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*** TRANSFERASE 02-JUL-16 5KP5 ***elNémo ID: 2309111023563978993Job options:ID = 2309111023563978993 JOBID = TRANSFERASE 02-JUL-16 5KP5 USERID = unknown PRIVAT = 0 NMODES = 5 DQMIN = -100 DQMAX = 100 DQSTEP = 20 DOGRAPHS = on DOPROJMODS = 0 DORMSD = 0 NRBL = 0 CUTOFF = 0 CAONLY = 0 Input data for this run:HEADER TRANSFERASE 02-JUL-16 5KP5 TITLE CRYSTAL STRUCTURE OF THE CURACIN BIOSYNTHETIC PATHWAY HMG SYNTHASE COMPND MOL_ID: 1; COMPND 2 MOLECULE: CURD; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: HYDROXYMETHYLGLUTARYL-COA SYNTHASE; COMPND 5 EC: 2.3.3.10; COMPND 6 ENGINEERED: YES; COMPND 7 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MOOREA PRODUCENS 3L; SOURCE 3 ORGANISM_TAXID: 489825; SOURCE 4 GENE: LYNGBM3L_74540; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PMCSG7 KEYWDS HMG SYNTHASE, TRANSFERASE EXPDTA X-RAY DIFFRACTION AUTHOR F.P.MALONEY,J.L.SMITH REVDAT 5 04-DEC-19 5KP5 1 REMARK REVDAT 4 20-SEP-17 5KP5 1 JRNL REMARK REVDAT 3 21-SEP-16 5KP5 1 JRNL REVDAT 2 14-SEP-16 5KP5 1 JRNL REVDAT 1 31-AUG-16 5KP5 0 JRNL AUTH F.P.MALONEY,L.GERWICK,W.H.GERWICK,D.H.SHERMAN,J.L.SMITH JRNL TITL ANATOMY OF THE BETA-BRANCHING ENZYME OF POLYKETIDE JRNL TITL 2 BIOSYNTHESIS AND ITS INTERACTION WITH AN ACYL-ACP SUBSTRATE. JRNL REF PROC.NATL.ACAD.SCI.USA V. 113 10316 2016 JRNL REFN ESSN 1091-6490 JRNL PMID 27573844 JRNL DOI 10.1073/PNAS.1607210113 REMARK 2 REMARK 2 RESOLUTION. 2.10 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.8.0073 REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER, REMARK 3 : NICHOLLS,WINN,LONG,VAGIN REMARK 3 REMARK 3 REFINEMENT TARGET : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 87.61 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 3 NUMBER OF REFLECTIONS : 35297 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING + TEST SET) : 0.160 REMARK 3 R VALUE (WORKING SET) : 0.159 REMARK 3 FREE R VALUE : 0.190 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900 REMARK 3 FREE R VALUE TEST SET COUNT : 1826 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.10 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.16 REMARK 3 REFLECTION IN BIN (WORKING SET) : 2586 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0 REMARK 3 BIN R VALUE (WORKING SET) : 0.3000 REMARK 3 BIN FREE R VALUE SET COUNT : 131 REMARK 3 BIN FREE R VALUE : 0.3280 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 3133 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 5 REMARK 3 SOLVENT ATOMS : 156 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 51.10 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 58.41 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.85000 REMARK 3 B22 (A**2) : 0.85000 REMARK 3 B33 (A**2) : -2.75000 REMARK 3 B12 (A**2) : 0.42000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.131 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.124 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.104 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.454 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.976 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.962 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3205 ; 0.011 ; 0.019 REMARK 3 BOND LENGTHS OTHERS (A): 3011 ; 0.001 ; 0.020 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4327 ; 1.362 ; 1.964 REMARK 3 BOND ANGLES OTHERS (DEGREES): 6919 ; 0.763 ; 3.000 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 403 ; 5.822 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 148 ;38.384 ;23.581 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 545 ;13.488 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 24 ;21.607 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 467 ; 0.080 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3682 ; 0.006 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 758 ; 0.001 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1615 ; 2.554 ; 4.204 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1614 ; 2.550 ; 4.203 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2017 ; 3.589 ; 6.288 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 NCS RESTRAINTS STATISTICS REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 6 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 2 A 33 REMARK 3 ORIGIN FOR THE GROUP (A): 40.6711 31.9602 15.6323 REMARK 3 T TENSOR REMARK 3 T11: 0.1521 T22: 0.1566 REMARK 3 T33: 0.1802 T12: 0.0218 REMARK 3 T13: 0.0237 T23: -0.0044 REMARK 3 L TENSOR REMARK 3 L11: 1.1444 L22: 3.0070 REMARK 3 L33: 1.6369 