 -180 C ATOM 967 CD2 LEU A 159 22.611 -23.645 9.381 1.00 45.02 C ANISOU 967 CD2 LEU A 159 7357 5015 4732 -3312 1332 -202 C ATOM 968 N VAL A 160 18.200 -21.595 9.306 1.00 52.35 N ANISOU 968 N VAL A 160 7876 6114 5901 -3366 1587 -40 N ATOM 969 CA VAL A 160 17.063 -20.913 8.719 1.00 52.31 C ANISOU 969 CA VAL A 160 7707 6166 6002 -3366 1628 15 C ATOM 970 C VAL A 160 17.479 -20.499 7.317 1.00 54.90 C ANISOU 970 C VAL A 160 7992 6501 6367 -3334 1527 -17 C ATOM 971 O VAL A 160 18.543 -19.897 7.124 1.00 53.22 O ANISOU 971 O VAL A 160 7856 6252 6113 -3276 1472 -76 O ATOM 972 CB VAL A 160 16.656 -19.687 9.551 1.00 50.45 C ANISOU 972 CB VAL A 160 7474 5934 5761 -3356 1745 15 C ATOM 973 CG1 VAL A 160 15.360 -19.076 9.037 1.00 49.64 C ANISOU 973 CG1 VAL A 160 7198 5897 5766 -3381 1812 79 C ATOM 974 CG2 VAL A 160 16.563 -20.075 10.995 1.00 52.51 C ANISOU 974 CG2 VAL A 160 7851 6180 5921 -3412 1854 9 C ATOM 975 N VAL A 161 16.644 -20.818 6.349 1.00 53.39 N ANISOU 975 N VAL A 161 7680 6358 6250 -3374 1504 28 N ATOM 976 CA VAL A 161 16.906 -20.518 4.959 1.00 51.73 C ANISOU 976 CA VAL A 161 7426 6160 6067 -3358 1412 8 C ATOM 977 C VAL A 161 15.841 -19.521 4.527 1.00 50.80 C ANISOU 977 C VAL A 161 7149 6082 6071 -3351 1442 76 C ATOM 978 O VAL A 161 14.660 -19.882 4.421 1.00 53.64 O ANISOU 978 O VAL A 161 7386 6486 6510 -3404 1482 152 O ATOM 979 CB VAL A 161 16.869 -21.794 4.112 1.00 47.88 C ANISOU 979 CB VAL A 161 6944 5690 5558 -3421 1349 5 C ATOM 980 CG1 VAL A 161 16.872 -21.466 2.653 1.00 48.30 C ANISOU 980 CG1 VAL A 161 6938 5770 5644 -3419 1270 0 C ATOM 981 CG2 VAL A 161 18.038 -22.668 4.468 1.00 46.64 C ANISOU 981 CG2 VAL A 161 6938 5486 5294 -3416 1317 -58 C ATOM 982 N ILE A 162 16.237 -18.264 4.295 1.00 46.53 N ANISOU 982 N ILE A 162 6600 5524 5555 -3288 1424 58 N ATOM 983 CA ILE A 162 15.312 -17.224 3.844 1.00 52.15 C ANISOU 983 CA ILE A 162 7158 6262 6393 -3275 1443 126 C ATOM 984 C ILE A 162 15.387 -17.077 2.330 1.00 49.56 C ANISOU 984 C ILE A 162 6779 5951 6099 -3286 1336 126 C ATOM 985 O ILE A 162 16.480 -16.905 1.769 1.00 47.39 O ANISOU 985 O ILE A 162 6600 5654 5753 -3255 1260 61 O ATOM 986 CB ILE A 162 15.614 -15.879 4.517 1.00 46.68 C ANISOU 986 CB ILE A 162 6504 5537 5696 -3230 1500 101 C ATOM 987 CG1 ILE A 162 15.750 -16.056 6.017 1.00 47.29 C ANISOU 987 CG1 ILE A 162 6698 5594 5675 -3253 1618 62 C ATOM 988 CG2 ILE A 162 14.544 -14.857 4.159 1.00 47.79 C ANISOU 988 CG2 ILE A 162 6502 5711 5947 -3262 1554 159 C ATOM 989 CD1 ILE A 162 15.857 -14.751 6.725 1.00 47.63 C ANISOU 989 CD1 ILE A 162 6802 5605 5688 -3252 1713 18 C ATOM 990 N GLU A 163 14.223 -17.102 1.679 1.00 49.83 N ANISOU 990 N GLU A 163 6660 6028 6245 -3330 1335 207 N ATOM 991 CA GLU A 163 14.091 -16.873 0.246 1.00 56.43 C ANISOU 991 CA GLU A 163 7433 6882 7126 -3350 1238 222 C ATOM 992 C GLU A 163 13.291 -15.599 0.002 1.00 57.61 C ANISOU 992 C GLU A 163 7429 7033 7426 -3326 1254 300 C ATOM 993 O GLU A 163 12.218 -15.427 0.580 1.00 61.14 O ANISOU 993 O GLU A 163 7750 7504 7978 -3343 1342 378 O ATOM 994 CB GLU A 163 13.392 -18.045 -0.458 1.00 61.40 C ANISOU 994 CB GLU A 163 8012 7551 7766 -3436 1204 254 C ATOM 995 CG GLU A 163 14.102 -19.400 -0.385 1.00 70.00 C ANISOU 995 CG GLU A 163 9242 8635 8722 -3471 1180 186 C ATOM 996 CD GLU A 163 13.360 -20.486 -1.172 1.00 82.28 C ANISOU 996 CD GLU A 163 10745 10223 10293 -3563 1140 221 C ATOM 997 OE1 GLU A 163 12.162 -20.291 -1.490 1.00 86.24 O ANISOU 997 OE1 GLU A 163 11093 10755 10920 -3604 1150 307 O ATOM 998 OE2 GLU A 163 13.979 -21.532 -1.485 1.00 86.17 O ANISOU 998 OE2 GLU A 163 11349 10709 10682 -3596 1098 166 O ATOM 999 N ASP A 164 13.811 -14.702 -0.835 1.00 59.23 N ANISOU 999 N ASP A 164 7644 7219 7643 -3295 1175 282 N ATOM 1000 CA ASP A 164 12.996 -13.641 -1.408 1.00 65.12 C ANISOU 1000 CA ASP A 164 8232 7963 8547 -3290 1159 363 C ATOM 1001 C ASP A 164 12.901 -13.896 -2.904 1.00 71.47 C ANISOU 1001 C ASP A 164 9011 8791 9353 -3342 1049 369 C ATOM 1002 O ASP A 164 13.554 -14.792 -3.442 1.00 71.43 O ANISOU 1002 O ASP A 164 9120 8804 9215 -3373 993 307 O ATOM 1003 CB ASP A 164 13.553 -12.233 -1.103 1.00 64.36 C ANISOU 1003 CB ASP A 164 8182 7827 8443 -3256 1174 332 C ATOM 1004 CG ASP A 164 14.998 -12.035 -1.551 1.00 65.84 C ANISOU 1004 CG ASP A 164 8505 7973 8538 -3183 1078 260 C ATOM 1005 OD1 ASP A 164 15.479 -12.844 -2.354 1.00 69.03 O ANISOU 1005 OD1 ASP A 164 8979 8406 8843 -3218 1013 217 O ATOM 1006 OD2 ASP A 164 15.667 -11.069 -1.103 1.00 66.12 O ANISOU 1006 OD2 ASP A 164 8614 7966 8542 -3150 1092 220 O ATOM 1007 N ASP A 165 12.068 -13.105 -3.578 1.00 79.96 N ANISOU 1007 N ASP A 165 9936 9865 10580 -3355 1020 446 N ATOM 1008 CA ASP A 165 11.868 -13.300 -5.011 1.00 86.62 C ANISOU 1008 CA ASP A 165 10754 10733 11424 -3415 914 456 C ATOM 1009 C ASP A 165 13.142 -13.011 -5.799 1.00 80.35 C ANISOU 1009 C ASP A 165 10108 9931 10490 -3395 825 382 C ATOM 1010 O ASP A 165 13.423 -13.684 -6.803 1.00 81.38 O ANISOU 1010 O ASP A 165 10305 10098 10518 -3449 750 353 O ATOM 1011 CB ASP A 165 10.719 -12.415 -5.488 1.00100.72 C ANISOU 1011 CB ASP A 165 12345 12510 13415 -3434 906 552 C ATOM 1012 CG ASP A 165 10.781 -11.022 -4.892 1.00113.76 C ANISOU 1012 CG ASP A 165 13971 14134 15117 -3419 956 562 C ATOM 1013 OD1 ASP A 165 11.073 -10.910 -3.674 1.00115.94 O ANISOU 1013 OD1 ASP A 165 14306 14404 15342 -3391 1054 534 O ATOM 1014 OD2 ASP A 165 10.565 -10.042 -5.646 1.00119.13 O ANISOU 1014 OD2 ASP A 165 14586 14798 15880 -3442 897 592 O ATOM 1015 N GLU A 166 13.917 -12.009 -5.358 1.00 73.34 N ANISOU 1015 N GLU A 166 9272 8997 9596 -3321 834 355 N ATOM 1016 CA GLU A 166 15.161 -11.634 -6.028 1.00 72.46 C ANISOU 1016 CA GLU A 166 9290 8878 9364 -3298 760 293 C ATOM 1017 C GLU A 166 16.038 -12.848 -6.292 1.00 70.61 C ANISOU 1017 C GLU A 166 9201 8680 8945 -3323 741 214 C ATOM 1018 O GLU A 166 16.511 -13.064 -7.415 1.00 78.12 O ANISOU 1018 O GLU A 166 10213 9664 9807 -3358 669 192 O ATOM 1019 CB GLU A 166 15.931 -10.616 -5.183 1.00 70.54 C ANISOU 1019 CB GLU A 166 9098 8576 9129 -3216 790 266 C ATOM 1020 CG GLU A 166 17.351 -10.328 -5.692 1.00 73.89 C ANISOU 1020 CG GLU A 166 9662 8992 9420 -3187 728 199 C ATOM 1021 CD GLU A 166 18.170 -9.471 -4.724 1.00 75.87 C ANISOU 1021 CD GLU A 166 9978 9181 9668 -3111 760 165 C ATOM 1022 OE1 GLU A 166 18.307 -9.912 -3.550 1.00 77.31 O ANISOU 1022 OE1 GLU A 166 10208 9350 9817 -3086 835 132 O ATOM 1023 OE2 GLU A 166 18.672 -8.382 -5.137 1.00 72.39 O ANISOU 1023 OE2 GLU A 166 9546 8705 9255 -3084 706 173 O ATOM 1024 N ILE A 167 16.237 -13.671 -5.268 1.00 67.97 N ANISOU 1024 N ILE A 167 8926 8342 8556 -3309 812 175 N ATOM 1025 CA ILE A 167 17.247 -14.710 -5.358 1.00 65.35 C ANISOU 1025 CA ILE A 167 8738 8027 8065 -3317 802 94 C ATOM 1026 C ILE A 167 16.749 -15.877 -6.192 1.00 64.39 C ANISOU 1026 C ILE A 167 8612 7952 7902 -3402 769 102 C ATOM 1027 O ILE A 167 17.545 -16.574 -6.832 1.00 67.76 O ANISOU 1027 O ILE A 167 9144 8398 8204 -3424 736 46 O ATOM 1028 CB ILE A 167 17.669 -15.133 -3.942 1.00 44.08 C ANISOU 1028 CB ILE A 167 6114 5302 5333 -3275 882 52 C ATOM 1029 CG1 ILE A 167 18.987 -15.885 -3.968 1.00 43.25 C ANISOU 1029 CG1 ILE A 167 6159 5194 5082 -3261 870 -33 C ATOM 1030 CG2 ILE A 167 16.606 -15.984 -3.297 1.00 45.09 C ANISOU 1030 CG2 ILE A 167 6176 5445 5512 -3320 942 91 C ATOM 1031 CD1 ILE A 167 19.583 -16.035 -2.596 1.00 42.72 C ANISOU 1031 CD1 ILE A 167 6169 5085 4979 -3211 933 -74 C ATOM 1032 N LEU A 168 15.441 -16.122 -6.220 1.00 62.44 N ANISOU 1032 N LEU A 168 8240 7723 7760 -3455 780 172 N ATOM 1033 CA LEU A 168 14.954 -17.177 -7.099 1.00 65.51 C ANISOU 1033 CA LEU A 168 8628 8154 8111 -3545 735 182 C ATOM 1034 C LEU A 168 15.133 -16.749 -8.544 1.00 69.10 C ANISOU 1034 C LEU A 168 9094 8636 8527 -3581 642 188 C ATOM 1035 O LEU A 168 15.611 -17.528 -9.385 1.00 75.65 O ANISOU 1035 O LEU A 168 10017 9493 9233 -3631 599 147 O ATOM 1036 CB LEU A 168 13.494 -17.497 -6.783 1.00 61.81 C ANISOU 1036 CB LEU A 168 8010 7696 7777 -3597 767 263 C ATOM 1037 CG LEU A 168 13.418 -18.102 -5.372 1.00 59.29 C ANISOU 1037 CG LEU A 168 7706 7359 7462 -3574 864 253 C ATOM 1038 CD1 LEU A 168 12.112 -17.706 -4.721 1.00 57.52 C ANISOU 1038 CD1 LEU A 168 7309 7136 7410 -3581 931 346 C ATOM 1039 CD2 LEU A 168 13.674 -19.622 -5.258 1.00 71.25 C ANISOU 1039 CD2 LEU A 168 9319 8882 8868 -3627 868 208 C ATOM 1040 N LYS A 169 14.852 -15.475 -8.830 1.00 66.52 N ANISOU 1040 N LYS A 169 8682 8296 8297 -3554 613 237 N ATOM 1041 CA LYS A 169 15.024 -15.015 -10.196 1.00 65.58 C ANISOU 1041 CA LYS A 169 8580 8204 8135 -3594 521 250 C ATOM 1042 C LYS A 169 16.489 -15.101 -10.598 1.00 67.84 C ANISOU 1042 C LYS A 169 9025 8497 8255 -3568 504 171 C ATOM 1043 O LYS A 169 16.819 -14.859 -11.762 1.00 74.81 O ANISOU 1043 O LYS A 169 9950 9409 9065 -3608 436 172 O ATOM 1044 CB LYS A 169 14.475 -13.597 -10.363 1.00 71.23 C ANISOU 1044 CB LYS A 169 9174 8893 8998 -3569 493 319 C ATOM 1045 CG LYS A 169 13.031 -13.438 -9.811 1.00 81.37 C ANISOU 1045 CG LYS A 169 10277 10161 10479 -3583 535 400 C ATOM 1046 CD LYS A 169 12.297 -12.187 -10.334 1.00 86.41 C ANISOU 1046 CD LYS A 169 10777 10776 11278 -3586 491 475 C ATOM 1047 CE LYS A 169 12.883 -10.894 -9.768 1.00 88.53 C ANISOU 1047 CE LYS A 169 11047 10984 11607 -3495 517 469 C ATOM 1048 NZ LYS A 169 12.090 -9.682 -10.130 1.00 89.33 N ANISOU 1048 NZ LYS A 169 11000 11045 11895 -3495 487 541 N ATOM 1049 N LEU A 170 17.370 -15.491 -9.671 1.00 66.21 N ANISOU 1049 N LEU A 170 8906 8266 7986 -3509 568 104 N ATOM 1050 CA LEU A 170 18.810 -15.410 -9.911 1.00 65.86 C ANISOU 1050 CA LEU A 170 8990 8218 7815 -3471 564 34 C ATOM 1051 C LEU A 170 19.404 -16.599 -10.658 1.00 70.81 C ANISOU 1051 C LEU A 170 9724 8879 8301 -3525 556 -22 C ATOM 1052 O LEU A 170 20.406 -16.416 -11.362 1.00 74.25 O ANISOU 1052 O LEU A 170 10242 9328 8642 -3521 537 -59 O ATOM 1053 CB LEU A 170 19.575 -15.231 -8.596 1.00 59.42 C ANISOU 1053 CB LEU A 170 8220 7355 7002 -3383 631 -10 C ATOM 1054 CG LEU A 170 20.051 -13.819 -8.278 1.00 50.24 C ANISOU 1054 CG LEU A 170 7042 6154 5892 -3312 624 2 C ATOM 1055 CD1 LEU A 170 20.959 -13.799 -7.067 1.00 49.01 C ANISOU 1055 CD1 LEU A 170 6959 5955 5709 -3238 681 -51 C ATOM 1056 CD2 LEU A 170 20.786 -13.320 -9.471 1.00 45.92 C ANISOU 1056 CD2 LEU A 170 6542 5631 5273 -3328 561 -4 C ATOM 1057 N MET A 171 18.842 -17.804 -10.517 1.00 68.00 N ANISOU 1057 N MET A 171 9370 8533 7933 -3578 574 -27 N ATOM 1058 CA MET A 171 19.403 -19.005 -11.158 1.00 66.73 C ANISOU 1058 CA MET A 171 9314 8392 7647 -3631 575 -84 C ATOM 1059 C MET A 171 20.741 -19.414 -10.535 1.00 60.85 C ANISOU 1059 C MET A 171 8674 7614 6831 -3567 633 -163 C ATOM 1060 O MET A 171 21.720 -19.702 -11.235 1.00 52.00 O ANISOU 1060 O MET A 171 7642 6503 5612 -3576 634 -214 O ATOM 1061 CB MET A 171 19.564 -18.817 -12.663 1.00 69.78 C ANISOU 1061 CB MET A 171 9737 8824 7954 -3697 512 -78 C ATOM 1062 CG MET A 171 18.326 -19.022 -13.469 1.00 72.60 C ANISOU 1062 CG MET A 171 10027 9216 8342 -3794 448 -14 C ATOM 1063 SD MET A 171 18.852 -19.961 -14.907 1.00 74.29 S ANISOU 1063 SD MET A 171 10368 9471 8389 -3893 419 -61 S ATOM 1064 CE MET A 171 19.635 -21.346 -14.066 1.00 75.78 C ANISOU 1064 CE MET A 171 10649 9618 8526 -3863 507 -148 C ATOM 1065 N LEU A 172 20.777 -19.416 -9.208 1.00 58.77 N ANISOU 1065 N LEU A 172 8397 7311 6623 -3506 683 -169 N ATOM 1066 CA LEU A 172 21.857 -20.026 -8.462 1.00 53.25 C ANISOU 1066 CA LEU A 172 7786 6574 5871 -3457 735 -233 C ATOM 1067 C LEU A 172 21.613 -21.519 -8.401 1.00 50.05 C ANISOU 1067 C LEU A 172 7422 6163 5432 -3514 754 -254 C ATOM 1068 O LEU A 172 20.542 -21.986 -8.786 1.00 50.12 O ANISOU 1068 O LEU A 172 7382 6196 5466 -3588 730 -215 O ATOM 1069 CB LEU A 172 21.903 -19.422 -7.070 1.00 42.84 C ANISOU 1069 CB LEU A 172 6444 5216 4619 -3382 774 -224 C ATOM 1070 CG LEU A 172 22.477 -18.026 -7.030 1.00 42.07 C ANISOU 1070 CG LEU A 172 6334 5107 4544 -3316 759 -218 C ATOM 1071 CD1 LEU A 172 22.182 -17.391 -5.726 1.00 41.79 C ANISOU 1071 CD1 LEU A 172 6260 5033 4584 -3261 795 -198 C ATOM 1072 CD2 LEU A 172 23.954 -18.186 -7.213 1.00 41.35 C ANISOU 1072 CD2 LEU A 172 6337 5001 4372 -3280 768 -278 C ATOM 1073 N PRO A 173 22.595 -22.305 -7.970 1.00 43.70 N ANISOU 1073 N PRO A 173 6704 5323 4578 -3488 794 -310 N ATOM 1074 CA PRO A 173 22.317 -23.715 -7.685 1.00 44.38 C ANISOU 1074 CA PRO A 173 6824 5388 4652 -3538 814 -322 C ATOM 1075 C PRO A 173 21.266 -23.841 -6.588 1.00 44.84 C ANISOU 1075 C PRO A 173 6817 5433 4786 -3546 832 -274 C ATOM 1076 O PRO A 173 21.395 -23.241 -5.523 1.00 51.90 O ANISOU 1076 O PRO A 173 7696 6304 5720 -3483 861 -266 O ATOM 1077 CB PRO A 173 23.686 -24.258 -7.253 1.00 43.75 C ANISOU 1077 CB PRO A 173 6835 5260 4530 -3487 854 -383 C ATOM 1078 CG PRO A 173 24.667 -23.409 -7.942 1.00 43.04 C ANISOU 1078 CG PRO A 173 6766 5185 4404 -3446 846 -410 C ATOM 1079 CD PRO A 173 24.041 -22.030 -7.965 1.00 42.80 C ANISOU 1079 CD PRO A 173 6658 5186 4418 -3424 814 -362 C ATOM 1080 N LYS A 174 20.205 -24.623 -6.851 1.00 45.95 N ANISOU 1080 N LYS A 174 6920 5590 4949 -3629 816 -238 N ATOM 1081 CA LYS A 174 19.026 -24.590 -5.994 1.00 46.60 C ANISOU 1081 CA LYS A 174 6913 5674 5120 -3649 834 -176 C ATOM 1082 C LYS A 174 18.585 -25.948 -5.468 1.00 53.59 C ANISOU 1082 C LYS A 174 7819 6533 6008 -3710 854 -166 C ATOM 1083 O LYS A 174 17.685 -26.004 -4.614 1.00 59.70 O ANISOU 1083 O LYS A 174 8524 7306 6854 -3728 883 -114 O ATOM 1084 CB LYS A 174 17.845 -23.944 -6.733 1.00 47.34 C ANISOU 1084 CB LYS A 174 6891 5815 5282 -3698 792 -109 C ATOM 1085 CG LYS A 174 17.408 -24.634 -8.014 1.00 54.97 C ANISOU 1085 CG LYS A 174 7863 6812 6211 -3794 735 -101 C ATOM 1086 CD LYS A 174 16.332 -23.807 -8.755 1.00 60.88 C ANISOU 1086 CD LYS A 174 8493 7605 7035 -3835 683 -29 C ATOM 1087 CE LYS A 174 16.057 -24.269 -10.210 1.00 63.36 C ANISOU 1087 CE LYS A 174 8830 7954 7290 -3931 612 -24 C ATOM 1088 NZ LYS A 174 15.067 -25.419 -10.297 1.00 61.81 N ANISOU 1088 NZ LYS A 174 8603 7760 7123 -4033 594 13 N ATOM 1089 N GLN A 175 19.187 -27.035 -5.932 1.00 49.64 N ANISOU 1089 N GLN A 175 7411 6011 5441 -3745 844 -211 N ATOM 1090 CA GLN A 175 18.774 -28.376 -5.535 1.00 48.68 C ANISOU 1090 CA GLN A 175 7314 5858 5325 -3812 853 -198 C ATOM 1091 C GLN A 175 19.293 -28.682 -4.147 1.00 48.29 C ANISOU 1091 C GLN A 175 7310 5756 5281 -3762 902 -209 C ATOM 1092 O GLN A 175 20.415 -29.161 -4.004 1.00 47.76 O ANISOU 1092 O GLN A 175 7337 5644 5166 -3726 914 -261 O ATOM 1093 CB GLN A 175 19.313 -29.404 -6.510 1.00 49.06 C ANISOU 1093 CB GLN A 175 7449 5887 5305 -3864 828 -244 C ATOM 1094 CG GLN A 175 19.011 -29.131 -7.936 1.00 49.43 C ANISOU 1094 CG GLN A 175 7479 5981 5320 -3916 780 -244 C ATOM 1095 CD GLN A 175 19.323 -30.341 -8.742 1.00 50.15 C ANISOU 1095 CD GLN A 175 7657 6046 5352 -3987 765 -283 C ATOM 1096 OE1 GLN A 175 18.456 -31.204 -8.947 1.00 55.96 O ANISOU 1096 OE1 GLN A 175 8379 6777 6107 -4080 738 -250 O ATOM 1097 NE2 GLN A 175 20.574 -30.440 -9.197 1.00 49.49 N ANISOU 1097 NE2 GLN A 175 7660 5939 5204 -3947 788 -352 N ATOM 1098 N TRP A 176 18.469 -28.447 -3.124 1.00 51.52 N ANISOU 1098 N TRP A 176 7653 6170 5752 -3765 935 -155 N ATOM 1099 CA TRP A 176 18.901 -28.664 -1.742 1.00 48.41 C ANISOU 1099 CA TRP A 176 7308 5729 5355 -3725 982 -159 C ATOM 1100 C TRP A 176 19.432 -30.074 -1.547 1.00 48.86 C ANISOU 1100 C TRP A 176 7460 5729 5375 -3762 978 -181 C ATOM 1101 O TRP A 176 18.829 -31.048 -2.002 1.00 49.94 O ANISOU 1101 O TRP A 176 7591 5862 5522 -3847 956 -159 O ATOM 1102 CB TRP A 176 17.752 -28.399 -0.772 1.00 49.16 C ANISOU 1102 CB TRP A 176 7315 5842 5522 -3749 1027 -89 C ATOM 1103 CG TRP A 176 18.077 -28.598 0.701 1.00 49.08 C ANISOU 1103 CG TRP A 176 7359 5789 5499 -3721 1081 -86 C ATOM 1104 CD1 TRP A 176 17.874 -29.717 1.433 1.00 49.97 C ANISOU 1104 CD1 TRP A 176 7513 5868 5607 -3777 1099 -60 C ATOM 1105 CD2 TRP A 176 18.681 -27.648 1.596 1.00 48.13 C ANISOU 1105 CD2 TRP A 176 7268 5654 5364 -3638 1117 -106 C ATOM 1106 NE1 TRP A 176 18.288 -29.526 2.728 1.00 49.68 N ANISOU 1106 NE1 TRP A 176 7529 5798 5549 -3737 1145 -60 N ATOM 1107 CE2 TRP A 176 18.789 -28.260 2.846 1.00 50.97 C ANISOU 1107 CE2 TRP A 176 7688 5972 5705 -3652 1156 -91 C ATOM 1108 CE3 TRP A 176 19.139 -26.337 1.456 1.00 47.39 C ANISOU 1108 CE3 TRP A 176 7161 5575 5272 -3560 1116 -133 C ATOM 1109 CZ2 TRP A 176 19.334 -27.614 3.934 1.00 51.79 C ANISOU 1109 CZ2 TRP A 176 7844 6051 5785 -3592 1194 -105 C ATOM 1110 CZ3 TRP A 176 19.677 -25.706 2.534 1.00 46.43 C ANISOU 1110 CZ3 TRP A 176 7085 5424 5132 -3499 1153 -147 C ATOM 1111 CH2 TRP A 176 19.777 -26.338 3.750 1.00 46.86 C ANISOU 1111 CH2 TRP A 176 7205 5440 5162 -3515 1192 -135 C ATOM 1112 N GLY A 177 20.583 -30.176 -0.886 1.00 51.13 N ANISOU 1112 N GLY A 177 7834 5966 5627 -3700 994 -221 N ATOM 1113 CA GLY A 177 21.227 -31.447 -0.665 1.00 48.48 C ANISOU 1113 CA GLY A 177 7587 5563 5270 -3724 987 -238 C ATOM 1114 C GLY A 177 21.929 -32.031 -1.862 1.00 48.44 C ANISOU 1114 C GLY A 177 7630 5540 5236 -3735 958 -288 C ATOM 1115 O GLY A 177 22.573 -33.064 -1.716 1.00 48.77 O ANISOU 1115 O GLY A 177 7743 5513 5273 -3747 954 -305 O ATOM 1116 N ILE A 178 21.846 -31.404 -3.034 1.00 52.64 N ANISOU 1116 N ILE A 178 8127 6125 5750 -3734 939 -309 N ATOM 1117 CA ILE A 178 22.559 -31.897 -4.209 1.00 56.02 C ANISOU 1117 CA ILE A 178 8606 6538 6140 -3748 923 -360 C ATOM 1118 C ILE A 178 23.696 -30.965 -4.631 1.00 55.50 C ANISOU 1118 C ILE A 178 8557 6485 6046 -3663 934 -408 C ATOM 1119 O ILE A 178 24.878 -31.315 -4.513 1.00 46.56 O ANISOU 1119 O ILE A 178 7483 5299 4910 -3618 951 -447 O ATOM 1120 CB ILE A 178 21.583 -32.116 -5.368 1.00 49.07 C ANISOU 1120 CB ILE A 178 7690 5705 5251 -3838 888 -345 C ATOM 1121 CG1 ILE A 178 20.629 -33.227 -4.977 1.00 50.41 C ANISOU 1121 CG1 ILE A 178 7851 5847 5454 -3928 876 -298 C ATOM 1122 CG2 ILE A 178 22.354 -32.448 -6.654 1.00 49.07 C ANISOU 1122 CG2 ILE A 178 7749 5697 5199 -3852 881 -404 C ATOM 1123 CD1 ILE A 178 20.026 -33.955 -6.155 1.00 63.92 C ANISOU 1123 CD1 ILE A 178 9569 7569 7150 -4030 836 -297 C ATOM 1124 N ASP A 179 23.343 -29.794 -5.166 1.00 52.76 N ANISOU 1124 N ASP A 179 8152 6205 5689 -3646 922 -400 N ATOM 1125 CA ASP A 179 24.306 -28.756 -5.506 1.00 46.76 C ANISOU 1125 CA ASP A 179 7397 5463 4908 -3571 929 -434 C ATOM 1126 C ASP A 179 24.082 -27.497 -4.671 1.00 49.17 C ANISOU 1126 C ASP A 179 7649 5791 5242 -3508 933 -405 C ATOM 1127 O ASP A 179 24.661 -26.448 -4.972 1.00 45.43 O ANISOU 1127 O ASP A 179 7165 5338 4758 -3453 929 -420 O ATOM 1128 CB ASP A 179 24.274 -28.454 -7.014 1.00 46.29 C ANISOU 1128 CB ASP A 179 7331 5453 4803 -3608 907 -455 C ATOM 1129 CG ASP A 179 22.935 -27.880 -7.500 1.00 50.47 C ANISOU 1129 CG ASP A 179 7783 6047 5346 -3663 868 -404 C ATOM 1130 OD1 ASP A 179 21.979 -27.773 -6.711 1.00 51.99 O ANISOU 1130 OD1 ASP A 179 7916 6246 5592 -3674 865 -354 O ATOM 1131 OD2 ASP A 179 22.840 -27.519 -8.692 1.00 52.30 O ANISOU 1131 OD2 ASP A 179 8009 6324 5539 -3698 841 -410 O ATOM 1132 N ASP A 180 23.269 -27.586 -3.614 1.00 51.29 N ANISOU 1132 N ASP A 180 7887 6051 5550 -3520 944 -362 N ATOM 1133 CA ASP A 180 23.050 -26.499 -2.656 1.00 44.48 C ANISOU 1133 CA ASP A 180 6983 5196 4720 -3465 961 -337 C ATOM 1134 C ASP A 180 23.096 -27.158 -1.280 1.00 44.73 C ANISOU 1134 C ASP A 180 7057 5177 4763 -3463 992 -323 C ATOM 1135 O ASP A 180 22.149 -27.821 -0.870 1.00 45.66 O ANISOU 1135 O ASP A 180 7151 5294 4904 -3524 1002 -285 O ATOM 1136 CB ASP A 180 21.724 -25.797 -2.928 1.00 44.94 C ANISOU 1136 CB ASP A 180 6940 5310 4826 -3499 951 -287 C ATOM 1137 CG ASP A 180 21.362 -24.776 -1.876 1.00 44.61 C ANISOU 1137 CG ASP A 180 6851 5267 4832 -3451 982 -257 C ATOM 1138 OD1 ASP A 180 22.251 -24.395 -1.092 1.00 43.84 O ANISOU 1138 OD1 ASP A 180 6808 5134 4714 -3386 1000 -283 O ATOM 1139 OD2 ASP A 180 20.186 -24.341 -1.849 1.00 45.20 O ANISOU 1139 OD2 ASP A 180 6831 5375 4969 -3481 988 -204 O ATOM 1140 N VAL A 181 24.211 -27.028 -0.575 1.00 44.03 N ANISOU 1140 N VAL A 181 7030 5042 4657 -3399 1003 -349 N ATOM 1141 CA VAL A 181 24.519 -27.917 0.530 1.00 44.37 C ANISOU 1141 CA VAL A 181 7136 5025 4698 -3406 1018 -340 C ATOM 1142 C VAL A 181 24.836 -27.147 1.799 1.00 43.84 C ANISOU 1142 C VAL A 181 7092 4936 4630 -3351 1039 -330 C ATOM 1143 O VAL A 181 25.790 -26.363 1.825 1.00 42.95 O ANISOU 1143 O VAL A 181 6999 4813 4508 -3283 1030 -355 O ATOM 1144 CB VAL A 181 25.689 -28.853 0.196 1.00 44.32 C ANISOU 1144 CB VAL A 181 7199 4962 4680 -3396 1003 -373 C ATOM 1145 CG1 VAL A 181 25.993 -29.742 1.378 1.00 44.77 C ANISOU 1145 CG1 VAL A 181 7318 4948 4744 -3406 1008 -353 C ATOM 1146 CG2 VAL A 181 25.364 -29.654 -1.021 1.00 44.97 C ANISOU 1146 CG2 VAL A 181 7272 5058 4756 -3458 989 -387 C ATOM 1147 N PRO A 182 24.084 -27.343 2.873 1.00 44.46 N ANISOU 1147 N PRO A 182 7171 5005 4716 -3383 1069 -293 N ATOM 1148 CA PRO A 182 24.525 -26.872 4.181 1.00 44.14 C ANISOU 1148 CA PRO A 182 7184 4928 4659 -3342 1090 -287 C ATOM 1149 C PRO A 182 25.795 -27.582 4.613 1.00 43.95 C ANISOU 1149 C PRO A 182 7251 4835 4614 -3318 1063 -301 C ATOM 1150 O PRO A 182 25.880 -28.808 4.564 1.00 44.62 O ANISOU 1150 O PRO A 182 7367 4883 4702 -3362 1050 -292 O ATOM 1151 CB PRO A 182 23.348 -27.238 5.085 1.00 45.17 C ANISOU 1151 CB PRO A 182 7298 5066 4800 -3405 1134 -239 C ATOM 1152 CG PRO A 182 22.655 -28.291 4.381 1.00 46.06 C ANISOU 1152 CG PRO A 182 7376 5193 4933 -3478 1122 -219 C ATOM 1153 CD PRO A 182 22.757 -27.952 2.948 1.00 45.59 C ANISOU 1153 CD PRO A 182 7265 5172 4884 -3463 1088 -248 C ATOM 1154 N VAL A 183 26.770 -26.806 5.075 1.00 43.15 N ANISOU 1154 N VAL A 183 7187 4709 4501 -3251 1052 -317 N ATOM 1155 CA VAL A 183 28.016 -27.344 5.611 1.00 43.04 C ANISOU 1155 CA VAL A 183 7248 4622 4483 -3224 1021 -318 C ATOM 1156 C VAL A 183 28.237 -26.711 6.984 1.00 44.92 C ANISOU 1156 C VAL A 183 7545 4830 4692 -3201 1029 -301 C ATOM 1157 O VAL A 183 28.850 -25.644 7.107 1.00 42.15 O ANISOU 1157 O VAL A 183 7198 4481 4338 -3143 1018 -315 O ATOM 1158 CB VAL A 183 29.201 -27.099 4.683 1.00 42.31 C ANISOU 1158 CB VAL A 183 7141 4520 4415 -3169 989 -351 C ATOM 1159 CG1 VAL A 183 30.445 -27.643 5.294 1.00 42.34 C ANISOU 1159 CG1 VAL A 183 7205 4442 4441 -3142 954 -342 C ATOM 1160 CG2 VAL A 183 28.936 -27.758 3.377 1.00 42.58 C ANISOU 1160 CG2 VAL A 183 7134 4581 4465 -3202 989 -371 C ATOM 1161 N ILE A 184 27.759 -27.391 8.027 1.00 44.89 N ANISOU 1161 N ILE A 184 7595 4797 4665 -3252 1047 -267 N ATOM 1162 CA ILE A 184 27.904 -26.965 9.417 1.00 43.89 C ANISOU 1162 CA ILE A 184 7545 4637 4496 -3247 1058 -248 C ATOM 1163 C ILE A 184 29.166 -27.603 9.977 1.00 43.97 C ANISOU 1163 C ILE A 184 7637 4565 4506 -3231 1000 -232 C ATOM 1164 O ILE A 184 29.196 -28.813 10.194 1.00 53.70 O ANISOU 1164 O ILE A 184 8904 5753 5748 -3276 982 -205 O ATOM 1165 CB ILE A 184 26.695 -27.387 10.249 1.00 44.95 C ANISOU 1165 CB ILE A 184 7694 4783 4604 -3321 1114 -212 C ATOM 1166 CG1 ILE A 184 25.419 -26.874 9.599 1.00 45.06 C ANISOU 1166 CG1 ILE A 184 7603 4873 4647 -3340 1166 -216 C ATOM 1167 CG2 ILE A 184 26.854 -26.859 11.648 1.00 45.14 C ANISOU 1167 CG2 ILE A 184 7808 4773 4572 -3319 1134 -198 C ATOM 1168 CD1 ILE A 184 24.184 -27.508 10.132 1.00 46.30 C ANISOU 1168 CD1 ILE A 184 7742 5048 4804 -3421 1221 -170 C ATOM 1169 N VAL A 185 30.197 -26.805 10.238 1.00 43.29 N ANISOU 1169 N VAL A 185 7578 4451 4417 -3170 964 -242 N ATOM 1170 CA VAL A 185 31.491 -27.315 10.675 1.00 43.38 C ANISOU 1170 CA VAL A 185 7649 4380 4454 -3148 897 -222 C ATOM 1171 C VAL A 185 31.690 -26.972 12.140 1.00 43.73 C ANISOU 1171 C VAL A 185 7797 4380 4438 -3158 884 -193 C ATOM 1172 O VAL A 185 31.564 -25.811 12.530 1.00 53.43 O ANISOU 1172 O VAL A 185 9042 5632 5626 -3134 904 -207 O ATOM 1173 CB VAL A 185 32.630 -26.747 9.823 1.00 42.52 C ANISOU 1173 CB VAL A 185 7486 4265 4404 -3078 855 -246 C ATOM 1174 CG1 VAL A 185 33.933 -27.352 10.259 1.00 42.80 C ANISOU 1174 CG1 VAL A 185 7563 4206 4494 -3058 782 -220 C ATOM 1175 CG2 VAL A 185 32.357 -27.016 8.347 1.00 42.26 C ANISOU 1175 CG2 VAL A 185 7362 4281 4412 -3076 877 -279 C ATOM 1176 N GLN A 186 31.989 -27.980 12.952 1.00 44.59 N ANISOU 1176 N GLN A 186 7985 4420 4540 -3198 848 -152 N ATOM 1177 CA GLN A 186 32.148 -27.798 14.387 1.00 45.15 C ANISOU 1177 CA GLN A 186 8173 4443 4538 -3221 830 -119 C ATOM 1178 C GLN A 186 33.277 -28.654 14.905 1.00 45.71 C ANISOU 1178 C GLN A 186 8307 4413 4647 -3222 738 -76 C ATOM 1179 O GLN A 186 33.543 -29.716 14.376 1.00 46.05 O ANISOU 1179 O GLN A 186 8315 4420 4763 -3231 710 -63 O ATOM 1180 CB GLN A 186 30.922 -28.204 15.158 1.00 46.10 C ANISOU 1180 CB GLN A 186 8344 4584 4586 -3300 897 -97 C ATOM 1181 CG GLN A 186 29.709 -27.548 14.694 1.00 45.84 C ANISOU 1181 CG GLN A 186 8237 4638 4542 -3309 987 -129 C ATOM 1182 CD GLN A 186 28.524 -28.183 15.292 1.00 57.53 C ANISOU 1182 CD GLN A 186 9740 6136 5983 -3392 1052 -98 C ATOM 1183 OE1 GLN A 186 28.601 -29.248 15.909 1.00 58.22 O ANISOU 1183 OE1 GLN A 186 9896 6172 6052 -3447 1026 -53 O ATOM 1184 NE2 GLN A 186 27.408 -27.532 15.149 1.00 60.66 N ANISOU 1184 NE2 GLN A 186 10075 6600 6373 -3404 1136 -115 N ATOM 1185 N ASP A 187 33.933 -28.210 15.952 1.00 50.15 N ANISOU 1185 N ASP A 187 8965 4924 5166 -3215 688 -52 N ATOM 1186 CA ASP A 187 34.828 -29.117 16.635 1.00 48.04 C ANISOU 1186 CA ASP A 187 8770 4553 4930 -3232 596 1 C ATOM 1187 C ASP A 187 34.157 -29.541 17.928 1.00 50.04 C ANISOU 1187 C ASP A 187 9155 4786 5073 -3313 613 43 C ATOM 1188 O ASP A 187 33.277 -28.844 18.451 1.00 48.05 O ANISOU 1188 O ASP A 187 8947 4588 4720 -3342 689 27 O ATOM 1189 CB ASP A 187 36.201 -28.496 16.907 1.00 49.73 C ANISOU 1189 CB ASP A 187 9002 4704 5188 -3174 500 10 C ATOM 1190 CG ASP A 187 36.157 -27.301 17.888 1.00 59.37 C ANISOU 1190 CG ASP A 187 10322 5936 6298 -3174 502 8 C ATOM 1191 OD1 ASP A 187 35.086 -26.648 18.091 1.00 62.49 O ANISOU 1191 OD1 ASP A 187 10741 6403 6600 -3198 594 -20 O ATOM 1192 OD2 ASP A 187 37.234 -27.031 18.474 1.00 60.49 O ANISOU 1192 OD2 ASP A 187 10519 6007 6457 -3152 404 34 O ATOM 1193 N LYS A 188 34.538 -30.735 18.386 1.00 55.01 N ANISOU 1193 N LYS A 188 9838 5332 5731 -3352 548 97 N ATOM 1194 CA LYS A 188 34.200 -31.258 19.703 1.00 58.98 C ANISOU 1194 CA LYS A 188 10483 5791 6134 -3432 536 152 C ATOM 1195 C LYS A 188 35.374 -32.072 20.243 1.00 61.79 C ANISOU 1195 C LYS A 188 10904 6024 6549 -3434 406 211 C ATOM 1196 O LYS A 188 36.258 -32.517 19.496 1.00 64.36 O ANISOU 1196 O LYS A 188 11144 6294 7014 -3382 342 209 O ATOM 1197 CB LYS A 188 32.924 -32.107 19.672 1.00 51.01 C ANISOU 1197 CB LYS A 188 9467 4822 5093 -3512 618 168 C ATOM 1198 CG LYS A 188 31.729 -31.405 19.105 1.00 50.39 C ANISOU 1198 CG LYS A 188 9308 4856 4983 -3513 739 116 C ATOM 1199 CD LYS A 188 30.500 -32.054 19.601 1.00 51.56 C ANISOU 1199 CD LYS A 188 9487 5032 5072 -3607 813 149 C ATOM 1200 CE LYS A 188 29.296 -31.723 18.752 1.00 51.15 C ANISOU 1200 CE LYS A 188 9314 5081 5040 -3611 919 108 C ATOM 1201 NZ LYS A 188 28.916 -30.282 18.785 1.00 66.37 N ANISOU 1201 NZ LYS A 188 11218 7075 6925 -3571 989 57 N ATOM 1202 N LYS A 189 35.394 -32.222 21.567 1.00 64.35 N ANISOU 1202 N LYS A 189 11381 6299 6769 -3494 366 263 N ATOM 1203 CA LYS A 189 36.334 -33.097 22.257 1.00 69.91 C ANISOU 1203 CA LYS A 189 12168 6881 7513 -3514 237 332 C ATOM 1204 C LYS A 189 35.554 -34.155 23.046 1.00 75.79 C ANISOU 1204 C LYS A 189 13016 7602 8181 -3618 254 393 C ATOM 1205 O LYS A 189 34.469 -33.889 23.579 1.00 75.96 O ANISOU 1205 O LYS A 189 13107 7690 8063 -3687 350 389 O ATOM 1206 CB LYS A 189 37.285 -32.292 23.185 1.00 70.61 C ANISOU 1206 CB LYS A 189 12365 6917 7547 -3493 141 350 C ATOM 1207 CG LYS A 189 36.591 -31.342 24.153 1.00 69.18 C ANISOU 1207 CG LYS A 189 12357 6788 7139 -3568 203 334 C ATOM 1208 CD LYS A 189 37.315 -31.203 25.501 1.00 69.61 C ANISOU 1208 CD LYS A 189 12642 6755 7053 -3636 84 385 C ATOM 1209 CE LYS A 189 38.667 -30.490 25.402 1.00 73.98 C ANISOU 1209 CE LYS A 189 13160 7255 7696 -3548 -39 383 C ATOM 1210 NZ LYS A 189 39.061 -29.747 26.667 1.00 74.21 N ANISOU 1210 NZ LYS A 189 13435 7238 7526 -3618 -121 403 N ATOM 1211 N PHE A 190 36.089 -35.365 23.112 1.00 74.50 N ANISOU 1211 N PHE A 190 12865 7336 8107 -3637 164 449 N ATOM 1212 CA PHE A 190 35.351 -36.454 23.719 1.00 76.14 C ANISOU 1212 CA PHE A 190 13155 7516 8257 -3737 177 512 C ATOM 1213 C PHE A 190 36.182 -37.113 24.800 1.00 81.71 C ANISOU 1213 C PHE A 190 13999 8096 8951 -3776 38 596 C ATOM 1214 O PHE A 190 37.409 -37.231 24.690 1.00 73.83 O ANISOU 1214 O PHE A 190 12980 7005 8069 -3716 -80 608 O ATOM 1215 CB PHE A 190 34.952 -37.486 22.678 1.00 74.36 C ANISOU 1215 CB PHE A 190 12813 7285 8155 -3742 208 506 C ATOM 1216 CG PHE A 190 33.976 -36.974 21.674 1.00 71.57 C ANISOU 1216 CG PHE A 190 12339 7057 7799 -3723 338 435 C ATOM 1217 CD1 PHE A 190 32.650 -36.770 22.020 1.00 56.55 C ANISOU 1217 CD1 PHE A 190 10462 5246 5778 -3795 450 435 C ATOM 1218 CD2 PHE A 190 34.409 -36.617 20.397 1.00 54.85 C ANISOU 1218 CD2 PHE A 190 10077 4963 5799 -3634 348 369 C ATOM 1219 CE1 PHE A 190 31.751 -36.279 21.096 1.00 55.61 C ANISOU 1219 CE1 PHE A 190 10226 5237 5669 -3777 560 373 C ATOM 1220 CE2 PHE A 190 33.536 -36.120 19.478 1.00 53.89 C ANISOU 1220 CE2 PHE A 190 9853 4954 5670 -3619 454 308 C ATOM 1221 CZ PHE A 190 32.192 -35.953 19.825 1.00 58.51 C ANISOU 1221 CZ PHE A 190 10461 5626 6144 -3690 556 311 C ATOM 1222 N SER A 191 35.478 -37.544 25.840 1.00 95.07 N ANISOU 1222 N SER A 191 15863 9784 10475 -3904 52 653 N ATOM 1223 CA SER A 191 36.082 -38.194 26.989 1.00 97.22 C ANISOU 1223 CA SER A 191 16323 9942 10675 -3982 -82 741 C ATOM 1224 C SER A 191 36.557 -39.603 26.618 1.00 97.22 C ANISOU 1224 C SER A 191 16246 9828 10864 -3962 -168 797 C ATOM 1225 O SER A 191 36.441 -40.063 25.471 1.00 99.00 O ANISOU 1225 O SER A 191 16297 10061 11258 -3900 -123 760 O ATOM 1226 CB SER A 191 35.087 -38.203 28.153 1.00 97.54 C ANISOU 1226 CB SER A 191 16572 10020 10468 -4136 -23 780 C ATOM 1227 OG SER A 191 33.947 -38.991 27.859 1.00 95.58 O ANISOU 1227 OG SER A 191 16262 9818 10235 -4196 81 797 O ATOM 1228 N ALA A 192 37.135 -40.284 27.613 1.00 98.08 N ANISOU 1228 N ALA A 192 16518 9822 10927 -4030 -305 885 N ATOM 1229 CA ALA A 192 37.451 -41.701 27.460 1.00 93.17 C ANISOU 1229 CA ALA A 192 15862 9080 10459 -4037 -385 948 C ATOM 1230 C ALA A 192 36.226 -42.499 27.021 1.00 82.58 C ANISOU 1230 C ALA A 192 14459 7788 9128 -4094 -270 955 C ATOM 1231 O ALA A 192 36.324 -43.393 26.176 1.00 79.07 O ANISOU 1231 O ALA A 192 13904 7285 8856 -4063 -279 950 O ATOM 1232 CB ALA A 192 38.004 -42.243 28.782 1.00 94.72 C ANISOU 1232 CB ALA A 192 16281 9160 10548 -4132 -545 1054 C ATOM 1233 N ASP A 193 35.057 -42.142 27.556 1.00 81.67 N ANISOU 1233 N ASP A 193 14438 7779 8812 -4198 -162 959 N ATOM 1234 CA ASP A 193 33.833 -42.902 27.350 1.00 86.28 C ANISOU 1234 CA ASP A 193 14987 8410 9386 -4276 -61 983 C ATOM 1235 C ASP A 193 33.396 -42.887 25.899 1.00 93.24 C ANISOU 1235 C ASP A 193 15651 9356 10419 -4195 35 904 C ATOM 1236 O ASP A 193 32.646 -43.773 25.462 1.00100.89 O ANISOU 1236 O ASP A 193 16574 10326 11433 -4250 78 925 O ATOM 1237 CB ASP A 193 32.728 -42.299 28.199 1.00 88.93 C ANISOU 1237 CB ASP A 193 15453 8855 9484 -4394 52 989 C ATOM 1238 CG ASP A 193 33.232 -41.845 29.538 1.00 99.90 C ANISOU 1238 CG ASP A 193 17076 10203 10679 -4467 -31 1031 C ATOM 1239 OD1 ASP A 193 34.148 -42.507 30.061 1.00105.45 O ANISOU 1239 OD1 ASP A 193 17878 10779 11411 -4481 -190 1103 O ATOM 1240 OD2 ASP A 193 32.719 -40.834 30.069 1.00104.17 O ANISOU 1240 OD2 ASP A 193 17709 10832 11041 -4513 60 991 O ATOM 1241 N GLY A 194 33.840 -41.887 25.141 1.00 93.54 N ANISOU 1241 N GLY A 194 15584 9447 10508 -4088 61 816 N ATOM 1242 CA GLY A 194 33.265 -41.573 23.853 1.00 95.71 C ANISOU 1242 CA GLY A 194 15698 9815 10852 -4040 166 733 C ATOM 1243 C GLY A 194 32.168 -40.532 23.914 1.00 93.64 C ANISOU 1243 C GLY A 194 15416 9704 10459 -4060 306 688 C ATOM 1244 O GLY A 194 31.650 -40.140 22.859 1.00 93.20 O ANISOU 1244 O GLY A 194 15228 9734 10450 -4019 390 618 O ATOM 1245 N GLN A 195 31.802 -40.094 25.121 1.00 89.86 N ANISOU 1245 N GLN A 195 15068 9254 9822 -4124 333 724 N ATOM 1246 CA GLN A 195 30.828 -39.049 25.378 1.00 83.72 C ANISOU 1246 CA GLN A 195 14314 8600 8898 -4163 467 679 C ATOM 1247 C GLN A 195 31.493 -37.679 25.295 1.00 83.33 C ANISOU 1247 C GLN A 195 14268 8581 8813 -4078 461 606 C ATOM 1248 O GLN A 195 32.716 -37.547 25.389 1.00 86.35 O ANISOU 1248 O GLN A 195 14682 8886 9244 -4017 343 609 O ATOM 1249 CB GLN A 195 30.210 -39.237 26.754 1.00 82.80 C ANISOU 1249 CB GLN A 195 14399 8482 8580 -4314 498 744 C ATOM 1250 CG GLN A 195 29.572 -40.577 26.947 1.00 89.51 C ANISOU 1250 CG GLN A 195 15258 9297 9454 -4409 499 830 C ATOM 1251 CD GLN A 195 28.188 -40.603 26.359 1.00 98.39 C ANISOU 1251 CD GLN A 195 16246 10533 10606 -4437 646 814 C ATOM 1252 OE1 GLN A 195 27.547 -39.559 26.276 1.00 99.49 O ANISOU 1252 OE1 GLN A 195 16347 10775 10680 -4426 763 753 O ATOM 1253 NE2 GLN A 195 27.707 -41.791 25.948 1.00103.02 N ANISOU 1253 NE2 GLN A 195 16756 11092 11295 -4475 639 869 N ATOM 1254 N ILE A 196 30.667 -36.646 25.122 1.00 80.71 N ANISOU 1254 N ILE A 196 13900 8360 8405 -4077 589 541 N ATOM 1255 CA ILE A 196 31.185 -35.294 24.930 1.00 75.33 C ANISOU 1255 CA ILE A 196 13210 7712 7699 -3996 595 466 C ATOM 1256 C ILE A 196 31.789 -34.800 26.234 1.00 80.86 C ANISOU 1256 C ILE A 196 14142 8355 8226 -4058 533 486 C ATOM 1257 O ILE A 196 31.184 -34.923 27.309 1.00 87.83 O ANISOU 1257 O ILE A 196 15195 9237 8940 -4180 578 520 O ATOM 1258 CB ILE A 196 30.072 -34.350 24.450 1.00 70.85 C ANISOU 1258 CB ILE A 196 12552 7267 7100 -3988 748 396 C ATOM 1259 CG1 ILE A 196 29.445 -34.832 23.144 1.00 67.40 C ANISOU 1259 CG1 ILE A 196 11894 6886 6826 -3934 794 381 C ATOM 1260 CG2 ILE A 196 30.608 -32.963 24.248 1.00 71.48 C ANISOU 1260 CG2 ILE A 196 12630 7374 7157 -3908 750 322 C ATOM 1261 CD1 ILE A 196 28.302 -33.949 22.683 1.00 64.61 C ANISOU 1261 CD1 ILE A 196 11447 6649 6454 -3929 933 324 C ATOM 1262 N ASP A 197 32.982 -34.231 26.152 1.00 77.55 N ANISOU 1262 N ASP A 197 13732 7886 7845 -3976 429 468 N ATOM 1263 CA ASP A 197 33.697 -33.776 27.342 1.00 77.32 C ANISOU 1263 CA ASP A 197 13927 7790 7660 -4028 339 491 C ATOM 1264 C ASP A 197 33.701 -32.251 27.335 1.00 76.45 C ANISOU 1264 C ASP A 197 13848 7735 7464 -3992 398 410 C ATOM 1265 O ASP A 197 34.565 -31.626 26.726 1.00 76.80 O ANISOU 1265 O ASP A 197 13796 7771 7611 -3883 336 379 O ATOM 1266 CB ASP A 197 35.118 -34.346 27.374 1.00 74.36 C ANISOU 1266 CB ASP A 197 13550 7299 7403 -3972 154 548 C ATOM 1267 CG ASP A 197 35.965 -33.769 28.495 1.00 73.61 C ANISOU 1267 CG ASP A 197 13673 7133 7163 -4012 36 573 C ATOM 1268 OD1 ASP A 197 35.476 -33.623 29.651 1.00 77.95 O ANISOU 1268 OD1 ASP A 197 14450 7677 7489 -4138 58 591 O ATOM 1269 OD2 ASP A 197 37.132 -33.453 28.200 1.00 70.62 O ANISOU 1269 OD2 ASP A 197 13233 6702 6898 -3919 -80 573 O ATOM 1270 N TYR A 198 32.730 -31.652 28.009 1.00 79.33 N ANISOU 1270 N TYR A 198 14342 8149 7649 -4083 524 374 N ATOM 1271 CA TYR A 198 32.708 -30.211 28.206 1.00 76.97 C ANISOU 1271 CA TYR A 198 14121 7880 7244 -4069 581 297 C ATOM 1272 C TYR A 198 33.107 -29.886 29.636 1.00 86.54 C ANISOU 1272 C TYR A 198 15629 9014 8236 -4170 518 316 C ATOM 1273 O TYR A 198 32.888 -30.678 30.560 1.00 98.76 O ANISOU 1273 O TYR A 198 17331 10518 9676 -4281 497 378 O ATOM 1274 CB TYR A 198 31.325 -29.635 27.891 1.00 71.82 C ANISOU 1274 CB TYR A 198 13398 7329 6562 -4091 781 230 C ATOM 1275 CG TYR A 198 31.219 -28.116 27.805 1.00 71.86 C ANISOU 1275 CG TYR A 198 13434 7365 6504 -4055 858 139 C ATOM 1276 CD1 TYR A 198 31.022 -27.356 28.943 1.00 75.87 C ANISOU 1276 CD1 TYR A 198 14186 7837 6805 -4144 912 106 C ATOM 1277 CD2 TYR A 198 31.310 -27.439 26.581 1.00 69.45 C ANISOU 1277 CD2 TYR A 198 12923 7119 6346 -3935 878 86 C ATOM 1278 CE1 TYR A 198 30.910 -25.961 28.879 1.00 74.14 C ANISOU 1278 CE1 TYR A 198 14008 7630 6530 -4114 988 20 C ATOM 1279 CE2 TYR A 198 31.209 -26.040 26.511 1.00 65.08 C ANISOU 1279 CE2 TYR A 198 12403 6587 5738 -3905 945 9 C ATOM 1280 CZ TYR A 198 31.005 -25.313 27.670 1.00 68.52 C ANISOU 1280 CZ TYR A 198 13087 6977 5970 -3995 1002 -26 C ATOM 1281 OH TYR A 198 30.881 -23.943 27.672 1.00 57.17 O ANISOU 1281 OH TYR A 198 11708 5542 4472 -3974 1074 -104 O ATOM 1282 N GLN A 199 33.729 -28.727 29.800 1.00 86.17 N ANISOU 1282 N GLN A 199 15667 8946 8126 -4132 479 268 N ATOM 1283 CA GLN A 199 34.035 -28.214 31.128 1.00 90.49 C ANISOU 1283 CA GLN A 199 16517 9419 8445 -4229 428 269 C ATOM 1284 C GLN A 199 34.196 -26.712 30.984 1.00 87.90 C ANISOU 1284 C GLN A 199 16228 9105 8063 -4179 469 184 C ATOM 1285 O GLN A 199 34.935 -26.250 30.111 1.00 86.02 O ANISOU 1285 O GLN A 199 15827 8883 7975 -4056 400 175 O ATOM 1286 CB GLN A 199 35.299 -28.876 31.705 1.00 98.72 C ANISOU 1286 CB GLN A 199 17665 10357 9487 -4238 201 362 C ATOM 1287 CG GLN A 199 36.549 -28.840 30.798 1.00103.09 C ANISOU 1287 CG GLN A 199 18020 10888 10261 -4092 54 387 C ATOM 1288 CD GLN A 199 36.573 -29.916 29.700 1.00106.07 C ANISOU 1288 CD GLN A 199 18126 11290 10888 -4010 53 421 C ATOM 1289 OE1 GLN A 199 36.272 -29.635 28.537 1.00 99.86 O ANISOU 1289 OE1 GLN A 199 17113 10579 10252 -3914 145 369 O ATOM 1290 NE2 GLN A 199 36.920 -31.154 30.076 1.00112.89 N ANISOU 1290 NE2 GLN A 199 19023 12080 11790 -4051 -53 507 N ATOM 1291 N LEU A 200 33.474 -25.950 31.792 1.00 90.75 N ANISOU 1291 N LEU A 200 16795 9458 8229 -4270 593 120 N ATOM 1292 CA LEU A 200 33.585 -24.492 31.751 1.00 91.06 C ANISOU 1292 CA LEU A 200 16908 9492 8201 -4234 638 35 C ATOM 1293 C LEU A 200 34.514 -23.997 32.865 1.00 93.46 C ANISOU 1293 C LEU A 200 17511 9686 8316 -4290 489 49 C ATOM 1294 O LEU A 200 34.159 -23.186 33.722 1.00 98.80 O ANISOU 1294 O LEU A 200 18436 10308 8795 -4371 564 -17 O ATOM 1295 CB LEU A 200 32.194 -23.862 31.827 1.00 90.64 C ANISOU 1295 CB LEU A 200 16873 9484 8083 -4282 882 -54 C ATOM 1296 CG LEU A 200 32.032 -22.338 31.771 1.00 86.99 C ANISOU 1296 CG LEU A 200 16488 9009 7557 -4254 975 -155 C ATOM 1297 CD1 LEU A 200 33.085 -21.696 30.903 1.00 78.77 C ANISOU 1297 CD1 LEU A 200 15318 7980 6631 -4124 841 -149 C ATOM 1298 CD2 LEU A 200 30.644 -22.006 31.249 1.00 88.97 C ANISOU 1298 CD2 LEU A 200 16585 9338 7880 -4246 1211 -217 C ATOM 1299 N ASP A 201 35.738 -24.517 32.846 1.00 91.11 N ANISOU 1299 N ASP A 201 17183 9342 8092 -4244 270 138 N ATOM 1300 CA ASP A 201 36.745 -24.168 33.839 1.00 95.51 C ANISOU 1300 CA ASP A 201 17996 9795 8497 -4288 85 175 C ATOM 1301 C ASP A 201 37.437 -22.866 33.431 1.00 91.76 C ANISOU 1301 C ASP A 201 17493 9318 8054 -4190 32 144 C ATOM 1302 O ASP A 201 37.019 -22.195 32.482 1.00 91.42 O ANISOU 1302 O ASP A 201 17261 9349 8123 -4104 159 84 O ATOM 1303 CB ASP A 201 37.727 -25.322 34.006 1.00103.27 C ANISOU 1303 CB ASP A 201 18941 10724 9575 -4280 -128 293 C ATOM 1304 CG ASP A 201 38.561 -25.545 32.769 1.00108.30 C ANISOU 1304 CG ASP A 201 19248 11391 10509 -4121 -215 334 C ATOM 1305 OD1 ASP A 201 38.066 -25.241 31.666 1.00109.20 O ANISOU 1305 OD1 ASP A 201 19127 11594 10769 -4033 -79 279 O ATOM 1306 OD2 ASP A 201 39.716 -25.995 32.892 1.00111.35 O ANISOU 1306 OD2 ASP A 201 19610 11706 10991 -4084 -418 415 O ATOM 1307 N VAL A 202 38.519 -22.494 34.131 1.00 87.04 N ANISOU 1307 N VAL A 202 17071 8632 7367 -4199 -167 194 N ATOM 1308 CA VAL A 202 39.132 -21.186 33.876 1.00 80.25 C ANISOU 1308 CA VAL A 202 16207 7762 6524 -4115 -217 174 C ATOM 1309 C VAL A 202 39.944 -21.184 32.586 1.00 78.23 C ANISOU 1309 C VAL A 202 15582 7553 6590 -3950 -294 213 C ATOM 1310 O VAL A 202 40.289 -20.113 32.073 1.00 78.59 O ANISOU 1310 O VAL A 202 15537 7613 6712 -3862 -298 187 O ATOM 1311 CB VAL A 202 40.038 -20.714 35.034 1.00 73.71 C ANISOU 1311 CB VAL A 202 15682 6820 5503 -4175 -416 222 C ATOM 1312 CG1 VAL A 202 39.277 -20.788 36.331 1.00 70.88 C ANISOU 1312 CG1 VAL A 202 15707 6400 4824 -4349 -345 169 C ATOM 1313 CG2 VAL A 202 41.427 -21.409 35.033 1.00 65.12 C ANISOU 1313 CG2 VAL A 202 14486 5677 4581 -4122 -685 339 C ATOM 1314 N MET A 203 40.285 -22.348 32.049 1.00 77.08 N ANISOU 1314 N MET A 203 15224 7421 6641 -3906 -356 269 N ATOM 1315 CA MET A 203 40.969 -22.320 30.769 1.00 73.61 C ANISOU 1315 CA MET A 203 14440 7020 6506 -3754 -395 280 C ATOM 1316 C MET A 203 39.982 -22.087 29.645 1.00 69.44 C ANISOU 1316 C MET A 203 13698 6603 6081 -3696 -188 205 C ATOM 1317 O MET A 203 40.186 -21.198 28.815 1.00 68.97 O ANISOU 1317 O MET A 203 13475 6585 6147 -3599 -162 168 O ATOM 1318 CB MET A 203 41.738 -23.607 30.523 1.00 74.69 C ANISOU 1318 CB MET A 203 14427 7117 6834 -3720 -525 357 C ATOM 1319 CG MET A 203 41.962 -23.864 29.060 1.00 75.18 C ANISOU 1319 CG MET A 203 14131 7238 7197 -3585 -476 339 C ATOM 1320 SD MET A 203 43.250 -25.068 28.782 1.00 78.22 S ANISOU 1320 SD MET A 203 14348 7538 7833 -3524 -654 420 S ATOM 1321 CE MET A 203 42.568 -25.980 27.399 1.00 77.58 C ANISOU 1321 CE MET A 203 13976 7537 7964 -3453 -494 385 C ATOM 1322 N THR A 204 38.908 -22.877 29.594 1.00 66.45 N ANISOU 1322 N THR A 204 13315 6273 5659 -3757 -49 185 N ATOM 1323 CA THR A 204 37.938 -22.678 28.528 1.00 64.50 C ANISOU 1323 CA THR A 204 12865 6130 5512 -3707 134 118 C ATOM 1324 C THR A 204 37.249 -21.332 28.653 1.00 67.80 C ANISOU 1324 C THR A 204 13393 6576 5793 -3726 264 35 C ATOM 1325 O THR A 204 36.858 -20.747 27.640 1.00 71.61 O ANISOU 1325 O THR A 204 13684 7131 6395 -3648 360 -14 O ATOM 1326 CB THR A 204 36.891 -23.777 28.519 1.00 64.61 C ANISOU 1326 CB THR A 204 12856 6185 5507 -3776 250 117 C ATOM 1327 OG1 THR A 204 36.030 -23.620 29.657 1.00 67.12 O ANISOU 1327 OG1 THR A 204 13450 6481 5571 -3915 346 84 O ATOM 1328 CG2 THR A 204 37.582 -25.135 28.560 1.00 68.38 C ANISOU 1328 CG2 THR A 204 13270 6613 6099 -3770 114 205 C ATOM 1329 N ALA A 205 37.094 -20.810 29.872 1.00 63.91 N ANISOU 1329 N ALA A 205 13216 6018 5048 -3831 269 16 N ATOM 1330 CA ALA A 205 36.582 -19.452 29.960 1.00 61.67 C ANISOU 1330 CA ALA A 205 13043 5739 4652 -3837 387 -63 C ATOM 1331 C ALA A 205 37.577 -18.445 29.412 1.00 65.03 C ANISOU 1331 C ALA A 205 13355 6152 5200 -3721 271 -44 C ATOM 1332 O ALA A 205 37.174 -17.341 29.033 1.00 70.21 O ANISOU 1332 O ALA A 205 13991 6831 5854 -3684 370 -102 O ATOM 1333 CB ALA A 205 36.224 -19.093 31.390 1.00 59.71 C ANISOU 1333 CB ALA A 205 13181 5406 4100 -3976 425 -98 C ATOM 1334 N ALA A 206 38.857 -18.806 29.337 1.00 61.04 N ANISOU 1334 N ALA A 206 12762 5606 4826 -3660 66 35 N ATOM 1335 CA ALA A 206 39.883 -17.878 28.875 1.00 56.97 C ANISOU 1335 CA ALA A 206 12127 5069 4449 -3555 -56 51 C ATOM 1336 C ALA A 206 40.086 -17.955 27.360 1.00 56.88 C ANISOU 1336 C ALA A 206 11746 5137 4729 -3425 -35 40 C ATOM 1337 O ALA A 206 39.969 -16.941 26.661 1.00 54.98 O ANISOU 1337 O ALA A 206 11393 4934 4565 -3357 18 -2 O ATOM 1338 CB ALA A 206 41.195 -18.152 29.616 1.00 58.37 C ANISOU 1338 CB ALA A 206 12403 5150 4625 -3562 -290 133 C ATOM 1339 N VAL A 207 40.398 -19.148 26.841 1.00 56.10 N ANISOU 1339 N VAL A 207 11468 5057 4792 -3392 -76 78 N ATOM 1340 CA VAL A 207 40.698 -19.321 25.424 1.00 50.46 C ANISOU 1340 CA VAL A 207 10425 4403 4346 -3273 -64 69 C ATOM 1341 C VAL A 207 39.565 -19.971 24.644 1.00 49.68 C ANISOU 1341 C VAL A 207 10192 4394 4291 -3274 98 34 C ATOM 1342 O VAL A 207 39.576 -19.894 23.405 1.00 50.49 O ANISOU 1342 O VAL A 207 10047 4557 4579 -3182 135 12 O ATOM 1343 CB VAL A 207 42.002 -20.119 25.212 1.00 50.34 C ANISOU 1343 CB VAL A 207 10273 4330 4524 -3216 -225 130 C ATOM 1344 CG1 VAL A 207 43.166 -19.432 25.905 1.00 51.13 C ANISOU 1344 CG1 VAL A 207 10478 4343 4606 -3212 -397 165 C ATOM 1345 CG2 VAL A 207 41.845 -21.550 25.706 1.00 51.30 C ANISOU 1345 CG2 VAL A 207 10460 4420 4612 -3281 -244 176 C ATOM 1346 N GLY A 208 38.605 -20.596 25.307 1.00 50.75 N ANISOU 1346 N GLY A 208 10482 4537 4263 -3376 188 27 N ATOM 1347 CA GLY A 208 37.475 -21.221 24.652 1.00 52.84 C ANISOU 1347 CA GLY A 208 10629 4882 4564 -3387 334 -4 C ATOM 1348 C GLY A 208 37.462 -22.738 24.823 1.00 55.45 C ANISOU 1348 C GLY A 208 10942 5194 4933 -3425 302 48 C ATOM 1349 O GLY A 208 38.493 -23.381 25.066 1.00 53.16 O ANISOU 1349 O GLY A 208 10648 4834 4718 -3407 158 108 O ATOM 1350 N TRP A 209 36.266 -23.315 24.710 1.00 59.19 N ANISOU 1350 N TRP A 209 11404 5723 5362 -3481 434 24 N ATOM 1351 CA TRP A 209 36.115 -24.755 24.552 1.00 62.87 C ANISOU 1351 CA TRP A 209 11795 6184 5907 -3500 420 71 C ATOM 1352 C TRP A 209 36.442 -25.128 23.111 1.00 64.22 C ANISOU 1352 C TRP A 209 11680 6396 6324 -3380 405 70 C ATOM 1353 O TRP A 209 35.805 -24.635 22.172 1.00 69.99 O ANISOU 1353 O TRP A 209 12268 7208 7116 -3332 500 20 O ATOM 1354 CB TRP A 209 34.696 -25.191 24.915 1.00 66.92 C ANISOU 1354 CB TRP A 209 12383 6743 6299 -3602 566 48 C ATOM 1355 CG TRP A 209 34.529 -26.686 24.957 1.00 72.68 C ANISOU 1355 CG TRP A 209 13076 7454 7084 -3640 541 108 C ATOM 1356 CD1 TRP A 209 34.971 -27.528 25.930 1.00 74.82 C ANISOU 1356 CD1 TRP A 209 13503 7643 7281 -3714 446 175 C ATOM 1357 CD2 TRP A 209 33.883 -27.514 23.979 1.00 74.08 C ANISOU 1357 CD2 TRP A 209 13055 7690 7404 -3609 602 110 C ATOM 1358 NE1 TRP A 209 34.648 -28.826 25.620 1.00 74.59 N ANISOU 1358 NE1 TRP A 209 13381 7614 7345 -3729 448 219 N ATOM 1359 CE2 TRP A 209 33.978 -28.845 24.428 1.00 71.99 C ANISOU 1359 CE2 TRP A 209 12836 7369 7147 -3666 544 180 C ATOM 1360 CE3 TRP A 209 33.233 -27.257 22.771 1.00 76.21 C ANISOU 1360 CE3 TRP A 209 13120 8046 7789 -3542 690 64 C ATOM 1361 CZ2 TRP A 209 33.447 -29.913 23.719 1.00 71.41 C ANISOU 1361 CZ2 TRP A 209 12616 7321 7193 -3658 576 201 C ATOM 1362 CZ3 TRP A 209 32.710 -28.321 22.066 1.00 77.50 C ANISOU 1362 CZ3 TRP A 209 13143 8239 8066 -3535 716 86 C ATOM 1363 CH2 TRP A 209 32.817 -29.635 22.546 1.00 75.12 C ANISOU 1363 CH2 TRP A 209 12895 7877 7769 -3594 662 153 C ATOM 1364 N PHE A 210 37.443 -25.981 22.930 1.00 58.60 N ANISOU 1364 N PHE A 210 10891 5621 5754 -3335 285 122 N ATOM 1365 CA PHE A 210 37.844 -26.407 21.601 1.00 56.49 C ANISOU 1365 CA PHE A 210 10381 5372 5708 -3236 273 114 C ATOM 1366 C PHE A 210 38.385 -27.816 21.715 1.00 59.68 C ANISOU 1366 C PHE A 210 10788 5695 6191 -3260 191 170 C ATOM 1367 O PHE A 210 38.921 -28.188 22.761 1.00 63.67 O ANISOU 1367 O PHE A 210 11420 6118 6654 -3297 96 224 O ATOM 1368 CB PHE A 210 38.908 -25.487 21.011 1.00 55.70 C ANISOU 1368 CB PHE A 210 10198 5260 5705 -3155 206 95 C ATOM 1369 CG PHE A 210 40.231 -25.592 21.709 1.00 55.26 C ANISOU 1369 CG PHE A 210 10208 5097 5690 -3146 52 144 C ATOM 1370 CD1 PHE A 210 40.483 -24.860 22.848 1.00 57.54 C ANISOU 1370 CD1 PHE A 210 10666 5349 5850 -3178 -7 161 C ATOM 1371 CD2 PHE A 210 41.211 -26.458 21.252 1.00 53.85 C ANISOU 1371 CD2 PHE A 210 9942 4847 5673 -3118 -36 173 C ATOM 1372 CE1 PHE A 210 41.697 -24.971 23.499 1.00 56.81 C ANISOU 1372 CE1 PHE A 210 10638 5155 5792 -3176 -163 210 C ATOM 1373 CE2 PHE A 210 42.419 -26.576 21.904 1.00 52.32 C ANISOU 1373 CE2 PHE A 210 9798 4548 5532 -3110 -182 219 C ATOM 1374 CZ PHE A 210 42.662 -25.831 23.027 1.00 53.37 C ANISOU 1374 CZ PHE A 210 10084 4651 5542 -3136 -251 241 C ATOM 1375 N GLY A 211 38.268 -28.591 20.637 1.00 60.64 N ANISOU 1375 N GLY A 211 10776 5834 6432 -3240 223 158 N ATOM 1376 CA GLY A 211 38.667 -29.987 20.716 1.00 58.97 C ANISOU 1376 CA GLY A 211 10566 5536 6303 -3266 156 208 C ATOM 1377 C GLY A 211 39.576 -30.474 19.611 1.00 59.47 C ANISOU 1377 C GLY A 211 10482 5553 6562 -3202 111 195 C ATOM 1378 O GLY A 211 40.330 -29.692 19.018 1.00 61.58 O ANISOU 1378 O GLY A 211 10662 5826 6910 -3134 86 164 O ATOM 1379 N ASP A 212 39.495 -31.762 19.307 1.00 57.04 N ANISOU 1379 N ASP A 212 10143 5196 6335 -3226 104 216 N ATOM 1380 CA ASP A 212 40.320 -32.346 18.269 1.00 60.53 C ANISOU 1380 CA ASP A 212 10450 5578 6970 -3171 71 198 C ATOM 1381 C ASP A 212 39.546 -33.032 17.158 1.00 60.29 C ANISOU 1381 C ASP A 212 10329 5597 6984 -3180 161 162 C ATOM 1382 O ASP A 212 40.165 -33.424 16.162 1.00 61.57 O ANISOU 1382 O ASP A 212 10376 5718 7300 -3133 151 133 O ATOM 1383 CB ASP A 212 41.300 -33.347 18.885 1.00 65.53 C ANISOU 1383 CB ASP A 212 11124 6061 7711 -3180 -52 256 C ATOM 1384 CG ASP A 212 40.592 -34.368 19.719 1.00 71.56 C ANISOU 1384 CG ASP A 212 12010 6792 8389 -3264 -58 313 C ATOM 1385 OD1 ASP A 212 39.369 -34.200 19.881 1.00 74.44 O ANISOU 1385 OD1 ASP A 212 12423 7253 8607 -3317 36 306 O ATOM 1386 OD2 ASP A 212 41.227 -35.316 20.221 1.00 74.45 O ANISOU 1386 OD2 ASP A 212 12418 7034 8835 -3282 -154 366 O ATOM 1387 N THR A 213 38.228 -33.189 17.276 1.00 59.25 N ANISOU 1387 N THR A 213 10240 5544 6726 -3240 248 161 N ATOM 1388 CA THR A 213 37.468 -33.918 16.268 1.00 60.42 C ANISOU 1388 CA THR A 213 10311 5732 6913 -3258 320 133 C ATOM 1389 C THR A 213 36.540 -32.954 15.549 1.00 58.88 C ANISOU 1389 C THR A 213 10056 5676 6639 -3246 426 76 C ATOM 1390 O THR A 213 35.789 -32.223 16.201 1.00 64.03 O ANISOU 1390 O THR A 213 10771 6397 7162 -3275 474 76 O ATOM 1391 CB THR A 213 36.661 -35.049 16.899 1.00 64.53 C ANISOU 1391 CB THR A 213 10916 6223 7381 -3347 328 183 C ATOM 1392 OG1 THR A 213 37.393 -35.584 18.000 1.00 70.49 O ANISOU 1392 OG1 THR A 213 11772 6862 8148 -3369 225 249 O ATOM 1393 CG2 THR A 213 36.520 -36.159 15.907 1.00 66.91 C ANISOU 1393 CG2 THR A 213 11140 6489 7794 -3355 341 169 C ATOM 1394 N LEU A 214 36.582 -32.960 14.213 1.00 57.20 N ANISOU 1394 N LEU A 214 9726 5499 6508 -3207 462 25 N ATOM 1395 CA LEU A 214 35.883 -31.976 13.389 1.00 53.70 C ANISOU 1395 CA LEU A 214 9215 5179 6011 -3185 546 -29 C ATOM 1396 C LEU A 214 34.670 -32.602 12.709 1.00 50.23 C ANISOU 1396 C LEU A 214 8740 4800 5545 -3236 620 -46 C ATOM 1397 O LEU A 214 34.798 -33.581 11.972 1.00 53.25 O ANISOU 1397 O LEU A 214 9081 5142 6011 -3246 610 -53 O ATOM 1398 CB LEU A 214 36.829 -31.366 12.347 1.00 45.94 C ANISOU 1398 CB LEU A 214 8129 4200 5125 -3108 531 -73 C ATOM 1399 CG LEU A 214 36.404 -30.004 11.795 1.00 44.80 C ANISOU 1399 CG LEU A 214 7937 4168 4919 -3075 590 -117 C ATOM 1400 CD1 LEU A 214 36.551 -28.977 12.890 1.00 48.53 C ANISOU 1400 CD1 LEU A 214 8483 4642 5312 -3065 568 -98 C ATOM 1401 CD2 LEU A 214 37.183 -29.591 10.545 1.00 44.05 C ANISOU 1401 CD2 LEU A 214 7734 4084 4918 -3014 587 -159 C ATOM 1402 N LEU A 215 33.513 -31.996 12.916 1.00 46.89 N ANISOU 1402 N LEU A 215 8330 4470 5017 -3269 692 -57 N ATOM 1403 CA LEU A 215 32.214 -32.538 12.558 1.00 47.59 C ANISOU 1403 CA LEU A 215 8395 4614 5072 -3332 756 -60 C ATOM 1404 C LEU A 215 31.594 -31.686 11.472 1.00 46.42 C ANISOU 1404 C LEU A 215 8153 4571 4916 -3305 818 -115 C ATOM 1405 O LEU A 215 31.203 -30.544 11.717 1.00 51.01 O ANISOU 1405 O LEU A 215 8728 5213 5439 -3286 856 -132 O ATOM 1406 CB LEU A 215 31.287 -32.588 13.763 1.00 48.17 C ANISOU 1406 CB LEU A 215 8552 4703 5049 -3403 792 -20 C ATOM 1407 CG LEU A 215 31.739 -33.569 14.830 1.00 53.87 C ANISOU 1407 CG LEU A 215 9378 5323 5768 -3448 730 44 C ATOM 1408 CD1 LEU A 215 30.559 -33.971 15.666 1.00 50.42 C ANISOU 1408 CD1 LEU A 215 9000 4911 5248 -3540 782 84 C ATOM 1409 CD2 LEU A 215 32.359 -34.759 14.174 1.00 49.78 C ANISOU 1409 CD2 LEU A 215 8829 4724 5361 -3445 673 54 C ATOM 1410 N THR A 216 31.477 -32.260 10.299 1.00 46.40 N ANISOU 1410 N THR A 216 