L12: 1.7672 REMARK 3 L13: 0.7332 L23: 0.6339 REMARK 3 S TENSOR REMARK 3 S11: 0.2996 S12: 0.0375 S13: -0.1438 REMARK 3 S21: 0.5545 S22: -0.0971 S23: -0.0798 REMARK 3 S31: 0.1114 S32: 0.4105 S33: -0.2024 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 34 A 132 REMARK 3 ORIGIN FOR THE GROUP (A): 30.0633 28.3846 -0.3171 REMARK 3 T TENSOR REMARK 3 T11: 0.1085 T22: 0.1343 REMARK 3 T33: 0.1559 T12: 0.0454 REMARK 3 T13: -0.0123 T23: -0.0316 REMARK 3 L TENSOR REMARK 3 L11: 0.3167 L22: 0.4929 REMARK 3 L33: 0.5979 L12: -0.0495 REMARK 3 L13: 0.3577 L23: -0.3319 REMARK 3 S TENSOR REMARK 3 S11: 0.1149 S12: 0.0546 S13: -0.0898 REMARK 3 S21: -0.0120 S22: -0.0129 S23: 0.0284 REMARK 3 S31: 0.0822 S32: 0.1024 S33: -0.1019 REMARK 3 REMARK 3 TLS GROUP : 3 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 133 A 177 REMARK 3 ORIGIN FOR THE GROUP (A): 31.0190 29.1600 3.6886 REMARK 3 T TENSOR REMARK 3 T11: 0.0977 T22: 0.1260 REMARK 3 T33: 0.1742 T12: 0.0766 REMARK 3 T13: -0.0109 T23: 0.0002 REMARK 3 L TENSOR REMARK 3 L11: 0.8829 L22: 1.8889 REMARK 3 L33: 1.3536 L12: 1.2004 REMARK 3 L13: 0.7037 L23: 0.5463 REMARK 3 S TENSOR REMARK 3 S11: -0.0248 S12: 0.0756 S13: 0.0037 REMARK 3 S21: -0.0640 S22: 0.0694 S23: 0.1043 REMARK 3 S31: 0.0535 S32: 0.2261 S33: -0.0446 REMARK 3 REMARK 3 TLS GROUP : 4 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 178 A 242 REMARK 3 ORIGIN FOR THE GROUP (A): 19.5359 29.5255 17.1572 REMARK 3 T TENSOR REMARK 3 T11: 0.0682 T22: 0.1304 REMARK 3 T33: 0.1009 T12: 0.0132 REMARK 3 T13: 0.0355 T23: 0.0763 REMARK 3 L TENSOR REMARK 3 L11: 0.6785 L22: 0.5957 REMARK 3 L33: 1.2968 L12: -0.3022 REMARK 3 L13: 0.2291 L23: -0.2806 REMARK 3 S TENSOR REMARK 3 S11: -0.0019 S12: -0.2508 S13: -0.0996 REMARK 3 S21: 0.0811 S22: 0.1313 S23: 0.1498 REMARK 3 S31: -0.0410 S32: 0.0145 S33: -0.1294 REMARK 3 REMARK 3 TLS GROUP : 5 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 243 A 381 REMARK 3 ORIGIN FOR THE GROUP (A): 32.6725 25.9210 18.1075 REMARK 3 T TENSOR REMARK 3 T11: 0.1151 T22: 0.1402 REMARK 3 T33: 0.1354 T12: 0.0792 REMARK 3 T13: 0.0004 T23: 0.0673 REMARK 3 L TENSOR REMARK 3 L11: 0.2476 L22: 0.0953 REMARK 3 L33: 1.0227 L12: -0.0047 REMARK 3 L13: -0.0278 L23: -0.0632 REMARK 3 S TENSOR REMARK 3 S11: 0.0431 S12: -0.1013 S13: -0.0869 REMARK 3 S21: 0.0938 S22: 0.0819 S23: 0.0341 REMARK 3 S31: 0.0479 S32: 0.1198 S33: -0.1251 REMARK 3 REMARK 3 TLS GROUP : 6 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 382 A 419 REMARK 3 ORIGIN FOR THE GROUP (A): 46.2613 36.9663 -5.8286 REMARK 3 T TENSOR REMARK 3 T11: 0.0681 T22: 0.2536 REMARK 3 T33: 0.1481 T12: 0.0327 REMARK 3 T13: 0.0674 T23: -0.0708 REMARK 3 L TENSOR REMARK 3 L11: 1.3529 L22: 1.9108 REMARK 3 L33: 0.3556 L12: 1.1302 REMARK 3 L13: 0.1853 L23: -0.3888 REMARK 3 S TENSOR REMARK 3 S11: -0.0532 S12: 0.3099 S13: -0.1941 REMARK 3 S21: -0.2474 S22: 0.0955 S23: -0.2259 REMARK 3 S31: 0.0910 S32: 0.1700 S33: -0.0423 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : NULL REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.20 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING REMARK 3 POSITIONS U VALUES : WITH TLS ADDED REMARK 4 REMARK 4 5KP5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-JUL-16. REMARK 100 THE DEPOSITION ID IS D_1000222563. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 06-NOV-14 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 6.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 23-ID-D REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.033 REMARK 200 MONOCHROMATOR : CRYSTAL MONOCHROMATOR AND K-B REMARK 200 PAIR OF BIOMORPH MIRRORS REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XDS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 37159 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100 REMARK 200 RESOLUTION RANGE LOW (A) : 87.610 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 200 DATA REDUNDANCY : 19.50 REMARK 200 R MERGE (I) : 0.11200 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 15.5000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: 1YSL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 63.42 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.36 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 6% PEG 8000, 20 MM (NH4)2SO4, 1X MMT REMARK 280 PH 6.5, VAPOR DIFFUSION, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 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+1/3 REMARK 290 3555 -X+Y,-X,Z+2/3 REMARK 290 4555 Y,X,-Z REMARK 290 5555 X-Y,-Y,-Z+2/3 REMARK 290 6555 -X,-X+Y,-Z+1/3 REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 35.41133 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 70.82267 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 70.82267 REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 35.41133 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: 6380 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 27230 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -62.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMT1 2 -0.500000 0.866025 0.000000 0.00000 REMARK 350 BIOMT2 2 0.866025 0.500000 0.000000 0.00000 REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 MET A -23 REMARK 465 HIS A -22 REMARK 465 HIS A -21 REMARK 465 HIS A -20 REMARK 465 HIS A -19 REMARK 465 HIS A -18 REMARK 465 HIS A -17 REMARK 465 SER A -16 REMARK 465 SER A -15 REMARK 465 GLY A -14 REMARK 465 VAL A -13 REMARK 465 ASP A -12 REMARK 465 LEU A -11 REMARK 465 GLY A -10 REMARK 465 THR A -9 REMARK 465 GLU A -8 REMARK 465 ASN A -7 REMARK 465 LEU A -6 REMARK 465 TYR A -5 REMARK 465 PHE A -4 REMARK 465 GLN A -3 REMARK 465 SER A -2 REMARK 465 ASN A -1 REMARK 465 ALA A 0 REMARK 465 MET A 1 REMARK 465 LEU A 149 REMARK 465 VAL A 150 REMARK 465 ALA A 151 REMARK 465 GLU A 152 REMARK 465 GLY A 153 REMARK 465 GLY A 154 REMARK 465 GLU A 155 REMARK 465 ALA A 156 REMARK 465 ILE A 157 REMARK 465 ASN A 158 REMARK 465 TYR A 159 REMARK 465 ASP A 160 REMARK 465 TRP A 161 REMARK 465 SER A 162 REMARK 465 PHE A 163 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 MET A 38 34.13 71.84 REMARK 500 TYR A 48 30.32 -92.60 REMARK 500 GLN A 112 68.69 -170.49 REMARK 500 ALA A 113 -130.34 36.82 REMARK 500 MET A 199 54.55 -93.21 REMARK 500 MET A 298 -123.75 57.09 REMARK 500 PHE A 412 -9.21 77.90 REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 501 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 5KP6 RELATED DB: PDB REMARK 900 RELATED ID: 5KP7 RELATED DB: PDB DBREF 5KP5 A 1 419 UNP F4Y432 F4Y432_9CYAN 1 419 SEQADV 5KP5 MET A -23 UNP F4Y432 INITIATING METHIONINE SEQADV 5KP5 HIS A -22 UNP F4Y432 EXPRESSION TAG SEQADV 5KP5 HIS A -21 UNP F4Y432 EXPRESSION TAG SEQADV 5KP5 HIS A -20 UNP F4Y432 EXPRESSION TAG SEQADV 5KP5 HIS A -19 UNP F4Y432 EXPRESSION TAG SEQADV 5KP5 HIS A -18 UNP F4Y432 EXPRESSION TAG SEQADV 5KP5 HIS A -17 UNP F4Y432 EXPRESSION TAG SEQADV 5KP5 SER A -16 UNP F4Y432 EXPRESSION TAG SEQADV 5KP5 SER A -15 UNP F4Y432 EXPRESSION TAG SEQADV 5KP5 GLY A -14 UNP F4Y432 EXPRESSION TAG SEQADV 5KP5 VAL A -13 UNP F4Y432 EXPRESSION TAG SEQADV 5KP5 ASP A -12 UNP F4Y432 EXPRESSION TAG SEQADV 5KP5 LEU A -11 UNP F4Y432 EXPRESSION TAG SEQADV 5KP5 GLY A -10 UNP F4Y432 EXPRESSION TAG SEQADV 5KP5 THR A -9 UNP F4Y432 EXPRESSION TAG SEQADV 5KP5 GLU A -8 UNP F4Y432 EXPRESSION TAG SEQADV 5KP5 ASN A -7 UNP F4Y432 EXPRESSION TAG SEQADV 5KP5 LEU A -6 UNP F4Y432 EXPRESSION TAG SEQADV 5KP5 TYR A -5 UNP F4Y432 EXPRESSION TAG SEQADV 5KP5 PHE A -4 UNP F4Y432 EXPRESSION TAG SEQADV 5KP5 GLN A -3 UNP F4Y432 EXPRESSION TAG SEQADV 5KP5 SER A -2 UNP F4Y432 EXPRESSION TAG SEQADV 5KP5 ASN A -1 UNP F4Y432 EXPRESSION TAG SEQADV 5KP5 ALA A 0 UNP F4Y432 EXPRESSION TAG SEQADV 5KP5 ALA A 344 UNP F4Y432 LYS 344 ENGINEERED MUTATION SEQADV 5KP5 ALA A 345 UNP F4Y432 GLN 345 ENGINEERED MUTATION SEQADV 5KP5 ALA A 347 UNP F4Y432 GLN 347 ENGINEERED MUTATION SEQRES 1 A 443 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU SEQRES 2 A 443 GLY THR GLU ASN LEU TYR PHE GLN SER ASN ALA MET GLN SEQRES 3 A 443 GLN VAL GLY ILE GLU ALA LEU SER VAL TYR GLY GLY ALA SEQRES 4 A 443 ALA GLN LEU GLU LEU ARG LYS LEU ALA GLN ALA ARG GLN SEQRES 5 A 443 LEU ASP ILE SER ARG PHE ASP ASN LEU MET MET LYS GLU SEQRES 6 A 443 LYS ALA VAL SER LEU PRO TYR GLU ASP PRO VAL SER TYR SEQRES 7 A 443 ALA VAL ASN ALA ALA LYS PRO ILE ILE ASP ARG LEU SER SEQRES 8 A 443 ASP ALA ASP LYS GLN ARG ILE GLU MET VAL ILE THR CYS SEQRES 9 A 443 SER GLU SER GLY ILE ASP PHE GLY LYS SER MET SER THR SEQRES 10 A 443 TYR ILE GLN GLU TYR LEU GLY LEU SER ARG ASN CYS ARG SEQRES 11 A 443 MET PHE GLU LEU LYS GLN ALA CYS TYR SER GLY THR ALA SEQRES 12 A 443 GLY LEU GLN MET ALA ILE ASN LEU ILE LEU SER GLN THR SEQRES 13 A 443 PHE PRO GLY ALA LYS ALA LEU VAL ILE ALA THR ASP ILE SEQRES 14 A 443 SER ARG PHE LEU VAL ALA GLU GLY GLY GLU ALA ILE ASN SEQRES 15 A 443 TYR ASP TRP SER PHE ALA GLU PRO SER SER GLY ALA GLY SEQRES 16 A 443 ALA VAL ALA LEU LEU VAL SER ASP THR PRO HIS ILE PHE SEQRES 17 A 443 GLN ILE ASP VAL GLY CYS ASN GLY TYR TYR GLY TYR GLU SEQRES 18 A 443 VAL MET ASP THR CYS ARG PRO ASN PRO ASP SER GLU ALA SEQRES 19 A 443 GLY ASP ALA ASP LEU SER LEU LEU SER TYR LEU ASP CYS SEQRES 