8082 4580 4969 -3308 825 -140 N ATOM 1411 CA THR A 216 30.892 -31.607 9.145 1.00 49.00 C ANISOU 1411 CA THR A 216 8324 5001 5293 -3292 872 -187 C ATOM 1412 C THR A 216 29.449 -32.094 9.010 1.00 51.62 C ANISOU 1412 C THR A 216 8636 5384 5593 -3369 920 -175 C ATOM 1413 O THR A 216 29.191 -33.191 8.509 1.00 47.13 O ANISOU 1413 O THR A 216 8059 4789 5059 -3415 912 -167 O ATOM 1414 CB THR A 216 31.742 -31.936 7.935 1.00 52.87 C ANISOU 1414 CB THR A 216 8761 5467 5862 -3253 848 -222 C ATOM 1415 OG1 THR A 216 33.118 -32.026 8.359 1.00 45.27 O ANISOU 1415 OG1 THR A 216 7825 4415 4960 -3205 789 -210 O ATOM 1416 CG2 THR A 216 31.569 -30.881 6.863 1.00 44.39 C ANISOU 1416 CG2 THR A 216 7611 4480 4774 -3214 881 -269 C ATOM 1417 N ASN A 217 28.508 -31.269 9.460 1.00 51.24 N ANISOU 1417 N ASN A 217 8576 5402 5490 -3384 970 -172 N ATOM 1418 CA ASN A 217 27.109 -31.654 9.555 1.00 47.19 C ANISOU 1418 CA ASN A 217 8037 4934 4960 -3461 1018 -147 C ATOM 1419 C ASN A 217 26.929 -32.829 10.487 1.00 48.45 C ANISOU 1419 C ASN A 217 8270 5030 5108 -3533 1006 -91 C ATOM 1420 O ASN A 217 26.066 -33.679 10.280 1.00 53.91 O ANISOU 1420 O ASN A 217 8940 5730 5814 -3605 1021 -64 O ATOM 1421 CB ASN A 217 26.513 -31.950 8.183 1.00 47.21 C ANISOU 1421 CB ASN A 217 7954 4985 5000 -3482 1025 -170 C ATOM 1422 CG ASN A 217 26.011 -30.712 7.524 1.00 52.38 C ANISOU 1422 CG ASN A 217 8529 5723 5651 -3447 1056 -202 C ATOM 1423 OD1 ASN A 217 25.835 -29.705 8.204 1.00 55.73 O ANISOU 1423 OD1 ASN A 217 8956 6171 6048 -3420 1085 -200 O ATOM 1424 ND2 ASN A 217 25.800 -30.745 6.211 1.00 46.21 N ANISOU 1424 ND2 ASN A 217 7681 4981 4895 -3448 1048 -229 N ATOM 1425 N GLY A 218 27.728 -32.877 11.535 1.00 54.69 N ANISOU 1425 N GLY A 218 9151 5755 5874 -3518 974 -68 N ATOM 1426 CA GLY A 218 27.684 -33.981 12.453 1.00 56.13 C ANISOU 1426 CA GLY A 218 9414 5867 6044 -3586 952 -9 C ATOM 1427 C GLY A 218 28.615 -35.125 12.119 1.00 51.19 C ANISOU 1427 C GLY A 218 8816 5146 5489 -3582 879 3 C ATOM 1428 O GLY A 218 28.958 -35.897 13.016 1.00 51.94 O ANISOU 1428 O GLY A 218 8995 5160 5582 -3618 838 54 O ATOM 1429 N ALA A 219 29.054 -35.244 10.873 1.00 49.59 N ANISOU 1429 N ALA A 219 8546 4943 5352 -3540 861 -41 N ATOM 1430 CA ALA A 219 29.869 -36.369 10.450 1.00 50.08 C ANISOU 1430 CA ALA A 219 8621 4906 5500 -3538 802 -36 C ATOM 1431 C ALA A 219 31.347 -36.048 10.598 1.00 63.93 C ANISOU 1431 C ALA A 219 10391 6592 7308 -3458 746 -48 C ATOM 1432 O ALA A 219 31.738 -34.889 10.710 1.00 71.42 O ANISOU 1432 O ALA A 219 11325 7584 8227 -3398 755 -71 O ATOM 1433 CB ALA A 219 29.564 -36.725 9.003 1.00 49.96 C ANISOU 1433 CB ALA A 219 8530 4921 5531 -3544 819 -80 C ATOM 1434 N ILE A 220 32.175 -37.091 10.593 1.00 58.85 N ANISOU 1434 N ILE A 220 9772 5833 6758 -3456 685 -30 N ATOM 1435 CA ILE A 220 33.630 -36.930 10.610 1.00 56.50 C ANISOU 1435 CA ILE A 220 9466 5452 6548 -3381 624 -40 C ATOM 1436 C ILE A 220 34.151 -37.192 9.207 1.00 55.40 C ANISOU 1436 C ILE A 220 9245 5296 6508 -3342 629 -98 C ATOM 1437 O ILE A 220 34.015 -38.312 8.698 1.00 55.96 O ANISOU 1437 O ILE A 220 9313 5307 6642 -3380 620 -101 O ATOM 1438 CB ILE A 220 34.311 -37.878 11.609 1.00 55.19 C ANISOU 1438 CB ILE A 220 9376 5149 6443 -3401 544 20 C ATOM 1439 CG1 ILE A 220 34.109 -37.414 13.045 1.00 57.66 C ANISOU 1439 CG1 ILE A 220 9784 5474 6652 -3428 530 74 C ATOM 1440 CG2 ILE A 220 35.803 -37.929 11.326 1.00 52.46 C ANISOU 1440 CG2 ILE A 220 8992 4703 6238 -3325 478 2 C ATOM 1441 CD1 ILE A 220 34.665 -38.366 14.076 1.00 52.45 C ANISOU 1441 CD1 ILE A 220 9212 4682 6033 -3461 447 142 C ATOM 1442 N TYR A 221 34.752 -36.172 8.595 1.00 55.95 N ANISOU 1442 N TYR A 221 9253 5414 6590 -3272 643 -143 N ATOM 1443 CA TYR A 221 35.292 -36.247 7.242 1.00 54.87 C ANISOU 1443 CA TYR A 221 9041 5274 6534 -3236 658 -203 C ATOM 1444 C TYR A 221 34.330 -36.926 6.259 1.00 54.67 C ANISOU 1444 C TYR A 221 8999 5288 6486 -3293 704 -231 C ATOM 1445 O TYR A 221 34.698 -37.897 5.604 1.00 59.11 O ANISOU 1445 O TYR A 221 9551 5771 7139 -3304 689 -254 O ATOM 1446 CB TYR A 221 36.636 -36.964 7.233 1.00 51.45 C ANISOU 1446 CB TYR A 221 8594 4697 6259 -3198 593 -204 C ATOM 1447 CG TYR A 221 37.438 -36.821 5.955 1.00 53.63 C ANISOU 1447 CG TYR A 221 8789 4963 6626 -3149 610 -270 C ATOM 1448 CD1 TYR A 221 36.963 -36.088 4.863 1.00 54.20 C ANISOU 1448 CD1 TYR A 221 8814 5155 6623 -3145 679 -320 C ATOM 1449 CD2 TYR A 221 38.686 -37.395 5.849 1.00 57.31 C ANISOU 1449 CD2 TYR A 221 9222 5295 7257 -3110 556 -281 C ATOM 1450 CE1 TYR A 221 37.710 -35.959 3.695 1.00 53.91 C ANISOU 1450 CE1 TYR A 221 8714 5112 6659 -3109 700 -380 C ATOM 1451 CE2 TYR A 221 39.440 -37.260 4.688 1.00 59.30 C ANISOU 1451 CE2 TYR A 221 9400 5536 7596 -3071 578 -345 C ATOM 1452 CZ TYR A 221 38.947 -36.547 3.623 1.00 55.21 C ANISOU 1452 CZ TYR A 221 8848 5145 6983 -3074 653 -393 C ATOM 1453 OH TYR A 221 39.713 -36.434 2.497 1.00 57.18 O ANISOU 1453 OH TYR A 221 9034 5383 7306 -3043 680 -455 O ATOM 1454 N PRO A 222 33.119 -36.415 6.111 1.00 48.09 N ANISOU 1454 N PRO A 222 8160 4570 5542 -3331 756 -233 N ATOM 1455 CA PRO A 222 32.191 -37.065 5.191 1.00 50.50 C ANISOU 1455 CA PRO A 222 8449 4909 5830 -3393 788 -254 C ATOM 1456 C PRO A 222 32.514 -36.803 3.731 1.00 52.48 C ANISOU 1456 C PRO A 222 8641 5196 6103 -3366 816 -322 C ATOM 1457 O PRO A 222 33.479 -36.105 3.394 1.00 57.12 O ANISOU 1457 O PRO A 222 9193 5784 6724 -3297 816 -352 O ATOM 1458 CB PRO A 222 30.845 -36.490 5.623 1.00 48.51 C ANISOU 1458 CB PRO A 222 8198 4762 5471 -3439 826 -229 C ATOM 1459 CG PRO A 222 31.175 -35.125 6.055 1.00 47.40 C ANISOU 1459 CG PRO A 222 8044 4679 5288 -3375 838 -236 C ATOM 1460 CD PRO A 222 32.552 -35.178 6.657 1.00 47.29 C ANISOU 1460 CD PRO A 222 8058 4569 5341 -3318 786 -223 C ATOM 1461 N GLN A 223 31.712 -37.392 2.858 1.00 52.64 N ANISOU 1461 N GLN A 223 8653 5242 6104 -3426 838 -342 N ATOM 1462 CA GLN A 223 31.934 -37.324 1.426 1.00 55.97 C ANISOU 1462 CA GLN A 223 9036 5692 6536 -3419 866 -406 C ATOM 1463 C GLN A 223 30.618 -36.945 0.789 1.00 48.39 C ANISOU 1463 C GLN A 223 8054 4847 5485 -3474 899 -412 C ATOM 1464 O GLN A 223 29.582 -37.488 1.165 1.00 49.15 O ANISOU 1464 O GLN A 223 8169 4951 5556 -3544 892 -374 O ATOM 1465 CB GLN A 223 32.448 -38.662 0.894 1.00 62.59 C ANISOU 1465 CB GLN A 223 9899 6413 7468 -3446 847 -432 C ATOM 1466 CG GLN A 223 32.476 -38.804 -0.603 1.00 67.23 C ANISOU 1466 CG GLN A 223 10467 7026 8052 -3465 882 -500 C ATOM 1467 CD GLN A 223 33.422 -39.909 -1.017 1.00 78.93 C ANISOU 1467 CD GLN A 223 11967 8369 9654 -3461 864 -539 C ATOM 1468 OE1 GLN A 223 34.114 -40.501 -0.172 1.00 83.16 O ANISOU 1468 OE1 GLN A 223 12520 8787 10288 -3435 817 -511 O ATOM 1469 NE2 GLN A 223 33.472 -40.194 -2.319 1.00 83.29 N ANISOU 1469 NE2 GLN A 223 12516 8927 10203 -3487 898 -604 N ATOM 1470 N HIS A 224 30.653 -35.985 -0.129 1.00 47.57 N ANISOU 1470 N HIS A 224 7906 4829 5339 -3446 928 -453 N ATOM 1471 CA HIS A 224 29.466 -35.496 -0.814 1.00 49.95 C ANISOU 1471 CA HIS A 224 8176 5237 5566 -3493 948 -457 C ATOM 1472 C HIS A 224 29.607 -35.713 -2.307 1.00 56.19 C ANISOU 1472 C HIS A 224 8957 6044 6347 -3517 965 -513 C ATOM 1473 O HIS A 224 30.686 -35.538 -2.869 1.00 55.97 O ANISOU 1473 O HIS A 224 8926 5992 6350 -3470 981 -558 O ATOM 1474 CB HIS A 224 29.198 -34.012 -0.569 1.00 47.78 C ANISOU 1474 CB HIS A 224 7858 5057 5240 -3446 962 -449 C ATOM 1475 CG HIS A 224 27.958 -33.506 -1.241 1.00 46.80 C ANISOU 1475 CG HIS A 224 7690 5030 5060 -3494 971 -446 C ATOM 1476 ND1 HIS A 224 26.718 -33.545 -0.647 1.00 49.51 N ANISOU 1476 ND1 HIS A 224 8015 5407 5388 -3546 968 -400 N ATOM 1477 CD2 HIS A 224 27.767 -32.959 -2.464 1.00 47.44 C ANISOU 1477 CD2 HIS A 224 7738 5179 5109 -3502 979 -479 C ATOM 1478 CE1 HIS A 224 25.820 -33.028 -1.468 1.00 49.23 C ANISOU 1478 CE1 HIS A 224 7928 5452 5325 -3580 969 -401 C ATOM 1479 NE2 HIS A 224 26.430 -32.664 -2.579 1.00 47.74 N ANISOU 1479 NE2 HIS A 224 7734 5285 5119 -3556 972 -448 N ATOM 1480 N ALA A 225 28.476 -36.037 -2.931 1.00 56.27 N ANISOU 1480 N ALA A 225 8963 6101 6316 -3597 963 -508 N ATOM 1481 CA ALA A 225 28.384 -36.358 -4.344 1.00 48.85 C ANISOU 1481 CA ALA A 225 8030 5179 5353 -3645 974 -556 C ATOM 1482 C ALA A 225 27.804 -35.164 -5.091 1.00 54.81 C ANISOU 1482 C ALA A 225 8736 6052 6037 -3646 982 -562 C ATOM 1483 O ALA A 225 26.620 -34.839 -4.943 1.00 48.38 O ANISOU 1483 O ALA A 225 7888 5301 5194 -3688 964 -522 O ATOM 1484 CB ALA A 225 27.517 -37.591 -4.526 1.00 50.23 C ANISOU 1484 CB ALA A 225 8236 5313 5537 -3744 950 -539 C ATOM 1485 N ALA A 226 28.634 -34.530 -5.913 1.00 56.85 N ANISOU 1485 N ALA A 226 8988 6336 6278 -3604 1007 -610 N ATOM 1486 CA ALA A 226 28.228 -33.304 -6.570 1.00 46.93 C ANISOU 1486 CA ALA A 226 7688 5183 4960 -3597 1008 -612 C ATOM 1487 C ALA A 226 28.069 -33.526 -8.068 1.00 47.52 C ANISOU 1487 C ALA A 226 7782 5291 4983 -3663 1016 -653 C ATOM 1488 O ALA A 226 28.802 -34.322 -8.656 1.00 48.04 O ANISOU 1488 O ALA A 226 7892 5298 5064 -3679 1043 -702 O ATOM 1489 CB ALA A 226 29.263 -32.202 -6.318 1.00 45.75 C ANISOU 1489 CB ALA A 226 7516 5048 4821 -3502 1025 -625 C ATOM 1490 N PRO A 227 27.107 -32.867 -8.709 1.00 47.58 N ANISOU 1490 N PRO A 227 7757 5386 4935 -3708 992 -633 N ATOM 1491 CA PRO A 227 27.126 -32.784 -10.168 1.00 53.37 C ANISOU 1491 CA PRO A 227 8512 6162 5605 -3763 999 -672 C ATOM 1492 C PRO A 227 28.409 -32.125 -10.617 1.00 60.41 C ANISOU 1492 C PRO A 227 9411 7058 6486 -3699 1042 -720 C ATOM 1493 O PRO A 227 29.063 -31.425 -9.845 1.00 65.81 O ANISOU 1493 O PRO A 227 10064 7733 7206 -3613 1051 -711 O ATOM 1494 CB PRO A 227 25.922 -31.892 -10.493 1.00 50.46 C ANISOU 1494 CB PRO A 227 8089 5887 5198 -3800 953 -623 C ATOM 1495 CG PRO A 227 25.767 -31.063 -9.306 1.00 51.16 C ANISOU 1495 CG PRO A 227 8121 5987 5330 -3726 944 -580 C ATOM 1496 CD PRO A 227 26.040 -32.024 -8.157 1.00 53.74 C ANISOU 1496 CD PRO A 227 8474 6230 5713 -3705 959 -574 C ATOM 1497 N ARG A 228 28.779 -32.373 -11.872 1.00 62.07 N ANISOU 1497 N ARG A 228 9661 7276 6646 -3750 1070 -772 N ATOM 1498 CA ARG A 228 29.752 -31.522 -12.538 1.00 59.94 C ANISOU 1498 CA ARG A 228 9388 7039 6348 -3712 1109 -810 C ATOM 1499 C ARG A 228 29.109 -30.169 -12.744 1.00 54.62 C ANISOU 1499 C ARG A 228 8666 6461 5624 -3706 1066 -766 C ATOM 1500 O ARG A 228 27.928 -30.094 -13.080 1.00 66.80 O ANISOU 1500 O ARG A 228 10197 8053 7129 -3771 1017 -728 O ATOM 1501 CB ARG A 228 30.142 -32.119 -13.875 1.00 65.27 C ANISOU 1501 CB ARG A 228 10123 7707 6969 -3785 1153 -875 C ATOM 1502 CG ARG A 228 29.943 -33.607 -13.925 1.00 76.94 C ANISOU 1502 CG ARG A 228 11655 9105 8475 -3844 1161 -899 C ATOM 1503 CD ARG A 228 31.259 -34.256 -14.179 1.00 85.91 C ANISOU 1503 CD ARG A 228 12823 10155 9662 -3820 1232 -972 C ATOM 1504 NE ARG A 228 31.174 -35.707 -14.191 1.00 94.48 N ANISOU 1504 NE ARG A 228 13961 11143 10793 -3870 1237 -1001 N ATOM 1505 CZ ARG A 228 32.241 -36.500 -14.134 1.00101.76 C ANISOU 1505 CZ ARG A 228 14905 11960 11801 -3842 1286 -1058 C ATOM 1506 NH1 ARG A 228 33.472 -35.975 -14.094 1.00101.97 N ANISOU 1506 NH1 ARG A 228 14898 11971 11876 -3767 1338 -1092 N ATOM 1507 NH2 ARG A 228 32.077 -37.820 -14.142 1.00105.19 N ANISOU 1507 NH2 ARG A 228 15391 12296 12282 -3891 1278 -1082 N ATOM 1508 N GLY A 229 29.848 -29.101 -12.511 1.00 45.55 N ANISOU 1508 N GLY A 229 7484 5332 4490 -3630 1076 -765 N ATOM 1509 CA GLY A 229 29.235 -27.796 -12.597 1.00 45.00 C ANISOU 1509 CA GLY A 229 7367 5340 4393 -3619 1028 -718 C ATOM 1510 C GLY A 229 29.502 -26.941 -11.376 1.00 46.38 C ANISOU 1510 C GLY A 229 7491 5501 4630 -3522 1014 -684 C ATOM 1511 O GLY A 229 30.558 -27.054 -10.743 1.00 43.50 O ANISOU 1511 O GLY A 229 7131 5080 4315 -3457 1047 -706 O ATOM 1512 N TRP A 230 28.550 -26.088 -11.035 1.00 44.43 N ANISOU 1512 N TRP A 230 7194 5298 4388 -3516 965 -630 N ATOM 1513 CA TRP A 230 28.659 -25.274 -9.840 1.00 47.37 C ANISOU 1513 CA TRP A 230 7526 5656 4818 -3434 953 -597 C ATOM 1514 C TRP A 230 28.081 -26.007 -8.635 1.00 48.32 C ANISOU 1514 C TRP A 230 7642 5732 4984 -3427 953 -574 C ATOM 1515 O TRP A 230 27.038 -26.660 -8.740 1.00 46.94 O ANISOU 1515 O TRP A 230 7462 5568 4804 -3492 936 -553 O ATOM 1516 CB TRP A 230 27.943 -23.948 -10.055 1.00 53.51 C ANISOU 1516 CB TRP A 230 8246 6492 5591 -3430 906 -551 C ATOM 1517 CG TRP A 230 28.706 -22.994 -10.940 1.00 56.23 C ANISOU 1517 CG TRP A 230 8593 6869 5901 -3418 902 -565 C ATOM 1518 CD1 TRP A 230 28.241 -22.350 -12.050 1.00 55.53 C ANISOU 1518 CD1 TRP A 230 8492 6842 5766 -3471 866 -546 C ATOM 1519 CD2 TRP A 230 30.070 -22.564 -10.768 1.00 55.84 C ANISOU 1519 CD2 TRP A 230 8556 6792 5867 -3354 931 -593 C ATOM 1520 NE1 TRP A 230 29.232 -21.555 -12.573 1.00 55.68 N ANISOU 1520 NE1 TRP A 230 8520 6872 5764 -3446 874 -562 N ATOM 1521 CE2 TRP A 230 30.361 -21.673 -11.802 1.00 52.98 C ANISOU 1521 CE2 TRP A 230 8190 6477 5464 -3374 915 -592 C ATOM 1522 CE3 TRP A 230 31.070 -22.851 -9.836 1.00 56.05 C ANISOU 1522 CE3 TRP A 230 8595 6756 5946 -3288 963 -613 C ATOM 1523 CZ2 TRP A 230 31.607 -21.075 -11.931 1.00 48.25 C ANISOU 1523 CZ2 TRP A 230 7594 5865 4875 -3331 935 -612 C ATOM 1524 CZ3 TRP A 230 32.292 -22.248 -9.971 1.00 51.00 C ANISOU 1524 CZ3 TRP A 230 7953 6103 5323 -3243 978 -630 C ATOM 1525 CH2 TRP A 230 32.550 -21.375 -11.008 1.00 45.88 C ANISOU 1525 CH2 TRP A 230 7296 5502 4634 -3265 966 -631 C ATOM 1526 N LEU A 231 28.772 -25.899 -7.501 1.00 50.48 N ANISOU 1526 N LEU A 231 7919 5956 5304 -3355 968 -572 N ATOM 1527 CA LEU A 231 28.334 -26.449 -6.225 1.00 42.54 C ANISOU 1527 CA LEU A 231 6917 4908 4337 -3345 969 -546 C ATOM 1528 C LEU A 231 28.199 -25.286 -5.259 1.00 41.81 C ANISOU 1528 C LEU A 231 6789 4825 4272 -3284 957 -513 C ATOM 1529 O LEU A 231 29.161 -24.546 -5.047 1.00 41.10 O ANISOU 1529 O LEU A 231 6702 4721 4193 -3222 958 -522 O ATOM 1530 CB LEU A 231 29.335 -27.483 -5.705 1.00 42.66 C ANISOU 1530 CB LEU A 231 6982 4844 4382 -3324 995 -571 C ATOM 1531 CG LEU A 231 29.172 -28.042 -4.309 1.00 42.78 C ANISOU 1531 CG LEU A 231 7016 4804 4436 -3309 993 -542 C ATOM 1532 CD1 LEU A 231 27.768 -28.487 -4.179 1.00 43.50 C ANISOU 1532 CD1 LEU A 231 7091 4921 4517 -3377 982 -510 C ATOM 1533 CD2 LEU A 231 30.084 -29.211 -4.146 1.00 43.18 C ANISOU 1533 CD2 LEU A 231 7112 4772 4522 -3307 1007 -565 C ATOM 1534 N ARG A 232 27.010 -25.095 -4.707 1.00 42.07 N ANISOU 1534 N ARG A 232 6786 4879 4322 -3307 946 -473 N ATOM 1535 CA ARG A 232 26.775 -24.025 -3.748 1.00 41.53 C ANISOU 1535 CA ARG A 232 6685 4812 4284 -3256 943 -444 C ATOM 1536 C ARG A 232 26.877 -24.589 -2.348 1.00 41.72 C ANISOU 1536 C ARG A 232 6746 4782 4326 -3239 965 -434 C ATOM 1537 O ARG A 232 26.264 -25.610 -2.048 1.00 46.29 O ANISOU 1537 O ARG A 232 7335 5345 4906 -3290 974 -421 O ATOM 1538 CB ARG A 232 25.406 -23.401 -3.972 1.00 41.89 C ANISOU 1538 CB ARG A 232 6657 4908 4353 -3291 927 -403 C ATOM 1539 CG ARG A 232 24.963 -22.370 -2.963 1.00 41.56 C ANISOU 1539 CG ARG A 232 6574 4861 4355 -3249 936 -371 C ATOM 1540 CD ARG A 232 23.632 -21.823 -3.466 1.00 42.09 C ANISOU 1540 CD ARG A 232 6550 4975 4465 -3290 919 -325 C ATOM 1541 NE ARG A 232 23.058 -20.758 -2.658 1.00 41.93 N ANISOU 1541 NE ARG A 232 6474 4951 4505 -3256 934 -290 N ATOM 1542 CZ ARG A 232 21.771 -20.420 -2.670 1.00 42.58 C ANISOU 1542 CZ ARG A 232 6463 5059 4656 -3290 938 -237 C ATOM 1543 NH1 ARG A 232 20.918 -21.076 -3.428 1.00 48.00 N ANISOU 1543 NH1 ARG A 232 7104 5780 5354 -3362 918 -211 N ATOM 1544 NH2 ARG A 232 21.326 -19.437 -1.907 1.00 42.47 N ANISOU 1544 NH2 ARG A 232 6399 5034 4706 -3254 964 -207 N ATOM 1545 N LEU A 233 27.667 -23.952 -1.503 1.00 40.94 N ANISOU 1545 N LEU A 233 6669 4650 4236 -3174 968 -436 N ATOM 1546 CA LEU A 233 27.920 -24.462 -0.162 1.00 41.04 C ANISOU 1546 CA LEU A 233 6730 4606 4256 -3160 983 -425 C ATOM 1547 C LEU A 233 27.611 -23.350 0.824 1.00 41.86 C ANISOU 1547 C LEU A 233 6822 4711 4370 -3124 991 -404 C ATOM 1548 O LEU A 233 28.265 -22.300 0.783 1.00 39.97 O ANISOU 1548 O LEU A 233 6579 4472 4136 -3070 976 -411 O ATOM 1549 CB LEU A 233 29.366 -24.920 -0.013 1.00 40.76 C ANISOU 1549 CB LEU A 233 6746 4513 4227 -3122 975 -446 C ATOM 1550 CG LEU A 233 29.833 -26.167 -0.728 1.00 41.25 C ANISOU 1550 CG LEU A 233 6831 4547 4295 -3153 977 -469 C ATOM 1551 CD1 LEU A 233 31.106 -26.582 -0.104 1.00 41.12 C ANISOU 1551 CD1 LEU A 233 6854 4454 4313 -3112 968 -473 C ATOM 1552 CD2 LEU A 233 28.813 -27.223 -0.578 1.00 42.13 C ANISOU 1552 CD2 LEU A 233 6952 4656 4400 -3222 985 -453 C ATOM 1553 N ARG A 234 26.607 -23.569 1.688 1.00 41.21 N ANISOU 1553 N ARG A 234 6736 4628 4295 -3157 1017 -376 N ATOM 1554 CA ARG A 234 26.272 -22.632 2.765 1.00 41.04 C ANISOU 1554 CA ARG A 234 6714 4597 4282 -3130 1040 -358 C ATOM 1555 C ARG A 234 27.102 -23.031 3.970 1.00 40.99 C ANISOU 1555 C ARG A 234 6796 4528 4250 -3110 1042 -360 C ATOM 1556 O ARG A 234 26.735 -23.948 4.700 1.00 48.62 O ANISOU 1556 O ARG A 234 7799 5471 5204 -3152 1062 -342 O ATOM 1557 CB ARG A 234 24.787 -22.642 3.106 1.00 41.81 C ANISOU 1557 CB ARG A 234 6754 4723 4407 -3180 1078 -324 C ATOM 1558 CG ARG A 234 23.847 -22.983 1.987 1.00 42.35 C ANISOU 1558 CG ARG A 234 6745 4844 4504 -3233 1067 -307 C ATOM 1559 CD ARG A 234 22.484 -22.278 2.168 1.00 42.88 C ANISOU 1559 CD ARG A 234 6716 4945 4631 -3255 1100 -262 C ATOM 1560 NE ARG A 234 21.599 -22.424 1.001 1.00 43.42 N ANISOU 1560 NE ARG A 234 6696 5064 4737 -3305 1076 -237 N ATOM 1561 CZ ARG A 234 20.565 -21.634 0.711 1.00 43.78 C ANISOU 1561 CZ ARG A 234 6636 5146 4854 -3316 1084 -192 C ATOM 1562 NH1 ARG A 234 20.244 -20.614 1.495 1.00 43.67 N ANISOU 1562 NH1 ARG A 234 6587 5122 4884 -3279 1126 -170 N ATOM 1563 NH2 ARG A 234 19.856 -21.867 -0.383 1.00 44.35 N ANISOU 1563 NH2 ARG A 234 6636 5259 4956 -3368 1051 -166 N ATOM 1564 N LEU A 235 28.240 -22.362 4.171 1.00 40.28 N ANISOU 1564 N LEU A 235 6742 4409 4155 -3051 1017 -373 N ATOM 1565 CA LEU A 235 29.167 -22.698 5.236 1.00 40.27 C ANISOU 1565 CA LEU A 235 6822 4343 4135 -3032 1004 -368 C ATOM 1566 C LEU A 235 28.777 -21.987 6.508 1.00 40.36 C ANISOU 1566 C LEU A 235 6875 4336 4124 -3027 1030 -353 C ATOM 1567 O LEU A 235 28.434 -20.801 6.480 1.00 44.03 O ANISOU 1567 O LEU A 235 7308 4822 4598 -3002 1043 -357 O ATOM 1568 CB LEU A 235 30.581 -22.280 4.887 1.00 39.61 C ANISOU 1568 CB LEU A 235 6748 4233 4069 -2976 960 -380 C ATOM 1569 CG LEU A 235 31.208 -22.926 3.687 1.00 39.55 C ANISOU 1569 CG LEU A 235 6709 4232 4087 -2976 942 -399 C ATOM 1570 CD1 LEU A 235 32.350 -22.052 3.319 1.00 38.91 C ANISOU 1570 CD1 LEU A 235 6612 4140 4030 -2921 910 -406 C ATOM 1571 CD2 LEU A 235 31.680 -24.301 4.043 1.00 40.11 C ANISOU 1571 CD2 LEU A 235 6824 4245 4169 -2999 934 -392 C ATOM 1572 N LEU A 236 28.891 -22.702 7.625 1.00 40.89 N ANISOU 1572 N LEU A 236 7019 4356 4160 -3052 1036 -335 N ATOM 1573 CA LEU A 236 28.557 -22.162 8.935 1.00 41.15 C ANISOU 1573 CA LEU A 236 7114 4365 4157 -3058 1069 -323 C ATOM 1574 C LEU A 236 29.589 -22.612 9.940 1.00 41.32 C ANISOU 1574 C LEU A 236 7240 4315 4144 -3053 1030 -308 C ATOM 1575 O LEU A 236 29.749 -23.812 10.166 1.00 41.88 O ANISOU 1575 O LEU A 236 7345 4357 4211 -3088 1015 -289 O ATOM 1576 CB LEU A 236 27.176 -22.609 9.387 1.00 42.05 C ANISOU 1576 CB LEU A 236 7211 4502 4262 -3121 1134 -304 C ATOM 1577 CG LEU A 236 26.981 -22.546 10.902 1.00 42.65 C ANISOU 1577 CG LEU A 236 7382 4538 4285 -3146 1173 -286 C ATOM 1578 CD1 LEU A 236 26.992 -21.097 11.397 1.00 42.24 C ANISOU 1578 CD1 LEU A 236 7349 4478 4223 -3106 1198 -300 C ATOM 1579 CD2 LEU A 236 25.695 -23.259 11.301 1.00 43.75 C ANISOU 1579 CD2 LEU A 236 7499 4702 4424 -3219 1240 -255 C ATOM 1580 N ASN A 237 30.278 -21.657 10.546 1.00 40.92 N ANISOU 1580 N ASN A 237 7241 4233 4076 -3012 1006 -310 N ATOM 1581 CA ASN A 237 31.189 -21.980 11.630 1.00 41.23 C ANISOU 1581 CA ASN A 237 7385 4200 4079 -3013 962 -287 C ATOM 1582 C ASN A 237 30.358 -22.097 12.887 1.00 42.03 C ANISOU 1582 C ASN A 237 7571 4286 4113 -3065 1016 -273 C ATOM 1583 O ASN A 237 29.865 -21.095 13.409 1.00 42.02 O ANISOU 1583 O ASN A 237 7594 4290 4081 -3060 1061 -286 O ATOM 1584 CB ASN A 237 32.267 -20.926 11.814 1.00 40.65 C ANISOU 1584 CB ASN A 237 7339 4092 4012 -2957 906 -290 C ATOM 1585 CG ASN A 237 33.349 -21.383 12.771 1.00 45.27 C ANISOU 1585 CG ASN A 237 8020 4598 4581 -2959 837 -258 C ATOM 1586 OD1 ASN A 237 33.116 -22.234 13.635 1.00 41.81 O ANISOU 1586 OD1 ASN A 237 7660 4128 4099 -3006 843 -235 O ATOM 1587 ND2 ASN A 237 34.541 -20.798 12.640 1.00 47.21 N ANISOU 1587 ND2 ASN A 237 8262 4809 4868 -2910 765 -251 N ATOM 1588 N GLY A 238 30.200 -23.309 13.369 1.00 42.83 N ANISOU 1588 N GLY A 238 7718 4363 4193 -3118 1016 -246 N ATOM 1589 CA GLY A 238 29.424 -23.491 14.560 1.00 43.75 C ANISOU 1589 CA GLY A 238 7917 4466 4242 -3176 1072 -227 C ATOM 1590 C GLY A 238 30.290 -23.972 15.688 1.00 44.30 C ANISOU 1590 C GLY A 238 8119 4457 4256 -3195 1015 -194 C ATOM 1591 O GLY A 238 29.775 -24.588 16.621 1.00 45.31 O ANISOU 1591 O GLY A 238 8325 4564 4326 -3259 1047 -166 O ATOM 1592 N CYS A 239 31.595 -23.728 15.618 1.00 43.79 N ANISOU 1592 N CYS A 239 8077 4347 4214 -3145 926 -190 N ATOM 1593 CA CYS A 239 32.436 -24.115 16.734 1.00 49.42 C ANISOU 1593 CA CYS A 239 8917 4978 4881 -3164 857 -152 C ATOM 1594 C CYS A 239 32.130 -23.260 17.954 1.00 52.69 C ANISOU 1594 C CYS A 239 9459 5374 5188 -3190 893 -157 C ATOM 1595 O CYS A 239 31.479 -22.214 17.877 1.00 44.78 O ANISOU 1595 O CYS A 239 8466 4410 4139 -3197 971 -201 O ATOM 1596 CB CYS A 239 33.903 -23.966 16.393 1.00 48.30 C ANISOU 1596 CB CYS A 239 8758 4788 4807 -3104 751 -141 C ATOM 1597 SG CYS A 239 34.452 -25.150 15.242 1.00 49.41 S ANISOU 1597 SG CYS A 239 8790 4918 5064 -3088 708 -132 S ATOM 1598 N ASN A 240 32.629 -23.701 19.098 1.00 52.97 N ANISOU 1598 N ASN A 240 9658 5338 5130 -3248 846 -124 N ATOM 1599 CA ASN A 240 32.420 -22.854 20.254 1.00 50.10 C ANISOU 1599 CA ASN A 240 9500 4944 4591 -3321 892 -149 C ATOM 1600 C ASN A 240 33.405 -21.704 20.239 1.00 48.10 C ANISOU 1600 C ASN A 240 9272 4660 4344 -3259 820 -162 C ATOM 1601 O ASN A 240 33.011 -20.536 20.294 1.00 47.96 O ANISOU 1601 O ASN A 240 9300 4658 4265 -3263 886 -209 O ATOM 1602 CB ASN A 240 32.526 -23.674 21.527 1.00 54.90 C ANISOU 1602 CB ASN A 240 10300 5487 5074 -3419 866 -108 C ATOM 1603 CG ASN A 240 31.209 -24.326 21.883 1.00 60.05 C ANISOU 1603 CG ASN A 240 10985 6172 5658 -3515 985 -110 C ATOM 1604 OD1 ASN A 240 30.403 -24.627 20.994 1.00 60.73 O ANISOU 1604 OD1 ASN A 240 10904 6326 5844 -3492 1048 -119 O ATOM 1605 ND2 ASN A 240 30.969 -24.533 23.176 1.00 61.91 N ANISOU 1605 ND2 ASN A 240 11436 6360 5729 -3624 1014 -98 N ATOM 1606 N ALA A 241 34.687 -22.004 20.124 1.00 47.52 N ANISOU 1606 N ALA A 241 9157 4537 4363 -3198 687 -119 N ATOM 1607 CA ALA A 241 35.668 -20.940 20.013 1.00 47.20 C ANISOU 1607 CA ALA A 241 9107 4467 4361 -3132 608 -122 C ATOM 1608 C ALA A 241 36.526 -21.051 18.781 1.00 49.29 C ANISOU 1608 C ALA A 241 9160 4746 4823 -3029 536 -112 C ATOM 1609 O ALA A 241 37.200 -20.072 18.436 1.00 43.71 O ANISOU 1609 O ALA A 241 8415 4031 4161 -2977 488 -123 O ATOM 1610 CB ALA A 241 36.584 -20.907 21.240 1.00 47.83 C ANISOU 1610 CB ALA A 241 9378 4452 4342 -3174 501 -84 C ATOM 1611 N ARG A 242 36.540 -22.203 18.118 1.00 51.04 N ANISOU 1611 N ARG A 242 9298 4978 5118 -3036 535 -99 N ATOM 1612 CA ARG A 242 37.472 -22.413 17.027 1.00 43.42 C ANISOU 1612 CA ARG A 242 8203 4005 4288 -2982 476 -98 C ATOM 1613 C ARG A 242 37.040 -21.611 15.826 1.00 42.40 C ANISOU 1613 C ARG A 242 7952 3958 4201 -2941 541 -144 C ATOM 1614 O ARG A 242 35.918 -21.752 15.340 1.00 43.21 O ANISOU 1614 O ARG A 242 8010 4129 4279 -2960 634 -170 O ATOM 1615 CB ARG A 242 37.566 -23.884 16.668 1.00 43.85 C ANISOU 1615 CB ARG A 242 8214 4037 4409 -3004 464 -76 C ATOM 1616 CG ARG A 242 38.382 -24.110 15.427 1.00 43.30 C ANISOU 1616 CG ARG A 242 8005 3963 4482 -2952 431 -87 C ATOM 1617 CD ARG A 242 38.636 -25.581 15.227 1.00 49.80 C ANISOU 1617 CD ARG A 242 8805 4734 5382 -2972 405 -64 C ATOM 1618 NE ARG A 242 39.254 -26.240 16.377 1.00 48.37 N ANISOU 1618 NE ARG A 242 8728 4454 5197 -3002 317 -11 N ATOM 1619 CZ ARG A 242 40.549 -26.183 16.651 1.00 48.61 C ANISOU 1619 CZ ARG A 242 8755 4397 5317 -2970 208 15 C ATOM 1620 NH1 ARG A 242 41.371 -25.514 15.851 1.00 44.57 N ANISOU 1620 NH1 ARG A 242 8138 3887 4910 -2911 182 -8 N ATOM 1621 NH2 ARG A 242 41.025 -26.828 17.702 1.00 53.41 N ANISOU 1621 NH2 ARG A 242 9462 4913 5917 -3002 124 67 N ATOM 1622 N SER A 243 37.915 -20.749 15.365 1.00 42.17 N ANISOU 1622 N SER A 243 7869 3918 4236 -2888 486 -149 N ATOM 1623 CA SER A 243 37.689 -20.123 14.089 1.00 40.98 C ANISOU 1623 CA SER A 243 7595 3836 4140 -2850 530 -184 C ATOM 1624 C SER A 243 38.222 -21.039 12.996 1.00 46.32 C ANISOU 1624 C SER A 243 8160 4514 4924 -2834 515 -185 C ATOM 1625 O SER A 243 39.123 -21.853 13.221 1.00 45.91 O ANISOU 1625 O SER A 243 8113 4392 4938 -2833 447 -157 O ATOM 1626 CB SER A 243 38.363 -18.765 14.053 1.00 40.58 C ANISOU 1626 CB SER A 243 7536 3771 4111 -2807 480 -188 C ATOM 1627 OG SER A 243 39.736 -18.958 13.812 1.00 40.81 O ANISOU 1627 OG SER A 243 7519 3742 4244 -2778 385 -165 O ATOM 1628 N LEU A 244 37.621 -20.937 11.817 1.00 47.05 N ANISOU 1628 N LEU A 244 8158 4682 5037 -2824 580 -218 N ATOM 1629 CA LEU A 244 37.958 -21.785 10.689 1.00 40.14 C ANISOU 1629 CA LEU A 244 7187 3816 4247 -2815 584 -229 C ATOM 1630 C LEU A 244 38.455 -20.954 9.510 1.00 43.79 C ANISOU 1630 C LEU A 244 7550 4314 4772 -2772 580 -251 C ATOM 1631 O LEU A 244 38.292 -19.733 9.446 1.00 38.99 O ANISOU 1631 O LEU A 244 6938 3740 4138 -2752 585 -260 O ATOM 1632 CB LEU A 244 36.753 -22.623 10.276 1.00 40.30 C ANISOU 1632 CB LEU A 244 7195 3891 4226 -2856 661 -246 C ATOM 1633 CG LEU A 244 36.403 -23.602 11.383 1.00 41.49 C ANISOU 1633 CG LEU A 244 7439 3995 4330 -2905 658 -217 C ATOM 1634 CD1 LEU A 244 34.989 -24.129 11.251 1.00 41.40 C ANISOU 1634 CD1 LEU A 244 7428 4042 4260 -2955 738 -230 C ATOM 1635 CD2 LEU A 244 37.418 -24.723 11.376 1.00 41.66 C ANISOU 1635 CD2 LEU A 244 7453 3934 4441 -2903 594 -192 C ATOM 1636 N ASN A 245 39.067 -21.637 8.557 1.00 42.36 N ANISOU 1636 N ASN A 245 7292 4123 4679 -2762 574 -261 N ATOM 1637 CA ASN A 245 39.566 -20.944 7.383 1.00 38.92 C ANISOU 1637 CA ASN A 245 6766 3722 4299 -2730 576 -283 C ATOM 1638 C ASN A 245 39.528 -21.903 6.211 1.00 39.00 C ANISOU 1638 C ASN A 245 6711 3754 4354 -2742 617 -310 C ATOM 1639 O ASN A 245 40.481 -22.646 5.988 1.00 39.37 O ANISOU 1639 O ASN A 245 6724 3736 4498 -2734 586 -308 O ATOM 1640 CB ASN A 245 40.967 -20.436 7.608 1.00 50.29 C ANISOU 1640 CB ASN A 245 8183 5094 5833 -2697 495 -263 C ATOM 1641 CG ASN A 245 41.424 -19.579 6.483 1.00 47.82 C ANISOU 1641 CG ASN A 245 7784 4819 5567 -2672 499 -281 C ATOM 1642 OD1 ASN A 245 40.615 -19.151 5.648 1.00 38.07 O ANISOU 1642 OD1 ASN A 245 6522 3666 4276 -2679 557 -305 O ATOM 1643 ND2 ASN A 245 42.711 -19.254 6.478 1.00 47.75 N ANISOU 1643 ND2 ASN A 245 7731 4748 5662 -2648 432 -266 N ATOM 1644 N PHE A 246 38.453 -21.832 5.452 1.00 44.95 N ANISOU 1644 N PHE A 246 7446 4590 5042 -2762 682 -337 N ATOM 1645 CA PHE A 246 38.180 -22.780 4.396 1.00 38.93 C ANISOU 1645 CA PHE A 246 6644 3853 4295 -2786 726 -366 C ATOM 1646 C PHE A 246 39.052 -22.506 3.175 1.00 46.96 C ANISOU 1646 C PHE A 246 7586 4880 5379 -2766 726 -390 C ATOM 1647 O PHE A 246 39.553 -21.398 2.960 1.00 38.31 O ANISOU 1647 O PHE A 246 6459 3798 4298 -2738 704 -386 O ATOM 1648 CB PHE A 246 36.701 -22.726 4.047 1.00 38.83 C ANISOU 1648 CB PHE A 246 6638 3923 4194 -2821 784 -382 C ATOM 1649 CG PHE A 246 35.826 -23.078 5.195 1.00 45.20 C ANISOU 1649 CG PHE A 246 7511 4719 4942 -2850 794 -362 C ATOM 1650 CD1 PHE A 246 35.919 -24.320 5.797 1.00 39.85 C ANISOU 1650 CD1 PHE A 246 6877 3982 4281 -2877 784 -345 C ATOM 1651 CD2 PHE A 246 34.956 -22.141 5.731 1.00 45.36 C ANISOU 1651 CD2 PHE A 246 7554 4780 4901 -2852 813 -357 C ATOM 1652 CE1 PHE A 246 35.135 -24.631 6.878 1.00 40.27 C ANISOU 1652 CE1 PHE A 246 6998 4026 4276 -2911 795 -323 C ATOM 1653 CE2 PHE A 246 34.161 -22.461 6.821 1.00 39.38 C ANISOU 1653 CE2 PHE A 246 6861 4011 4092 -2885 833 -340 C ATOM 1654 CZ PHE A 246 34.263 -23.693 7.394 1.00 40.04 C ANISOU 1654 CZ PHE A 246 6991 4043 4179 -2916 824 -322 C ATOM 1655 N ALA A 247 39.276 -23.568 2.419 1.00 45.96 N ANISOU 1655 N ALA A 247 7433 4735 5295 -2784 751 -415 N ATOM 1656 CA ALA A 247 40.053 -23.607 1.192 1.00 43.02 C ANISOU 1656 CA ALA A 247 6997 4366 4983 -2778 769 -448 C ATOM 1657 C ALA A 247 39.822 -24.997 0.614 1.00 49.37 C ANISOU 1657 C ALA A 247 7806 5150 5802 -2813 809 -477 C ATOM 1658 O ALA A 247 39.162 -25.833 1.236 1.00 42.39 O ANISOU 1658 O ALA A 247 6969 4244 4892 -2838 809 -464 O ATOM 1659 CB ALA A 247 41.523 -23.343 1.461 1.00 39.25 C ANISOU 1659 CB ALA A 247 6478 3809 4624 -2741 715 -432 C ATOM 1660 N THR A 248 40.349 -25.243 -0.585 1.00 55.89 N ANISOU 1660 N THR A 248 8587 5982 6667 -2822 843 -518 N ATOM 1661 CA THR A 248 40.202 -26.535 -1.237 1.00 51.74 C ANISOU 1661 CA THR A 248 8069 5430 6159 -2858 883 -555 C ATOM 1662 C THR A 248 41.555 -27.217 -1.323 1.00 46.88 C ANISOU 1662 C THR A 248 7415 4708 5690 -2839 866 -569 C ATOM 1663 O THR A 248 42.571 -26.569 -1.585 1.00 47.93 O ANISOU 1663 O THR A 248 7494 4825 5894 -2810 852 -572 O ATOM 1664 CB THR A 248 39.609 -26.410 -2.645 1.00 42.33 C ANISOU 1664 CB THR A 248 6869 4327 4888 -2897 946 -601 C ATOM 1665 OG1 THR A 248 40.510 -25.683 -3.477 1.00 41.90 O ANISOU 1665 OG1 THR A 248 6764 4289 4867 -2881 961 -625 O ATOM 1666 CG2 THR A 248 38.254 -25.731 -2.630 1.00 40.11 C ANISOU 1666 CG2 THR A 248 6613 4142 4486 -2918 952 -586 C ATOM 1667 N SER A 249 41.546 -28.533 -1.119 1.00 48.26 N ANISOU 1667 N SER A 249 7612 4804 5919 -2858 863 -576 N ATOM 1668 CA SER A 249 42.729 -29.384 -1.175 1.00 51.87 C ANISOU 1668 CA SER A 249 8033 5140 6534 -2843 841 -593 C ATOM 1669 C SER A 249 43.625 -29.061 -2.370 1.00 52.01 C ANISOU 1669 C SER A 249 7987 5168 6607 -2839 886 -644 C ATOM 1670 O SER A 249 44.861 -29.037 -2.245 1.00 51.91 O ANISOU 1670 O SER A 249 7916 5070 6736 -2808 849 -642 O ATOM 1671 CB SER A 249 42.303 -30.860 -1.194 1.00 55.00 C ANISOU 1671 CB SER A 249 8471 5471 6954 -2880 851 -609 C ATOM 1672 OG SER A 249 42.111 -31.363 -2.509 1.00 54.46 O ANISOU 1672 OG SER A 249 8402 5432 6860 -2918 925 -675 O ATOM 1673 N ASP A 250 43.022 -28.794 -3.531 1.00 48.57 N ANISOU 1673 N ASP A 250 7560 4832 6061 -2874 962 -689 N ATOM 1674 CA ASP A 250 43.793 -28.582 -4.743 1.00 52.39 C ANISOU 1674 CA ASP A 250 7998 5330 6578 -2884 1019 -744 C ATOM 1675 C ASP A 250 43.752 -27.136 -5.199 1.00 55.31 C ANISOU 1675 C ASP A 250 8344 5805 6868 -2878 1032 -736 C ATOM 1676 O ASP A 250 44.062 -26.853 -6.359 1.00 61.31 O ANISOU 1676 O ASP A 250 9082 6610 7604 -2904 1093 -783 O ATOM 1677 CB ASP A 250 43.304 -29.489 -5.866 1.00 55.29 C ANISOU 1677 CB ASP A 250 8400 5716 6891 -2940 1098 -812 C ATOM 1678 CG ASP A 250 41.867 -29.243 -6.235 1.00 61.80 C ANISOU 1678 CG ASP A 250 9280 6654 7548 -2983 1124 -809 C ATOM 1679 OD1 ASP A 250 41.286 -28.229 -5.789 1.00 61.74 O ANISOU 1679 OD1 ASP A 250 9276 6721 7463 -2967 1092 -764 O ATOM 1680 OD2 ASP A 250 41.324 -30.068 -7.000 1.00 67.70 O ANISOU 1680 OD2 ASP A 250 10065 7410 8246 -3036 1172 -854 O ATOM 1681 N ASN A 251 43.318 -26.227 -4.332 1.00 57.06 N ANISOU 1681 N ASN A 251 8577 6064 7040 -2851 977 -678 N ATOM 1682 CA ASN A 251 43.500 -24.782 -4.499 1.00 58.74 C ANISOU 1682 CA ASN A 251 8760 6343 7216 -2834 961 -657 C ATOM 1683 C ASN A 251 42.694 -24.202 -5.645 1.00 56.93 C ANISOU 1683 C ASN A 251 8549 6229 6854 -2874 1015 -686 C ATOM 1684 O ASN A 251 43.106 -23.211 -6.231 1.00 56.86 O ANISOU 1684 O ASN A 251 8507 6264 6834 -2874 1020 -687 O ATOM 1685 CB ASN A 251 44.972 -24.405 -4.667 1.00 63.46 C ANISOU 1685 CB ASN A 251 9284 6883 7946 -2811 944 -658 C ATOM 1686 CG ASN A 251 45.771 -24.690 -3.426 1.00 75.06 C ANISOU 1686 CG ASN A 251 10729 8238 9553 -2769 862 -614 C ATOM 1687 OD1 ASN A 251 46.688 -25.511 -3.449 1.00 80.54 O ANISOU 1687 OD1 ASN A 251 11383 8834 10383 -2764 854 -630 O ATOM 1688 ND2 ASN A 251 45.417 -24.026 -2.315 1.00 78.65 N ANISOU 1688 ND2 ASN A 251 11212 8697 9975 -2743 795 -558 N ATOM 1689 N ARG A 252 41.544 -24.782 -5.969 1.00 51.27 N ANISOU 1689 N ARG A 252 7882 5558 6040 -2913 1047 -705 N ATOM 1690 CA ARG A 252 40.602 -24.057 -6.798 1.00 48.05 C ANISOU 1690 CA ARG A 252 7494 5258 5507 -2949 1067 -712 C ATOM 1691 C ARG A 252 39.933 -22.964 -5.968 1.00 49.07 C ANISOU 1691 C ARG A 252 7628 5426 5591 -2919 1010 -656 C ATOM 1692 O ARG A 252 39.754 -23.114 -4.755 1.00 57.28 O ANISOU 1692 O ARG A 252 8683 6423 6658 -2889 971 -620 O ATOM 1693 CB ARG A 252 39.571 -25.004 -7.407 1.00 46.55 C ANISOU 1693 CB ARG A 252 7351 5099 5238 -3007 1106 -744 C ATOM 1694 CG ARG A 252 38.503 -25.522 -6.507 1.00 45.93 C ANISOU 1694 CG ARG A 252 7310 5014 5129 -3011 1078 -712 C ATOM 1695 CD ARG A 252 37.817 -26.708 -7.155 1.00 44.74 C ANISOU 1695 CD ARG A 252 7198 4864 4937 -3073 1116 -749 C ATOM 1696 NE ARG A 252 38.691 -27.868 -7.273 1.00 46.14 N ANISOU 1696 NE ARG A 252 7378 4950 5204 -3076 1146 -787 N ATOM 1697 CZ ARG A 252 38.330 -29.013 -7.845 1.00 57.34 C ANISOU 1697 CZ ARG A 252 8832 6345 6608 -3130 1180 -825 C ATOM 1698 NH1 ARG A 252 37.112 -29.155 -8.359 1.00 59.78 N ANISOU 1698 NH1 ARG A 252 9178 6722 6815 -3189 1186 -826 N ATOM 1699 NH2 ARG A 252 39.186 -30.024 -7.916 1.00 64.71 N ANISOU 1699 NH2 ARG A 252 9764 7181 7641 -3127 1204 -861 N ATOM 1700 N PRO A 253 39.589 -21.844 -6.585 1.00 41.67 N ANISOU 1700 N PRO A 253 6680 4562 4589 -2930 1003 -648 N ATOM 1701 CA PRO A 253 39.078 -20.710 -5.819 1.00 38.51 C ANISOU 1701 CA PRO A 253 6279 4187 4166 -2899 949 -597 C ATOM 1702 C PRO A 253 37.667 -20.964 -5.319 1.00 38.43 C ANISOU 1702 C PRO A 253 6304 4207 4092 -2914 942 -582 C ATOM 1703 O PRO A 253 36.912 -21.738 -5.899 1.00 62.03 O ANISOU 1703 O PRO A 253 9313 7225 7032 -2961 973 -606 O ATOM 1704 CB PRO A 253 39.098 -19.583 -6.850 1.00 38.37 C ANISOU 1704 CB PRO A 253 6239 4235 4106 -2918 946 -597 C ATOM 1705 CG PRO A 253 38.777 -20.273 -8.089 1.00 38.90 C ANISOU 1705 CG PRO A 253 6322 4344 4114 -2978 997 -643 C ATOM 1706 CD PRO A 253 39.471 -21.605 -8.025 1.00 39.40 C ANISOU 1706 CD PRO A 253 6391 4342 4236 -2980 1041 -683 C ATOM 1707 N LEU A 254 37.306 -20.298 -4.236 1.00 38.01 N ANISOU 1707 N LEU A 254 6257 4143 4043 -2880 903 -542 N ATOM 1708 CA LEU A 254 35.921 -20.240 -3.812 1.00 37.96 C ANISOU 1708 CA LEU A 254 6269 4171 3981 -2897 899 -525 C ATOM 1709 C LEU A 254 35.337 -18.901 -4.216 1.00 37.63 C ANISOU 1709 C LEU A 254 6202 4185 3908 -2897 875 -504 C ATOM 1710 O LEU A 254 35.965 -17.866 -4.014 1.00 48.22 O ANISOU 1710 O LEU A 254 7528 5513 5279 -2862 844 -484 O ATOM 1711 CB LEU A 254 35.811 -20.428 -2.309 1.00 37.85 C ANISOU 1711 CB LEU A 254 6286 4106 3991 -2868 882 -499 C ATOM 1712 CG LEU A 254 36.550 -21.659 -1.835 1.00 38.23 C ANISOU 1712 CG LEU A 254 6355 4083 4088 -2865 889 -508 C ATOM 1713 CD1 LEU A 254 36.433 -21.781 -0.360 1.00 38.21 C ANISOU 1713 CD1 LEU A 254 6392 4032 4096 -2845 864 -476 C ATOM 1714 CD2 LEU A 254 35.924 -22.838 -2.500 1.00 38.78 C ANISOU 1714 CD2 LEU A 254 6437 4169 4128 -2916 927 -536 C ATOM 1715 N TYR A 255 34.143 -18.910 -4.774 1.00 37.83 N ANISOU 1715 N TYR A 255 6222 4265 3886 -2938 880 -504 N ATOM 1716 CA TYR A 255 33.463 -17.676 -5.145 1.00 37.64 C ANISOU 1716 CA TYR A 255 6166 4285 3849 -2942 850 -476 C ATOM 1717 C TYR A 255 32.428 -17.343 -4.081 1.00 38.96 C ANISOU 1717 C TYR A 255 6331 4444 4029 -2928 841 -448 C ATOM 1718 O TYR A 255 31.341 -17.919 -4.062 1.00 42.05 O ANISOU 1718 O TYR A 255 6717 4857 4404 -2964 855 -446 O ATOM 1719 CB TYR A 255 32.826 -17.806 -6.523 1.00 42.40 C ANISOU 1719 CB TYR A 255 6755 4951 4403 -3003 853 -486 C ATOM 1720 CG TYR A 255 33.832 -17.890 -7.637 1.00 46.14 C ANISOU 1720 CG TYR A 255 7235 5438 4857 -3022 867 -514 C ATOM 1721 CD1 TYR A 255 34.507 -19.069 -7.903 1.00 49.88 C ANISOU 1721 CD1 TYR A 255 7735 5890 5329 -3038 912 -558 C ATOM 1722 CD2 TYR A 255 34.143 -16.766 -8.399 1.00 47.38 C ANISOU 1722 CD2 TYR A 255 7371 5626 5006 -3027 839 -497 C ATOM 1723 CE1 TYR A 255 35.457 -19.141 -8.922 1.00 55.86 C ANISOU 1723 CE1 TYR A 255 8494 6656 6076 -3060 938 -591 C ATOM 1724 CE2 TYR A 255 35.095 -16.815 -9.411 1.00 53.02 C ANISOU 1724 CE2 TYR A 255 8091 6354 5701 -3053 859 -525 C ATOM 1725 CZ TYR A 255 35.750 -18.009 -9.676 1.00 57.75 C ANISOU 1725 CZ TYR A 255 8714 6932 6297 -3069 914 -575 C ATOM 1726 OH TYR A 255 36.690 -18.067 -10.698 1.00 61.40 O ANISOU 1726 OH TYR A 255 9178 7405 6745 -3099 947 -609 O ATOM 1727 N VAL A 256 32.763 -16.407 -3.192 1.00 43.26 N ANISOU 1727 N VAL A 256 6877 4952 4606 -2881 819 -426 N ATOM 1728 CA VAL A 256 31.823 -15.986 -2.162 1.00 44.47 C ANISOU 1728 CA VAL A 256 7031 5092 4773 -2869 821 -404 C ATOM 1729 C VAL A 256 30.688 -15.232 -2.819 1.00 37.25 C ANISOU 1729 C VAL A 256 6063 4222 3869 -2894 808 -381 C ATOM 1730 O VAL A 256 30.916 -14.308 -3.599 1.00 41.23 O ANISOU 1730 O VAL A 256 6539 4742 4383 -2891 775 -366 O ATOM 1731 CB VAL A 256 32.493 -15.098 -1.104 1.00 36.70 C ANISOU 1731 CB VAL A 256 6072 4055 3818 -2818 800 -389 C ATOM 1732 CG1 VAL A 256 31.503 -14.849 -0.028 1.00 38.77 C ANISOU 1732 CG1 VAL A 256 6345 4298 4086 -2816 819 -376 C ATOM 1733 CG2 VAL A 256 33.746 -15.724 -0.515 1.00 36.62 C ANISOU 1733 CG2 VAL A 256 6104 3995 3815 -2794 796 -400 C ATOM 1734 N ILE A 257 29.457 -15.620 -2.508 1.00 37.63 N ANISOU 1734 N ILE A 257 6091 4284 3923 -2923 830 -372 N ATOM 1735 CA ILE A 257 28.291 -14.923 -3.043 1.00 37.92 C ANISOU 1735 CA ILE A 257 6061 4353 3994 -2948 814 -338 C ATOM 1736 C ILE A 257 27.362 -14.413 -1.964 1.00 45.04 C ANISOU 1736 C ILE A 257 6937 5227 4947 -2935 837 -314 C ATOM 1737 O ILE A 257 26.470 -13.601 -2.270 1.00 38.29 O ANISOU 1737 O ILE A 257 6015 4384 4150 -2945 824 -278 O ATOM 1738 CB ILE A 257 27.502 -15.811 -4.019 1.00 38.52 C ANISOU 1738 CB ILE A 257 6109 4480 4047 -3013 816 -338 C ATOM 1739 CG1 ILE A 257 26.764 -16.918 -3.251 1.00 38.97 C ANISOU 1739 CG1 ILE A 257 6174 4530 4103 -3040 856 -343 C ATOM 1740 CG2 ILE A 257 28.447 -16.420 -5.016 1.00 38.49 C ANISOU 1740 CG2 ILE A 257 6142 4497 3985 -3031 809 -371 C ATOM 1741 CD1 ILE A 257 25.598 -17.499 -3.949 1.00 39.72 C ANISOU 1741 CD1 ILE A 257 6219 4668 4205 -3107 852 -322 C ATOM 1742 N ALA A 258 27.471 -14.889 -0.722 1.00 38.39 N ANISOU 1742 N ALA A 258 6145 4348 4094 -2919 875 -329 N ATOM 1743 CA ALA A 258 26.697 -14.210 0.303 1.00 38.18 C ANISOU 1743 CA ALA A 258 6101 4291 4114 -2906 905 -308 C ATOM 1744 C ALA A 258 27.368 -14.342 1.651 1.00 37.96 C ANISOU 1744 C ALA A 258 6159 4210 4055 -2876 929 -328 C ATOM 1745 O ALA A 258 28.171 -15.252 1.886 1.00 37.86 O ANISOU 1745 O ALA A 258 6206 4186 3992 -2875 928 -351 O ATOM 1746 CB ALA A 258 25.281 -14.734 0.370 1.00 38.91 C ANISOU 1746 CB ALA A 258 6133 4411 4240 -2954 944 -284 C ATOM 1747 N SER A 259 27.009 -13.410 2.527 1.00 37.99 N ANISOU 1747 N SER A 259 6167 4175 4092 -2854 951 -316 N ATOM 1748 CA SER A 259 27.470 -13.320 3.899 1.00 37.92 C ANISOU 1748 CA SER A 259 6246 4111 4052 -2832 975 -330 C ATOM 1749 C SER A 259 26.294 -13.486 4.847 1.00 48.85 C ANISOU 1749 C SER A 259 7624 5485 5450 -2859 1050 -320 C ATOM 1750 O SER A 259 25.152 -13.689 4.428 1.00 52.11 O ANISOU 1750 O SER A 259 7953 5938 5909 -2893 1081 -296 O ATOM 1751 CB SER A 259 28.158 -11.985 4.151 1.00 52.79 C ANISOU 1751 CB SER A 259 8156 5945 5956 -2786 939 -328 C ATOM 1752 OG SER A 259 27.272 -10.917 3.885 1.00 51.52 O ANISOU 1752 OG SER A 259 7926 5780 5870 -2783 948 -303 O ATOM 1753 N ASP A 260 26.591 -13.379 6.141 1.00 45.91 N ANISOU 1753 N ASP A 260 7343 5062 5040 -2848 1081 -332 N ATOM 1754 CA ASP A 260 25.619 -13.540 7.222 1.00 44.34 C ANISOU 1754 CA ASP A 260 7161 4848 4838 -2876 1165 -323 C ATOM 1755 C ASP A 260 24.199 -13.132 6.850 1.00 39.92 C ANISOU 1755 C ASP A 260 6484 4321 4364 -2898 1219 -288 C ATOM 1756 O ASP A 260 23.265 -13.895 7.077 1.00 40.72 O ANISOU 1756 O ASP A 260 6551 4454 4467 -2949 1281 -270 O ATOM 1757 CB ASP A 260 26.059 -12.733 8.444 1.00 42.39 C ANISOU 1757 CB ASP A 260 7040 4531 4537 -2870 1196 -348 C ATOM 1758 CG ASP A 260 27.396 -13.140 8.955 1.00 42.62 C ANISOU 1758 CG ASP A 260 7159 4523 4511 -2835 1131 -357 C ATOM 1759 OD1 ASP A 260 28.100 -13.924 8.283 1.00 44.83 O ANISOU 1759 OD1 ASP A 260 7428 4830 4776 -2835 1078 -360 O ATOM 1760 OD2 ASP A 260 27.755 -12.648 10.027 1.00 44.57 O ANISOU 1760 OD2 ASP A 260 7544 4711 4680 -2857 1160 -383 O ATOM 1761 N GLY A 261 24.022 -11.948 6.278 1.00 47.05 N ANISOU 1761 N GLY A 261 7338 5216 5322 -2886 1204 -280 N ATOM 1762 CA GLY A 261 22.710 -11.374 6.094 1.00 53.02 C ANISOU 1762 CA GLY A 261 8014 5991 6140 -2938 1278 -256 C ATOM 1763 C GLY A 261 22.109 -11.470 4.715 1.00 58.26 C ANISOU 1763 C GLY A 261 8519 6712 6906 -2929 1217 -200 C ATOM 1764 O GLY A 261 20.953 -11.067 4.535 1.00 66.54 O ANISOU 1764 O GLY A 261 9480 7782 8021 -2977 1275 -165 O ATOM 1765 N GLY A 262 22.834 -11.983 3.737 1.00 55.82 N ANISOU 1765 N GLY A 262 8199 6430 6578 -2907 1126 -206 N ATOM 1766 CA GLY A 262 22.288 -12.105 2.405 1.00 52.65 C ANISOU 1766 CA GLY A 262 7694 6082 6228 -2935 1082 -172 C ATOM 1767 C GLY A 262 23.364 -11.957 1.351 1.00 49.92 C ANISOU 1767 C GLY A 262 7381 5747 5840 -2918 996 -196 C ATOM 1768 O GLY A 262 24.562 -11.972 1.639 1.00 51.52 O ANISOU 1768 O GLY A 262 7677 5923 5974 -2886 972 -236 O ATOM 1769 N LEU A 263 22.895 -11.809 0.118 1.00 44.14 N ANISOU 1769 N LEU A 263 6564 5056 5152 -2943 951 -163 N ATOM 1770 CA LEU A 263 23.784 -11.793 -1.024 1.00 42.14 C ANISOU 1770 CA LEU A 263 6336 4826 4850 -2942 880 -180 C ATOM 1771 C LEU A 263 24.768 -10.634 -0.931 1.00 58.67 C ANISOU 1771 C LEU A 263 8471 6874 6947 -2890 842 -188 C ATOM 1772 O LEU A 263 24.482 -9.585 -0.346 1.00 59.16 O ANISOU 1772 O LEU A 263 8513 6886 7078 -2863 851 -168 O ATOM 1773 CB LEU A 263 22.975 -11.666 -2.297 1.00 39.72 C ANISOU 1773 CB LEU A 263 5933 4564 4593 -2985 838 -134 C ATOM 1774 CG LEU A 263 22.223 -12.918 -2.699 1.00 43.09 C ANISOU 1774 CG LEU A 263 6329 5042 5000 -3046 853 -128 C ATOM 1775 CD1 LEU A 263 21.236 -12.569 -3.801 1.00 45.10 C ANISOU 1775 CD1 LEU A 263 6476 5333 5329 -3091 811 -68 C ATOM 1776 CD2 LEU A 263 23.232 -13.944 -3.144 1.00 40.43 C ANISOU 1776 CD2 LEU A 263 6084 4729 4549 -3057 837 -182 C ATOM 1777 N LEU A 264 25.956 -10.847 -1.499 1.00 70.26 N ANISOU 1777 N LEU A 264 9997 8355 8344 -2880 801 -217 N ATOM 1778 CA LEU A 264 26.856 -9.773 -1.851 1.00 37.67 C ANISOU 1778 CA LEU A 264 5886 4200 4225 -2847 748 -211 C ATOM 1779 C LEU A 264 26.318 -9.137 -3.121 1.00 51.23 C ANISOU 1779 C LEU A 264 7526 5948 5991 -2876 698 -168 C ATOM 1780 O LEU A 264 25.444 -9.699 -3.784 1.00 55.98 O ANISOU 1780 O LEU A 264 8073 6596 6600 -2922 700 -149 O ATOM 1781 CB LEU A 264 28.258 -10.320 -2.089 1.00 37.22 C ANISOU 1781 CB LEU A 264 5901 4154 4087 -2836 730 -248 C ATOM 1782 CG LEU A 264 28.873 -10.939 -0.864 1.00 36.98 C ANISOU 1782 CG LEU A 264 5946 4088 4018 -2810 767 -281 C ATOM 1783 CD1 LEU A 264 30.309 -11.320 -1.084 1.00 36.63 C ANISOU 1783 CD1 LEU A 264 5952 4040 3925 -2794 744 -304 C ATOM 1784 CD2 LEU A 264 28.728 -9.958 0.247 1.00 36.92 C ANISOU 1784 CD2 LEU A 264 5958 4017 4054 -2775 774 -272 C ATOM 1785 N PRO A 265 26.811 -7.974 -3.494 1.00 46.46 N ANISOU 1785 N PRO A 265 6916 5315 5422 -2856 646 -145 N ATOM 1786 CA PRO A 265 26.504 -7.453 -4.832 1.00 42.73 C ANISOU 1786 CA PRO A 265 6386 4875 4975 -2891 588 -103 C ATOM 1787 C PRO A 265 27.097 -8.276 -5.969 1.00 38.68 C ANISOU 1787 C PRO A 265 5903 4430 4362 -2932 571 -123 C ATOM 1788 O PRO A 265 26.382 -8.660 -6.896 1.00 42.31 O ANISOU 1788 O PRO A 265 6323 4940 4814 -2984 556 -102 O ATOM 1789 CB PRO A 265 27.085 -6.036 -4.790 1.00 41.01 C ANISOU 1789 CB PRO A 265 6172 4597 4811 -2858 538 -80 C ATOM 1790 CG PRO A 265 28.014 -6.018 -3.640 1.00 39.76 C ANISOU 1790 CG PRO A 265 6091 4391 4624 -2809 561 -119 C ATOM 1791 CD PRO A 265 27.414 -6.944 -2.643 1.00 41.39 C ANISOU 1791 CD PRO A 265 6311 4599 4816 -2806 633 -147 C ATOM 1792 N GLU A 266 28.381 -8.561 -5.923 1.00 37.71 N ANISOU 1792 N GLU A 266 5850 4308 4170 -2912 575 -161 N ATOM 1793 CA GLU A 266 29.023 -9.380 -6.937 1.00 48.40 C ANISOU 1793 CA GLU A 266 7236 5717 5435 -2950 574 -187 C ATOM 1794 C GLU A 266 29.787 -10.487 -6.236 1.00 42.76 C ANISOU 1794 C GLU A 266 6582 4995 4670 -2929 626 -241 C ATOM 1795 O GLU A 266 30.111 -10.374 -5.049 1.00 39.56 O ANISOU 1795 O GLU A 266 6203 4540 4289 -2882 644 -253 O ATOM 1796 CB GLU A 266 29.999 -8.560 -7.800 1.00 56.03 C ANISOU 1796 CB GLU A 266 8215 6690 6384 -2956 527 -171 C ATOM 1797 CG GLU A 266 29.463 -7.264 -8.372 1.00 61.04 C ANISOU 1797 CG GLU A 266 8800 7314 7080 -2970 465 -110 C ATOM 1798 CD GLU A 266 30.532 -6.496 -9.095 1.00 66.27 C ANISOU 1798 CD GLU A 266 9483 7977 7719 -2978 421 -94 C ATOM 1799 OE1 GLU A 266 31.654 -7.030 -9.161 1.00 67.88 O ANISOU 1799 OE1 GLU A 266 9733 8193 7865 -2974 447 -133 O ATOM 1800 OE2 GLU A 266 30.261 -5.368 -9.572 1.00 69.53 O ANISOU 1800 OE2 GLU A 266 9864 8373 8182 -2991 363 -41 O ATOM 1801 N PRO A 267 30.111 -11.555 -6.948 1.00 37.62 N ANISOU 1801 N PRO A 267 5957 4386 3950 -2966 647 -274 N ATOM 1802 CA PRO A 267 30.920 -12.618 -6.362 1.00 37.39 C ANISOU 1802 CA PRO A 267 5980 4340 3888 -2947 692 -321 C ATOM 1803 C PRO A 267 32.336 -12.155 -6.075 1.00 36.99 C ANISOU 1803 C PRO A 267 5955 4252 3848 -2905 682 -329 C ATOM 1804 O PRO A 267 32.983 -11.543 -6.920 1.00 61.98 O ANISOU 1804 O PRO A 267 9113 7432 7006 -2916 654 -319 O ATOM 1805 CB PRO A 267 30.900 -13.684 -7.448 1.00 37.82 C ANISOU 1805 CB PRO A 267 6048 4444 3878 -3004 711 -350 C ATOM 1806 CG PRO A 267 29.581 -13.495 -8.064 1.00 38.30 C ANISOU 1806 CG PRO A 267 6065 4545 3943 -3052 686 -316 C ATOM 1807 CD PRO A 267 29.372 -12.028 -8.117 1.00 38.19 C ANISOU 1807 CD PRO A 267 6008 4518 3984 -3033 637 -267 C ATOM 1808 N VAL A 268 32.832 -12.480 -4.893 1.00 36.70 N ANISOU 1808 N VAL A 268 5950 4166 3829 -2863 701 -344 N ATOM 1809 CA VAL A 268 34.210 -12.199 -4.514 1.00 36.43 C ANISOU 1809 CA VAL A 268 5936 4089 3816 -2826 687 -348 C ATOM 1810 C VAL A 268 34.985 -13.498 -4.647 1.00 36.54 C ANISOU 1810 C VAL A 268 5974 4101 3810 -2835 725 -386 C ATOM 1811 O VAL A 268 34.611 -14.507 -4.049 1.00 36.63 O ANISOU 1811 O VAL A 268 6008 4101 3809 -2838 757 -405 O ATOM 1812 CB VAL A 268 34.270 -11.642 -3.084 1.00 36.15 C ANISOU 1812 CB VAL A 268 5924 3993 3820 -2779 673 -332 C ATOM 1813 CG1 VAL A 268 35.689 -11.331 -2.642 1.00 35.98 C ANISOU 1813 CG1 VAL A 268 5921 3921 3830 -2747 645 -328 C ATOM 1814 CG2 VAL A 268 33.426 -10.412 -3.001 1.00 36.15 C ANISOU 1814 CG2 VAL A 268 5898 3986 3851 -2774 644 -299 C ATOM 1815 N LYS A 269 36.026 -13.514 -5.466 1.00 37.42 N ANISOU 1815 N LYS A 269 6076 4219 3925 -2846 725 -398 N ATOM 1816 CA LYS A 269 36.821 -14.728 -5.646 1.00 45.06 C ANISOU 1816 CA LYS A 269 7056 5172 4894 -2854 766 -436 C ATOM 1817 C LYS A 269 37.899 -14.742 -4.587 1.00 41.52 C ANISOU 1817 C LYS A 269 6613 4652 4510 -2807 749 -428 C ATOM 1818 O LYS A 269 38.557 -13.726 -4.366 1.00 50.01 O ANISOU 1818 O LYS A 269 7673 5702 5627 -2783 707 -400 O ATOM 1819 CB LYS A 269 37.433 -14.779 -7.046 1.00 45.82 C ANISOU 1819 CB LYS A 269 7136 5305 4969 -2894 784 -458 C ATOM 1820 CG LYS A 269 38.441 -15.884 -7.384 1.00 49.62 C ANISOU 1820 CG LYS A 269 7620 5761 5472 -2905 832 -502 C ATOM 1821 CD LYS A 269 38.861 -15.622 -8.857 1.00 59.78 C ANISOU 1821 CD LYS A 269 8894 7096 6724 -2956 853 -522 C ATOM 1822 CE LYS A 269 39.772 -16.656 -9.513 1.00 66.54 C ANISOU 1822 CE LYS A 269 9749 7936 7595 -2981 916 -576 C ATOM 1823 NZ LYS A 269 41.136 -16.618 -8.938 1.00 71.80 N ANISOU 1823 NZ LYS A 269 10380 8533 8367 -2940 912 -572 N ATOM 1824 N VAL A 270 38.050 -15.855 -3.891 1.00 36.78 N ANISOU 1824 N VAL A 270 6036 4013 3924 -2798 772 -445 N ATOM 1825 CA VAL A 270 39.018 -15.913 -2.809 1.00 36.71 C ANISOU 1825 CA VAL A 270 6035 3930 3982 -2758 744 -430 C ATOM 1826 C VAL A 270 39.733 -17.241 -2.876 1.00 37.08 C ANISOU 1826 C VAL A 270 6080 3938 4070 -2764 773 -457 C ATOM 1827 O VAL A 270 39.207 -18.218 -3.403 1.00 42.36 O ANISOU 1827 O VAL A 270 6761 4633 4703 -2796 819 -488 O ATOM 1828 CB VAL A 270 38.381 -15.714 -1.419 1.00 36.51 C ANISOU 1828 CB VAL A 270 6052 3875 3944 -2734 723 -406 C ATOM 1829 CG1 VAL A 270 37.382 -14.591 -1.464 1.00 36.26 C ANISOU 1829 CG1 VAL A 270 6020 3883 3876 -2736 710 -388 C ATOM 1830 CG2 VAL A 270 37.736 -16.996 -0.920 1.00 36.74 C ANISOU 1830 CG2 VAL A 270 6116 3898 3945 -2751 759 -422 C ATOM 1831 N SER A 271 40.955 -17.260 -2.372 1.00 37.18 N ANISOU 1831 N SER A 271 6074 3883 4171 -2737 742 -444 N ATOM 1832 CA SER A 271 41.711 -18.490 -2.283 1.00 37.62 C ANISOU 1832 CA SER A 271 6120 3879 4295 -2738 758 -464 C ATOM 1833 C SER A 271 41.476 -19.180 -0.966 1.00 39.16 C ANISOU 1833 C SER A 271 6360 4018 4501 -2722 735 -445 C ATOM 1834 O SER A 271 41.591 -20.408 -0.890 1.00 43.97 O ANISOU 1834 O SER A 271 6979 4589 5141 -2733 756 -462 O ATOM 1835 CB SER A 271 43.195 -18.201 -2.420 1.00 59.39 C ANISOU 1835 CB SER A 271 8821 6580 7166 -2721 727 -456 C ATOM 1836 OG SER A 271 43.696 -17.656 -1.193 1.00 61.14 O ANISOU 1836 OG SER A 271 9049 6738 7443 -2687 653 -412 O ATOM 1837 N GLU A 272 41.159 -18.412 0.071 1.00 37.40 N ANISOU 1837 N GLU A 272 6172 3786 4253 -2701 692 -411 N ATOM 1838 CA GLU A 272 40.781 -18.980 1.348 1.00 37.53 C ANISOU 1838 CA GLU A 272 6248 3759 4255 -2697 675 -393 C ATOM 1839 C GLU A 272 39.784 -18.042 1.994 1.00 37.17 C ANISOU 1839 C GLU A 272 6246 3750 4128 -2694 670 -376 C ATOM 1840 O GLU A 272 39.774 -16.844 1.715 1.00 36.85 O ANISOU 1840 O GLU A 272 6187 3737 4079 -2682 652 -367 O ATOM 1841 CB GLU A 272 41.990 -19.235 2.252 1.00 37.87 C ANISOU 1841 CB GLU A 272 6290 3701 4396 -2673 611 -367 C ATOM 1842 CG GLU A 272 42.803 -18.010 2.582 1.00 51.94 C ANISOU 1842 CG GLU A 272 8053 5455 6225 -2647 548 -339 C ATOM 1843 CD GLU A 272 44.274 -18.331 2.789 1.00 52.27 C ANISOU 1843 CD GLU A 272 8047 5404 6408 -2631 489 -325 C ATOM 1844 OE1 GLU A 272 44.905 -18.850 1.823 1.00 55.32 O ANISOU 1844 OE1 GLU A 272 8366 5783 6871 -2638 516 -349 O ATOM 1845 OE2 GLU A 272 44.798 -18.031 3.895 1.00 47.43 O ANISOU 1845 OE2 GLU A 272 7463 4723 5834 -2615 416 -293 O ATOM 1846 N LEU A 273 38.915 -18.621 2.825 1.00 45.38 N ANISOU 1846 N LEU A 273 7342 4787 5114 -2709 688 -372 N ATOM 1847 CA LEU A 273 37.781 -17.936 3.436 1.00 37.12 C ANISOU 1847 CA LEU A 273 6337 3774 3995 -2714 703 -364 C ATOM 1848 C LEU A 273 37.863 -18.209 4.924 1.00 51.72 C ANISOU 1848 C LEU A 273 8261 5560 5829 -2713 678 -341 C ATOM 1849 O LEU A 273 37.388 -19.252 5.395 1.00 54.57 O ANISOU 1849 O LEU A 273 8660 5910 6164 -2739 702 -342 O ATOM 1850 CB LEU A 273 36.447 -18.421 2.883 1.00 37.19 C ANISOU 1850 CB LEU A 273 6338 3848 3946 -2750 762 -386 C ATOM 1851 CG LEU A 273 35.217 -17.766 3.495 1.00 37.12 C ANISOU 1851 CG LEU A 273 6354 3866 3884 -2759 784 -380 C ATOM 1852 CD1 LEU A 273 35.387 -16.264 3.620 1.00 36.75 C ANISOU 1852 CD1 LEU A 273 6300 3816 3848 -2729 754 -366 C ATOM 1853 CD2 LEU A 273 34.030 -18.105 2.673 1.00 37.24 C ANISOU 1853 CD2 LEU A 273 6333 3946 3872 -2795 828 -397 C ATOM 1854 N PRO