20 A 443 CYS GLU ASN ALA TYR ARG HIS TYR GLN ASN ARG VAL GLU SEQRES 21 A 443 GLY VAL ASP TYR ARG GLU SER PHE ASP TYR LEU SER PHE SEQRES 22 A 443 HIS THR PRO PHE GLY GLY MET VAL LYS GLY ALA HIS ARG SEQRES 23 A 443 ASN MET MET ARG ARG LEU LYS ARG ALA LYS PRO ALA GLU SEQRES 24 A 443 ILE GLU ALA ASP PHE GLN ARG ARG VAL MET PRO GLY LEU SEQRES 25 A 443 VAL TYR CYS GLN GLN VAL GLY ASN ILE MET GLY ALA THR SEQRES 26 A 443 LEU PHE LEU SER LEU ALA SER THR ILE ASP ASN GLY ASP SEQRES 27 A 443 PHE SER THR PRO ARG ARG ILE GLY MET PHE SER TYR GLY SEQRES 28 A 443 SER GLY CYS CYS SER GLU PHE TYR SER GLY VAL VAL THR SEQRES 29 A 443 PRO GLU GLY ALA ALA ILE ALA ALA GLN GLN GLY ILE SER SEQRES 30 A 443 ALA GLN LEU ALA ASP ARG TYR SER LEU SER MET GLU GLU SEQRES 31 A 443 TYR GLU GLN LEU LEU TYR HIS SER SER ALA VAL ALA PHE SEQRES 32 A 443 GLY THR ARG ASN VAL THR LEU ASP TYR GLN LEU PHE PRO SEQRES 33 A 443 GLY VAL TRP LYS LYS ILE ALA GLY LYS GLY ARG LEU VAL SEQRES 34 A 443 LEU LYS ALA ILE LYS GLU PHE HIS ARG LYS TYR GLU TRP SEQRES 35 A 443 VAL HET SO4 A 501 5 HETNAM SO4 SULFATE ION FORMUL 2 SO4 O4 S 2- FORMUL 3 HOH *156(H2 O) HELIX 1 AA1 LEU A 20 ARG A 27 1 8 HELIX 2 AA2 ILE A 31 MET A 38 1 8 HELIX 3 AA3 ASP A 50 LEU A 66 1 17 HELIX 4 AA4 SER A 67 ARG A 73 1 7 HELIX 5 AA5 MET A 91 GLY A 100 1 10 HELIX 6 AA6 GLN A 112 CYS A 114 5 3 HELIX 7 AA7 TYR A 115 SER A 130 1 16 HELIX 8 AA8 ASP A 212 VAL A 235 1 24 HELIX 9 AA9 PHE A 253 ARG A 270 1 18 HELIX 10 AB1 LYS A 272 VAL A 284 1 13 HELIX 11 AB2 VAL A 284 GLY A 295 1 12 HELIX 12 AB3 ILE A 297 GLY A 299 5 3 HELIX 13 AB4 ALA A 300 GLY A 313 1 14 HELIX 14 AB5 THR A 340 GLN A 349 1 10 HELIX 15 AB6 GLY A 351 ASP A 358 1 8 HELIX 16 AB7 SER A 363 SER A 374 1 12 HELIX 17 AB8 SER A 375 ALA A 378 5 4 HELIX 18 AB9 PHE A 391 LYS A 397 1 7 SHEET 1 AA1 9 ARG A 106 LEU A 110 0 SHEET 2 AA1 9 ILE A 74 CYS A 80 1 N THR A 79 O LEU A 110 SHEET 3 AA1 9 LYS A 137 ILE A 145 1 O ILE A 141 N CYS A 80 SHEET 4 AA1 9 ALA A 170 SER A 178 -1 O LEU A 175 N VAL A 140 SHEET 5 AA1 9 GLY A 5 TYR A 12 -1 N SER A 10 O ALA A 174 SHEET 6 AA1 9 PHE A 184 GLY A 195 -1 O PHE A 184 N ILE A 6 SHEET 7 AA1 9 CYS A 331 VAL A 339 -1 O PHE A 334 N GLY A 192 SHEET 8 AA1 9 ARG A 319 GLY A 327 -1 N MET A 323 O TYR A 335 SHEET 9 AA1 9 TYR A 246 PHE A 249 1 N SER A 248 O GLY A 322 SHEET 1 AA2 3 GLU A 41 VAL A 44 0 SHEET 2 AA2 3 ALA A 16 GLU A 19 -1 N ALA A 16 O VAL A 44 SHEET 3 AA2 3 TYR A 360 SER A 361 1 O TYR A 360 N GLN A 17 SHEET 1 AA3 2 THR A 201 CYS A 202 0 SHEET 2 AA3 2 ALA A 210 GLY A 211 -1 O ALA A 210 N CYS A 202 SHEET 1 AA4 3 VAL A 384 THR A 385 0 SHEET 2 AA4 3 LEU A 404 LYS A 410 -1 O ILE A 409 N VAL A 384 SHEET 3 AA4 3 HIS A 413 TRP A 418 -1 O LYS A 415 N ALA A 408 CISPEP 1 GLY A 329 CYS A 330 0 -6.56 SITE 1 AC1 3 TYR A 231 VAL A 235 ARG A 320 CRYST1 101.162 101.162 106.234 90.00 90.00 120.00 P 31 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 0.009885 0.005707 0.000000 0.00000 SCALE2 0.000000 0.011414 0.000000 0.00000 SCALE3 0.000000 0.000000 0.009413 0.00000 ATOM 1 N GLN A 2 13.117 9.468 5.482 1.00 94.90 N ANISOU 1 N GLN A 2 12411 10043 13604 -598 -192 688 N ATOM 2 CA GLN A 2 14.089 9.668 4.373 1.00 92.25 C ANISOU 2 CA GLN A 2 12089 9744 13216 -420 -343 711 C ATOM 3 C GLN A 2 15.395 10.237 4.913 1.00 83.04 C ANISOU 3 C GLN A 2 10971 8634 11947 -288 -293 649 C ATOM 4 O GLN A 2 15.430 10.843 5.989 1.00 82.17 O ANISOU 4 O GLN A 2 10816 8541 11862 -325 -136 600 O ATOM 5 CB GLN A 2 13.532 10.612 3.295 1.00 93.09 C ANISOU 5 CB GLN A 2 11945 9879 13546 -399 -383 761 C ATOM 6 CG GLN A 2 13.987 10.209 1.894 1.00 94.92 C ANISOU 6 CG GLN A 2 12261 10113 13691 -326 -580 812 C ATOM 7 CD GLN A 2 14.400 11.374 1.016 1.00 90.72 C ANISOU 7 CD GLN A 2 11576 9640 13255 -239 -620 830 C ATOM 8 OE1 GLN A 2 13.569 12.195 0.633 1.00 93.60 O ANISOU 8 OE1 GLN A 2 11730 9991 13842 -289 -629 881 O ATOM 9 NE2 GLN A 2 15.688 11.428 0.660 1.00 79.78 N ANISOU 9 NE2 GLN A 2 10295 8311 11706 -115 -658 787 N ATOM 10 N GLN A 3 16.481 10.041 4.182 1.00 71.17 N ANISOU 10 N GLN A 3 9555 7158 10325 -143 -418 640 N ATOM 11 CA GLN A 3 17.744 10.507 4.702 1.00 69.54 C ANISOU 11 CA GLN A 3 9387 7007 10027 -22 -383 578 C ATOM 12 C GLN A 3 18.409 11.620 3.942 1.00 64.43 C ANISOU 12 C GLN A 3 8582 6451 9445 91 -381 565 C ATOM 13 O GLN A 3 18.296 11.768 2.711 1.00 61.53 O ANISOU 13 O GLN A 3 8148 6105 9123 113 -469 600 O ATOM 14 CB GLN A 3 18.708 9.377 4.977 1.00 75.48 C ANISOU 14 CB GLN A 3 10388 7712 10577 51 -497 542 C ATOM 15 CG GLN A 3 18.823 8.307 3.942 1.00 78.26 C ANISOU 15 CG GLN A 3 10865 8018 10852 95 -661 553 C ATOM 