A 274 38.450 -17.303 5.696 1.00 37.34 N ANISOU 1854 N PRO A 274 6470 3695 4020 -2688 626 -319 N ATOM 1855 CA PRO A 274 38.326 -17.414 7.137 1.00 46.31 C ANISOU 1855 CA PRO A 274 7698 4781 5117 -2695 607 -300 C ATOM 1856 C PRO A 274 36.901 -17.093 7.535 1.00 41.59 C ANISOU 1856 C PRO A 274 7140 4227 4436 -2717 667 -311 C ATOM 1857 O PRO A 274 36.297 -16.135 7.022 1.00 38.52 O ANISOU 1857 O PRO A 274 6717 3883 4037 -2709 690 -323 O ATOM 1858 CB PRO A 274 39.295 -16.358 7.656 1.00 37.63 C ANISOU 1858 CB PRO A 274 6617 3629 4053 -2666 533 -278 C ATOM 1859 CG PRO A 274 39.569 -15.484 6.517 1.00 37.21 C ANISOU 1859 CG PRO A 274 6482 3613 4042 -2647 528 -286 C ATOM 1860 CD PRO A 274 38.820 -15.940 5.330 1.00 36.98 C ANISOU 1860 CD PRO A 274 6395 3660 3998 -2663 594 -313 C ATOM 1861 N VAL A 275 36.374 -17.927 8.440 1.00 41.34 N ANISOU 1861 N VAL A 275 7176 4176 4354 -2748 691 -306 N ATOM 1862 CA VAL A 275 35.045 -17.781 9.013 1.00 41.46 C ANISOU 1862 CA VAL A 275 7234 4220 4300 -2778 755 -316 C ATOM 1863 C VAL A 275 35.139 -17.902 10.535 1.00 43.34 C ANISOU 1863 C VAL A 275 7589 4396 4482 -2796 741 -297 C ATOM 1864 O VAL A 275 35.798 -18.800 11.071 1.00 39.24 O ANISOU 1864 O VAL A 275 7115 3827 3967 -2808 700 -275 O ATOM 1865 CB VAL A 275 34.055 -18.807 8.431 1.00 38.49 C ANISOU 1865 CB VAL A 275 6817 3895 3912 -2816 814 -330 C ATOM 1866 CG1 VAL A 275 32.679 -18.580 8.995 1.00 38.78 C ANISOU 1866 CG1 VAL A 275 6878 3957 3898 -2848 881 -338 C ATOM 1867 CG2 VAL A 275 34.016 -18.699 6.937 1.00 38.08 C ANISOU 1867 CG2 VAL A 275 6667 3898 3903 -2804 821 -349 C ATOM 1868 N LEU A 276 34.465 -16.990 11.224 1.00 42.65 N ANISOU 1868 N LEU A 276 7553 4307 4344 -2800 774 -305 N ATOM 1869 CA LEU A 276 34.374 -16.917 12.669 1.00 42.10 C ANISOU 1869 CA LEU A 276 7611 4183 4201 -2824 776 -294 C ATOM 1870 C LEU A 276 33.079 -17.545 13.193 1.00 49.38 C ANISOU 1870 C LEU A 276 8567 5130 5064 -2877 866 -303 C ATOM 1871 O LEU A 276 32.095 -17.729 12.469 1.00 53.49 O ANISOU 1871 O LEU A 276 9006 5711 5608 -2890 928 -320 O ATOM 1872 CB LEU A 276 34.436 -15.462 13.110 1.00 39.33 C ANISOU 1872 CB LEU A 276 7304 3804 3834 -2798 766 -302 C ATOM 1873 CG LEU A 276 35.627 -14.663 12.612 1.00 38.90 C ANISOU 1873 CG LEU A 276 7212 3725 3843 -2751 677 -291 C ATOM 1874 CD1 LEU A 276 35.492 -13.234 13.080 1.00 38.91 C ANISOU 1874 CD1 LEU A 276 7264 3693 3826 -2732 672 -301 C ATOM 1875 CD2 LEU A 276 36.934 -15.282 13.080 1.00 50.18 C ANISOU 1875 CD2 LEU A 276 8682 5093 5290 -2748 584 -259 C ATOM 1876 N MET A 277 33.085 -17.828 14.490 1.00 48.65 N ANISOU 1876 N MET A 277 8600 4986 4897 -2911 868 -289 N ATOM 1877 CA MET A 277 31.990 -18.492 15.169 1.00 41.43 C ANISOU 1877 CA MET A 277 7734 4084 3924 -2970 950 -289 C ATOM 1878 C MET A 277 30.641 -17.811 14.946 1.00 41.71 C ANISOU 1878 C MET A 277 7746 4166 3935 -3005 1064 -328 C ATOM 1879 O MET A 277 30.403 -16.696 15.427 1.00 42.15 O ANISOU 1879 O MET A 277 7895 4197 3921 -3030 1115 -360 O ATOM 1880 CB MET A 277 32.311 -18.564 16.662 1.00 53.35 C ANISOU 1880 CB MET A 277 9454 5522 5296 -3038 946 -283 C ATOM 1881 CG MET A 277 33.595 -19.328 16.994 1.00 48.88 C ANISOU 1881 CG MET A 277 8910 4898 4766 -3012 824 -234 C ATOM 1882 SD MET A 277 35.042 -18.301 16.792 1.00 41.88 S ANISOU 1882 SD MET A 277 8005 3966 3942 -2936 707 -223 S ATOM 1883 CE MET A 277 35.224 -17.610 18.417 1.00 43.19 C ANISOU 1883 CE MET A 277 8430 4052 3927 -3007 697 -225 C ATOM 1884 N GLY A 278 29.737 -18.493 14.247 1.00 42.55 N ANISOU 1884 N GLY A 278 7734 4331 4101 -3014 1108 -322 N ATOM 1885 CA GLY A 278 28.405 -17.996 14.013 1.00 48.33 C ANISOU 1885 CA GLY A 278 8422 5108 4834 -3052 1213 -346 C ATOM 1886 C GLY A 278 28.237 -17.314 12.683 1.00 53.12 C ANISOU 1886 C GLY A 278 8869 5763 5552 -2986 1187 -348 C ATOM 1887 O GLY A 278 27.105 -16.995 12.310 1.00 55.56 O ANISOU 1887 O GLY A 278 9108 6112 5889 -3013 1261 -355 O ATOM 1888 N GLU A 279 29.328 -17.085 11.961 1.00 48.39 N ANISOU 1888 N GLU A 279 8238 5160 4990 -2931 1099 -348 N ATOM 1889 CA GLU A 279 29.252 -16.469 10.654 1.00 39.58 C ANISOU 1889 CA GLU A 279 7006 4088 3943 -2896 1079 -357 C ATOM 1890 C GLU A 279 28.859 -17.502 9.616 1.00 39.63 C ANISOU 1890 C GLU A 279 6926 4150 3981 -2921 1080 -354 C ATOM 1891 O GLU A 279 29.104 -18.698 9.772 1.00 39.96 O ANISOU 1891 O GLU A 279 6999 4184 3999 -2950 1068 -346 O ATOM 1892 CB GLU A 279 30.591 -15.864 10.264 1.00 42.03 C ANISOU 1892 CB GLU A 279 7326 4373 4271 -2845 994 -357 C ATOM 1893 CG GLU A 279 30.796 -14.451 10.743 1.00 45.81 C ANISOU 1893 CG GLU A 279 7845 4810 4752 -2812 984 -362 C ATOM 1894 CD GLU A 279 32.176 -13.920 10.415 1.00 46.16 C ANISOU 1894 CD GLU A 279 7894 4825 4819 -2769 891 -352 C ATOM 1895 OE1 GLU A 279 33.093 -14.752 10.317 1.00 48.54 O ANISOU 1895 OE1 GLU A 279 8206 5118 5121 -2768 842 -340 O ATOM 1896 OE2 GLU A 279 32.353 -12.682 10.303 1.00 46.28 O ANISOU 1896 OE2 GLU A 279 7903 4819 4863 -2738 867 -354 O ATOM 1897 N ARG A 280 28.251 -17.029 8.542 1.00 41.56 N ANISOU 1897 N ARG A 280 7067 4444 4281 -2914 1088 -357 N ATOM 1898 CA ARG A 280 27.921 -17.876 7.409 1.00 39.44 C ANISOU 1898 CA ARG A 280 6720 4227 4038 -2937 1078 -356 C ATOM 1899 C ARG A 280 28.382 -17.228 6.107 1.00 50.10 C ANISOU 1899 C ARG A 280 8002 5607 5427 -2903 1030 -363 C ATOM 1900 O ARG A 280 28.238 -16.014 5.912 1.00 50.28 O ANISOU 1900 O ARG A 280 7992 5630 5482 -2875 1025 -360 O ATOM 1901 CB ARG A 280 26.439 -18.137 7.337 1.00 40.12 C ANISOU 1901 CB ARG A 280 6740 4353 4152 -2985 1140 -340 C ATOM 1902 CG ARG A 280 25.954 -18.983 8.394 1.00 40.91 C ANISOU 1902 CG ARG A 280 6893 4435 4216 -3031 1189 -326 C ATOM 1903 CD ARG A 280 25.630 -18.182 9.602 1.00 41.19 C ANISOU 1903 CD ARG A 280 6982 4436 4233 -3026 1245 -322 C ATOM 1904 NE ARG A 280 24.643 -17.161 9.310 1.00 41.31 N ANISOU 1904 NE ARG A 280 6905 4477 4313 -3018 1292 -309 N ATOM 1905 CZ ARG A 280 24.523 -16.039 10.006 1.00 41.52 C ANISOU 1905 CZ ARG A 280 6982 4470 4322 -3012 1343 -323 C ATOM 1906 NH1 ARG A 280 25.334 -15.789 11.019 1.00 43.43 N ANISOU 1906 NH1 ARG A 280 7377 4652 4472 -3018 1347 -354 N ATOM 1907 NH2 ARG A 280 23.598 -15.162 9.693 1.00 42.01 N ANISOU 1907 NH2 ARG A 280 6977 4553 4431 -3032 1404 -319 N ATOM 1908 N PHE A 281 28.921 -18.043 5.209 1.00 38.67 N ANISOU 1908 N PHE A 281 6536 4179 3978 -2909 998 -371 N ATOM 1909 CA PHE A 281 29.208 -17.591 3.860 1.00 38.25 C ANISOU 1909 CA PHE A 281 6418 4163 3953 -2892 964 -377 C ATOM 1910 C PHE A 281 28.736 -18.648 2.904 1.00 38.62 C ANISOU 1910 C PHE A 281 6424 4252 3997 -2936 970 -383 C ATOM 1911 O PHE A 281 29.039 -19.825 3.090 1.00 42.83 O ANISOU 1911 O PHE A 281 6996 4768 4510 -2958 974 -389 O ATOM 1912 CB PHE A 281 30.688 -17.323 3.645 1.00 37.73 C ANISOU 1912 CB PHE A 281 6380 4069 3888 -2850 915 -384 C ATOM 1913 CG PHE A 281 31.207 -16.137 4.401 1.00 48.79 C ANISOU 1913 CG PHE A 281 7814 5428 5296 -2809 894 -375 C ATOM 1914 CD1 PHE A 281 31.166 -14.859 3.851 1.00 37.07 C ANISOU 1914 CD1 PHE A 281 6286 3956 3844 -2785 872 -368 C ATOM 1915 CD2 PHE A 281 31.704 -16.291 5.686 1.00 51.16 C ANISOU 1915 CD2 PHE A 281 8197 5671 5570 -2800 890 -369 C ATOM 1916 CE1 PHE A 281 31.631 -13.785 4.558 1.00 36.88 C ANISOU 1916 CE1 PHE A 281 6298 3883 3829 -2751 848 -359 C ATOM 1917 CE2 PHE A 281 32.165 -15.189 6.412 1.00 48.84 C ANISOU 1917 CE2 PHE A 281 7947 5333 5278 -2768 865 -361 C ATOM 1918 CZ PHE A 281 32.126 -13.951 5.846 1.00 46.74 C ANISOU 1918 CZ PHE A 281 7635 5076 5048 -2743 845 -358 C ATOM 1919 N GLU A 282 27.979 -18.236 1.902 1.00 44.24 N ANISOU 1919 N GLU A 282 7062 5013 4734 -2954 966 -375 N ATOM 1920 CA GLU A 282 27.604 -19.119 0.799 1.00 48.78 C ANISOU 1920 CA GLU A 282 7603 5630 5302 -3000 961 -381 C ATOM 1921 C GLU A 282 28.615 -18.899 -0.307 1.00 46.92 C ANISOU 1921 C GLU A 282 7365 5407 5055 -2980 926 -400 C ATOM 1922 O GLU A 282 28.758 -17.760 -0.783 1.00 52.50 O ANISOU 1922 O GLU A 282 8039 6128 5779 -2956 901 -391 O ATOM 1923 CB GLU A 282 26.192 -18.821 0.286 1.00 39.55 C ANISOU 1923 CB GLU A 282 6352 4506 4169 -3040 969 -353 C ATOM 1924 CG GLU A 282 25.105 -19.017 1.335 1.00 42.08 C ANISOU 1924 CG GLU A 282 6656 4818 4514 -3066 1016 -328 C ATOM 1925 CD GLU A 282 23.717 -18.637 0.862 1.00 41.66 C ANISOU 1925 CD GLU A 282 6499 4806 4523 -3103 1026 -286 C ATOM 1926 OE1 GLU A 282 23.300 -19.110 -0.203 1.00 41.84 O ANISOU 1926 OE1 GLU A 282 6479 4868 4550 -3147 1000 -278 O ATOM 1927 OE2 GLU A 282 23.047 -17.831 1.551 1.00 42.79 O ANISOU 1927 OE2 GLU A 282 6601 4938 4717 -3090 1060 -259 O ATOM 1928 N VAL A 283 29.331 -19.970 -0.673 1.00 38.75 N ANISOU 1928 N VAL A 283 6365 4361 3998 -2993 927 -423 N ATOM 1929 CA VAL A 283 30.344 -19.941 -1.720 1.00 38.50 C ANISOU 1929 CA VAL A 283 6332 4338 3958 -2982 910 -445 C ATOM 1930 C VAL A 283 29.891 -20.830 -2.869 1.00 48.20 C ANISOU 1930 C VAL A 283 7548 5604 5162 -3041 918 -461 C ATOM 1931 O VAL A 283 29.075 -21.734 -2.692 1.00 53.73 O ANISOU 1931 O VAL A 283 8252 6307 5855 -3086 933 -457 O ATOM 1932 CB VAL A 283 31.717 -20.402 -1.201 1.00 38.30 C ANISOU 1932 CB VAL A 283 6352 4254 3945 -2946 908 -458 C ATOM 1933 CG1 VAL A 283 32.051 -19.709 0.065 1.00 37.95 C ANISOU 1933 CG1 VAL A 283 6334 4168 3919 -2902 895 -438 C ATOM 1934 CG2 VAL A 283 31.707 -21.865 -0.968 1.00 38.83 C ANISOU 1934 CG2 VAL A 283 6453 4291 4009 -2978 928 -469 C ATOM 1935 N LEU A 284 30.412 -20.575 -4.061 1.00 43.03 N ANISOU 1935 N LEU A 284 6882 4978 4491 -3049 908 -478 N ATOM 1936 CA LEU A 284 30.310 -21.528 -5.157 1.00 39.72 C ANISOU 1936 CA LEU A 284 6472 4582 4038 -3106 921 -504 C ATOM 1937 C LEU A 284 31.688 -22.116 -5.440 1.00 39.46 C ANISOU 1937 C LEU A 284 6472 4510 4011 -3088 942 -541 C ATOM 1938 O LEU A 284 32.706 -21.478 -5.189 1.00 50.45 O ANISOU 1938 O LEU A 284 7860 5877 5430 -3038 936 -541 O ATOM 1939 CB LEU A 284 29.742 -20.864 -6.404 1.00 39.68 C ANISOU 1939 CB LEU A 284 6432 4641 4003 -3145 897 -495 C ATOM 1940 CG LEU A 284 28.230 -20.947 -6.539 1.00 40.22 C ANISOU 1940 CG LEU A 284 6464 4747 4073 -3198 880 -464 C ATOM 1941 CD1 LEU A 284 27.538 -20.377 -5.322 1.00 40.02 C ANISOU 1941 CD1 LEU A 284 6405 4704 4098 -3165 878 -428 C ATOM 1942 CD2 LEU A 284 27.827 -20.201 -7.775 1.00 40.41 C ANISOU 1942 CD2 LEU A 284 6454 4828 4074 -3235 845 -447 C ATOM 1943 N VAL A 285 31.735 -23.356 -5.907 1.00 40.05 N ANISOU 1943 N VAL A 285 6575 4571 4073 -3132 968 -570 N ATOM 1944 CA VAL A 285 33.003 -23.959 -6.288 1.00 40.16 C ANISOU 1944 CA VAL A 285 6609 4541 4110 -3120 996 -608 C ATOM 1945 C VAL A 285 32.740 -24.769 -7.541 1.00 43.74 C ANISOU 1945 C VAL A 285 7081 5019 4518 -3191 1022 -644 C ATOM 1946 O VAL A 285 31.609 -25.164 -7.825 1.00 47.99 O ANISOU 1946 O VAL A 285 7625 5590 5019 -3247 1012 -634 O ATOM 1947 CB VAL A 285 33.616 -24.816 -5.154 1.00 40.24 C ANISOU 1947 CB VAL A 285 6642 4467 4179 -3088 1002 -604 C ATOM 1948 CG1 VAL A 285 32.871 -26.076 -4.980 1.00 40.94 C ANISOU 1948 CG1 VAL A 285 6761 4534 4260 -3138 1012 -606 C ATOM 1949 CG2 VAL A 285 35.073 -25.131 -5.400 1.00 40.27 C ANISOU 1949 CG2 VAL A 285 6645 4416 4242 -3060 1021 -634 C ATOM 1950 N GLU A 286 33.791 -24.984 -8.319 1.00 43.19 N ANISOU 1950 N GLU A 286 7020 4934 4457 -3193 1056 -686 N ATOM 1951 CA GLU A 286 33.679 -25.637 -9.616 1.00 43.19 C ANISOU 1951 CA GLU A 286 7048 4958 4406 -3265 1089 -730 C ATOM 1952 C GLU A 286 34.048 -27.109 -9.520 1.00 47.55 C ANISOU 1952 C GLU A 286 7634 5435 4997 -3284 1126 -765 C ATOM 1953 O GLU A 286 35.074 -27.466 -8.936 1.00 47.91 O ANISOU 1953 O GLU A 286 7673 5407 5123 -3236 1141 -776 O ATOM 1954 CB GLU A 286 34.573 -24.950 -10.636 1.00 47.13 C ANISOU 1954 CB GLU A 286 7538 5485 4884 -3267 1114 -761 C ATOM 1955 CG GLU A 286 33.945 -24.748 -11.979 1.00 58.47 C ANISOU 1955 CG GLU A 286 8995 6996 6225 -3346 1116 -775 C ATOM 1956 CD GLU A 286 34.899 -24.063 -12.940 1.00 71.37 C ANISOU 1956 CD GLU A 286 10625 8656 7835 -3355 1145 -805 C ATOM 1957 OE1 GLU A 286 35.657 -23.168 -12.482 1.00 71.70 O ANISOU 1957 OE1 GLU A 286 10630 8688 7927 -3293 1131 -786 O ATOM 1958 OE2 GLU A 286 34.917 -24.439 -14.141 1.00 80.15 O ANISOU 1958 OE2 GLU A 286 11775 9798 8880 -3429 1182 -848 O ATOM 1959 N VAL A 287 33.213 -27.954 -10.107 1.00 49.78 N ANISOU 1959 N VAL A 287 7950 5730 5233 -3359 1132 -778 N ATOM 1960 CA VAL A 287 33.437 -29.389 -10.190 1.00 53.95 C ANISOU 1960 CA VAL A 287 8519 6186 5796 -3392 1163 -814 C ATOM 1961 C VAL A 287 33.491 -29.750 -11.671 1.00 57.95 C ANISOU 1961 C VAL A 287 9061 6719 6238 -3468 1205 -869 C ATOM 1962 O VAL A 287 32.533 -29.491 -12.396 1.00 57.33 O ANISOU 1962 O VAL A 287 8996 6713 6075 -3532 1184 -858 O ATOM 1963 CB VAL A 287 32.317 -30.154 -9.470 1.00 50.48 C ANISOU 1963 CB VAL A 287 8094 5727 5358 -3425 1128 -775 C ATOM 1964 CG1 VAL A 287 32.753 -31.526 -9.193 1.00 49.10 C ANISOU 1964 CG1 VAL A 287 7954 5454 5248 -3436 1146 -799 C ATOM 1965 CG2 VAL A 287 31.918 -29.450 -8.166 1.00 43.73 C ANISOU 1965 CG2 VAL A 287 7206 4883 4528 -3368 1086 -716 C ATOM 1966 N ASN A 288 34.610 -30.313 -12.139 1.00 65.97 N ANISOU 1966 N ASN A 288 10092 7677 7298 -3465 1264 -929 N ATOM 1967 CA ASN A 288 34.719 -30.536 -13.584 1.00 74.16 C ANISOU 1967 CA ASN A 288 11170 8745 8262 -3542 1316 -988 C ATOM 1968 C ASN A 288 35.099 -31.950 -13.973 1.00 82.87 C ANISOU 1968 C ASN A 288 12320 9761 9406 -3584 1367 -1050 C ATOM 1969 O ASN A 288 34.304 -32.673 -14.576 1.00 83.39 O ANISOU 1969 O ASN A 288 12438 9832 9413 -3668 1364 -1063 O ATOM 1970 CB ASN A 288 35.753 -29.620 -14.210 1.00 73.30 C ANISOU 1970 CB ASN A 288 11037 8669 8146 -3518 1359 -1020 C ATOM 1971 CG ASN A 288 35.775 -28.294 -13.580 1.00 72.54 C ANISOU 1971 CG ASN A 288 10887 8620 8056 -3453 1309 -964 C ATOM 1972 OD1 ASN A 288 34.868 -27.487 -13.786 1.00 72.39 O ANISOU 1972 OD1 ASN A 288 10863 8679 7960 -3475 1261 -922 O ATOM 1973 ND2 ASN A 288 36.815 -28.038 -12.794 1.00 72.81 N ANISOU 1973 ND2 ASN A 288 10876 8598 8190 -3373 1314 -958 N ATOM 1974 N ASP A 289 36.342 -32.325 -13.707 1.00 93.17 N ANISOU 1974 N ASP A 289 13603 10978 10818 -3533 1410 -1089 N ATOM 1975 CA ASP A 289 36.736 -33.698 -13.937 1.00103.18 C ANISOU 1975 CA ASP A 289 14910 12140 12152 -3563 1450 -1147 C ATOM 1976 C ASP A 289 36.130 -34.584 -12.864 1.00 95.57 C ANISOU 1976 C ASP A 289 13957 11104 11249 -3552 1388 -1100 C ATOM 1977 O ASP A 289 35.491 -34.120 -11.920 1.00 94.24 O ANISOU 1977 O ASP A 289 13764 10970 11072 -3519 1327 -1028 O ATOM 1978 CB ASP A 289 38.261 -33.829 -13.973 1.00112.83 C ANISOU 1978 CB ASP A 289 16096 13282 13493 -3510 1509 -1202 C ATOM 1979 CG ASP A 289 38.748 -34.963 -14.925 1.00123.78 C ANISOU 1979 CG ASP A 289 17532 14589 14909 -3568 1586 -1298 C ATOM 1980 OD1 ASP A 289 37.916 -35.745 -15.477 1.00127.05 O ANISOU 1980 OD1 ASP A 289 18017 15000 15256 -3649 1586 -1319 O ATOM 1981 OD2 ASP A 289 39.979 -35.052 -15.143 1.00126.10 O ANISOU 1981 OD2 ASP A 289 17794 14821 15298 -3536 1646 -1357 O ATOM 1982 N ASN A 290 36.337 -35.863 -13.015 1.00 96.61 N ANISOU 1982 N ASN A 290 14130 11133 11446 -3583 1406 -1145 N ATOM 1983 CA ASN A 290 36.120 -36.717 -11.877 1.00 99.12 C ANISOU 1983 CA ASN A 290 14451 11355 11855 -3559 1347 -1103 C ATOM 1984 C ASN A 290 37.103 -36.465 -10.776 1.00 93.78 C ANISOU 1984 C ASN A 290 13718 10613 11302 -3461 1323 -1074 C ATOM 1985 O ASN A 290 37.050 -37.273 -9.838 1.00 97.58 O ANISOU 1985 O ASN A 290 14208 10999 11869 -3444 1272 -1042 O ATOM 1986 CB ASN A 290 36.200 -38.178 -12.310 1.00109.08 C ANISOU 1986 CB ASN A 290 15772 12500 13173 -3613 1361 -1161 C ATOM 1987 CG ASN A 290 35.075 -38.560 -13.225 1.00116.84 C ANISOU 1987 CG ASN A 290 16820 13536 14038 -3720 1361 -1175 C ATOM 1988 OD1 ASN A 290 33.925 -38.673 -12.795 1.00117.90 O ANISOU 1988 OD1 ASN A 290 16967 13706 14124 -3757 1301 -1112 O ATOM 1989 ND2 ASN A 290 35.387 -38.726 -14.510 1.00119.62 N ANISOU 1989 ND2 ASN A 290 17213 13895 14341 -3776 1429 -1256 N ATOM 1990 N LYS A 291 37.968 -35.438 -10.864 1.00 82.60 N ANISOU 1990 N LYS A 291 12247 9237 9900 -3405 1350 -1082 N ATOM 1991 CA LYS A 291 38.929 -35.119 -9.823 1.00 72.51 C ANISOU 1991 CA LYS A 291 10911 7896 8742 -3317 1317 -1049 C ATOM 1992 C LYS A 291 38.161 -34.840 -8.535 1.00 63.13 C ANISOU 1992 C LYS A 291 9721 6728 7536 -3290 1240 -959 C ATOM 1993 O LYS A 291 37.455 -33.827 -8.446 1.00 62.92 O ANISOU 1993 O LYS A 291 9684 6812 7409 -3289 1227 -920 O ATOM 1994 CB LYS A 291 39.789 -33.917 -10.238 1.00 75.87 C ANISOU 1994 CB LYS A 291 11281 8382 9162 -3278 1354 -1065 C ATOM 1995 CG LYS A 291 41.016 -33.643 -9.315 1.00 84.53 C ANISOU 1995 CG LYS A 291 12313 9397 10408 -3193 1318 -1040 C ATOM 1996 CD LYS A 291 42.064 -32.659 -9.932 1.00 90.39 C ANISOU 1996 CD LYS A 291 12997 10177 11171 -3168 1366 -1071 C ATOM 1997 CE LYS A 291 42.602 -33.113 -11.331 1.00 92.79 C ANISOU 1997 CE LYS A 291 13314 10470 11473 -3219 1466 -1171 C ATOM 1998 NZ LYS A 291 43.781 -32.324 -11.858 1.00 86.99 N ANISOU 1998 NZ LYS A 291 12516 9749 10788 -3198 1518 -1205 N ATOM 1999 N PRO A 292 38.222 -35.722 -7.541 1.00 56.14 N ANISOU 1999 N PRO A 292 8848 5737 6744 -3274 1188 -927 N ATOM 2000 CA PRO A 292 37.710 -35.367 -6.223 1.00 55.22 C ANISOU 2000 CA PRO A 292 8728 5636 6619 -3244 1124 -846 C ATOM 2001 C PRO A 292 38.652 -34.374 -5.576 1.00 57.81 C ANISOU 2001 C PRO A 292 9000 5963 7002 -3166 1102 -818 C ATOM 2002 O PRO A 292 39.781 -34.141 -6.017 1.00 64.75 O ANISOU 2002 O PRO A 292 9838 6807 7956 -3132 1126 -856 O ATOM 2003 CB PRO A 292 37.693 -36.689 -5.451 1.00 54.23 C ANISOU 2003 CB PRO A 292 8637 5380 6588 -3256 1076 -825 C ATOM 2004 CG PRO A 292 38.069 -37.721 -6.434 1.00 59.59 C ANISOU 2004 CG PRO A 292 9340 5980 7323 -3294 1112 -899 C ATOM 2005 CD PRO A 292 38.888 -37.022 -7.489 1.00 60.27 C ANISOU 2005 CD PRO A 292 9389 6111 7400 -3276 1179 -964 C ATOM 2006 N PHE A 293 38.170 -33.784 -4.499 1.00 58.24 N ANISOU 2006 N PHE A 293 9055 6052 7021 -3141 1056 -752 N ATOM 2007 CA PHE A 293 38.945 -32.763 -3.829 1.00 56.99 C ANISOU 2007 CA PHE A 293 8854 5898 6903 -3074 1026 -720 C ATOM 2008 C PHE A 293 38.233 -32.458 -2.535 1.00 61.67 C ANISOU 2008 C PHE A 293 9471 6509 7451 -3063 976 -651 C ATOM 2009 O PHE A 293 37.006 -32.548 -2.460 1.00 65.01 O ANISOU 2009 O PHE A 293 9928 6993 7779 -3107 984 -634 O ATOM 2010 CB PHE A 293 39.073 -31.506 -4.684 1.00 52.13 C ANISOU 2010 CB PHE A 293 8201 5388 6216 -3062 1066 -744 C ATOM 2011 CG PHE A 293 37.799 -30.752 -4.826 1.00 52.29 C ANISOU 2011 CG PHE A 293 8240 5529 6097 -3090 1072 -723 C ATOM 2012 CD1 PHE A 293 37.523 -29.672 -4.001 1.00 55.79 C ANISOU 2012 CD1 PHE A 293 8672 6020 6504 -3053 1036 -674 C ATOM 2013 CD2 PHE A 293 36.854 -31.144 -5.749 1.00 53.77 C ANISOU 2013 CD2 PHE A 293 8457 5772 6200 -3157 1105 -752 C ATOM 2014 CE1 PHE A 293 36.339 -28.961 -4.136 1.00 59.84 C ANISOU 2014 CE1 PHE A 293 9194 6634 6909 -3077 1038 -658 C ATOM 2015 CE2 PHE A 293 35.662 -30.451 -5.879 1.00 57.48 C ANISOU 2015 CE2 PHE A 293 8934 6344 6562 -3184 1098 -729 C ATOM 2016 CZ PHE A 293 35.403 -29.358 -5.075 1.00 60.28 C ANISOU 2016 CZ PHE A 293 9268 6742 6892 -3142 1065 -683 C ATOM 2017 N ASP A 294 39.004 -32.122 -1.517 1.00 60.36 N ANISOU 2017 N ASP A 294 9289 6285 7359 -3011 925 -612 N ATOM 2018 CA ASP A 294 38.396 -31.839 -0.237 1.00 55.19 C ANISOU 2018 CA ASP A 294 8669 5642 6658 -3006 884 -550 C ATOM 2019 C ASP A 294 38.216 -30.348 -0.032 1.00 55.15 C ANISOU 2019 C ASP A 294 8646 5731 6577 -2974 884 -533 C ATOM 2020 O ASP A 294 38.913 -29.526 -0.628 1.00 54.25 O ANISOU 2020 O ASP A 294 8485 5644 6482 -2943 895 -555 O ATOM 2021 CB ASP A 294 39.214 -32.446 0.887 1.00 55.00 C ANISOU 2021 CB ASP A 294 8658 5491 6749 -2980 816 -512 C ATOM 2022 CG ASP A 294 39.472 -33.915 0.671 1.00 61.17 C ANISOU 2022 CG ASP A 294 9454 6161 7629 -3007 806 -530 C ATOM 2023 OD1 ASP A 294 39.265 -34.438 -0.452 1.00 65.16 O ANISOU 2023 OD1 ASP A 294 9953 6678 8125 -3040 855 -583 O ATOM 2024 OD2 ASP A 294 39.826 -34.580 1.657 1.00 63.20 O ANISOU 2024 OD2 ASP A 294 9735 6312 7968 -3001 744 -490 O ATOM 2025 N LEU A 295 37.200 -30.019 0.752 1.00 52.30 N ANISOU 2025 N LEU A 295 8322 5419 6129 -2991 877 -497 N ATOM 2026 CA LEU A 295 37.141 -28.751 1.446 1.00 50.82 C ANISOU 2026 CA LEU A 295 8134 5279 5897 -2956 858 -468 C ATOM 2027 C LEU A 295 38.008 -28.915 2.677 1.00 54.39 C ANISOU 2027 C LEU A 295 8609 5634 6423 -2924 797 -428 C ATOM 2028 O LEU A 295 37.906 -29.921 3.373 1.00 56.41 O ANISOU 2028 O LEU A 295 8907 5820 6706 -2948 773 -403 O ATOM 2029 CB LEU A 295 35.699 -28.408 1.825 1.00 47.48 C ANISOU 2029 CB LEU A 295 7740 4934 5365 -2990 878 -451 C ATOM 2030 CG LEU A 295 35.404 -27.048 2.460 1.00 46.24 C ANISOU 2030 CG LEU A 295 7586 4829 5154 -2961 869 -431 C ATOM 2031 CD1 LEU A 295 35.846 -25.968 1.520 1.00 40.14 C ANISOU 2031 CD1 LEU A 295 6760 4109 4384 -2928 877 -456 C ATOM 2032 CD2 LEU A 295 33.918 -26.876 2.769 1.00 41.30 C ANISOU 2032 CD2 LEU A 295 6978 4268 4445 -3002 896 -420 C ATOM 2033 N VAL A 296 38.908 -27.976 2.914 1.00 55.12 N ANISOU 2033 N VAL A 296 8673 5715 6556 -2876 764 -418 N ATOM 2034 CA VAL A 296 39.794 -28.035 4.062 1.00 52.26 C ANISOU 2034 CA VAL A 296 8331 5258 6269 -2848 694 -377 C ATOM 2035 C VAL A 296 39.684 -26.732 4.841 1.00 49.68 C ANISOU 2035 C VAL A 296 8027 4972 5876 -2825 671 -350 C ATOM 2036 O VAL A 296 39.168 -25.724 4.352 1.00 42.48 O ANISOU 2036 O VAL A 296 7097 4150 4893 -2819 706 -367 O ATOM 2037 CB VAL A 296 41.250 -28.305 3.636 1.00 41.92 C ANISOU 2037 CB VAL A 296 6956 3859 5113 -2815 658 -391 C ATOM 2038 CG1 VAL A 296 41.305 -29.589 2.884 1.00 42.63 C ANISOU 2038 CG1 VAL A 296 7031 3900 5267 -2840 685 -424 C ATOM 2039 CG2 VAL A 296 41.718 -27.203 2.740 1.00 41.97 C ANISOU 2039 CG2 VAL A 296 6899 3926 5123 -2788 680 -418 C ATOM 2040 N THR A 297 40.128 -26.785 6.094 1.00 44.63 N ANISOU 2040 N THR A 297 7436 4260 5261 -2816 609 -308 N ATOM 2041 CA THR A 297 40.248 -25.615 6.950 1.00 45.87 C ANISOU 2041 CA THR A 297 7627 4431 5371 -2795 574 -282 C ATOM 2042 C THR A 297 41.717 -25.499 7.322 1.00 46.47 C ANISOU 2042 C THR A 297 7673 4408 5574 -2759 491 -262 C ATOM 2043 O THR A 297 42.329 -26.462 7.798 1.00 51.09 O ANISOU 2043 O THR A 297 8269 4894 6251 -2763 440 -241 O ATOM 2044 CB THR A 297 39.332 -25.712 8.178 1.00 41.18 C ANISOU 2044 CB THR A 297 7133 3844 4670 -2829 576 -252 C ATOM 2045 OG1 THR A 297 39.513 -24.587 9.035 1.00 40.90 O ANISOU 2045 OG1 THR A 297 7143 3810 4588 -2811 542 -232 O ATOM 2046 CG2 THR A 297 39.567 -26.973 8.950 1.00 48.19 C ANISOU 2046 CG2 THR A 297 8072 4638 5598 -2856 535 -220 C ATOM 2047 N LEU A 298 42.278 -24.381 7.034 1.00 50.07 N ANISOU 2047 N LEU A 298 8087 4886 6053 -2726 473 -267 N ATOM 2048 CA LEU A 298 43.698 -24.141 7.161 1.00 49.72 C ANISOU 2048 CA LEU A 298 7988 4755 6146 -2694 396 -253 C ATOM 2049 C LEU A 298 44.004 -23.723 8.588 1.00 54.65 C ANISOU 2049 C LEU A 298 8690 5323 6751 -2691 316 -208 C ATOM 2050 O LEU A 298 43.139 -23.160 9.267 1.00 57.07 O ANISOU 2050 O LEU A 298 9082 5682 6921 -2707 334 -197 O ATOM 2051 CB LEU A 298 44.125 -23.040 6.205 1.00 45.49 C ANISOU 2051 CB LEU A 298 7375 4272 5636 -2669 411 -275 C ATOM 2052 CG LEU A 298 43.790 -23.345 4.756 1.00 41.34 C ANISOU 2052 CG LEU A 298 6790 3813 5106 -2679 492 -321 C ATOM 2053 CD1 LEU A 298 44.173 -22.191 3.906 1.00 39.58 C ANISOU 2053 CD1 LEU A 298 6504 3643 4890 -2662 503 -335 C ATOM 2054 CD2 LEU A 298 44.509 -24.582 4.339 1.00 40.77 C ANISOU 2054 CD2 LEU A 298 6669 3657 5164 -2682 488 -337 C ATOM 2055 N PRO A 299 45.227 -23.972 9.061 1.00 53.82 N ANISOU 2055 N PRO A 299 8559 5107 6783 -2673 229 -186 N ATOM 2056 CA PRO A 299 45.561 -23.604 10.445 1.00 51.63 C ANISOU 2056 CA PRO A 299 8369 4771 6478 -2677 144 -143 C ATOM 2057 C PRO A 299 45.391 -22.111 10.620 1.00 41.64 C ANISOU 2057 C PRO A 299 7131 3568 5122 -2666 139 -142 C ATOM 2058 O PRO A 299 45.661 -21.348 9.694 1.00 41.10 O ANISOU 2058 O PRO A 299 6979 3543 5094 -2643 161 -165 O ATOM 2059 CB PRO A 299 47.022 -24.033 10.584 1.00 47.92 C ANISOU 2059 CB PRO A 299 7829 4173 6206 -2656 54 -129 C ATOM 2060 CG PRO A 299 47.282 -24.982 9.394 1.00 50.24 C ANISOU 2060 CG PRO A 299 8012 4445 6631 -2648 103 -165 C ATOM 2061 CD PRO A 299 46.391 -24.489 8.316 1.00 51.83 C ANISOU 2061 CD PRO A 299 8192 4777 6724 -2651 203 -202 C ATOM 2062 N VAL A 300 44.891 -21.694 11.789 1.00 41.78 N ANISOU 2062 N VAL A 300 7274 3590 5013 -2686 114 -117 N ATOM 2063 CA VAL A 300 44.508 -20.301 12.008 1.00 52.65 C ANISOU 2063 CA VAL A 300 8694 5022 6287 -2679 120 -122 C ATOM 2064 C VAL A 300 45.320 -19.721 13.163 1.00 56.14 C ANISOU 2064 C VAL A 300 9213 5385 6732 -2679 10 -87 C ATOM 2065 O VAL A 300 45.591 -20.404 14.155 1.00 61.19 O ANISOU 2065 O VAL A 300 9933 5952 7364 -2701 -51 -55 O ATOM 2066 CB VAL A 300 42.984 -20.161 12.250 1.00 46.74 C ANISOU 2066 CB VAL A 300 8028 4360 5372 -2708 211 -136 C ATOM 2067 CG1 VAL A 300 42.615 -20.536 13.672 1.00 41.84 C ANISOU 2067 CG1 VAL A 300 7551 3696 4649 -2745 184 -107 C ATOM 2068 CG2 VAL A 300 42.460 -18.747 11.857 1.00 47.21 C ANISOU 2068 CG2 VAL A 300 8077 4493 5368 -2691 251 -159 C ATOM 2069 N SER A 301 45.731 -18.457 13.015 1.00 62.68 N ANISOU 2069 N SER A 301 10020 6225 7572 -2657 -23 -91 N ATOM 2070 CA SER A 301 46.529 -17.720 13.996 1.00 68.00 C ANISOU 2070 CA SER A 301 10764 6828 8246 -2658 -135 -62 C ATOM 2071 C SER A 301 45.756 -17.382 15.263 1.00 69.42 C ANISOU 2071 C SER A 301 11119 7009 8250 -2688 -142 -49 C ATOM 2072 O SER A 301 45.519 -16.204 15.543 1.00 72.57 O ANISOU 2072 O SER A 301 11574 7425 8574 -2684 -149 -57 O ATOM 2073 CB SER A 301 47.012 -16.413 13.376 1.00 72.65 C ANISOU 2073 CB SER A 301 11283 7437 8886 -2631 -155 -74 C ATOM 2074 OG SER A 301 45.891 -15.562 13.102 1.00 75.60 O ANISOU 2074 OG SER A 301 11690 7897 9139 -2630 -75 -98 O ATOM 2075 N GLN A 302 45.347 -18.379 16.032 1.00 63.83 N ANISOU 2075 N GLN A 302 10502 6276 7476 -2722 -137 -31 N ATOM 2076 CA GLN A 302 44.496 -18.127 17.182 1.00 58.06 C ANISOU 2076 CA GLN A 302 9941 5551 6567 -2759 -120 -24 C ATOM 2077 C GLN A 302 44.972 -18.973 18.348 1.00 59.24 C ANISOU 2077 C GLN A 302 10204 5612 6691 -2795 -212 22 C ATOM 2078 O GLN A 302 45.341 -20.139 18.173 1.00 61.08 O ANISOU 2078 O GLN A 302 10386 5807 7015 -2800 -232 40 O ATOM 2079 CB GLN A 302 43.025 -18.433 16.871 1.00 53.42 C ANISOU 2079 CB GLN A 302 9363 5052 5881 -2779 20 -54 C ATOM 2080 CG GLN A 302 42.064 -18.023 17.981 1.00 53.49 C ANISOU 2080 CG GLN A 302 9537 5071 5716 -2819 62 -58 C ATOM 2081 CD GLN A 302 40.639 -18.487 17.747 1.00 49.75 C ANISOU 2081 CD GLN A 302 9064 4674 5163 -2848 200 -86 C ATOM 2082 OE1 GLN A 302 40.349 -19.141 16.760 1.00 48.24 O ANISOU 2082 OE1 GLN A 302 8758 4532 5039 -2838 255 -99 O ATOM 2083 NE2 GLN A 302 39.765 -18.225 18.703 1.00 48.88 N ANISOU 2083 NE2 GLN A 302 9090 4570 4914 -2888 253 -94 N ATOM 2084 N MET A 303 44.964 -18.372 19.533 1.00 59.13 N ANISOU 2084 N MET A 303 10351 5561 6554 -2822 -271 40 N ATOM 2085 CA MET A 303 45.415 -19.028 20.756 1.00 61.29 C ANISOU 2085 CA MET A 303 10763 5750 6777 -2864 -374 88 C ATOM 2086 C MET A 303 44.728 -20.370 20.946 1.00 52.59 C ANISOU 2086 C MET A 303 9692 4654 5636 -2903 -315 102 C ATOM 2087 O MET A 303 43.507 -20.437 21.125 1.00 46.39 O ANISOU 2087 O MET A 303 8972 3930 4723 -2935 -203 81 O ATOM 2088 CB MET A 303 45.161 -18.107 21.962 1.00 75.32 C ANISOU 2088 CB MET A 303 12734 7503 8381 -2895 -412 94 C ATOM 2089 CG MET A 303 46.203 -18.121 23.084 1.00 82.29 C ANISOU 2089 CG MET A 303 13744 8282 9242 -2920 -583 146 C ATOM 2090 SD MET A 303 47.933 -18.052 22.523 1.00 90.77 S ANISOU 2090 SD MET A 303 14662 9284 10543 -2874 -736 174 S ATOM 2091 CE MET A 303 47.919 -16.820 21.200 1.00 85.28 C ANISOU 2091 CE MET A 303 13799 8662 9942 -2815 -660 119 C ATOM 2092 N GLY A 304 45.508 -21.439 20.882 1.00 50.38 N ANISOU 2092 N GLY A 304 9359 4306 5478 -2902 -389 137 N ATOM 2093 CA GLY A 304 44.981 -22.766 21.114 1.00 58.61 C ANISOU 2093 CA GLY A 304 10437 5336 6497 -2943 -355 158 C ATOM 2094 C GLY A 304 44.287 -23.435 19.946 1.00 62.94 C ANISOU 2094 C GLY A 304 10850 5951 7113 -2928 -232 123 C ATOM 2095 O GLY A 304 43.619 -24.451 20.140 1.00 63.76 O ANISOU 2095 O GLY A 304 10995 6058 7175 -2968 -186 137 O ATOM 2096 N MET A 305 44.413 -22.921 18.740 1.00 63.72 N ANISOU 2096 N MET A 305 10797 6102 7311 -2876 -180 81 N ATOM 2097 CA MET A 305 43.676 -23.497 17.635 1.00 64.34 C ANISOU 2097 CA MET A 305 10767 6250 7429 -2868 -65 46 C ATOM 2098 C MET A 305 44.590 -24.093 16.591 1.00 69.39 C ANISOU 2098 C MET A 305 11247 6847 8270 -2826 -89 36 C ATOM 2099 O MET A 305 44.104 -24.582 15.556 1.00 72.71 O ANISOU 2099 O MET A 305 11574 7318 8734 -2818 -4 5 O ATOM 2100 CB MET A 305 42.779 -22.436 17.005 1.00 64.61 C ANISOU 2100 CB MET A 305 10768 6395 7385 -2852 39 -1 C ATOM 2101 CG MET A 305 41.926 -21.739 18.023 1.00 59.69 C ANISOU 2101 CG MET A 305 10295 5802 6583 -2889 72 -2 C ATOM 2102 SD MET A 305 40.813 -22.939 18.700 1.00 45.02 S ANISOU 2102 SD MET A 305 8538 3952 4614 -2960 138 15 S ATOM 2103 CE MET A 305 39.807 -21.903 19.734 1.00 55.47 C ANISOU 2103 CE MET A 305 10018 5314 5744 -2999 203 -3 C ATOM 2104 N ALA A 306 45.896 -24.040 16.824 1.00 67.91 N ANISOU 2104 N ALA A 306 11029 6566 8209 -2803 -202 59 N ATOM 2105 CA ALA A 306 46.873 -24.665 15.954 1.00 67.26 C ANISOU 2105 CA ALA A 306 10795 6419 8340 -2768 -225 47 C ATOM 2106 C ALA A 306 47.691 -25.690 16.724 1.00 69.50 C ANISOU 2106 C ALA A 306 11114 6572 8719 -2783 -329 91 C ATOM 2107 O ALA A 306 48.862 -25.921 16.416 1.00 72.26 O ANISOU 2107 O ALA A 306 11362 6834 9261 -2753 -389 89 O ATOM 2108 CB ALA A 306 47.771 -23.621 15.298 1.00 63.92 C ANISOU 2108 CB ALA A 306 10261 5999 8026 -2723 -251 23 C ATOM 2109 N ILE A 307 47.089 -26.298 17.746 1.00 70.97 N ANISOU 2109 N ILE A 307 11447 6740 8777 -2833 -350 132 N ATOM 2110 CA ILE A 307 47.608 -27.570 18.225 1.00 73.66 C ANISOU 2110 CA ILE A 307 11809 6964 9213 -2852 -423 172 C ATOM 2111 C ILE A 307 47.167 -28.672 17.275 1.00 72.82 C ANISOU 2111 C ILE A 307 11610 6860 9198 -2848 -335 143 C ATOM 2112 O ILE A 307 46.192 -28.530 16.539 1.00 75.99 O ANISOU 2112 O ILE A 307 11980 7366 9525 -2851 -222 106 O ATOM 2113 CB ILE A 307 47.175 -27.874 19.669 1.00 79.39 C ANISOU 2113 CB ILE A 307 12734 7662 9768 -2915 -487 233 C ATOM 2114 CG1 ILE A 307 47.311 -26.635 20.558 1.00 81.04 C ANISOU 2114 CG1 ILE A 307 13060 7893 9838 -2927 -551 250 C ATOM 2115 CG2 ILE A 307 47.981 -29.033 20.242 1.00 82.17 C ANISOU 2115 CG2 ILE A 307 13112 7874 10235 -2931 -598 285 C ATOM 2116 CD1 ILE A 307 46.022 -26.051 20.974 1.00 79.64 C ANISOU 2116 CD1 ILE A 307 13003 7819 9437 -2965 -462 237 C ATOM 2117 N ALA A 308 47.920 -29.767 17.265 1.00 70.03 N ANISOU 2117 N ALA A 308 11211 6384 9014 -2843 -390 159 N ATOM 2118 CA ALA A 308 47.507 -30.925 16.494 1.00 68.64 C ANISOU 2118 CA ALA A 308 10969 6190 8922 -2846 -320 135 C ATOM 2119 C ALA A 308 46.078 -31.257 16.903 1.00 70.15 C ANISOU 2119 C ALA A 308 11283 6463 8908 -2905 -257 155 C ATOM 2120 O ALA A 308 45.707 -31.009 18.061 1.00 71.15 O ANISOU 2120 O ALA A 308 11558 6602 8874 -2949 -299 202 O ATOM 2121 CB ALA A 308 48.455 -32.095 16.735 1.00 70.74 C ANISOU 2121 CB ALA A 308 11206 6291 9380 -2842 -400 158 C ATOM 2122 N PRO A 309 45.229 -31.773 15.985 1.00 67.11 N ANISOU 2122 N PRO A 309 10844 6138 8516 -2913 -153 118 N ATOM 2123 CA PRO A 309 45.518 -32.113 14.589 1.00 63.30 C ANISOU 2123 CA PRO A 309 10208 5650 8194 -2872 -97 60 C ATOM 2124 C PRO A 309 45.377 -30.941 13.632 1.00 62.61 C ANISOU 2124 C PRO A 309 10036 5679 8074 -2835 -26 7 C ATOM 2125 O PRO A 309 45.512 -31.126 12.410 1.00 64.27 O ANISOU 2125 O PRO A 309 10131 5903 8385 -2809 28 -43 O ATOM 2126 CB PRO A 309 44.454 -33.159 14.275 1.00 65.26 C ANISOU 2126 CB PRO A 309 10486 5922 8388 -2917 -29 56 C ATOM 2127 CG PRO A 309 43.288 -32.746 15.100 1.00 65.88 C ANISOU 2127 CG PRO A 309 10697 6099 8236 -2972 6 88 C ATOM 2128 CD PRO A 309 43.862 -32.184 16.368 1.00 67.87 C ANISOU 2128 CD PRO A 309 11047 6306 8434 -2977 -89 137 C ATOM 2129 N PHE A 310 45.091 -29.760 14.182 1.00 59.51 N ANISOU 2129 N PHE A 310 9708 5366 7537 -2838 -28 19 N ATOM 2130 CA PHE A 310 44.868 -28.540 13.411 1.00 56.11 C ANISOU 2130 CA PHE A 310 9217 5047 7055 -2809 33 -23 C ATOM 2131 C PHE A 310 46.133 -27.708 13.209 1.00 57.34 C ANISOU 2131 C PHE A 310 9288 5159 7340 -2759 -30 -32 C ATOM 2132 O PHE A 310 46.035 -26.529 12.832 1.00 57.76 O ANISOU 2132 O PHE A 310 9314 5294 7337 -2739 -1 -53 O ATOM 2133 CB PHE A 310 43.800 -27.690 14.087 1.00 52.23 C ANISOU 2133 CB PHE A 310 8840 4658 6349 -2839 74 -12 C ATOM 2134 CG PHE A 310 42.461 -28.364 14.181 1.00 50.75 C ANISOU 2134 CG PHE A 310 8717 4529 6037 -2892 153 -11 C ATOM 2135 CD1 PHE A 310 41.755 -28.696 13.040 1.00 44.98 C ANISOU 2135 CD1 PHE A 310 7912 3868 5310 -2893 244 -53 C ATOM 2136 CD2 PHE A 310 41.910 -28.660 15.414 1.00 51.99 C ANISOU 2136 CD2 PHE A 310 9014 4670 6072 -2945 133 32 C ATOM 2137 CE1 PHE A 310 40.526 -29.292 13.129 1.00 45.18 C ANISOU 2137 CE1 PHE A 310 7990 3945 5231 -2946 312 -51 C ATOM 2138 CE2 PHE A 310 40.670 -29.256 15.515 1.00 49.42 C ANISOU 2138 CE2 PHE A 310 8740 4396 5640 -3000 209 34 C ATOM 2139 CZ PHE A 310 39.982 -29.577 14.364 1.00 48.05 C ANISOU 2139 CZ PHE A 310 8481 4291 5486 -2999 296 -8 C ATOM 2140 N ASP A 311 47.307 -28.293 13.478 1.00 59.90 N ANISOU 2140 N ASP A 311 9569 5350 7841 -2743 -116 -15 N ATOM 2141 CA ASP A 311 48.573 -27.640 13.159 1.00 61.65 C ANISOU 2141 CA ASP A 311 9684 5519 8222 -2701 -167 -30 C ATOM 2142 C ASP A 311 48.765 -27.511 11.655 1.00 53.61 C ANISOU 2142 C ASP A 311 8517 4540 7314 -2669 -92 -87 C ATOM 2143 O ASP A 311 49.326 -26.524 11.178 1.00 47.77 O ANISOU 2143 O ASP A 311 7701 3827 6622 -2642 -95 -104 O ATOM 2144 CB ASP A 311 49.742 -28.413 13.780 1.00 68.30 C ANISOU 2144 CB ASP A 311 10508 6200 9243 -2696 -266 -4 C ATOM 2145 CG ASP A 311 49.704 -29.912 13.466 1.00 73.89 C ANISOU 2145 CG ASP A 311 11183 6822 10071 -2703 -244 -14 C ATOM 2146 OD1 ASP A 311 48.683 -30.582 13.747 1.00 74.17 O ANISOU 2146 OD1 ASP A 311 11313 6891 9979 -2740 -213 5 O ATOM 2147 OD2 ASP A 311 50.703 -30.417 12.912 1.00 76.52 O ANISOU 2147 OD2 ASP A 311 11391 7049 10635 -2674 -253 -45 O ATOM 2148 N LYS A 312 48.305 -28.489 10.903 1.00 59.55 N ANISOU 2148 N LYS A 312 9234 5293 8098 -2677 -29 -114 N ATOM 2149 CA LYS A 312 48.350 -28.534 9.456 1.00 61.90 C ANISOU 2149 CA LYS A 312 9420 5632 8468 -2659 44 -167 C ATOM 2150 C LYS A 312 46.951 -28.301 8.888 1.00 59.58 C ANISOU 2150 C LYS A 312 9179 5488 7970 -2684 145 -187 C ATOM 2151 O LYS A 312 45.970 -28.211 9.635 1.00 62.47 O ANISOU 2151 O LYS A 312 9656 5912 8168 -2714 159 -161 O ATOM 2152 CB LYS A 312 48.920 -29.893 9.018 1.00 65.73 C ANISOU 2152 CB LYS A 312 9834 5992 9150 -2654 33 -188 C ATOM 2153 CG LYS A 312 48.362 -31.073 9.813 1.00 72.89 C ANISOU 2153 CG LYS A 312 10837 6836 10019 -2687 14 -158 C ATOM 2154 CD LYS A 312 49.467 -31.985 10.425 1.00 81.67 C ANISOU 2154 CD LYS A 312 11916 7762 11354 -2674 -72 -143 C ATOM 2155 CE LYS A 312 48.839 -33.137 11.297 1.00 85.13 C ANISOU 2155 CE LYS A 312 12472 8142 11731 -2716 -96 -102 C ATOM 2156 NZ LYS A 312 49.779 -34.089 11.996 1.00 85.58 N ANISOU 2156 NZ LYS A 312 12522 8016 11977 -2710 -174 -82 N ATOM 2157 N PRO A 313 46.831 -28.128 7.573 1.00 51.07 N ANISOU 2157 N PRO A 313 8026 4479 6901 -2676 217 -234 N ATOM 2158 CA PRO A 313 45.508 -28.153 6.942 1.00 48.26 C ANISOU 2158 CA PRO A 313 7713 4248 6375 -2705 316 -259 C ATOM 2159 C PRO A 313 44.746 -29.416 7.294 1.00 49.15 C ANISOU 2159 C PRO A 313 7894 4330 6451 -2743 331 -250 C ATOM 2160 O PRO A 313 45.308 -30.511 7.338 1.00 55.11 O ANISOU 2160 O PRO A 313 8626 4967 7344 -2744 293 -249 O ATOM 2161 CB PRO A 313 45.827 -28.105 5.450 1.00 45.11 C ANISOU 2161 CB PRO A 313 7219 3884 6037 -2695 376 -313 C ATOM 2162 CG PRO A 313 47.059 -27.350 5.386 1.00 52.09 C ANISOU 2162 CG PRO A 313 8022 4720 7050 -2660 320 -308 C ATOM 2163 CD PRO A 313 47.856 -27.647 6.641 1.00 53.73 C ANISOU 2163 CD PRO A 313 8242 4796 7376 -2646 214 -263 C ATOM 2164 N HIS A 314 43.449 -29.252 7.534 1.00 47.73 N ANISOU 2164 N HIS A 314 7793 4249 6092 -2777 386 -243 N ATOM 2165 CA HIS A 314 42.625 -30.323 8.064 1.00 49.32 C ANISOU 2165 CA HIS A 314 8072 4428 6239 -2823 395 -222 C ATOM 2166 C HIS A 314 41.389 -30.475 7.187 1.00 53.82 C ANISOU 2166 C HIS A 314 8647 5108 6695 -2858 491 -258 C ATOM 2167 O HIS A 314 40.714 -29.471 6.894 1.00 54.54 O ANISOU 2167 O HIS A 314 8738 5314 6671 -2856 542 -273 O ATOM 2168 CB HIS A 314 42.224 -29.999 9.505 1.00 49.35 C ANISOU 2168 CB HIS A 314 8182 4432 6135 -2844 355 -169 C ATOM 2169 CG HIS A 314 41.636 -31.155 10.253 1.00 51.22 C ANISOU 2169 CG HIS A 314 8503 4619 6340 -2896 343 -134 C ATOM 2170 ND1 HIS A 314 40.517 -31.833 9.817 1.00 51.73 N ANISOU 2170 ND1 HIS A 314 8587 4736 6332 -2941 412 -148 N ATOM 2171 CD2 HIS A 314 41.959 -31.697 11.452 1.00 53.16 C ANISOU 2171 CD2 HIS A 314 8826 4768 6604 -2915 268 -81 C ATOM 2172 CE1 HIS A 314 40.216 -32.781 10.685 1.00 54.21 C ANISOU 2172 CE1 HIS A 314 8980 4985 6633 -2987 380 -105 C ATOM 2173 NE2 HIS A 314 41.066 -32.711 11.694 1.00 53.59 N ANISOU 2173 NE2 HIS A 314 8943 4817 6603 -2972 294 -62 N ATOM 2174 N PRO A 315 41.037 -31.699 6.776 1.00 55.47 N ANISOU 2174 N PRO A 315 8861 5280 6937 -2891 512 -271 N ATOM 2175 CA PRO A 315 39.922 -31.885 5.833 1.00 49.46 C ANISOU 2175 CA PRO A 315 8097 4615 6080 -2928 596 -308 C ATOM 2176 C PRO A 315 38.566 -31.766 6.501 1.00 48.48 C ANISOU 2176 C PRO A 315 8046 4567 5806 -2975 627 -281 C ATOM 2177 O PRO A 315 38.323 -32.382 7.541 1.00 48.95 O ANISOU 2177 O PRO A 315 8175 4572 5850 -3006 593 -236 O ATOM 2178 CB PRO A 315 40.135 -33.305 5.319 1.00 51.53 C ANISOU 2178 CB PRO A 315 8348 4784 6446 -2951 592 -326 C ATOM 2179 CG PRO A 315 40.813 -34.001 6.450 1.00 54.86 C ANISOU 2179 CG PRO A 315 8806 5071 6969 -2946 506 -278 C ATOM 2180 CD PRO A 315 41.643 -32.983 7.175 1.00 56.45 C ANISOU 2180 CD PRO A 315 8995 5259 7194 -2900 452 -251 C ATOM 2181 N VAL A 316 37.694 -30.970 5.883 1.00 47.36 N ANISOU 2181 N VAL A 316 7887 4548 5561 -2983 690 -308 N ATOM 2182 CA VAL A 316 36.321 -30.746 6.319 1.00 48.30 C ANISOU 2182 CA VAL A 316 8051 4747 5552 -3027 730 -294 C ATOM 2183 C VAL A 316 35.363 -31.747 5.681 1.00 49.13 C ANISOU 2183 C VAL A 316 8157 4872 5637 -3087 770 -309 C ATOM 2184 O VAL A 316 34.464 -32.254 6.353 1.00 51.13 O ANISOU 2184 O VAL A 316 8461 5128 5837 -3140 777 -278 O ATOM 2185 CB VAL A 316 35.928 -29.292 5.991 1.00 45.49 C ANISOU 2185 CB VAL A 316 7665 4497 5123 -3000 765 -316 C ATOM 2186 CG1 VAL A 316 34.480 -29.044 6.305 1.00 42.60 C ANISOU 2186 CG1 VAL A 316 7326 4210 4652 -3045 811 -310 C ATOM 2187 CG2 VAL A 316 36.795 -28.327 6.770 1.00 45.71 C ANISOU 2187 CG2 VAL A 316 7706 4498 5165 -2951 719 -295 C ATOM 2188 N MET A 317 35.558 -32.054 4.401 1.00 48.26 N ANISOU 2188 N MET A 317 7996 4772 5569 -3085 794 -354 N ATOM 2189 CA MET A 317 34.717 -32.988 3.671 1.00 50.27 C ANISOU 2189 CA MET A 317 8253 5040 5806 -3145 826 -372 C ATOM 2190 C MET A 317 35.291 -33.156 2.271 1.00 54.80 C ANISOU 2190 C MET A 317 8777 5613 6432 -3132 849 -429 C ATOM 2191 O MET A 317 35.977 -32.269 1.755 1.00 57.44 O ANISOU 2191 O MET A 317 9068 5978 6780 -3084 858 -455 O ATOM 2192 CB MET A 317 33.280 -32.491 3.571 1.00 47.27 C ANISOU 2192 CB MET A 317 7872 4770 5317 -3187 867 -369 C ATOM 2193 CG MET A 317 32.976 -31.726 2.311 1.00 49.72 C ANISOU 2193 CG MET A 317 8126 5173 5590 -3179 905 -414 C ATOM 2194 SD MET A 317 31.348 -30.994 2.352 1.00 43.79 S ANISOU 2194 SD MET A 317 7359 4535 4744 -3220 936 -402 S ATOM 2195 CE MET A 317 30.961 -30.942 0.623 1.00 43.76 C ANISOU 2195 CE MET A 317 7306 4599 4721 -3247 961 -450 C ATOM 2196 N ARG A 318 34.998 -34.297 1.656 1.00 52.80 N ANISOU 2196 N ARG A 318 8536 5321 6205 -3181 859 -448 N ATOM 2197 CA ARG A 318 35.484 -34.619 0.324 1.00 52.22 C ANISOU 2197 CA ARG A 318 8431 5236 6174 -3182 888 -508 C ATOM 2198 C ARG A 318 34.354 -34.498 -0.680 1.00 49.20 C ANISOU 2198 C ARG A 318 8045 4956 5694 -3237 933 -535 C ATOM 2199 O ARG A 318 33.263 -34.996 -0.435 1.00 51.79 O ANISOU 2199 O ARG A 318 8401 5301 5974 -3296 930 -510 O ATOM 2200 CB ARG A 318 36.037 -36.035 0.285 1.00 58.96 C ANISOU 2200 CB ARG A 318 9306 5955 7139 -3201 862 -518 C ATOM 2201 CG ARG A 318 36.807 -36.341 -0.963 1.00 70.78 C ANISOU 2201 CG ARG A 318 10773 7419 8702 -3192 893 -587 C ATOM 2202 CD ARG A 318 37.570 -37.627 -0.804 1.00 83.35 C ANISOU 2202 CD ARG A 318 12379 8852 10439 -3193 854 -597 C ATOM 2203 NE ARG A 318 36.889 -38.744 -1.459 1.00 92.34 N ANISOU 2203 NE ARG A 318 13558 9960 11568 -3263 870 -625 N ATOM 2204 CZ ARG A 318 37.451 -39.514 -2.391 1.00101.05 C ANISOU 2204 CZ ARG A 318 14660 10983 12751 -3274 888 -691 C ATOM 2205 NH1 ARG A 318 36.772 -40.520 -2.936 1.00104.33 N ANISOU 2205 NH1 ARG A 318 15122 11367 13153 -3344 896 -714 N ATOM 2206 NH2 ARG A 318 38.691 -39.265 -2.804 1.00104.31 N ANISOU 2206 NH2 ARG A 318 15025 11347 13260 -3218 899 -736 N ATOM 2207 N ILE A 319 34.603 -33.865 -1.818 1.00 47.95 N ANISOU 2207 N ILE A 319 7850 4858 5509 -3224 970 -583 N ATOM 2208 CA ILE A 319 33.607 -33.781 -2.888 1.00 51.69 C ANISOU 2208 CA ILE A 319 8323 5420 5897 -3282 1003 -610 C ATOM 2209 C ILE A 319 33.980 -34.760 -3.993 1.00 53.96 C ANISOU 2209 C ILE A 319 8626 5656 6221 -3321 1028 -666 C ATOM 2210 O ILE A 319 35.098 -34.716 -4.513 1.00 61.85 O ANISOU 2210 O ILE A 319 9606 6614 7279 -3285 1049 -708 O ATOM 2211 CB ILE A 319 33.490 -32.360 -3.451 1.00 44.45 C ANISOU 2211 CB ILE A 319 7366 4612 4911 -3255 1022 -622 C ATOM 2212 CG1 ILE A 319 32.795 -31.453 -2.450 1.00 43.82 C ANISOU 2212 CG1 ILE A 319 7277 4587 4787 -3235 1000 -572 C ATOM 2213 CG2 ILE A 319 32.739 -32.370 -4.763 1.00 44.76 C ANISOU 2213 CG2 ILE A 319 7404 4724 4878 -3317 1048 -655 C ATOM 2214 CD1 ILE A 319 33.676 -30.406 -1.937 1.00 42.96 C ANISOU 2214 CD1 ILE A 319 7144 4477 4701 -3160 989 -563 C ATOM 2215 N GLN A 320 33.047 -35.630 -4.366 1.00 54.54 N ANISOU 2215 N GLN A 320 8733 5728 6263 -3397 1027 -668 N ATOM 2216 CA GLN A 320 33.222 -36.574 -5.452 1.00 59.15 C ANISOU 2216 CA GLN A 320 9344 6264 6866 -3448 1051 -724 C ATOM 2217 C GLN A 320 32.196 -36.304 -6.544 1.00 55.87 C ANISOU 2217 C GLN A 320 8934 5950 6343 -3517 1070 -742 C ATOM 2218 O GLN A 320 30.984 -36.330 -6.281 1.00 54.03 O ANISOU 2218 O GLN A 320 8704 5766 6057 -3568 1044 -699 O ATOM 2219 CB GLN A 320 33.097 -38.031 -4.979 1.00 67.11 C ANISOU 2219 CB GLN A 320 10398 7152 7948 -3489 1018 -711 C ATOM 2220 CG GLN A 320 33.218 -39.023 -6.123 1.00 73.53 C ANISOU 2220 CG GLN A 320 11247 7907 8782 -3546 1041 -776 C ATOM 2221 CD GLN A 320 34.595 -39.639 -6.213 1.00 81.26 C ANISOU 2221 CD GLN A 320 12226 8756 9891 -3500 1049 -825 C ATOM 2222 OE1 GLN A 320 35.112 -40.202 -5.232 1.00 85.64 O ANISOU 2222 OE1 GLN A 320 12784 9201 10553 -3466 1003 -794 O ATOM 2223 NE2 GLN A 320 35.216 -39.517 -7.395 1.00 80.61 N ANISOU 2223 NE2 GLN A 320 12140 8682 9805 -3502 1105 -901 N ATOM 2224 N PRO A 321 32.626 -36.025 -7.765 1.00 51.73 N ANISOU 2224 N PRO A 321 8408 5459 5787 -3528 1113 -801 N ATOM 2225 CA PRO A 321 31.662 -35.693 -8.811 1.00 52.41 C ANISOU 2225 CA PRO A 321 8503 5644 5767 -3599 1120 -812 C ATOM 2226 C PRO A 321 31.140 -36.948 -9.472 1.00 53.51 C ANISOU 2226 C PRO A 321 8698 5733 5900 -3691 1117 -837 C ATOM 2227 O PRO A 321 31.876 -37.909 -9.711 1.00 50.59 O ANISOU 2227 O PRO A 321 8363 5260 5598 -3697 1137 -885 O ATOM 2228 CB PRO A 321 32.482 -34.853 -9.795 1.00 47.93 C ANISOU 2228 CB PRO A 321 7919 5125 5165 -3573 1169 -863 C ATOM 2229 CG PRO A 321 33.848 -34.712 -9.155 1.00 47.41 C ANISOU 2229 CG PRO A 321 7825 4988 5200 -3484 1185 -875 C ATOM 2230 CD PRO A 321 34.004 -35.836 -8.217 1.00 51.72 C ANISOU 2230 CD PRO A 321 8392 5417 5843 -3476 1155 -856 C ATOM 2231 N ILE A 322 29.833 -36.921 -9.734 1.00 56.12 N ANISOU 2231 N ILE A 322 9033 6132 6159 -3765 1084 -804 N ATOM 2232 CA ILE A 322 29.182 -37.973 -10.503 1.00 51.57 C ANISOU 2232 CA ILE A 322 8509 5524 5560 -3869 1071 -824 C ATOM 2233 C ILE A 322 28.109 -37.396 -11.416 1.00 51.74 C ANISOU 2233 C ILE A 322 8522 5657 5478 -3943 1050 -809 C ATOM 2234 O ILE A 322 27.860 -36.188 -11.432 1.00 50.80 O ANISOU 2234 O ILE A 322 8354 5634 5313 -3911 1044 -782 O ATOM 2235 CB ILE A 322 28.571 -39.052 -9.601 1.00 52.42 C ANISOU 2235 CB ILE A 322 8636 5552 5728 -3905 1025 -778 C ATOM 2236 CG1 ILE A 322 27.678 -38.432 -8.577 1.00 51.82 C ANISOU 2236 CG1 ILE A 322 8510 5541 5640 -3891 989 -699 C ATOM 2237 CG2 ILE A 322 29.624 -39.832 -8.877 1.00 52.61 C ANISOU 2237 CG2 ILE A 322 8682 5446 5862 -3850 1033 -795 C ATOM 2238 CD1 ILE A 322 27.094 -39.467 -7.745 1.00 52.75 C ANISOU 2238 CD1 ILE A 322 8647 5586 5810 -3937 951 -654 C ATOM 2239 N ALA A 323 27.445 -38.275 -12.159 1.00 53.05 N ANISOU 2239 N ALA A 323 8738 5802 5616 -4047 1029 -821 N ATOM 2240 CA ALA A 323 26.579 -37.886 -13.263 1.00 53.51 C ANISOU 2240 CA ALA A 323 8802 5951 5578 -4133 1006 -817 C ATOM 2241 C ALA A 323 25.238 -37.324 -12.828 1.00 59.38 C ANISOU 2241 C ALA A 323 9482 6774 6305 -4162 941 -733 C ATOM 2242 O ALA A 323 24.253 -37.481 -13.553 1.00 54.30 O ANISOU 2242 O ALA A 323 8846 6172 5615 -4260 896 -712 O ATOM 2243 CB ALA A 323 26.330 -39.079 -14.172 1.00 55.13 C ANISOU 2243 CB ALA A 323 9087 6095 5764 -4241 997 -858 C ATOM 2244 N ILE A 324 25.186 -36.668 -11.667 1.00 57.23 N ANISOU 2244 N ILE A 324 9146 6522 6076 -4082 936 -686 N ATOM 2245 CA ILE A 324 23.945 -36.070 -11.188 1.00 52.27 C ANISOU 2245 CA ILE A 324 8446 5965 5450 -4102 887 -611 C ATOM 2246 C ILE A 324 23.649 -34.792 -11.964 1.00 51.71 C ANISOU 2246 C ILE A 324 8330 5998 5318 -4099 872 -601 C ATOM 2247 O ILE A 324 24.548 -34.140 -12.504 1.00 55.77 O ANISOU 2247 O ILE A 324 8861 6534 5794 -4052 908 -646 O ATOM 2248 CB ILE A 324 24.067 -35.767 -9.692 1.00 55.87 C ANISOU 2248 CB ILE A 324 8858 6400 5970 -4018 896 -572 C ATOM 2249 CG1 ILE A 324 24.745 -36.887 -8.964 1.00 51.80 C ANISOU 2249 CG1 ILE A 324 8395 5774 5514 -4001 914 -588 C ATOM 2250 CG2 ILE A 324 22.727 -35.616 -9.058 1.00 60.61 C ANISOU 2250 CG2 ILE A 324 9392 7040 6597 -4060 855 -496 C ATOM 2251 CD1 ILE A 324 25.011 -36.440 -7.583 1.00 50.92 C ANISOU 2251 CD1 ILE A 324 8250 5650 5448 -3918 924 -553 C ATOM 2252 N SER A 325 22.376 -34.397 -11.960 1.00 52.09 N ANISOU 2252 N SER A 325 8315 6107 5371 -4150 817 -536 N ATOM 2253 CA SER A 325 21.955 -33.156 -12.598 1.00 51.68 C ANISOU 2253 CA SER A 325 8208 6146 5281 -4150 788 -512 C ATOM 2254 C SER A 325 22.504 -31.926 -11.875 1.00 54.31 C ANISOU 2254 C SER A 325 8490 6506 5638 -4033 814 -506 C ATOM 2255 O SER A 325 22.436 -31.826 -10.647 1.00 56.26 O ANISOU 2255 O SER A 325 8700 6728 5947 -3975 827 -479 O ATOM 2256 CB SER A 325 20.439 -33.079 -12.646 1.00 52.58 C ANISOU 2256 CB SER A 325 8247 6306 5425 -4230 721 -435 C ATOM 2257 OG SER A 325 19.941 -33.979 -13.599 1.00 53.98 O ANISOU 2257 OG SER A 325 8473 6473 5563 -4348 684 -440 O ATOM 2258 N ALA A 326 23.033 -30.971 -12.639 1.00 51.93 N ANISOU 2258 N ALA A 326 8192 6253 5286 -4006 819 -528 N ATOM 2259 CA ALA A 326 23.418 -29.686 -12.085 1.00 48.33 C ANISOU 2259 CA ALA A 326 7683 5826 4855 -3908 828 -515 C ATOM 2260 C ALA A 326 22.275 -28.686 -12.260 1.00 49.67 C ANISOU 2260 C ALA A 326 7765 6064 5045 -3931 770 -447 C ATOM 2261 O ALA A 326 21.240 -28.978 -12.864 1.00 49.48 O ANISOU 2261 O ALA A 326 7717 6068 5015 -4023 721 -409 O ATOM 2262 CB ALA A 326 24.697 -29.197 -12.733 1.00 47.65 C ANISOU 2262 CB ALA A 326 7644 5745 4717 -3864 868 -572 C ATOM 2263 N SER A 327 22.437 -27.486 -11.713 1.00 47.55 N ANISOU 2263 N SER A 327 7441 5815 4812 -3849 771 -426 N ATOM 2264 CA SER A 327 21.264 -26.630 -11.701 1.00 48.31 C ANISOU 2264 CA SER A 327 7439 5958 4960 -3868 720 -354 C ATOM 2265 C SER A 327 21.523 -25.139 -11.802 1.00 50.94 C ANISOU 2265 C SER A 327 7726 6324 5305 -3804 706 -336 C ATOM 2266 O SER A 327 20.599 -24.385 -12.128 1.00 54.39 O ANISOU 2266 O SER A 327 8083 6800 5782 -3831 656 -276 O ATOM 2267 CB SER A 327 20.466 -26.883 -10.438 1.00 51.77 C ANISOU 2267 CB SER A 327 7813 6371 5486 -3854 731 -310 C ATOM 2268 OG SER A 327 19.648 -25.761 -10.199 1.00 56.12 O ANISOU 2268 OG SER A 327 8258 6955 6108 -3834 705 -247 O ATOM 2269 N GLY A 328 22.741 -24.683 -11.509 1.00 45.88 N ANISOU 2269 N GLY A 328 7127 5662 4643 -3721 745 -381 N ATOM 2270 CA GLY A 328 22.973 -23.274 -11.297 1.00 46.97 C ANISOU 2270 CA GLY A 328 7218 5816 4814 -3652 733 -359 C ATOM 2271 C GLY A 328 24.151 -22.726 -12.079 1.00 48.09 C ANISOU 2271 C GLY A 328 7413 5970 4889 -3628 741 -400 C ATOM 2272 O GLY A 328 24.898 -23.457 -12.742 1.00 44.61 O ANISOU 2272 O GLY A 328 7048 5525 4379 -3658 770 -453 O ATOM 2273 N ALA A 329 24.299 -21.406 -11.980 1.00 43.77 N ANISOU 2273 N ALA A 329 6822 5436 4372 -3575 719 -372 N ATOM 2274 CA ALA A 329 25.391 -20.676 -12.601 1.00 43.62 C ANISOU 2274 CA ALA A 329 6839 5429 4306 -3548 723 -397 C ATOM 2275 C ALA A 329 25.954 -19.703 -11.591 1.00 49.61 C ANISOU 2275 C ALA A 329 7568 6154 5125 -3450 734 -389 C ATOM 2276 O ALA A 329 25.353 -19.442 -10.547 1.00 56.79 O ANISOU 2276 O ALA A 329 8428 7041 6110 -3411 733 -358 O ATOM 2277 CB ALA A 329 24.947 -19.905 -13.849 1.00 45.23 C ANISOU 2277 CB ALA A 329 7024 5689 4472 -3610 663 -358 C ATOM 2278 N LEU A 330 27.119 -19.166 -11.920 1.00 49.50 N ANISOU 2278 N LEU A 330 7588 6138 5081 -3416 746 -416 N ATOM 2279 CA LEU A 330 27.783 -18.146 -11.117 1.00 40.89 C ANISOU 2279 CA LEU A 330 6477 5016 4043 -3331 747 -406 C ATOM 2280 C LEU A 330 27.578 -16.770 -11.732 1.00 42.47 C ANISOU 2280 C LEU A 330 6636 5245 4255 -3335 691 -357 C ATOM 2281 O LEU A 330 28.369 -16.334 -12.585 1.00 43.28 O ANISOU 2281 O LEU A 330 6767 5368 4310 -3350 683 -368 O ATOM 2282 CB LEU A 330 29.266 -18.467 -10.997 1.00 48.74 C ANISOU 2282 CB LEU A 330 7525 5979 5015 -3291 794 -461 C ATOM 2283 CG LEU A 330 30.235 -17.416 -10.462 1.00 48.85 C ANISOU 2283 CG LEU A 330 7528 5964 5070 -3217 789 -453 C ATOM 2284 CD1 LEU A 330 29.763 -16.771 -9.164 1.00 47.18 C ANISOU 2284 CD1 LEU A 330 7278 5717 4930 -3157 772 -417 C ATOM 2285 CD2 LEU A 330 31.579 -18.097 -10.266 1.00 48.60 C ANISOU 2285 CD2 LEU A 330 7538 5893 5033 -3189 840 -505 C ATOM 2286 N PRO A 331 26.535 -16.058 -11.319 1.00 42.52 N ANISOU 2286 N PRO A 331 6572 5249 4333 -3326 653 -300 N ATOM 2287 CA PRO A 331 26.197 -14.781 -11.953 1.00 50.30 C ANISOU 2287 CA PRO A 331 7511 6255 5346 -3338 592 -243 C ATOM 2288 C PRO A 331 27.299 -13.748 -11.773 1.00 60.59 C ANISOU 2288 C PRO A 331 8829 7532 6660 -3279 587 -246 C ATOM 2289 O PRO A 331 28.125 -13.839 -10.865 1.00 66.06 O ANISOU 2289 O PRO A 331 9548 8184 7368 -3216 626 -279 O ATOM 2290 CB PRO A 331 24.929 -14.353 -11.215 1.00 46.48 C ANISOU 2290 CB PRO A 331 6940 5752 4969 -3323 574 -188 C ATOM 2291 CG PRO A 331 24.430 -15.590 -10.532 1.00 43.13 C ANISOU 2291 CG PRO A 331 6521 5319 4546 -3334 619 -213 C ATOM 2292 CD PRO A 331 25.635 -16.381 -10.207 1.00 40.96 C ANISOU 2292 CD PRO A 331 6332 5025 4207 -3305 670 -282 C ATOM 2293 N ASP A 332 27.299 -12.733 -12.637 1.00 65.31 N ANISOU 2293 N ASP A 332 9409 8152 7254 -3305 532 -203 N ATOM 2294 CA ASP A 332 28.299 -11.687 -12.477 1.00 62.54 C ANISOU 2294 CA ASP A 332 9066 7773 6922 -3256 520 -196 C ATOM 2295 C ASP A 332 27.786 -10.533 -11.641 1.00 58.07 C ANISOU 2295 C ASP A 332 8438 7159 6468 -3201 488 -145 C ATOM 2296 O ASP A 332 28.586 -9.706 -11.187 1.00 60.86 O ANISOU 2296 O ASP A 332 8800 7472 6853 -3150 481 -142 O ATOM 2297 CB ASP A 332 28.761 -11.205 -13.839 1.00 69.46 C ANISOU 2297 CB ASP A 332 9970 8694 7729 -3316 482 -180 C ATOM 2298 CG ASP A 332 28.829 -12.325 -14.820 1.00 78.38 C ANISOU 2298 CG ASP A 332 11153 9876 8751 -3393 509 -222 C ATOM 2299 OD1 ASP A 332 29.713 -13.192 -14.658 1.00 81.52 O ANISOU 2299 OD1 ASP A 332 11601 10267 9108 -3379 574 -288 O ATOM 2300 OD2 ASP A 332 27.994 -12.346 -15.741 1.00 82.77 O ANISOU 2300 OD2 ASP A 332 11702 10477 9271 -3469 465 -187 O ATOM 2301 N THR A 333 26.479 -10.463 -11.449 1.00 53.61 N ANISOU 2301 N THR A 333 7807 6591 5970 -3216 470 -104 N ATOM 2302 CA THR A 333 25.863 -9.660 -10.414 1.00 58.66 C ANISOU 2302 CA THR A 333 8384 7175 6731 -3162 469 -69 C ATOM 2303 C THR A 333 24.912 -10.544 -9.625 1.00 64.20 C ANISOU 2303 C THR A 333 9052 7872 7468 -3163 515 -79 C ATOM 2304 O THR A 333 24.321 -11.479 -10.169 1.00 68.47 O ANISOU 2304 O THR A 333 9588 8456 7970 -3222 518 -82 O ATOM 2305 CB THR A 333 25.084 -8.502 -10.989 1.00 63.22 C ANISOU 2305 CB THR A 333 8887 7743 7391 -3184 402 6 C ATOM 2306 OG1 THR A 333 23.794 -8.984 -11.399 1.00 72.04 O ANISOU 2306 OG1 THR A 333 9940 8892 8541 -3241 389 41 O ATOM 2307 CG2 THR A 333 25.804 -7.937 -12.178 1.00 62.68 C ANISOU 2307 CG2 THR A 333 8856 7705 7255 -3222 347 23 C ATOM 2308 N LEU A 334 24.737 -10.222 -8.348 1.00 61.42 N ANISOU 2308 N LEU A 334 8679 7465 7192 -3105 551 -80 N ATOM 2309 CA LEU A 334 23.880 -11.006 -7.471 1.00 56.46 C ANISOU 2309 CA LEU A 334 8022 6831 6600 -3106 604 -86 C ATOM 2310 C LEU A 334 22.724 -10.194 -6.919 1.00 55.50 C ANISOU 2310 C LEU A 334 7798 6672 6616 -3094 608 -28 C ATOM 2311 O LEU A 334 21.570 -10.629 -6.996 1.00 59.05 O ANISOU 2311 O LEU A 334 8172 7143 7121 -3135 620 7 O ATOM 2312 CB LEU A 334 24.709 -11.576 -6.317 1.00 52.35 C ANISOU 2312 CB LEU A 334 7578 6280 6034 -3057 660 -144 C ATOM 2313 CG LEU A 334 25.841 -12.514 -6.702 1.00 45.35 C ANISOU 2313 CG LEU A 334 6779 5416 5036 -3065 671 -201 C ATOM 2314 CD1 LEU A 334 26.875 -12.483 -5.609 1.00 38.87 C ANISOU 2314 CD1 LEU A 334 6021 4548 4201 -3003 702 -238 C ATOM 2315 CD2 LEU A 334 25.278 -13.897 -6.900 1.00 41.78 C ANISOU 2315 CD2 LEU A 334 6334 4998 4543 -3117 697 -219 C ATOM 2316 N SER A 335 22.998 -9.027 -6.357 1.00 56.58 N ANISOU 2316 N SER A 335 7926 6752 6820 -3041 603 -13 N ATOM 2317 CA SER A 335 21.917 -8.232 -5.813 1.00 69.11 C ANISOU 2317 CA SER A 335 9413 8294 8553 -3029 619 41 C ATOM 2318 C SER A 335 22.369 -6.790 -5.739 1.00 82.49 C ANISOU 2318 C SER A 335 11105 9924 10313 -2986 580 62 C ATOM 2319 O SER A 335 23.552 -6.476 -5.886 1.00 74.44 O ANISOU 2319 O SER A 335 10167 8896 9221 -2962 550 30 O ATOM 2320 CB SER A 335 21.511 -8.710 -4.431 1.00 64.27 C ANISOU 2320 CB SER A 335 8802 7657 7963 -3005 704 23 C ATOM 2321 OG SER A 335 22.159 -7.905 -3.472 1.00 64.44 O ANISOU 2321 OG SER A 335 8875 7612 7998 -2946 722 1 O ATOM 2322 N SER A 336 21.407 -5.918 -5.482 1.00100.20 N ANISOU 2322 N SER A 336 13248 12118 12707 -2979 583 118 N ATOM 2323 CA SER A 336 21.698 -4.521 -5.226 1.00102.36 C ANISOU 2323 CA SER A 336 13516 12309 13069 -2938 552 137 C ATOM 2324 C SER A 336 21.861 -4.300 -3.725 1.00 99.71 C ANISOU 2324 C SER A 336 13224 11909 12754 -2886 620 105 C ATOM 2325 O SER A 336 21.250 -4.998 -2.907 1.00103.74 O ANISOU 2325 O SER A 336 13732 12437 13248 -2906 704 91 O ATOM 2326 CB SER A 336 20.580 -3.642 -5.783 1.00107.69 C ANISOU 2326 CB SER A 336 14058 12949 13909 -2963 519 216 C ATOM 2327 OG SER A 336 20.918 -2.270 -5.683 1.00112.56 O ANISOU 2327 OG SER A 336 14703 13487 14576 -2963 480 225 O ATOM 2328 N LEU A 337 22.681 -3.316 -3.362 1.00 94.83 N ANISOU 2328 N LEU A 337 12676 11222 12134 -2854 592 85 N ATOM 2329 CA LEU A 337 22.970 -3.038 -1.956 1.00 81.68 C ANISOU 2329 CA LEU A 337 11111 9496 10428 -2846 658 33 C ATOM 2330 C LEU A 337 22.903 -1.538 -1.683 1.00 74.48 C ANISOU 2330 C LEU A 337 10232 8483 9584 -2870 640 40 C ATOM 2331 O LEU A 337 23.672 -0.762 -2.294 1.00 72.09 O ANISOU 2331 O LEU A 337 9940 8146 9304 -2839 547 54 O ATOM 2332 CB LEU A 337 24.339 -3.609 -1.598 1.00 73.14 C ANISOU 2332 CB LEU A 337 10118 8424 9246 -2777 640 -16 C ATOM 2333 CG LEU A 337 24.510 -4.179 -0.205 1.00 65.82 C ANISOU 2333 CG LEU A 337 9289 7482 8240 -2773 725 -72 C ATOM 2334 CD1 LEU A 337 25.746 -5.026 -0.193 1.00 63.36 C ANISOU 2334 CD1 LEU A 337 9057 7208 7807 -2749 706 -116 C ATOM 2335 CD2 LEU A 337 24.631 -3.064 0.797 1.00 68.42 C ANISOU 2335 CD2 LEU A 337 9716 7712 8568 -2788 756 -104 C ATOM 2336 N PRO A 338 22.047 -1.084 -0.761 1.00 69.85 N ANISOU 2336 N PRO A 338 9671 7838 9030 -2925 733 24 N ATOM 2337 CA PRO A 338 21.779 0.355 -0.626 1.00 68.85 C ANISOU 2337 CA PRO A 338 9570 7597 8992 -2960 718 31 C ATOM 2338 C PRO A 338 23.008 1.148 -0.231 1.00 65.34 C ANISOU 2338 C PRO A 338 9254 7065 8509 -2907 654 -11 C ATOM 2339 O PRO A 338 23.998 0.608 0.269 1.00 68.61 O ANISOU 2339 O PRO A 338 9746 7500 8821 -2853 653 -54 O ATOM 2340 CB PRO A 338 20.717 0.419 0.481 1.00 72.03 C ANISOU 2340 CB PRO A 338 10001 7958 9411 -3026 878 -5 C ATOM 2341 CG PRO A 338 20.933 -0.818 1.271 1.00 72.71 C ANISOU 2341 CG PRO A 338 10140 8113 9373 -3005 966 -53 C ATOM 2342 CD PRO A 338 21.333 -1.869 0.261 1.00 71.71 C ANISOU 2342 CD PRO A 338 9928 8101 9219 -2960 872 -11 C ATOM 2343 N ALA A 339 22.917 2.460 -0.444 1.00 61.46 N ANISOU 2343 N ALA A 339 8778 6465 8109 -2926 595 7 N ATOM 2344 CA ALA A 339 24.006 3.352 -0.076 1.00 58.85 C ANISOU 2344 CA ALA A 339 8566 6035 7759 -2879 522 -27 C ATOM 2345 C ALA A 339 24.077 3.519 1.430 1.00 59.80 C ANISOU 2345 C ALA A 339 8850 6059 7812 -2880 622 -115 C ATOM 2346 O ALA A 339 23.171 3.137 2.171 1.00 67.04 O ANISOU 2346 O ALA A 339 9793 6969 8711 -2929 766 -154 O ATOM 2347 CB ALA A 339 23.838 4.723 -0.703 1.00 57.85 C ANISOU 2347 CB ALA A 339 8422 5801 7755 -2899 424 14 C ATOM 2348 N LEU A 340 25.167 4.101 1.875 1.00 56.94 N ANISOU 2348 N LEU A 340 8601 5621 7412 -2827 553 -150 N ATOM 2349 CA LEU A 340 25.200 4.298 3.316 1.00 60.97 C ANISOU 2349 CA LEU A 340 9290 6025 7849 -2828 647 -240 C ATOM 2350 C LEU A 340 24.861 5.744 3.657 1.00 70.06 C ANISOU 2350 C LEU A 340 10551 6984 9086 -2837 631 -278 C ATOM 2351 O LEU A 340 25.264 6.664 2.940 1.00 75.10 O ANISOU 2351 O LEU A 340 11157 7568 9808 -2814 490 -234 O ATOM 2352 CB LEU A 340 26.579 3.954 3.885 1.00 55.57 C ANISOU 2352 CB LEU A 340 8691 5363 7059 -2762 594 -268 C ATOM 2353 CG LEU A 340 27.274 2.701 3.345 1.00 52.59 C ANISOU 2353 CG LEU A 340 8210 5148 6626 -2727 565 -228 C ATOM 2354 CD1 LEU A 340 28.182 3.003 2.112 1.00 56.32 C ANISOU 2354 CD1 LEU A 340 8573 5667 7159 -2681 426 -165 C ATOM 2355 CD2 LEU A 340 28.060 2.045 4.445 1.00 44.08 C ANISOU 2355 CD2 LEU A 340 7246 4076 5427 -2699 600 -278 C ATOM 2356 N PRO A 341 24.121 5.981 4.733 1.00 74.73 N ANISOU 2356 N PRO A 341 11280 7455 9657 -2866 783 -367 N ATOM 2357 CA PRO A 341 23.759 7.354 5.098 1.00 78.61 C ANISOU 2357 CA PRO A 341 11904 7726 10237 -2854 781 -426 C ATOM 2358 C PRO A 341 24.937 8.116 5.671 1.00 79.85 C ANISOU 2358 C PRO A 341 12221 7777 10340 -2771 656 -471 C ATOM 2359 O PRO A 341 25.858 7.535 6.246 1.00 81.27 O ANISOU 2359 O PRO A 341 12456 8026 10395 -2737 640 -488 O ATOM 2360 CB PRO A 341 22.677 7.149 6.156 1.00 80.82 C ANISOU 2360 CB PRO A 341 12292 7917 10498 -2892 1034 -531 C ATOM 2361 CG PRO A 341 23.065 5.855 6.812 1.00 77.04 C ANISOU 2361 CG PRO A 341 11833 7583 9854 -2901 1118 -545 C ATOM 2362 CD PRO A 341 23.606 4.995 5.701 1.00 72.65 C ANISOU 2362 CD PRO A 341 11076 7238 9291 -2900 979 -428 C ATOM 2363 N SER A 342 24.894 9.441 5.505 1.00 85.16 N ANISOU 2363 N SER A 342 12962 8276 11120 -2736 559 -486 N ATOM 2364 CA SER A 342 25.988 10.268 5.996 1.00 90.68 C ANISOU 2364 CA SER A 342 13795 8874 11784 -2654 423 -521 C ATOM 2365 C SER A 342 26.201 9.970 7.471 1.00 85.83 C ANISOU 2365 C SER A 342 13385 8204 11022 -2615 536 -637 C ATOM 2366 O SER A 342 25.251 9.739 8.227 1.00 84.49 O ANISOU 2366 O SER A 342 13324 7962 10818 -2630 733 -730 O ATOM 2367 CB SER A 342 25.725 11.758 5.781 1.00 96.40 C ANISOU 2367 CB SER A 342 14595 9388 12644 -2612 322 -540 C ATOM 2368 OG SER A 342 24.472 12.144 6.309 1.00105.88 O ANISOU 2368 OG SER A 342 15914 10413 13902 -2607 480 -638 O ATOM 2369 N LEU A 343 27.466 9.902 7.856 1.00 92.46 N ANISOU 2369 N LEU A 343 14627 9466 11038 -2015 445 -1108 N ATOM 2370 CA LEU A 343 27.840 9.178 9.051 1.00 82.65 C ANISOU 2370 CA LEU A 343 13436 8245 9721 -1912 602 -1192 C ATOM 2371 C LEU A 343 28.079 10.107 10.216 1.00 91.49 C ANISOU 2371 C LEU A 343 14632 9252 10877 -1822 525 -1248 C ATOM 2372 O LEU A 343 28.811 9.760 11.144 1.00 96.30 O ANISOU 2372 O LEU A 343 15303 9882 11404 -1772 600 -1283 O ATOM 2373 CB LEU A 343 29.079 8.337 8.790 1.00 68.54 C ANISOU 2373 CB LEU A 343 11657 6596 7790 -1977 673 -1141 C ATOM 2374 CG LEU A 343 28.925 7.150 7.846 1.00 64.48 C ANISOU 2374 CG LEU A 343 11086 6201 7212 -2026 777 -1127 C ATOM 2375 CD1 LEU A 343 29.275 7.533 6.381 1.00 66.29 C ANISOU 2375 CD1 LEU A 343 11255 6520 7413 -2169 658 -1013 C ATOM 2376 CD2 LEU A 343 29.793 6.036 8.341 1.00 63.61 C ANISOU 2376 CD2 LEU A 343 11007 6178 6983 -1988 908 -1163 C ATOM 2377 N GLU A 344 27.499 11.288 10.185 1.00 98.88 N ANISOU 2377 N GLU A 344 15574 10062 11935 -1796 360 -1259 N ATOM 2378 CA GLU A 344 27.598 12.190 11.311 1.00108.13 C ANISOU 2378 CA GLU A 344 16827 11111 13147 -1686 271 -1338 C ATOM 2379 C GLU A 344 26.193 12.579 11.718 1.00105.87 C ANISOU 2379 C GLU A 344 16510 10738 12978 -1546 277 -1461 C ATOM 2380 O GLU A 344 25.245 12.476 10.935 1.00105.98 O ANISOU 2380 O GLU A 344 16439 10758 13071 -1569 279 -1449 O ATOM 2381 CB GLU A 344 28.482 13.415 10.995 1.00114.66 C ANISOU 2381 CB GLU A 344 17708 11852 14007 -1779 12 -1239 C ATOM 2382 CG GLU A 344 28.237 14.093 9.639 1.00119.98 C ANISOU 2382 CG GLU A 344 18326 12498 14764 -1919 -177 -1117 C ATOM 2383 CD GLU A 344 28.827 13.296 8.472 1.00121.92 C ANISOU 2383 CD GLU A 344 18500 12922 14904 -2084 -106 -985 C ATOM 2384 OE1 GLU A 344 29.851 12.609 8.684 1.00122.60 O ANISOU 2384 OE1 GLU A 344 18595 13128 14858 -2115 2 -957 O ATOM 2385 OE2 GLU A 344 28.276 13.351 7.348 1.00122.00 O ANISOU 2385 OE2 GLU A 344 18442 12956 14956 -2175 -161 -918 O ATOM 2386 N GLY A 345 26.072 12.984 12.978 1.00109.66 N ANISOU 2386 N GLY A 345 17054 11152 13460 -1394 287 -1585 N ATOM 2387 CA GLY A 345 24.772 13.149 13.592 1.00108.79 C ANISOU 2387 CA GLY A 345 16900 11012 13424 -1230 350 -1727 C ATOM 2388 C GLY A 345 24.323 11.827 14.170 1.00106.98 C ANISOU 2388 C GLY A 345 16621 10924 13100 -1185 626 -1776 C ATOM 2389 O GLY A 345 23.573 11.784 15.158 1.00110.80 O ANISOU 2389 O GLY A 345 17088 11433 13577 -1037 732 -1902 O ATOM 2390 N LEU A 346 24.798 10.737 13.551 1.00 98.89 N ANISOU 2390 N LEU A 346 15575 10002 11997 -1314 734 -1674 N ATOM 2391 CA LEU A 346 24.499 9.384 14.006 1.00 82.26 C ANISOU 2391 CA LEU A 346 13437 8016 9803 -1301 965 -1694 C ATOM 2392 C LEU A 346 24.960 9.193 15.438 1.00 79.83 C ANISOU 2392 C LEU A 346 13212 7728 9390 -1206 1060 -1771 C ATOM 2393 O LEU A 346 26.151 9.346 15.737 1.00 79.41 O ANISOU 2393 O LEU A 346 13254 7651 9268 -1236 1004 -1742 O ATOM 2394 CB LEU A 346 25.171 8.356 13.103 1.00 65.58 C ANISOU 2394 CB LEU A 346 11315 5982 7621 -1444 1016 -1583 C ATOM 2395 CG LEU A 346 24.865 8.507 11.626 1.00 61.63 C ANISOU 2395 CG LEU A 346 10744 5477 7194 -1554 917 -1498 C ATOM 2396 CD1 LEU A 346 25.333 7.293 10.845 1.00 58.49 C ANISOU 2396 CD1 LEU A 346 10331 5181 6712 -1660 1001 -1425 C ATOM 2397 CD2 LEU A 346 23.386 8.702 11.451 1.00 62.99 C ANISOU 2397 CD2 LEU A 346 10825 5622 7485 -1499 927 -1544 C ATOM 2398 N THR A 347 24.008 8.891 16.325 1.00 77.43 N ANISOU 2398 N THR A 347 12868 7481 9071 -1096 1200 -1865 N ATOM 2399 CA THR A 347 24.323 8.442 17.674 1.00 74.50 C ANISOU 2399 CA THR A 347 12565 7166 8575 -1025 1326 -1926 C ATOM 2400 C THR A 347 25.485 7.460 17.623 1.00 76.22 C ANISOU 2400 C THR A 347 12851 7419 8688 -1134 1377 -1836 C ATOM 2401 O THR A 347 25.505 6.554 16.788 1.00 82.06 O ANISOU 2401 O THR A 347 13546 8206 9427 -1238 1424 -1754 O ATOM 2402 CB THR A 347 23.101 7.758 18.294 1.00 71.63 C ANISOU 2402 CB THR A 347 12109 6921 8187 -961 1511 -1979 C ATOM 2403 OG1 THR A 347 21.913 8.486 17.964 1.00 73.70 O ANISOU 2403 OG1 THR A 347 12262 7170 8570 -881 1467 -2041 O ATOM 2404 CG2 THR A 347 23.252 7.649 19.807 1.00 72.04 C ANISOU 2404 CG2 THR A 347 12226 7034 8110 -861 1616 -2064 C ATOM 2405 N VAL A 348 26.466 7.649 18.494 1.00 74.09 N ANISOU 2405 N VAL A 348 12693 7124 8332 -1103 1354 -1859 N ATOM 2406 CA VAL A 348 27.661 6.814 18.502 1.00 72.88 C ANISOU 2406 CA VAL A 348 12606 6998 8088 -1190 1382 -1783 C ATOM 2407 C VAL A 348 27.805 6.191 19.878 1.00 75.68 C ANISOU 2407 C VAL A 348 13030 7401 8324 -1133 1508 -1832 C ATOM 2408 O VAL A 348 27.657 6.887 20.889 1.00 82.77 O ANISOU 2408 O VAL A 348 13982 8275 9191 -1026 1496 -1922 O ATOM 2409 CB VAL A 348 28.913 7.627 18.129 1.00 59.25 C ANISOU 2409 CB VAL A 348 10945 5196 6370 -1238 1207 -1732 C ATOM 2410 CG1 VAL A 348 30.162 6.924 18.588 1.00 58.56 C ANISOU 2410 CG1 VAL A 348 10935 5140 6176 -1280 1240 -1690 C ATOM 2411 CG2 VAL A 348 28.948 7.823 16.640 1.00 59.00 C ANISOU 2411 CG2 VAL A 348 10837 5163 6417 -1343 1112 -1644 C ATOM 2412 N ARG A 349 28.083 4.881 19.920 1.00 67.84 N ANISOU 2412 N ARG A 349 12042 6472 7261 -1202 1614 -1775 N ATOM 2413 CA ARG A 349 28.202 4.143 21.178 1.00 66.27 C ANISOU 2413 CA ARG A 349 11910 6323 6946 -1175 1728 -1797 C ATOM 2414 C ARG A 349 29.513 3.377 21.207 1.00 61.85 C ANISOU 2414 C ARG A 349 11429 5749 6320 -1243 1706 -1734 C ATOM 2415 O ARG A 349 29.798 2.618 20.278 1.00 65.04 O ANISOU 2415 O ARG A 349 11797 6168 6748 -1321 1701 -1670 O ATOM 2416 CB ARG A 349 27.029 3.183 21.350 1.00 65.36 C ANISOU 2416 CB ARG A 349 11716 6302 6817 -1193 1876 -1785 C ATOM 2417 CG ARG A 349 25.776 3.682 20.681 1.00 66.47 C ANISOU 2417 CG ARG A 349 11732 6462 7064 -1167 1880 -1810 C ATOM 2418 CD ARG A 349 24.535 2.989 21.207 1.00 71.64 C ANISOU 2418 CD ARG A 349 12300 7231 7688 -1162 2030 -1810 C ATOM 2419 NE ARG A 349 23.334 3.717 20.822 1.00 74.10 N ANISOU 2419 NE ARG A 349 12488 7567 8098 -1100 2030 -1860 N ATOM 2420 CZ ARG A 349 22.631 4.459 21.662 1.00 73.87 C ANISOU 2420 CZ ARG A 349 12421 7597 8048 -974 2074 -1963 C ATOM 2421 NH1 ARG A 349 23.017 4.549 22.928 1.00 73.15 N ANISOU 2421 NH1 ARG A 349 12414 7549 7829 -907 2127 -2021 N ATOM 2422 NH2 ARG A 349 21.555 5.107 21.237 1.00 75.45 N ANISOU 2422 NH2 ARG A 349 12500 7816 8353 -908 2061 -2014 N ATOM 2423 N LYS A 350 30.315 3.578 22.259 1.00 62.63 N ANISOU 2423 N LYS A 350 11636 5823 6336 -1204 1686 -1760 N ATOM 2424 CA LYS A 350 31.554 2.825 22.445 1.00 69.15 C ANISOU 2424 CA LYS A 350 12536 6639 7099 -1256 1666 -1707 C ATOM 2425 C LYS A 350 31.333 1.685 23.423 1.00 69.03 C ANISOU 2425 C LYS A 350 12567 6670 6989 -1266 1782 -1700 C ATOM 2426 O LYS A 350 30.883 1.894 24.555 1.00 69.22 O ANISOU 2426 O LYS A 350 12637 6723 6942 -1212 1843 -1749 O ATOM 2427 CB LYS A 350 32.723 3.682 22.947 1.00 77.25 C ANISOU 2427 CB LYS A 350 13657 7598 8096 -1229 1547 -1717 C ATOM 2428 CG LYS A 350 33.782 2.886 23.846 1.00 80.19 C ANISOU 2428 CG LYS A 350 14133 7967 8370 -1246 1558 -1692 C ATOM 2429 CD LYS A 350 35.205 2.707 23.215 1.00 76.69 C ANISOU 2429 CD LYS A 350 13692 7508 7938 -1303 1458 -1624 C ATOM 2430 CE LYS A 350 36.298 2.558 24.305 1.00 71.97 C ANISOU 2430 CE LYS A 350 13211 6874 7260 -1291 1416 -1618 C ATOM 2431 NZ LYS A 350 37.670 2.554 23.710 1.00 67.60 N ANISOU 2431 NZ LYS A 350 12639 6323 6724 -1337 1312 -1555 N ATOM 2432 N LEU A 351 31.666 0.487 22.971 1.00 69.77 N ANISOU 2432 N LEU A 351 12653 6776 7080 -1336 1800 -1639 N ATOM 2433 CA LEU A 351 31.700 -0.708 23.787 1.00 65.89 C ANISOU 2433 CA LEU A 351 12221 6304 6509 -1370 1865 -1608 C ATOM 2434 C LEU A 351 33.157 -1.132 23.842 1.00 66.46 C ANISOU 2434 C LEU A 351 12370 6327 6552 -1386 1782 -1582 C ATOM 2435 O LEU A 351 33.818 -1.212 22.802 1.00 67.00 O ANISOU 2435 O LEU A 351 12398 6385 6675 -1403 1714 -1564 O ATOM 2436 CB LEU A 351 30.808 -1.802 23.186 1.00 62.50 C ANISOU 2436 CB LEU A 351 11721 5911 6118 -1435 1924 -1561 C ATOM 2437 CG LEU A 351 29.293 -1.726 23.459 1.00 61.74 C ANISOU 2437 CG LEU A 351 11546 5888 6026 -1436 2029 -1566 C ATOM 2438 CD1 LEU A 351 28.719 -0.344 23.248 1.00 59.35 C ANISOU 2438 CD1 LEU A 351 11177 5599 5773 -1359 2027 -1635 C ATOM 2439 CD2 LEU A 351 28.553 -2.679 22.559 1.00 64.79 C ANISOU 2439 CD2 LEU A 351 11853 6286 6477 -1511 2046 -1509 C ATOM 2440 N GLN A 352 33.666 -1.348 25.044 1.00 66.21 N ANISOU 2440 N GLN A 352 12445 6280 6432 -1376 1785 -1581 N ATOM 2441 CA GLN A 352 35.060 -1.707 25.255 1.00 57.75 C ANISOU 2441 CA GLN A 352 11448 5159 5334 -1383 1700 -1559 C ATOM 2442 C GLN A 352 35.113 -3.084 25.907 1.00 69.91 C ANISOU 2442 C GLN A 352 13055 6689 6819 -1429 1725 -1517 C ATOM 2443 O GLN A 352 34.808 -3.219 27.096 1.00 73.46 O ANISOU 2443 O GLN A 352 13579 7151 7180 -1437 1772 -1510 O ATOM 2444 CB GLN A 352 35.732 -0.645 26.109 1.00 58.05 C ANISOU 2444 CB GLN A 352 11569 5164 5325 -1336 1644 -1590 C ATOM 2445 CG GLN A 352 37.001 -1.087 26.724 1.00 58.03 C ANISOU 2445 CG GLN A 352 11659 5116 5273 -1345 1572 -1562 C ATOM 2446 CD GLN A 352 38.079 -1.287 25.732 1.00 57.31 C ANISOU 2446 CD GLN A 352 11513 5018 5243 -1359 1485 -1533 C ATOM 2447 OE1 GLN A 352 38.758 -0.341 25.357 1.00 78.29 O ANISOU 2447 OE1 GLN A 352 14147 7670 7931 -1348 1404 -1530 O ATOM 2448 NE2 GLN A 352 38.271 -2.518 25.303 1.00 57.10 N ANISOU 2448 NE2 GLN A 352 11466 4999 5232 -1382 1490 -1512 N ATOM 2449 N LEU A 353 35.486 -4.108 25.138 1.00 57.72 N ANISOU 2449 N LEU A 353 11486 5125 5322 -1458 1683 -1490 N ATOM 2450 CA LEU A 353 35.549 -5.471 25.662 1.00 58.21 C ANISOU 2450 CA LEU A 353 11617 5150 5350 -1505 1669 -1446 C ATOM 2451 C LEU A 353 36.819 -5.683 26.481 1.00 65.12 C ANISOU 2451 C LEU A 353 12598 5970 6176 -1489 1588 -1439 C ATOM 2452 O LEU A 353 37.878 -5.151 26.153 1.00 67.80 O ANISOU 2452 O LEU A 353 12927 6299 6536 -1444 1521 -1463 O ATOM 2453 CB LEU A 353 35.512 -6.492 24.531 1.00 57.93 C ANISOU 2453 CB LEU A 353 11528 5093 5388 -1522 1625 -1440 C ATOM 2454 CG LEU A 353 34.501 -6.255 23.410 1.00 58.49 C ANISOU 2454 CG LEU A 353 11486 5209 5528 -1533 1674 -1450 C ATOM 2455 CD1 LEU A 353 34.671 -7.315 22.347 1.00 57.47 C ANISOU 2455 CD1 LEU A 353 11329 5049 5456 -1538 1606 -1457 C ATOM 2456 CD2 LEU A 353 33.061 -6.207 23.899 1.00 58.25 C ANISOU 2456 CD2 LEU A 353 11431 5222 5480 -1583 1773 -1417 C ATOM 2457 N SER A 354 36.717 -6.482 27.544 1.00 61.77 N ANISOU 2457 N SER A 354 12271 5516 5684 -1537 1587 -1393 N ATOM 2458 CA SER A 354 37.804 -6.589 28.510 1.00 60.38 C ANISOU 2458 CA SER A 354 12207 5286 5449 -1529 1512 -1381 C ATOM 2459 C SER A 354 37.762 -7.945 29.181 1.00 60.30 C ANISOU 2459 C SER A 354 12286 5220 5406 -1599 1467 -1316 C ATOM 2460 O SER A 354 36.767 -8.296 29.816 1.00 61.24 O ANISOU 2460 O SER A 354 12429 5377 5463 -1672 1534 -1263 O ATOM 2461 CB SER A 354 37.722 -5.480 29.565 1.00 62.48 C ANISOU 2461 CB SER A 354 12532 5584 5624 -1509 1559 -1400 C ATOM 2462 OG SER A 354 36.381 -5.199 29.948 1.00 63.40 O ANISOU 2462 OG SER A 354 12621 5781 5686 -1531 1679 -1400 O ATOM 2463 N MET A 355 38.848 -8.681 29.056 1.00 60.27 N ANISOU 2463 N MET A 355 12325 5133 5440 -1579 1344 -1315 N ATOM 2464 CA MET A 355 39.043 -9.914 29.790 1.00 63.81 C ANISOU 2464 CA MET A 355 12881 5499 5864 -1640 1256 -1252 C ATOM 2465 C MET A 355 39.865 -9.598 31.023 1.00 66.90 C ANISOU 2465 C MET A 355 13387 5861 6172 -1643 1213 -1232 C ATOM 2466 O MET A 355 41.020 -9.186 30.890 1.00 69.64 O ANISOU 2466 O MET A 355 13733 6179 6548 -1572 1142 -1273 O ATOM 2467 CB MET A 355 39.791 -10.930 28.947 1.00 69.34 C ANISOU 2467 CB MET A 355 13567 6114 6664 -1596 1124 -1280 C ATOM 2468 CG MET A 355 39.005 -12.077 28.467 1.00 77.43 C ANISOU 2468 CG MET A 355 14590 7092 7740 -1649 1086 -1249 C ATOM 2469 SD MET A 355 40.247 -13.260 27.934 1.00 82.57 S ANISOU 2469 SD MET A 355 15275 7617 8482 -1566 886 -1303 S ATOM 2470 CE MET A 355 41.157 -13.456 29.447 1.00 78.89 C ANISOU 2470 CE MET A 355 14954 7071 7950 -1599 793 -1244 C ATOM 2471 N ASP A 356 39.276 -9.790 32.210 1.00 71.25 N ANISOU 2471 N ASP A 356 14029 6430 6612 -1729 1251 -1163 N ATOM 2472 CA ASP A 356 39.937 -9.591 33.498 1.00 72.31 C ANISOU 2472 CA ASP A 356 14291 6538 6645 -1748 1207 -1134 C ATOM 2473 C ASP A 356 41.347 -10.190 33.439 1.00 72.05 C ANISOU 2473 C ASP A 356 14313 6382 6682 -1710 1038 -1138 C ATOM 2474 O ASP A 356 41.492 -11.403 33.217 1.00 73.43 O ANISOU 2474 O ASP A 356 14512 6470 6916 -1740 932 -1104 O ATOM 2475 CB ASP A 356 39.098 -10.251 34.604 1.00 77.45 C ANISOU 2475 CB ASP A 356 15029 7224 7175 -1875 1240 -1033 C ATOM 2476 CG ASP A 356 39.669 -10.089 36.033 1.00 75.58 C ANISOU 2476 CG ASP A 356 14937 6974 6804 -1910 1198 -995 C ATOM 2477 OD1 ASP A 356 40.892 -10.215 36.220 1.00 74.86 O ANISOU 2477 OD1 ASP A 356 14916 6777 6750 -1874 1066 -1005 O ATOM 2478 OD2 ASP A 356 38.863 -9.895 36.988 1.00 74.13 O ANISOU 2478 OD2 ASP A 356 14795 6899 6471 -1980 1296 -951 O ATOM 2479 N PRO A 357 42.393 -9.376 33.610 1.00 71.16 N ANISOU 2479 N PRO A 357 14213 6256 6569 -1640 994 -1182 N ATOM 2480 CA PRO A 357 43.775 -9.818 33.324 1.00 70.42 C ANISOU 2480 CA PRO A 357 14122 6073 6559 -1580 844 -1200 C ATOM 2481 C PRO A 357 44.216 -11.041 34.106 1.00 73.56 C ANISOU 2481 C PRO A 357 14645 6357 6949 -1635 705 -1136 C ATOM 2482 O PRO A 357 45.093 -11.790 33.646 1.00 74.46 O ANISOU 2482 O PRO A 357 14742 6391 7160 -1579 572 -1160 O ATOM 2483 CB PRO A 357 44.615 -8.589 33.698 1.00 66.19 C ANISOU 2483 CB PRO A 357 13598 5559 5992 -1533 832 -1227 C ATOM 2484 CG PRO A 357 43.692 -7.429 33.614 1.00 66.60 C ANISOU 2484 CG PRO A 357 13607 5706 5991 -1530 972 -1258 C ATOM 2485 CD PRO A 357 42.299 -7.930 33.873 1.00 70.73 C ANISOU 2485 CD PRO A 357 14146 6274 6454 -1601 1079 -1226 C ATOM 2486 N ILE A 358 43.645 -11.252 35.291 1.00 76.26 N ANISOU 2486 N ILE A 358 15108 6695 7173 -1740 724 -1056 N ATOM 2487 CA ILE A 358 43.944 -12.458 36.049 1.00 80.27 C ANISOU 2487 CA ILE A 358 15742 7088 7668 -1819 579 -973 C ATOM 2488 C ILE A 358 43.473 -13.688 35.280 1.00 85.38 C ANISOU 2488 C ILE A 358 16355 7672 8415 -1843 512 -955 C ATOM 2489 O ILE A 358 44.188 -14.699 35.177 1.00 83.83 O ANISOU 2489 O ILE A 358 16204 7342 8305 -1823 333 -950 O ATOM 2490 CB ILE A 358 43.310 -12.383 37.453 1.00 84.05 C ANISOU 2490 CB ILE A 358 16348 7612 7975 -1945 629 -878 C ATOM 2491 CG1 ILE A 358 43.497 -10.982 38.065 1.00 83.54 C ANISOU 2491 CG1 ILE A 358 16306 7634 7804 -1902 724 -926 C ATOM 2492 CG2 ILE A 358 43.858 -13.470 38.365 1.00 87.29 C ANISOU 2492 CG2 ILE A 358 16908 7896 8364 -2034 450 -780 C ATOM 2493 CD1 ILE A 358 44.816 -10.753 38.809 1.00 78.93 C ANISOU 2493 CD1 ILE A 358 15826 6960 7204 -1874 588 -924 C ATOM 2494 N LEU A 359 42.266 -13.611 34.712 1.00 86.51 N ANISOU 2494 N LEU A 359 16418 7901 8553 -1878 640 -952 N ATOM 2495 CA LEU A 359 41.739 -14.727 33.944 1.00 82.92 C ANISOU 2495 CA LEU A 359 15933 7381 8192 -1906 569 -934 C ATOM 2496 C LEU A 359 42.690 -15.110 32.829 1.00 80.39 C ANISOU 2496 C LEU A 359 15547 6981 8017 -1765 453 -1041 C ATOM 2497 O LEU A 359 42.986 -16.291 32.639 1.00 74.19 O ANISOU 2497 O LEU A 359 14813 6063 7314 -1761 280 -1035 O ATOM 2498 CB LEU A 359 40.370 -14.376 33.374 1.00 78.63 C ANISOU 2498 CB LEU A 359 15288 6957 7632 -1947 734 -927 C ATOM 2499 CG LEU A 359 39.863 -15.439 32.413 1.00 77.79 C ANISOU 2499 CG LEU A 359 15144 6778 7636 -1963 652 -922 C ATOM 2500 CD1 LEU A 359 39.718 -16.797 33.114 1.00 73.49 C ANISOU 2500 CD1 LEU A 359 14730 6103 7089 -2094 479 -798 C ATOM 2501 CD2 LEU A 359 38.558 -14.974 31.783 1.00 80.23 C ANISOU 2501 CD2 LEU A 359 15337 7211 7937 -1996 818 -920 C ATOM 2502 N ASP A 360 43.167 -14.110 32.077 1.00 87.60 N ANISOU 2502 N ASP A 360 16343 7982 8959 -1648 538 -1141 N ATOM 2503 CA ASP A 360 44.133 -14.326 31.000 1.00 92.61 C ANISOU 2503 CA ASP A 360 16887 8595 9706 -1507 453 -1248 C ATOM 2504 C ASP A 360 45.394 -15.029 31.504 1.00 93.66 C ANISOU 2504 C ASP A 360 17098 8607 9881 -1457 263 -1255 C ATOM 2505 O ASP A 360 45.791 -16.077 30.976 1.00 96.79 O ANISOU 2505 O ASP A 360 17495 8909 10372 -1389 115 -1306 O ATOM 2506 CB ASP A 360 44.485 -12.983 30.349 1.00 93.00 C ANISOU 2506 CB ASP A 360 16806 8781 9750 -1426 576 -1317 C ATOM 2507 CG ASP A 360 45.164 -13.141 28.981 1.00 97.24 C ANISOU 2507 CG ASP A 360 17206 9359 10381 -1294 535 -1423 C ATOM 2508 OD1 ASP A 360 46.089 -13.985 28.841 1.00 92.40 O ANISOU 2508 OD1 ASP A 360 16603 8674 9831 -1214 386 -1469 O ATOM 2509 OD2 ASP A 360 44.773 -12.399 28.042 1.00106.06 O ANISOU 2509 OD2 ASP A 360 18202 10591 11504 -1267 650 -1464 O ATOM 2510 N MET A 361 46.058 -14.451 32.510 1.00 89.29 N ANISOU 2510 N MET A 361 16612 8051 9263 -1479 251 -1215 N ATOM 2511 CA MET A 361 47.298 -15.048 33.007 1.00 82.01 C ANISOU 2511 CA MET A 361 15757 7016 8387 -1431 65 -1219 C ATOM 2512 C MET A 361 47.095 -16.509 33.393 1.00 80.41 C ANISOU 2512 C MET A 361 15677 6648 8226 -1488 -111 -1167 C ATOM 2513 O MET A 361 47.880 -17.395 33.015 1.00 79.20 O ANISOU 2513 O MET A 361 15522 6391 8180 -1390 -287 -1229 O ATOM 2514 CB MET A 361 47.809 -14.241 34.196 1.00 78.43 C ANISOU 2514 CB MET A 361 15388 6572 7840 -1482 77 -1158 C ATOM 2515 CG MET A 361 49.297 -14.370 34.455 1.00 76.71 C ANISOU 2515 CG MET A 361 15178 6289 7680 -1399 -80 -1184 C ATOM 2516 SD MET A 361 49.610 -13.740 36.110 1.00 76.15 S ANISOU 2516 SD MET A 361 15271 6181 7481 -1506 -101 -1082 S ATOM 2517 CE MET A 361 48.587 -14.808 37.120 1.00 76.31 C ANISOU 2517 CE MET A 361 15472 6102 7420 -1671 -152 -962 C ATOM 2518 N MET A 362 45.998 -16.782 34.102 1.00 83.67 N ANISOU 2518 N MET A 362 16190 7043 8557 -1646 -72 -1053 N ATOM 2519 CA MET A 362 45.747 -18.124 34.621 1.00 93.51 C ANISOU 2519 CA MET A 362 17570 8129 9830 -1743 -256 -965 C ATOM 2520 C MET A 362 45.389 -19.117 33.509 1.00 98.64 C ANISOU 2520 C MET A 362 18174 8700 10604 -1688 -354 -1026 C ATOM 2521 O MET A 362 45.931 -20.239 33.449 1.00101.00 O ANISOU 2521 O MET A 362 18542 8830 11003 -1645 -586 -1045 O ATOM 2522 CB MET A 362 44.628 -18.051 35.656 1.00 93.03 C ANISOU 2522 CB MET A 362 17604 8116 9627 -1943 -168 -812 C ATOM 2523 CG MET A 362 44.923 -17.156 36.846 1.00 90.56 C ANISOU 2523 CG MET A 362 17362 7875 9173 -1998 -89 -759 C ATOM 2524 SD MET A 362 43.847 -17.657 38.215 1.00 91.61 S ANISOU 2524 SD MET A 362 17641 8027 9140 -2242 -83 -562 S ATOM 2525 CE MET A 362 44.487 -19.284 38.628 1.00 88.93 C ANISOU 2525 CE MET A 362 17453 7440 8896 -2310 -414 -474 C ATOM 2526 N GLY A 363 44.421 -18.749 32.663 1.00101.73 N ANISOU 2526 N GLY A 363 18462 9200 10989 -1692 -196 -1053 N ATOM 2527 CA GLY A 363 44.090 -19.574 31.519 1.00102.17 C ANISOU 2527 CA GLY A 363 18470 9194 11157 -1627 -281 -1125 C ATOM 2528 C GLY A 363 45.307 -19.947 30.709 1.00103.57 C ANISOU 2528 C GLY A 363 18589 9316 11447 -1423 -417 -1283 C ATOM 2529 O GLY A 363 45.561 -21.131 30.470 1.00106.85 O ANISOU 2529 O GLY A 363 19069 9568 11961 -1373 -637 -1321 O ATOM 2530 N MET A 364 46.116 -18.950 30.338 1.00 97.51 N ANISOU 2530 N MET A 364 17701 8684 10665 -1302 -304 -1374 N ATOM 2531 CA MET A 364 47.318 -19.247 29.579 1.00 96.57 C ANISOU 2531 CA MET A 364 17498 8558 10636 -1104 -415 -1522 C ATOM 2532 C MET A 364 48.271 -20.155 30.334 1.00 97.60 C ANISOU 2532 C MET A 364 17742 8515 10828 -1068 -656 -1517 C ATOM 2533 O MET A 364 48.996 -20.923 29.704 1.00 93.88 O ANISOU 2533 O MET A 364 17236 7977 10456 -907 -817 -1643 O ATOM 2534 CB MET A 364 48.039 -17.972 29.160 1.00 98.26 C ANISOU 2534 CB MET A 364 17557 8965 10812 -1015 -258 -1584 C ATOM 2535 CG MET A 364 48.575 -18.049 27.722 1.00105.60 C ANISOU 2535 CG MET A 364 18320 9999 11803 -830 -257 -1746 C ATOM 2536 SD MET A 364 47.285 -17.966 26.456 1.00112.13 S ANISOU 2536 SD MET A 364 19066 10913 12626 -845 -123 -1787 S ATOM 2537 CE MET A 364 46.363 -16.561 27.101 1.00111.64 C ANISOU 2537 CE MET A 364 19006 10956 12454 -1021 109 -1649 C ATOM 2538 N GLN A 365 48.297 -20.106 31.667 1.00103.77 N ANISOU 2538 N GLN A 365 18659 9221 11548 -1206 -696 -1381 N ATOM 2539 CA GLN A 365 49.139 -21.078 32.364 1.00108.29 C ANISOU 2539 CA GLN A 365 19351 9603 12189 -1183 -956 -1368 C ATOM 2540 C GLN A 365 48.620 -22.502 32.178 1.00109.72 C ANISOU 2540 C GLN A 365 19641 9587 12461 -1209 -1174 -1359 C ATOM 2541 O GLN A 365 49.400 -23.429 31.905 1.00111.58 O ANISOU 2541 O GLN A 365 19899 9681 12815 -1070 -1407 -1458 O ATOM 2542 CB GLN A 365 49.257 -20.742 33.842 1.00113.87 C ANISOU 2542 CB GLN A 365 20191 10272 12800 -1338 -962 -1216 C ATOM 2543 CG GLN A 365 50.267 -19.653 34.113 1.00120.09 C ANISOU 2543 CG GLN A 365 20904 11176 13549 -1268 -873 -1248 C ATOM 2544 CD GLN A 365 51.684 -20.183 34.070 1.00124.11 C ANISOU 2544 CD GLN A 365 21392 11595 14169 -1112 -1079 -1335 C ATOM 2545 OE1 GLN A 365 52.592 -19.507 33.578 1.00122.71 O ANISOU 2545 OE1 GLN A 365 21069 11541 14014 -978 -1021 -1425 O ATOM 2546 NE2 GLN A 365 51.872 -21.425 34.536 1.00126.98 N ANISOU 2546 NE2 GLN A 365 21891 11745 14609 -1127 -1334 -1307 N ATOM 2547 N MET A 366 47.306 -22.702 32.341 1.00107.83 N ANISOU 2547 N MET A 366 19468 9333 12170 -1385 -1119 -1240 N ATOM 2548 CA MET A 366 46.746 -24.035 32.103 1.00107.44 C ANISOU 2548 CA MET A 366 19521 9091 12211 -1428 -1342 -1216 C ATOM 2549 C MET A 366 47.066 -24.528 30.695 1.00104.79 C ANISOU 2549 C MET A 366 19087 8731 11995 -1207 -1425 -1420 C ATOM 2550 O MET A 366 47.457 -25.688 30.493 1.00101.70 O ANISOU 2550 O MET A 366 18776 8142 11725 -1118 -1703 -1488 O ATOM 2551 CB MET A 366 45.234 -24.056 32.326 1.00108.92 C ANISOU 2551 CB MET A 366 19752 9312 12321 -1649 -1239 -1057 C ATOM 2552 CG MET A 366 44.780 -24.058 33.763 1.00112.59 C ANISOU 2552 CG MET A 366 20350 9758 12671 -1888 -1241 -840 C ATOM 2553 SD MET A 366 43.000 -24.394 33.834 1.00116.59 S ANISOU 2553 SD MET A 366 20885 10301 13113 -2134 -1172 -660 S ATOM 2554 CE MET A 366 42.931 -26.122 33.330 1.00114.49 C ANISOU 2554 CE MET A 366 20738 9742 13023 -2134 -1553 -660 C ATOM 2555 N LEU A 367 46.919 -23.638 29.713 1.00101.37 N ANISOU 2555 N LEU A 367 18485 8504 11529 -1111 -1195 -1522 N ATOM 2556 CA LEU A 367 47.152 -23.990 28.315 1.00 98.91 C ANISOU 2556 CA LEU A 367 18065 8216 11299 -906 -1238 -1718 C ATOM 2557 C LEU A 367 48.628 -24.280 28.054 1.00105.37 C ANISOU 2557 C LEU A 367 18826 9016 12192 -672 -1380 -1885 C ATOM 2558 O LEU A 367 48.972 -25.300 27.445 1.00111.72 O ANISOU 2558 O LEU A 367 19652 9695 13102 -515 -1596 -2024 O ATOM 2559 CB LEU A 367 46.632 -22.865 27.411 1.00 82.80 C ANISOU 2559 CB LEU A 367 15857 6419 9186 -889 -949 -1761 C ATOM 2560 CG LEU A 367 46.743 -22.879 25.887 1.00 73.85 C ANISOU 2560 CG LEU A 367 14581 5392 8089 -701 -911 -1949 C ATOM 2561 CD1 LEU A 367 46.508 -24.238 25.347 1.00 74.73 C ANISOU 2561 CD1 LEU A 367 14780 5311 8304 -627 -1159 -2034 C ATOM 2562 CD2 LEU A 367 45.697 -21.948 25.353 1.00 72.48 C ANISOU 2562 CD2 LEU A 367 14315 5384 7839 -798 -661 -1899 C ATOM 2563 N MET A 368 49.517 -23.395 28.508 1.00107.02 N ANISOU 2563 N MET A 368 18959 9353 12351 -639 -1270 -1878 N ATOM 2564 CA MET A 368 50.946 -23.588 28.322 1.00109.34 C ANISOU 2564 CA MET A 368 19174 9659 12711 -427 -1390 -2021 C ATOM 2565 C MET A 368 51.455 -24.817 29.043 1.00112.57 C ANISOU 2565 C MET A 368 19744 9803 13225 -401 -1712 -2016 C ATOM 2566 O MET A 368 52.531 -25.320 28.698 1.00111.71 O ANISOU 2566 O MET A 368 19577 9665 13204 -185 -1871 -2173 O ATOM 2567 CB MET A 368 51.707 -22.354 28.796 1.00112.13 C ANISOU 2567 CB MET A 368 19427 10188 12987 -441 -1220 -1974 C ATOM 2568 CG MET A 368 51.665 -21.199 27.822 1.00116.84 C ANISOU 2568 CG MET A 368 19823 11058 13513 -388 -961 -2034 C ATOM 2569 SD MET A 368 52.056 -21.681 26.112 1.00123.44 S ANISOU 2569 SD MET A 368 20480 12017 14404 -126 -988 -2275 S ATOM 2570 CE MET A 368 51.093 -20.410 25.249 1.00120.96 C ANISOU 2570 CE MET A 368 20035 11944 13981 -221 -676 -2236 C ATOM 2571 N GLU A 369 50.721 -25.306 30.043 1.00114.76 N ANISOU 2571 N GLU A 369 20216 9896 13493 -615 -1818 -1838 N ATOM 2572 CA GLU A 369 51.105 -26.597 30.589 1.00117.17 C ANISOU 2572 CA GLU A 369 20685 9923 13913 -597 -2163 -1832 C ATOM 2573 C GLU A 369 50.578 -27.742 29.727 1.00119.26 C ANISOU 2573 C GLU A 369 21003 10029 14282 -515 -2364 -1935 C ATOM 2574 O GLU A 369 51.342 -28.642 29.352 1.00119.93 O ANISOU 2574 O GLU A 369 21050 10022 14494 -306 -2598 -2075 O ATOM 2575 CB GLU A 369 50.637 -26.753 32.038 1.00121.04 C ANISOU 2575 CB GLU A 369 21367 10274 14348 -867 -2236 -1589 C ATOM 2576 CG GLU A 369 50.630 -28.223 32.544 1.00130.97 C ANISOU 2576 CG GLU A 369 22776 11262 15725 -906 -2600 -1518 C ATOM 2577 CD GLU A 369 51.945 -29.018 32.358 1.00137.25 C ANISOU 2577 CD GLU A 369 23521 11954 16673 -652 -2866 -1674 C ATOM 2578 OE1 GLU A 369 52.934 -28.516 31.774 1.00137.53 O ANISOU 2578 OE1 GLU A 369 23436 12092 16728 -431 -2798 -1869 O ATOM 2579 OE2 GLU A 369 51.968 -30.186 32.809 1.00139.31 O ANISOU 2579 OE2 GLU A 369 23866 12032 17034 -676 -3159 -1595 O ATOM 2580 N LYS A 370 49.280 -27.731 29.400 1.00115.40 N ANISOU 2580 N LYS A 370 20544 9556 13748 -665 -2265 -1850 N ATOM 2581 CA LYS A 370 48.664 -28.944 28.873 1.00109.88 C ANISOU 2581 CA LYS A 370 19870 8723 13157 -641 -2481 -1858 C ATOM 2582 C LYS A 370 49.281 -29.375 27.542 1.00111.31 C ANISOU 2582 C LYS A 370 19916 8948 13430 -330 -2560 -2126 C ATOM 2583 O LYS A 370 49.490 -30.573 27.313 1.00115.40 O ANISOU 2583 O LYS A 370 20451 9319 14075 -212 -2840 -2185 O ATOM 2584 CB LYS A 370 47.159 -28.751 28.731 1.00100.28 C ANISOU 2584 CB LYS A 370 18699 7532 11870 -863 -2345 -1717 C ATOM 2585 CG LYS A 370 46.375 -30.023 29.014 1.00101.63 C ANISOU 2585 CG LYS A 370 18981 7508 12126 -996 -2613 -1570 C ATOM 2586 CD LYS A 370 45.113 -30.124 28.181 1.00102.90 C ANISOU 2586 CD LYS A 370 19124 7694 12280 -1076 -2545 -1550 C ATOM 2587 CE LYS A 370 44.196 -31.245 28.646 1.00105.17 C ANISOU 2587 CE LYS A 370 19536 7802 12624 -1277 -2791 -1347 C ATOM 2588 NZ LYS A 370 43.344 -30.803 29.781 1.00104.28 N ANISOU 2588 NZ LYS A 370 19526 7709 12387 -1606 -2671 -1082 N ATOM 2589 N TYR A 371 49.621 -28.423 26.667 1.00110.30 N ANISOU 2589 N TYR A 371 19652 9028 13229 -190 -2325 -2293 N ATOM 2590 CA TYR A 371 50.013 -28.763 25.299 1.00114.24 C ANISOU 2590 CA TYR A 371 20014 9612 13778 86 -2362 -2544 C ATOM 2591 C TYR A 371 51.442 -28.344 24.941 1.00117.31 C ANISOU 2591 C TYR A 371 20274 10141 14157 343 -2328 -2755 C ATOM 2592 O TYR A 371 51.769 -28.213 23.758 1.00116.84 O ANISOU 2592 O TYR A 371 20057 10257 14078 557 -2251 -2959 O ATOM 2593 CB TYR A 371 49.032 -28.162 24.284 1.00109.80 C ANISOU 2593 CB TYR A 371 19386 9201 13132 44 -2136 -2577 C ATOM 2594 CG TYR A 371 47.547 -28.290 24.599 1.00100.79 C ANISOU 2594 CG TYR A 371 18354 7968 11973 -228 -2107 -2366 C ATOM 2595 CD1 TYR A 371 46.955 -27.519 25.576 1.00 94.18 C ANISOU 2595 CD1 TYR A 371 17584 7160 11042 -487 -1936 -2149 C ATOM 2596 CD2 TYR A 371 46.741 -29.162 23.883 1.00 96.24 C ANISOU 2596 CD2 TYR A 371 17792 7306 11468 -217 -2243 -2383 C ATOM 2597 CE1 TYR A 371 45.613 -27.623 25.842 1.00 91.56 C ANISOU 2597 CE1 TYR A 371 17340 6766 10683 -727 -1903 -1968 C ATOM 2598 CE2 TYR A 371 45.401 -29.271 24.147 1.00 93.07 C ANISOU 2598 CE2 TYR A 371 17483 6830 11049 -467 -2224 -2190 C ATOM 2599 CZ TYR A 371 44.841 -28.497 25.129 1.00 93.60 C ANISOU 2599 CZ TYR A 371 17624 6923 11017 -723 -2052 -1986 C ATOM 2600 OH TYR A 371 43.496 -28.597 25.405 1.00 98.60 O ANISOU 2600 OH TYR A 371 18340 7499 11623 -975 -2025 -1795 O ATOM 2601 N GLY A 372 52.315 -28.155 25.933 1.00122.73 N ANISOU 2601 N GLY A 372 20979 10797 14857 326 -2375 -2688 N ATOM 2602 CA GLY A 372 53.641 -27.662 25.589 1.00132.30 C ANISOU 2602 CA GLY A 372 21992 12217 16058 549 -2302 -2840 C ATOM 2603 C GLY A 372 53.487 -26.257 25.034 1.00138.41 C ANISOU 2603 C GLY A 372 22569 13325 16693 501 -1935 -2810 C ATOM 2604 O GLY A 372 52.457 -25.603 25.218 1.00135.15 O ANISOU 2604 O GLY A 372 22196 12955 16200 282 -1748 -2649 O ATOM 2605 N ASP A 373 54.524 -25.788 24.333 1.00149.14 N ANISOU 2605 N ASP A 373 23707 14933 18024 710 -1839 -2964 N ATOM 2606 CA ASP A 373 54.445 -24.489 23.669 1.00152.68 C ANISOU 2606 CA ASP A 373 23960 15706 18348 674 -1520 -2942 C ATOM 2607 C ASP A 373 54.131 -24.613 22.180 1.00151.81 C ANISOU 2607 C ASP A 373 23723 15759 18200 828 -1446 -3121 C ATOM 2608 O ASP A 373 54.249 -23.626 21.442 1.00151.21 O ANISOU 2608 O ASP A 373 23455 15976 18022 840 -1210 -3136 O ATOM 2609 CB ASP A 373 55.711 -23.645 23.910 1.00155.86 C ANISOU 2609 CB ASP A 373 24184 16322 18714 740 -1423 -2938 C ATOM 2610 CG ASP A 373 57.006 -24.401 23.646 1.00161.59 C ANISOU 2610 CG ASP A 373 24809 17066 19522 1021 -1616 -3137 C ATOM 2611 OD1 ASP A 373 57.214 -24.912 22.523 1.00162.58 O ANISOU 2611 OD1 ASP A 373 24821 17299 19652 1247 -1654 -3353 O ATOM 2612 OD2 ASP A 373 57.841 -24.444 24.577 1.00162.94 O ANISOU 2612 OD2 ASP A 373 25007 17157 19746 1020 -1728 -3082 O ATOM 2613 N GLN A 374 53.692 -25.795 21.734 1.00148.50 N ANISOU 2613 N GLN A 374 23418 15147 17857 930 -1655 -3247 N ATOM 2614 CA GLN A 374 52.960 -25.883 20.475 1.00131.82 C ANISOU 2614 CA GLN A 374 21253 13135 15699 993 -1579 -3361 C ATOM 2615 C GLN A 374 51.632 -25.140 20.545 1.00121.65 C ANISOU 2615 C GLN A 374 20019 11861 14341 722 -1377 -3166 C ATOM 2616 O GLN A 374 50.947 -25.027 19.523 1.00116.95 O ANISOU 2616 O GLN A 374 19371 11366 13697 738 -1282 -3228 O ATOM 2617 CB GLN A 374 52.709 -27.348 20.104 1.00125.07 C ANISOU 2617 CB GLN A 374 20544 12023 14952 1142 -1885 -3523 C ATOM 2618 CG GLN A 374 53.466 -27.861 18.876 1.00123.14 C ANISOU 2618 CG GLN A 374 20155 11932 14703 1481 -1960 -3830 C ATOM 2619 CD GLN A 374 52.778 -27.541 17.557 1.00118.57 C ANISOU 2619 CD GLN A 374 19479 11550 14023 1515 -1794 -3920 C ATOM 2620 OE1 GLN A 374 51.915 -26.662 17.488 1.00114.12 O ANISOU 2620 OE1 GLN A 374 18899 11081 13381 1294 -1568 -3751 O ATOM 2621 NE2 GLN A 374 53.135 -28.286 16.508 1.00117.49 N ANISOU 2621 NE2 GLN A 374 19278 11473 13890 1795 -1918 -4187 N ATOM 2622 N ALA A 375 51.266 -24.631 21.723 1.00116.77 N ANISOU 2622 N ALA A 375 19500 11153 13713 485 -1313 -2939 N ATOM 2623 CA ALA A 375 49.963 -24.037 21.973 1.00115.73 C ANISOU 2623 CA ALA A 375 19438 11008 13527 231 -1151 -2751 C ATOM 2624 C ALA A 375 49.814 -22.725 21.230 1.00120.58 C ANISOU 2624 C ALA A 375 19863 11922 14029 202 -856 -2739 C ATOM 2625 O ALA A 375 49.036 -22.605 20.275 1.00120.10 O ANISOU 2625 O ALA A 375 19758 11941 13935 196 -766 -2779 O ATOM 2626 CB ALA A 375 49.765 -23.795 23.469 1.00107.43 C ANISOU 2626 CB ALA A 375 18524 9819 12475 12 -1156 -2533 C ATOM 2627 N MET A 376 50.563 -21.733 21.681 1.00123.98 N ANISOU 2627 N MET A 376 20191 12510 14406 176 -722 -2674 N ATOM 2628 CA MET A 376 50.451 -20.382 21.154 1.00127.06 C ANISOU 2628 CA MET A 376 20418 13164 14696 114 -463 -2624 C ATOM 2629 C MET A 376 51.031 -20.233 19.755 1.00123.23 C ANISOU 2629 C MET A 376 19728 12931 14164 304 -400 -2798 C ATOM 2630 O MET A 376 51.029 -19.109 19.233 1.00122.82 O ANISOU 2630 O MET A 376 19527 13112 14026 253 -203 -2754 O ATOM 2631 CB MET A 376 51.120 -19.430 22.145 1.00129.65 C ANISOU 2631 CB MET A 376 20719 13552 14990 22 -382 -2495 C ATOM 2632 CG MET A 376 52.627 -19.651 22.240 1.00136.99 C ANISOU 2632 CG MET A 376 21550 14550 15949 197 -488 -2591 C ATOM 2633 SD MET A 376 53.536 -18.613 23.420 1.00136.49 S ANISOU 2633 SD MET A 376 21464 14539 15859 96 -435 -2441 S ATOM 2634 CE MET A 376 54.694 -19.825 24.075 1.00137.15 C ANISOU 2634 CE MET A 376 21609 14450 16050 258 -711 -2533 C ATOM 2635 N ALA A 377 51.492 -21.329 19.145 1.00122.68 N ANISOU 2635 N ALA A 377 19648 12821 14142 518 -571 -2992 N ATOM 2636 CA ALA A 377 52.001 -21.301 17.781 1.00114.13 C ANISOU 2636 CA ALA A 377 18371 11995 12996 716 -517 -3176 C ATOM 2637 C ALA A 377 51.037 -20.565 16.859 1.00110.77 C ANISOU 2637 C ALA A 377 17881 11722 12486 612 -326 -3135 C ATOM 2638 O ALA A 377 49.837 -20.852 16.842 1.00111.99 O ANISOU 2638 O ALA A 377 18173 11710 12668 496 -343 -3080 O ATOM 2639 CB ALA A 377 52.218 -22.731 17.285 1.00108.21 C ANISOU 2639 CB ALA A 377 17683 11113 12317 945 -753 -3397 C ATOM 2640 N GLY A 378 51.570 -19.597 16.107 1.00111.39 N ANISOU 2640 N GLY A 378 17744 12119 12460 640 -153 -3148 N ATOM 2641 CA GLY A 378 50.777 -18.788 15.194 1.00115.69 C ANISOU 2641 CA GLY A 378 18207 12831 12917 540 25 -3101 C ATOM 2642 C GLY A 378 50.652 -17.339 15.631 1.00115.02 C ANISOU 2642 C GLY A 378 18062 12856 12784 335 207 -2898 C ATOM 2643 O GLY A 378 50.634 -16.411 14.811 1.00112.11 O ANISOU 2643 O GLY A 378 17540 12731 12325 292 356 -2868 O ATOM 2644 N MET A 379 50.531 -17.141 16.940 1.00124.99 N ANISOU 2644 N MET A 379 19455 13930 14104 203 182 -2756 N ATOM 2645 CA MET A 379 50.619 -15.820 17.541 1.00136.64 C ANISOU 2645 CA MET A 379 20888 15485 15543 39 314 -2583 C ATOM 2646 C MET A 379 51.729 -15.797 18.588 1.00146.69 C ANISOU 2646 C MET A 379 22170 16716 16849 65 236 -2544 C ATOM 2647 O MET A 379 51.640 -15.085 19.597 1.00146.99 O ANISOU 2647 O MET A 379 22281 16677 16892 -81 273 -2395 O ATOM 2648 CB MET A 379 49.274 -15.403 18.136 1.00137.48 C ANISOU 2648 CB MET A 379 21144 15425 15668 -162 382 -2439 C ATOM 2649 CG MET A 379 49.020 -13.884 18.076 1.00136.12 C ANISOU 2649 CG MET A 379 20888 15398 15435 -309 550 -2306 C ATOM 2650 SD MET A 379 48.444 -13.289 16.453 1.00135.75 S ANISOU 2650 SD MET A 379 20686 15577 15316 -316 676 -2342 S ATOM 2651 CE MET A 379 46.693 -13.151 16.747 1.00135.15 C ANISOU 2651 CE MET A 379 20761 15313 15278 -480 733 -2249 C ATOM 2652 N ASP A 380 52.788 -16.580 18.341 1.00155.91 N ANISOU 2652 N ASP A 380 23261 17940 18038 262 119 -2687 N ATOM 2653 CA ASP A 380 53.893 -16.782 19.280 1.00162.74 C ANISOU 2653 CA ASP A 380 24134 18749 18951 316 9 -2675 C ATOM 2654 C ASP A 380 55.049 -15.861 18.890 1.00160.88 C ANISOU 2654 C ASP A 380 23661 18817 18648 353 95 -2655 C ATOM 2655 O ASP A 380 55.739 -16.111 17.894 1.00162.53 O ANISOU 2655 O ASP A 380 23684 19258 18813 522 100 -2793 O ATOM 2656 CB ASP A 380 54.322 -18.254 19.287 1.00169.73 C ANISOU 2656 CB ASP A 380 25082 19491 19918 518 -198 -2847 C ATOM 2657 CG ASP A 380 55.717 -18.479 19.886 1.00175.95 C ANISOU 2657 CG ASP A 380 25802 20302 20748 636 -314 -2882 C ATOM 2658 OD1 ASP A 380 55.844 -18.560 21.132 1.00177.15 O ANISOU 2658 OD1 ASP A 380 26100 20248 20962 545 -405 -2774 O ATOM 2659 OD2 ASP A 380 56.682 -18.609 19.105 1.00178.76 O ANISOU 2659 OD2 ASP A 380 25956 20891 21074 826 -319 -3020 O ATOM 2660 N HIS A 381 55.261 -14.795 19.675 1.00157.88 N ANISOU 2660 N HIS A 381 23286 18447 18254 194 156 -2483 N ATOM 2661 CA HIS A 381 56.340 -13.860 19.373 1.00144.73 C ANISOU 2661 CA HIS A 381 21402 17059 16531 195 220 -2430 C ATOM 2662 C HIS A 381 56.745 -13.012 20.580 1.00133.65 C ANISOU 2662 C HIS A 381 20062 15570 15148 48 203 -2257 C ATOM 2663 O HIS A 381 56.954 -13.530 21.685 1.00127.82 O ANISOU 2663 O HIS A 381 19475 14613 14480 50 84 -2240 O ATOM 2664 CB HIS A 381 55.952 -12.967 18.174 1.00134.65 C ANISOU 2664 CB HIS A 381 19967 16040 15154 131 379 -2401 C ATOM 2665 CG HIS A 381 54.687 -12.179 18.356 1.00123.82 C ANISOU 2665 CG HIS A 381 18722 14551 13771 -66 475 -2274 C ATOM 2666 ND1 HIS A 381 53.588 -12.658 19.039 1.00120.59 N ANISOU 2666 ND1 HIS A 381 18542 13859 13419 -130 447 -2260 N ATOM 2667 CD2 HIS A 381 54.337 -10.954 17.897 1.00120.05 C ANISOU 2667 CD2 HIS A 381 18166 14216 13232 -209 592 -2158 C ATOM 2668 CE1 HIS A 381 52.629 -11.751 19.018 1.00118.43 C ANISOU 2668 CE1 HIS A 381 18314 13567 13118 -290 553 -2151 C ATOM 2669 NE2 HIS A 381 53.057 -10.708 18.330 1.00118.70 N ANISOU 2669 NE2 HIS A 381 18172 13842 13088 -337 634 -2092 N ATOM 2670 N SER A 382 56.873 -11.706 20.359 1.00134.95 N ANISOU 2670 N SER A 382 20116 15907 15251 -83 307 -2127 N ATOM 2671 CA SER A 382 57.473 -10.774 21.303 1.00137.71 C ANISOU 2671 CA SER A 382 20482 16232 15609 -205 279 -1972 C ATOM 2672 C SER A 382 56.499 -10.234 22.358 1.00138.96 C ANISOU 2672 C SER A 382 20874 16142 15783 -376 296 -1855 C ATOM 2673 O SER A 382 56.931 -9.490 23.250 1.00139.83 O ANISOU 2673 O SER A 382 21033 16198 15899 -474 257 -1736 O ATOM 2674 CB SER A 382 58.115 -9.621 20.519 1.00132.86 C ANISOU 2674 CB SER A 382 19634 15924 14924 -269 355 -1882 C ATOM 2675 OG SER A 382 57.358 -9.286 19.365 1.00128.01 O ANISOU 2675 OG SER A 382 18938 15455 14243 -300 474 -1902 O ATOM 2676 N GLN A 383 55.213 -10.601 22.298 1.00139.62 N ANISOU 2676 N GLN A 383 21099 16082 15870 -409 346 -1888 N ATOM 2677 CA GLN A 383 54.246 -10.114 23.278 1.00139.74 C ANISOU 2677 CA GLN A 383 21315 15896 15884 -558 375 -1788 C ATOM 2678 C GLN A 383 54.637 -10.570 24.678 1.00135.50 C ANISOU 2678 C GLN A 383 20944 15153 15386 -569 256 -1753 C ATOM 2679 O GLN A 383 54.854 -11.760 24.936 1.00140.23 O ANISOU 2679 O GLN A 383 21606 15639 16034 -473 152 -1832 O ATOM 2680 CB GLN A 383 52.835 -10.600 22.938 1.00144.39 C ANISOU 2680 CB GLN A 383 22004 16385 16473 -580 442 -1834 C ATOM 2681 CG GLN A 383 51.972 -10.933 24.164 1.00151.40 C ANISOU 2681 CG GLN A 383 23124 17023 17376 -667 416 -1782 C ATOM 2682 CD GLN A 383 51.990 -12.414 24.528 1.00157.01 C ANISOU 2682 CD GLN A 383 23944 17570 18142 -585 292 -1858 C ATOM 2683 OE1 GLN A 383 51.804 -13.281 23.662 1.00157.99 O ANISOU 2683 OE1 GLN A 383 24023 17713 18294 -484 266 -1966 O ATOM 2684 NE2 GLN A 383 52.217 -12.711 25.820 1.00158.69 N ANISOU 2684 NE2 GLN A 383 24311 17613 18370 -631 198 -1798 N ATOM 2685 N MET A 384 54.740 -9.617 25.587 1.00126.32 N ANISOU 2685 N MET A 384 19858 13936 14202 -686 255 -1636 N ATOM 2686 CA MET A 384 55.235 -9.921 26.903 1.00106.22 C ANISOU 2686 CA MET A 384 17459 11221 11678 -705 138 -1592 C ATOM 2687 C MET A 384 54.505 -9.036 27.891 1.00 98.64 C ANISOU 2687 C MET A 384 16665 10146 10670 -851 182 -1490 C ATOM 2688 O MET A 384 53.546 -8.323 27.563 1.00 95.26 O ANISOU 2688 O MET A 384 16243 9750 10203 -921 296 -1468 O ATOM 2689 CB MET A 384 56.754 -9.731 26.969 1.00 93.45 C ANISOU 2689 CB MET A 384 15709 9709 10088 -647 40 -1572 C ATOM 2690 CG MET A 384 57.440 -10.607 27.965 1.00 88.24 C ANISOU 2690 CG MET A 384 15157 8890 9480 -596 -115 -1584 C ATOM 2691 SD MET A 384 58.906 -9.707 28.484 1.00 87.81 S ANISOU 2691 SD MET A 384 15007 8922 9435 -627 -207 -1481 S ATOM 2692 CE MET A 384 60.181 -10.522 27.540 1.00 90.20 C ANISOU 2692 CE MET A 384 15056 9421 9797 -432 -277 -1593 C ATOM 2693 N THR A 385 54.990 -9.086 29.114 1.00 88.16 N ANISOU 2693 N THR A 385 15470 8686 9341 -886 81 -1435 N ATOM 2694 CA THR A 385 54.307 -8.445 30.210 1.00 77.81 C ANISOU 2694 CA THR A 385 14342 7252 7969 -1004 107 -1359 C ATOM 2695 C THR A 385 55.386 -8.107 31.227 1.00 76.22 C ANISOU 2695 C THR A 385 14204 6989 7768 -1029 -21 -1291 C ATOM 2696 O THR A 385 56.250 -8.942 31.512 1.00 73.02 O ANISOU 2696 O THR A 385 13796 6534 7412 -966 -143 -1308 O ATOM 2697 CB THR A 385 53.203 -9.371 30.738 1.00 73.05 C ANISOU 2697 CB THR A 385 13905 6507 7345 -1034 131 -1379 C ATOM 2698 OG1 THR A 385 52.041 -9.257 29.893 1.00 70.32 O ANISOU 2698 OG1 THR A 385 13510 6224 6985 -1047 267 -1414 O ATOM 2699 CG2 THR A 385 52.838 -9.023 32.149 1.00 76.07 C ANISOU 2699 CG2 THR A 385 14487 6764 7654 -1135 116 -1305 C ATOM 2700 N SER A 386 55.376 -6.858 31.691 1.00 73.50 N ANISOU 2700 N SER A 386 13904 6649 7375 -1114 -8 -1219 N ATOM 2701 CA SER A 386 56.454 -6.257 32.459 1.00 64.04 C ANISOU 2701 CA SER A 386 12735 5418 6178 -1147 -133 -1145 C ATOM 2702 C SER A 386 56.459 -6.775 33.881 1.00 64.59 C ANISOU 2702 C SER A 386 13026 5304 6212 -1182 -222 -1119 C ATOM 2703 O SER A 386 55.542 -7.464 34.313 1.00 64.51 O ANISOU 2703 O SER A 386 13147 5202 6162 -1200 -176 -1145 O ATOM 2704 CB SER A 386 56.279 -4.755 32.463 1.00 63.57 C ANISOU 2704 CB SER A 386 12675 5400 6078 -1227 -105 -1084 C ATOM 2705 OG SER A 386 54.903 -4.491 32.604 1.00 62.85 O ANISOU 2705 OG SER A 386 12693 5262 5926 -1264 15 -1114 O ATOM 2706 N PHE A 387 57.496 -6.423 34.639 1.00 65.28 N ANISOU 2706 N PHE A 387 13154 5342 6307 -1206 -358 -1056 N ATOM 2707 CA PHE A 387 57.425 -6.774 36.051 1.00 65.84 C ANISOU 2707 CA PHE A 387 13455 5241 6322 -1258 -441 -1022 C ATOM 2708 C PHE A 387 56.388 -5.933 36.765 1.00 65.41 C ANISOU 2708 C PHE A 387 13566 5137 6151 -1341 -357 -1006 C ATOM 2709 O PHE A 387 55.709 -6.420 37.672 1.00 78.20 O ANISOU 2709 O PHE A 387 15364 6659 7691 -1384 -342 -1005 O ATOM 2710 CB PHE A 387 58.755 -6.610 36.766 1.00 66.77 C ANISOU 2710 CB PHE A 387 13595 5303 6473 -1267 -619 -957 C ATOM 2711 CG PHE A 387 58.647 -6.854 38.247 1.00 67.41 C ANISOU 2711 CG PHE A 387 13925 5211 6476 -1335 -706 -915 C ATOM 2712 CD1 PHE A 387 58.593 -5.807 39.135 1.00 67.52 C ANISOU 2712 CD1 PHE A 387 14083 5170 6401 -1413 -736 -865 C ATOM 2713 CD2 PHE A 387 58.556 -8.138 38.745 1.00 69.12 C ANISOU 2713 CD2 PHE A 387 14241 5320 6702 -1324 -767 -926 C ATOM 2714 CE1 PHE A 387 58.478 -6.034 40.482 1.00 68.24 C ANISOU 2714 CE1 PHE A 387 14403 5125 6401 -1474 -810 -832 C ATOM 2715 CE2 PHE A 387 58.442 -8.365 40.100 1.00 68.76 C ANISOU 2715 CE2 PHE A 387 14424 5132 6570 -1403 -849 -874 C ATOM 2716 CZ PHE A 387 58.403 -7.310 40.965 1.00 68.86 C ANISOU 2716 CZ PHE A 387 14569 5113 6479 -1477 -861 -829 C ATOM 2717 N ALA A 388 56.274 -4.663 36.387 1.00 64.92 N ANISOU 2717 N ALA A 388 13447 5146 6073 -1365 -314 -993 N ATOM 2718 CA ALA A 388 55.319 -3.783 37.041 1.00 64.71 C ANISOU 2718 CA ALA A 388 13570 5075 5940 -1418 -248 -1000 C ATOM 2719 C ALA A 388 53.886 -4.238 36.800 1.00 64.16 C ANISOU 2719 C ALA A 388 13526 5031 5820 -1414 -81 -1060 C ATOM 2720 O ALA A 388 53.049 -4.156 37.702 1.00 70.24 O ANISOU 2720 O ALA A 388 14457 5750 6481 -1451 -29 -1071 O ATOM 2721 CB ALA A 388 55.522 -2.356 36.558 1.00 64.43 C ANISOU 2721 CB ALA A 388 13458 5099 5923 -1436 -267 -977 C ATOM 2722 N GLU A 389 53.582 -4.733 35.600 1.00 63.98 N ANISOU 2722 N GLU A 389 13341 5100 5870 -1370 4 -1098 N ATOM 2723 CA GLU A 389 52.245 -5.260 35.341 1.00 63.11 C ANISOU 2723 CA GLU A 389 13248 5008 5724 -1373 148 -1144 C ATOM 2724 C GLU A 389 51.984 -6.503 36.186 1.00 63.79 C ANISOU 2724 C GLU A 389 13469 4998 5769 -1400 119 -1130 C ATOM 2725 O GLU A 389 50.917 -6.657 36.787 1.00 63.96 O ANISOU 2725 O GLU A 389 13602 5001 5697 -1450 203 -1129 O ATOM 2726 CB GLU A 389 52.085 -5.567 33.845 1.00 62.43 C ANISOU 2726 CB GLU A 389 12963 5032 5726 -1319 219 -1187 C ATOM 2727 CG GLU A 389 50.646 -5.899 33.422 1.00 61.92 C ANISOU 2727 CG GLU A 389 12896 4996 5635 -1329 367 -1229 C ATOM 2728 CD GLU A 389 50.398 -5.843 31.915 1.00 69.25 C ANISOU 2728 CD GLU A 389 13636 6041 6634 -1285 442 -1271 C ATOM 2729 OE1 GLU A 389 51.363 -5.947 31.110 1.00 73.10 O ANISOU 2729 OE1 GLU A 389 13982 6602 7190 -1233 385 -1278 O ATOM 2730 OE2 GLU A 389 49.215 -5.689 31.541 1.00 64.94 O ANISOU 2730 OE2 GLU A 389 13080 5527 6067 -1302 562 -1296 O ATOM 2731 N TYR A 390 52.947 -7.410 36.231 1.00 64.35 N ANISOU 2731 N TYR A 390 13525 5014 5909 -1369 -8 -1116 N ATOM 2732 CA TYR A 390 52.768 -8.604 37.038 1.00 65.17 C ANISOU 2732 CA TYR A 390 