16 CD GLN A 3 19.796 7.272 4.435 1.00 80.80 C ANISOU 16 CD GLN A 3 11418 8272 11011 180 -769 501 C ATOM 17 OE1 GLN A 3 20.572 6.708 3.676 1.00 81.74 O ANISOU 17 OE1 GLN A 3 11610 8380 11066 302 -884 455 O ATOM 18 NE2 GLN A 3 19.794 7.063 5.734 1.00 80.08 N ANISOU 18 NE2 GLN A 3 11441 8127 10858 111 -733 501 N ATOM 19 N VAL A 4 19.070 12.450 4.725 1.00 58.99 N ANISOU 19 N VAL A 4 7845 5814 8753 139 -279 518 N ATOM 20 CA VAL A 4 19.567 13.700 4.216 1.00 56.81 C ANISOU 20 CA VAL A 4 7405 5623 8555 213 -247 509 C ATOM 21 C VAL A 4 20.560 14.234 5.217 1.00 54.34 C ANISOU 21 C VAL A 4 7119 5357 8170 273 -163 447 C ATOM 22 O VAL A 4 20.431 14.032 6.430 1.00 52.35 O ANISOU 22 O VAL A 4 6949 5064 7875 208 -82 426 O ATOM 23 CB VAL A 4 18.416 14.722 3.988 1.00 55.84 C ANISOU 23 CB VAL A 4 7061 5490 8664 132 -173 556 C ATOM 24 CG1 VAL A 4 17.740 15.117 5.295 1.00 53.53 C ANISOU 24 CG1 VAL A 4 6708 5163 8467 40 2 524 C ATOM 25 CG2 VAL A 4 18.942 15.976 3.308 1.00 58.89 C ANISOU 25 CG2 VAL A 4 7307 5947 9120 201 -181 560 C ATOM 26 N GLY A 5 21.553 14.929 4.695 1.00 54.36 N ANISOU 26 N GLY A 5 7059 5446 8148 375 -184 419 N ATOM 27 CA GLY A 5 22.507 15.586 5.540 1.00 53.27 C ANISOU 27 CA GLY A 5 6920 5361 7956 428 -113 367 C ATOM 28 C GLY A 5 23.764 15.941 4.814 1.00 49.53 C ANISOU 28 C GLY A 5 6416 4985 7415 545 -172 324 C ATOM 29 O GLY A 5 23.771 16.126 3.590 1.00 47.20 O ANISOU 29 O GLY A 5 6057 4732 7144 561 -228 338 O ATOM 30 N ILE A 6 24.827 16.060 5.586 1.00 48.44 N ANISOU 30 N ILE A 6 6327 4884 7191 609 -159 269 N ATOM 31 CA ILE A 6 26.104 16.488 5.059 1.00 48.73 C ANISOU 31 CA ILE A 6 6312 5027 7174 712 -191 209 C ATOM 32 C ILE A 6 26.870 15.252 4.621 1.00 47.85 C ANISOU 32 C ILE A 6 6308 4903 6967 810 -317 148 C ATOM 33 O ILE A 6 27.200 14.433 5.451 1.00 47.35 O ANISOU 33 O ILE A 6 6372 4771 6845 844 -379 126 O ATOM 34 CB ILE A 6 26.900 17.280 6.114 1.00 47.51 C ANISOU 34 CB ILE A 6 6140 4919 6992 730 -123 178 C ATOM 35 CG1 ILE A 6 26.105 18.523 6.500 1.00 46.89 C ANISOU 35 CG1 ILE A 6 5952 4839 7022 635 13 222 C ATOM 36 CG2 ILE A 6 28.260 17.700 5.562 1.00 48.43 C ANISOU 36 CG2 ILE A 6 6187 5155 7058 829 -155 108 C ATOM 37 CD1 ILE A 6 26.637 19.268 7.708 1.00 46.57 C ANISOU 37 CD1 ILE A 6 5925 4818 6950 616 100 197 C ATOM 38 N GLU A 7 27.124 15.164 3.314 1.00 48.62 N ANISOU 38 N GLU A 7 6361 5058 7055 843 -357 117 N ATOM 39 CA GLU A 7 27.871 14.093 2.672 1.00 50.42 C ANISOU 39 CA GLU A 7 6662 5281 7211 939 -453 29 C ATOM 40 C GLU A 7 29.371 14.333 2.829 1.00 50.81 C ANISOU 40 C GLU A 7 6654 5423 7226 1055 -455 -82 C ATOM 41 O GLU A 7 30.139 13.388 2.981 1.00 49.38 O ANISOU 41 O GLU A 7 6538 5204 7018 1164 -543 -168 O ATOM 42 CB GLU A 7 27.506 14.018 1.176 1.00 51.58 C ANISOU 42 CB GLU A 7 6786 5459 7349 892 -469 31 C ATOM 43 CG GLU A 7 28.302 12.989 0.371 1.00 57.29 C ANISOU 43 CG GLU A 7 7577 6188 8001 980 -537 -87 C ATOM 44 CD GLU A 7 27.887 12.853 -1.111 1.00 59.80 C ANISOU 44 CD GLU A 7 7913 6526 8281 898 -549 -86 C ATOM 45 OE1 GLU A 7 26.702 13.053 -1.473 1.00 60.00 O ANISOU 45 OE1 GLU A 7 7949 6504 8341 776 -565 32 O ATOM 46 OE2 GLU A 7 28.765 12.515 -1.940 1.00 60.96 O ANISOU 46 OE2 GLU A 7 8064 6733 8364 946 -544 -214 O ATOM 47 N ALA A 8 29.779 15.601 2.804 1.00 46.93 N ANISOU 47 N ALA A 8 6036 5045 6751 1030 -367 -83 N ATOM 48 CA ALA A 8 31.179 15.958 2.999 1.00 46.34 C ANISOU 48 CA ALA A 8 5885 5070 6652 1121 -359 -184 C ATOM 49 C ALA A 8 31.336 17.386 3.524 1.00 45.69 C ANISOU 49 C ALA A 8 5705 5068 6587 1063 -265 -142 C ATOM 50 O ALA A 8 30.517 18.275 3.230 1.00 44.94 O ANISOU 50 O ALA A 8 5561 4983 6528 961 -196 -60 O ATOM 51 CB ALA A 8 31.921 15.816 1.685 1.00 46.55 C ANISOU 51 CB ALA A 8 5848 5196 6643 1157 -351 -298 C ATOM 52 N LEU A 9 32.421 17.607 4.256 1.00 44.91 N ANISOU 52 N LEU A 9 5573 5017 6472 1132 -276 -202 N ATOM 53 CA LEU A 9 32.669 18.854 4.932 1.00 46.49 C ANISOU 53 CA LEU A 9 5707 5279 6676 1081 -198 -168 C ATOM 54 C LEU A 9 34.133 19.158 4.826 1.00 47.30 C ANISOU 54 C LEU A 9 5710 5506 6754 1155 -208 -276 C ATOM 55 O LEU A 9 34.952 18.328 5.216 1.00 47.97 O ANISOU 55 O LEU A 9 5816 5567 6843 1264 -304 -352 O ATOM 56 CB LEU A 9 32.283 18.742 6.404 1.00 48.73 C ANISOU 56 CB LEU A 9 6099 5456 6961 1051 -209 -104 C ATOM 57 CG LEU A 9 32.324 20.068 7.177 1.00 53.16 C ANISOU 57 CG LEU A 9 6614 6058 7524 974 -108 -63 C ATOM 58 CD1 LEU A 9 31.364 20.074 8.361 1.00 54.59 C ANISOU 58 CD1 LEU A 9 6909 6120 7712 879 -59 9 C ATOM 59 CD2 LEU A 9 33.742 20.431 7.651 1.00 55.08 C ANISOU 59 CD2 LEU A 9 6812 6389 7727 1032 -145 -129 C ATOM 60 N ASER A 10 34.472 20.334 4.296 1.00 46.40 N ANISOU 60 N ASER A 10 5487 5518 6625 1094 -120 -284 N ATOM 61 CA ASER A 10 35.864 20.801 4.270 1.00 46.73 C ANISOU 61 CA ASER A 10 5417 5694 6643 1136 -109 -386 C ATOM 62 C ASER A 10 35.974 22.239 4.733 1.00 45.81 C ANISOU 62 C ASER A 10 5251 5642 6510 1046 -29 -328 C ATOM 63 O ASER A 10 35.032 23.047 4.584 1.00 44.50 O ANISOU 63 O ASER A 10 5102 5447 6358 944 34 -232 O ATOM 64 CB ASER A 10 36.465 20.665 2.876 1.00 49.56 C ANISOU 64 CB ASER A 10 5687 6172 6972 1141 -77 -501 C ATOM 65 OG ASER A 10 36.682 19.304 2.536 1.00 54.77 O ANISOU 65 OG ASER A 10 6376 6778 7654 1249 -150 -596 O ATOM 66 N VAL A 11 37.146 22.563 5.265 1.00 43.98 N ANISOU 66 N VAL A 11 4952 5494 6264 1084 -44 -393 N ATOM 67 CA VAL A 11 37.394 23.828 5.916 1.00 44.73 C ANISOU 67 CA VAL A 11 5020 5638 6335 1006 14 -345 C ATOM 68 C VAL A 11 38.605 24.542 5.352 1.00 45.23 C ANISOU 68 C VAL A 11 4946 5878 6361 987 52 -437 C ATOM 69 O VAL A 11 39.588 23.890 5.010 1.00 45.92 O ANISOU 69 O VAL A 11 4947 6038 6461 1073 9 -562 O ATOM 70 CB VAL A 11 37.687 23.513 7.383 1.00 46.80 C ANISOU 70 CB VAL A 11 5363 5818 6601 1047 -60 -322 C ATOM 71 CG1 VAL A 11 38.136 24.749 8.128 1.00 50.58 C ANISOU 71 CG1 VAL A 11 5822 6351 7043 968 -8 -290 C ATOM 72 CG2 VAL A 11 36.450 22.908 8.022 1.00 47.36 C ANISOU 72 CG2 VAL A 11 5585 5721 6688 1024 -74 -232 C ATOM 73 N TYR A 12 38.568 25.875 5.301 1.00 43.26 N ANISOU 73 N TYR A 12 4671 5691 6074 872 132 -386 N ATOM 74 CA TYR A 12 39.777 26.668 5.025 1.00 43.51 C ANISOU 74 CA TYR A 12 4586 5889 6055 828 169 -463 C ATOM 75 C TYR A 12 39.894 27.757 6.090 1.00 42.53 C ANISOU 75 C TYR A 12 4492 5754 5910 762 191 -390 C ATOM 76 O TYR A 12 39.018 28.603 6.219 1.00 41.27 O ANISOU 76 O TYR A 12 4398 5528 5751 674 246 -290 O ATOM 77 CB TYR A 12 39.777 27.284 3.610 1.00 43.19 C ANISOU 77 CB TYR A 12 4496 5960 5954 715 244 -489 C ATOM 78 CG TYR A 12 41.012 28.147 3.287 1.00 43.58 C ANISOU 78 CG TYR A 12 4432 6192 5934 635 298 -574 C ATOM 79 CD1 TYR A 12 42.290 27.598 3.267 1.00 44.74 C ANISOU 79 CD1 TYR A 12 4446 6457 6094 712 287 -729 C ATOM 80 CD2 TYR A 12 40.897 29.501 3.057 1.00 43.12 C ANISOU 80 CD2 TYR A 12 4394 6179 5811 484 352 -504 C ATOM 81 CE1 TYR A 12 43.408 28.372 2.995 1.00 43.89 C ANISOU 81 CE1 TYR A 12 4219 6525 5930 627 346 -815 C ATOM 82 CE2 TYR A 12 42.016 30.285 2.777 1.00 44.41 C ANISOU 82 CE2 TYR A 12 4465 6511 5895 390 402 -578 C ATOM 83 CZ TYR A 12 43.260 29.718 2.753 1.00 45.08 C ANISOU 83 CZ TYR A 12 4410 6728 5989 456 407 -735 C ATOM 84 OH TYR A 12 44.359 30.506 2.464 1.00 48.30 O ANISOU 84 OH TYR A 12 4712 7314 6325 348 468 -817 O ATOM 85 N GLY A 13 41.006 27.749 6.812 1.00 42.33 N ANISOU 85 N GLY A 13 4413 5792 5878 802 143 -447 N ATOM 86 CA GLY A 13 41.193 28.542 8.009 1.00 43.84 C ANISOU 86 CA GLY A 13 4661 5955 6042 747 140 -383 C ATOM 87 C GLY A 13 42.255 29.603 7.837 1.00 46.58 C ANISOU 87 C GLY A 13 4904 6461 6333 666 178 -427 C ATOM 88 O GLY A 13 42.836 30.089 8.821 1.00 47.27 O ANISOU 88 O GLY A 13 5009 6557 6395 636 146 -408 O ATOM 89 N GLY A 14 42.497 29.984 6.590 1.00 45.57 N ANISOU 89 N GLY A 14 4683 6457 6171 607 244 -482 N ATOM 90 CA GLY A 14 43.463 31.019 6.278 1.00 48.58 C ANISOU 90 CA GLY A 14 4973 7003 6483 498 294 -528 C ATOM 91 C GLY A 14 44.841 30.459 5.973 1.00 49.94 C ANISOU 91 C GLY A 14 4968 7329 6675 559 266 -687 C ATOM 92 O GLY A 14 45.134 29.277 6.171 1.00 48.90 O ANISOU 92 O GLY A 14 4785 7162 6630 705 185 -761 O ATOM 93 N ALA A 15 45.679 31.348 5.474 1.00 50.01 N ANISOU 93 N ALA A 15 4880 7506 6614 438 332 -745 N ATOM 94 CA ALA A 15 47.049 31.060 5.209 1.00 50.40 C ANISOU 94 CA ALA A 15 4732 7725 6692 464 332 -910 C ATOM 95 C ALA A 15 47.923 31.626 6.314 1.00 51.85 C ANISOU 95 C ALA A 15 4868 7947 6882 449 266 -894 C ATOM 96 O ALA A 15 49.092 31.284 6.412 1.00 54.02 O ANISOU 96 O ALA A 15 4964 8334 7226 503 223 -1023 O ATOM 97 CB ALA A 15 47.447 31.686 3.890 1.00 52.56 C ANISOU 97 CB ALA A 15 4930 8175 6865 303 463 -997 C ATOM 98 N ALA A 16 47.381 32.534 7.105 1.00 50.22 N ANISOU 98 N ALA A 16 4815 7653 6612 365 261 -746 N ATOM 99 CA ALA A 16 48.136 33.180 8.165 1.00 51.98 C ANISOU 99 CA ALA A 16 5030 7903 6814 319 201 -716 C ATOM 100 C ALA A 16 47.273 33.392 9.394 1.00 52.25 C ANISOU 100 C ALA A 16 5273 7745 6832 319 153 -566 C ATOM 101 O ALA A 16 46.026 33.430 9.308 1.00 52.81 O ANISOU 101 O ALA A 16 5486 7683 6896 314 206 -479 O ATOM 102 CB ALA A 16 48.673 34.505 7.677 1.00 52.25 C ANISOU 102 CB ALA A 16 5023 8091 6737 131 295 -724 C ATOM 103 N GLN A 17 47.925 33.560 10.541 1.00 55.05 N ANISOU 103 N