13767 5008 5985 -1406 -73 -1089 C ATOM 2733 C TYR A 390 52.510 -8.235 38.482 1.00 65.82 C ANISOU 2733 C TYR A 390 14052 5022 5933 -1494 -91 -1034 C ATOM 2734 O TYR A 390 51.596 -8.770 39.121 1.00 69.03 O ANISOU 2734 O TYR A 390 14576 5403 6250 -1563 -41 -1009 O ATOM 2735 CB TYR A 390 53.999 -9.497 36.926 1.00 79.03 C ANISOU 2735 CB TYR A 390 15479 6701 7847 -1345 -240 -1088 C ATOM 2736 CG TYR A 390 54.010 -10.443 35.730 1.00 65.75 C ANISOU 2736 CG TYR A 390 13650 5056 6274 -1254 -240 -1157 C ATOM 2737 CD1 TYR A 390 52.910 -11.223 35.413 1.00 65.65 C ANISOU 2737 CD1 TYR A 390 13664 5025 6256 -1274 -171 -1180 C ATOM 2738 CD2 TYR A 390 55.138 -10.567 34.948 1.00 65.94 C ANISOU 2738 CD2 TYR A 390 13510 5142 6403 -1148 -317 -1201 C ATOM 2739 CE1 TYR A 390 52.939 -12.080 34.346 1.00 65.71 C ANISOU 2739 CE1 TYR A 390 13555 5052 6359 -1183 -191 -1253 C ATOM 2740 CE2 TYR A 390 55.174 -11.417 33.885 1.00 66.27 C ANISOU 2740 CE2 TYR A 390 13423 5226 6528 -1047 -322 -1283 C ATOM 2741 CZ TYR A 390 54.080 -12.178 33.577 1.00 66.17 C ANISOU 2741 CZ TYR A 390 13457 5173 6511 -1061 -266 -1315 C ATOM 2742 OH TYR A 390 54.145 -13.041 32.493 1.00 67.64 O ANISOU 2742 OH TYR A 390 13525 5392 6782 -948 -290 -1410 O ATOM 2743 N TRP A 391 53.283 -7.286 38.999 1.00 65.99 N ANISOU 2743 N TRP A 391 14114 5028 5930 -1497 -162 -1013 N ATOM 2744 CA TRP A 391 53.166 -6.926 40.402 1.00 66.80 C ANISOU 2744 CA TRP A 391 14419 5066 5895 -1568 -200 -972 C ATOM 2745 C TRP A 391 51.870 -6.179 40.675 1.00 66.61 C ANISOU 2745 C TRP A 391 14454 5114 5741 -1596 -38 -1006 C ATOM 2746 O TRP A 391 51.245 -6.387 41.717 1.00 72.25 O ANISOU 2746 O TRP A 391 15322 5814 6314 -1660 -8 -984 O ATOM 2747 CB TRP A 391 54.377 -6.106 40.822 1.00 67.12 C ANISOU 2747 CB TRP A 391 14487 5061 5955 -1559 -342 -944 C ATOM 2748 CG TRP A 391 54.416 -5.834 42.264 1.00 68.12 C ANISOU 2748 CG TRP A 391 14830 5108 5944 -1624 -410 -906 C ATOM 2749 CD1 TRP A 391 54.003 -4.706 42.893 1.00 68.34 C ANISOU 2749 CD1 TRP A 391 14965 5150 5850 -1639 -373 -930 C ATOM 2750 CD2 TRP A 391 54.895 -6.709 43.284 1.00 69.22 C ANISOU 2750 CD2 TRP A 391 15116 5140 6043 -1679 -541 -843 C ATOM 2751 NE1 TRP A 391 54.201 -4.814 44.239 1.00 69.51 N ANISOU 2751 NE1 TRP A 391 15317 5221 5873 -1698 -462 -891 N ATOM 2752 CE2 TRP A 391 54.747 -6.041 44.505 1.00 70.62 C ANISOU 2752 CE2 TRP A 391 15485 5286 6060 -1733 -566 -828 C ATOM 2753 CE3 TRP A 391 55.446 -7.992 43.280 1.00 69.72 C ANISOU 2753 CE3 TRP A 391 15171 5125 6193 -1684 -655 -802 C ATOM 2754 CZ2 TRP A 391 55.120 -6.609 45.710 1.00 75.17 C ANISOU 2754 CZ2 TRP A 391 16243 5767 6551 -1806 -690 -761 C ATOM 2755 CZ3 TRP A 391 55.814 -8.555 44.470 1.00 70.95 C ANISOU 2755 CZ3 TRP A 391 15507 5170 6279 -1757 -791 -733 C ATOM 2756 CH2 TRP A 391 55.647 -7.869 45.672 1.00 74.71 C ANISOU 2756 CH2 TRP A 391 16172 5628 6586 -1825 -803 -706 C ATOM 2757 N ALA A 392 51.448 -5.301 39.766 1.00 65.70 N ANISOU 2757 N ALA A 392 14213 5085 5664 -1549 63 -1061 N ATOM 2758 CA ALA A 392 50.160 -4.646 39.944 1.00 65.62 C ANISOU 2758 CA ALA A 392 14240 5147 5546 -1556 215 -1108 C ATOM 2759 C ALA A 392 49.027 -5.657 39.918 1.00 65.76 C ANISOU 2759 C ALA A 392 14259 5209 5520 -1597 334 -1100 C ATOM 2760 O ALA A 392 48.038 -5.515 40.640 1.00 66.38 O ANISOU 2760 O ALA A 392 14425 5339 5459 -1634 434 -1109 O ATOM 2761 CB ALA A 392 49.957 -3.586 38.876 1.00 64.68 C ANISOU 2761 CB ALA A 392 13978 5097 5500 -1500 275 -1160 C ATOM 2762 N LEU A 393 49.161 -6.707 39.116 1.00 65.38 N ANISOU 2762 N LEU A 393 14113 5147 5583 -1591 316 -1084 N ATOM 2763 CA LEU A 393 48.163 -7.765 39.146 1.00 65.73 C ANISOU 2763 CA LEU A 393 14172 5207 5594 -1648 389 -1057 C ATOM 2764 C LEU A 393 48.156 -8.456 40.492 1.00 67.06 C ANISOU 2764 C LEU A 393 14520 5316 5644 -1742 321 -980 C ATOM 2765 O LEU A 393 47.094 -8.765 41.037 1.00 75.16 O ANISOU 2765 O LEU A 393 15606 6400 6551 -1819 415 -946 O ATOM 2766 CB LEU A 393 48.438 -8.770 38.037 1.00 67.69 C ANISOU 2766 CB LEU A 393 14299 5428 5994 -1611 342 -1065 C ATOM 2767 CG LEU A 393 47.990 -8.302 36.660 1.00 64.11 C ANISOU 2767 CG LEU A 393 13668 5066 5623 -1546 452 -1132 C ATOM 2768 CD1 LEU A 393 48.403 -9.304 35.638 1.00 65.38 C ANISOU 2768 CD1 LEU A 393 13723 5201 5917 -1494 386 -1154 C ATOM 2769 CD2 LEU A 393 46.482 -8.185 36.657 1.00 64.06 C ANISOU 2769 CD2 LEU A 393 13660 5139 5541 -1592 613 -1136 C ATOM 2770 N LEU A 394 49.340 -8.721 41.035 1.00 67.57 N ANISOU 2770 N LEU A 394 14664 5274 5736 -1745 152 -943 N ATOM 2771 CA LEU A 394 49.416 -9.318 42.360 1.00 68.95 C ANISOU 2771 CA LEU A 394 15022 5385 5791 -1844 66 -860 C ATOM 2772 C LEU A 394 48.672 -8.463 43.369 1.00 69.62 C ANISOU 2772 C LEU A 394 15219 5560 5674 -1888 175 -866 C ATOM 2773 O LEU A 394 47.733 -8.930 44.022 1.00 73.05 O ANISOU 2773 O LEU A 394 15727 6058 5972 -1980 251 -815 O ATOM 2774 CB LEU A 394 50.869 -9.485 42.779 1.00 69.36 C ANISOU 2774 CB LEU A 394 15136 5310 5908 -1827 -137 -830 C ATOM 2775 CG LEU A 394 51.128 -9.461 44.282 1.00 70.71 C ANISOU 2775 CG LEU A 394 15514 5427 5926 -1915 -225 -761 C ATOM 2776 CD1 LEU A 394 50.401 -10.582 44.987 1.00 71.92 C ANISOU 2776 CD1 LEU A 394 15778 5568 5980 -2042 -233 -669 C ATOM 2777 CD2 LEU A 394 52.590 -9.559 44.520 1.00 73.68 C ANISOU 2777 CD2 LEU A 394 15922 5677 6395 -1885 -430 -737 C ATOM 2778 N SER A 395 49.078 -7.189 43.491 1.00 80.45 N ANISOU 2778 N SER A 395 16601 6946 7022 -1820 177 -930 N ATOM 2779 CA SER A 395 48.503 -6.291 44.487 1.00 70.14 C ANISOU 2779 CA SER A 395 15414 5714 5522 -1831 254 -963 C ATOM 2780 C SER A 395 47.012 -6.161 44.318 1.00 70.22 C ANISOU 2780 C SER A 395 15366 5876 5440 -1837 458 -1001 C ATOM 2781 O SER A 395 46.294 -5.995 45.307 1.00 73.71 O ANISOU 2781 O SER A 395 15909 6412 5686 -1879 538 -1001 O ATOM 2782 CB SER A 395 49.119 -4.913 44.385 1.00 69.70 C ANISOU 2782 CB SER A 395 15357 5632 5492 -1742 205 -1038 C ATOM 2783 OG SER A 395 50.480 -4.994 44.070 1.00 69.27 O ANISOU 2783 OG SER A 395 15275 5462 5582 -1723 34 -1003 O ATOM 2784 N MET A 396 46.523 -6.258 43.086 1.00 69.07 N ANISOU 2784 N MET A 396 15050 5769 5424 -1795 545 -1033 N ATOM 2785 CA MET A 396 45.127 -5.929 42.864 1.00 69.12 C ANISOU 2785 CA MET A 396 14984 5922 5356 -1785 736 -1080 C ATOM 2786 C MET A 396 44.178 -6.999 43.389 1.00 72.74 C ANISOU 2786 C MET A 396 15474 6462 5703 -1903 813 -993 C ATOM 2787 O MET A 396 43.129 -6.654 43.939 1.00 78.16 O ANISOU 2787 O MET A 396 16171 7297 6230 -1919 955 -1014 O ATOM 2788 CB MET A 396 44.872 -5.622 41.399 1.00 79.05 C ANISOU 2788 CB MET A 396 16058 7198 6781 -1711 798 -1137 C ATOM 2789 CG MET A 396 44.907 -4.136 41.170 1.00 85.92 C ANISOU 2789 CG MET A 396 16900 8090 7658 -1611 821 -1238 C ATOM 2790 SD MET A 396 45.047 -3.571 39.469 1.00 94.01 S ANISOU 2790 SD MET A 396 17725 9107 8885 -1532 831 -1288 S ATOM 2791 CE MET A 396 45.338 -1.784 39.740 1.00 92.86 C ANISOU 2791 CE MET A 396 17631 8942 8710 -1446 777 -1376 C ATOM 2792 N ASN A 397 44.495 -8.290 43.276 1.00 70.40 N ANISOU 2792 N ASN A 397 15190 6080 5479 -1988 714 -893 N ATOM 2793 CA ASN A 397 43.596 -9.250 43.926 1.00 77.84 C ANISOU 2793 CA ASN A 397 16181 7098 6295 -2128 762 -786 C ATOM 2794 C ASN A 397 44.148 -9.643 45.303 1.00 79.14 C ANISOU 2794 C ASN A 397 16536 7221 6314 -2226 645 -697 C ATOM 2795 O ASN A 397 44.361 -10.802 45.643 1.00 81.90 O ANISOU 2795 O ASN A 397 16955 7490 6672 -2343 525 -577 O ATOM 2796 CB ASN A 397 43.265 -10.443 43.013 1.00 83.31 C ANISOU 2796 CB ASN A 397 16781 7740 7133 -2183 730 -720 C ATOM 2797 CG ASN A 397 44.321 -11.534 42.999 1.00 88.08 C ANISOU 2797 CG ASN A 397 17455 8156 7856 -2221 510 -650 C ATOM 2798 OD1 ASN A 397 45.523 -11.266 43.062 1.00 93.42 O ANISOU 2798 OD1 ASN A 397 18173 8722 8598 -2151 385 -686 O ATOM 2799 ND2 ASN A 397 43.863 -12.789 42.963 1.00 83.89 N ANISOU 2799 ND2 ASN A 397 16939 7587 7350 -2336 448 -542 N ATOM 2800 N HIS A 398 44.312 -8.603 46.128 1.00 76.01 N ANISOU 2800 N HIS A 398 16229 6881 5771 -2178 678 -762 N ATOM 2801 CA HIS A 398 44.649 -8.795 47.533 1.00 83.89 C ANISOU 2801 CA HIS A 398 17412 7879 6581 -2270 598 -690 C ATOM 2802 C HIS A 398 43.603 -9.638 48.256 1.00 88.44 C ANISOU 2802 C HIS A 398 18024 8603 6978 -2432 680 -568 C ATOM 2803 O HIS A 398 43.937 -10.434 49.141 1.00 87.79 O ANISOU 2803 O HIS A 398 18076 8476 6804 -2566 560 -442 O ATOM 2804 CB HIS A 398 44.806 -7.440 48.219 1.00 88.29 C ANISOU 2804 CB HIS A 398 18052 8496 6999 -2173 638 -805 C ATOM 2805 CG HIS A 398 44.939 -7.529 49.713 1.00 91.46 C ANISOU 2805 CG HIS A 398 18646 8944 7161 -2263 591 -747 C ATOM 2806 ND1 HIS A 398 43.902 -7.230 50.571 1.00 93.52 N ANISOU 2806 ND1 HIS A 398 18944 9426 7163 -2294 749 -764 N ATOM 2807 CD2 HIS A 398 45.984 -7.878 50.498 1.00 90.55 C ANISOU 2807 CD2 HIS A 398 18692 8694 7020 -2326 402 -674 C ATOM 2808 CE1 HIS A 398 44.301 -7.394 51.819 1.00 94.15 C ANISOU 2808 CE1 HIS A 398 19205 9512 7055 -2378 663 -703 C ATOM 2809 NE2 HIS A 398 45.561 -7.787 51.803 1.00 93.26 N ANISOU 2809 NE2 HIS A 398 19177 9174 7084 -2403 447 -644 N ATOM 2810 N GLY A 399 42.330 -9.471 47.912 1.00 93.69 N ANISOU 2810 N GLY A 399 18563 9451 7584 -2430 876 -593 N ATOM 2811 CA GLY A 399 41.332 -10.325 48.520 1.00 97.36 C ANISOU 2811 CA GLY A 399 19034 10073 7886 -2602 948 -454 C ATOM 2812 C GLY A 399 41.453 -11.783 48.137 1.00100.09 C ANISOU 2812 C GLY A 399 19377 10286 8368 -2745 805 -296 C ATOM 2813 O GLY A 399 40.881 -12.637 48.816 1.00101.72 O ANISOU 2813 O GLY A 399 19630 10579 8439 -2928 796 -138 O ATOM 2814 N GLY A 400 42.191 -12.093 47.074 1.00105.34 N ANISOU 2814 N GLY A 400 19988 10747 9290 -2667 682 -333 N ATOM 2815 CA GLY A 400 42.115 -13.427 46.525 1.00113.55 C ANISOU 2815 CA GLY A 400 21002 11669 10472 -2771 558 -216 C ATOM 2816 C GLY A 400 40.725 -13.813 46.090 1.00119.44 C ANISOU 2816 C GLY A 400 21622 12567 11192 -2855 700 -156 C ATOM 2817 O GLY A 400 40.474 -14.994 45.828 1.00121.99 O ANISOU 2817 O GLY A 400 21944 12811 11594 -2980 590 -30 O ATOM 2818 N LYS A 401 39.803 -12.852 46.054 1.00123.87 N ANISOU 2818 N LYS A 401 22081 13343 11641 -2792 930 -240 N ATOM 2819 CA LYS A 401 38.484 -13.050 45.475 1.00126.01 C ANISOU 2819 CA LYS A 401 22198 13766 11914 -2841 1080 -207 C ATOM 2820 C LYS A 401 38.610 -12.779 43.980 1.00124.73 C ANISOU 2820 C LYS A 401 21902 13496 11995 -2692 1089 -330 C ATOM 2821 O LYS A 401 38.805 -11.633 43.550 1.00118.48 O ANISOU 2821 O LYS A 401 21050 12726 11240 -2524 1178 -487 O ATOM 2822 CB LYS A 401 37.442 -12.141 46.126 1.00125.39 C ANISOU 2822 CB LYS A 401 22060 13977 11606 -2826 1316 -253 C ATOM 2823 CG LYS A 401 35.985 -12.585 45.872 1.00123.09 C ANISOU 2823 CG LYS A 401 21619 13885 11264 -2940 1460 -158 C ATOM 2824 CD LYS A 401 35.058 -11.380 45.737 1.00119.26 C ANISOU 2824 CD LYS A 401 20994 13630 10689 -2804 1702 -303 C ATOM 2825 CE LYS A 401 34.950 -10.970 44.268 1.00113.57 C ANISOU 2825 CE LYS A 401 20132 12808 10209 -2660 1731 -424 C ATOM 2826 NZ LYS A 401 34.149 -11.932 43.465 1.00111.33 N ANISOU 2826 NZ LYS A 401 19732 12524 10042 -2777 1726 -306 N ATOM 2827 N PHE A 402 38.511 -13.839 43.199 1.00128.74 N ANISOU 2827 N PHE A 402 22368 13883 12662 -2756 981 -254 N ATOM 2828 CA PHE A 402 38.549 -13.758 41.753 1.00128.22 C ANISOU 2828 CA PHE A 402 22176 13730 12812 -2635 983 -355 C ATOM 2829 C PHE A 402 37.559 -14.811 41.254 1.00131.36 C ANISOU 2829 C PHE A 402 22504 14140 13265 -2768 967 -236 C ATOM 2830 O PHE A 402 37.926 -15.943 40.927 1.00134.10 O ANISOU 2830 O PHE A 402 22904 14312 13736 -2831 774 -162 O ATOM 2831 CB PHE A 402 39.959 -13.984 41.216 1.00128.80 C ANISOU 2831 CB PHE A 402 22301 13576 13062 -2529 794 -423 C ATOM 2832 CG PHE A 402 40.017 -14.161 39.725 1.00127.64 C ANISOU 2832 CG PHE A 402 22029 13346 13124 -2426 771 -506 C ATOM 2833 CD1 PHE A 402 39.231 -13.385 38.890 1.00127.75 C ANISOU 2833 CD1 PHE A 402 21893 13479 13166 -2350 945 -592 C ATOM 2834 CD2 PHE A 402 40.831 -15.128 39.160 1.00123.58 C ANISOU 2834 CD2 PHE A 402 21546 12637 12773 -2402 568 -503 C ATOM 2835 CE1 PHE A 402 39.278 -13.564 37.530 1.00125.21 C ANISOU 2835 CE1 PHE A 402 21464 13090 13020 -2265 920 -663 C ATOM 2836 CE2 PHE A 402 40.877 -15.305 37.805 1.00119.65 C ANISOU 2836 CE2 PHE A 402 20935 12082 12444 -2301 549 -590 C ATOM 2837 CZ PHE A 402 40.101 -14.527 36.991 1.00121.06 C ANISOU 2837 CZ PHE A 402 20972 12387 12638 -2240 728 -664 C ATOM 2838 N ASP A 403 36.281 -14.444 41.237 1.00128.08 N ANISOU 2838 N ASP A 403 21973 13935 12756 -2811 1159 -216 N ATOM 2839 CA ASP A 403 35.242 -15.292 40.657 1.00124.66 C ANISOU 2839 CA ASP A 403 21448 13532 12385 -2932 1160 -106 C ATOM 2840 C ASP A 403 35.263 -15.093 39.146 1.00121.93 C ANISOU 2840 C ASP A 403 20985 13092 12251 -2790 1164 -233 C ATOM 2841 O ASP A 403 34.709 -14.117 38.635 1.00121.66 O ANISOU 2841 O ASP A 403 20824 13182 12219 -2686 1339 -340 O ATOM 2842 CB ASP A 403 33.877 -14.941 41.231 1.00126.57 C ANISOU 2842 CB ASP A 403 21591 14059 12441 -3029 1369 -35 C ATOM 2843 CG ASP A 403 32.779 -15.794 40.653 1.00128.67 C ANISOU 2843 CG ASP A 403 21752 14365 12770 -3170 1364 95 C ATOM 2844 OD1 ASP A 403 33.105 -16.854 40.084 1.00129.59 O ANISOU 2844 OD1 ASP A 403 21921 14273 13044 -3232 1162 164 O ATOM 2845 OD2 ASP A 403 31.599 -15.391 40.734 1.00129.74 O ANISOU 2845 OD2 ASP A 403 21750 14737 12808 -3207 1554 120 O ATOM 2846 N PHE A 404 35.891 -16.023 38.414 1.00114.00 N ANISOU 2846 N PHE A 404 20024 11869 11423 -2782 964 -226 N ATOM 2847 CA PHE A 404 36.104 -15.821 36.979 1.00102.50 C ANISOU 2847 CA PHE A 404 18467 10326 10153 -2631 957 -361 C ATOM 2848 C PHE A 404 34.833 -15.931 36.157 1.00 95.16 C ANISOU 2848 C PHE A 404 17398 9486 9272 -2675 1055 -335 C ATOM 2849 O PHE A 404 34.913 -15.882 34.928 1.00 92.63 O ANISOU 2849 O PHE A 404 17000 9095 9100 -2570 1038 -433 O ATOM 2850 CB PHE A 404 37.147 -16.810 36.437 1.00 94.75 C ANISOU 2850 CB PHE A 404 17566 9101 9332 -2589 712 -380 C ATOM 2851 CG PHE A 404 36.613 -18.203 36.158 1.00 89.03 C ANISOU 2851 CG PHE A 404 16875 8264 8687 -2726 547 -256 C ATOM 2852 CD1 PHE A 404 36.165 -18.558 34.911 1.00 84.60 C ANISOU 2852 CD1 PHE A 404 16225 7652 8267 -2682 521 -304 C ATOM 2853 CD2 PHE A 404 36.603 -19.167 37.143 1.00 91.45 C ANISOU 2853 CD2 PHE A 404 17314 8504 8930 -2902 394 -87 C ATOM 2854 CE1 PHE A 404 35.690 -19.842 34.671 1.00 85.94 C ANISOU 2854 CE1 PHE A 404 16441 7698 8515 -2809 341 -190 C ATOM 2855 CE2 PHE A 404 36.133 -20.452 36.890 1.00 89.32 C ANISOU 2855 CE2 PHE A 404 17086 8109 8743 -3038 207 38 C ATOM 2856 CZ PHE A 404 35.685 -20.786 35.657 1.00 85.02 C ANISOU 2856 CZ PHE A 404 16458 7504 8344 -2987 177 -18 C ATOM 2857 N HIS A 405 33.672 -16.083 36.769 1.00 94.50 N ANISOU 2857 N HIS A 405 17275 9566 9065 -2828 1155 -205 N ATOM 2858 CA HIS A 405 32.427 -16.125 36.023 1.00 93.49 C ANISOU 2858 CA HIS A 405 17001 9539 8983 -2872 1254 -174 C ATOM 2859 C HIS A 405 31.862 -14.735 35.762 1.00 91.55 C ANISOU 2859 C HIS A 405 16614 9478 8692 -2746 1490 -300 C ATOM 2860 O HIS A 405 30.765 -14.599 35.202 1.00 92.07 O ANISOU 2860 O HIS A 405 16542 9654 8786 -2771 1595 -284 O ATOM 2861 CB HIS A 405 31.423 -17.005 36.756 1.00 98.45 C ANISOU 2861 CB HIS A 405 17630 10267 9507 -3110 1237 44 C ATOM 2862 CG HIS A 405 31.845 -18.433 36.821 1.00100.31 C ANISOU 2862 CG HIS A 405 17999 10290 9822 -3244 970 176 C ATOM 2863 ND1 HIS A 405 30.979 -19.475 36.581 1.00103.59 N ANISOU 2863 ND1 HIS A 405 18393 10680 10287 -3425 865 342 N ATOM 2864 CD2 HIS A 405 33.055 -18.993 37.058 1.00101.47 C ANISOU 2864 CD2 HIS A 405 18303 10226 10024 -3215 763 161 C ATOM 2865 CE1 HIS A 405 31.634 -20.619 36.683 1.00105.71 C ANISOU 2865 CE1 HIS A 405 18811 10717 10635 -3502 594 422 C ATOM 2866 NE2 HIS A 405 32.895 -20.354 36.972 1.00104.08 N ANISOU 2866 NE2 HIS A 405 18711 10398 10435 -3370 532 310 N ATOM 2867 N HIS A 406 32.595 -13.701 36.148 1.00 86.50 N ANISOU 2867 N HIS A 406 16010 8863 7993 -2611 1555 -424 N ATOM 2868 CA HIS A 406 32.310 -12.352 35.693 1.00 83.73 C ANISOU 2868 CA HIS A 406 15547 8620 7648 -2458 1719 -573 C ATOM 2869 C HIS A 406 33.593 -11.679 35.215 1.00 74.21 C ANISOU 2869 C HIS A 406 14388 7277 6531 -2292 1651 -718 C ATOM 2870 O HIS A 406 33.639 -10.455 35.094 1.00 73.79 O ANISOU 2870 O HIS A 406 14284 7289 6462 -2168 1751 -837 O ATOM 2871 CB HIS A 406 31.618 -11.550 36.802 1.00 91.31 C ANISOU 2871 CB HIS A 406 16480 9810 8406 -2467 1896 -574 C ATOM 2872 CG HIS A 406 30.527 -12.308 37.509 1.00 97.71 C ANISOU 2872 CG HIS A 406 17252 10783 9089 -2656 1952 -402 C ATOM 2873 ND1 HIS A 406 29.212 -12.299 37.091 1.00 97.99 N ANISOU 2873 ND1 HIS A 406 17124 10976 9133 -2704 2074 -360 N ATOM 2874 CD2 HIS A 406 30.563 -13.096 38.613 1.00 99.59 C ANISOU 2874 CD2 HIS A 406 17590 11064 9186 -2820 1896 -249 C ATOM 2875 CE1 HIS A 406 28.487 -13.048 37.906 1.00 99.67 C ANISOU 2875 CE1 HIS A 406 17326 11333 9211 -2894 2096 -183 C ATOM 2876 NE2 HIS A 406 29.283 -13.544 38.836 1.00100.16 N ANISOU 2876 NE2 HIS A 406 17551 11329 9177 -2972 1987 -110 N ATOM 2877 N ALA A 407 34.625 -12.475 34.917 1.00 71.30 N ANISOU 2877 N ALA A 407 14108 6721 6260 -2291 1470 -706 N ATOM 2878 CA ALA A 407 35.920 -11.961 34.497 1.00 66.79 C ANISOU 2878 CA ALA A 407 13570 6037 5769 -2150 1393 -822 C ATOM 2879 C ALA A 407 35.894 -11.343 33.109 1.00 70.09 C ANISOU 2879 C ALA A 407 13861 6452 6320 -2031 1435 -934 C ATOM 2880 O ALA A 407 36.787 -10.558 32.785 1.00 73.27 O ANISOU 2880 O ALA A 407 14256 6822 6761 -1916 1417 -1030 O ATOM 2881 CB ALA A 407 36.961 -13.073 34.541 1.00 67.02 C ANISOU 2881 CB ALA A 407 13709 5886 5868 -2175 1186 -781 C ATOM 2882 N ASN A 408 34.913 -11.672 32.275 1.00 69.88 N ANISOU 2882 N ASN A 408 13733 6459 6360 -2066 1479 -914 N ATOM 2883 CA ASN A 408 34.779 -11.055 30.959 1.00 67.07 C ANISOU 2883 CA ASN A 408 13254 6114 6116 -1967 1522 -1012 C ATOM 2884 C ASN A 408 33.712 -9.978 31.012 1.00 71.28 C ANISOU 2884 C ASN A 408 13685 6801 6597 -1948 1696 -1042 C ATOM 2885 O ASN A 408 32.614 -10.204 31.532 1.00 69.80 O ANISOU 2885 O ASN A 408 13466 6719 6337 -2039 1782 -966 O ATOM 2886 CB ASN A 408 34.453 -12.090 29.892 1.00 63.83 C ANISOU 2886 CB ASN A 408 12802 5626 5825 -2001 1438 -987 C ATOM 2887 CG ASN A 408 35.567 -13.059 29.714 1.00 65.31 C ANISOU 2887 CG ASN A 408 13080 5657 6078 -1978 1254 -995 C ATOM 2888 OD1 ASN A 408 36.664 -12.839 30.200 1.00 67.56 O ANISOU 2888 OD1 ASN A 408 13434 5898 6338 -1922 1198 -1029 O ATOM 2889 ND2 ASN A 408 35.298 -14.152 29.047 1.00 67.79 N ANISOU 2889 ND2 ASN A 408 13397 5883 6479 -2017 1145 -966 N ATOM 2890 N LYS A 409 34.048 -8.803 30.494 1.00 70.01 N ANISOU 2890 N LYS A 409 13469 6658 6472 -1832 1736 -1148 N ATOM 2891 CA LYS A 409 33.215 -7.634 30.650 1.00 66.32 C ANISOU 2891 CA LYS A 409 12925 6315 5959 -1785 1872 -1200 C ATOM 2892 C LYS A 409 33.168 -6.885 29.333 1.00 64.79 C ANISOU 2892 C LYS A 409 12622 6110 5886 -1703 1877 -1280 C ATOM 2893 O LYS A 409 34.077 -6.977 28.504 1.00 60.79 O ANISOU 2893 O LYS A 409 12115 5517 5464 -1662 1784 -1310 O ATOM 2894 CB LYS A 409 33.742 -6.732 31.760 1.00 67.66 C ANISOU 2894 CB LYS A 409 13181 6515 6014 -1728 1893 -1248 C ATOM 2895 CG LYS A 409 33.824 -7.403 33.126 1.00 69.67 C ANISOU 2895 CG LYS A 409 13551 6794 6126 -1815 1887 -1167 C ATOM 2896 CD LYS A 409 35.053 -6.949 33.902 1.00 70.23 C ANISOU 2896 CD LYS A 409 13751 6796 6137 -1764 1808 -1205 C ATOM 2897 CE LYS A 409 35.031 -7.484 35.321 1.00 74.17 C ANISOU 2897 CE LYS A 409 14368 7340 6474 -1852 1811 -1126 C ATOM 2898 NZ LYS A 409 36.325 -7.289 36.031 1.00 76.20 N ANISOU 2898 NZ LYS A 409 14764 7500 6687 -1821 1701 -1143 N ATOM 2899 N ILE A 410 32.037 -6.229 29.125 1.00 67.25 N ANISOU 2899 N ILE A 410 12830 6520 6200 -1686 1986 -1305 N ATOM 2900 CA ILE A 410 31.875 -5.145 28.171 1.00 67.80 C ANISOU 2900 CA ILE A 410 12806 6597 6356 -1601 2001 -1386 C ATOM 2901 C ILE A 410 31.711 -3.910 29.019 1.00 69.19 C ANISOU 2901 C ILE A 410 13001 6837 6452 -1522 2060 -1458 C ATOM 2902 O ILE A 410 30.944 -3.934 29.987 1.00 71.99 O ANISOU 2902 O ILE A 410 13358 7295 6699 -1538 2154 -1447 O ATOM 2903 CB ILE A 410 30.640 -5.322 27.264 1.00 61.19 C ANISOU 2903 CB ILE A 410 11836 5813 5598 -1634 2061 -1367 C ATOM 2904 CG1 ILE A 410 30.708 -6.595 26.426 1.00 60.85 C ANISOU 2904 CG1 ILE A 410 11787 5700 5632 -1709 1988 -1303 C ATOM 2905 CG2 ILE A 410 30.393 -4.082 26.417 1.00 60.53 C ANISOU 2905 CG2 ILE A 410 11663 5742 5595 -1549 2071 -1448 C ATOM 2906 CD1 ILE A 410 29.396 -6.898 25.787 1.00 61.21 C ANISOU 2906 CD1 ILE A 410 11719 5802 5737 -1764 2043 -1263 C ATOM 2907 N ASN A 411 32.441 -2.853 28.685 1.00 69.15 N ANISOU 2907 N ASN A 411 13009 6775 6489 -1439 1995 -1530 N ATOM 2908 CA ASN A 411 32.279 -1.555 29.329 1.00 69.82 C ANISOU 2908 CA ASN A 411 13115 6891 6521 -1345 2016 -1617 C ATOM 2909 C ASN A 411 32.617 -1.598 30.814 1.00 74.37 C ANISOU 2909 C ASN A 411 13817 7493 6946 -1338 2032 -1623 C ATOM 2910 O ASN A 411 32.158 -0.746 31.579 1.00 75.51 O ANISOU 2910 O ASN A 411 13979 7702 7008 -1261 2081 -1701 O ATOM 2911 CB ASN A 411 30.857 -1.020 29.144 1.00 64.61 C ANISOU 2911 CB ASN A 411 12337 6333 5878 -1304 2119 -1664 C ATOM 2912 CG ASN A 411 30.738 -0.147 27.953 1.00 65.87 C ANISOU 2912 CG ASN A 411 12411 6444 6172 -1255 2064 -1709 C ATOM 2913 OD1 ASN A 411 31.682 -0.025 27.170 1.00 67.79 O ANISOU 2913 OD1 ASN A 411 12670 6596 6490 -1268 1958 -1692 O ATOM 2914 ND2 ASN A 411 29.585 0.484 27.795 1.00 67.63 N ANISOU 2914 ND2 ASN A 411 12536 6737 6424 -1200 2130 -1764 N ATOM 2915 N GLY A 412 33.391 -2.590 31.260 1.00 77.03 N ANISOU 2915 N GLY A 412 14245 7783 7238 -1412 1984 -1549 N ATOM 2916 CA GLY A 412 33.782 -2.682 32.644 1.00 78.60 C ANISOU 2916 CA GLY A 412 14574 8001 7291 -1420 1984 -1542 C ATOM 2917 C GLY A 412 32.964 -3.640 33.498 1.00 81.07 C ANISOU 2917 C GLY A 412 14895 8426 7483 -1512 2082 -1465 C ATOM 2918 O GLY A 412 33.519 -4.237 34.423 1.00 84.60 O ANISOU 2918 O GLY A 412 15458 8857 7831 -1570 2045 -1408 O ATOM 2919 N GLN A 413 31.668 -3.804 33.233 1.00 80.05 N ANISOU 2919 N GLN A 413 14642 8417 7356 -1537 2197 -1449 N ATOM 2920 CA GLN A 413 30.858 -4.720 34.024 1.00 82.72 C ANISOU 2920 CA GLN A 413 14970 8885 7573 -1647 2286 -1352 C ATOM 2921 C GLN A 413 30.376 -5.876 33.155 1.00 77.21 C ANISOU 2921 C GLN A 413 14194 8161 6980 -1764 2269 -1241 C ATOM 2922 O GLN A 413 30.061 -5.702 31.972 1.00 68.48 O ANISOU 2922 O GLN A 413 12988 7017 6015 -1734 2262 -1269 O ATOM 2923 CB GLN A 413 29.663 -3.995 34.696 1.00 95.14 C ANISOU 2923 CB GLN A 413 16460 10664 9024 -1589 2441 -1414 C ATOM 2924 CG GLN A 413 28.454 -4.878 35.185 1.00105.93 C ANISOU 2924 CG GLN A 413 17736 12225 10288 -1715 2564 -1298 C ATOM 2925 CD GLN A 413 28.659 -5.640 36.531 1.00108.51 C ANISOU 2925 CD GLN A 413 18172 12636 10421 -1830 2575 -1194 C ATOM 2926 OE1 GLN A 413 29.778 -5.754 37.043 1.00108.58 O ANISOU 2926 OE1 GLN A 413 18338 12526 10390 -1835 2473 -1190 O ATOM 2927 NE2 GLN A 413 27.556 -6.165 37.090 1.00108.76 N ANISOU 2927 NE2 GLN A 413 18112 12882 10330 -1934 2696 -1098 N ATOM 2928 N ALA A 414 30.348 -7.060 33.765 1.00 81.16 N ANISOU 2928 N ALA A 414 14754 8675 7410 -1902 2245 -1112 N ATOM 2929 CA ALA A 414 29.863 -8.282 33.151 1.00 78.53 C ANISOU 2929 CA ALA A 414 14372 8308 7157 -2031 2204 -991 C ATOM 2930 C ALA A 414 28.340 -8.287 33.090 1.00 68.69 C ANISOU 2930 C ALA A 414 12973 7244 5883 -2084 2340 -944 C ATOM 2931 O ALA A 414 27.661 -7.359 33.521 1.00 69.45 O ANISOU 2931 O ALA A 414 12991 7500 5896 -2008 2473 -1016 O ATOM 2932 CB ALA A 414 30.363 -9.495 33.926 1.00 73.21 C ANISOU 2932 CB ALA A 414 13827 7575 6415 -2167 2104 -860 C ATOM 2933 N PHE A 415 27.797 -9.361 32.544 1.00 77.12 N ANISOU 2933 N PHE A 415 13993 8284 7025 -2212 2295 -824 N ATOM 2934 CA PHE A 415 26.380 -9.369 32.245 1.00 79.63 C ANISOU 2934 CA PHE A 415 14144 8757 7353 -2264 2405 -775 C ATOM 2935 C PHE A 415 25.559 -9.457 33.514 1.00 86.50 C ANISOU 2935 C PHE A 415 14972 9863 8030 -2351 2533 -689 C ATOM 2936 O PHE A 415 25.877 -10.203 34.447 1.00 93.18 O ANISOU 2936 O PHE A 415 15920 10724 8759 -2471 2489 -578 O ATOM 2937 CB PHE A 415 26.024 -10.519 31.310 1.00 77.16 C ANISOU 2937 CB PHE A 415 13801 8342 7175 -2387 2300 -662 C ATOM 2938 CG PHE A 415 24.639 -10.406 30.724 1.00 79.35 C ANISOU 2938 CG PHE A 415 13896 8749 7506 -2423 2395 -626 C ATOM 2939 CD1 PHE A 415 24.129 -9.176 30.352 1.00 82.10 C ANISOU 2939 CD1 PHE A 415 14121 9191 7881 -2282 2514 -755 C ATOM 2940 CD2 PHE A 415 23.847 -11.530 30.545 1.00 78.07 C ANISOU 2940 CD2 PHE A 415 13684 8603 7375 -2600 2346 -459 C ATOM 2941 CE1 PHE A 415 22.854 -9.070 29.809 1.00 81.28 C ANISOU 2941 CE1 PHE A 415 13842 9204 7836 -2310 2592 -724 C ATOM 2942 CE2 PHE A 415 22.581 -11.428 30.008 1.00 76.36 C ANISOU 2942 CE2 PHE A 415 13292 8507 7213 -2638 2426 -418 C ATOM 2943 CZ PHE A 415 22.084 -10.200 29.637 1.00 77.57 C ANISOU 2943 CZ PHE A 415 13317 8762 7395 -2490 2554 -553 C ATOM 2944 N ASP A 416 24.502 -8.663 33.540 1.00 90.46 N ANISOU 2944 N ASP A 416 15315 10560 8495 -2286 2689 -746 N ATOM 2945 CA ASP A 416 23.487 -8.737 34.572 1.00 98.91 C ANISOU 2945 CA ASP A 416 16287 11909 9383 -2364 2836 -666 C ATOM 2946 C ASP A 416 22.202 -8.477 33.809 1.00100.01 C ANISOU 2946 C ASP A 416 16214 12174 9613 -2351 2931 -668 C ATOM 2947 O ASP A 416 22.101 -7.476 33.095 1.00 98.65 O ANISOU 2947 O ASP A 416 15976 11962 9544 -2186 2959 -822 O ATOM 2948 CB ASP A 416 23.742 -7.691 35.674 1.00103.49 C ANISOU 2948 CB ASP A 416 16911 12628 9784 -2224 2942 -801 C ATOM 2949 CG ASP A 416 23.203 -8.109 37.040 1.00107.52 C ANISOU 2949 CG ASP A 416 17402 13401 10048 -2344 3050 -688 C ATOM 2950 OD1 ASP A 416 22.036 -8.546 37.151 1.00109.32 O ANISOU 2950 OD1 ASP A 416 17468 13845 10223 -2459 3149 -568 O ATOM 2951 OD2 ASP A 416 23.979 -8.014 38.013 1.00108.26 O ANISOU 2951 OD2 ASP A 416 17646 13492 9998 -2331 3028 -710 O ATOM 2952 N MET A 417 21.261 -9.409 33.880 1.00106.77 N ANISOU 2952 N MET A 417 16966 13157 10446 -2536 2954 -484 N ATOM 2953 CA MET A 417 20.017 -9.229 33.148 1.00115.76 C ANISOU 2953 CA MET A 417 17893 14414 11677 -2538 3034 -469 C ATOM 2954 C MET A 417 19.244 -7.997 33.611 1.00123.50 C ANISOU 2954 C MET A 417 18718 15648 12559 -2372 3226 -613 C ATOM 2955 O MET A 417 18.402 -7.498 32.856 1.00126.25 O ANISOU 2955 O MET A 417 18900 16050 13019 -2301 3280 -668 O ATOM 2956 CB MET A 417 19.160 -10.479 33.302 1.00120.85 C ANISOU 2956 CB MET A 417 18455 15169 12294 -2789 3016 -223 C ATOM 2957 CG MET A 417 19.853 -11.732 32.803 1.00122.63 C ANISOU 2957 CG MET A 417 18838 15125 12632 -2943 2796 -91 C ATOM 2958 SD MET A 417 19.951 -13.059 34.031 1.00126.39 S ANISOU 2958 SD MET A 417 19414 15673 12937 -3211 2722 162 S ATOM 2959 CE MET A 417 21.391 -12.579 34.998 1.00123.76 C ANISOU 2959 CE MET A 417 19297 15257 12470 -3089 2707 34 C ATOM 2960 N ASN A 418 19.540 -7.479 34.818 1.00127.99 N ANISOU 2960 N ASN A 418 19342 16363 12924 -2297 3317 -687 N ATOM 2961 CA ASN A 418 18.692 -6.463 35.445 1.00129.58 C ANISOU 2961 CA ASN A 418 19387 16853 12993 -2147 3504 -815 C ATOM 2962 C ASN A 418 18.709 -5.144 34.674 1.00124.65 C ANISOU 2962 C ASN A 418 18723 16127 12513 -1901 3502 -1046 C ATOM 2963 O ASN A 418 17.665 -4.494 34.523 1.00126.23 O ANISOU 2963 O ASN A 418 18728 16509 12726 -1797 3616 -1125 O ATOM 2964 CB ASN A 418 19.111 -6.235 36.913 1.00135.67 C ANISOU 2964 CB ASN A 418 20257 17788 13504 -2116 3580 -854 C ATOM 2965 CG ASN A 418 20.262 -5.217 37.081 1.00135.49 C ANISOU 2965 CG ASN A 418 20417 17579 13483 -1908 3514 -1068 C ATOM 2966 OD1 ASN A 418 21.187 -5.149 36.257 1.00133.50 O ANISOU 2966 OD1 ASN A 418 20292 17024 13408 -1874 3362 -1109 O ATOM 2967 ND2 ASN A 418 20.193 -4.418 38.158 1.00134.33 N ANISOU 2967 ND2 ASN A 418 20278 17628 13132 -1770 3624 -1203 N ATOM 2968 N LYS A 419 19.875 -4.724 34.190 1.00117.07 N ANISOU 2968 N LYS A 419 17936 14883 11661 -1807 3366 -1150 N ATOM 2969 CA LYS A 419 20.017 -3.402 33.586 1.00110.37 C ANISOU 2969 CA LYS A 419 17075 13931 10929 -1584 3341 -1360 C ATOM 2970 C LYS A 419 20.415 -3.526 32.125 1.00106.59 C ANISOU 2970 C LYS A 419 16622 13185 10692 -1606 3197 -1344 C ATOM 2971 O LYS A 419 21.574 -3.860 31.820 1.00106.79 O ANISOU 2971 O LYS A 419 16813 12988 10773 -1646 3065 -1320 O ATOM 2972 CB LYS A 419 21.037 -2.563 34.355 1.00108.03 C ANISOU 2972 CB LYS A 419 16952 13565 10530 -1437 3304 -1512 C ATOM 2973 CG LYS A 419 20.712 -1.071 34.352 1.00108.52 C ANISOU 2973 CG LYS A 419 16956 13667 10611 -1190 3336 -1740 C ATOM 2974 CD LYS A 419 21.055 -0.445 35.716 1.00109.90 C ANISOU 2974 CD LYS A 419 17230 13962 10564 -1067 3389 -1866 C ATOM 2975 CE LYS A 419 20.016 0.595 36.166 1.00109.38 C ANISOU 2975 CE LYS A 419 17012 14129 10417 -860 3513 -2049 C ATOM 2976 NZ LYS A 419 20.554 1.582 37.161 1.00107.21 N ANISOU 2976 NZ LYS A 419 16872 13870 9992 -670 3498 -2243 N ATOM 2977 N PRO A 420 19.492 -3.317 31.188 1.00 99.57 N ANISOU 2977 N PRO A 420 15567 12320 9944 -1587 3216 -1349 N ATOM 2978 CA PRO A 420 19.907 -3.031 29.815 1.00 92.73 C ANISOU 2978 CA PRO A 420 14728 11214 9291 -1552 3084 -1390 C ATOM 2979 C PRO A 420 20.855 -1.848 29.814 1.00 90.25 C ANISOU 2979 C PRO A 420 14534 10759 8998 -1378 3008 -1562 C ATOM 2980 O PRO A 420 20.620 -0.843 30.488 1.00 92.68 O ANISOU 2980 O PRO A 420 14819 11169 9226 -1221 3069 -1703 O ATOM 2981 CB PRO A 420 18.588 -2.718 29.102 1.00 92.00 C ANISOU 2981 CB PRO A 420 14421 11227 9309 -1524 3144 -1399 C ATOM 2982 CG PRO A 420 17.572 -3.475 29.858 1.00 95.89 C ANISOU 2982 CG PRO A 420 14779 11978 9676 -1642 3278 -1272 C ATOM 2983 CD PRO A 420 18.030 -3.449 31.301 1.00102.41 C ANISOU 2983 CD PRO A 420 15700 12934 10276 -1621 3353 -1296 C ATOM 2984 N MET A 421 21.954 -1.989 29.074 1.00 84.57 N ANISOU 2984 N MET A 421 13944 9809 8379 -1406 2866 -1549 N ATOM 2985 CA MET A 421 23.003 -0.983 29.130 1.00 81.77 C ANISOU 2985 CA MET A 421 13716 9316 8034 -1277 2775 -1677 C ATOM 2986 C MET A 421 22.538 0.339 28.535 1.00 80.97 C ANISOU 2986 C MET A 421 13530 9191 8042 -1122 2748 -1815 C ATOM 2987 O MET A 421 22.919 1.405 29.028 1.00 81.80 O ANISOU 2987 O MET A 421 13701 9268 8109 -980 2712 -1949 O ATOM 2988 CB MET A 421 24.255 -1.497 28.420 1.00 76.25 C ANISOU 2988 CB MET A 421 13147 8410 7416 -1352 2635 -1618 C ATOM 2989 CG MET A 421 25.457 -0.581 28.525 1.00 73.23 C ANISOU 2989 CG MET A 421 12896 7893 7036 -1252 2529 -1715 C ATOM 2990 SD MET A 421 27.033 -1.466 28.566 1.00 75.01 S ANISOU 2990 SD MET A 421 13291 7969 7241 -1346 2417 -1633 S ATOM 2991 CE MET A 421 26.728 -2.721 29.813 1.00 79.40 C ANISOU 2991 CE MET A 421 13888 8650 7632 -1464 2510 -1523 C ATOM 2992 N PHE A 422 21.697 0.304 27.507 1.00 80.81 N ANISOU 2992 N PHE A 422 13371 9175 8160 -1147 2748 -1786 N ATOM 2993 CA PHE A 422 21.248 1.554 26.914 1.00 83.66 C ANISOU 2993 CA PHE A 422 13654 9498 8636 -1006 2700 -1911 C ATOM 2994 C PHE A 422 20.014 1.313 26.061 1.00 84.43 C ANISOU 2994 C PHE A 422 13566 9663 8849 -1049 2742 -1860 C ATOM 2995 O PHE A 422 19.623 0.176 25.759 1.00 85.97 O ANISOU 2995 O PHE A 422 13707 9903 9055 -1199 2784 -1721 O ATOM 2996 CB PHE A 422 22.352 2.200 26.075 1.00 82.47 C ANISOU 2996 CB PHE A 422 13615 9126 8595 -981 2529 -1945 C ATOM 2997 CG PHE A 422 22.951 1.273 25.061 1.00 82.89 C ANISOU 2997 CG PHE A 422 13704 9067 8726 -1129 2460 -1819 C ATOM 2998 CD1 PHE A 422 24.015 0.438 25.401 1.00 79.94 C ANISOU 2998 CD1 PHE A 422 13461 8639 8276 -1214 2434 -1749 C ATOM 2999 CD2 PHE A 422 22.459 1.234 23.760 1.00 79.78 C ANISOU 2999 CD2 PHE A 422 13213 8623 8478 -1174 2411 -1780 C ATOM 3000 CE1 PHE A 422 24.563 -0.442 24.467 1.00 72.56 C ANISOU 3000 CE1 PHE A 422 12554 7609 7407 -1327 2366 -1654 C ATOM 3001 CE2 PHE A 422 23.008 0.367 22.826 1.00 74.10 C ANISOU 3001 CE2 PHE A 422 12529 7813 7814 -1295 2346 -1682 C ATOM 3002 CZ PHE A 422 24.062 -0.469 23.183 1.00 71.47 C ANISOU 3002 CZ PHE A 422 12322 7433 7401 -1363 2324 -1627 C ATOM 3003 N ALA A 423 19.405 2.422 25.679 1.00 89.88 N ANISOU 3003 N ALA A 423 14165 10349 9635 -914 2711 -1976 N ATOM 3004 CA ALA A 423 18.259 2.438 24.793 1.00 91.94 C ANISOU 3004 CA ALA A 423 14249 10652 10031 -929 2724 -1948 C ATOM 3005 C ALA A 423 18.696 3.104 23.500 1.00 89.25 C ANISOU 3005 C ALA A 423 13946 10104 9862 -917 2555 -1970 C ATOM 3006 O ALA A 423 19.122 4.263 23.511 1.00 94.23 O ANISOU 3006 O ALA A 423 14639 10637 10529 -789 2454 -2088 O ATOM 3007 CB ALA A 423 17.091 3.183 25.436 1.00 96.52 C ANISOU 3007 CB ALA A 423 14673 11418 10582 -772 2824 -2069 C ATOM 3008 N ALA A 424 18.619 2.366 22.403 1.00 82.75 N ANISOU 3008 N ALA A 424 13093 9214 9136 -1056 2511 -1850 N ATOM 3009 CA ALA A 424 18.955 2.866 21.081 1.00 73.87 C ANISOU 3009 CA ALA A 424 11986 7921 8158 -1072 2360 -1847 C ATOM 3010 C ALA A 424 17.689 3.022 20.246 1.00 72.31 C ANISOU 3010 C ALA A 424 11617 7759 8097 -1076 2357 -1831 C ATOM 3011 O ALA A 424 16.665 2.391 20.514 1.00 71.53 O ANISOU 3011 O ALA A 424 11389 7805 7984 -1115 2471 -1780 O ATOM 3012 CB ALA A 424 19.945 1.931 20.388 1.00 69.00 C ANISOU 3012 CB ALA A 424 11478 7201 7538 -1217 2298 -1737 C ATOM 3013 N ALA A 425 17.764 3.877 19.229 1.00 65.97 N ANISOU 3013 N ALA A 425 10810 6828 7429 -1045 2215 -1864 N ATOM 3014 CA ALA A 425 16.574 4.385 18.564 1.00 66.86 C ANISOU 3014 CA ALA A 425 10765 6958 7681 -1005 2186 -1886 C ATOM 3015 C ALA A 425 16.099 3.458 17.459 1.00 77.79 C ANISOU 3015 C ALA A 425 12082 8328 9146 -1161 2173 -1753 C ATOM 3016 O ALA A 425 16.900 2.899 16.702 1.00 75.69 O ANISOU 3016 O ALA A 425 11914 7965 8879 -1275 2104 -1675 O ATOM 3017 CB ALA A 425 16.840 5.768 17.988 1.00 67.31 C ANISOU 3017 CB ALA A 425 10856 6869 7851 -908 2013 -1975 C ATOM 3018 N LYS A 426 14.784 3.304 17.371 1.00 78.86 N ANISOU 3018 N LYS A 426 12045 8570 9349 -1158 2236 -1734 N ATOM 3019 CA LYS A 426 14.214 2.481 16.320 1.00 82.36 C ANISOU 3019 CA LYS A 426 12419 8994 9880 -1302 2208 -1610 C ATOM 3020 C LYS A 426 14.288 3.229 14.996 1.00 91.18 C ANISOU 3020 C LYS A 426 13545 9960 11141 -1307 2038 -1620 C ATOM 3021 O LYS A 426 14.207 4.461 14.946 1.00 91.08 O ANISOU 3021 O LYS A 426 13514 9893 11199 -1184 1956 -1720 O ATOM 3022 CB LYS A 426 12.769 2.095 16.664 1.00 75.86 C ANISOU 3022 CB LYS A 426 11395 8343 9086 -1309 2322 -1572 C ATOM 3023 CG LYS A 426 12.042 1.276 15.608 1.00 70.66 C ANISOU 3023 CG LYS A 426 10654 7663 8531 -1459 2278 -1440 C ATOM 3024 CD LYS A 426 10.998 0.362 16.220 1.00 70.48 C ANISOU 3024 CD LYS A 426 10482 7827 8471 -1535 2411 -1343 C ATOM 3025 CE LYS A 426 9.987 -0.107 15.183 1.00 71.85 C ANISOU 3025 CE LYS A 426 10530 7987 8784 -1648 2350 -1234 C ATOM 3026 NZ LYS A 426 8.874 -0.910 15.767 1.00 73.13 N ANISOU 3026 NZ LYS A 426 10519 8346 8922 -1732 2468 -1124 N ATOM 3027 N GLY A 427 14.491 2.469 13.921 1.00 98.08 N ANISOU 3027 N GLY A 427 14458 10760 12050 -1451 1971 -1515 N ATOM 3028 CA GLY A 427 14.485 3.026 12.578 1.00 98.28 C ANISOU 3028 CA GLY A 427 14482 10664 12195 -1485 1814 -1500 C ATOM 3029 C GLY A 427 15.581 4.021 12.320 1.00 96.77 C ANISOU 3029 C GLY A 427 14411 10362 11996 -1437 1694 -1557 C ATOM 3030 O GLY A 427 15.511 4.785 11.356 1.00 97.69 O ANISOU 3030 O GLY A 427 14515 10388 12215 -1448 1551 -1554 O ATOM 3031 N GLN A 428 16.601 4.021 13.150 1.00 91.80 N ANISOU 3031 N GLN A 428 13897 9738 11247 -1399 1736 -1596 N ATOM 3032 CA GLN A 428 17.597 5.065 13.131 1.00 92.15 C ANISOU 3032 CA GLN A 428 14043 9688 11282 -1344 1621 -1650 C ATOM 3033 C GLN A 428 18.968 4.453 12.951 1.00 89.00 C ANISOU 3033 C GLN A 428 13780 9263 10772 -1430 1610 -1598 C ATOM 3034 O GLN A 428 19.253 3.390 13.507 1.00 89.53 O ANISOU 3034 O GLN A 428 13888 9391 10740 -1466 1720 -1571 O ATOM 3035 CB GLN A 428 17.543 5.845 14.417 1.00 96.85 C ANISOU 3035 CB GLN A 428 14644 10313 11841 -1188 1665 -1768 C ATOM 3036 CG GLN A 428 16.943 7.205 14.311 1.00 99.28 C ANISOU 3036 CG GLN A 428 14892 10558 12273 -1067 1548 -1858 C ATOM 3037 CD GLN A 428 17.383 8.022 15.478 1.00103.33 C ANISOU 3037 CD GLN A 428 15475 11061 12724 -917 1544 -1982 C ATOM 3038 OE1 GLN A 428 16.590 8.319 16.370 1.00108.54 O ANISOU 3038 OE1 GLN A 428 16056 11808 13378 -777 1625 -2087 O ATOM 3039 NE2 GLN A 428 18.680 8.311 15.540 1.00101.07 N ANISOU 3039 NE2 GLN A 428 15339 10689 12376 -947 1458 -1969 N ATOM 3040 N TYR A 429 19.809 5.137 12.177 1.00 89.02 N ANISOU 3040 N TYR A 429 13847 9183 10793 -1464 1467 -1580 N ATOM 3041 CA TYR A 429 21.180 4.699 11.966 1.00 83.60 C ANISOU 3041 CA TYR A 429 13271 8491 10002 -1533 1447 -1537 C ATOM 3042 C TYR A 429 22.079 5.134 13.117 1.00 86.27 C ANISOU 3042 C TYR A 429 13703 8819 10256 -1454 1463 -1595 C ATOM 3043 O TYR A 429 21.962 6.247 13.649 1.00 90.95 O ANISOU 3043 O TYR A 429 14303 9364 10890 -1359 1402 -1663 O ATOM 3044 CB TYR A 429 21.717 5.241 10.647 1.00 80.64 C ANISOU 3044 CB TYR A 429 12909 8067 9664 -1618 1291 -1478 C ATOM 3045 CG TYR A 429 21.249 4.433 9.466 1.00 83.01 C ANISOU 3045 CG TYR A 429 13158 8393 9989 -1720 1287 -1411 C ATOM 3046 CD1 TYR A 429 21.752 3.165 9.229 1.00 80.63 C ANISOU 3046 CD1 TYR A 429 12899 8143 9594 -1780 1354 -1379 C ATOM 3047 CD2 TYR A 429 20.284 4.927 8.595 1.00 85.95 C ANISOU 3047 CD2 TYR A 429 13446 8728 10482 -1749 1200 -1386 C ATOM 3048 CE1 TYR A 429 21.310 2.408 8.154 1.00 80.20 C ANISOU 3048 CE1 TYR A 429 12811 8103 9558 -1863 1335 -1331 C ATOM 3049 CE2 TYR A 429 19.842 4.179 7.510 1.00 83.58 C ANISOU 3049 CE2 TYR A 429 13110 8448 10201 -1845 1186 -1326 C ATOM 3050 CZ TYR A 429 20.357 2.918 7.296 1.00 80.42 C ANISOU 3050 CZ TYR A 429 12760 8099 9699 -1899 1254 -1302 C ATOM 3051 OH TYR A 429 19.921 2.158 6.228 1.00 80.18 O ANISOU 3051 OH TYR A 429 12705 8078 9681 -1984 1224 -1255 O ATOM 3052 N GLU A 430 22.972 4.235 13.518 1.00 81.61 N ANISOU 3052 N GLU A 430 13191 8267 9551 -1487 1534 -1573 N ATOM 3053 CA GLU A 430 23.862 4.492 14.634 1.00 76.48 C ANISOU 3053 CA GLU A 430 12636 7610 8813 -1424 1553 -1617 C ATOM 3054 C GLU A 430 25.214 3.869 14.339 1.00 73.10 C ANISOU 3054 C GLU A 430 12288 7191 8296 -1495 1533 -1566 C ATOM 3055 O GLU A 430 25.311 2.878 13.609 1.00 75.27 O ANISOU 3055 O GLU A 430 12549 7500 8550 -1569 1557 -1516 O ATOM 3056 CB GLU A 430 23.306 3.924 15.942 1.00 76.08 C ANISOU 3056 CB GLU A 430 12584 7624 8700 -1359 1703 -1664 C ATOM 3057 CG GLU A 430 21.869 4.300 16.227 1.00 76.73 C ANISOU 3057 CG GLU A 430 12553 7746 8855 -1289 1755 -1714 C ATOM 3058 CD GLU A 430 21.552 4.196 17.691 1.00 77.23 C ANISOU 3058 CD GLU A 430 12624 7890 8831 -1199 1880 -1780 C ATOM 3059 OE1 GLU A 430 22.054 3.252 18.349 1.00 71.08 O ANISOU 3059 OE1 GLU A 430 11910 7156 7940 -1241 1966 -1745 O ATOM 3060 OE2 GLU A 430 20.838 5.096 18.185 1.00 82.78 O ANISOU 3060 OE2 GLU A 430 13271 8611 9570 -1080 1881 -1871 O ATOM 3061 N ARG A 431 26.252 4.445 14.930 1.00 67.65 N ANISOU 3061 N ARG A 431 11680 6471 7551 -1462 1481 -1584 N ATOM 3062 CA ARG A 431 27.625 3.984 14.762 1.00 62.85 C ANISOU 3062 CA ARG A 431 11138 5883 6859 -1514 1456 -1541 C ATOM 3063 C ARG A 431 28.050 3.319 16.064 1.00 64.11 C ANISOU 3063 C ARG A 431 11376 6057 6924 -1467 1552 -1574 C ATOM 3064 O ARG A 431 28.420 4.000 17.022 1.00 70.24 O ANISOU 3064 O ARG A 431 12217 6800 7671 -1404 1530 -1616 O ATOM 3065 CB ARG A 431 28.546 5.147 14.418 1.00 59.37 C ANISOU 3065 CB ARG A 431 10724 5402 6431 -1535 1306 -1512 C ATOM 3066 CG ARG A 431 28.401 5.648 13.031 1.00 60.51 C ANISOU 3066 CG ARG A 431 10799 5550 6641 -1616 1198 -1450 C ATOM 3067 CD ARG A 431 29.209 6.902 12.841 1.00 67.10 C ANISOU 3067 CD ARG A 431 11662 6338 7494 -1648 1030 -1406 C ATOM 3068 NE ARG A 431 30.649 6.654 12.812 1.00 74.97 N ANISOU 3068 NE ARG A 431 12695 7395 8394 -1699 1007 -1352 N ATOM 3069 CZ ARG A 431 31.517 7.347 12.069 1.00 79.57 C ANISOU 3069 CZ ARG A 431 13259 8006 8967 -1792 870 -1261 C ATOM 3070 NH1 ARG A 431 31.091 8.314 11.273 1.00 80.44 N ANISOU 3070 NH1 ARG A 431 13329 8075 9158 -1852 732 -1209 N ATOM 3071 NH2 ARG A 431 32.814 7.059 12.095 1.00 80.90 N ANISOU 3071 NH2 ARG A 431 13442 8254 9043 -1832 864 -1214 N ATOM 3072 N TRP A 432 28.024 1.998 16.110 1.00 56.76 N ANISOU 3072 N TRP A 432 10452 5168 5946 -1500 1640 -1554 N ATOM 3073 CA TRP A 432 28.554 1.331 17.286 1.00 56.81 C ANISOU 3073 CA TRP A 432 10543 5181 5859 -1473 1707 -1569 C ATOM 3074 C TRP A 432 30.036 1.051 17.089 1.00 62.17 C ANISOU 3074 C TRP A 432 11281 5859 6479 -1496 1646 -1545 C ATOM 3075 O TRP A 432 30.452 0.576 16.026 1.00 59.06 O ANISOU 3075 O TRP A 432 10855 5495 6091 -1544 1609 -1513 O ATOM 3076 CB TRP A 432 27.811 0.031 17.586 1.00 57.05 C ANISOU 3076 CB TRP A 432 10562 5244 5869 -1503 1809 -1550 C ATOM 3077 CG TRP A 432 26.389 0.204 17.953 1.00 57.89 C ANISOU 3077 CG TRP A 432 10595 5384 6016 -1483 1885 -1564 C ATOM 3078 CD1 TRP A 432 25.581 1.254 17.644 1.00 63.48 C ANISOU 3078 CD1 TRP A 432 11226 6090 6805 -1442 1863 -1598 C ATOM 3079 CD2 TRP A 432 25.592 -0.715 18.701 1.00 58.58 C ANISOU 3079 CD2 TRP A 432 10669 5524 6066 -1506 1990 -1540 C ATOM 3080 NE1 TRP A 432 24.321 1.046 18.153 1.00 64.09 N ANISOU 3080 NE1 TRP A 432 11228 6227 6895 -1424 1961 -1607 N ATOM 3081 CE2 TRP A 432 24.303 -0.155 18.810 1.00 60.81 C ANISOU 3081 CE2 TRP A 432 10847 5856 6402 -1473 2044 -1563 C ATOM 3082 CE3 TRP A 432 25.842 -1.958 19.292 1.00 60.00 C ANISOU 3082 CE3 TRP A 432 10910 5715 6173 -1558 2032 -1494 C ATOM 3083 CZ2 TRP A 432 23.269 -0.791 19.482 1.00 62.93 C ANISOU 3083 CZ2 TRP A 432 11057 6211 6644 -1497 2152 -1533 C ATOM 3084 CZ3 TRP A 432 24.808 -2.599 19.956 1.00 63.12 C ANISOU 3084 CZ3 TRP A 432 11262 6178 6545 -1596 2124 -1454 C ATOM 3085 CH2 TRP A 432 23.535 -2.011 20.042 1.00 65.44 C ANISOU 3085 CH2 TRP A 432 11436 6545 6882 -1569 2191 -1469 C ATOM 3086 N VAL A 433 30.832 1.329 18.126 1.00 56.28 N ANISOU 3086 N VAL A 433 10621 5092 5672 -1457 1636 -1563 N ATOM 3087 CA VAL A 433 32.279 1.137 18.075 1.00 58.76 C ANISOU 3087 CA VAL A 433 10982 5411 5932 -1472 1575 -1539 C ATOM 3088 C VAL A 433 32.701 0.150 19.153 1.00 58.84 C ANISOU 3088 C VAL A 433 11079 5413 5865 -1454 1632 -1548 C ATOM 3089 O VAL A 433 32.670 0.471 20.347 1.00 63.65 O ANISOU 3089 O VAL A 433 11758 5994 6430 -1414 1657 -1574 O ATOM 3090 CB VAL A 433 33.043 2.450 18.234 1.00 55.97 C ANISOU 3090 CB VAL A 433 10655 5027 5584 -1460 1468 -1533 C ATOM 3091 CG1 VAL A 433 34.489 2.143 18.508 1.00 55.72 C ANISOU 3091 CG1 VAL A 433 10674 5010 5487 -1470 1423 -1506 C ATOM 3092 CG2 VAL A 433 32.921 3.250 16.981 1.00 55.89 C ANISOU 3092 CG2 VAL A 433 10562 5031 5643 -1508 1380 -1495 C ATOM 3093 N ILE A 434 33.170 -1.015 18.736 1.00 55.64 N ANISOU 3093 N ILE A 434 10675 5027 5437 -1479 1636 -1531 N ATOM 3094 CA ILE A 434 33.524 -2.086 19.653 1.00 55.83 C ANISOU 3094 CA ILE A 434 10783 5028 5402 -1472 1667 -1531 C ATOM 3095 C ILE A 434 35.040 -2.129 19.764 1.00 55.60 C ANISOU 3095 C ILE A 434 10795 5000 5331 -1454 1594 -1528 C ATOM 3096 O ILE A 434 35.732 -2.431 18.783 1.00 55.31 O ANISOU 3096 O ILE A 434 10707 5008 5302 -1459 1546 -1525 O ATOM 3097 CB ILE A 434 32.977 -3.438 19.175 1.00 65.94 C ANISOU 3097 CB ILE A 434 12048 6308 6700 -1506 1693 -1519 C ATOM 3098 CG1 ILE A 434 31.453 -3.418 19.084 1.00 56.27 C ANISOU 3098 CG1 ILE A 434 10768 5091 5519 -1536 1762 -1507 C ATOM 3099 CG2 ILE A 434 33.451 -4.555 20.094 1.00 67.10 C ANISOU 3099 CG2 ILE A 434 12291 6413 6792 -1508 1689 -1509 C ATOM 3100 CD1 ILE A 434 30.928 -2.848 17.789 1.00 55.97 C ANISOU 3100 CD1 ILE A 434 10630 5080 5554 -1550 1740 -1510 C ATOM 3101 N SER A 435 35.564 -1.835 20.948 1.00 55.85 N ANISOU 3101 N SER A 435 10914 4996 5312 -1431 1585 -1530 N ATOM 3102 CA SER A 435 36.994 -1.918 21.195 1.00 55.76 C ANISOU 3102 CA SER A 435 10942 4980 5264 -1416 1512 -1520 C ATOM 3103 C SER A 435 37.356 -3.256 21.811 1.00 56.00 C ANISOU 3103 C SER A 435 11045 4976 5255 -1411 1517 -1521 C ATOM 3104 O SER A 435 36.543 -3.934 22.436 1.00 56.36 O ANISOU 3104 O SER A 435 11141 4990 5284 -1429 1573 -1516 O ATOM 3105 CB SER A 435 37.479 -0.791 22.112 1.00 57.16 C ANISOU 3105 CB SER A 435 11184 5122 5413 -1398 1467 -1518 C ATOM 3106 OG SER A 435 38.883 -0.879 22.336 1.00 55.98 O ANISOU 3106 OG SER A 435 11063 4972 5233 -1393 1388 -1497 O ATOM 3107 N GLY A 436 38.602 -3.624 21.634 1.00 55.93 N ANISOU 3107 N GLY A 436 11038 4981 5234 -1389 1446 -1520 N ATOM 3108 CA GLY A 436 39.051 -4.879 22.155 1.00 56.27 C ANISOU 3108 CA GLY A 436 11151 4976 5254 -1375 1420 -1526 C ATOM 3109 C GLY A 436 40.505 -4.717 22.476 1.00 56.36 C ANISOU 3109 C GLY A 436 11179 4993 5240 -1343 1340 -1522 C ATOM 3110 O GLY A 436 41.264 -5.688 22.459 1.00 56.63 O ANISOU 3110 O GLY A 436 11229 5015 5274 -1308 1284 -1539 O ATOM 3111 N VAL A 437 40.903 -3.472 22.740 1.00 56.24 N ANISOU 3111 N VAL A 437 11160 4995 5214 -1351 1317 -1499 N ATOM 3112 CA VAL A 437 42.288 -3.189 23.085 1.00 56.42 C ANISOU 3112 CA VAL A 437 11192 5027 5217 -1335 1231 -1478 C ATOM 3113 C VAL A 437 42.522 -3.619 24.515 1.00 56.84 C ANISOU 3113 C VAL A 437 11387 4985 5226 -1330 1212 -1472 C ATOM 3114 O VAL A 437 41.711 -3.330 25.399 1.00 57.02 O ANISOU 3114 O VAL A 437 11497 4955 5214 -1349 1261 -1471 O ATOM 3115 CB VAL A 437 42.611 -1.701 22.936 1.00 59.70 C ANISOU 3115 CB VAL A 437 11570 5473 5639 -1362 1185 -1441 C ATOM 3116 CG1 VAL A 437 44.097 -1.535 23.014 1.00 59.06 C ANISOU 3116 CG1 VAL A 437 11463 5430 5547 -1357 1088 -1404 C ATOM 3117 CG2 VAL A 437 42.055 -1.143 21.649 1.00 60.81 C ANISOU 3117 CG2 VAL A 437 11591 5692 5820 -1388 1207 -1434 C ATOM 3118 N GLY A 438 43.628 -4.319 24.750 1.00 57.14 N ANISOU 3118 N GLY A 438 11443 5011 5259 -1301 1138 -1470 N ATOM 3119 CA GLY A 438 43.998 -4.758 26.078 1.00 58.85 C ANISOU 3119 CA GLY A 438 11794 5133 5432 -1304 1097 -1454 C ATOM 3120 C GLY A 438 44.102 -6.259 26.215 1.00 68.15 C ANISOU 3120 C GLY A 438 13015 6258 6621 -1285 1066 -1470 C ATOM 3121 O GLY A 438 44.828 -6.745 27.093 1.00 77.30 O ANISOU 3121 O GLY A 438 14262 7348 7760 -1278 990 -1454 O ATOM 3122 N ASP A 439 43.373 -7.006 25.387 1.00 67.02 N ANISOU 3122 N ASP A 439 12822 6131 6513 -1279 1104 -1500 N ATOM 3123 CA ASP A 439 43.630 -8.433 25.256 1.00 73.23 C ANISOU 3123 CA ASP A 439 13635 6861 7329 -1245 1035 -1527 C ATOM 3124 C ASP A 439 43.685 -8.811 23.790 1.00 67.32 C ANISOU 3124 C ASP A 439 12759 6192 6628 -1186 1032 -1590 C ATOM 3125 O ASP A 439 43.056 -8.185 22.930 1.00 57.81 O ANISOU 3125 O ASP A 439 11466 5067 5431 -1202 1106 -1596 O ATOM 3126 CB ASP A 439 42.605 -9.355 26.017 1.00 73.27 C ANISOU 3126 CB ASP A 439 13759 6764 7318 -1309 1046 -1492 C ATOM 3127 CG ASP A 439 41.206 -9.352 25.415 1.00 75.42 C ANISOU 3127 CG ASP A 439 13985 7066 7604 -1354 1141 -1489 C ATOM 3128 OD1 ASP A 439 41.038 -9.684 24.228 1.00 78.67 O ANISOU 3128 OD1 ASP A 439 14310 7514 8067 -1318 1137 -1534 O ATOM 3129 OD2 ASP A 439 40.249 -9.048 26.152 1.00 76.54 O ANISOU 3129 OD2 ASP A 439 14178 7203 7700 -1424 1219 -1441 O ATOM 3130 N MET A 440 44.454 -9.864 23.534 1.00 72.73 N ANISOU 3130 N MET A 440 13440 6851 7342 -1111 934 -1642 N ATOM 3131 CA MET A 440 44.621 -10.435 22.210 1.00 78.44 C ANISOU 3131 CA MET A 440 14057 7649 8098 -1029 911 -1725 C ATOM 3132 C MET A 440 43.734 -11.655 21.979 1.00 77.45 C ANISOU 3132 C MET A 440 13998 7420 8010 -1030 873 -1757 C ATOM 3133 O MET A 440 44.124 -12.578 21.260 1.00 81.18 O ANISOU 3133 O MET A 440 14441 7889 8513 -935 789 -1845 O ATOM 3134 CB MET A 440 46.090 -10.790 22.001 1.00 92.59 C ANISOU 3134 CB MET A 440 15784 9497 9897 -919 816 -1784 C ATOM 3135 CG MET A 440 46.609 -10.475 20.610 1.00103.68 C ANISOU 3135 CG MET A 440 17010 11094 11288 -846 843 -1848 C ATOM 3136 SD MET A 440 46.240 -8.781 20.116 1.00110.81 S ANISOU 3136 SD MET A 440 17811 12138 12153 -945 961 -1766 S ATOM 3137 CE MET A 440 47.026 -7.805 21.442 1.00111.73 C ANISOU 3137 CE MET A 440 17987 12214 12253 -1003 932 -1670 C ATOM 3138 N MET A 441 42.547 -11.683 22.567 1.00 74.47 N ANISOU 3138 N MET A 441 13706 6962 7628 -1133 925 -1688 N ATOM 3139 CA MET A 441 41.645 -12.817 22.435 1.00 70.02 C ANISOU 3139 CA MET A 441 13209 6293 7101 -1164 875 -1688 C ATOM 3140 C MET A 441 40.595 -12.481 21.392 1.00 65.87 C ANISOU 3140 C MET A 441 12599 5839 6591 -1193 963 -1698 C ATOM 3141 O MET A 441 39.895 -11.473 21.526 1.00 65.73 O ANISOU 3141 O MET A 441 12546 5881 6548 -1261 1081 -1645 O ATOM 3142 CB MET A 441 40.986 -13.143 23.774 1.00 71.66 C ANISOU 3142 CB MET A 441 13551 6390 7286 -1278 870 -1586 C ATOM 3143 CG MET A 441 41.968 -13.612 24.834 1.00 75.36 C ANISOU 3143 CG MET A 441 14123 6768 7742 -1263 760 -1567 C ATOM 3144 SD MET A 441 43.053 -14.945 24.287 1.00 77.52 S ANISOU 3144 SD MET A 441 14411 6952 8089 -1128 560 -1671 S ATOM 3145 CE MET A 441 43.090 -15.888 25.804 1.00 79.25 C ANISOU 3145 CE MET A 441 14819 6986 8305 -1218 424 -1574 C ATOM 3146 N LEU A 442 40.498 -13.321 20.358 1.00 63.69 N ANISOU 3146 N LEU A 442 12295 5550 6355 -1131 894 -1775 N ATOM 3147 CA LEU A 442 39.477 -13.171 19.323 1.00 59.64 C ANISOU 3147 CA LEU A 442 11715 5086 5861 -1161 953 -1785 C ATOM 3148 C LEU A 442 38.099 -12.951 19.925 1.00 59.44 C ANISOU 3148 C LEU A 442 11731 5014 5840 -1296 1032 -1679 C ATOM 3149 O LEU A 442 37.695 -13.662 20.841 1.00 74.97 O ANISOU 3149 O LEU A 442 13802 6870 7813 -1366 983 -1613 O ATOM 3150 CB LEU A 442 39.467 -14.410 18.436 1.00 60.53 C ANISOU 3150 CB LEU A 442 11845 5137 6017 -1085 827 -1876 C ATOM 3151 CG LEU A 442 38.431 -14.330 17.338 1.00 60.31 C ANISOU 3151 CG LEU A 442 11757 5150 6008 -1117 870 -1888 C ATOM 3152 CD1 LEU A 442 38.787 -13.187 16.452 1.00 59.52 C ANISOU 3152 CD1 LEU A 442 11517 5233 5864 -1080 974 -1922 C ATOM 3153 CD2 LEU A 442 38.492 -15.614 16.565 1.00 61.39 C ANISOU 3153 CD2 LEU A 442 11936 5206 6184 -1032 720 -1989 C ATOM 3154 N HIS A 443 37.377 -11.955 19.423 1.00 58.69 N ANISOU 3154 N HIS A 443 11547 5014 5740 -1336 1148 -1658 N ATOM 3155 CA HIS A 443 36.055 -11.615 19.949 1.00 58.61 C ANISOU 3155 CA HIS A 443 11546 4992 5731 -1447 1238 -1569 C ATOM 3156 C HIS A 443 35.086 -11.361 18.808 1.00 58.31 C ANISOU 3156 C HIS A 443 11418 5005 5733 -1470 1283 -1578 C ATOM 3157 O HIS A 443 34.706 -10.216 18.543 1.00 61.78 O ANISOU 3157 O HIS A 443 11776 5530 6167 -1484 1378 -1567 O ATOM 3158 CB HIS A 443 36.116 -10.388 20.859 1.00 58.11 C ANISOU 3158 CB HIS A 443 11476 4988 5617 -1472 1340 -1526 C ATOM 3159 CG HIS A 443 36.751 -10.632 22.191 1.00 60.75 C ANISOU 3159 CG HIS A 443 11916 5264 5903 -1482 1306 -1492 C ATOM 3160 ND1 HIS A 443 36.416 -11.700 22.993 1.00 62.97 N ANISOU 3160 ND1 HIS A 443 12299 5450 6178 -1546 1248 -1434 N ATOM 3161 CD2 HIS A 443 37.639 -9.896 22.901 1.00 58.30 C ANISOU 3161 CD2 HIS A 443 11630 4975 5546 -1451 1316 -1495 C ATOM 3162 CE1 HIS A 443 37.115 -11.645 24.114 1.00 64.79 C ANISOU 3162 CE1 HIS A 443 12613 5650 6356 -1549 1224 -1408 C ATOM 3163 NE2 HIS A 443 37.861 -10.557 24.085 1.00 63.49 N ANISOU 3163 NE2 HIS A 443 12405 5553 6167 -1487 1266 -1448 N ATOM 3164 N PRO A 444 34.644 -12.411 18.123 1.00 58.89 N ANISOU 3164 N PRO A 444 11511 5014 5852 -1475 1199 -1598 N ATOM 3165 CA PRO A 444 33.572 -12.239 17.144 1.00 58.74 C ANISOU 3165 CA PRO A 444 11418 5027 5874 -1515 1233 -1591 C ATOM 3166 C PRO A 444 32.345 -11.732 17.862 1.00 58.73 C ANISOU 3166 C PRO A 444 11396 5039 5879 -1623 1336 -1489 C ATOM 3167 O PRO A 444 31.864 -12.362 18.794 1.00 59.97 O ANISOU 3167 O PRO A 444 11621 5134 6032 -1699 1322 -1412 O ATOM 3168 CB PRO A 444 33.360 -13.647 16.605 1.00 59.67 C ANISOU 3168 CB PRO A 444 11599 5036 6037 -1509 1092 -1619 C ATOM 3169 CG PRO A 444 34.539 -14.408 17.022 1.00 60.20 C ANISOU 3169 CG PRO A 444 11750 5035 6088 -1428 982 -1676 C ATOM 3170 CD PRO A 444 34.999 -13.818 18.287 1.00 59.88 C ANISOU 3170 CD PRO A 444 11737 5012 6001 -1453 1050 -1619 C ATOM 3171 N PHE A 445 31.853 -10.578 17.437 1.00 42.16 N ANISOU 3171 N PHE A 445 8697 4297 3024 -2351 1266 -533 N ATOM 3172 CA PHE A 445 30.922 -9.791 18.235 1.00 44.16 C ANISOU 3172 CA PHE A 445 8963 4589 3226 -2281 1353 -594 C ATOM 3173 C PHE A 445 29.578 -9.710 17.535 1.00 45.46 C ANISOU 3173 C PHE A 445 8981 4800 3494 -2268 1430 -602 C ATOM 3174 O PHE A 445 29.486 -9.193 16.418 1.00 46.82 O ANISOU 3174 O PHE A 445 9075 4942 3772 -2263 1362 -618 O ATOM 3175 CB PHE A 445 31.477 -8.393 18.492 1.00 42.93 C ANISOU 3175 CB PHE A 445 8894 4381 3035 -2213 1266 -669 C ATOM 3176 CG PHE A 445 30.679 -7.610 19.485 1.00 47.75 C ANISOU 3176 CG PHE A 445 9560 5019 3564 -2122 1355 -742 C ATOM 3177 CD1 PHE A 445 29.711 -6.712 19.063 1.00 46.20 C ANISOU 3177 CD1 PHE A 445 9286 4830 3439 -2044 1392 -803 C ATOM 3178 CD2 PHE A 445 30.891 -7.774 20.846 1.00 52.85 C ANISOU 3178 CD2 PHE A 445 10342 5682 4055 -2106 1404 -752 C ATOM 3179 CE1 PHE A 445 28.978 -6.009 19.971 1.00 50.46 C ANISOU 3179 CE1 PHE A 445 9876 5395 3901 -1940 1486 -876 C ATOM 3180 CE2 PHE A 445 30.155 -7.067 21.771 1.00 46.84 C ANISOU 3180 CE2 PHE A 445 9646 4950 3202 -2011 1500 -827 C ATOM 3181 CZ PHE A 445 29.198 -6.191 21.339 1.00 53.51 C ANISOU 3181 CZ PHE A 445 10406 5803 4122 -1921 1548 -892 C ATOM 3182 N HIS A 446 28.544 -10.183 18.218 1.00 44.34 N ANISOU 3182 N HIS A 446 8798 4733 3317 -2265 1569 -585 N ATOM 3183 CA HIS A 446 27.213 -10.408 17.675 1.00 47.30 C ANISOU 3183 CA HIS A 446 9012 5169 3790 -2275 1652 -564 C ATOM 3184 C HIS A 446 26.243 -9.387 18.260 1.00 52.22 C ANISOU 3184 C HIS A 446 9597 5848 4397 -2161 1751 -631 C ATOM 3185 O HIS A 446 26.319 -9.054 19.448 1.00 56.54 O ANISOU 3185 O HIS A 446 10250 6417 4816 -2099 1820 -670 O ATOM 3186 CB HIS A 446 26.776 -11.855 17.984 1.00 47.47 C ANISOU 3186 CB HIS A 446 9001 5242 3793 -2374 1737 -472 C ATOM 3187 CG HIS A 446 25.469 -12.269 17.375 1.00 50.41 C ANISOU 3187 CG HIS A 446 9200 5677 4275 -2419 1804 -427 C ATOM 3188 ND1 HIS A 446 24.928 -11.669 16.261 1.00 50.55 N ANISOU 3188 ND1 HIS A 446 9097 5687 4424 -2398 1751 -451 N ATOM 3189 CD2 HIS A 446 24.583 -13.227 17.745 1.00 53.62 C ANISOU 3189 CD2 HIS A 446 9534 6157 4682 -2493 1910 -350 C ATOM 3190 CE1 HIS A 446 23.770 -12.238 15.969 1.00 53.46 C ANISOU 3190 CE1 HIS A 446 9320 6122 4872 -2455 1816 -392 C ATOM 3191 NE2 HIS A 446 23.538 -13.189 16.853 1.00 54.41 N ANISOU 3191 NE2 HIS A 446 9462 6294 4917 -2518 1915 -328 N ATOM 3192 N ILE A 447 25.342 -8.886 17.413 1.00 50.21 N ANISOU 3192 N ILE A 447 9198 5613 4269 -2128 1752 -646 N ATOM 3193 CA ILE A 447 24.346 -7.878 17.766 1.00 50.39 C ANISOU 3193 CA ILE A 447 9156 5684 4308 -2000 1839 -710 C ATOM 3194 C ILE A 447 22.993 -8.363 17.257 1.00 54.63 C ANISOU 3194 C ILE A 447 9482 6312 4962 -2030 1924 -650 C ATOM 3195 O ILE A 447 22.808 -8.519 16.043 1.00 59.14 O ANISOU 3195 O ILE A 447 9951 6856 5662 -2089 1833 -615 O ATOM 3196 CB ILE A 447 24.699 -6.501 17.170 1.00 47.42 C ANISOU 3196 CB ILE A 447 8817 5218 3984 -1910 1718 -792 C ATOM 3197 CG1 ILE A 447 26.039 -6.008 17.709 1.00 46.55 C ANISOU 3197 CG1 ILE A 447 8909 5018 3759 -1896 1623 -841 C ATOM 3198 CG2 ILE A 447 23.607 -5.472 17.396 1.00 48.64 C ANISOU 3198 CG2 ILE A 447 8896 5409 4177 -1763 1798 -859 C ATOM 3199 CD1 ILE A 447 26.593 -4.855 16.911 1.00 47.95 C ANISOU 3199 CD1 ILE A 447 9126 5092 4000 -1858 1468 -892 C ATOM 3200 N HIS A 448 22.054 -8.612 18.173 1.00 54.41 N ANISOU 3200 N HIS A 448 9388 6397 4888 -1996 2095 -630 N ATOM 3201 CA HIS A 448 20.782 -9.187 17.752 1.00 59.67 C ANISOU 3201 CA HIS A 448 9839 7163 5670 -2047 2174 -552 C ATOM 3202 C HIS A 448 19.898 -8.145 17.070 1.00 60.89 C ANISOU 3202 C HIS A 448 9842 7333 5960 -1937 2160 -594 C ATOM 3203 O HIS A 448 20.091 -6.938 17.208 1.00 56.19 O ANISOU 3203 O HIS A 448 9314 6686 5347 -1796 2133 -692 O ATOM 3204 CB HIS A 448 19.985 -9.769 18.923 1.00 63.43 C ANISOU 3204 CB HIS A 448 10264 7773 6062 -2050 2374 -502 C ATOM 3205 CG HIS A 448 20.708 -10.808 19.725 1.00 61.92 C ANISOU 3205 CG HIS A 448 10220 7576 5731 -2154 2401 -448 C ATOM 3206 ND1 HIS A 448 20.038 -11.731 20.497 1.00 61.34 N ANISOU 3206 ND1 HIS A 448 10091 7615 5602 -2228 2549 -358 N ATOM 3207 CD2 HIS A 448 22.027 -11.036 19.924 1.00 59.16 C ANISOU 3207 CD2 HIS A 448 10067 7125 5285 -2192 2299 -467 C ATOM 3208 CE1 HIS A 448 20.915 -12.503 21.112 1.00 61.08 C ANISOU 3208 CE1 HIS A 448 10226 7539 5444 -2308 2530 -324 C ATOM 3209 NE2 HIS A 448 22.129 -12.099 20.787 1.00 59.68 N ANISOU 3209 NE2 HIS A 448 10198 7234 5242 -2283 2379 -390 N ATOM 3210 N GLY A 449 18.906 -8.641 16.327 1.00 71.44 N ANISOU 3210 N GLY A 449 10975 8733 7435 -2007 2166 -514 N ATOM 3211 CA GLY A 449 17.826 -7.805 15.829 1.00 73.49 C ANISOU 3211 CA GLY A 449 11051 9041 7832 -1903 2180 -531 C ATOM 3212 C GLY A 449 18.154 -6.897 14.669 1.00 69.59 C ANISOU 3212 C GLY A 449 10569 8433 7437 -1859 2002 -582 C ATOM 3213 O GLY A 449 17.420 -5.931 14.416 1.00 69.52 O ANISOU 3213 O GLY A 449 10452 8440 7521 -1731 2004 -620 O ATOM 3214 N THR A 450 19.227 -7.187 13.942 1.00 66.26 N ANISOU 3214 N THR A 450 10274 7902 7001 -1960 1850 -578 N ATOM 3215 CA THR A 450 19.656 -6.311 12.870 1.00 59.87 C ANISOU 3215 CA THR A 450 9497 6986 6265 -1929 1683 -621 C ATOM 3216 C THR A 450 20.644 -7.076 12.000 1.00 53.43 C ANISOU 3216 C THR A 450 8772 6091 5439 -2079 1551 -580 C ATOM 3217 O THR A 450 21.294 -8.021 12.457 1.00 50.99 O ANISOU 3217 O THR A 450 8556 5781 5037 -2166 1583 -551 O ATOM 3218 CB THR A 450 20.283 -5.036 13.450 1.00 53.59 C ANISOU 3218 CB THR A 450 8852 6117 5394 -1780 1666 -731 C ATOM 3219 OG1 THR A 450 20.628 -4.112 12.410 1.00 51.04 O ANISOU 3219 OG1 THR A 450 8556 5690 5148 -1752 1502 -763 O ATOM 3220 CG2 THR A 450 21.520 -5.390 14.260 1.00 48.79 C ANISOU 3220 CG2 THR A 450 8447 5466 4626 -1820 1673 -755 C ATOM 3221 N GLN A 451 20.684 -6.701 10.726 1.00 49.97 N ANISOU 3221 N GLN A 451 8300 5591 5096 -2107 1407 -573 N ATOM 3222 CA GLN A 451 21.837 -6.905 9.865 1.00 45.20 C ANISOU 3222 CA GLN A 451 7817 4891 4465 -2193 1272 -568 C ATOM 3223 C GLN A 451 22.501 -5.555 9.686 1.00 51.89 C ANISOU 3223 C GLN A 451 8760 5654 5302 -2097 1180 -640 C ATOM 3224 O GLN A 451 21.814 -4.564 9.425 1.00 63.20 O ANISOU 3224 O GLN A 451 10121 7078 6815 -2002 1151 -668 O ATOM 3225 CB GLN A 451 21.428 -7.479 8.509 1.00 44.80 C ANISOU 3225 CB GLN A 451 7678 4832 4513 -2306 1172 -504 C ATOM 3226 CG GLN A 451 21.071 -8.971 8.516 1.00 48.87 C ANISOU 3226 CG GLN A 451 8148 5395 5026 -2440 1220 -427 C ATOM 3227 CD GLN A 451 22.140 -9.852 9.130 1.00 47.72 C ANISOU 3227 CD GLN A 451 8152 5222 4758 -2495 1259 -424 C ATOM 3228 OE1 GLN A 451 23.275 -9.431 9.314 1.00 52.10 O ANISOU 3228 OE1 GLN A 451 8841 5719 5236 -2454 1225 -470 O ATOM 3229 NE2 GLN A 451 21.753 -11.044 9.547 1.00 44.39 N ANISOU 3229 NE2 GLN A 451 7701 4845 4319 -2585 1331 -362 N ATOM 3230 N PHE A 452 23.811 -5.501 9.873 1.00 52.06 N ANISOU 3230 N PHE A 452 8941 5611 5229 -2119 1132 -664 N ATOM 3231 CA PHE A 452 24.537 -4.232 9.868 1.00 53.78 C ANISOU 3231 CA PHE A 452 9266 5745 5424 -2043 1043 -725 C ATOM 3232 C PHE A 452 25.648 -4.263 8.825 1.00 53.36 C ANISOU 3232 C PHE A 452 9286 5623 5366 -2134 908 -696 C ATOM 3233 O PHE A 452 25.866 -5.274 8.152 1.00 56.28 O ANISOU 3233 O PHE A 452 9634 6009 5741 -2238 894 -641 O ATOM 3234 CB PHE A 452 25.084 -3.915 11.265 1.00 54.06 C ANISOU 3234 CB PHE A 452 9429 5773 5340 -1971 1112 -782 C ATOM 3235 CG PHE A 452 26.051 -4.958 11.813 1.00 47.90 C ANISOU 3235 CG PHE A 452 8741 5006 4454 -2058 1144 -751 C ATOM 3236 CD1 PHE A 452 27.316 -5.125 11.273 1.00 41.56 C ANISOU 3236 CD1 PHE A 452 8022 4146 3623 -2134 1039 -726 C ATOM 3237 CD2 PHE A 452 25.708 -5.713 12.927 1.00 48.37 C ANISOU 3237 CD2 PHE A 452 8803 5137 4440 -2053 1280 -742 C ATOM 3238 CE1 PHE A 452 28.184 -6.044 11.798 1.00 41.00 C ANISOU 3238 CE1 PHE A 452 8027 4086 3466 -2195 1064 -696 C ATOM 3239 CE2 PHE A 452 26.588 -6.633 13.464 1.00 42.90 C ANISOU 3239 CE2 PHE A 452 8201 4446 3651 -2125 1297 -710 C ATOM 3240 CZ PHE A 452 27.811 -6.804 12.900 1.00 41.66 C ANISOU 3240 CZ PHE A 452 8119 4228 3480 -2190 1187 -688 C ATOM 3241 N ARG A 453 26.363 -3.142 8.700 1.00 47.36 N ANISOU 3241 N ARG A 453 8618 4785 4593 -2092 811 -732 N ATOM 3242 CA ARG A 453 27.462 -3.026 7.748 1.00 46.99 C ANISOU 3242 CA ARG A 453 8634 4682 4537 -2174 690 -699 C ATOM 3243 C ARG A 453 28.721 -2.564 8.465 1.00 43.97 C ANISOU 3243 C ARG A 453 8390 4252 4064 -2166 654 -724 C ATOM 3244 O ARG A 453 28.652 -1.731 9.368 1.00 41.06 O ANISOU 3244 O ARG A 453 8087 3850 3663 -2080 661 -783 O ATOM 3245 CB ARG A 453 27.097 -2.078 6.609 1.00 48.08 C ANISOU 3245 CB ARG A 453 8734 4768 4764 -2164 572 -691 C ATOM 3246 CG ARG A 453 25.842 -2.524 5.867 1.00 51.91 C ANISOU 3246 CG ARG A 453 9077 5300 5345 -2179 587 -659 C ATOM 3247 CD ARG A 453 25.598 -1.788 4.590 1.00 52.67 C ANISOU 3247 CD ARG A 453 9145 5348 5521 -2195 454 -633 C ATOM 3248 NE ARG A 453 26.783 -1.783 3.757 1.00 57.72 N ANISOU 3248 NE ARG A 453 9872 5946 6111 -2286 364 -598 N ATOM 3249 CZ ARG A 453 26.910 -1.021 2.675 1.00 68.21 C ANISOU 3249 CZ ARG A 453 11217 7223 7478 -2312 238 -570 C ATOM 3250 NH1 ARG A 453 25.901 -0.230 2.295 1.00 68.87 N ANISOU 3250 NH1 ARG A 453 11235 7276 7654 -2252 175 -575 N ATOM 3251 NH2 ARG A 453 28.032 -1.054 1.962 1.00 73.37 N ANISOU 3251 NH2 ARG A 453 11946 7856 8076 -2397 175 -531 N ATOM 3252 N ILE A 454 29.864 -3.129 8.082 1.00 43.97 N ANISOU 3252 N ILE A 454 8434 4251 4021 -2254 614 -678 N ATOM 3253 CA ILE A 454 31.116 -2.925 8.804 1.00 42.07 C ANISOU 3253 CA ILE A 454 8305 3983 3698 -2265 582 -682 C ATOM 3254 C ILE A 454 31.860 -1.789 8.137 1.00 39.76 C ANISOU 3254 C ILE A 454 8060 3620 3426 -2288 443 -670 C ATOM 3255 O ILE A 454 32.145 -1.856 6.938 1.00 41.00 O ANISOU 3255 O ILE A 454 8177 3778 3622 -2352 385 -619 O ATOM 3256 CB ILE A 454 31.993 -4.182 8.791 1.00 43.57 C ANISOU 3256 CB ILE A 454 8502 4215 3837 -2340 617 -629 C ATOM 3257 CG1 ILE A 454 31.344 -5.364 9.501 1.00 45.16 C ANISOU 3257 CG1 ILE A 454 8674 4475 4011 -2334 744 -628 C ATOM 3258 CG2 ILE A 454 33.339 -3.866 9.416 1.00 43.38 C ANISOU 3258 CG2 ILE A 454 8574 4165 3745 -2356 558 -619 C ATOM 3259 CD1 ILE A 454 32.106 -6.649 9.268 1.00 43.13 C ANISOU 3259 CD1 ILE A 454 8423 4243 3722 -2402 766 -574 C ATOM 3260 N LEU A 455 32.202 -0.767 8.914 1.00 39.60 N ANISOU 3260 N LEU A 455 8137 3538 3372 -2242 387 -714 N ATOM 3261 CA LEU A 455 32.995 0.338 8.402 1.00 42.13 C ANISOU 3261 CA LEU A 455 8507 3790 3710 -2270 243 -688 C ATOM 3262 C LEU A 455 34.454 0.127 8.725 1.00 47.61 C ANISOU 3262 C LEU A 455 9211 4527 4353 -2305 200 -615 C ATOM 3263 O LEU A 455 35.314 0.296 7.863 1.00 52.94 O ANISOU 3263 O LEU A 455 9834 5230 5052 -2351 125 -531 O ATOM 3264 CB LEU A 455 32.537 1.659 8.994 1.00 40.81 C ANISOU 3264 CB LEU A 455 8438 3523 3546 -2189 183 -767 C ATOM 3265 CG LEU A 455 31.051 1.956 8.858 1.00 41.53 C ANISOU 3265 CG LEU A 455 8463 3611 3706 -2085 238 -818 C ATOM 3266 CD1 LEU A 455 30.695 3.039 9.845 1.00 46.64 C ANISOU 3266 CD1 LEU A 455 9219 4175 4325 -1968 218 -909 C ATOM 3267 CD2 LEU A 455 30.686 2.357 7.478 1.00 41.37 C ANISOU 3267 CD2 LEU A 455 8371 3566 3780 -2116 156 -774 C ATOM 3268 N SER A 456 34.745 -0.240 9.961 1.00 51.86 N ANISOU 3268 N SER A 456 9821 5070 4814 -2288 247 -646 N ATOM 3269 CA SER A 456 36.083 -0.659 10.341 1.00 51.90 C ANISOU 3269 CA SER A 456 9835 5115 4770 -2334 214 -579 C ATOM 3270 C SER A 456 35.972 -2.040 10.957 1.00 50.77 C ANISOU 3270 C SER A 456 9694 5023 4571 -2348 335 -589 C ATOM 3271 O SER A 456 35.121 -2.260 11.812 1.00 54.25 O ANISOU 3271 O SER A 456 10194 5453 4967 -2308 420 -664 O ATOM 3272 CB SER A 456 36.717 0.329 11.326 1.00 52.00 C ANISOU 3272 CB SER A 456 9952 5069 4738 -2310 116 -592 C ATOM 3273 OG SER A 456 38.029 -0.066 11.697 1.00 50.51 O ANISOU 3273 OG SER A 456 9771 4914 4507 -2368 69 -523 O ATOM 3274 N GLU A 457 36.800 -2.971 10.518 1.00 42.78 N ANISOU 3274 N GLU A 457 8628 4067 3558 -2402 347 -518 N ATOM 3275 CA GLU A 457 36.838 -4.279 11.158 1.00 41.73 C ANISOU 3275 CA GLU A 457 8517 3969 3371 -2418 442 -519 C ATOM 3276 C GLU A 457 38.225 -4.495 11.754 1.00 40.84 C ANISOU 3276 C GLU A 457 8444 3864 3207 -2453 382 -466 C ATOM 3277 O GLU A 457 39.178 -4.785 11.029 1.00 37.69 O ANISOU 3277 O GLU A 457 7989 3494 2835 -2498 344 -399 O ATOM 3278 CB GLU A 457 36.473 -5.376 10.182 1.00 41.67 C ANISOU 3278 CB GLU A 457 8425 4002 3403 -2445 517 -492 C ATOM 3279 CG GLU A 457 36.386 -6.733 10.843 1.00 44.03 C ANISOU 3279 CG GLU A 457 8745 4328 3656 -2452 612 -486 C ATOM 3280 CD GLU A 457 35.909 -7.807 9.909 1.00 49.88 C ANISOU 3280 CD GLU A 457 9417 5097 4438 -2473 677 -463 C ATOM 3281 OE1 GLU A 457 36.254 -7.741 8.690 1.00 51.33 O ANISOU 3281 OE1 GLU A 457 9541 5297 4666 -2487 638 -429 O ATOM 3282 OE2 GLU A 457 35.178 -8.705 10.401 1.00 49.94 O ANISOU 3282 OE2 GLU A 457 9425 5123 4429 -2465 764 -470 O ATOM 3283 N ASN A 458 38.334 -4.376 13.077 1.00 38.73 N ANISOU 3283 N ASN A 458 8280 3574 2863 -2434 375 -498 N ATOM 3284 CA ASN A 458 39.613 -4.513 13.765 1.00 39.02 C ANISOU 3284 CA ASN A 458 8368 3610 2849 -2474 297 -450 C ATOM 3285 C ASN A 458 40.668 -3.575 13.188 1.00 42.82 C ANISOU 3285 C ASN A 458 8813 4081 3375 -2518 159 -389 C ATOM 3286 O ASN A 458 41.834 -3.941 13.036 1.00 46.03 O ANISOU 3286 O ASN A 458 9195 4510 3786 -2582 104 -321 O ATOM 3287 CB ASN A 458 40.117 -5.948 13.726 1.00 38.59 C ANISOU 3287 CB ASN A 458 8278 3602 2782 -2500 357 -398 C ATOM 3288 CG ASN A 458 40.918 -6.314 14.949 1.00 40.68 C ANISOU 3288 CG ASN A 458 8620 3869 2969 -2507 316 -369 C ATOM 3289 OD1 ASN A 458 40.554 -5.979 16.067 1.00 39.88 O ANISOU 3289 OD1 ASN A 458 8628 3739 2786 -2484 314 -418 O ATOM 3290 ND2 ASN A 458 42.027 -6.998 14.742 1.00 42.84 N ANISOU 3290 ND2 ASN A 458 8838 4175 3262 -2534 281 -286 N ATOM 3291 N GLY A 459 40.271 -2.354 12.866 1.00 41.79 N ANISOU 3291 N GLY A 459 8682 3913 3283 -2489 100 -411 N ATOM 3292 CA GLY A 459 41.244 -1.348 12.528 1.00 43.69 C ANISOU 3292 CA GLY A 459 8911 4136 3554 -2537 -44 -352 C ATOM 3293 C GLY A 459 41.606 -1.247 11.072 1.00 45.43 C ANISOU 3293 C GLY A 459 9016 4397 3849 -2582 -64 -288 C ATOM 3294 O GLY A 459 42.417 -0.383 10.725 1.00 46.88 O ANISOU 3294 O GLY A 459 9182 4572 4058 -2634 -182 -228 O ATOM 3295 N LYS A 460 41.053 -2.105 10.217 1.00 50.02 N ANISOU 3295 N LYS A 460 9523 5023 4458 -2570 45 -293 N ATOM 3296 CA LYS A 460 41.212 -2.075 8.772 1.00 49.55 C ANISOU 3296 CA LYS A 460 9366 5007 4455 -2600 45 -243 C ATOM 3297 C LYS A 460 39.833 -2.053 8.127 1.00 44.15 C ANISOU 3297 C LYS A 460 8656 4313 3807 -2544 112 -297 C ATOM 3298 O LYS A 460 38.837 -2.399 8.772 1.00 44.34 O ANISOU 3298 O LYS A 460 8719 4314 3815 -2494 186 -365 O ATOM 3299 CB LYS A 460 42.004 -3.298 8.290 1.00 55.71 C ANISOU 3299 CB LYS A 460 10087 5849 5230 -2643 109 -191 C ATOM 3300 CG LYS A 460 43.385 -3.344 8.884 1.00 59.84 C ANISOU 3300 CG LYS A 460 10620 6381 5734 -2709 37 -126 C ATOM 3301 CD LYS A 460 44.417 -4.072 8.053 1.00 64.26 C ANISOU 3301 CD LYS A 460 11093 7005 6318 -2763 71 -40 C ATOM 3302 CE LYS A 460 45.518 -3.077 7.685 1.00 69.18 C ANISOU 3302 CE LYS A 460 11662 7651 6970 -2844 -49 51 C ATOM 3303 NZ LYS A 460 46.860 -3.709 7.757 1.00 74.45 N ANISOU 3303 NZ LYS A 460 12241 8397 7648 -2868 -49 150 N ATOM 3304 N PRO A 461 39.722 -1.617 6.871 1.00 40.53 N ANISOU 3304 N PRO A 461 8135 3871 3394 -2559 83 -264 N ATOM 3305 CA PRO A 461 38.419 -1.644 6.213 1.00 37.31 C ANISOU 3305 CA PRO A 461 7700 3453 3024 -2517 131 -307 C ATOM 3306 C PRO A 461 38.023 -3.077 5.889 1.00 36.72 C ANISOU 3306 C PRO A 461 7586 3427 2937 -2514 249 -318 C ATOM 3307 O PRO A 461 38.881 -3.906 5.549 1.00 43.30 O ANISOU 3307 O PRO A 461 8396 4309 3747 -2547 280 -276 O ATOM 3308 CB PRO A 461 38.646 -0.831 4.928 1.00 37.91 C ANISOU 3308 CB PRO A 461 7730 3536 3138 -2550 51 -252 C ATOM 3309 CG PRO A 461 39.926 -0.127 5.104 1.00 41.06 C ANISOU 3309 CG PRO A 461 8141 3935 3524 -2604 -47 -189 C ATOM 3310 CD PRO A 461 40.744 -0.932 6.065 1.00 41.84 C ANISOU 3310 CD PRO A 461 8261 4059 3578 -2623 -10 -183 C ATOM 3311 N PRO A 462 36.740 -3.391 5.952 1.00 36.66 N ANISOU 3311 N PRO A 462 7576 3403 2951 -2479 311 -373 N ATOM 3312 CA PRO A 462 36.324 -4.780 5.778 1.00 36.27 C ANISOU 3312 CA PRO A 462 7501 3389 2889 -2482 412 -381 C ATOM 3313 C PRO A 462 36.822 -5.348 4.462 1.00 40.59 C ANISOU 3313 C PRO A 462 7999 3987 3438 -2509 415 -332 C ATOM 3314 O PRO A 462 37.000 -4.631 3.473 1.00 35.97 O ANISOU 3314 O PRO A 462 7386 3409 2872 -2526 351 -301 O ATOM 3315 CB PRO A 462 34.797 -4.688 5.798 1.00 40.46 C ANISOU 3315 CB PRO A 462 8022 3891 3461 -2461 448 -437 C ATOM 3316 CG PRO A 462 34.511 -3.319 5.336 1.00 40.54 C ANISOU 3316 CG PRO A 462 8028 3859 3517 -2447 355 -443 C ATOM 3317 CD PRO A 462 35.589 -2.483 5.959 1.00 40.77 C ANISOU 3317 CD PRO A 462 8108 3867 3517 -2444 282 -424 C ATOM 3318 N ALA A 463 37.089 -6.652 4.475 1.00 42.49 N ANISOU 3318 N ALA A 463 8244 4254 3648 -2514 489 -327 N ATOM 3319 CA ALA A 463 37.423 -7.334 3.242 1.00 35.49 C ANISOU 3319 CA ALA A 463 7335 3401 2750 -2532 508 -300 C ATOM 3320 C ALA A 463 36.238 -7.293 2.290 1.00 47.93 C ANISOU 3320 C ALA A 463 8879 4975 4357 -2529 500 -316 C ATOM 3321 O ALA A 463 35.087 -7.038 2.678 1.00 35.65 O ANISOU 3321 O ALA A 463 7310 3394 2841 -2515 500 -349 O ATOM 3322 CB ALA A 463 37.846 -8.772 3.508 1.00 35.40 C ANISOU 3322 CB ALA A 463 7353 3396 2703 -2527 586 -301 C ATOM 3323 N ALA A 464 36.556 -7.528 1.014 1.00 48.41 N ANISOU 3323 N ALA A 464 8937 5059 4399 -2552 491 -292 N ATOM 3324 CA ALA A 464 35.602 -7.333 -0.070 1.00 35.67 C ANISOU 3324 CA ALA A 464 7302 3442 2807 -2564 455 -294 C ATOM 3325 C ALA A 464 34.286 -8.079 0.169 1.00 37.75 C ANISOU 3325 C ALA A 464 7551 3690 3102 -2552 488 -329 C ATOM 3326 O ALA A 464 33.209 -7.552 -0.115 1.00 35.98 O ANISOU 3326 O ALA A 464 7293 3448 2931 -2558 443 -338 O ATOM 3327 CB ALA A 464 36.251 -7.770 -1.370 1.00 35.79 C ANISOU 3327 CB ALA A 464 7348 3483 2768 -2598 462 -269 C ATOM 3328 N HIS A 465 34.345 -9.299 0.695 1.00 36.45 N ANISOU 3328 N HIS A 465 7412 3525 2912 -2544 558 -344 N ATOM 3329 CA HIS A 465 33.147 -10.090 0.965 1.00 36.57 C ANISOU 3329 CA HIS A 465 7412 3526 2955 -2552 588 -366 C ATOM 3330 C HIS A 465 32.520 -9.826 2.343 1.00 41.71 C ANISOU 3330 C HIS A 465 8047 4160 3640 -2546 623 -390 C ATOM 3331 O HIS A 465 31.393 -10.277 2.621 1.00 39.50 O ANISOU 3331 O HIS A 465 7743 3870 3395 -2571 650 -404 O ATOM 3332 CB HIS A 465 33.513 -11.553 0.827 1.00 35.92 C ANISOU 3332 CB HIS A 465 7382 3441 2826 -2553 640 -366 C ATOM 3333 CG HIS A 465 34.659 -11.941 1.692 1.00 35.72 C ANISOU 3333 CG HIS A 465 7400 3412 2760 -2531 689 -363 C ATOM 3334 ND1 HIS A 465 35.941 -11.530 1.438 1.00 35.57 N ANISOU 3334 ND1 HIS A 465 7401 3404 2710 -2527 682 -344 N ATOM 3335 CD2 HIS A 465 34.722 -12.698 2.809 1.00 49.18 C ANISOU 3335 CD2 HIS A 465 9132 5101 4453 -2521 740 -369 C ATOM 3336 CE1 HIS A 465 36.748 -12.016 2.364 1.00 35.54 C ANISOU 3336 CE1 HIS A 465 7430 3389 2684 -2513 721 -338 C ATOM 3337 NE2 HIS A 465 36.033 -12.729 3.209 1.00 35.64 N ANISOU 3337 NE2 HIS A 465 7454 3383 2704 -2505 755 -354 N ATOM 3338 N ARG A 466 33.200 -9.094 3.211 1.00 43.61 N ANISOU 3338 N ARG A 466 8309 4395 3867 -2526 624 -396 N ATOM 3339 CA ARG A 466 32.628 -8.746 4.494 1.00 42.14 C ANISOU 3339 CA ARG A 466 8136 4180 3693 -2524 661 -429 C ATOM 3340 C ARG A 466 32.089 -7.317 4.500 1.00 49.88 C ANISOU 3340 C ARG A 466 9103 5127 4721 -2515 606 -456 C ATOM 3341 O ARG A 466 31.675 -6.808 5.549 1.00 53.17 O ANISOU 3341 O ARG A 466 9555 5507 5140 -2508 634 -501 O ATOM 3342 CB ARG A 466 33.692 -8.964 5.551 1.00 36.00 C ANISOU 3342 CB ARG A 466 7418 3402 2858 -2510 690 -425 C ATOM 3343 CG ARG A 466 34.443 -10.232 5.265 1.00 35.77 C ANISOU 3343 CG ARG A 466 7408 3393 2789 -2510 721 -395 C ATOM 3344 CD ARG A 466 35.543 -10.335 6.216 1.00 37.24 C ANISOU 3344 CD ARG A 466 7648 3573 2930 -2502 730 -383 C ATOM 3345 NE ARG A 466 35.057 -10.257 7.580 1.00 36.06 N ANISOU 3345 NE ARG A 466 7543 3398 2760 -2509 770 -409 N ATOM 3346 CZ ARG A 466 34.680 -11.326 8.263 1.00 38.49 C ANISOU 3346 CZ ARG A 466 7884 3697 3043 -2524 839 -406 C ATOM 3347 NH1 ARG A 466 34.793 -12.513 7.669 1.00 42.60 N ANISOU 3347 NH1 ARG A 466 8396 4227 3563 -2522 857 -383 N ATOM 3348 NH2 ARG A 466 34.229 -11.217 9.514 1.00 36.74 N ANISOU 3348 NH2 ARG A 466 7701 3470 2789 -2523 885 -424 N ATOM 3349 N ALA A 467 32.090 -6.664 3.339 1.00 41.82 N ANISOU 3349 N ALA A 467 8047 4109 3732 -2515 527 -433 N ATOM 3350 CA ALA A 467 31.332 -5.448 3.109 1.00 41.48 C ANISOU 3350 CA ALA A 467 7989 4022 3750 -2510 463 -456 C ATOM 3351 C ALA A 467 29.833 -5.674 3.034 1.00 43.08 C ANISOU 3351 C ALA A 467 8152 4200 4016 -2542 487 -485 C ATOM 3352 O ALA A 467 29.083 -4.713 2.836 1.00 37.92 O ANISOU 3352 O ALA A 467 7471 3512 3425 -2522 434 -504 O ATOM 3353 CB ALA A 467 31.778 -4.819 1.809 1.00 37.50 C ANISOU 3353 CB ALA A 467 7466 3529 3255 -2515 368 -409 C ATOM 3354 N GLY A 468 29.368 -6.899 3.169 1.00 47.96 N ANISOU 3354 N GLY A 468 8748 4846 4628 -2577 558 -479 N ATOM 3355 CA GLY A 468 27.978 -7.191 2.897 1.00 48.48 C ANISOU 3355 CA GLY A 468 8735 4921 4765 -2603 566 -477 C ATOM 3356 C GLY A 468 27.099 -6.795 4.050 1.00 52.08 C ANISOU 3356 C GLY A 468 9126 5404 5257 -2530 634 -506 C ATOM 3357 O GLY A 468 27.358 -5.812 4.764 1.00 50.72 O ANISOU 3357 O GLY A 468 8982 5216 5074 -2453 635 -542 O ATOM 3358 N TRP A 469 26.032 -7.577 4.221 1.00 52.55 N ANISOU 3358 N TRP A 469 9102 5506 5359 -2556 690 -487 N ATOM 3359 CA TRP A 469 25.269 -7.621 5.456 1.00 49.58 C ANISOU 3359 CA TRP A 469 8664 5181 4994 -2500 798 -502 C ATOM 3360 C TRP A 469 25.936 -8.612 6.405 1.00 46.04 C ANISOU 3360 C TRP A 469 8291 4749 4455 -2524 887 -497 C ATOM 3361 O TRP A 469 26.175 -9.767 6.041 1.00 45.66 O ANISOU 3361 O TRP A 469 8272 4694 4383 -2607 889 -461 O ATOM 3362 CB TRP A 469 23.815 -8.030 5.183 1.00 50.03 C ANISOU 3362 CB TRP A 469 8578 5288 5144 -2532 816 -466 C ATOM 3363 CG TRP A 469 23.091 -7.108 4.265 1.00 50.79 C ANISOU 3363 CG TRP A 469 8591 5370 5339 -2505 718 -463 C ATOM 3364 CD1 TRP A 469 22.676 -7.384 3.011 1.00 55.21 C ANISOU 3364 CD1 TRP A 469 9111 5913 5952 -2587 618 -421 C ATOM 3365 CD2 TRP A 469 22.737 -5.739 4.517 1.00 52.59 C ANISOU 3365 CD2 TRP A 469 8781 5586 5616 -2386 699 -503 C ATOM 3366 NE1 TRP A 469 22.062 -6.285 2.458 1.00 61.44 N ANISOU 3366 NE1 TRP A 469 9830 6687 6828 -2531 534 -424 N ATOM 3367 CE2 TRP A 469 22.095 -5.257 3.359 1.00 58.65 C ANISOU 3367 CE2 TRP A 469 9475 6332 6477 -2402 582 -475 C ATOM 3368 CE3 TRP A 469 22.906 -4.874 5.608 1.00 49.98 C ANISOU 3368 CE3 TRP A 469 8486 5252 5254 -2265 762 -562 C ATOM 3369 CZ2 TRP A 469 21.616 -3.950 3.254 1.00 60.06 C ANISOU 3369 CZ2 TRP A 469 9608 6484 6729 -2296 526 -500 C ATOM 3370 CZ3 TRP A 469 22.431 -3.580 5.508 1.00 53.75 C ANISOU 3370 CZ3 TRP A 469 8928 5698 5799 -2157 711 -596 C ATOM 3371 CH2 TRP A 469 21.790 -3.129 4.336 1.00 59.77 C ANISOU 3371 CH2 TRP A 469 9609 6436 6664 -2170 593 -563 C ATOM 3372 N LYS A 470 26.248 -8.163 7.615 1.00 46.69 N ANISOU 3372 N LYS A 470 8418 4842 4480 -2450 952 -533 N ATOM 3373 CA LYS A 470 26.792 -9.067 8.611 1.00 48.51 C ANISOU 3373 CA LYS A 470 8719 5090 4622 -2470 1033 -521 C ATOM 3374 C LYS A 470 26.121 -8.819 9.952 1.00 54.39 C ANISOU 3374 C LYS A 470 9439 5889 5337 -2400 1146 -545 C ATOM 3375 O LYS A 470 25.610 -7.726 10.220 1.00 55.29 O ANISOU 3375 O LYS A 470 9518 6011 5479 -2309 1154 -590 O ATOM 3376 CB LYS A 470 28.310 -8.918 8.754 1.00 49.10 C ANISOU 3376 CB LYS A 470 8918 5118 4619 -2464 984 -533 C ATOM 3377 CG LYS A 470 29.108 -9.380 7.545 1.00 50.31 C ANISOU 3377 CG LYS A 470 9102 5234 4780 -2529 904 -503 C ATOM 3378 CD LYS A 470 30.556 -9.510 7.933 1.00 46.17 C ANISOU 3378 CD LYS A 470 8676 4687 4178 -2523 886 -498 C ATOM 3379 CE LYS A 470 30.735 -10.667 8.860 1.00 41.06 C ANISOU 3379 CE LYS A 470 8071 4056 3472 -2541 963 -475 C ATOM 3380 NZ LYS A 470 30.547 -11.918 8.043 1.00 38.44 N ANISOU 3380 NZ LYS A 470 7731 3712 3161 -2610 966 -437 N ATOM 3381 N ASP A 471 26.124 -9.867 10.787 1.00 53.13 N ANISOU 3381 N ASP A 471 9306 5765 5116 -2441 1235 -512 N ATOM 3382 CA ASP A 471 25.685 -9.796 12.173 1.00 50.30 C ANISOU 3382 CA ASP A 471 8954 5465 4693 -2385 1356 -527 C ATOM 3383 C ASP A 471 26.792 -10.196 13.144 1.00 49.35 C ANISOU 3383 C ASP A 471 8979 5324 4448 -2388 1374 -528 C ATOM 3384 O ASP A 471 26.493 -10.603 14.263 1.00 52.77 O ANISOU 3384 O ASP A 471 9436 5807 4808 -2381 1478 -516 O ATOM 3385 CB ASP A 471 24.424 -10.648 12.394 1.00 49.95 C ANISOU 3385 CB ASP A 471 8788 5501 4689 -2437 1458 -470 C ATOM 3386 CG ASP A 471 24.627 -12.158 12.129 1.00 49.90 C ANISOU 3386 CG ASP A 471 8806 5479 4672 -2567 1450 -395 C ATOM 3387 OD1 ASP A 471 25.564 -12.782 12.679 1.00 50.71 O ANISOU 3387 OD1 ASP A 471 9032 5550 4684 -2591 1454 -383 O ATOM 3388 OD2 ASP A 471 23.778 -12.747 11.423 1.00 48.77 O ANISOU 3388 OD2 ASP A 471 8560 5355 4614 -2646 1438 -345 O ATOM 3389 N THR A 472 28.061 -10.081 12.742 1.00 49.83 N ANISOU 3389 N THR A 472 9132 5318 4484 -2401 1273 -535 N ATOM 3390 CA THR A 472 29.205 -10.455 13.570 1.00 50.70 C ANISOU 3390 CA THR A 472 9369 5406 4490 -2407 1265 -526 C ATOM 3391 C THR A 472 30.393 -9.622 13.087 1.00 49.27 C ANISOU 3391 C THR A 472 9249 5165 4308 -2385 1144 -552 C ATOM 3392 O THR A 472 30.521 -9.387 11.880 1.00 50.45 O ANISOU 3392 O THR A 472 9350 5287 4532 -2407 1071 -547 O ATOM 3393 CB THR A 472 29.515 -11.980 13.481 1.00 53.22 C ANISOU 3393 CB THR A 472 9710 5718 4792 -2493 1280 -457 C ATOM 3394 OG1 THR A 472 28.459 -12.785 14.059 1.00 52.44 O ANISOU 3394 OG1 THR A 472 9564 5674 4685 -2532 1389 -418 O ATOM 3395 CG2 THR A 472 30.819 -12.316 14.200 1.00 54.67 C ANISOU 3395 CG2 THR A 472 10016 5871 4884 -2491 1248 -441 C ATOM 3396 N VAL A 473 31.258 -9.172 14.011 1.00 44.33 N ANISOU 3396 N VAL A 473 8730 4519 3595 -2352 1118 -574 N ATOM 3397 CA VAL A 473 32.413 -8.351 13.651 1.00 39.32 C ANISOU 3397 CA VAL A 473 8147 3832 2960 -2345 997 -586 C ATOM 3398 C VAL A 473 33.636 -8.859 14.378 1.00 39.20 C ANISOU 3398 C VAL A 473 8225 3805 2863 -2367 963 -551 C ATOM 3399 O VAL A 473 33.603 -8.988 15.603 1.00 42.38 O ANISOU 3399 O VAL A 473 8706 4221 3175 -2347 1008 -561 O ATOM 3400 CB VAL A 473 32.242 -6.884 14.056 1.00 48.68 C ANISOU 3400 CB VAL A 473 9378 4988 4132 -2274 958 -655 C ATOM 3401 CG1 VAL A 473 33.190 -5.983 13.225 1.00 44.82 C ANISOU 3401 CG1 VAL A 473 8903 4441 3684 -2292 819 -652 C ATOM 3402 CG2 VAL A 473 30.813 -6.482 14.052 1.00 54.15 C ANISOU 3402 CG2 VAL A 473 9998 5709 4869 -2216 1038 -698 C ATOM 3403 N LYS A 474 34.747 -9.025 13.656 1.00 46.04 N ANISOU 3403 N LYS A 474 9086 4649 3758 -2403 878 -510 N ATOM 3404 CA LYS A 474 35.999 -9.387 14.320 1.00 42.17 C ANISOU 3404 CA LYS A 474 8668 4150 3205 -2417 828 -470 C ATOM 3405 C LYS A 474 36.444 -8.270 15.246 1.00 45.74 C ANISOU 3405 C LYS A 474 9212 4576 3592 -2390 760 -507 C ATOM 3406 O LYS A 474 36.433 -7.096 14.872 1.00 45.87 O ANISOU 3406 O LYS A 474 9227 4561 3639 -2377 694 -544 O ATOM 3407 CB LYS A 474 37.118 -9.674 13.317 1.00 37.79 C ANISOU 3407 CB LYS A 474 8069 3588 2700 -2448 756 -417 C ATOM 3408 CG LYS A 474 38.436 -10.122 13.999 1.00 40.02 C ANISOU 3408 CG LYS A 474 8403 3870 2933 -2455 701 -363 C ATOM 3409 CD LYS A 474 39.644 -9.890 13.098 1.00 46.60 C ANISOU 3409 CD LYS A 474 9181 4707 3818 -2473 617 -316 C ATOM 3410 CE LYS A 474 40.877 -10.723 13.456 1.00 48.91 C ANISOU 3410 CE LYS A 474 9480 5013 4092 -2471 584 -245 C ATOM 3411 NZ LYS A 474 41.165 -11.889 12.517 1.00 53.32 N ANISOU 3411 NZ LYS A 474 9980 5584 4695 -2457 633 -206 N ATOM 3412 N VAL A 475 36.843 -8.638 16.457 1.00 39.68 N ANISOU 3412 N VAL A 475 8537 3812 2728 -2388 764 -494 N ATOM 3413 CA VAL A 475 37.540 -7.742 17.369 1.00 40.35 C ANISOU 3413 CA VAL A 475 8732 3863 2736 -2379 672 -517 C ATOM 3414 C VAL A 475 38.692 -8.567 17.925 1.00 40.44 C ANISOU 3414 C VAL A 475 8784 3881 2701 -2413 619 -443 C ATOM 3415 O VAL A 475 38.461 -9.564 18.606 1.00 46.73 O ANISOU 3415 O VAL A 475 9616 4699 3438 -2413 691 -417 O ATOM 3416 CB VAL A 475 36.631 -7.220 18.500 1.00 43.92 C ANISOU 3416 CB VAL A 475 9284 4314 3091 -2324 739 -592 C ATOM 3417 CG1 VAL A 475 37.315 -6.116 19.271 1.00 42.20 C ANISOU 3417 CG1 VAL A 475 9171 4043 2819 -2303 622 -616 C ATOM 3418 CG2 VAL A 475 35.288 -6.719 17.963 1.00 43.34 C ANISOU 3418 CG2 VAL A 475 9138 4251 3077 -2274 827 -653 C ATOM 3419 N GLU A 476 39.920 -8.208 17.589 1.00 42.80 N ANISOU 3419 N GLU A 476 9066 4163 3032 -2445 494 -398 N ATOM 3420 CA GLU A 476 41.092 -8.948 18.097 1.00 49.88 C ANISOU 3420 CA GLU A 476 9984 5069 3899 -2470 429 -319 C ATOM 3421 C GLU A 476 42.205 -7.940 18.431 1.00 49.83 C ANISOU 3421 C GLU A 476 10022 5035 3877 -2505 267 -299 C ATOM 3422 O GLU A 476 43.120 -7.692 17.643 1.00 46.31 O ANISOU 3422 O GLU A 476 9487 4598 3509 -2538 185 -243 O ATOM 3423 CB GLU A 476 41.578 -10.021 17.108 1.00 52.84 C ANISOU 3423 CB GLU A 476 10243 5473 4360 -2475 457 -249 C ATOM 3424 CG GLU A 476 42.458 -11.119 17.725 1.00 56.23 C ANISOU 3424 CG GLU A 476 10695 5911 4758 -2474 431 -172 C ATOM 3425 CD GLU A 476 43.009 -12.117 16.703 1.00 61.67 C ANISOU 3425 CD GLU A 476 11278 6619 5533 -2458 456 -112 C ATOM 3426 OE1 GLU A 476 42.771 -11.931 15.498 1.00 64.50 O ANISOU 3426 OE1 GLU A 476 11552 6989 5966 -2456 490 -130 O ATOM 3427 OE2 GLU A 476 43.686 -13.091 17.095 1.00 63.24 O ANISOU 3427 OE2 GLU A 476 11488 6818 5721 -2441 440 -49 O ATOM 3428 N GLY A 477 42.130 -7.360 19.630 1.00 51.58 N ANISOU 3428 N GLY A 477 10387 5223 3989 -2503 219 -340 N ATOM 3429 CA GLY A 477 43.156 -6.450 20.088 1.00 50.81 C ANISOU 3429 CA GLY A 477 10357 5087 3864 -2549 48 -320 C ATOM 3430 C GLY A 477 43.046 -5.031 19.578 1.00 48.04 C ANISOU 3430 C GLY A 477 10006 4687 3559 -2558 -27 -365 C ATOM 3431 O GLY A 477 43.828 -4.178 20.018 1.00 48.81 O ANISOU 3431 O GLY A 477 10158 4746 3643 -2592 -177 -340 O ATOM 3432 N ASN A 478 42.081 -4.742 18.699 1.00 46.42 N ANISOU 3432 N ASN A 478 9724 4487 3427 -2513 67 -411 N ATOM 3433 CA ASN A 478 41.921 -3.435 18.063 1.00 42.20 C ANISOU 3433 CA ASN A 478 9155 3915 2965 -2498 1 -430 C ATOM 3434 C ASN A 478 40.470 -2.962 18.106 1.00 48.90 C ANISOU 3434 C ASN A 478 10018 4745 3816 -2403 109 -520 C ATOM 3435 O ASN A 478 39.705 -3.342 18.993 1.00 51.29 O ANISOU 3435 O ASN A 478 10389 5057 4042 -2348 209 -572 O ATOM 3436 CB ASN A 478 42.423 -3.523 16.620 1.00 48.08 C ANISOU 3436 CB ASN A 478 9764 4688 3816 -2557 -22 -373 C ATOM 3437 CG ASN A 478 43.081 -2.268 16.140 1.00 41.65 C ANISOU 3437 CG ASN A 478 8925 3843 3059 -2594 -167 -333 C ATOM 3438 OD1 ASN A 478 42.423 -1.293 15.794 1.00 41.79 O ANISOU 3438 OD1 ASN A 478 8940 3825 3113 -2547 -177 -372 O ATOM 3439 ND2 ASN A 478 44.396 -2.271 16.150 1.00 42.89 N ANISOU 3439 ND2 ASN A 478 9064 4010 3224 -2684 -288 -251 N ATOM 3440 N VAL A 479 40.063 -2.137 17.154 1.00 42.04 N ANISOU 3440 N VAL A 479 9086 3856 3032 -2385 90 -538 N ATOM 3441 CA VAL A 479 38.760 -1.489 17.208 1.00 42.44 C ANISOU 3441 CA VAL A 479 9161 3875 3088 -2296 162 -630 C ATOM 3442 C VAL A 479 38.004 -1.709 15.905 1.00 43.39 C ANISOU 3442 C VAL A 479 9162 4023 3303 -2296 236 -636 C ATOM 3443 O VAL A 479 38.561 -1.551 14.811 1.00 40.85 O ANISOU 3443 O VAL A 479 8750 3710 3060 -2348 170 -574 O ATOM 3444 CB VAL A 479 38.905 0.016 17.476 1.00 43.45 C ANISOU 3444 CB VAL A 479 9369 3920 3220 -2258 35 -660 C ATOM 3445 CG1 VAL A 479 37.545 0.719 17.385 1.00 43.95 C ANISOU 3445 CG1 VAL A 479 9456 3943 3300 -2156 106 -762 C ATOM 3446 CG2 VAL A 479 39.587 0.234 18.805 1.00 50.89 C ANISOU 3446 CG2 VAL A 479 10444 4830 4063 -2258 -44 -657 C ATOM 3447 N SER A 480 36.723 -2.049 16.026 1.00 41.59 N ANISOU 3447 N SER A 480 8931 3810 3060 -2242 371 -708 N ATOM 3448 CA SER A 480 35.834 -2.120 14.884 1.00 42.21 C ANISOU 3448 CA SER A 480 8913 3900 3224 -2240 428 -727 C ATOM 3449 C SER A 480 34.745 -1.069 15.032 1.00 46.09 C ANISOU 3449 C SER A 480 9453 4338 3723 -2153 445 -824 C ATOM 3450 O SER A 480 34.453 -0.603 16.136 1.00 53.25 O ANISOU 3450 O SER A 480 10468 5216 4547 -2080 467 -891 O ATOM 3451 CB SER A 480 35.217 -3.515 14.758 1.00 42.81 C ANISOU 3451 CB SER A 480 8925 4047 3294 -2262 570 -717 C ATOM 3452 OG SER A 480 36.175 -4.515 15.046 1.00 42.07 O ANISOU 3452 OG SER A 480 8839 3987 3160 -2319 565 -651 O ATOM 3453 N GLU A 481 34.142 -0.711 13.904 1.00 44.29 N ANISOU 3453 N GLU A 481 9148 4091 3589 -2155 435 -833 N ATOM 3454 CA GLU A 481 33.011 0.203 13.842 1.00 50.32 C ANISOU 3454 CA GLU A 481 9917 4811 4391 -2057 454 -911 C ATOM 3455 C GLU A 481 32.000 -0.308 12.830 1.00 51.75 C ANISOU 3455 C GLU A 481 9937 5051 4676 -2051 531 -886 C ATOM 3456 O GLU A 481 32.355 -0.561 11.669 1.00 51.25 O ANISOU 3456 O GLU A 481 9796 4997 4681 -2129 476 -820 O ATOM 3457 CB GLU A 481 33.468 1.611 13.461 1.00 58.19 C ANISOU 3457 CB GLU A 481 10978 5703 5428 -2049 292 -919 C ATOM 3458 CG GLU A 481 32.350 2.611 13.258 1.00 63.03 C ANISOU 3458 CG GLU A 481 11612 6245 6090 -1947 291 -1003 C ATOM 3459 CD GLU A 481 32.862 4.022 13.220 1.00 69.97 C ANISOU 3459 CD GLU A 481 12588 7011 6989 -1922 126 -1012 C ATOM 3460 OE1 GLU A 481 33.996 4.233 12.739 1.00 72.34 O ANISOU 3460 OE1 GLU A 481 12848 7317 7321 -2001 2 -908 O ATOM 3461 OE2 GLU A 481 32.134 4.920 13.682 1.00 73.02 O ANISOU 3461 OE2 GLU A 481 13075 7309 7360 -1811 124 -1115 O ATOM 3462 N VAL A 482 30.746 -0.449 13.276 1.00 49.06 N ANISOU 3462 N VAL A 482 9547 4753 4341 -1959 656 -934 N ATOM 3463 CA VAL A 482 29.656 -0.930 12.438 1.00 46.50 C ANISOU 3463 CA VAL A 482 9063 4488 4116 -1952 726 -908 C ATOM 3464 C VAL A 482 28.536 0.104 12.387 1.00 46.51 C ANISOU 3464 C VAL A 482 9034 4456 4181 -1830 734 -973 C ATOM 3465 O VAL A 482 28.297 0.857 13.341 1.00 54.77 O ANISOU 3465 O VAL A 482 10176 5464 5170 -1722 760 -1052 O ATOM 3466 CB VAL A 482 29.118 -2.285 12.938 1.00 48.81 C ANISOU 3466 CB VAL A 482 9283 4886 4377 -1973 877 -879 C ATOM 3467 CG1 VAL A 482 30.252 -3.217 13.199 1.00 49.30 C ANISOU 3467 CG1 VAL A 482 9402 4964 4367 -2067 866 -826 C ATOM 3468 CG2 VAL A 482 28.313 -2.108 14.213 1.00 51.72 C ANISOU 3468 CG2 VAL A 482 9684 5290 4677 -1864 1004 -944 C ATOM 3469 N LEU A 483 27.843 0.129 11.251 1.00 44.01 N ANISOU 3469 N LEU A 483 8589 4152 3982 -1841 708 -939 N ATOM 3470 CA LEU A 483 26.677 0.977 11.038 1.00 44.62 C ANISOU 3470 CA LEU A 483 8600 4208 4146 -1723 713 -982 C ATOM 3471 C LEU A 483 25.438 0.105 11.177 1.00 57.30 C ANISOU 3471 C LEU A 483 10044 5930 5796 -1696 864 -963 C ATOM 3472 O LEU A 483 25.194 -0.779 10.348 1.00 57.86 O ANISOU 3472 O LEU A 483 10000 6057 5926 -1791 867 -891 O ATOM 3473 CB LEU A 483 26.736 1.641 9.666 1.00 44.22 C ANISOU 3473 CB LEU A 483 8514 4089 4198 -1761 564 -945 C ATOM 3474 CG LEU A 483 25.850 2.865 9.445 1.00 49.36 C ANISOU 3474 CG LEU A 483 9148 4672 4937 -1631 512 -994 C ATOM 3475 CD1 LEU A 483 26.010 3.780 10.642 1.00 56.74 C ANISOU 3475 CD1 LEU A 483 10234 5532 5793 -1508 524 -1093 C ATOM 3476 CD2 LEU A 483 26.246 3.616 8.187 1.00 45.12 C ANISOU 3476 CD2 LEU A 483 8629 4042 4470 -1690 334 -950 C ATOM 3477 N VAL A 484 24.657 0.346 12.224 1.00 60.43 N ANISOU 3477 N VAL A 484 10436 6366 6160 -1569 988 -1025 N ATOM 3478 CA VAL A 484 23.574 -0.556 12.583 1.00 60.03 C ANISOU 3478 CA VAL A 484 10234 6444 6130 -1555 1150 -996 C ATOM 3479 C VAL A 484 22.275 0.233 12.693 1.00 63.85 C ANISOU 3479 C VAL A 484 10610 6951 6699 -1394 1212 -1042 C ATOM 3480 O VAL A 484 22.275 1.413 13.061 1.00 64.11 O ANISOU 3480 O VAL A 484 10740 6902 6717 -1260 1178 -1126 O ATOM 3481 CB VAL A 484 23.904 -1.272 13.898 1.00 61.66 C ANISOU 3481 CB VAL A 484 10525 6710 6192 -1564 1281 -1010 C ATOM 3482 CG1 VAL A 484 24.188 -0.256 14.978 1.00 62.42 C ANISOU 3482 CG1 VAL A 484 10789 6744 6183 -1435 1294 -1112 C ATOM 3483 CG2 VAL A 484 22.795 -2.188 14.289 1.00 67.43 C ANISOU 3483 CG2 VAL A 484 11101 7577 6943 -1563 1450 -967 C ATOM 3484 N LYS A 485 21.159 -0.426 12.354 1.00 69.14 N ANISOU 3484 N LYS A 485 11077 7729 7464 -1408 1296 -982 N ATOM 3485 CA LYS A 485 19.821 0.162 12.453 1.00 73.21 C ANISOU 3485 CA LYS A 485 11443 8297 8078 -1256 1372 -1006 C ATOM 3486 C LYS A 485 18.820 -0.944 12.762 1.00 77.89 C ANISOU 3486 C LYS A 485 11844 9050 8701 -1297 1534 -935 C ATOM 3487 O LYS A 485 18.731 -1.920 12.008 1.00 83.47 O ANISOU 3487 O LYS A 485 12452 9799 9465 -1451 1496 -843 O ATOM 3488 CB LYS A 485 19.465 0.903 11.154 1.00 75.63 C ANISOU 3488 CB LYS A 485 11669 8531 8536 -1239 1213 -986 C ATOM 3489 CG LYS A 485 17.991 0.898 10.735 1.00 77.11 C ANISOU 3489 CG LYS A 485 11611 8810 8878 -1171 1262 -941 C ATOM 3490 CD LYS A 485 17.749 1.709 9.448 1.00 76.77 C ANISOU 3490 CD LYS A 485 11518 8678 8974 -1155 1078 -920 C ATOM 3491 CE LYS A 485 16.278 1.676 9.052 1.00 80.09 C ANISOU 3491 CE LYS A 485 11681 9193 9556 -1088 1116 -866 C ATOM 3492 NZ LYS A 485 15.648 3.034 8.852 1.00 80.29 N ANISOU 3492 NZ LYS A 485 11672 9147 9687 -892 1052 -918 N ATOM 3493 N PHE A 486 18.081 -0.805 13.867 1.00 75.92 N ANISOU 3493 N PHE A 486 11550 8891 8407 -1164 1714 -976 N ATOM 3494 CA PHE A 486 17.098 -1.804 14.283 1.00 76.32 C ANISOU 3494 CA PHE A 486 11411 9107 8479 -1202 1885 -900 C ATOM 3495 C PHE A 486 15.698 -1.324 13.945 1.00 77.09 C ANISOU 3495 C PHE A 486 11272 9284 8737 -1080 1934 -881 C ATOM 3496 O PHE A 486 15.335 -0.192 14.269 1.00 81.44 O ANISOU 3496 O PHE A 486 11838 9802 9304 -880 1961 -968 O ATOM 3497 CB PHE A 486 17.174 -2.093 15.779 1.00 73.86 C ANISOU 3497 CB PHE A 486 11192 8872 8001 -1147 2075 -940 C ATOM 3498 CG PHE A 486 18.573 -2.111 16.333 1.00 69.12 C ANISOU 3498 CG PHE A 486 10858 8172 7234 -1197 2018 -993 C ATOM 3499 CD1 PHE A 486 19.177 -0.954 16.768 1.00 66.17 C ANISOU 3499 CD1 PHE A 486 10677 7684 6780 -1068 1963 -1108 C ATOM 3500 CD2 PHE A 486 19.272 -3.296 16.459 1.00 65.09 C ANISOU 3500 CD2 PHE A 486 10406 7679 6646 -1372 2014 -924 C ATOM 3501 CE1 PHE A 486 20.455 -0.990 17.300 1.00 59.61 C ANISOU 3501 CE1 PHE A 486 10079 6768 5801 -1126 1900 -1145 C ATOM 3502 CE2 PHE A 486 20.557 -3.320 16.989 1.00 58.81 C ANISOU 3502 CE2 PHE A 486 9840 6800 5706 -1414 1957 -963 C ATOM 3503 CZ PHE A 486 21.138 -2.176 17.407 1.00 54.02 C ANISOU 3503 CZ PHE A 486 9408 6091 5026 -1297 1898 -1069 C ATOM 3504 N ASN A 487 14.916 -2.186 13.304 1.00 78.13 N ANISOU 3504 N ASN A 487 11187 9513 8987 -1198 1938 -767 N ATOM 3505 CA ASN A 487 13.578 -1.839 12.852 1.00 83.72 C ANISOU 3505 CA ASN A 487 11637 10304 9869 -1109 1960 -723 C ATOM 3506 C ASN A 487 12.508 -2.568 13.639 1.00 88.62 C ANISOU 3506 C ASN A 487 12052 11119 10501 -1104 2176 -653 C ATOM 3507 O ASN A 487 11.384 -2.713 13.153 1.00 94.13 O ANISOU 3507 O ASN A 487 12491 11917 11359 -1105 2188 -570 O ATOM 3508 CB ASN A 487 13.418 -2.148 11.363 1.00 84.12 C ANISOU 3508 CB ASN A 487 11582 10314 10067 -1254 1766 -635 C ATOM 3509 CG ASN A 487 14.654 -1.820 10.571 1.00 82.72 C ANISOU 3509 CG ASN A 487 11618 9966 9844 -1328 1567 -673 C ATOM 3510 OD1 ASN A 487 15.209 -0.730 10.697 1.00 83.29 O ANISOU 3510 OD1 ASN A 487 11842 9927 9877 -1203 1510 -768 O ATOM 3511 ND2 ASN A 487 15.116 -2.771 9.770 1.00 80.89 N ANISOU 3511 ND2 ASN A 487 11409 9711 9613 -1532 1464 -600 N ATOM 3512 N HIS A 488 12.837 -3.055 14.829 1.00 91.18 N ANISOU 3512 N HIS A 488 12481 11503 10660 -1110 2340 -675 N ATOM 3513 CA HIS A 488 11.918 -3.909 15.564 1.00 95.90 C ANISOU 3513 CA HIS A 488 12894 12290 11253 -1147 2545 -586 C ATOM 3514 C HIS A 488 12.041 -3.600 17.049 1.00103.03 C ANISOU 3514 C HIS A 488 13922 13250 11975 -1000 2754 -672 C ATOM 3515 O HIS A 488 13.146 -3.381 17.550 1.00102.20 O ANISOU 3515 O HIS A 488 14086 13035 11709 -990 2721 -760 O ATOM 3516 CB HIS A 488 12.199 -5.390 15.256 1.00 94.82 C ANISOU 3516 CB HIS A 488 12747 12178 11100 -1415 2502 -465 C ATOM 3517 CG HIS A 488 11.879 -5.773 13.839 1.00 95.68 C ANISOU 3517 CG HIS A 488 12717 12254 11382 -1559 2317 -375 C ATOM 3518 ND1 HIS A 488 10.615 -6.147 13.434 1.00 98.37 N ANISOU 3518 ND1 HIS A 488 12768 12722 11884 -1606 2345 -262 N ATOM 3519 CD2 HIS A 488 12.649 -5.786 12.722 1.00 93.66 C ANISOU 3519 CD2 HIS A 488 12576 11852 11159 -1661 2098 -382 C ATOM 3520 CE1 HIS A 488 10.627 -6.400 12.136 1.00 97.13 C ANISOU 3520 CE1 HIS A 488 12569 12491 11845 -1738 2140 -206 C ATOM 3521 NE2 HIS A 488 11.850 -6.187 11.680 1.00 93.93 N ANISOU 3521 NE2 HIS A 488 12409 11921 11358 -1768 1996 -280 N ATOM 3522 N ASP A 489 10.898 -3.552 17.736 1.00105.22 N ANISOU 3522 N ASP A 489 14001 13700 12278 -884 2967 -644 N ATOM 3523 CA ASP A 489 10.851 -3.119 19.128 1.00101.52 C ANISOU 3523 CA ASP A 489 13639 13297 11637 -708 3184 -735 C ATOM 3524 C ASP A 489 11.409 -4.199 20.055 1.00 94.10 C ANISOU 3524 C ASP A 489 12836 12412 10507 -862 3290 -689 C ATOM 3525 O ASP A 489 11.160 -5.392 19.865 1.00 91.88 O ANISOU 3525 O ASP A 489 12432 12216 10264 -1067 3304 -550 O ATOM 3526 CB ASP A 489 9.404 -2.783 19.526 1.00107.47 C ANISOU 3526 CB ASP A 489 14111 14239 12482 -533 3395 -707 C ATOM 3527 CG ASP A 489 8.905 -1.452 18.947 1.00111.29 C ANISOU 3527 CG ASP A 489 14513 14657 13114 -301 3322 -792 C ATOM 3528 OD1 ASP A 489 9.688 -0.485 18.897 1.00112.52 O ANISOU 3528 OD1 ASP A 489 14911 14634 13208 -185 3205 -929 O ATOM 3529 OD2 ASP A 489 7.718 -1.369 18.551 1.00114.05 O ANISOU 3529 OD2 ASP A 489 14555 15133 13646 -237 3377 -716 O ATOM 3530 N ALA A 490 12.175 -3.771 21.072 1.00 95.04 N ANISOU 3530 N ALA A 490 13223 12471 10416 -764 3354 -805 N ATOM 3531 CA ALA A 490 12.621 -4.662 22.145 1.00 97.92 C ANISOU 3531 CA ALA A 490 13727 12899 10579 -871 3479 -769 C ATOM 3532 C ALA A 490 12.606 -3.956 23.502 1.00102.41 C ANISOU 3532 C ALA A 490 14456 13509 10945 -665 3670 -889 C ATOM 3533 O ALA A 490 13.318 -2.961 23.693 1.00 97.63 O ANISOU 3533 O ALA A 490 14082 12757 10255 -530 3586 -1034 O ATOM 3534 CB ALA A 490 14.019 -5.216 21.865 1.00 90.24 C ANISOU 3534 CB ALA A 490 12989 11769 9527 -1054 3285 -765 C ATOM 3535 N PRO A 491 11.797 -4.459 24.480 1.00110.61 N ANISOU 3535 N PRO A 491 15385 14748 11894 -641 3931 -829 N ATOM 3536 CA PRO A 491 11.714 -3.827 25.810 1.00113.59 C ANISOU 3536 CA PRO A 491 15921 15180 12057 -438 4136 -944 C ATOM 3537 C PRO A 491 12.607 -4.452 26.876 1.00109.08 C ANISOU 3537 C PRO A 491 15624 14595 11228 -544 4180 -946 C ATOM 3538 O PRO A 491 13.160 -5.534 26.663 1.00109.10 O ANISOU 3538 O PRO A 491 15654 14575 11223 -781 4085 -836 O ATOM 3539 CB PRO A 491 10.245 -4.037 26.181 1.00118.20 C ANISOU 3539 CB PRO A 491 16195 16012 12704 -355 4404 -859 C ATOM 3540 CG PRO A 491 9.928 -5.382 25.558 1.00117.83 C ANISOU 3540 CG PRO A 491 15928 16053 12790 -632 4360 -658 C ATOM 3541 CD PRO A 491 10.717 -5.447 24.276 1.00113.29 C ANISOU 3541 CD PRO A 491 15407 15281 12357 -770 4051 -654 C ATOM 3542 N LYS A 492 12.713 -3.802 28.042 1.00105.61 N ANISOU 3542 N LYS A 492 15389 14170 10570 -365 4326 -1069 N ATOM 3543 CA LYS A 492 13.486 -4.364 29.145 1.00100.15 C ANISOU 3543 CA LYS A 492 14960 13477 9616 -455 4378 -1069 C ATOM 3544 C LYS A 492 13.084 -5.806 29.413 1.00100.74 C ANISOU 3544 C LYS A 492 14884 13719 9675 -671 4499 -879 C ATOM 3545 O LYS A 492 13.937 -6.640 29.741 1.00100.09 O ANISOU 3545 O LYS A 492 14973 13584 9472 -853 4421 -820 O ATOM 3546 CB LYS A 492 13.312 -3.492 30.401 1.00 96.77 C ANISOU 3546 CB LYS A 492 14724 13087 8956 -214 4571 -1216 C ATOM 3547 CG LYS A 492 13.324 -4.233 31.759 1.00 94.55 C ANISOU 3547 CG LYS A 492 14574 12944 8406 -272 4779 -1166 C ATOM 3548 CD LYS A 492 12.531 -3.469 32.837 1.00 93.57 C ANISOU 3548 CD LYS A 492 14458 12950 8142 -2 5012 -1263 C ATOM 3549 CE LYS A 492 12.377 -4.268 34.129 1.00 92.96 C ANISOU 3549 CE LYS A 492 14386 13042 7893 -57 5108 -1161 C ATOM 3550 NZ LYS A 492 13.672 -4.552 34.817 1.00 91.86 N ANISOU 3550 NZ LYS A 492 14545 12765 7593 -165 4884 -1173 N ATOM 3551 N GLU A 493 11.800 -6.124 29.234 1.00106.79 N ANISOU 3551 N GLU A 493 15323 14678 10573 -661 4675 -773 N ATOM 3552 CA GLU A 493 11.268 -7.470 29.417 1.00111.83 C ANISOU 3552 CA GLU A 493 15784 15483 11223 -875 4790 -577 C ATOM 3553 C GLU A 493 11.979 -8.462 28.502 1.00118.24 C ANISOU 3553 C GLU A 493 16604 16171 12151 -1145 4543 -468 C ATOM 3554 O GLU A 493 12.685 -9.357 28.979 1.00120.38 O ANISOU 3554 O GLU A 493 17044 16411 12285 -1315 4508 -402 O ATOM 3555 CB GLU A 493 9.765 -7.461 29.155 1.00107.74 C ANISOU 3555 CB GLU A 493 14882 15176 10879 -809 4977 -486 C ATOM 3556 CG GLU A 493 9.006 -6.480 30.029 1.00108.92 C ANISOU 3556 CG GLU A 493 15004 15458 10922 -517 5240 -594 C ATOM 3557 CD GLU A 493 8.511 -5.267 29.262 1.00108.00 C ANISOU 3557 CD GLU A 493 14749 15289 10998 -285 5185 -706 C ATOM 3558 OE1 GLU A 493 7.905 -5.452 28.186 1.00103.02 O ANISOU 3558 OE1 GLU A 493 13829 14685 10628 -355 5093 -610 O ATOM 3559 OE2 GLU A 493 8.698 -4.132 29.758 1.00111.34 O ANISOU 3559 OE2 GLU A 493 15357 15641 11304 -31 5233 -887 O ATOM 3560 N HIS A 494 11.809 -8.308 27.187 1.00123.74 N ANISOU 3560 N HIS A 494 17128 16794 13094 -1178 4369 -450 N ATOM 3561 CA HIS A 494 12.528 -9.105 26.190 1.00127.62 C ANISOU 3561 CA HIS A 494 17644 17147 13698 -1403 4121 -374 C ATOM 3562 C HIS A 494 13.526 -8.187 25.488 1.00120.87 C ANISOU 3562 C HIS A 494 16968 16075 12882 -1320 3888 -517 C ATOM 3563 O HIS A 494 13.184 -7.499 24.521 1.00123.44 O ANISOU 3563 O HIS A 494 17158 16354 13389 -1240 3790 -556 O ATOM 3564 CB HIS A 494 11.577 -9.745 25.180 1.00130.42 C ANISOU 3564 CB HIS A 494 17674 17585 14295 -1538 4089 -228 C ATOM 3565 CG HIS A 494 10.235 -10.091 25.737 1.00134.36 C ANISOU 3565 CG HIS A 494 17908 18327 14817 -1530 4343 -113 C ATOM 3566 ND1 HIS A 494 9.126 -9.295 25.550 1.00136.25 N ANISOU 3566 ND1 HIS A 494 17892 18689 15186 -1352 4462 -134 N ATOM 3567 CD2 HIS A 494 9.824 -11.147 26.477 1.00136.15 C ANISOU 3567 CD2 HIS A 494 18076 18702 14955 -1682 4501 32 C ATOM 3568 CE1 HIS A 494 8.087 -9.849 26.146 1.00139.79 C ANISOU 3568 CE1 HIS A 494 18121 19362 15629 -1392 4690 -4 C ATOM 3569 NE2 HIS A 494 8.484 -10.973 26.717 1.00139.23 N ANISOU 3569 NE2 HIS A 494 18167 19310 15422 -1599 4719 101 N ATOM 3570 N ALA A 495 14.762 -8.186 25.967 1.00109.20 N ANISOU 3570 N ALA A 495 15790 14467 11234 -1346 3793 -584 N ATOM 3571 CA ALA A 495 15.768 -7.253 25.496 1.00 91.14 C ANISOU 3571 CA ALA A 495 13692 11984 8952 -1265 3589 -718 C ATOM 3572 C ALA A 495 16.665 -7.909 24.464 1.00 84.41 C ANISOU 3572 C ALA A 495 12877 10996 8201 -1454 3350 -659 C ATOM 3573 O ALA A 495 16.854 -9.129 24.469 1.00 85.14 O ANISOU 3573 O ALA A 495 12959 11112 8279 -1643 3338 -540 O ATOM 3574 CB ALA A 495 16.627 -6.752 26.652 1.00 86.84 C ANISOU 3574 CB ALA A 495 13458 11375 8160 -1173 3614 -832 C ATOM 3575 N TYR A 496 17.222 -7.081 23.579 1.00 76.89 N ANISOU 3575 N TYR A 496 11975 9896 7345 -1398 3161 -744 N ATOM 3576 CA TYR A 496 18.247 -7.564 22.665 1.00 64.89 C ANISOU 3576 CA TYR A 496 10528 8239 5889 -1552 2938 -709 C ATOM 3577 C TYR A 496 19.560 -7.741 23.409 1.00 63.62 C ANISOU 3577 C TYR A 496 10645 7985 5542 -1595 2871 -745 C ATOM 3578 O TYR A 496 19.775 -7.163 24.471 1.00 64.27 O ANISOU 3578 O TYR A 496 10892 8071 5458 -1483 2950 -828 O ATOM 3579 CB TYR A 496 18.454 -6.597 21.502 1.00 58.39 C ANISOU 3579 CB TYR A 496 9675 7296 5215 -1485 2763 -779 C ATOM 3580 CG TYR A 496 17.382 -6.601 20.427 1.00 59.68 C ANISOU 3580 CG TYR A 496 9567 7516 5593 -1494 2751 -719 C ATOM 3581 CD1 TYR A 496 16.799 -7.784 19.991 1.00 60.52 C ANISOU 3581 CD1 TYR A 496 9498 7708 5790 -1659 2776 -582 C ATOM 3582 CD2 TYR A 496 16.989 -5.421 19.816 1.00 61.41 C ANISOU 3582 CD2 TYR A 496 9718 7690 5927 -1346 2693 -796 C ATOM 3583 CE1 TYR A 496 15.836 -7.784 18.999 1.00 60.41 C ANISOU 3583 CE1 TYR A 496 9241 7740 5970 -1679 2744 -524 C ATOM 3584 CE2 TYR A 496 16.028 -5.414 18.823 1.00 62.83 C ANISOU 3584 CE2 TYR A 496 9651 7918 6304 -1357 2664 -735 C ATOM 3585 CZ TYR A 496 15.450 -6.593 18.420 1.00 61.02 C ANISOU 3585 CZ TYR A 496 9245 7782 6159 -1526 2688 -599 C ATOM 3586 OH TYR A 496 14.486 -6.579 17.430 1.00 61.54 O ANISOU 3586 OH TYR A 496 9067 7894 6421 -1545 2642 -534 O ATOM 3587 N MET A 497 20.455 -8.529 22.831 1.00 69.23 N ANISOU 3587 N MET A 497 11413 8610 6283 -1753 2718 -682 N ATOM 3588 CA MET A 497 21.771 -8.742 23.417 1.00 75.12 C ANISOU 3588 CA MET A 497 12401 9264 6879 -1801 2628 -702 C ATOM 3589 C MET A 497 22.883 -8.269 22.487 1.00 64.34 C ANISOU 3589 C MET A 497 11117 7744 5585 -1819 2404 -746 C ATOM 3590 O MET A 497 22.675 -7.922 21.322 1.00 62.47 O ANISOU 3590 O MET A 497 10758 7468 5509 -1817 2313 -751 O ATOM 3591 CB MET A 497 22.034 -10.216 23.714 1.00 84.97 C ANISOU 3591 CB MET A 497 13669 10543 8074 -1972 2647 -577 C ATOM 3592 CG MET A 497 20.846 -11.023 24.085 1.00 92.45 C ANISOU 3592 CG MET A 497 14457 11640 9029 -2028 2829 -477 C ATOM 3593 SD MET A 497 20.301 -10.665 25.719 1.00 97.73 S ANISOU 3593 SD MET A 497 15210 12437 9486 -1914 3060 -514 S ATOM 3594 CE MET A 497 19.023 -11.940 25.810 1.00 99.54 C ANISOU 3594 CE MET A 497 15210 12837 9773 -2052 3234 -345 C ATOM 3595 N ALA A 498 24.086 -8.291 23.036 1.00 58.08 N ANISOU 3595 N ALA A 498 10532 6871 4665 -1845 2314 -769 N ATOM 3596 CA ALA A 498 25.287 -8.069 22.252 1.00 56.98 C ANISOU 3596 CA ALA A 498 10469 6602 4580 -1892 2109 -783 C ATOM 3597 C ALA A 498 26.400 -8.823 22.947 1.00 60.84 C ANISOU 3597 C ALA A 498 11122 7055 4938 -1979 2054 -738 C ATOM 3598 O ALA A 498 26.573 -8.682 24.158 1.00 67.09 O ANISOU 3598 O ALA A 498 12062 7866 5563 -1938 2115 -768 O ATOM 3599 CB ALA A 498 25.627 -6.584 22.149 1.00 58.22 C ANISOU 3599 CB ALA A 498 10714 6671 4736 -1769 2018 -901 C ATOM 3600 N HIS A 499 27.134 -9.644 22.208 1.00 58.71 N ANISOU 3600 N HIS A 499 10833 6734 4740 -2092 1942 -665 N ATOM 3601 CA HIS A 499 28.027 -10.543 22.928 1.00 56.84 C ANISOU 3601 CA HIS A 499 10729 6479 4389 -2172 1910 -604 C ATOM 3602 C HIS A 499 29.169 -11.029 22.057 1.00 51.60 C ANISOU 3602 C HIS A 499 10074 5727 3803 -2250 1747 -559 C ATOM 3603 O HIS A 499 29.107 -11.032 20.830 1.00 50.42 O ANISOU 3603 O HIS A 499 9811 5551 3797 -2274 1686 -551 O ATOM 3604 CB HIS A 499 27.270 -11.752 23.508 1.00 53.35 C ANISOU 3604 CB HIS A 499 10230 6126 3914 -2240 2045 -511 C ATOM 3605 CG HIS A 499 26.411 -12.484 22.520 1.00 51.88 C ANISOU 3605 CG HIS A 499 9865 5980 3866 -2319 2091 -443 C ATOM 3606 ND1 HIS A 499 26.759 -13.710 21.989 1.00 53.17 N ANISOU 3606 ND1 HIS A 499 10009 6106 4087 -2439 2030 -350 N ATOM 3607 CD2 HIS A 499 25.203 -12.176 21.990 1.00 51.27 C ANISOU 3607 CD2 HIS A 499 9613 5971 3896 -2289 2175 -451 C ATOM 3608 CE1 HIS A 499 25.811 -14.118 21.162 1.00 52.25 C ANISOU 3608 CE1 HIS A 499 9728 6028 4098 -2491 2068 -308 C ATOM 3609 NE2 HIS A 499 24.858 -13.203 21.142 1.00 51.66 N ANISOU 3609 NE2 HIS A 499 9546 6021 4060 -2405 2153 -362 N ATOM 3610 N CYS A 500 30.218 -11.440 22.726 1.00 46.77 N ANISOU 3610 N CYS A 500 9570 5071 3129 -2271 1660 -526 N ATOM 3611 CA CYS A 500 31.218 -12.249 22.076 1.00 50.04 C ANISOU 3611 CA CYS A 500 9978 5424 3612 -2343 1539 -460 C ATOM 3612 C CYS