GLN A 17 5649 8083 7183 310 57 -540 N ATOM 104 CA GLN A 17 47.208 33.896 11.778 1.00 54.60 C ANISOU 104 CA GLN A 17 5809 7856 7080 265 34 -411 C ATOM 105 C GLN A 17 48.028 34.759 12.739 1.00 53.65 C ANISOU 105 C GLN A 17 5721 7774 6889 154 -15 -378 C ATOM 106 O GLN A 17 49.267 34.848 12.638 1.00 53.06 O ANISOU 106 O GLN A 17 5482 7847 6830 144 -81 -453 O ATOM 107 CB GLN A 17 46.723 32.619 12.476 1.00 56.65 C ANISOU 107 CB GLN A 17 6162 7953 7407 392 -76 -387 C ATOM 108 CG GLN A 17 47.803 31.587 12.745 1.00 60.06 C ANISOU 108 CG GLN A 17 6468 8418 7932 514 -256 -468 C ATOM 109 CD GLN A 17 48.636 31.885 13.978 1.00 66.89 C ANISOU 109 CD GLN A 17 7381 9266 8767 455 -397 -427 C ATOM 110 OE1 GLN A 17 48.352 32.817 14.732 1.00 75.84 O ANISOU 110 OE1 GLN A 17 8673 10352 9790 316 -348 -335 O ATOM 111 NE2 GLN A 17 49.662 31.082 14.201 1.00 68.17 N ANISOU 111 NE2 GLN A 17 7409 9454 9037 561 -582 -498 N ATOM 112 N LEU A 18 47.318 35.380 13.674 1.00 51.53 N ANISOU 112 N LEU A 18 5661 7369 6549 63 21 -274 N ATOM 113 CA LEU A 18 47.925 36.199 14.747 1.00 54.40 C ANISOU 113 CA LEU A 18 6116 7730 6824 -61 -23 -226 C ATOM 114 C LEU A 18 47.595 35.592 16.113 1.00 57.08 C ANISOU 114 C LEU A 18 6650 7893 7142 -57 -123 -159 C ATOM 115 O LEU A 18 46.411 35.369 16.440 1.00 55.07 O ANISOU 115 O LEU A 18 6558 7484 6882 -56 -46 -111 O ATOM 116 CB LEU A 18 47.384 37.623 14.701 1.00 53.03 C ANISOU 116 CB LEU A 18 6050 7537 6561 -210 127 -170 C ATOM 117 CG LEU A 18 47.932 38.646 15.711 1.00 54.42 C ANISOU 117 CG LEU A 18 6340 7708 6627 -364 110 -123 C ATOM 118 CD1 LEU A 18 49.377 39.051 15.421 1.00 54.50 C ANISOU 118 CD1 LEU A 18 6177 7918 6609 -420 34 -175 C ATOM 119 CD2 LEU A 18 47.009 39.854 15.709 1.00 53.39 C ANISOU 119 CD2 LEU A 18 6354 7488 6445 -476 270 -72 C ATOM 120 N GLU A 19 48.636 35.318 16.897 1.00 64.80 N ANISOU 120 N GLU A 19 7614 8892 8112 -68 -300 -159 N ATOM 121 CA GLU A 19 48.471 34.961 18.313 1.00 66.80 C ANISOU 121 CA GLU A 19 8099 8980 8301 -127 -415 -81 C ATOM 122 C GLU A 19 48.011 36.186 19.057 1.00 62.35 C ANISOU 122 C GLU A 19 7741 8351 7597 -315 -283 -15 C ATOM 123 O GLU A 19 48.662 37.223 19.003 1.00 61.50 O ANISOU 123 O GLU A 19 7586 8348 7432 -416 -254 -17 O ATOM 124 CB GLU A 19 49.786 34.465 18.904 1.00 75.09 C ANISOU 124 CB GLU A 19 9074 10068 9387 -106 -670 -90 C ATOM 125 CG GLU A 19 50.158 33.073 18.413 1.00 83.37 C ANISOU 125 CG GLU A 19 9956 11122 10600 93 -829 -160 C ATOM 126 CD GLU A 19 51.644 32.796 18.538 1.00 98.18 C ANISOU 126 CD GLU A 19 11629 13095 12579 146 -1054 -216 C ATOM 127 OE1 GLU A 19 52.238 33.189 19.573 1.00109.17 O ANISOU 127 OE1 GLU A 19 13127 14450 13900 26 -1196 -147 O ATOM 128 OE2 GLU A 19 52.219 32.194 17.600 1.00104.83 O ANISOU 128 OE2 GLU A 19 12202 14047 13580 300 -1087 -335 O ATOM 129 N LEU A 20 46.887 36.072 19.745 1.00 62.09 N ANISOU 129 N LEU A 20 7935 8145 7510 -371 -193 33 N ATOM 130 CA LEU A 20 46.265 37.240 20.357 1.00 68.56 C ANISOU 130 CA LEU A 20 8942 8886 8222 -539 -20 67 C ATOM 131 C LEU A 20 47.035 37.784 21.568 1.00 74.00 C ANISOU 131 C LEU A 20 9795 9550 8770 -710 -115 113 C ATOM 132 O LEU A 20 46.852 38.947 21.918 1.00 72.19 O ANISOU 132 O LEU A 20 9676 9299 8453 -852 18 124 O ATOM 133 CB LEU A 20 44.796 36.964 20.717 1.00 67.76 C ANISOU 133 CB LEU A 20 9011 8609 8124 -556 134 78 C ATOM 134 CG LEU A 20 43.933 36.816 19.461 1.00 71.42 C ANISOU 134 CG LEU A 20 9317 9096 8722 -423 257 41 C ATOM 135 CD1 LEU A 20 42.560 36.273 19.783 1.00 71.55 C ANISOU 135 CD1 LEU A 20 9463 8950 8773 -419 373 44 C ATOM 136 CD2 LEU A 20 43.836 38.143 18.717 1.00 73.08 C ANISOU 136 CD2 LEU A 20 9439 9376 8951 -464 395 26 C ATOM 137 N ARG A 21 47.894 36.961 22.181 1.00 77.75 N ANISOU 137 N ARG A 21 10289 10018 9232 -699 -358 140 N ATOM 138 CA ARG A 21 48.778 37.423 23.253 1.00 83.45 C ANISOU 138 CA ARG A 21 11149 10728 9828 -864 -497 193 C ATOM 139 C ARG A 21 49.675 38.542 22.755 1.00 79.15 C ANISOU 139 C ARG A 21 10441 10355 9275 -911 -474 170 C ATOM 140 O ARG A 21 49.917 39.500 23.470 1.00 79.25 O ANISOU 140 O ARG A 21 10606 10348 9155 -1091 -444 206 O ATOM 141 CB ARG A 21 49.621 36.271 23.837 1.00 92.34 C ANISOU 141 CB ARG A 21 12282 11815 10986 -818 -814 229 C ATOM 142 CG ARG A 21 48.908 35.548 24.977 1.00101.10 C ANISOU 142 CG ARG A 21 13713 12711 11987 -919 -872 295 C ATOM 143 CD ARG A 21 49.732 34.434 25.614 1.00109.05 C ANISOU 143 CD ARG A 21 14764 13646 13021 -892 -1227 348 C ATOM 144 NE ARG A 21 49.015 33.775 26.717 1.00113.41 N ANISOU 144 NE ARG A 21 15667 13985 13435 -1030 -1282 419 N ATOM 145 CZ ARG A 21 49.443 32.689 27.377 