A 500 30.584 -13.595 21.735 1.00 51.96 C ANISOU 3612 C CYS A 500 10124 5698 3918 -2420 1605 -377 C ATOM 3613 O CYS A 500 29.858 -14.160 22.551 1.00 60.45 O ANISOU 3613 O CYS A 500 11184 6832 4952 -2429 1704 -342 O ATOM 3614 CB CYS A 500 32.394 -12.385 23.021 1.00 49.16 C ANISOU 3614 CB CYS A 500 9983 5266 3432 -2334 1434 -438 C ATOM 3615 SG CYS A 500 33.832 -13.095 22.350 1.00 53.59 S ANISOU 3615 SG CYS A 500 10552 5752 4056 -2390 1281 -373 S ATOM 3616 N HIS A 501 30.776 -14.070 20.505 1.00 45.80 N ANISOU 3616 N HIS A 501 9278 4881 3242 -2475 1552 -348 N ATOM 3617 CA HIS A 501 30.288 -15.380 20.081 1.00 44.38 C ANISOU 3617 CA HIS A 501 9019 4704 3138 -2548 1575 -275 C ATOM 3618 C HIS A 501 31.351 -16.460 20.164 1.00 47.40 C ANISOU 3618 C HIS A 501 9456 5020 3535 -2569 1471 -222 C ATOM 3619 O HIS A 501 31.167 -17.548 19.603 1.00 47.97 O ANISOU 3619 O HIS A 501 9481 5068 3677 -2619 1454 -175 O ATOM 3620 CB HIS A 501 29.684 -15.311 18.670 1.00 47.64 C ANISOU 3620 CB HIS A 501 9327 5114 3660 -2591 1582 -277 C ATOM 3621 CG HIS A 501 28.427 -16.111 18.513 1.00 51.60 C ANISOU 3621 CG HIS A 501 9721 5666 4221 -2656 1667 -224 C ATOM 3622 ND1 HIS A 501 28.413 -17.486 18.581 1.00 50.74 N ANISOU 3622 ND1 HIS A 501 9600 5534 4147 -2710 1634 -158 N ATOM 3623 CD2 HIS A 501 27.130 -15.731 18.391 1.00 53.42 C ANISOU 3623 CD2 HIS A 501 9837 5973 4487 -2666 1771 -226 C ATOM 3624 CE1 HIS A 501 27.171 -17.918 18.452 1.00 51.45 C ANISOU 3624 CE1 HIS A 501 9582 5680 4285 -2772 1712 -114 C ATOM 3625 NE2 HIS A 501 26.370 -16.875 18.342 1.00 49.82 N ANISOU 3625 NE2 HIS A 501 9311 5542 4078 -2756 1808 -146 N ATOM 3626 N LEU A 502 32.474 -16.163 20.806 1.00 43.91 N ANISOU 3626 N LEU A 502 9115 4544 3027 -2531 1393 -230 N ATOM 3627 CA LEU A 502 33.276 -17.164 21.498 1.00 44.27 C ANISOU 3627 CA LEU A 502 9232 4551 3037 -2542 1331 -170 C ATOM 3628 C LEU A 502 32.490 -17.543 22.733 1.00 45.71 C ANISOU 3628 C LEU A 502 9439 4788 3142 -2551 1421 -142 C ATOM 3629 O LEU A 502 32.417 -16.763 23.680 1.00 55.26 O ANISOU 3629 O LEU A 502 10707 6032 4257 -2510 1455 -175 O ATOM 3630 CB LEU A 502 34.624 -16.591 21.888 1.00 44.00 C ANISOU 3630 CB LEU A 502 9291 4477 2949 -2506 1223 -180 C ATOM 3631 CG LEU A 502 35.724 -17.616 21.986 1.00 43.91 C ANISOU 3631 CG LEU A 502 9331 4411 2943 -2516 1129 -114 C ATOM 3632 CD1 LEU A 502 36.990 -16.896 21.728 1.00 43.29 C ANISOU 3632 CD1 LEU A 502 9290 4303 2857 -2492 1021 -123 C ATOM 3633 CD2 LEU A 502 35.699 -18.283 23.363 1.00 45.19 C ANISOU 3633 CD2 LEU A 502 9577 4580 3014 -2526 1139 -65 C ATOM 3634 N LEU A 503 31.893 -18.733 22.741 1.00 46.24 N ANISOU 3634 N LEU A 503 9466 4863 3241 -2605 1458 -80 N ATOM 3635 CA LEU A 503 30.759 -18.945 23.633 1.00 47.70 C ANISOU 3635 CA LEU A 503 9624 5128 3370 -2626 1579 -51 C ATOM 3636 C LEU A 503 31.156 -18.810 25.095 1.00 65.62 C ANISOU 3636 C LEU A 503 12009 7416 5510 -2595 1583 -40 C ATOM 3637 O LEU A 503 30.456 -18.146 25.871 1.00 49.89 O ANISOU 3637 O LEU A 503 10018 5500 3437 -2562 1687 -67 O ATOM 3638 CB LEU A 503 30.125 -20.298 23.354 1.00 48.17 C ANISOU 3638 CB LEU A 503 9626 5185 3492 -2704 1595 26 C ATOM 3639 CG LEU A 503 29.452 -20.336 21.987 1.00 47.42 C ANISOU 3639 CG LEU A 503 9412 5088 3517 -2740 1605 13 C ATOM 3640 CD1 LEU A 503 28.763 -21.650 21.820 1.00 48.17 C ANISOU 3640 CD1 LEU A 503 9459 5180 3664 -2822 1610 92 C ATOM 3641 CD2 LEU A 503 28.475 -19.186 21.878 1.00 47.66 C ANISOU 3641 CD2 LEU A 503 9356 5206 3545 -2719 1718 -35 C ATOM 3642 N GLU A 504 32.312 -19.377 25.466 1.00 61.45 N ANISOU 3642 N GLU A 504 11580 6818 4952 -2598 1469 -3 N ATOM 3643 CA GLU A 504 32.778 -19.368 26.851 1.00 62.27 C ANISOU 3643 CA GLU A 504 11804 6926 4928 -2580 1449 20 C ATOM 3644 C GLU A 504 33.065 -17.957 27.367 1.00 64.55 C ANISOU 3644 C GLU A 504 12156 7234 5137 -2512 1445 -58 C ATOM 3645 O GLU A 504 33.079 -17.735 28.583 1.00 66.02 O ANISOU 3645 O GLU A 504 12435 7447 5202 -2490 1465 -57 O ATOM 3646 CB GLU A 504 34.033 -20.231 26.977 1.00 61.77 C ANISOU 3646 CB GLU A 504 11828 6778 4863 -2597 1311 79 C ATOM 3647 CG GLU A 504 33.809 -21.715 26.840 1.00 63.26 C ANISOU 3647 CG GLU A 504 12003 6937 5095 -2655 1305 162 C ATOM 3648 CD GLU A 504 33.421 -22.115 25.447 1.00 67.48 C ANISOU 3648 CD GLU A 504 12431 7447 5762 -2677 1311 153 C ATOM 3649 OE1 GLU A 504 34.270 -22.006 24.554 1.00 70.05 O ANISOU 3649 OE1 GLU A 504 12754 7713 6151 -2650 1228 130 O ATOM 3650 OE2 GLU A 504 32.265 -22.520 25.229 1.00 70.24 O ANISOU 3650 OE2 GLU A 504 12698 7840 6149 -2724 1398 172 O ATOM 3651 N HIS A 505 33.350 -17.008 26.473 1.00 64.79 N ANISOU 3651 N HIS A 505 12151 7240 5225 -2479 1407 -126 N ATOM 3652 CA HIS A 505 33.404 -15.607 26.878 1.00 64.52 C ANISOU 3652 CA HIS A 505 12171 7221 5123 -2413 1410 -207 C ATOM 3653 C HIS A 505 32.016 -15.052 27.161 1.00 72.79 C ANISOU 3653 C HIS A 505 13166 8357 6135 -2374 1574 -255 C ATOM 3654 O HIS A 505 31.816 -14.319 28.138 1.00 72.52 O ANISOU 3654 O HIS A 505 13209 8354 5990 -2313 1617 -300 O ATOM 3655 CB HIS A 505 34.077 -14.783 25.797 1.00 60.18 C ANISOU 3655 CB HIS A 505 11596 6620 4649 -2398 1318 -256 C ATOM 3656 CG HIS A 505 35.526 -15.073 25.645 1.00 59.25 C ANISOU 3656 CG HIS A 505 11536 6432 4545 -2420 1162 -214 C ATOM 3657 ND1 HIS A 505 36.316 -14.435 24.715 1.00 59.16 N ANISOU 3657 ND1 HIS A 505 11503 6382 4594 -2417 1067 -238 N ATOM 3658 CD2 HIS A 505 36.345 -15.893 26.339 1.00 60.40 C ANISOU 3658 CD2 HIS A 505 11759 6547 4643 -2445 1085 -145 C ATOM 3659 CE1 HIS A 505 37.558 -14.868 24.826 1.00 58.92 C ANISOU 3659 CE1 HIS A 505 11524 6307 4554 -2438 945 -181 C ATOM 3660 NE2 HIS A 505 37.604 -15.750 25.808 1.00 60.49 N ANISOU 3660 NE2 HIS A 505 11788 6507 4689 -2452 950 -126 N ATOM 3661 N GLU A 506 31.050 -15.367 26.301 1.00 78.60 N ANISOU 3661 N GLU A 506 13770 9136 6960 -2404 1666 -245 N ATOM 3662 CA GLU A 506 29.702 -14.870 26.522 1.00 79.20 C ANISOU 3662 CA GLU A 506 13777 9311 7007 -2366 1832 -279 C ATOM 3663 C GLU A 506 29.137 -15.419 27.828 1.00 78.96 C ANISOU 3663 C GLU A 506 13778 9355 6868 -2367 1934 -230 C ATOM 3664 O GLU A 506 28.467 -14.701 28.587 1.00 75.90 O ANISOU 3664 O GLU A 506 13410 9043 6387 -2294 2048 -277 O ATOM 3665 CB GLU A 506 28.826 -15.242 25.334 1.00 79.62 C ANISOU 3665 CB GLU A 506 13676 9394 7183 -2420 1895 -256 C ATOM 3666 CG GLU A 506 27.434 -14.725 25.480 1.00 89.57 C ANISOU 3666 CG GLU A 506 14844 10766 8424 -2384 2071 -282 C ATOM 3667 CD GLU A 506 26.398 -15.764 25.169 1.00 94.64 C ANISOU 3667 CD GLU A 506 15346 11476 9138 -2472 2162 -191 C ATOM 3668 OE1 GLU A 506 26.398 -16.224 24.000 1.00 95.37 O ANISOU 3668 OE1 GLU A 506 15362 11523 9352 -2542 2100 -163 O ATOM 3669 OE2 GLU A 506 25.600 -16.106 26.087 1.00 96.89 O ANISOU 3669 OE2 GLU A 506 15599 11857 9356 -2474 2288 -145 O ATOM 3670 N ASP A 507 29.447 -16.685 28.122 1.00 78.29 N ANISOU 3670 N ASP A 507 13709 9248 6788 -2443 1888 -136 N ATOM 3671 CA ASP A 507 28.946 -17.338 29.324 1.00 71.39 C ANISOU 3671 CA ASP A 507 12868 8445 5813 -2462 1974 -71 C ATOM 3672 C ASP A 507 29.612 -16.808 30.573 1.00 66.65 C ANISOU 3672 C ASP A 507 12428 7832 5063 -2403 1936 -103 C ATOM 3673 O ASP A 507 29.022 -16.870 31.653 1.00 71.91 O ANISOU 3673 O ASP A 507 13128 8581 5614 -2383 2043 -83 O ATOM 3674 CB ASP A 507 29.157 -18.847 29.233 1.00 65.53 C ANISOU 3674 CB ASP A 507 12114 7665 5120 -2562 1915 38 C ATOM 3675 CG ASP A 507 28.100 -19.522 28.398 1.00 65.05 C ANISOU 3675 CG ASP A 507 11896 7649 5172 -2631 1991 90 C ATOM 3676 OD1 ASP A 507 27.102 -18.842 28.040 1.00 54.82 O ANISOU 3676 OD1 ASP A 507 10491 6436 3902 -2606 2112 53 O ATOM 3677 OD2 ASP A 507 28.263 -20.735 28.124 1.00 61.27 O ANISOU 3677 OD2 ASP A 507 11408 7120 4751 -2711 1926 169 O ATOM 3678 N THR A 508 30.838 -16.315 30.466 1.00 62.30 N ANISOU 3678 N THR A 508 11977 7184 4509 -2380 1783 -144 N ATOM 3679 CA THR A 508 31.505 -15.783 31.648 1.00 65.20 C ANISOU 3679 CA THR A 508 12506 7532 4737 -2333 1726 -171 C ATOM 3680 C THR A 508 31.527 -14.249 31.659 1.00 64.14 C ANISOU 3680 C THR A 508 12418 7389 4563 -2235 1725 -288 C ATOM 3681 O THR A 508 32.474 -13.626 32.139 1.00 61.40 O ANISOU 3681 O THR A 508 12201 6977 4153 -2208 1601 -322 O ATOM 3682 CB THR A 508 32.903 -16.398 31.796 1.00 55.15 C ANISOU 3682 CB THR A 508 11330 6160 3465 -2385 1544 -113 C ATOM 3683 OG1 THR A 508 33.699 -16.155 30.637 1.00 53.28 O ANISOU 3683 OG1 THR A 508 11052 5846 3346 -2394 1427 -134 O ATOM 3684 CG2 THR A 508 32.789 -17.898 31.974 1.00 55.54 C ANISOU 3684 CG2 THR A 508 11358 6214 3530 -2465 1552 -3 C ATOM 3685 N GLY A 509 30.470 -13.607 31.152 1.00 62.67 N ANISOU 3685 N GLY A 509 12131 7267 4412 -2181 1856 -349 N ATOM 3686 CA GLY A 509 30.227 -12.205 31.423 1.00 56.61 C ANISOU 3686 CA GLY A 509 11423 6507 3580 -2069 1890 -463 C ATOM 3687 C GLY A 509 30.300 -11.247 30.248 1.00 63.38 C ANISOU 3687 C GLY A 509 12226 7314 4543 -2033 1842 -541 C ATOM 3688 O GLY A 509 29.863 -10.105 30.403 1.00 55.96 O ANISOU 3688 O GLY A 509 11320 6384 3558 -1930 1892 -640 O ATOM 3689 N MET A 510 30.843 -11.639 29.086 1.00 60.49 N ANISOU 3689 N MET A 510 11786 6889 4308 -2107 1744 -504 N ATOM 3690 CA MET A 510 31.086 -10.688 27.985 1.00 56.17 C ANISOU 3690 CA MET A 510 11207 6286 3851 -2080 1672 -573 C ATOM 3691 C MET A 510 29.881 -10.598 27.058 1.00 51.69 C ANISOU 3691 C MET A 510 10493 5784 3364 -2071 1809 -597 C ATOM 3692 O MET A 510 29.832 -11.180 25.974 1.00 50.39 O ANISOU 3692 O MET A 510 10223 5612 3312 -2144 1794 -552 O ATOM 3693 CB MET A 510 32.336 -11.056 27.206 1.00 52.44 C ANISOU 3693 CB MET A 510 10734 5727 3466 -2157 1500 -524 C ATOM 3694 CG MET A 510 32.786 -9.943 26.287 1.00 51.35 C ANISOU 3694 CG MET A 510 10590 5525 3394 -2130 1400 -591 C ATOM 3695 SD MET A 510 34.342 -10.313 25.489 1.00 51.79 S ANISOU 3695 SD MET A 510 10646 5500 3533 -2212 1206 -527 S ATOM 3696 CE MET A 510 35.443 -10.365 26.917 1.00 52.77 C ANISOU 3696 CE MET A 510 10932 5582 3535 -2216 1089 -493 C ATOM 3697 N MET A 511 28.927 -9.783 27.482 1.00 53.05 N ANISOU 3697 N MET A 511 10667 6016 3474 -1971 1939 -673 N ATOM 3698 CA MET A 511 27.625 -9.650 26.846 1.00 58.39 C ANISOU 3698 CA MET A 511 11206 6777 4202 -1947 2101 -695 C ATOM 3699 C MET A 511 26.798 -8.602 27.578 1.00 62.64 C ANISOU 3699 C MET A 511 11786 7371 4644 -1802 2232 -796 C ATOM 3700 O MET A 511 26.854 -8.512 28.808 1.00 68.86 O ANISOU 3700 O MET A 511 12675 8183 5306 -1744 2265 -808 O ATOM 3701 CB MET A 511 26.882 -10.977 26.852 1.00 53.68 C ANISOU 3701 CB MET A 511 10484 6274 3639 -2040 2217 -583 C ATOM 3702 CG MET A 511 25.436 -10.869 26.441 1.00 57.42 C ANISOU 3702 CG MET A 511 10804 6860 4152 -2020 2406 -587 C ATOM 3703 SD MET A 511 24.789 -12.525 26.626 1.00 66.73 S ANISOU 3703 SD MET A 511 11853 8129 5372 -2153 2492 -431 S ATOM 3704 CE MET A 511 23.033 -12.264 26.447 1.00 68.29 C ANISOU 3704 CE MET A 511 11860 8489 5600 -2120 2736 -426 C ATOM 3705 N LEU A 512 26.009 -7.824 26.846 1.00 62.27 N ANISOU 3705 N LEU A 512 11667 7345 4648 -1735 2313 -870 N ATOM 3706 CA LEU A 512 25.097 -6.862 27.444 1.00 66.20 C ANISOU 3706 CA LEU A 512 12187 7900 5068 -1577 2461 -972 C ATOM 3707 C LEU A 512 23.701 -7.057 26.864 1.00 75.98 C ANISOU 3707 C LEU A 512 13223 9261 6384 -1565 2658 -952 C ATOM 3708 O LEU A 512 23.482 -7.880 25.954 1.00 79.28 O ANISOU 3708 O LEU A 512 13465 9702 6957 -1678 2630 -852 O ATOM 3709 CB LEU A 512 25.591 -5.436 27.205 1.00 63.19 C ANISOU 3709 CB LEU A 512 11929 7394 4685 -1468 2335 -1103 C ATOM 3710 CG LEU A 512 25.749 -5.089 25.724 1.00 63.06 C ANISOU 3710 CG LEU A 512 11817 7304 4840 -1507 2219 -1114 C ATOM 3711 CD1 LEU A 512 24.497 -4.432 25.127 1.00 61.26 C ANISOU 3711 CD1 LEU A 512 11406 7124 4746 -1385 2317 -1159 C ATOM 3712 CD2 LEU A 512 26.981 -4.223 25.524 1.00 65.26 C ANISOU 3712 CD2 LEU A 512 12264 7427 5105 -1507 2000 -1177 C ATOM 3713 N GLY A 513 22.765 -6.259 27.379 1.00 77.49 N ANISOU 3713 N GLY A 513 13393 9522 6526 -1403 2815 -1034 N ATOM 3714 CA GLY A 513 21.442 -6.132 26.795 1.00 78.00 C ANISOU 3714 CA GLY A 513 13201 9690 6745 -1337 2944 -1017 C ATOM 3715 C GLY A 513 21.186 -4.705 26.359 1.00 76.88 C ANISOU 3715 C GLY A 513 13055 9475 6682 -1159 2896 -1147 C ATOM 3716 O GLY A 513 21.903 -3.804 26.791 1.00 77.88 O ANISOU 3716 O GLY A 513 13403 9487 6700 -1074 2807 -1259 O ATOM 3717 N PHE A 514 20.203 -4.489 25.486 1.00 77.34 N ANISOU 3717 N PHE A 514 12871 9585 6931 -1109 2936 -1128 N ATOM 3718 CA PHE A 514 19.794 -3.134 25.137 1.00 78.46 C ANISOU 3718 CA PHE A 514 12997 9665 7149 -920 2910 -1246 C ATOM 3719 C PHE A 514 18.351 -3.147 24.657 1.00 75.64 C ANISOU 3719 C PHE A 514 12344 9442 6954 -846 3052 -1202 C ATOM 3720 O PHE A 514 17.759 -4.211 24.433 1.00 78.15 O ANISOU 3720 O PHE A 514 12465 9885 7344 -970 3136 -1073 O ATOM 3721 CB PHE A 514 20.731 -2.479 24.089 1.00 80.85 C ANISOU 3721 CB PHE A 514 13372 9784 7561 -954 2647 -1285 C ATOM 3722 CG PHE A 514 20.769 -3.164 22.727 1.00 78.38 C ANISOU 3722 CG PHE A 514 12871 9464 7447 -1110 2527 -1174 C ATOM 3723 CD1 PHE A 514 21.790 -4.054 22.407 1.00 74.35 C ANISOU 3723 CD1 PHE A 514 12422 8904 6923 -1295 2403 -1096 C ATOM 3724 CD2 PHE A 514 19.824 -2.864 21.750 1.00 77.72 C ANISOU 3724 CD2 PHE A 514 12561 9412 7557 -1062 2527 -1153 C ATOM 3725 CE1 PHE A 514 21.836 -4.663 21.167 1.00 70.91 C ANISOU 3725 CE1 PHE A 514 11838 8455 6651 -1425 2298 -1007 C ATOM 3726 CE2 PHE A 514 19.866 -3.468 20.502 1.00 75.08 C ANISOU 3726 CE2 PHE A 514 12079 9063 7386 -1206 2408 -1058 C ATOM 3727 CZ PHE A 514 20.876 -4.369 20.212 1.00 71.88 C ANISOU 3727 CZ PHE A 514 11751 8609 6952 -1385 2298 -990 C ATOM 3728 N THR A 515 17.785 -1.939 24.516 1.00 77.96 N ANISOU 3728 N THR A 515 12609 9703 7308 -642 3071 -1308 N ATOM 3729 CA THR A 515 16.375 -1.790 24.161 1.00 76.51 C ANISOU 3729 CA THR A 515 12143 9652 7278 -534 3212 -1276 C ATOM 3730 C THR A 515 16.212 -0.815 22.999 1.00 76.35 C ANISOU 3730 C THR A 515 12039 9516 7453 -447 3048 -1323 C ATOM 3731 O THR A 515 17.088 0.006 22.732 1.00 75.92 O ANISOU 3731 O THR A 515 12181 9284 7380 -414 2867 -1412 O ATOM 3732 CB THR A 515 15.542 -1.305 25.357 1.00 75.11 C ANISOU 3732 CB THR A 515 11980 9594 6966 -322 3467 -1354 C ATOM 3733 OG1 THR A 515 16.083 -0.074 25.862 1.00 70.06 O ANISOU 3733 OG1 THR A 515 11608 8808 6204 -143 3410 -1524 O ATOM 3734 CG2 THR A 515 15.541 -2.361 26.459 1.00 70.20 C ANISOU 3734 CG2 THR A 515 11405 9112 6156 -423 3648 -1282 C ATOM 3735 N VAL A 516 15.070 -0.907 22.311 1.00 77.28 N ANISOU 3735 N VAL A 516 11862 9739 7763 -415 3106 -1253 N ATOM 3736 CA VAL A 516 14.803 -0.082 21.135 1.00 83.66 C ANISOU 3736 CA VAL A 516 12564 10451 8771 -346 2947 -1274 C ATOM 3737 C VAL A 516 13.313 0.230 20.991 1.00 96.41 C ANISOU 3737 C VAL A 516 13891 12206 10536 -186 3095 -1251 C ATOM 3738 O VAL A 516 12.488 -0.689 20.941 1.00103.79 O ANISOU 3738 O VAL A 516 14580 13313 11541 -276 3218 -1126 O ATOM 3739 CB VAL A 516 15.372 -0.777 19.882 1.00 78.73 C ANISOU 3739 CB VAL A 516 11882 9759 8272 -579 2737 -1169 C ATOM 3740 CG1 VAL A 516 14.993 -2.220 19.881 1.00 78.19 C ANISOU 3740 CG1 VAL A 516 11648 9839 8222 -768 2828 -1024 C ATOM 3741 CG2 VAL A 516 14.826 -0.138 18.624 1.00 78.68 C ANISOU 3741 CG2 VAL A 516 11709 9701 8485 -529 2601 -1155 C ATOM 3742 N LYS A 517 12.956 1.525 20.925 1.00103.80 N ANISOU 3742 N LYS A 517 14850 13064 11523 51 3077 -1365 N ATOM 3743 CA LYS A 517 11.566 1.977 20.800 1.00114.50 C ANISOU 3743 CA LYS A 517 15935 14540 13029 242 3210 -1355 C ATOM 3744 C LYS A 517 11.518 3.284 20.013 1.00122.20 C ANISOU 3744 C LYS A 517 16941 15349 14140 408 3036 -1442 C ATOM 3745 O LYS A 517 12.466 4.074 20.037 1.00122.65 O ANISOU 3745 O LYS A 517 17278 15209 14113 448 2886 -1553 O ATOM 3746 CB LYS A 517 10.898 2.174 22.175 1.00116.00 C ANISOU 3746 CB LYS A 517 16131 14874 13071 447 3505 -1424 C ATOM 3747 CG LYS A 517 9.400 2.570 22.168 1.00118.83 C ANISOU 3747 CG LYS A 517 16178 15393 13580 663 3684 -1405 C ATOM 3748 CD LYS A 517 8.474 1.453 22.691 1.00119.18 C ANISOU 3748 CD LYS A 517 15950 15710 13622 581 3936 -1264 C ATOM 3749 CE LYS A 517 7.021 1.599 22.216 1.00117.69 C ANISOU 3749 CE LYS A 517 15365 15687 13665 703 4038 -1180 C ATOM 3750 NZ LYS A 517 6.345 0.283 22.005 1.00114.57 N ANISOU 3750 NZ LYS A 517 14668 15499 13364 478 4122 -977 N ATOM 3751 N ASP A 518 10.399 3.505 19.318 1.00132.41 N ANISOU 3751 N ASP A 518 17941 16720 15647 497 3048 -1382 N ATOM 3752 CA ASP A 518 10.208 4.701 18.494 1.00135.79 C ANISOU 3752 CA ASP A 518 18364 17000 16229 655 2878 -1444 C ATOM 3753 C ASP A 518 10.217 5.972 19.341 1.00133.64 C ANISOU 3753 C ASP A 518 18299 16626 15851 954 2950 -1625 C ATOM 3754 O ASP A 518 9.342 6.139 20.207 1.00138.65 O ANISOU 3754 O ASP A 518 18833 17401 16448 1161 3196 -1667 O ATOM 3755 CB ASP A 518 8.906 4.582 17.698 1.00141.84 C ANISOU 3755 CB ASP A 518 18750 17899 17244 696 2896 -1330 C ATOM 3756 CG ASP A 518 7.759 4.022 18.525 1.00152.68 C ANISOU 3756 CG ASP A 518 19864 19530 18616 781 3195 -1271 C ATOM 3757 OD1 ASP A 518 7.977 3.685 19.706 1.00155.76 O ANISOU 3757 OD1 ASP A 518 20379 19999 18803 802 3394 -1318 O ATOM 3758 OD2 ASP A 518 6.638 3.900 17.989 1.00155.83 O ANISOU 3758 OD2 ASP A 518 19929 20060 19217 818 3229 -1169 O ATOM 3759 N PRO A 519 11.161 6.886 19.115 1.00121.85 N ANISOU 3759 N PRO A 519 17094 14895 14309 985 2746 -1731 N ATOM 3760 CA PRO A 519 11.413 7.970 20.080 1.00120.67 C ANISOU 3760 CA PRO A 519 17222 14623 14004 1228 2801 -1914 C ATOM 3761 C PRO A 519 10.181 8.805 20.440 1.00121.02 C ANISOU 3761 C PRO A 519 17129 14728 14127 1564 2968 -1991 C ATOM 3762 O PRO A 519 9.470 9.332 19.577 1.00122.87 O ANISOU 3762 O PRO A 519 17169 14937 14577 1669 2882 -1958 O ATOM 3763 CB PRO A 519 12.491 8.804 19.376 1.00113.31 C ANISOU 3763 CB PRO A 519 16548 13420 13086 1167 2496 -1970 C ATOM 3764 CG PRO A 519 13.250 7.783 18.562 1.00105.78 C ANISOU 3764 CG PRO A 519 15548 12478 12164 836 2348 -1831 C ATOM 3765 CD PRO A 519 12.196 6.824 18.068 1.00110.69 C ANISOU 3765 CD PRO A 519 15797 13317 12942 762 2461 -1683 C ATOM 3766 N ASN A 520 9.943 8.930 21.745 1.00118.02 N ANISOU 3766 N ASN A 520 16855 14427 13560 1742 3210 -2096 N ATOM 3767 CA ASN A 520 8.758 9.590 22.282 1.00119.59 C ANISOU 3767 CA ASN A 520 16920 14722 13799 2078 3429 -2173 C ATOM 3768 C ASN A 520 8.889 11.116 22.230 1.00120.44 C ANISOU 3768 C ASN A 520 17260 14581 13919 2345 3297 -2344 C ATOM 3769 O ASN A 520 7.978 11.850 22.625 1.00121.61 O ANISOU 3769 O ASN A 520 17338 14764 14106 2663 3451 -2433 O ATOM 3770 CB ASN A 520 8.505 9.127 23.726 1.00119.68 C ANISOU 3770 CB ASN A 520 16982 14912 13577 2163 3749 -2222 C ATOM 3771 CG ASN A 520 8.388 7.602 23.852 1.00113.68 C ANISOU 3771 CG ASN A 520 16013 14389 12792 1892 3879 -2048 C ATOM 3772 OD1 ASN A 520 8.440 6.869 22.859 1.00108.48 O ANISOU 3772 OD1 ASN A 520 15161 13761 12295 1650 3737 -1894 O ATOM 3773 ND2 ASN A 520 8.228 7.126 25.085 1.00114.16 N ANISOU 3773 ND2 ASN A 520 16127 14608 12640 1932 4147 -2072 N TER 3774 ASN A 520 ATOM 3775 N GLU B 25 39.733 -2.391 53.434 1.00 61.65 N ANISOU 3775 N GLU B 25 10633 5838 6952 2151 -328 -1191 N ATOM 3776 CA GLU B 25 41.170 -2.146 53.584 1.00 63.82 C ANISOU 3776 CA GLU B 25 11084 6216 6949 2089 -179 -1006 C ATOM 3777 C GLU B 25 41.692 -2.793 54.831 1.00 66.97 C ANISOU 3777 C GLU B 25 11521 6485 7441 1885 -5 -1039 C ATOM 3778 O GLU B 25 40.914 -3.395 55.563 1.00 71.27 O ANISOU 3778 O GLU B 25 11963 6863 8252 1816 49 -1152 O ATOM 3779 CB GLU B 25 41.495 -0.661 53.653 1.00 69.02 C ANISOU 3779 CB GLU B 25 11815 6845 7566 2085 -40 -746 C ATOM 3780 CG GLU B 25 41.784 -0.045 52.295 1.00 78.91 C ANISOU 3780 CG GLU B 25 13099 8312 8572 2340 -110 -553 C ATOM 3781 CD GLU B 25 43.270 0.119 52.007 1.00 80.59 C ANISOU 3781 CD GLU B 25 13416 8624 8581 2360 30 -339 C ATOM 3782 OE1 GLU B 25 44.080 -0.732 52.481 1.00 78.85 O ANISOU 3782 OE1 GLU B 25 13245 8404 8311 2226 61 -437 O ATOM 3783 OE2 GLU B 25 43.609 1.107 51.303 1.00 79.16 O ANISOU 3783 OE2 GLU B 25 13242 8501 8333 2526 133 -42 O ATOM 3784 N THR B 26 42.996 -2.623 55.092 1.00 63.19 N ANISOU 3784 N THR B 26 11170 6072 6767 1818 101 -913 N ATOM 3785 CA THR B 26 43.704 -3.414 56.103 1.00 59.72 C ANISOU 3785 CA THR B 26 10779 5589 6323 1688 218 -947 C ATOM 3786 C THR B 26 45.020 -2.748 56.506 1.00 54.87 C ANISOU 3786 C THR B 26 10276 5002 5569 1618 307 -818 C ATOM 3787 O THR B 26 45.839 -2.401 55.650 1.00 51.01 O ANISOU 3787 O THR B 26 9814 4615 4951 1677 279 -698 O ATOM 3788 CB THR B 26 43.933 -4.858 55.586 1.00 56.20 C ANISOU 3788 CB THR B 26 10278 5225 5850 1728 127 -1075 C ATOM 3789 OG1 THR B 26 44.886 -5.558 56.402 1.00 46.29 O ANISOU 3789 OG1 THR B 26 9082 3966 4540 1631 249 -1041 O ATOM 3790 CG2 THR B 26 44.322 -4.869 54.110 1.00 58.18 C ANISOU 3790 CG2 THR B 26 10548 5686 5870 1898 -42 -1083 C ATOM 3791 N LEU B 27 45.220 -2.593 57.817 1.00 55.79 N ANISOU 3791 N LEU B 27 10440 5028 5729 1529 414 -848 N ATOM 3792 CA LEU B 27 46.346 -1.865 58.398 1.00 53.65 C ANISOU 3792 CA LEU B 27 10229 4741 5416 1471 444 -817 C ATOM 3793 C LEU B 27 47.234 -2.802 59.209 1.00 51.45 C ANISOU 3793 C LEU B 27 10010 4531 5008 1440 468 -866 C ATOM 3794 O LEU B 27 46.729 -3.649 59.955 1.00 48.40 O ANISOU 3794 O LEU B 27 9641 4149 4599 1467 544 -909 O ATOM 3795 CB LEU B 27 45.862 -0.714 59.295 1.00 53.92 C ANISOU 3795 CB LEU B 27 10265 4637 5585 1456 492 -884 C ATOM 3796 CG LEU B 27 46.952 -0.016 60.119 1.00 45.34 C ANISOU 3796 CG LEU B 27 9200 3504 4522 1417 467 -971 C ATOM 3797 CD1 LEU B 27 47.519 1.179 59.417 1.00 46.31 C ANISOU 3797 CD1 LEU B 27 9217 3506 4872 1387 447 -879 C ATOM 3798 CD2 LEU B 27 46.403 0.381 61.468 1.00 46.27 C ANISOU 3798 CD2 LEU B 27 9374 3572 4635 1466 505 -1149 C ATOM 3799 N VAL B 28 48.563 -2.625 59.073 1.00 51.05 N ANISOU 3799 N VAL B 28 9969 4516 4913 1403 426 -826 N ATOM 3800 CA VAL B 28 49.548 -3.623 59.479 1.00 50.14 C ANISOU 3800 CA VAL B 28 9888 4491 4671 1388 421 -837 C ATOM 3801 C VAL B 28 50.827 -2.969 59.994 1.00 51.77 C ANISOU 3801 C VAL B 28 10081 4664 4924 1350 355 -878 C ATOM 3802 O VAL B 28 51.154 -1.825 59.668 1.00 53.79 O ANISOU 3802 O VAL B 28 10261 4803 5376 1321 329 -858 O ATOM 3803 CB VAL B 28 49.931 -4.566 58.311 1.00 51.91 C ANISOU 3803 CB VAL B 28 10087 4809 4829 1401 411 -750 C ATOM 3804 CG1 VAL B 28 48.689 -5.041 57.514 1.00 49.75 C ANISOU 3804 CG1 VAL B 28 9771 4550 4581 1465 395 -782 C ATOM 3805 CG2 VAL B 28 51.031 -3.949 57.421 1.00 54.04 C ANISOU 3805 CG2 VAL B 28 10324 5085 5124 1402 401 -619 C ATOM 3806 N ARG B 29 51.582 -3.757 60.758 1.00 54.99 N ANISOU 3806 N ARG B 29 10530 5160 5205 1365 328 -927 N ATOM 3807 CA ARG B 29 52.859 -3.383 61.375 1.00 56.82 C ANISOU 3807 CA ARG B 29 10725 5377 5486 1354 210 -1024 C ATOM 3808 C ARG B 29 53.954 -4.302 60.839 1.00 57.88 C ANISOU 3808 C ARG B 29 10827 5575 5591 1318 215 -905 C ATOM 3809 O ARG B 29 53.934 -5.518 61.118 1.00 56.92 O ANISOU 3809 O ARG B 29 10765 5572 5291 1357 265 -865 O ATOM 3810 CB ARG B 29 52.769 -3.510 62.895 1.00 58.82 C ANISOU 3810 CB ARG B 29 11070 5727 5551 1478 149 -1204 C ATOM 3811 CG ARG B 29 52.919 -2.230 63.684 1.00 62.32 C ANISOU 3811 CG ARG B 29 11479 6088 6110 1525 -3 -1461 C ATOM 3812 CD ARG B 29 52.924 -2.539 65.182 1.00 65.19 C ANISOU 3812 CD ARG B 29 11920 6661 6187 1719 -79 -1619 C ATOM 3813 NE ARG B 29 53.337 -1.379 65.955 1.00 70.97 N ANISOU 3813 NE ARG B 29 12567 7354 7046 1782 -304 -1944 N ATOM 3814 CZ ARG B 29 52.479 -0.497 66.451 1.00 79.40 C ANISOU 3814 CZ ARG B 29 13597 8404 8166 1827 -298 -2075 C ATOM 3815 NH1 ARG B 29 51.171 -0.667 66.230 1.00 78.91 N ANISOU 3815 NH1 ARG B 29 13595 8349 8039 1816 -72 -1881 N ATOM 3816 NH2 ARG B 29 52.921 0.552 67.156 1.00 84.06 N ANISOU 3816 NH2 ARG B 29 14070 8950 8921 1887 -528 -2424 N ATOM 3817 N PRO B 30 54.894 -3.804 60.041 1.00 58.87 N ANISOU 3817 N PRO B 30 10839 5603 5924 1258 204 -815 N ATOM 3818 CA PRO B 30 55.967 -4.674 59.537 1.00 56.44 C ANISOU 3818 CA PRO B 30 10498 5349 5599 1238 234 -695 C ATOM 3819 C PRO B 30 56.921 -5.082 60.647 1.00 59.16 C ANISOU 3819 C PRO B 30 10826 5737 5914 1251 102 -824 C ATOM 3820 O PRO B 30 57.479 -4.235 61.352 1.00 59.57 O ANISOU 3820 O PRO B 30 10790 5696 6147 1252 -54 -994 O ATOM 3821 CB PRO B 30 56.667 -3.805 58.488 1.00 53.73 C ANISOU 3821 CB PRO B 30 10018 4858 5541 1213 306 -528 C ATOM 3822 CG PRO B 30 55.608 -2.905 58.025 1.00 56.84 C ANISOU 3822 CG PRO B 30 10419 5192 5984 1243 365 -483 C ATOM 3823 CD PRO B 30 54.794 -2.569 59.257 1.00 60.21 C ANISOU 3823 CD PRO B 30 10905 5610 6361 1233 251 -726 C ATOM 3824 N LYS B 31 57.104 -6.395 60.785 1.00 57.92 N ANISOU 3824 N LYS B 31 10732 5716 5558 1281 148 -760 N ATOM 3825 CA LYS B 31 58.086 -6.940 61.696 1.00 59.61 C ANISOU 3825 CA LYS B 31 10928 6005 5714 1328 37 -823 C ATOM 3826 C LYS B 31 59.453 -6.363 61.339 1.00 63.84 C ANISOU 3826 C LYS B 31 11292 6401 6564 1256 -58 -826 C ATOM 3827 O LYS B 31 59.613 -5.787 60.264 1.00 64.00 O ANISOU 3827 O LYS B 31 11222 6280 6814 1185 46 -696 O ATOM 3828 CB LYS B 31 58.067 -8.475 61.609 1.00 55.98 C ANISOU 3828 CB LYS B 31 10521 5666 5081 1362 166 -682 C ATOM 3829 CG LYS B 31 56.789 -9.086 62.206 1.00 51.46 C ANISOU 3829 CG LYS B 31 10055 5178 4320 1459 283 -666 C ATOM 3830 CD LYS B 31 56.686 -10.609 62.079 1.00 42.58 C ANISOU 3830 CD LYS B 31 8916 4096 3168 1488 445 -519 C ATOM 3831 CE LYS B 31 55.284 -11.079 62.505 1.00 46.20 C ANISOU 3831 CE LYS B 31 9410 4544 3601 1575 612 -474 C ATOM 3832 NZ LYS B 31 54.934 -12.546 62.485 1.00 43.19 N ANISOU 3832 NZ LYS B 31 8950 4125 3335 1618 811 -333 N ATOM 3833 N PRO B 32 60.439 -6.442 62.265 1.00 69.61 N ANISOU 3833 N PRO B 32 10542 8200 7706 731 -1274 -12 N ATOM 3834 CA PRO B 32 61.712 -5.732 62.073 1.00 73.19 C ANISOU 3834 CA PRO B 32 10896 8671 8241 709 -1258 -82 C ATOM 3835 C PRO B 32 62.287 -5.764 60.666 1.00 75.12 C ANISOU 3835 C PRO B 32 11112 8767 8663 813 -1130 -147 C ATOM 3836 O PRO B 32 62.335 -4.728 59.993 1.00 75.48 O ANISOU 3836 O PRO B 32 11196 8793 8689 771 -1030 -261 O ATOM 3837 CB PRO B 32 62.640 -6.451 63.059 1.00 74.01 C ANISOU 3837 CB PRO B 32 10832 8891 8399 673 -1434 102 C ATOM 3838 CG PRO B 32 61.751 -6.758 64.213 1.00 73.59 C ANISOU 3838 CG PRO B 32 10813 9008 8139 577 -1543 206 C ATOM 3839 CD PRO B 32 60.365 -7.024 63.621 1.00 71.76 C ANISOU 3839 CD PRO B 32 10733 8668 7864 641 -1444 168 C ATOM 3840 N LEU B 33 62.700 -6.950 60.209 1.00 75.43 N ANISOU 3840 N LEU B 33 11068 8712 8878 945 -1144 -78 N ATOM 3841 CA LEU B 33 63.518 -7.048 59.003 1.00 73.44 C ANISOU 3841 CA LEU B 33 10725 8407 8772 1054 -1020 -163 C ATOM 3842 C LEU B 33 62.771 -6.551 57.772 1.00 70.95 C ANISOU 3842 C LEU B 33 10549 8033 8376 1061 -851 -296 C ATOM 3843 O LEU B 33 63.369 -5.939 56.875 1.00 75.71 O ANISOU 3843 O LEU B 33 11084 8700 8983 1049 -732 -362 O ATOM 3844 CB LEU B 33 63.957 -8.490 58.798 1.00 76.52 C ANISOU 3844 CB LEU B 33 11002 8684 9390 1225 -1080 -121 C ATOM 3845 CG LEU B 33 65.207 -8.626 57.946 1.00 82.42 C ANISOU 3845 CG LEU B 33 11553 9466 10297 1347 -978 -208 C ATOM 3846 CD1 LEU B 33 66.344 -7.838 58.583 1.00 84.73 C ANISOU 3846 CD1 LEU B 33 11678 9926 10591 1239 -1023 -113 C ATOM 3847 CD2 LEU B 33 65.566 -10.089 57.723 1.00 86.05 C ANISOU 3847 CD2 LEU B 33 11892 9767 11035 1556 -1049 -226 C ATOM 3848 N LEU B 34 61.465 -6.820 57.698 1.00 67.11 N ANISOU 3848 N LEU B 34 10238 7450 7811 1063 -851 -305 N ATOM 3849 CA LEU B 34 60.669 -6.253 56.616 1.00 61.69 C ANISOU 3849 CA LEU B 34 9684 6714 7040 1035 -719 -397 C ATOM 3850 C LEU B 34 60.653 -4.733 56.688 1.00 59.13 C ANISOU 3850 C LEU B 34 9378 6459 6631 887 -688 -423 C ATOM 3851 O LEU B 34 60.792 -4.064 55.663 1.00 58.12 O ANISOU 3851 O LEU B 34 9241 6345 6495 838 -591 -458 O ATOM 3852 CB LEU B 34 59.242 -6.801 56.642 1.00 57.39 C ANISOU 3852 CB LEU B 34 9308 6053 6443 1049 -750 -369 C ATOM 3853 CG LEU B 34 58.318 -5.981 55.732 1.00 46.44 C ANISOU 3853 CG LEU B 34 8056 4627 4963 978 -642 -428 C ATOM 3854 CD1 LEU B 34 58.824 -6.045 54.318 1.00 42.62 C ANISOU 3854 CD1 LEU B 34 7539 4156 4498 1015 -521 -511 C ATOM 3855 CD2 LEU B 34 56.902 -6.477 55.781 1.00 40.67 C ANISOU 3855 CD2 LEU B 34 7474 3793 4188 982 -679 -377 C ATOM 3856 N LEU B 35 60.456 -4.172 57.889 1.00 58.32 N ANISOU 3856 N LEU B 35 9289 6404 6465 805 -788 -408 N ATOM 3857 CA LEU B 35 60.538 -2.723 58.053 1.00 60.69 C ANISOU 3857 CA LEU B 35 9592 6726 6744 678 -804 -472 C ATOM 3858 C LEU B 35 61.879 -2.207 57.536 1.00 62.87 C ANISOU 3858 C LEU B 35 9713 7062 7112 629 -791 -442 C ATOM 3859 O LEU B 35 61.930 -1.205 56.807 1.00 65.63 O ANISOU 3859 O LEU B 35 10055 7384 7498 533 -762 -446 O ATOM 3860 CB LEU B 35 60.304 -2.344 59.529 1.00 68.10 C ANISOU 3860 CB LEU B 35 10542 7747 7586 619 -922 -515 C ATOM 3861 CG LEU B 35 59.631 -1.014 59.977 1.00 70.73 C ANISOU 3861 CG LEU B 35 10946 8053 7877 533 -958 -665 C ATOM 3862 CD1 LEU B 35 59.147 -1.072 61.428 1.00 70.47 C ANISOU 3862 CD1 LEU B 35 10927 8176 7673 517 -1038 -740 C ATOM 3863 CD2 LEU B 35 60.509 0.216 59.827 1.00 70.42 C ANISOU 3863 CD2 LEU B 35 10833 7971 7952 426 -1026 -720 C ATOM 3864 N LYS B 36 62.970 -2.916 57.852 1.00 66.89 N ANISOU 3864 N LYS B 36 10075 7660 7680 686 -823 -379 N ATOM 3865 CA LYS B 36 64.280 -2.537 57.326 1.00 72.19 C ANISOU 3865 CA LYS B 36 10560 8428 8440 650 -797 -327 C ATOM 3866 C LYS B 36 64.252 -2.449 55.809 1.00 76.95 C ANISOU 3866 C LYS B 36 11141 9057 9039 664 -639 -337 C ATOM 3867 O LYS B 36 64.604 -1.414 55.228 1.00 82.34 O ANISOU 3867 O LYS B 36 11757 9796 9733 530 -627 -285 O ATOM 3868 CB LYS B 36 65.356 -3.529 57.763 1.00 72.07 C ANISOU 3868 CB LYS B 36 10370 8493 8521 751 -838 -257 C ATOM 3869 CG LYS B 36 66.745 -3.125 57.272 1.00 77.38 C ANISOU 3869 CG LYS B 36 10811 9304 9285 715 -805 -189 C ATOM 3870 CD LYS B 36 67.849 -3.746 58.125 1.00 84.22 C ANISOU 3870 CD LYS B 36 11489 10241 10271 762 -915 -92 C ATOM 3871 CE LYS B 36 68.884 -4.523 57.294 1.00 87.96 C ANISOU 3871 CE LYS B 36 11723 10812 10888 919 -798 -80 C ATOM 3872 NZ LYS B 36 70.109 -3.728 56.938 1.00 89.47 N ANISOU 3872 NZ LYS B 36 11680 11190 11124 821 -773 18 N ATOM 3873 N LEU B 37 63.820 -3.535 55.153 1.00 78.89 N ANISOU 3873 N LEU B 37 11436 9272 9268 809 -538 -395 N ATOM 3874 CA LEU B 37 63.693 -3.545 53.697 1.00 79.68 C ANISOU 3874 CA LEU B 37 11527 9441 9308 818 -384 -434 C ATOM 3875 C LEU B 37 62.793 -2.421 53.192 1.00 74.32 C ANISOU 3875 C LEU B 37 10973 8710 8555 650 -382 -394 C ATOM 3876 O LEU B 37 63.005 -1.913 52.085 1.00 76.78 O ANISOU 3876 O LEU B 37 11212 9148 8813 556 -297 -344 O ATOM 3877 CB LEU B 37 63.156 -4.896 53.233 1.00 85.20 C ANISOU 3877 CB LEU B 37 12305 10063 10004 998 -321 -546 C ATOM 3878 CG LEU B 37 62.983 -5.121 51.728 1.00 91.27 C ANISOU 3878 CG LEU B 37 13075 10933 10670 1024 -161 -640 C ATOM 3879 CD1 LEU B 37 63.176 -6.601 51.406 1.00 97.56 C ANISOU 3879 CD1 LEU B 37 13837 11686 11543 1254 -122 -806 C ATOM 3880 CD2 LEU B 37 61.614 -4.636 51.213 1.00 88.42 C ANISOU 3880 CD2 LEU B 37 12926 10476 10193 907 -157 -616 C ATOM 3881 N LEU B 38 61.781 -2.036 53.974 1.00 70.60 N ANISOU 3881 N LEU B 38 10666 8075 8085 608 -480 -406 N ATOM 3882 CA LEU B 38 60.827 -1.015 53.558 1.00 61.23 C ANISOU 3882 CA LEU B 38 9586 6789 6888 476 -500 -378 C ATOM 3883 C LEU B 38 61.403 0.380 53.597 1.00 69.62 C ANISOU 3883 C LEU B 38 10547 7860 8045 301 -594 -301 C ATOM 3884 O LEU B 38 60.972 1.235 52.819 1.00 73.95 O ANISOU 3884 O LEU B 38 11107 8361 8630 167 -610 -220 O ATOM 3885 CB LEU B 38 59.595 -1.030 54.439 1.00 45.88 C ANISOU 3885 CB LEU B 38 7810 4690 4932 509 -568 -441 C ATOM 3886 CG LEU B 38 58.560 -2.027 53.993 1.00 41.40 C ANISOU 3886 CG LEU B 38 7376 4061 4294 604 -501 -456 C ATOM 3887 CD1 LEU B 38 57.265 -1.826 54.735 1.00 40.34 C ANISOU 3887 CD1 LEU B 38 7371 3812 4143 605 -558 -481 C ATOM 3888 CD2 LEU B 38 58.381 -1.867 52.517 1.00 41.84 C ANISOU 3888 CD2 LEU B 38 7440 4146 4313 538 -411 -412 C ATOM 3889 N LYS B 39 62.332 0.654 54.502 1.00 73.74 N ANISOU 3889 N LYS B 39 10966 8423 8630 282 -689 -303 N ATOM 3890 CA LYS B 39 62.867 2.004 54.518 1.00 77.10 C ANISOU 3890 CA LYS B 39 11295 8820 9180 100 -819 -223 C ATOM 3891 C LYS B 39 64.083 2.180 53.617 1.00 83.23 C ANISOU 3891 C LYS B 39 11851 9801 9971 6 -773 -54 C ATOM 3892 O LYS B 39 64.471 3.326 53.356 1.00 87.41 O ANISOU 3892 O LYS B 39 12281 10312 10618 -185 -894 79 O ATOM 3893 CB LYS B 39 63.201 2.428 55.940 1.00 76.57 C ANISOU 3893 CB LYS B 39 11230 8691 9172 84 -982 -316 C ATOM 3894 CG LYS B 39 61.994 2.618 56.846 1.00 78.79 C ANISOU 3894 CG LYS B 39 11689 8822 9426 135 -1040 -494 C ATOM 3895 CD LYS B 39 62.470 2.840 58.282 1.00 84.35 C ANISOU 3895 CD LYS B 39 12374 9562 10114 122 -1182 -610 C ATOM 3896 CE LYS B 39 61.435 3.502 59.181 1.00 84.87 C ANISOU 3896 CE LYS B 39 12565 9515 10168 130 -1268 -832 C ATOM 3897 NZ LYS B 39 62.032 3.876 60.501 1.00 84.92 N ANISOU 3897 NZ LYS B 39 12536 9597 10134 82 -1423 -967 N ATOM 3898 N SER B 40 64.670 1.086 53.114 1.00 87.86 N ANISOU 3898 N SER B 40 12640 10581 10161 423 -829 -1227 N ATOM 3899 CA SER B 40 65.778 1.190 52.166 1.00 90.20 C ANISOU 3899 CA SER B 40 12809 10896 10569 322 -799 -1121 C ATOM 3900 C SER B 40 65.380 1.908 50.881 1.00 88.26 C ANISOU 3900 C SER B 40 12638 10465 10433 387 -644 -989 C ATOM 3901 O SER B 40 66.255 2.354 50.124 1.00 87.02 O ANISOU 3901 O SER B 40 12405 10261 10398 296 -579 -896 O ATOM 3902 CB SER B 40 66.304 -0.204 51.829 1.00 87.15 C ANISOU 3902 CB SER B 40 12243 10748 10121 399 -853 -1009 C ATOM 3903 OG SER B 40 65.241 -1.100 51.559 1.00 83.81 O ANISOU 3903 OG SER B 40 11841 10368 9635 611 -820 -957 O ATOM 3904 N VAL B 41 64.078 2.017 50.618 1.00 89.45 N ANISOU 3904 N VAL B 41 12924 10527 10536 561 -574 -968 N ATOM 3905 CA VAL B 41 63.584 2.695 49.432 1.00 90.42 C ANISOU 3905 CA VAL B 41 13115 10520 10720 676 -420 -829 C ATOM 3906 C VAL B 41 63.044 4.083 49.739 1.00 94.30 C ANISOU 3906 C VAL B 41 13786 10738 11307 628 -311 -878 C ATOM 3907 O VAL B 41 62.807 4.866 48.802 1.00 99.75 O ANISOU 3907 O VAL B 41 14530 11293 12079 711 -147 -732 O ATOM 3908 CB VAL B 41 62.506 1.847 48.730 1.00 88.84 C ANISOU 3908 CB VAL B 41 12905 10446 10403 934 -405 -770 C ATOM 3909 CG1 VAL B 41 63.064 0.502 48.354 1.00 86.51 C ANISOU 3909 CG1 VAL B 41 12415 10392 10063 976 -482 -736 C ATOM 3910 CG2 VAL B 41 61.313 1.674 49.641 1.00 89.19 C ANISOU 3910 CG2 VAL B 41 13074 10446 10370 1013 -444 -900 C ATOM 3911 N GLY B 42 62.846 4.422 51.005 1.00 92.14 N ANISOU 3911 N GLY B 42 13598 10386 11025 515 -380 -1070 N ATOM 3912 CA GLY B 42 62.476 5.784 51.312 1.00 97.26 C ANISOU 3912 CA GLY B 42 14397 10754 11804 439 -264 -1142 C ATOM 3913 C GLY B 42 61.259 5.883 52.196 1.00 96.84 C ANISOU 3913 C GLY B 42 14505 10643 11647 522 -296 -1273 C ATOM 3914 O GLY B 42 60.812 6.988 52.536 1.00 98.71 O ANISOU 3914 O GLY B 42 14879 10640 11985 473 -197 -1351 O ATOM 3915 N ALA B 43 60.707 4.733 52.569 1.00 94.44 N ANISOU 3915 N ALA B 43 14179 10540 11164 652 -412 -1293 N ATOM 3916 CA ALA B 43 59.649 4.735 53.569 1.00 94.31 C ANISOU 3916 CA ALA B 43 14298 10487 11048 723 -450 -1423 C ATOM 3917 C ALA B 43 60.198 5.232 54.896 1.00 96.55 C ANISOU 3917 C ALA B 43 14594 10756 11333 534 -538 -1644 C ATOM 3918 O ALA B 43 61.396 5.147 55.171 1.00100.06 O ANISOU 3918 O ALA B 43 14901 11310 11809 372 -618 -1710 O ATOM 3919 CB ALA B 43 59.061 3.339 53.751 1.00 91.62 C ANISOU 3919 CB ALA B 43 13897 10354 10558 895 -531 -1395 C ATOM 3920 N GLN B 44 59.306 5.755 55.721 1.00 93.49 N ANISOU 3920 N GLN B 44 14360 10256 10904 566 -526 -1775 N ATOM 3921 CA GLN B 44 59.697 6.306 57.015 1.00 93.30 C ANISOU 3921 CA GLN B 44 14347 10240 10861 411 -610 -2028 C ATOM 3922 C GLN B 44 58.797 5.872 58.159 1.00 86.18 C ANISOU 3922 C GLN B 44 13533 9447 9766 540 -687 -2129 C ATOM 3923 O GLN B 44 59.275 5.791 59.294 1.00 85.78 O ANISOU 3923 O GLN B 44 13422 9566 9603 472 -807 -2311 O ATOM 3924 CB GLN B 44 59.706 7.838 56.932 1.00101.27 C ANISOU 3924 CB GLN B 44 15456 10934 12089 264 -475 -2140 C ATOM 3925 CG GLN B 44 60.691 8.410 55.902 1.00106.69 C ANISOU 3925 CG GLN B 44 16046 11482 13012 126 -361 -2039 C ATOM 3926 CD GLN B 44 60.595 9.915 55.741 1.00110.19 C ANISOU 3926 CD GLN B 44 16582 11560 13725 9 -165 -2109 C ATOM 3927 OE1 GLN B 44 59.525 10.497 55.870 1.00109.80 O ANISOU 3927 OE1 GLN B 44 16704 11324 13689 103 -64 -2115 O ATOM 3928 NE2 GLN B 44 61.725 10.552 55.446 1.00114.79 N ANISOU 3928 NE2 GLN B 44 17040 12023 14552 -196 -91 -2156 N ATOM 3929 N LYS B 45 57.540 5.538 57.884 1.00 82.06 N ANISOU 3929 N LYS B 45 13129 8861 9191 739 -621 -2014 N ATOM 3930 CA LYS B 45 56.515 5.158 58.853 1.00 79.19 C ANISOU 3930 CA LYS B 45 12862 8554 8673 888 -652 -2073 C ATOM 3931 C LYS B 45 56.889 3.972 59.749 1.00 82.89 C ANISOU 3931 C LYS B 45 13200 9327 8965 960 -775 -2077 C ATOM 3932 O LYS B 45 57.974 3.397 59.620 1.00 86.75 O ANISOU 3932 O LYS B 45 13518 9999 9442 891 -847 -2037 O ATOM 3933 CB LYS B 45 55.233 4.863 58.067 1.00 69.56 C ANISOU 3933 CB LYS B 45 11735 7222 7472 1089 -546 -1918 C ATOM 3934 CG LYS B 45 53.962 5.391 58.685 1.00 67.12 C ANISOU 3934 CG LYS B 45 11615 6766 7121 1190 -490 -1994 C ATOM 3935 CD LYS B 45 52.707 4.976 57.921 1.00 62.70 C ANISOU 3935 CD LYS B 45 11110 6142 6572 1400 -398 -1858 C ATOM 3936 CE LYS B 45 52.525 5.647 56.584 1.00 59.87 C ANISOU 3936 CE LYS B 45 10785 5634 6331 1421 -283 -1744 C ATOM 3937 NZ LYS B 45 51.135 5.351 56.087 1.00 51.95 N ANISOU 3937 NZ LYS B 45 9839 4599 5301 1646 -209 -1673 N ATOM 3938 N ASP B 46 55.998 3.610 60.678 1.00 84.94 N ANISOU 3938 N ASP B 46 13538 9646 9091 1115 -782 -2108 N ATOM 3939 CA ASP B 46 56.131 2.397 61.474 1.00 82.77 C ANISOU 3939 CA ASP B 46 13146 9642 8660 1252 -841 -2044 C ATOM 3940 C ASP B 46 54.851 1.583 61.470 1.00 76.10 C ANISOU 3940 C ASP B 46 12355 8750 7809 1483 -745 -1912 C ATOM 3941 O ASP B 46 54.700 0.693 62.303 1.00 80.25 O ANISOU 3941 O ASP B 46 12817 9450 8223 1634 -747 -1851 O ATOM 3942 CB ASP B 46 56.527 2.743 62.912 1.00 88.11 C ANISOU 3942 CB ASP B 46 13816 10510 9151 1227 -945 -2232 C ATOM 3943 CG ASP B 46 58.034 2.910 63.081 1.00 95.28 C ANISOU 3943 CG ASP B 46 14556 11616 10031 1047 -1065 -2342 C ATOM 3944 OD1 ASP B 46 58.758 2.791 62.063 1.00 97.17 O ANISOU 3944 OD1 ASP B 46 14701 11808 10412 933 -1056 -2252 O ATOM 3945 OD2 ASP B 46 58.485 3.216 64.219 1.00 97.97 O ANISOU 3945 OD2 ASP B 46 14850 12169 10206 1021 -1170 -2538 O ATOM 3946 N THR B 47 53.932 1.862 60.551 1.00 72.29 N ANISOU 3946 N THR B 47 11971 8043 7451 1528 -649 -1863 N ATOM 3947 CA THR B 47 52.625 1.220 60.544 1.00 68.85 C ANISOU 3947 CA THR B 47 11580 7541 7038 1735 -554 -1786 C ATOM 3948 C THR B 47 51.846 1.620 59.286 1.00 70.49 C ANISOU 3948 C THR B 47 11854 7552 7377 1765 -468 -1751 C ATOM 3949 O THR B 47 51.286 2.719 59.203 1.00 72.03 O ANISOU 3949 O THR B 47 12216 7568 7584 1737 -431 -1816 O ATOM 3950 CB THR B 47 51.861 1.569 61.833 1.00 67.94 C ANISOU 3950 CB THR B 47 11606 7412 6796 1824 -547 -1874 C ATOM 3951 OG1 THR B 47 50.478 1.217 61.698 1.00 62.60 O ANISOU 3951 OG1 THR B 47 11000 6606 6179 2002 -437 -1817 O ATOM 3952 CG2 THR B 47 52.013 3.074 62.203 1.00 71.72 C ANISOU 3952 CG2 THR B 47 12242 7770 7239 1667 -590 -2059 C ATOM 3953 N TYR B 48 51.776 0.710 58.316 1.00 64.13 N ANISOU 3953 N TYR B 48 10904 6796 6665 1842 -429 -1654 N ATOM 3954 CA TYR B 48 51.359 0.971 56.944 1.00 52.48 C ANISOU 3954 CA TYR B 48 9423 5235 5282 1879 -371 -1619 C ATOM 3955 C TYR B 48 50.027 0.301 56.647 1.00 47.22 C ANISOU 3955 C TYR B 48 8730 4535 4675 2078 -288 -1621 C ATOM 3956 O TYR B 48 49.538 -0.524 57.418 1.00 47.21 O ANISOU 3956 O TYR B 48 8687 4560 4688 2177 -257 -1626 O ATOM 3957 CB TYR B 48 52.417 0.444 55.977 1.00 50.19 C ANISOU 3957 CB TYR B 48 8948 5073 5047 1813 -403 -1547 C ATOM 3958 CG TYR B 48 53.823 0.941 56.250 1.00 54.60 C ANISOU 3958 CG TYR B 48 9487 5684 5573 1612 -484 -1549 C ATOM 3959 CD1 TYR B 48 54.535 0.555 57.380 1.00 59.89 C ANISOU 3959 CD1 TYR B 48 10107 6484 6164 1548 -562 -1581 C ATOM 3960 CD2 TYR B 48 54.439 1.802 55.366 1.00 57.72 C ANISOU 3960 CD2 TYR B 48 9898 6013 6020 1502 -470 -1517 C ATOM 3961 CE1 TYR B 48 55.818 1.028 57.608 1.00 61.22 C ANISOU 3961 CE1 TYR B 48 10231 6722 6307 1363 -645 -1619 C ATOM 3962 CE2 TYR B 48 55.701 2.272 55.583 1.00 59.32 C ANISOU 3962 CE2 TYR B 48 10062 6243 6234 1310 -529 -1539 C ATOM 3963 CZ TYR B 48 56.390 1.886 56.693 1.00 60.39 C ANISOU 3963 CZ TYR B 48 10138 6515 6292 1232 -626 -1608 C ATOM 3964 OH TYR B 48 57.660 2.383 56.854 1.00 65.14 O ANISOU 3964 OH TYR B 48 10676 7160 6912 1037 -691 -1661 O ATOM 3965 N THR B 49 49.432 0.656 55.513 1.00 47.82 N ANISOU 3965 N THR B 49 8812 4564 4792 2153 -238 -1616 N ATOM 3966 CA THR B 49 48.312 -0.127 55.001 1.00 52.19 C ANISOU 3966 CA THR B 49 9198 5182 5450 2278 -172 -1606 C ATOM 3967 C THR B 49 48.865 -1.246 54.111 1.00 50.93 C ANISOU 3967 C THR B 49 8828 5160 5364 2336 -180 -1630 C ATOM 3968 O THR B 49 50.062 -1.316 53.837 1.00 45.00 O ANISOU 3968 O THR B 49 8027 4482 4588 2240 -236 -1589 O ATOM 3969 CB THR B 49 47.284 0.773 54.266 1.00 45.60 C ANISOU 3969 CB THR B 49 8390 4318 4619 2313 -120 -1566 C ATOM 3970 OG1 THR B 49 47.607 0.913 52.885 1.00 45.74 O ANISOU 3970 OG1 THR B 49 8358 4410 4611 2395 -116 -1563 O ATOM 3971 CG2 THR B 49 47.243 2.141 54.861 1.00 46.67 C ANISOU 3971 CG2 THR B 49 8773 4285 4677 2248 -110 -1556 C ATOM 3972 N MET B 50 48.000 -2.156 53.671 1.00 56.73 N ANISOU 3972 N MET B 50 11096 6126 4332 992 -115 -618 N ATOM 3973 CA MET B 50 48.512 -3.220 52.816 1.00 56.73 C ANISOU 3973 CA MET B 50 11100 6038 4416 955 -136 -492 C ATOM 3974 C MET B 50 48.969 -2.665 51.471 1.00 53.65 C ANISOU 3974 C MET B 50 10737 5529 4117 932 -225 -545 C ATOM 3975 O MET B 50 50.078 -2.968 51.009 1.00 48.66 O ANISOU 3975 O MET B 50 10131 4870 3489 909 -266 -505 O ATOM 3976 CB MET B 50 47.463 -4.303 52.600 1.00 63.48 C ANISOU 3976 CB MET B 50 11891 6844 5383 929 -38 -419 C ATOM 3977 CG MET B 50 48.014 -5.506 51.812 1.00 67.06 C ANISOU 3977 CG MET B 50 12342 7178 5961 882 -22 -344 C ATOM 3978 SD MET B 50 49.346 -6.324 52.730 1.00 66.63 S ANISOU 3978 SD MET B 50 12321 7163 5833 939 16 -145 S ATOM 3979 CE MET B 50 48.476 -6.499 54.261 1.00 70.44 C ANISOU 3979 CE MET B 50 12770 7801 6192 984 144 -17 C ATOM 3980 N LYS B 51 48.116 -1.862 50.823 1.00 49.87 N ANISOU 3980 N LYS B 51 10238 5001 3708 956 -243 -607 N ATOM 3981 CA LYS B 51 48.480 -1.284 49.538 1.00 45.70 C ANISOU 3981 CA LYS B 51 9730 4401 3232 960 -311 -595 C ATOM 3982 C LYS B 51 49.799 -0.528 49.644 1.00 49.01 C ANISOU 3982 C LYS B 51 10212 4767 3645 935 -338 -610 C ATOM 3983 O LYS B 51 50.603 -0.509 48.700 1.00 53.12 O ANISOU 3983 O LYS B 51 10750 5251 4182 909 -366 -557 O ATOM 3984 CB LYS B 51 47.359 -0.374 49.041 1.00 46.45 C ANISOU 3984 CB LYS B 51 9778 4477 3394 1038 -320 -603 C ATOM 3985 CG LYS B 51 45.986 -1.061 48.827 1.00 67.53 C ANISOU 3985 CG LYS B 51 12332 7241 6085 1050 -310 -616 C ATOM 3986 CD LYS B 51 44.870 -0.005 48.572 1.00 63.32 C ANISOU 3986 CD LYS B 51 11718 6718 5622 1172 -321 -609 C ATOM 3987 CE LYS B 51 43.520 -0.559 48.116 1.00 60.33 C ANISOU 3987 CE LYS B 51 11170 6485 5269 1186 -344 -630 C ATOM 3988 NZ LYS B 51 43.488 -0.654 46.644 1.00 63.72 N ANISOU 3988 NZ LYS B 51 11541 7033 5638 1204 -459 -581 N ATOM 3989 N GLU B 52 50.070 0.037 50.821 1.00 48.06 N ANISOU 3989 N GLU B 52 10101 4670 3489 929 -320 -706 N ATOM 3990 CA GLU B 52 51.299 0.800 51.025 1.00 46.86 C ANISOU 3990 CA GLU B 52 9967 4482 3357 872 -347 -782 C ATOM 3991 C GLU B 52 52.524 -0.117 51.017 1.00 46.36 C ANISOU 3991 C GLU B 52 9883 4514 3216 828 -391 -714 C ATOM 3992 O GLU B 52 53.569 0.208 50.430 1.00 46.39 O ANISOU 3992 O GLU B 52 9879 4467 3280 776 -412 -707 O ATOM 3993 CB GLU B 52 51.208 1.574 52.339 1.00 48.36 C ANISOU 3993 CB GLU B 52 10141 4728 3504 862 -323 -978 C ATOM 3994 CG GLU B 52 50.390 2.810 52.298 1.00 52.05 C ANISOU 3994 CG GLU B 52 10619 5027 4131 902 -257 -1090 C ATOM 3995 CD GLU B 52 51.000 3.879 53.142 1.00 64.04 C ANISOU 3995 CD GLU B 52 12123 6507 5704 831 -231 -1352 C ATOM 3996 OE1 GLU B 52 50.699 3.891 54.355 1.00 65.02 O ANISOU 3996 OE1 GLU B 52 12217 6808 5680 836 -210 -1536 O ATOM 3997 OE2 GLU B 52 51.774 4.704 52.585 1.00 72.78 O ANISOU 3997 OE2 GLU B 52 13235 7417 7001 760 -218 -1386 O ATOM 3998 N VAL B 53 52.411 -1.284 51.650 1.00 46.24 N ANISOU 3998 N VAL B 53 9847 4628 3096 862 -382 -637 N ATOM 3999 CA VAL B 53 53.522 -2.221 51.610 1.00 46.17 C ANISOU 3999 CA VAL B 53 9803 4683 3055 864 -406 -535 C ATOM 4000 C VAL B 53 53.717 -2.748 50.204 1.00 45.23 C ANISOU 4000 C VAL B 53 9698 4440 3047 852 -386 -470 C ATOM 4001 O VAL B 53 54.845 -2.846 49.718 1.00 45.25 O ANISOU 4001 O VAL B 53 9673 4442 3080 832 -403 -450 O ATOM 4002 CB VAL B 53 53.321 -3.376 52.599 1.00 46.88 C ANISOU 4002 CB VAL B 53 9864 4903 3046 932 -368 -403 C ATOM 4003 CG1 VAL B 53 54.648 -4.027 52.839 1.00 47.57 C ANISOU 4003 CG1 VAL B 53 9888 5092 3096 971 -407 -295 C ATOM 4004 CG2 VAL B 53 52.770 -2.890 53.894 1.00 51.34 C ANISOU 4004 CG2 VAL B 53 10419 5641 3448 954 -360 -470 C ATOM 4005 N LEU B 54 52.632 -3.135 49.546 1.00 44.77 N ANISOU 4005 N LEU B 54 9659 4314 3039 860 -347 -461 N ATOM 4006 CA LEU B 54 52.760 -3.687 48.208 1.00 44.44 C ANISOU 4006 CA LEU B 54 9613 4218 3053 842 -330 -456 C ATOM 4007 C LEU B 54 53.517 -2.723 47.309 1.00 52.35 C ANISOU 4007 C LEU B 54 10632 5210 4050 819 -359 -460 C ATOM 4008 O LEU B 54 54.502 -3.106 46.658 1.00 57.06 O ANISOU 4008 O LEU B 54 11209 5815 4657 804 -339 -443 O ATOM 4009 CB LEU B 54 51.375 -4.014 47.664 1.00 44.51 C ANISOU 4009 CB LEU B 54 9604 4220 3089 838 -312 -500 C ATOM 4010 CG LEU B 54 50.846 -5.255 48.382 1.00 44.98 C ANISOU 4010 CG LEU B 54 9628 4243 3219 831 -233 -477 C ATOM 4011 CD1 LEU B 54 49.364 -5.493 48.203 1.00 45.46 C ANISOU 4011 CD1 LEU B 54 9631 4311 3332 801 -206 -544 C ATOM 4012 CD2 LEU B 54 51.629 -6.443 47.883 1.00 45.38 C ANISOU 4012 CD2 LEU B 54 9662 4215 3366 817 -171 -472 C ATOM 4013 N PHE B 55 53.085 -1.455 47.285 1.00 49.53 N ANISOU 4013 N PHE B 55 10300 4816 3703 823 -378 -468 N ATOM 4014 CA PHE B 55 53.832 -0.386 46.625 1.00 46.70 C ANISOU 4014 CA PHE B 55 9955 4398 3391 795 -366 -428 C ATOM 4015 C PHE B 55 55.316 -0.413 46.936 1.00 45.49 C ANISOU 4015 C PHE B 55 9762 4257 3267 730 -361 -448 C ATOM 4016 O PHE B 55 56.123 -0.600 46.021 1.00 46.49 O ANISOU 4016 O PHE B 55 9867 4402 3395 709 -325 -393 O ATOM 4017 CB PHE B 55 53.284 0.977 47.033 1.00 47.73 C ANISOU 4017 CB PHE B 55 10110 4414 3613 810 -353 -448 C ATOM 4018 CG PHE B 55 52.147 1.458 46.204 1.00 47.95 C ANISOU 4018 CG PHE B 55 10147 4418 3652 899 -346 -352 C ATOM 4019 CD1 PHE B 55 52.130 1.262 44.847 1.00 48.77 C ANISOU 4019 CD1 PHE B 55 10244 4610 3677 933 -349 -225 C ATOM 4020 CD2 PHE B 55 51.086 2.097 46.788 1.00 50.18 C ANISOU 4020 CD2 PHE B 55 10427 4636 4005 965 -337 -390 C ATOM 4021 CE1 PHE B 55 51.070 1.718 44.079 1.00 49.33 C ANISOU 4021 CE1 PHE B 55 10292 4735 3715 1041 -367 -110 C ATOM 4022 CE2 PHE B 55 50.032 2.544 46.023 1.00 54.86 C ANISOU 4022 CE2 PHE B 55 10994 5237 4614 1079 -341 -273 C ATOM 4023 CZ PHE B 55 50.028 2.345 44.665 1.00 48.46 C ANISOU 4023 CZ PHE B 55 10164 4548 3700 1120 -370 -120 C ATOM 4024 N TYR B 56 55.685 -0.199 48.209 1.00 47.89 N ANISOU 4024 N TYR B 56 10033 4593 3572 702 -397 -539 N ATOM 4025 CA TYR B 56 57.104 -0.022 48.509 1.00 49.86 C ANISOU 4025 CA TYR B 56 10198 4895 3852 631 -415 -582 C ATOM 4026 C TYR B 56 57.889 -1.290 48.181 1.00 51.50 C ANISOU 4026 C TYR B 56 10349 5199 4021 673 -412 -499 C ATOM 4027 O TYR B 56 59.033 -1.219 47.729 1.00 52.15 O ANISOU 4027 O TYR B 56 10354 5304 4158 630 -392 -487 O ATOM 4028 CB TYR B 56 57.318 0.391 49.978 1.00 53.20 C ANISOU 4028 CB TYR B 56 10563 5425 4226 596 -480 -734 C ATOM 4029 CG TYR B 56 57.082 1.875 50.368 1.00 60.08 C ANISOU 4029 CG TYR B 56 11444 6171 5213 510 -455 -912 C ATOM 4030 CD1 TYR B 56 58.072 2.850 50.193 1.00 63.00 C ANISOU 4030 CD1 TYR B 56 11741 6446 5751 377 -426 -1018 C ATOM 4031 CD2 TYR B 56 55.889 2.281 50.977 1.00 64.01 C ANISOU 4031 CD2 TYR B 56 12004 6630 5689 558 -438 -998 C ATOM 4032 CE1 TYR B 56 57.857 4.198 50.572 1.00 66.08 C ANISOU 4032 CE1 TYR B 56 12132 6653 6322 286 -368 -1214 C ATOM 4033 CE2 TYR B 56 55.666 3.621 51.354 1.00 68.47 C ANISOU 4033 CE2 TYR B 56 12570 7037 6408 494 -385 -1194 C ATOM 4034 CZ TYR B 56 56.652 4.574 51.153 1.00 72.28 C ANISOU 4034 CZ TYR B 56 12991 7379 7092 355 -346 -1309 C ATOM 4035 OH TYR B 56 56.420 5.890 51.546 1.00 80.24 O ANISOU 4035 OH TYR B 56 13997 8170 8323 281 -260 -1534 O ATOM 4036 N LEU B 57 57.273 -2.459 48.339 1.00 52.65 N ANISOU 4036 N LEU B 57 10519 5370 4114 757 -405 -442 N ATOM 4037 CA LEU B 57 57.984 -3.715 48.115 1.00 51.55 C ANISOU 4037 CA LEU B 57 10322 5263 4003 817 -370 -370 C ATOM 4038 C LEU B 57 58.310 -3.907 46.640 1.00 51.08 C ANISOU 4038 C LEU B 57 10269 5149 3992 798 -294 -379 C ATOM 4039 O LEU B 57 59.474 -4.137 46.274 1.00 47.88 O ANISOU 4039 O LEU B 57 9779 4782 3632 802 -259 -365 O ATOM 4040 CB LEU B 57 57.141 -4.875 48.644 1.00 50.48 C ANISOU 4040 CB LEU B 57 10213 5100 3868 896 -337 -305 C ATOM 4041 CG LEU B 57 57.633 -6.315 48.560 1.00 48.79 C ANISOU 4041 CG LEU B 57 9946 4835 3756 983 -258 -212 C ATOM 4042 CD1 LEU B 57 58.990 -6.506 49.248 1.00 50.81 C ANISOU 4042 CD1 LEU B 57 10079 5221 4005 1059 -300 -112 C ATOM 4043 CD2 LEU B 57 56.599 -7.218 49.195 1.00 46.96 C ANISOU 4043 CD2 LEU B 57 9747 4526 3568 1030 -194 -132 C ATOM 4044 N GLY B 58 57.280 -3.834 45.785 1.00 53.41 N ANISOU 4044 N GLY B 58 10640 5399 4253 788 -268 -408 N ATOM 4045 CA GLY B 58 57.521 -3.770 44.356 1.00 45.79 C ANISOU 4045 CA GLY B 58 9679 4468 3253 769 -206 -422 C ATOM 4046 C GLY B 58 58.541 -2.711 43.996 1.00 54.47 C ANISOU 4046 C GLY B 58 10744 5586 4366 715 -180 -362 C ATOM 4047 O GLY B 58 59.412 -2.931 43.145 1.00 47.26 O ANISOU 4047 O GLY B 58 9779 4731 3445 708 -99 -353 O ATOM 4048 N GLN B 59 58.487 -1.565 44.678 1.00 54.77 N ANISOU 4048 N GLN B 59 10794 5563 4453 667 -223 -342 N ATOM 4049 CA GLN B 59 59.481 -0.533 44.423 1.00 56.02 C ANISOU 4049 CA GLN B 59 10899 5688 4700 581 -171 -302 C ATOM 4050 C GLN B 59 60.882 -1.027 44.751 1.00 58.27 C ANISOU 4050 C GLN B 59 11046 6054 5042 553 -163 -341 C ATOM 4051 O GLN B 59 61.839 -0.740 44.024 1.00 60.03 O ANISOU 4051 O GLN B 59 11193 6300 5317 499 -71 -298 O ATOM 4052 CB GLN B 59 59.159 0.728 45.211 1.00 57.90 C ANISOU 4052 CB GLN B 59 11159 5800 5042 518 -200 -341 C ATOM 4053 CG GLN B 59 60.221 1.795 45.142 1.00 64.44 C ANISOU 4053 CG GLN B 59 11905 6540 6040 390 -128 -346 C ATOM 4054 CD GLN B 59 59.639 3.192 45.282 1.00 71.04 C ANISOU 4054 CD GLN B 59 12799 7157 7038 341 -77 -342 C ATOM 4055 OE1 GLN B 59 58.482 3.423 44.957 1.00 74.58 O ANISOU 4055 OE1 GLN B 59 13351 7538 7448 437 -71 -252 O ATOM 4056 NE2 GLN B 59 60.437 4.127 45.778 1.00 74.62 N ANISOU 4056 NE2 GLN B 59 13162 7490 7702 193 -32 -458 N ATOM 4057 N TYR B 60 61.006 -1.803 45.825 1.00 56.64 N ANISOU 4057 N TYR B 60 10787 5914 4819 606 -248 -392 N ATOM 4058 CA TYR B 60 62.296 -2.345 46.227 1.00 59.75 C ANISOU 4058 CA TYR B 60 11016 6426 5261 624 -263 -398 C ATOM 4059 C TYR B 60 62.844 -3.278 45.156 1.00 63.49 C ANISOU 4059 C TYR B 60 11451 6914 5758 691 -149 -356 C ATOM 4060 O TYR B 60 64.009 -3.173 44.748 1.00 64.35 O ANISOU 4060 O TYR B 60 11423 7089 5937 660 -86 -351 O ATOM 4061 CB TYR B 60 62.128 -3.089 47.547 1.00 59.40 C ANISOU 4061 CB TYR B 60 10934 6478 5156 720 -369 -387 C ATOM 4062 CG TYR B 60 63.325 -3.867 48.048 1.00 63.63 C ANISOU 4062 CG TYR B 60 11283 7172 5721 808 -401 -332 C ATOM 4063 CD1 TYR B 60 64.330 -3.236 48.773 1.00 67.72 C ANISOU 4063 CD1 TYR B 60 11618 7876 6238 743 -499 -398 C ATOM 4064 CD2 TYR B 60 63.447 -5.221 47.809 1.00 65.74 C ANISOU 4064 CD2 TYR B 60 11532 7403 6042 961 -331 -225 C ATOM 4065 CE1 TYR B 60 65.411 -3.937 49.256 1.00 72.30 C ANISOU 4065 CE1 TYR B 60 11986 8655 6828 851 -552 -326 C ATOM 4066 CE2 TYR B 60 64.531 -5.933 48.278 1.00 71.24 C ANISOU 4066 CE2 TYR B 60 12039 8234 6794 1085 -352 -131 C ATOM 4067 CZ TYR B 60 65.512 -5.292 49.005 1.00 76.33 C ANISOU 4067 CZ TYR B 60 12488 9116 7396 1043 -476 -163 C ATOM 4068 OH TYR B 60 66.591 -6.023 49.470 1.00 82.11 O ANISOU 4068 OH TYR B 60 12994 10034 8171 1197 -515 -44 O ATOM 4069 N ILE B 61 61.997 -4.202 44.692 1.00 65.09 N ANISOU 4069 N ILE B 61 11754 7059 5916 773 -106 -360 N ATOM 4070 CA ILE B 61 62.421 -5.186 43.694 1.00 59.45 C ANISOU 4070 CA ILE B 61 11004 6351 5233 836 19 -395 C ATOM 4071 C ILE B 61 62.843 -4.489 42.415 1.00 58.61 C ANISOU 4071 C ILE B 61 10892 6315 5062 762 123 -398 C ATOM 4072 O ILE B 61 63.850 -4.847 41.795 1.00 60.40 O ANISOU 4072 O ILE B 61 11010 6611 5329 783 237 -418 O ATOM 4073 CB ILE B 61 61.304 -6.210 43.407 1.00 55.04 C ANISOU 4073 CB ILE B 61 10545 5704 4663 891 53 -468 C ATOM 4074 CG1 ILE B 61 61.038 -7.095 44.626 1.00 52.58 C ANISOU 4074 CG1 ILE B 61 10219 5302 4456 981 12 -407 C ATOM 4075 CG2 ILE B 61 61.649 -7.029 42.153 1.00 52.16 C ANISOU 4075 CG2 ILE B 61 10149 5359 4311 921 202 -594 C ATOM 4076 CD1 ILE B 61 59.697 -7.754 44.589 1.00 48.30 C ANISOU 4076 CD1 ILE B 61 9776 4646 3931 980 34 -469 C ATOM 4077 N MET B 62 62.073 -3.500 41.983 1.00 57.87 N ANISOU 4077 N MET B 62 10905 6216 4868 695 106 -352 N ATOM 4078 CA MET B 62 62.406 -2.830 40.738 1.00 62.43 C ANISOU 4078 CA MET B 62 11482 6882 5357 649 226 -281 C ATOM 4079 C MET B 62 63.564 -1.868 40.881 1.00 66.81 C ANISOU 4079 C MET B 62 11924 7420 6040 550 285 -194 C ATOM 4080 O MET B 62 64.144 -1.458 39.870 1.00 65.83 O ANISOU 4080 O MET B 62 11759 7376 5875 512 433 -106 O ATOM 4081 CB MET B 62 61.191 -2.099 40.224 1.00 60.03 C ANISOU 4081 CB MET B 62 11308 6584 4915 647 194 -200 C ATOM 4082 CG MET B 62 60.000 -2.977 40.180 1.00 59.42 C ANISOU 4082 CG MET B 62 11302 6537 4739 712 119 -319 C ATOM 4083 SD MET B 62 58.732 -2.124 39.299 1.00 63.44 S ANISOU 4083 SD MET B 62 11900 7157 5048 740 85 -202 S ATOM 4084 CE MET B 62 59.776 -1.117 38.315 1.00 68.98 C ANISOU 4084 CE MET B 62 12567 7945 5698 709 241 14 C ATOM 4085 N THR B 63 63.900 -1.490 42.110 1.00 70.40 N ANISOU 4085 N THR B 63 12311 7798 6639 497 183 -227 N ATOM 4086 CA THR B 63 65.068 -0.657 42.311 1.00 68.94 C ANISOU 4086 CA THR B 63 11970 7610 6615 370 234 -212 C ATOM 4087 C THR B 63 66.332 -1.492 42.336 1.00 63.65 C ANISOU 4087 C THR B 63 11099 7076 6008 410 273 -261 C ATOM 4088 O THR B 63 67.382 -1.032 41.888 1.00 62.70 O ANISOU 4088 O THR B 63 10827 7006 5991 319 393 -231 O ATOM 4089 CB THR B 63 64.924 0.131 43.607 1.00 71.16 C ANISOU 4089 CB THR B 63 12227 7803 7006 281 100 -298 C ATOM 4090 OG1 THR B 63 63.598 0.667 43.677 1.00 74.10 O ANISOU 4090 OG1 THR B 63 12787 8043 7326 298 62 -268 O ATOM 4091 CG2 THR B 63 65.884 1.285 43.600 1.00 75.39 C ANISOU 4091 CG2 THR B 63 12619 8278 7748 96 184 -312 C ATOM 4092 N LYS B 64 66.241 -2.724 42.825 1.00 75.89 N ANISOU 4092 N LYS B 64 10415 8790 9630 851 2078 754 N ATOM 4093 CA LYS B 64 67.401 -3.582 42.998 1.00 78.43 C ANISOU 4093 CA LYS B 64 10482 9257 10062 940 2114 592 C ATOM 4094 C LYS B 64 67.560 -4.596 41.872 1.00 76.07 C ANISOU 4094 C LYS B 64 10154 9002 9746 1030 2166 449 C ATOM 4095 O LYS B 64 68.270 -5.584 42.058 1.00 75.23 O ANISOU 4095 O LYS B 64 9870 8973 9742 1180 2161 324 O ATOM 4096 CB LYS B 64 67.324 -4.326 44.342 1.00 80.48 C ANISOU 4096 CB LYS B 64 10622 9442 10515 1124 1967 624 C ATOM 4097 CG LYS B 64 67.427 -3.461 45.602 1.00 78.05 C ANISOU 4097 CG LYS B 64 10278 9125 10250 1055 1917 737 C ATOM 4098 CD LYS B 64 67.758 -4.303 46.846 1.00 75.13 C ANISOU 4098 CD LYS B 64 9733 8748 10064 1257 1804 716 C ATOM 4099 CE LYS B 64 69.150 -4.004 47.431 1.00 77.14 C ANISOU 4099 CE LYS B 64 9731 9245 10331 1227 1874 612 C ATOM 4100 NZ LYS B 64 69.172 -3.908 48.933 1.00 78.14 N ANISOU 4100 NZ LYS B 64 9769 9340 10580 1308 1760 694 N ATOM 4101 N ARG B 65 66.889 -4.405 40.735 1.00 77.98 N ANISOU 4101 N ARG B 65 10575 9198 9854 965 2211 463 N ATOM 4102 CA ARG B 65 67.020 -5.252 39.548 1.00 80.90 C ANISOU 4102 CA ARG B 65 10935 9616 10186 1022 2275 327 C ATOM 4103 C ARG B 65 66.408 -6.649 39.733 1.00 80.40 C ANISOU 4103 C ARG B 65 10867 9430 10252 1225 2163 291 C ATOM 4104 O ARG B 65 66.412 -7.448 38.789 1.00 79.48 O ANISOU 4104 O ARG B 65 10759 9330 10107 1279 2210 180 O ATOM 4105 CB ARG B 65 68.495 -5.390 39.121 1.00 91.47 C ANISOU 4105 CB ARG B 65 12072 11174 11509 986 2416 155 C ATOM 4106 CG ARG B 65 68.801 -6.191 37.839 1.00103.49 C ANISOU 4106 CG ARG B 65 13571 12770 12979 1034 2503 3 C ATOM 4107 CD ARG B 65 69.295 -7.608 38.134 1.00109.74 C ANISOU 4107 CD ARG B 65 14200 13584 13911 1263 2459 -121 C ATOM 4108 NE ARG B 65 68.781 -8.548 37.138 1.00115.60 N ANISOU 4108 NE ARG B 65 15039 14251 14632 1346 2467 -190 N ATOM 4109 CZ ARG B 65 68.731 -9.869 37.311 1.00119.42 C ANISOU 4109 CZ ARG B 65 15497 14657 15219 1552 2416 -263 C ATOM 4110 NH1 ARG B 65 68.244 -10.654 36.350 1.00121.57 N ANISOU 4110 NH1 ARG B 65 15874 14864 15455 1592 2441 -332 N ATOM 4111 NH2 ARG B 65 69.171 -10.406 38.446 1.00117.97 N ANISOU 4111 NH2 ARG B 65 15200 14459 15163 1720 2348 -271 N ATOM 4112 N LEU B 66 65.826 -6.953 40.893 1.00 79.97 N ANISOU 4112 N LEU B 66 10823 9238 10323 1324 2026 383 N ATOM 4113 CA LEU B 66 65.627 -8.340 41.311 1.00 75.45 C ANISOU 4113 CA LEU B 66 10222 8558 9886 1518 1951 322 C ATOM 4114 C LEU B 66 64.870 -9.207 40.313 1.00 73.80 C ANISOU 4114 C LEU B 66 10137 8275 9630 1550 1962 249 C ATOM 4115 O LEU B 66 65.031 -10.427 40.345 1.00 73.80 O ANISOU 4115 O LEU B 66 10117 8214 9709 1696 1961 149 O ATOM 4116 CB LEU B 66 64.905 -8.376 42.652 1.00 71.66 C ANISOU 4116 CB LEU B 66 9787 7921 9522 1581 1806 450 C ATOM 4117 CG LEU B 66 65.669 -7.886 43.879 1.00 72.73 C ANISOU 4117 CG LEU B 66 9779 8109 9746 1606 1774 502 C ATOM 4118 CD1 LEU B 66 65.223 -8.698 45.094 1.00 72.63 C ANISOU 4118 CD1 LEU B 66 9783 7929 9886 1774 1646 550 C ATOM 4119 CD2 LEU B 66 67.144 -8.001 43.675 1.00 67.98 C ANISOU 4119 CD2 LEU B 66 8972 7716 9140 1642 1881 363 C ATOM 4120 N TYR B 67 64.031 -8.636 39.449 1.00 73.58 N ANISOU 4120 N TYR B 67 10246 8250 9461 1429 1976 293 N ATOM 4121 CA TYR B 67 63.386 -9.492 38.467 1.00 76.94 C ANISOU 4121 CA TYR B 67 10762 8641 9832 1453 1995 199 C ATOM 4122 C TYR B 67 64.361 -9.810 37.328 1.00 87.92 C ANISOU 4122 C TYR B 67 12077 10164 11164 1450 2136 50 C ATOM 4123 O TYR B 67 65.374 -9.132 37.128 1.00 90.21 O ANISOU 4123 O TYR B 67 12269 10594 11414 1388 2224 30 O ATOM 4124 CB TYR B 67 62.122 -8.843 37.909 1.00 71.04 C ANISOU 4124 CB TYR B 67 10172 7886 8935 1355 1955 279 C ATOM 4125 CG TYR B 67 62.395 -7.550 37.175 1.00 73.51 C ANISOU 4125 CG TYR B 67 10532 8320 9080 1232 2038 332 C ATOM 4126 CD1 TYR B 67 62.638 -7.544 35.796 1.00 77.62 C ANISOU 4126 CD1 TYR B 67 11083 8945 9464 1184 2153 236 C ATOM 4127 CD2 TYR B 67 62.426 -6.335 37.846 1.00 73.44 C ANISOU 4127 CD2 TYR B 67 10559 8310 9036 1162 2016 476 C ATOM 4128 CE1 TYR B 67 62.907 -6.359 35.108 1.00 78.00 C ANISOU 4128 CE1 TYR B 67 11210 9085 9340 1070 2248 282 C ATOM 4129 CE2 TYR B 67 62.688 -5.141 37.164 1.00 73.98 C ANISOU 4129 CE2 TYR B 67 10720 8463 8927 1042 2117 522 C ATOM 4130 CZ TYR B 67 62.928 -5.161 35.798 1.00 74.56 C ANISOU 4130 CZ TYR B 67 10837 8631 8862 998 2235 425 C ATOM 4131 OH TYR B 67 63.192 -3.982 35.136 1.00 72.45 O ANISOU 4131 OH TYR B 67 10695 8426 8405 878 2350 471 O ATOM 4132 N ASP B 68 64.038 -10.857 36.569 1.00 94.17 N ANISOU 4132 N ASP B 68 12921 10919 11942 1505 2164 -64 N ATOM 4133 CA ASP B 68 64.830 -11.252 35.405 1.00 96.70 C ANISOU 4133 CA ASP B 68 13187 11355 12200 1509 2292 -209 C ATOM 4134 C ASP B 68 64.362 -10.478 34.174 1.00 97.46 C ANISOU 4134 C ASP B 68 13377 11542 12112 1366 2352 -199 C ATOM 4135 O ASP B 68 63.157 -10.373 33.926 1.00 98.98 O ANISOU 4135 O ASP B 68 13700 11682 12227 1326 2291 -149 O ATOM 4136 CB ASP B 68 64.711 -12.761 35.188 1.00 97.61 C ANISOU 4136 CB ASP B 68 13337 11371 12378 1638 2304 -338 C ATOM 4137 CG ASP B 68 65.261 -13.208 33.862 1.00100.63 C ANISOU 4137 CG ASP B 68 13698 11859 12679 1635 2429 -485 C ATOM 4138 OD1 ASP B 68 64.536 -13.119 32.850 1.00100.58 O ANISOU 4138 OD1 ASP B 68 13789 11874 12553 1539 2456 -509 O ATOM 4139 OD2 ASP B 68 66.430 -13.641 33.830 1.00102.66 O ANISOU 4139 OD2 ASP B 68 13832 12194 12980 1738 2499 -581 O ATOM 4140 N GLU B 69 65.315 -9.932 33.407 1.00 95.04 N ANISOU 4140 N GLU B 69 13005 11385 11721 1295 2475 -254 N ATOM 4141 CA GLU B 69 64.943 -9.076 32.281 1.00 93.72 C ANISOU 4141 CA GLU B 69 12954 11295 11361 1167 2543 -231 C ATOM 4142 C GLU B 69 64.030 -9.790 31.290 1.00 89.90 C ANISOU 4142 C GLU B 69 12571 10789 10798 1190 2537 -303 C ATOM 4143 O GLU B 69 63.167 -9.154 30.675 1.00 87.30 O ANISOU 4143 O GLU B 69 12374 10487 10308 1128 2527 -246 O ATOM 4144 CB GLU B 69 66.190 -8.557 31.565 1.00101.41 C ANISOU 4144 CB GLU B 69 13846 12426 12258 1079 2698 -310 C ATOM 4145 CG GLU B 69 67.072 -7.670 32.431 1.00109.42 C ANISOU 4145 CG GLU B 69 14764 13503 13307 1005 2727 -254 C ATOM 4146 CD GLU B 69 67.163 -6.228 31.918 1.00114.48 C ANISOU 4146 CD GLU B 69 15531 14204 13760 818 2829 -181 C ATOM 4147 OE1 GLU B 69 66.227 -5.781 31.219 1.00115.47 O ANISOU 4147 OE1 GLU B 69 15853 14282 13737 785 2825 -113 O ATOM 4148 OE2 GLU B 69 68.160 -5.532 32.230 1.00115.52 O ANISOU 4148 OE2 GLU B 69 15578 14438 13878 706 2921 -198 O ATOM 4149 N LYS B 70 64.183 -11.105 31.141 1.00 87.76 N ANISOU 4149 N LYS B 70 12250 10475 10620 1286 2547 -432 N ATOM 4150 CA LYS B 70 63.446 -11.860 30.119 1.00 88.89 C ANISOU 4150 CA LYS B 70 12478 10615 10682 1286 2568 -532 C ATOM 4151 C LYS B 70 62.108 -12.338 30.672 1.00 88.27 C ANISOU 4151 C LYS B 70 12492 10420 10626 1302 2449 -497 C ATOM 4152 O LYS B 70 61.051 -11.860 30.252 1.00 74.66 O ANISOU 4152 O LYS B 70 10861 8743 8764 1240 2405 -454 O ATOM 4153 CB LYS B 70 64.295 -13.029 29.615 1.00 87.46 C ANISOU 4153 CB LYS B 70 12223 10441 10566 1369 2659 -699 C ATOM 4154 CG LYS B 70 65.458 -12.649 28.669 1.00 90.88 C ANISOU 4154 CG LYS B 70 12569 11036 10927 1330 2795 -777 C ATOM 4155 CD LYS B 70 66.603 -11.940 29.403 1.00 93.30 C ANISOU 4155 CD LYS B 70 12737 11420 11292 1324 2821 -733 C ATOM 4156 CE LYS B 70 67.976 -12.447 28.968 1.00 96.05 C ANISOU 4156 CE LYS B 70 12932 11897 11666 1385 2935 -882 C ATOM 4157 NZ LYS B 70 69.041 -12.010 29.928 1.00 97.30 N ANISOU 4157 NZ LYS B 70 12922 12146 11900 1410 2940 -867 N ATOM 4158 N GLN B 71 62.150 -13.303 31.598 1.00 89.70 N ANISOU 4158 N GLN B 71 12655 10461 10966 1391 2403 -526 N ATOM 4159 CA GLN B 71 60.992 -13.743 32.385 1.00 94.31 C ANISOU 4159 CA GLN B 71 13323 10917 11594 1392 2295 -489 C ATOM 4160 C GLN B 71 60.906 -12.843 33.602 1.00 95.58 C ANISOU 4160 C GLN B 71 13458 11038 11819 1395 2193 -321 C ATOM 4161 O GLN B 71 61.616 -13.058 34.585 1.00 98.13 O ANISOU 4161 O GLN B 71 13716 11281 12288 1480 2174 -291 O ATOM 4162 CB GLN B 71 61.148 -15.186 32.851 1.00 99.29 C ANISOU 4162 CB GLN B 71 13986 11387 12354 1487 2314 -595 C ATOM 4163 CG GLN B 71 61.370 -16.215 31.780 1.00105.11 C ANISOU 4163 CG GLN B 71 14762 12130 13046 1501 2427 -768 C ATOM 4164 CD GLN B 71 60.079 -16.768 31.236 1.00107.30 C ANISOU 4164 CD GLN B 71 15157 12391 13223 1396 2422 -853 C ATOM 4165 OE1 GLN B 71 59.465 -16.185 30.344 1.00111.39 O ANISOU 4165 OE1 GLN B 71 15676 13059 13587 1298 2420 -859 O ATOM 4166 NE2 GLN B 71 59.650 -17.900 31.781 1.00107.21 N ANISOU 4166 NE2 GLN B 71 15251 12203 13279 1416 2425 -926 N ATOM 4167 N GLN B 72 60.049 -11.827 33.560 1.00 91.34 N ANISOU 4167 N GLN B 72 12977 10564 11162 1318 2127 -212 N ATOM 4168 CA GLN B 72 60.065 -10.857 34.643 1.00 83.71 C ANISOU 4168 CA GLN B 72 11996 9567 10244 1316 2045 -47 C ATOM 4169 C GLN B 72 58.887 -11.003 35.595 1.00 79.92 C ANISOU 4169 C GLN B 72 11575 8990 9802 1320 1912 24 C ATOM 4170 O GLN B 72 58.589 -10.070 36.340 1.00 84.44 O ANISOU 4170 O GLN B 72 12162 9554 10366 1306 1832 170 O ATOM 4171 CB GLN B 72 60.164 -9.429 34.106 1.00 80.80 C ANISOU 4171 CB GLN B 72 11667 9322 9713 1244 2079 52 C ATOM 4172 CG GLN B 72 59.474 -9.141 32.817 1.00 80.79 C ANISOU 4172 CG GLN B 72 11759 9438 9498 1202 2116 12 C ATOM 4173 CD GLN B 72 59.930 -7.806 32.266 1.00 85.30 C ANISOU 4173 CD GLN B 72 12394 10101 9914 1146 2192 96 C ATOM 4174 OE1 GLN B 72 60.782 -7.142 32.854 1.00 82.37 O ANISOU 4174 OE1 GLN B 72 11988 9708 9602 1114 2226 170 O ATOM 4175 NE2 GLN B 72 59.371 -7.409 31.133 1.00 93.11 N ANISOU 4175 NE2 GLN B 72 13490 11198 10690 1130 2230 78 N ATOM 4176 N HIS B 73 58.221 -12.149 35.609 1.00 74.39 N ANISOU 4176 N HIS B 73 10917 8214 9136 1326 1896 -82 N ATOM 4177 CA HIS B 73 57.454 -12.532 36.785 1.00 74.23 C ANISOU 4177 CA HIS B 73 10934 8061 9209 1336 1791 -37 C ATOM 4178 C HIS B 73 58.321 -13.280 37.778 1.00 74.90 C ANISOU 4178 C HIS B 73 10986 7979 9494 1439 1801 -44 C ATOM 4179 O HIS B 73 57.815 -13.791 38.779 1.00 76.41 O ANISOU 4179 O HIS B 73 11227 8026 9778 1460 1734 -23 O ATOM 4180 CB HIS B 73 56.251 -13.391 36.405 1.00 75.28 C ANISOU 4180 CB HIS B 73 11146 8193 9263 1266 1779 -158 C ATOM 4181 CG HIS B 73 56.615 -14.628 35.645 1.00 80.71 C ANISOU 4181 CG HIS B 73 11866 8836 9965 1270 1897 -340 C ATOM 4182 ND1 HIS B 73 55.954 -15.824 35.814 1.00 79.97 N ANISOU 4182 ND1 HIS B 73 11865 8628 9893 1225 1917 -465 N ATOM 4183 CD2 HIS B 73 57.563 -14.851 34.703 1.00 81.76 C ANISOU 4183 CD2 HIS B 73 11964 9020 10082 1305 2009 -421 C ATOM 4184 CE1 HIS B 73 56.480 -16.731 35.013 1.00 82.22 C ANISOU 4184 CE1 HIS B 73 12184 8884 10174 1240 2038 -610 C ATOM 4185 NE2 HIS B 73 57.460 -16.167 34.330 1.00 83.06 N ANISOU 4185 NE2 HIS B 73 12204 9095 10261 1298 2089 -585 N ATOM 4186 N ILE B 74 59.621 -13.328 37.528 1.00 70.97 N ANISOU 4186 N ILE B 74 12424 7098 7443 3044 1472 -1725 N ATOM 4187 CA ILE B 74 60.548 -14.170 38.264 1.00 72.34 C ANISOU 4187 CA ILE B 74 12425 7348 7712 3280 1448 -1786 C ATOM 4188 C ILE B 74 61.480 -13.256 39.042 1.00 76.69 C ANISOU 4188 C ILE B 74 12890 8016 8232 3286 1432 -1783 C ATOM 4189 O ILE B 74 62.137 -12.384 38.456 1.00 82.49 O ANISOU 4189 O ILE B 74 13487 8980 8874 3068 1491 -1768 O ATOM 4190 CB ILE B 74 61.334 -15.083 37.312 1.00 72.77 C ANISOU 4190 CB ILE B 74 12309 7580 7759 3441 1571 -1957 C ATOM 4191 CG1 ILE B 74 60.373 -15.824 36.364 1.00 67.99 C ANISOU 4191 CG1 ILE B 74 11763 6883 7188 3344 1567 -1934 C ATOM 4192 CG2 ILE B 74 62.259 -16.006 38.095 1.00 77.38 C ANISOU 4192 CG2 ILE B 74 12716 8215 8470 3715 1477 -2042 C ATOM 4193 CD1 ILE B 74 59.244 -16.577 37.051 1.00 64.48 C ANISOU 4193 CD1 ILE B 74 11431 6208 6860 3291 1378 -1776 C ATOM 4194 N VAL B 75 61.539 -13.449 40.357 1.00 75.76 N ANISOU 4194 N VAL B 75 12762 7809 8212 3402 1294 -1730 N ATOM 4195 CA VAL B 75 62.360 -12.627 41.233 1.00 75.57 C ANISOU 4195 CA VAL B 75 12564 7932 8218 3315 1212 -1664 C ATOM 4196 C VAL B 75 63.418 -13.497 41.890 1.00 82.81 C ANISOU 4196 C VAL B 75 13272 8960 9233 3562 1182 -1729 C ATOM 4197 O VAL B 75 63.096 -14.535 42.490 1.00 86.14 O ANISOU 4197 O VAL B 75 13796 9196 9738 3775 1088 -1739 O ATOM 4198 CB VAL B 75 61.511 -11.914 42.290 1.00 71.07 C ANISOU 4198 CB VAL B 75 12142 7196 7665 3222 1050 -1562 C ATOM 4199 CG1 VAL B 75 62.376 -10.965 43.066 1.00 75.30 C ANISOU 4199 CG1 VAL B 75 12509 7878 8224 3114 958 -1501 C ATOM 4200 CG2 VAL B 75 60.378 -11.173 41.620 1.00 67.33 C ANISOU 4200 CG2 VAL B 75 11888 6588 7105 3048 1035 -1549 C ATOM 4201 N TYR B 76 64.679 -13.054 41.775 1.00 87.64 N ANISOU 4201 N TYR B 76 13598 9881 9818 3511 1234 -1770 N ATOM 4202 CA TYR B 76 65.884 -13.753 42.231 1.00 92.41 C ANISOU 4202 CA TYR B 76 13939 10675 10499 3754 1208 -1880 C ATOM 4203 C TYR B 76 66.420 -13.032 43.457 1.00 97.83 C ANISOU 4203 C TYR B 76 14515 11422 11233 3669 1093 -1764 C ATOM 4204 O TYR B 76 67.108 -12.018 43.321 1.00 99.46 O ANISOU 4204 O TYR B 76 14551 11883 11357 3437 1132 -1723 O ATOM 4205 CB TYR B 76 66.964 -13.752 41.150 1.00 96.54 C ANISOU 4205 CB TYR B 76 14155 11615 10911 3742 1368 -2050 C ATOM 4206 CG TYR B 76 66.621 -14.457 39.860 1.00100.66 C ANISOU 4206 CG TYR B 76 14720 12160 11366 3836 1495 -2209 C ATOM 4207 CD1 TYR B 76 66.022 -15.710 39.865 1.00 99.93 C ANISOU 4207 CD1 TYR B 76 14818 11770 11383 4148 1422 -2299 C ATOM 4208 CD2 TYR B 76 66.906 -13.867 38.629 1.00105.91 C ANISOU 4208 CD2 TYR B 76 15246 13156 11840 3583 1667 -2259 C ATOM 4209 CE1 TYR B 76 65.712 -16.356 38.687 1.00101.54 C ANISOU 4209 CE1 TYR B 76 15066 11986 11528 4245 1524 -2457 C ATOM 4210 CE2 TYR B 76 66.603 -14.506 37.444 1.00107.93 C ANISOU 4210 CE2 TYR B 76 15523 13464 12021 3666 1789 -2417 C ATOM 4211 CZ TYR B 76 66.005 -15.751 37.482 1.00105.52 C ANISOU 4211 CZ TYR B 76 15403 12842 11849 4018 1721 -2526 C ATOM 4212 OH TYR B 76 65.696 -16.395 36.309 1.00108.64 O ANISOU 4212 OH TYR B 76 15828 13276 12175 4113 1828 -2696 O ATOM 4213 N CYS B 77 66.149 -13.560 44.650 1.00 98.77 N ANISOU 4213 N CYS B 77 14731 11330 11468 3828 935 -1704 N ATOM 4214 CA CYS B 77 66.501 -12.857 45.880 1.00 98.08 C ANISOU 4214 CA CYS B 77 14564 11282 11421 3738 817 -1589 C ATOM 4215 C CYS B 77 67.519 -13.597 46.729 1.00 97.59 C ANISOU 4215 C CYS B 77 14311 11301 11466 3982 715 -1639 C ATOM 4216 O CYS B 77 67.752 -13.188 47.870 1.00 95.80 O ANISOU 4216 O CYS B 77 14037 11079 11284 3935 601 -1538 O ATOM 4217 CB CYS B 77 65.243 -12.592 46.704 1.00 91.10 C ANISOU 4217 CB CYS B 77 13936 10139 10540 3645 697 -1466 C ATOM 4218 SG CYS B 77 64.344 -14.096 47.021 1.00 88.29 S ANISOU 4218 SG CYS B 77 13814 9505 10228 3849 601 -1462 S ATOM 4219 N SER B 78 68.137 -14.654 46.191 1.00102.76 N ANISOU 4219 N SER B 78 14854 12024 12164 4257 731 -1812 N ATOM 4220 CA SER B 78 69.020 -15.552 46.939 1.00109.97 C ANISOU 4220 CA SER B 78 15632 12952 13199 4561 571 -1898 C ATOM 4221 C SER B 78 70.053 -14.849 47.824 1.00114.90 C ANISOU 4221 C SER B 78 15993 13822 13842 4498 533 -1852 C ATOM 4222 O SER B 78 70.286 -15.241 48.979 1.00116.70 O ANISOU 4222 O SER B 78 16236 13932 14173 4621 345 -1787 O ATOM 4223 CB SER B 78 69.736 -16.450 45.936 1.00115.90 C ANISOU 4223 CB SER B 78 16210 13868 13958 4858 614 -2174 C ATOM 4224 OG SER B 78 70.658 -15.688 45.175 1.00120.11 O ANISOU 4224 OG SER B 78 16398 14875 14363 4730 811 -2293 O ATOM 4225 N ASN B 79 70.693 -13.823 47.277 1.00115.92 N ANISOU 4225 N ASN B 79 15887 14303 13856 4278 694 -1874 N ATOM 4226 CA ASN B 79 71.782 -13.108 47.920 1.00117.58 C ANISOU 4226 CA ASN B 79 15816 14810 14050 4184 677 -1845 C ATOM 4227 C ASN B 79 71.332 -11.801 48.561 1.00110.51 C ANISOU 4227 C ASN B 79 15038 13838 13114 3836 645 -1621 C ATOM 4228 O ASN B 79 72.157 -11.100 49.154 1.00109.62 O ANISOU 4228 O ASN B 79 14728 13938 12984 3716 612 -1568 O ATOM 4229 CB ASN B 79 72.880 -12.847 46.879 1.00125.52 C ANISOU 4229 CB ASN B 79 16458 16322 14910 4127 847 -2024 C ATOM 4230 CG ASN B 79 72.309 -12.378 45.540 1.00125.55 C ANISOU 4230 CG ASN B 79 16552 16398 14754 3871 1021 -2024 C ATOM 4231 OD1 ASN B 79 71.100 -12.477 45.302 1.00124.71 O ANISOU 4231 OD1 ASN B 79 16777 15932 14677 3833 1014 -1938 O ATOM 4232 ND2 ASN B 79 73.180 -11.904 44.648 1.00127.60 N ANISOU 4232 ND2 ASN B 79 16504 17154 14822 3680 1171 -2125 N ATOM 4233 N ASP B 80 70.047 -11.470 48.459 1.00104.86 N ANISOU 4233 N ASP B 80 14632 12832 12380 3692 632 -1513 N ATOM 4234 CA ASP B 80 69.486 -10.232 48.977 1.00100.79 C ANISOU 4234 CA ASP B 80 14250 12220 11827 3412 558 -1360 C ATOM 4235 C ASP B 80 68.873 -10.398 50.356 1.00 95.38 C ANISOU 4235 C ASP B 80 13696 11315 11227 3491 390 -1275 C ATOM 4236 O ASP B 80 68.630 -11.503 50.842 1.00 96.86 O ANISOU 4236 O ASP B 80 13951 11363 11488 3708 324 -1288 O ATOM 4237 CB ASP B 80 68.411 -9.670 48.043 1.00100.17 C ANISOU 4237 CB ASP B 80 14413 11990 11658 3217 609 -1335 C ATOM 4238 CG ASP B 80 68.327 -8.153 48.111 1.00 97.56 C ANISOU 4238 CG ASP B 80 14142 11671 11254 2894 518 -1232 C ATOM 4239 OD1 ASP B 80 68.673 -7.469 47.129 1.00 98.77 O ANISOU 4239 OD1 ASP B 80 14267 11972 11291 2647 574 -1212 O ATOM 4240 OD2 ASP B 80 67.918 -7.645 49.178 1.00 95.36 O ANISOU 4240 OD2 ASP B 80 13948 11259 11025 2877 357 -1175 O ATOM 4241 N LEU B 81 68.598 -9.246 50.969 1.00 89.54 N ANISOU 4241 N LEU B 81 13006 10556 10459 3286 294 -1190 N ATOM 4242 CA LEU B 81 67.881 -9.201 52.234 1.00 85.55 C ANISOU 4242 CA LEU B 81 12606 9912 9986 3312 139 -1135 C ATOM 4243 C LEU B 81 66.458 -9.738 52.088 1.00 84.02 C ANISOU 4243 C LEU B 81 12660 9509 9754 3353 130 -1154 C ATOM 4244 O LEU B 81 65.942 -10.387 53.007 1.00 80.52 O ANISOU 4244 O LEU B 81 12278 9000 9315 3427 34 -1120 O ATOM 4245 CB LEU B 81 67.895 -7.767 52.758 1.00 85.73 C ANISOU 4245 CB LEU B 81 12620 9977 9978 3105 20 -1095 C ATOM 4246 CG LEU B 81 66.774 -7.236 53.640 1.00 86.88 C ANISOU 4246 CG LEU B 81 12910 10006 10094 3068 -141 -1112 C ATOM 4247 CD1 LEU B 81 66.886 -7.835 54.998 1.00 85.15 C ANISOU 4247 CD1 LEU B 81 12598 9845 9911 3176 -224 -1076 C ATOM 4248 CD2 LEU B 81 66.946 -5.744 53.753 1.00 90.81 C ANISOU 4248 CD2 LEU B 81 13418 10517 10569 2881 -283 -1113 C ATOM 4249 N LEU B 82 65.810 -9.477 50.943 1.00 81.29 N ANISOU 4249 N LEU B 82 12456 9083 9346 3275 218 -1199 N ATOM 4250 CA LEU B 82 64.506 -10.066 50.662 1.00 72.04 C ANISOU 4250 CA LEU B 82 11503 7743 8126 3315 229 -1228 C ATOM 4251 C LEU B 82 64.571 -11.585 50.649 1.00 74.07 C ANISOU 4251 C LEU B 82 11792 7924 8426 3505 257 -1221 C ATOM 4252 O LEU B 82 63.593 -12.249 51.009 1.00 72.80 O ANISOU 4252 O LEU B 82 11794 7647 8219 3520 194 -1196 O ATOM 4253 CB LEU B 82 63.972 -9.554 49.332 1.00 64.81 C ANISOU 4253 CB LEU B 82 10719 6759 7146 3207 322 -1277 C ATOM 4254 CG LEU B 82 62.667 -10.177 48.818 1.00 64.06 C ANISOU 4254 CG LEU B 82 10841 6506 6992 3246 361 -1318 C ATOM 4255 CD1 LEU B 82 61.564 -10.128 49.862 1.00 62.98 C ANISOU 4255 CD1 LEU B 82 10791 6345 6793 3233 225 -1330 C ATOM 4256 CD2 LEU B 82 62.207 -9.482 47.568 1.00 64.81 C ANISOU 4256 CD2 LEU B 82 11060 6538 7026 3119 424 -1360 C ATOM 4257 N GLY B 83 65.699 -12.154 50.219 1.00 78.76 N ANISOU 4257 N GLY B 83 12236 8596 9094 3646 321 -1259 N ATOM 4258 CA GLY B 83 65.856 -13.597 50.290 1.00 84.53 C ANISOU 4258 CA GLY B 83 13015 9214 9890 3871 264 -1279 C ATOM 4259 C GLY B 83 65.686 -14.123 51.699 1.00 89.59 C ANISOU 4259 C GLY B 83 13710 9775 10556 3896 64 -1171 C ATOM 4260 O GLY B 83 65.005 -15.128 51.919 1.00 92.08 O ANISOU 4260 O GLY B 83 14225 9910 10853 3937 -48 -1120 O ATOM 4261 N ASP B 84 66.280 -13.431 52.675 1.00 94.14 N ANISOU 4261 N ASP B 84 14120 10495 11154 3832 -1 -1120 N ATOM 4262 CA ASP B 84 66.160 -13.837 54.071 1.00 95.69 C ANISOU 4262 CA ASP B 84 14346 10663 11351 3815 -195 -1008 C ATOM 4263 C ASP B 84 64.765 -13.552 54.612 1.00 91.64 C ANISOU 4263 C ASP B 84 13990 10137 10692 3614 -246 -951 C ATOM 4264 O ASP B 84 64.213 -14.349 55.380 1.00 93.13 O ANISOU 4264 O ASP B 84 14302 10268 10814 3561 -396 -853 O ATOM 4265 CB ASP B 84 67.213 -13.113 54.910 1.00 99.69 C ANISOU 4265 CB ASP B 84 14610 11354 11913 3802 -237 -986 C ATOM 4266 CG ASP B 84 68.602 -13.161 54.285 1.00109.36 C ANISOU 4266 CG ASP B 84 15612 12703 13235 3965 -156 -1080 C ATOM 4267 OD1 ASP B 84 68.816 -13.944 53.327 1.00113.74 O ANISOU 4267 OD1 ASP B 84 16188 13203 13827 4137 -99 -1182 O ATOM 4268 OD2 ASP B 84 69.476 -12.386 54.736 1.00112.31 O ANISOU 4268 OD2 ASP B 84 15772 13270 13632 3913 -151 -1073 O ATOM 4269 N LEU B 85 64.189 -12.417 54.224 1.00 88.62 N ANISOU 4269 N LEU B 85 13601 9830 10241 3490 -151 -1021 N ATOM 4270 CA LEU B 85 62.822 -12.077 54.600 1.00 81.86 C ANISOU 4270 CA LEU B 85 12855 9016 9232 3341 -198 -1042 C ATOM 4271 C LEU B 85 61.839 -13.180 54.222 1.00 75.31 C ANISOU 4271 C LEU B 85 12239 8064 8312 3323 -202 -1009 C ATOM 4272 O LEU B 85 61.146 -13.744 55.075 1.00 70.14 O ANISOU 4272 O LEU B 85 11652 7469 7529 3209 -325 -934 O ATOM 4273 CB LEU B 85 62.437 -10.775 53.910 1.00 83.07 C ANISOU 4273 CB LEU B 85 13008 9197 9359 3276 -127 -1161 C ATOM 4274 CG LEU B 85 61.455 -9.897 54.653 1.00 83.78 C ANISOU 4274 CG LEU B 85 13088 9421 9323 3173 -240 -1256 C ATOM 4275 CD1 LEU B 85 62.122 -9.518 55.947 1.00 88.87 C ANISOU 4275 CD1 LEU B 85 13555 10221 9991 3154 -361 -1221 C ATOM 4276 CD2 LEU B 85 61.148 -8.671 53.822 1.00 79.44 C ANISOU 4276 CD2 LEU B 85 12592 8815 8778 3144 -236 -1380 C ATOM 4277 N PHE B 86 61.758 -13.480 52.924 1.00 77.53 N ANISOU 4277 N PHE B 86 12626 8197 8634 3403 -73 -1059 N ATOM 4278 CA PHE B 86 60.812 -14.462 52.403 1.00 79.37 C ANISOU 4278 CA PHE B 86 13079 8292 8784 3383 -72 -1037 C ATOM 4279 C PHE B 86 61.239 -15.892 52.682 1.00 85.63 C ANISOU 4279 C PHE B 86 13980 8921 9633 3477 -213 -928 C ATOM 4280 O PHE B 86 60.393 -16.793 52.716 1.00 84.89 O ANISOU 4280 O PHE B 86 14096 8723 9433 3389 -307 -853 O ATOM 4281 CB PHE B 86 60.659 -14.275 50.899 1.00 73.68 C ANISOU 4281 CB PHE B 86 12429 7470 8096 3446 104 -1137 C ATOM 4282 CG PHE B 86 59.650 -13.247 50.527 1.00 68.03 C ANISOU 4282 CG PHE B 86 11752 6824 7272 3321 166 -1226 C ATOM 4283 CD1 PHE B 86 59.002 -12.521 51.502 1.00 62.63 C ANISOU 4283 CD1 PHE B 86 11007 6309 6479 3207 63 -1260 C ATOM 4284 CD2 PHE B 86 59.341 -13.001 49.197 1.00 69.46 C ANISOU 4284 CD2 PHE B 86 12024 6914 7455 3331 302 -1302 C ATOM 4285 CE1 PHE B 86 58.060 -11.584 51.162 1.00 61.43 C ANISOU 4285 CE1 PHE B 86 10890 6214 6236 3145 68 -1392 C ATOM 4286 CE2 PHE B 86 58.397 -12.052 48.854 1.00 66.36 C ANISOU 4286 CE2 PHE B 86 11691 6553 6972 3235 308 -1395 C ATOM 4287 CZ PHE B 86 57.756 -11.349 49.835 1.00 62.47 C ANISOU 4287 CZ PHE B 86 11142 6208 6385 3162 178 -1453 C ATOM 4288 N GLY B 87 62.538 -16.117 52.855 1.00 92.73 N ANISOU 4288 N GLY B 87 14126 9424 11683 3489 1080 -2160 N ATOM 4289 CA GLY B 87 63.049 -17.446 53.084 1.00 94.63 C ANISOU 4289 CA GLY B 87 14467 9545 11944 3584 1111 -2068 C ATOM 4290 C GLY B 87 63.283 -18.248 51.832 1.00 93.19 C ANISOU 4290 C GLY B 87 14148 9262 11998 3437 1172 -2077 C ATOM 4291 O GLY B 87 63.298 -19.479 51.894 1.00 99.21 O ANISOU 4291 O GLY B 87 15007 9892 12797 3497 1217 -2001 O ATOM 4292 N VAL B 88 63.464 -17.603 50.689 1.00 88.74 N ANISOU 4292 N VAL B 88 13379 8748 11590 3273 1165 -2168 N ATOM 4293 CA VAL B 88 63.653 -18.367 49.460 1.00 83.66 C ANISOU 4293 CA VAL B 88 12612 8050 11125 3176 1219 -2201 C ATOM 4294 C VAL B 88 64.836 -17.794 48.702 1.00 81.79 C ANISOU 4294 C VAL B 88 12211 7858 11009 3162 1166 -2263 C ATOM 4295 O VAL B 88 65.462 -16.835 49.173 1.00 80.23 O ANISOU 4295 O VAL B 88 12009 7691 10782 3219 1070 -2267 O ATOM 4296 CB VAL B 88 62.398 -18.348 48.578 1.00 76.08 C ANISOU 4296 CB VAL B 88 11585 7122 10201 3022 1314 -2235 C ATOM 4297 CG1 VAL B 88 61.264 -19.111 49.244 1.00 74.82 C ANISOU 4297 CG1 VAL B 88 11607 6879 9943 3073 1396 -2142 C ATOM 4298 CG2 VAL B 88 62.010 -16.914 48.294 1.00 72.22 C ANISOU 4298 CG2 VAL B 88 10991 6760 9688 2922 1302 -2290 C ATOM 4299 N PRO B 89 65.207 -18.390 47.571 1.00 84.96 N ANISOU 4299 N PRO B 89 12494 8253 11533 3128 1216 -2309 N ATOM 4300 CA PRO B 89 66.086 -17.704 46.615 1.00 85.43 C ANISOU 4300 CA PRO B 89 12391 8396 11671 3130 1223 -2354 C ATOM 4301 C PRO B 89 65.356 -17.221 45.363 1.00 81.39 C ANISOU 4301 C PRO B 89 11763 7974 11188 2990 1307 -2412 C ATOM 4302 O PRO B 89 65.916 -16.454 44.571 1.00 77.32 O ANISOU 4302 O PRO B 89 11135 7539 10706 3009 1328 -2426 O ATOM 4303 CB PRO B 89 67.118 -18.782 46.266 1.00 88.15 C ANISOU 4303 CB PRO B 89 12699 8707 12088 3260 1230 -2368 C ATOM 4304 CG PRO B 89 66.872 -19.919 47.259 1.00 88.20 C ANISOU 4304 CG PRO B 89 12874 8571 12069 3322 1185 -2321 C ATOM 4305 CD PRO B 89 65.415 -19.840 47.531 1.00 85.36 C ANISOU 4305 CD PRO B 89 12605 8188 11640 3202 1224 -2300 C ATOM 4306 N SER B 90 64.107 -17.655 45.180 1.00 83.53 N ANISOU 4306 N SER B 90 12068 8229 11440 2879 1346 -2435 N ATOM 4307 CA SER B 90 63.315 -17.280 44.013 1.00 80.10 C ANISOU 4307 CA SER B 90 11535 7878 11023 2757 1397 -2499 C ATOM 4308 C SER B 90 61.839 -17.245 44.360 1.00 76.12 C ANISOU 4308 C SER B 90 11095 7356 10469 2659 1394 -2492 C ATOM 4309 O SER B 90 61.393 -17.856 45.332 1.00 78.25 O ANISOU 4309 O SER B 90 11500 7538 10692 2703 1389 -2434 O ATOM 4310 CB SER B 90 63.506 -18.256 42.856 1.00 84.34 C ANISOU 4310 CB SER B 90 12008 8422 11614 2778 1447 -2576 C ATOM 4311 OG SER B 90 64.697 -17.950 42.177 1.00 89.49 O ANISOU 4311 OG SER B 90 12562 9168 12272 2878 1493 -2585 O ATOM 4312 N PHE B 91 61.082 -16.532 43.533 1.00 69.83 N ANISOU 4312 N PHE B 91 10215 6644 9672 2554 1409 -2539 N ATOM 4313 CA PHE B 91 59.626 -16.672 43.566 1.00 68.45 C ANISOU 4313 CA PHE B 91 10083 6462 9461 2482 1413 -2544 C ATOM 4314 C PHE B 91 59.029 -16.055 42.313 1.00 59.58 C ANISOU 4314 C PHE B 91 8848 5436 8352 2391 1409 -2616 C ATOM 4315 O PHE B 91 59.689 -15.313 41.581 1.00 59.66 O ANISOU 4315 O PHE B 91 8766 5522 8379 2385 1419 -2641 O ATOM 4316 CB PHE B 91 58.998 -16.037 44.817 1.00 71.56 C ANISOU 4316 CB PHE B 91 10569 6861 9760 2495 1418 -2477 C ATOM 4317 CG PHE B 91 59.412 -14.607 45.049 1.00 68.20 C ANISOU 4317 CG PHE B 91 10093 6496 9324 2480 1378 -2486 C ATOM 4318 CD1 PHE B 91 60.619 -14.313 45.661 1.00 69.12 C ANISOU 4318 CD1 PHE B 91 10244 6575 9444 2567 1333 -2456 C ATOM 4319 CD2 PHE B 91 58.606 -13.567 44.644 1.00 62.89 C ANISOU 4319 CD2 PHE B 91 9358 5885 8653 2397 1370 -2524 C ATOM 4320 CE1 PHE B 91 61.006 -13.009 45.862 1.00 68.73 C ANISOU 4320 CE1 PHE B 91 10189 6524 9403 2577 1267 -2460 C ATOM 4321 CE2 PHE B 91 58.976 -12.269 44.836 1.00 63.08 C ANISOU 4321 CE2 PHE B 91 9373 5901 8693 2395 1322 -2528 C ATOM 4322 CZ PHE B 91 60.182 -11.982 45.456 1.00 66.71 C ANISOU 4322 CZ PHE B 91 9890 6299 9156 2491 1261 -2492 C ATOM 4323 N SER B 92 57.766 -16.372 42.070 1.00 58.03 N ANISOU 4323 N SER B 92 8685 5225 8140 2345 1403 -2632 N ATOM 4324 CA SER B 92 57.070 -15.868 40.898 1.00 57.30 C ANISOU 4324 CA SER B 92 8510 5218 8042 2278 1379 -2700 C ATOM 4325 C SER B 92 55.895 -14.990 41.277 1.00 56.52 C ANISOU 4325 C SER B 92 8426 5160 7890 2229 1372 -2672 C ATOM 4326 O SER B 92 54.991 -15.427 41.990 1.00 57.00 O ANISOU 4326 O SER B 92 8584 5157 7918 2243 1413 -2621 O ATOM 4327 CB SER B 92 56.555 -16.991 40.018 1.00 66.80 C ANISOU 4327 CB SER B 92 9741 6361 9280 2278 1359 -2759 C ATOM 4328 OG SER B 92 55.396 -16.520 39.349 1.00 70.76 O ANISOU 4328 OG SER B 92 10232 6916 9738 2220 1327 -2774 O ATOM 4329 N VAL B 93 55.866 -13.790 40.721 1.00 55.65 N ANISOU 4329 N VAL B 93 8234 5145 7766 2176 1340 -2680 N ATOM 4330 CA VAL B 93 54.809 -12.840 41.012 1.00 55.10 C ANISOU 4330 CA VAL B 93 8157 5112 7667 2136 1323 -2676 C ATOM 4331 C VAL B 93 53.496 -13.262 40.357 1.00 57.64 C ANISOU 4331 C VAL B 93 8508 5439 7953 2121 1316 -2694 C ATOM 4332 O VAL B 93 52.543 -12.472 40.252 1.00 54.72 O ANISOU 4332 O VAL B 93 8119 5116 7556 2094 1298 -2698 O ATOM 4333 CB VAL B 93 55.241 -11.447 40.556 1.00 64.57 C ANISOU 4333 CB VAL B 93 9287 6348 8898 2090 1288 -2673 C ATOM 4334 CG1 VAL B 93 54.387 -10.416 41.226 1.00 66.90 C ANISOU 4334 CG1 VAL B 93 9580 6636 9201 2056 1282 -2678 C ATOM 4335 CG2 VAL B 93 56.707 -11.230 40.884 1.00 65.13 C ANISOU 4335 CG2 VAL B 93 9364 6362 9021 2130 1313 -2646 C ATOM 4336 N LYS B 94 53.431 -14.517 39.910 1.00 58.23 N ANISOU 4336 N LYS B 94 8640 5436 8047 2145 1328 -2712 N ATOM 4337 CA LYS B 94 52.171 -15.095 39.464 1.00 61.97 C ANISOU 4337 CA LYS B 94 9189 5833 8523 2139 1340 -2726 C ATOM 4338 C LYS B 94 51.478 -15.916 40.544 1.00 65.22 C ANISOU 4338 C LYS B 94 9725 6095 8960 2154 1465 -2637 C ATOM 4339 O LYS B 94 50.234 -15.935 40.602 1.00 64.97 O ANISOU 4339 O LYS B 94 9742 6006 8937 2128 1552 -2602 O ATOM 4340 CB LYS B 94 52.378 -15.968 38.231 1.00 57.00 C ANISOU 4340 CB LYS B 94 8570 5164 7924 2141 1276 -2792 C ATOM 4341 CG LYS B 94 52.921 -15.288 36.997 1.00 56.44 C ANISOU 4341 CG LYS B 94 8393 5253 7798 2120 1225 -2832 C ATOM 4342 CD LYS B 94 53.005 -16.329 35.867 1.00 63.82 C ANISOU 4342 CD LYS B 94 9329 6152 8767 2140 1185 -2935 C ATOM 4343 CE LYS B 94 52.685 -15.765 34.500 1.00 65.05 C ANISOU 4343 CE LYS B 94 9429 6429 8858 2122 1164 -2993 C ATOM 4344 NZ LYS B 94 53.332 -16.541 33.416 1.00 59.10 N ANISOU 4344 NZ LYS B 94 8570 5676 8209 2066 1275 -3131 N ATOM 4345 N GLU B 95 52.251 -16.605 41.397 1.00 72.54 N ANISOU 4345 N GLU B 95 10714 6940 9906 2202 1509 -2586 N ATOM 4346 CA GLU B 95 51.686 -17.408 42.489 1.00 81.51 C ANISOU 4346 CA GLU B 95 12004 7910 11057 2243 1671 -2466 C ATOM 4347 C GLU B 95 51.293 -16.454 43.611 1.00 78.58 C ANISOU 4347 C GLU B 95 11624 7675 10559 2291 1778 -2403 C ATOM 4348 O GLU B 95 52.015 -16.250 44.594 1.00 77.52 O ANISOU 4348 O GLU B 95 11518 7591 10344 2368 1790 -2365 O ATOM 4349 CB GLU B 95 52.658 -18.490 42.959 1.00 92.05 C ANISOU 4349 CB GLU B 95 13436 9093 12446 2307 1664 -2428 C ATOM 4350 CG GLU B 95 54.147 -18.164 42.830 1.00100.15 C ANISOU 4350 CG GLU B 95 14355 10243 13454 2333 1543 -2497 C ATOM 4351 CD GLU B 95 55.063 -19.333 43.249 1.00106.01 C ANISOU 4351 CD GLU B 95 15193 10820 14266 2412 1531 -2468 C ATOM 4352 OE1 GLU B 95 56.290 -19.106 43.448 1.00105.55 O ANISOU 4352 OE1 GLU B 95 15070 10842 14194 2450 1485 -2490 O ATOM 4353 OE2 GLU B 95 54.551 -20.475 43.373 1.00108.28 O ANISOU 4353 OE2 GLU B 95 15630 10864 14648 2436 1568 -2415 O ATOM 4354 N HIS B 96 50.109 -15.861 43.445 1.00 66.57 N ANISOU 4354 N HIS B 96 12230 5633 7432 2238 -693 -1490 N ATOM 4355 CA HIS B 96 49.723 -14.736 44.282 1.00 63.50 C ANISOU 4355 CA HIS B 96 11779 5297 7049 2218 -712 -1434 C ATOM 4356 C HIS B 96 49.596 -15.165 45.738 1.00 69.79 C ANISOU 4356 C HIS B 96 12546 6052 7920 2208 -678 -1380 C ATOM 4357 O HIS B 96 50.242 -14.589 46.621 1.00 69.92 O ANISOU 4357 O HIS B 96 12518 6120 7927 2240 -651 -1312 O ATOM 4358 CB HIS B 96 48.419 -14.124 43.771 1.00 58.70 C ANISOU 4358 CB HIS B 96 11173 4693 6437 2162 -783 -1475 C ATOM 4359 CG HIS B 96 48.567 -13.340 42.496 1.00 57.16 C ANISOU 4359 CG HIS B 96 10998 4562 6158 2175 -821 -1509 C ATOM 4360 ND1 HIS B 96 47.537 -12.589 41.955 1.00 53.26 N ANISOU 4360 ND1 HIS B 96 10506 4091 5638 2146 -890 -1540 N ATOM 4361 CD2 HIS B 96 49.611 -13.223 41.637 1.00 53.51 C ANISOU 4361 CD2 HIS B 96 10562 4144 5627 2220 -802 -1520 C ATOM 4362 CE1 HIS B 96 47.949 -12.028 40.832 1.00 53.32 C ANISOU 4362 CE1 HIS B 96 10542 4151 5566 2165 -911 -1563 C ATOM 4363 NE2 HIS B 96 49.201 -12.401 40.612 1.00 57.20 N ANISOU 4363 NE2 HIS B 96 11048 4655 6030 2207 -857 -1553 N ATOM 4364 N ARG B 97 48.797 -16.208 46.011 1.00 73.99 N ANISOU 4364 N ARG B 97 13112 6483 8520 2162 -680 -1409 N ATOM 4365 CA ARG B 97 48.533 -16.547 47.409 1.00 73.14 C ANISOU 4365 CA ARG B 97 12980 6330 8480 2144 -652 -1356 C ATOM 4366 C ARG B 97 49.811 -16.965 48.118 1.00 68.88 C ANISOU 4366 C ARG B 97 12429 5802 7941 2211 -588 -1299 C ATOM 4367 O ARG B 97 49.975 -16.693 49.310 1.00 71.41 O ANISOU 4367 O ARG B 97 12703 6141 8288 2219 -564 -1233 O ATOM 4368 CB ARG B 97 47.445 -17.625 47.512 1.00 78.60 C ANISOU 4368 CB ARG B 97 13733 6898 9233 2074 -669 -1404 C ATOM 4369 CG ARG B 97 46.520 -17.495 48.751 1.00 83.06 C ANISOU 4369 CG ARG B 97 14272 7431 9857 2029 -676 -1369 C ATOM 4370 CD ARG B 97 45.040 -17.576 48.350 1.00 88.37 C ANISOU 4370 CD ARG B 97 14986 8048 10543 1955 -740 -1441 C ATOM 4371 NE ARG B 97 44.822 -18.597 47.319 1.00 94.82 N ANISOU 4371 NE ARG B 97 15897 8779 11353 1912 -759 -1521 N ATOM 4372 CZ ARG B 97 43.876 -18.548 46.378 1.00 94.42 C ANISOU 4372 CZ ARG B 97 15888 8711 11277 1860 -825 -1604 C ATOM 4373 NH1 ARG B 97 43.779 -19.532 45.479 1.00 92.57 N ANISOU 4373 NH1 ARG B 97 15746 8394 11031 1816 -837 -1674 N ATOM 4374 NH2 ARG B 97 43.022 -17.526 46.340 1.00 92.71 N ANISOU 4374 NH2 ARG B 97 15626 8560 11041 1856 -882 -1620 N ATOM 4375 N LYS B 98 50.762 -17.537 47.388 1.00 66.43 N ANISOU 4375 N LYS B 98 12159 5492 7588 2270 -563 -1323 N ATOM 4376 CA LYS B 98 52.035 -17.893 48.002 1.00 69.85 C ANISOU 4376 CA LYS B 98 12584 5949 8006 2355 -507 -1274 C ATOM 4377 C LYS B 98 52.831 -16.658 48.413 1.00 70.33 C ANISOU 4377 C LYS B 98 12582 6128 8014 2397 -500 -1218 C ATOM 4378 O LYS B 98 53.418 -16.606 49.510 1.00 73.19 O ANISOU 4378 O LYS B 98 12910 6512 8386 2433 -466 -1155 O ATOM 4379 CB LYS B 98 52.855 -18.757 47.050 1.00 74.50 C ANISOU 4379 CB LYS B 98 13240 6518 8548 2427 -484 -1320 C ATOM 4380 CG LYS B 98 54.150 -19.237 47.680 1.00 79.30 C ANISOU 4380 CG LYS B 98 13848 7150 9131 2535 -429 -1274 C ATOM 4381 CD LYS B 98 55.044 -19.923 46.666 1.00 85.59 C ANISOU 4381 CD LYS B 98 14708 7950 9861 2631 -407 -1321 C ATOM 4382 CE LYS B 98 56.502 -20.021 47.137 1.00 89.43 C ANISOU 4382 CE LYS B 98 15179 8509 10289 2767 -358 -1278 C ATOM 4383 NZ LYS B 98 57.483 -19.723 46.036 1.00 90.21 N ANISOU 4383 NZ LYS B 98 15294 8698 10285 2864 -348 -1316 N ATOM 4384 N ILE B 99 52.894 -15.660 47.534 1.00 71.16 N ANISOU 4384 N ILE B 99 12680 6304 8054 2394 -533 -1241 N ATOM 4385 CA ILE B 99 53.662 -14.466 47.867 1.00 68.69 C ANISOU 4385 CA ILE B 99 12334 6090 7677 2427 -530 -1192 C ATOM 4386 C ILE B 99 52.960 -13.651 48.955 1.00 62.26 C ANISOU 4386 C ILE B 99 11471 5287 6899 2371 -549 -1138 C ATOM 4387 O ILE B 99 53.613 -13.003 49.791 1.00 56.14 O ANISOU 4387 O ILE B 99 10671 4564 6095 2396 -532 -1079 O ATOM 4388 CB ILE B 99 53.931 -13.672 46.580 1.00 64.61 C ANISOU 4388 CB ILE B 99 11844 5634 7070 2437 -561 -1233 C ATOM 4389 CG1 ILE B 99 54.850 -14.514 45.702 1.00 65.06 C ANISOU 4389 CG1 ILE B 99 11945 5691 7083 2515 -529 -1278 C ATOM 4390 CG2 ILE B 99 54.556 -12.319 46.895 1.00 60.47 C ANISOU 4390 CG2 ILE B 99 11310 5197 6470 2451 -569 -1186 C ATOM 4391 CD1 ILE B 99 55.442 -13.750 44.631 1.00 66.53 C ANISOU 4391 CD1 ILE B 99 12160 5951 7168 2546 -544 -1308 C ATOM 4392 N TYR B 100 51.632 -13.715 48.997 1.00 57.89 N ANISOU 4392 N TYR B 100 10910 4683 6403 2301 -583 -1159 N ATOM 4393 CA TYR B 100 50.899 -13.112 50.096 1.00 56.90 C ANISOU 4393 CA TYR B 100 10742 4562 6315 2262 -595 -1111 C ATOM 4394 C TYR B 100 51.205 -13.786 51.425 1.00 58.88 C ANISOU 4394 C TYR B 100 10969 4778 6624 2274 -546 -1057 C ATOM 4395 O TYR B 100 51.285 -13.110 52.451 1.00 56.48 O ANISOU 4395 O TYR B 100 10629 4512 6320 2273 -539 -997 O ATOM 4396 CB TYR B 100 49.407 -13.147 49.793 1.00 56.98 C ANISOU 4396 CB TYR B 100 10759 4526 6366 2202 -642 -1156 C ATOM 4397 CG TYR B 100 48.932 -11.940 49.035 1.00 60.15 C ANISOU 4397 CG TYR B 100 11163 4987 6703 2193 -699 -1176 C ATOM 4398 CD1 TYR B 100 49.601 -10.724 49.149 1.00 64.01 C ANISOU 4398 CD1 TYR B 100 11647 5557 7118 2218 -705 -1131 C ATOM 4399 CD2 TYR B 100 47.830 -12.004 48.206 1.00 64.23 C ANISOU 4399 CD2 TYR B 100 11704 5478 7225 2162 -751 -1241 C ATOM 4400 CE1 TYR B 100 49.170 -9.586 48.464 1.00 68.86 C ANISOU 4400 CE1 TYR B 100 12282 6220 7664 2212 -761 -1144 C ATOM 4401 CE2 TYR B 100 47.396 -10.876 47.500 1.00 70.00 C ANISOU 4401 CE2 TYR B 100 12443 6265 7888 2166 -808 -1257 C ATOM 4402 CZ TYR B 100 48.068 -9.667 47.635 1.00 70.85 C ANISOU 4402 CZ TYR B 100 12549 6449 7923 2192 -811 -1205 C ATOM 4403 OH TYR B 100 47.641 -8.547 46.943 1.00 69.86 O ANISOU 4403 OH TYR B 100 12450 6371 7723 2198 -869 -1217 O ATOM 4404 N THR B 101 51.338 -15.117 51.438 1.00 64.49 N ANISOU 4404 N THR B 101 11709 5411 7381 2286 -515 -1076 N ATOM 4405 CA THR B 101 51.642 -15.815 52.688 1.00 63.10 C ANISOU 4405 CA THR B 101 11523 5198 7257 2303 -470 -1023 C ATOM 4406 C THR B 101 53.032 -15.470 53.191 1.00 62.11 C ANISOU 4406 C THR B 101 11374 5147 7078 2380 -435 -970 C ATOM 4407 O THR B 101 53.236 -15.264 54.397 1.00 64.72 O ANISOU 4407 O THR B 101 11671 5494 7427 2386 -414 -907 O ATOM 4408 CB THR B 101 51.516 -17.319 52.494 1.00 67.55 C ANISOU 4408 CB THR B 101 12147 5653 7865 2303 -449 -1058 C ATOM 4409 OG1 THR B 101 50.163 -17.646 52.156 1.00 70.08 O ANISOU 4409 OG1 THR B 101 12501 5895 8232 2223 -485 -1108 O ATOM 4410 CG2 THR B 101 51.914 -18.037 53.756 1.00 73.33 C ANISOU 4410 CG2 THR B 101 12878 6345 8638 2329 -404 -1000 C ATOM 4411 N MET B 102 54.001 -15.406 52.279 1.00 66.14 N ANISOU 4411 N MET B 102 11910 5705 7517 2444 -430 -997 N ATOM 4412 CA MET B 102 55.308 -14.879 52.660 1.00 66.36 C ANISOU 4412 CA MET B 102 11924 5816 7473 2523 -404 -953 C ATOM 4413 C MET B 102 55.212 -13.437 53.180 1.00 61.18 C ANISOU 4413 C MET B 102 11238 5227 6780 2486 -430 -911 C ATOM 4414 O MET B 102 55.885 -13.072 54.152 1.00 53.90 O ANISOU 4414 O MET B 102 10298 4346 5836 2519 -409 -853 O ATOM 4415 CB MET B 102 56.277 -14.963 51.481 1.00 68.06 C ANISOU 4415 CB MET B 102 12178 6076 7604 2602 -398 -998 C ATOM 4416 CG MET B 102 57.068 -16.249 51.410 1.00 68.22 C ANISOU 4416 CG MET B 102 12229 6068 7622 2697 -354 -1010 C ATOM 4417 SD MET B 102 57.871 -16.431 49.807 1.00 72.45 S ANISOU 4417 SD MET B 102 12816 6647 8064 2783 -350 -1082 S ATOM 4418 CE MET B 102 56.473 -16.442 48.682 1.00 69.86 C ANISOU 4418 CE MET B 102 12515 6250 7779 2668 -401 -1150 C ATOM 4419 N ILE B 103 54.393 -12.592 52.549 1.00 62.48 N ANISOU 4419 N ILE B 103 11407 5403 6930 2424 -477 -937 N ATOM 4420 CA ILE B 103 54.266 -11.214 53.031 1.00 60.77 C ANISOU 4420 CA ILE B 103 11182 5240 6668 2393 -504 -896 C ATOM 4421 C ILE B 103 53.656 -11.183 54.431 1.00 48.00 C ANISOU 4421 C ILE B 103 9522 3601 5117 2358 -494 -842 C ATOM 4422 O ILE B 103 54.143 -10.485 55.324 1.00 47.47 O ANISOU 4422 O ILE B 103 9448 3574 5014 2368 -487 -786 O ATOM 4423 CB ILE B 103 53.445 -10.356 52.047 1.00 60.04 C ANISOU 4423 CB ILE B 103 11111 5160 6540 2345 -560 -936 C ATOM 4424 CG1 ILE B 103 54.250 -9.979 50.791 1.00 48.50 C ANISOU 4424 CG1 ILE B 103 9703 3742 4984 2380 -572 -975 C ATOM 4425 CG2 ILE B 103 52.877 -9.146 52.762 1.00 47.44 C ANISOU 4425 CG2 ILE B 103 9508 3592 4923 2306 -591 -892 C ATOM 4426 CD1 ILE B 103 53.507 -9.019 49.865 1.00 48.28 C ANISOU 4426 CD1 ILE B 103 9706 3730 4909 2336 -631 -1005 C ATOM 4427 N TYR B 104 52.573 -11.930 54.635 1.00 48.29 N ANISOU 4427 N TYR B 104 9538 3570 5241 2316 -496 -859 N ATOM 4428 CA TYR B 104 51.873 -11.948 55.912 1.00 48.47 C ANISOU 4428 CA TYR B 104 9524 3567 5325 2284 -486 -814 C ATOM 4429 C TYR B 104 52.703 -12.554 57.036 1.00 50.69 C ANISOU 4429 C TYR B 104 9790 3842 5631 2321 -436 -758 C ATOM 4430 O TYR B 104 52.425 -12.280 58.209 1.00 51.31 O ANISOU 4430 O TYR B 104 9839 3922 5734 2303 -426 -707 O ATOM 4431 CB TYR B 104 50.555 -12.698 55.759 1.00 50.80 C ANISOU 4431 CB TYR B 104 9821 3782 5698 2236 -499 -855 C ATOM 4432 CG TYR B 104 49.388 -11.802 55.459 1.00 54.48 C ANISOU 4432 CG TYR B 104 10283 4266 6151 2201 -551 -878 C ATOM 4433 CD1 TYR B 104 49.586 -10.531 55.000 1.00 54.65 C ANISOU 4433 CD1 TYR B 104 10311 4361 6091 2211 -585 -873 C ATOM 4434 CD2 TYR B 104 48.081 -12.237 55.618 1.00 64.27 C ANISOU 4434 CD2 TYR B 104 11524 5444 7451 2166 -569 -906 C ATOM 4435 CE1 TYR B 104 48.525 -9.695 54.716 1.00 57.28 C ANISOU 4435 CE1 TYR B 104 10650 4714 6402 2196 -636 -893 C ATOM 4436 CE2 TYR B 104 46.998 -11.394 55.330 1.00 65.64 C ANISOU 4436 CE2 TYR B 104 11698 5642 7602 2156 -621 -932 C ATOM 4437 CZ TYR B 104 47.235 -10.118 54.878 1.00 59.60 C ANISOU 4437 CZ TYR B 104 10934 4956 6754 2176 -654 -923 C ATOM 4438 OH TYR B 104 46.192 -9.265 54.575 1.00 52.76 O ANISOU 4438 OH TYR B 104 10075 4118 5854 2183 -708 -947 O ATOM 4439 N ARG B 105 53.703 -13.376 56.726 1.00 52.58 N ANISOU 4439 N ARG B 105 10049 4073 5856 2381 -405 -768 N ATOM 4440 CA ARG B 105 54.548 -13.866 57.804 1.00 51.74 C ANISOU 4440 CA ARG B 105 9930 3971 5758 2432 -361 -712 C ATOM 4441 C ARG B 105 55.274 -12.735 58.505 1.00 54.92 C ANISOU 4441 C ARG B 105 10320 4454 6093 2454 -363 -658 C ATOM 4442 O ARG B 105 55.377 -12.749 59.735 1.00 64.05 O ANISOU 4442 O ARG B 105 11452 5612 7273 2455 -342 -601 O ATOM 4443 CB ARG B 105 55.539 -14.887 57.292 1.00 56.35 C ANISOU 4443 CB ARG B 105 10546 4542 6321 2517 -331 -734 C ATOM 4444 CG ARG B 105 54.897 -16.216 57.090 1.00 63.72 C ANISOU 4444 CG ARG B 105 11509 5372 7328 2497 -319 -767 C ATOM 4445 CD ARG B 105 55.814 -17.187 56.401 1.00 67.64 C ANISOU 4445 CD ARG B 105 12052 5855 7791 2588 -294 -798 C ATOM 4446 NE ARG B 105 55.073 -18.408 56.146 1.00 71.96 N ANISOU 4446 NE ARG B 105 12652 6287 8402 2554 -291 -834 N ATOM 4447 CZ ARG B 105 55.400 -19.291 55.217 1.00 77.09 C ANISOU 4447 CZ ARG B 105 13364 6896 9032 2602 -284 -885 C ATOM 4448 NH1 ARG B 105 56.466 -19.071 54.458 1.00 79.62 N ANISOU 4448 NH1 ARG B 105 13690 7293 9270 2695 -276 -904 N ATOM 4449 NH2 ARG B 105 54.665 -20.385 55.055 1.00 78.51 N ANISOU 4449 NH2 ARG B 105 13610 6955 9264 2561 -285 -917 N ATOM 4450 N ASN B 106 55.774 -11.741 57.756 1.00 52.35 N ANISOU 4450 N ASN B 106 10022 4190 5678 2468 -389 -675 N ATOM 4451 CA ASN B 106 56.494 -10.608 58.349 1.00 52.33 C ANISOU 4451 CA ASN B 106 10037 4252 5594 2484 -396 -628 C ATOM 4452 C ASN B 106 55.580 -9.439 58.693 1.00 51.06 C ANISOU 4452 C ASN B 106 9877 4099 5423 2406 -434 -610 C ATOM 4453 O ASN B 106 56.059 -8.314 58.881 1.00 48.56 O ANISOU 4453 O ASN B 106 9606 3826 5020 2406 -454 -585 O ATOM 4454 CB ASN B 106 57.615 -10.133 57.425 1.00 53.22 C ANISOU 4454 CB ASN B 106 10205 4419 5596 2547 -402 -653 C ATOM 4455 CG ASN B 106 58.449 -11.283 56.904 1.00 58.97 C ANISOU 4455 CG ASN B 106 10934 5150 6322 2641 -365 -682 C ATOM 4456 OD1 ASN B 106 57.956 -12.113 56.146 1.00 57.90 O ANISOU 4456 OD1 ASN B 106 10792 4969 6237 2632 -363 -730 O ATOM 4457 ND2 ASN B 106 59.720 -11.330 57.285 1.00 63.36 N ANISOU 4457 ND2 ASN B 106 11504 5760 6810 2743 -336 -655 N ATOM 4458 N LEU B 107 54.283 -9.689 58.802 1.00 52.37 N ANISOU 4458 N LEU B 107 10008 4221 5668 2350 -446 -624 N ATOM 4459 CA LEU B 107 53.313 -8.679 59.170 1.00 51.07 C ANISOU 4459 CA LEU B 107 9841 4068 5495 2298 -480 -610 C ATOM 4460 C LEU B 107 52.741 -8.951 60.541 1.00 51.48 C ANISOU 4460 C LEU B 107 9849 4096 5614 2280 -456 -564 C ATOM 4461 O LEU B 107 52.605 -10.104 60.954 1.00 58.19 O ANISOU 4461 O LEU B 107 10668 4898 6543 2285 -422 -560 O ATOM 4462 CB LEU B 107 52.142 -8.653 58.206 1.00 51.50 C ANISOU 4462 CB LEU B 107 9895 4098 5574 2265 -517 -666 C ATOM 4463 CG LEU B 107 52.440 -7.948 56.916 1.00 53.66 C ANISOU 4463 CG LEU B 107 10220 4403 5764 2270 -554 -705 C ATOM 4464 CD1 LEU B 107 51.124 -7.422 56.443 1.00 55.67 C ANISOU 4464 CD1 LEU B 107 10476 4652 6024 2239 -601 -736 C ATOM 4465 CD2 LEU B 107 53.436 -6.851 57.156 1.00 55.95 C ANISOU 4465 CD2 LEU B 107 10566 4743 5948 2285 -563 -667 C ATOM 4466 N VAL B 108 52.337 -7.882 61.207 1.00 46.77 N ANISOU 4466 N VAL B 108 9261 3530 4980 2258 -476 -531 N ATOM 4467 CA VAL B 108 51.370 -7.968 62.287 1.00 47.81 C ANISOU 4467 CA VAL B 108 9354 3641 5172 2238 -466 -503 C ATOM 4468 C VAL B 108 50.144 -7.193 61.828 1.00 46.52 C ANISOU 4468 C VAL B 108 9200 3485 4989 2220 -510 -533 C ATOM 4469 O VAL B 108 50.185 -5.962 61.720 1.00 44.46 O ANISOU 4469 O VAL B 108 8984 3268 4642 2221 -544 -524 O ATOM 4470 CB VAL B 108 51.922 -7.430 63.610 1.00 45.06 C ANISOU 4470 CB VAL B 108 9008 3322 4788 2244 -447 -436 C ATOM 4471 CG1 VAL B 108 50.928 -7.684 64.724 1.00 44.53 C ANISOU 4471 CG1 VAL B 108 8900 3230 4788 2229 -429 -409 C ATOM 4472 CG2 VAL B 108 53.219 -8.116 63.911 1.00 45.64 C ANISOU 4472 CG2 VAL B 108 9082 3398 4862 2279 -411 -410 C ATOM 4473 N VAL B 109 49.061 -7.908 61.524 1.00 45.25 N ANISOU 4473 N VAL B 109 9013 3278 4902 2212 -515 -572 N ATOM 4474 CA VAL B 109 47.824 -7.226 61.177 1.00 45.29 C ANISOU 4474 CA VAL B 109 9027 3293 4888 2215 -559 -602 C ATOM 4475 C VAL B 109 47.305 -6.507 62.416 1.00 53.66 C ANISOU 4475 C VAL B 109 10079 4378 5931 2228 -555 -554 C ATOM 4476 O VAL B 109 47.329 -7.048 63.531 1.00 54.05 O ANISOU 4476 O VAL B 109 10098 4405 6033 2224 -514 -514 O ATOM 4477 CB VAL B 109 46.787 -8.212 60.608 1.00 48.89 C ANISOU 4477 CB VAL B 109 9470 3685 5420 2208 -567 -659 C ATOM 4478 CG1 VAL B 109 45.380 -7.623 60.657 1.00 46.16 C ANISOU 4478 CG1 VAL B 109 9127 3348 5062 2233 -607 -682 C ATOM 4479 CG2 VAL B 109 47.152 -8.613 59.176 1.00 49.87 C ANISOU 4479 CG2 VAL B 109 9618 3796 5534 2199 -586 -717 C ATOM 4480 N VAL B 110 46.875 -5.256 62.239 1.00 56.38 N ANISOU 4480 N VAL B 110 10460 4769 6192 2249 -597 -556 N ATOM 4481 CA VAL B 110 46.373 -4.461 63.351 1.00 57.63 C ANISOU 4481 CA VAL B 110 10625 4956 6316 2273 -597 -515 C ATOM 4482 C VAL B 110 44.856 -4.523 63.461 1.00 64.22 C ANISOU 4482 C VAL B 110 11439 5780 7180 2316 -615 -544 C ATOM 4483 O VAL B 110 44.314 -4.113 64.493 1.00 70.23 O ANISOU 4483 O VAL B 110 12196 6560 7929 2348 -605 -512 O ATOM 4484 CB VAL B 110 46.877 -3.007 63.233 1.00 44.25 C ANISOU 4484 CB VAL B 110 9005 3312 4494 2279 -631 -495 C ATOM 4485 CG1 VAL B 110 46.799 -2.328 64.524 1.00 44.04 C ANISOU 4485 CG1 VAL B 110 8996 3309 4429 2293 -618 -445 C ATOM 4486 CG2 VAL B 110 48.318 -3.008 62.803 1.00 43.98 C ANISOU 4486 CG2 VAL B 110 9006 3281 4423 2245 -624 -484 C ATOM 4487 N ASN B 111 44.157 -5.058 62.452 1.00 67.68 N ANISOU 4487 N ASN B 111 11871 6191 7654 2325 -642 -605 N ATOM 4488 CA ASN B 111 42.685 -5.280 62.479 1.00 65.34 C ANISOU 4488 CA ASN B 111 11562 5877 7387 2376 -665 -644 C ATOM 4489 C ASN B 111 42.199 -6.560 61.688 1.00 63.42 C ANISOU 4489 C ASN B 111 11311 5560 7227 2352 -671 -709 C ATOM 4490 O ASN B 111 41.997 -7.679 62.238 1.00 53.95 O ANISOU 4490 O ASN B 111 10097 4289 6111 2326 -635 -707 O ATOM 4491 CB ASN B 111 41.971 -4.006 61.959 1.00 55.14 C ANISOU 4491 CB ASN B 111 10309 4649 5995 2446 -726 -668 C ATOM 4492 CG ASN B 111 42.155 -3.788 60.442 1.00 50.48 C ANISOU 4492 CG ASN B 111 9752 4066 5364 2436 -774 -720 C ATOM 4493 OD1 ASN B 111 43.258 -3.438 59.989 1.00 46.38 O ANISOU 4493 OD1 ASN B 111 9262 3559 4801 2392 -772 -701 O ATOM 4494 ND2 ASN B 111 41.064 -3.951 59.660 1.00 47.67 N ANISOU 4494 ND2 ASN B 111 9397 3705 5010 2485 -822 -787 N TER 4495 ASN B 111 MASTER 481 0 0 14 35 0 0 6 4493 2 0 50 END
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RCSB PDB
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RCSB PDB
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RCSB PDB
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Complexes with the same small molecule ligand
PDB Code
Check Database
Ligand Name
4xxb
RCSB PDB
PDBbind
E3 ubiquitin-protein ligase Mdm2
Entry Information
PDB ID
6im9
Complex Type
Protein-Protein
PDBbind Subset
general set
Protein Name
Blue copper oxidase CueO-PM2 sensor
Ligand Name
E3 ubiquitin-protein ligase Mdm2
EC.Number
E.C.-.-.-.-
Resolution
3.3(Å)
Affinity (Kd/Ki/IC50)
Kd=25nM
Release Year
2019
Protein/NA Sequence
Check fasta file
Primary Reference
(2019) J.Biol.Chem. Vol. 294: pp. 7002-7012
Links to External Databases
RCSB PDB
The mother database
PDBsum
Enhanced annotations on PDB entries
Pubchem
Comprehensive collection of chemical and biological data
UniProtKB AC
UniProt accession number (AC):
P36649
Q00987
Entrez Gene ID
NCBI Entrez Gene ID:
947736
4193
ASD
Information of known allosteric effects of PDB entries
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