1.00121.71 C ANISOU 145 CZ ARG A 21 16840 14915 14489 -1033 -1597 484 C ATOM 146 NH1 ARG A 21 50.602 32.104 27.073 1.00119.10 N ANISOU 146 NH1 ARG A 21 16285 14643 14322 -879 -1899 480 N ATOM 147 NH2 ARG A 21 48.704 32.175 28.357 1.00125.09 N ANISOU 147 NH2 ARG A 21 17618 15150 14757 -1198 -1617 549 N ATOM 148 N LYS A 22 50.152 38.422 21.520 1.00 75.65 N ANISOU 148 N LYS A 22 9700 10079 8963 -767 -477 103 N ATOM 149 CA LYS A 22 50.935 39.486 20.906 1.00 72.32 C ANISOU 149 CA LYS A 22 9118 9833 8525 -828 -429 71 C ATOM 150 C LYS A 22 50.129 40.778 20.768 1.00 72.30 C ANISOU 150 C LYS A 22 9244 9793 8433 -948 -190 85 C ATOM 151 O LYS A 22 50.685 41.868 20.926 1.00 72.16 O ANISOU 151 O LYS A 22 9251 9840 8323 -1089 -168 100 O ATOM 152 CB LYS A 22 51.449 39.063 19.545 1.00 69.41 C ANISOU 152 CB LYS A 22 8427 9643 8301 -672 -439 -20 C ATOM 153 CG LYS A 22 52.440 37.927 19.593 1.00 73.26 C ANISOU 153 CG LYS A 22 8734 10186 8915 -546 -677 -63 C ATOM 154 CD LYS A 22 52.821 37.514 18.187 1.00 74.34 C ANISOU 154 CD LYS A 22 8558 10493 9194 -400 -634 -183 C ATOM 155 CE LYS A 22 53.545 36.186 18.190 1.00 76.02 C ANISOU 155 CE LYS A 22 8593 10713 9576 -230 -852 -247 C ATOM 156 NZ LYS A 22 53.951 35.853 16.801 1.00 78.89 N ANISOU 156 NZ LYS A 22 8650 11251 10071 -108 -775 -390 N ATOM 157 N LEU A 23 48.834 40.662 20.468 1.00 70.94 N ANISOU 157 N LEU A 23 9145 9507 8299 -891 -24 80 N ATOM 158 CA LEU A 23 47.975 41.838 20.296 1.00 73.70 C ANISOU 158 CA LEU A 23 9597 9791 8611 -978 188 84 C ATOM 159 C LEU A 23 47.787 42.518 21.646 1.00 77.37 C ANISOU 159 C LEU A 23 10340 10118 8937 -1161 235 124 C ATOM 160 O LEU A 23 48.094 43.698 21.798 1.00 76.81 O ANISOU 160 O LEU A 23 10330 10068 8783 -1294 292 133 O ATOM 161 CB LEU A 23 46.623 41.452 19.680 1.00 76.51 C ANISOU 161 CB LEU A 23 9943 10049 9078 -863 330 63 C ATOM 162 CG LEU A 23 45.678 42.591 19.254 1.00 78.62 C ANISOU 162 CG LEU A 23 10258 10240 9372 -911 525 58 C ATOM 163 CD1 LEU A 23 46.193 43.337 18.047 1.00 76.30 C ANISOU 163 CD1 LEU A 23 9796 10096 9096 -914 523 47 C ATOM 164 CD2 LEU A 23 44.271 42.086 18.967 1.00 80.29 C ANISOU 164 CD2 LEU A 23 10484 10316 9706 -811 642 43 C ATOM 165 N ALA A 24 47.318 41.749 22.624 1.00 81.24 N ANISOU 165 N ALA A 24 11011 10466 9390 -1182 208 145 N ATOM 166 CA ALA A 24 47.213 42.203 24.018 1.00 86.52 C ANISOU 166 CA ALA A 24 11974 11000 9899 -1383 239 176 C ATOM 167 C ALA A 24 48.423 43.014 24.456 1.00 89.16 C ANISOU 167 C ALA A 24 12340 11422 10112 -1530 123 210 C ATOM 168 O ALA A 24 48.306 44.200 24.755 1.00 88.50 O ANISOU 168 O ALA A 24 12381 11303 9942 -1671 252 206 O ATOM 169 CB ALA A 24 47.048 41.007 24.942 1.00 86.74 C ANISOU 169 CB ALA A 24 12164 10914 9878 -1402 121 207 C ATOM 170 N GLN A 25 49.583 42.364 24.470 1.00 96.00 N ANISOU 170 N GLN A 25 13083 12400 10990 -1491 -126 239 N ATOM 171 CA GLN A 25 50.825 42.989 24.923 1.00102.31 C ANISOU 171 CA GLN A 25 13890 13291 11692 -1629 -276 276 C ATOM 172 C GLN A 25 51.087 44.313 24.222 1.00 99.78 C ANISOU 172 C GLN A 25 13471 13086 11353 -1688 -148 250 C ATOM 173 O GLN A 25 51.402 45.305 24.876 1.00102.06 O ANISOU 173 O GLN A 25 13924 13350 11503 -1876 -126 279 O ATOM 174 CB GLN A 25 52.023 42.051 24.723 1.00105.91 C ANISOU 174 CB GLN A 25 14126 13871 12241 -1525 -561 284 C ATOM 175 CG GLN A 25 53.373 42.753 24.873 1.00112.85 C ANISOU 175 CG GLN A 25 14915 14891 13069 -1641 -708 303 C ATOM 176 CD GLN A 25 54.546 41.797 24.982 1.00116.50 C ANISOU 176 CD GLN A 25 15191 15432 13641 -1559 -1019 310 C ATOM 177 OE1 GLN A 25 55.651 42.197 25.358 1.00111.72 O ANISOU 177 OE1 GLN A 25 14537 14910 13002 -1667 -1187 338 O ATOM 178 NE2 GLN A 25 54.317 40.529 24.646 1.00118.79 N ANISOU 178 NE2 GLN A 25 15367 15688 14077 -1364 -1107 281 N ATOM 179 N ALA A 26 50.967 44.324 22.899 1.00 94.65 N ANISOU 179 N ALA A 26 12575 12554 10831 -1544 -74 199 N ATOM 180 CA ALA A 26 51.198 45.546 22.136 1.00 95.75 C ANISOU 180 CA ALA A 26 12633 12798 10947 -1611 30 180 C ATOM 181 C ALA A 26 50.094 46.576 22.369 1.00 92.93 C ANISOU 181 C ALA A 26 12491 12279 10539 -1700 249 182 C ATOM 182 O ALA A 26 50.355 47.761 22.364 1.00 92.21 O ANISOU 182 O ALA A 26 12464 12206 10366 -1835 303 191 O ATOM 183 CB ALA A 26 51.322 45.231 20.655 1.00 96.17 C ANISOU 183 CB ALA A 26 12397 13009 11132 -1461 47 125 C ATOM 184 N ARG A 27 48.867 46.121 22.592 1.00 98.03 N ANISOU 184 N ARG A 27 13241 12760 11245 -1628 371 165 N ATOM 185 CA ARG A 27 47.731 47.022 22.763 1.00102.96 C ANISOU 185 CA ARG A 27 14028 13216 11875 -1684 589 141 C ATOM 186 C ARG A 27 47.537 47.456 24.224 1.00108.35 C ANISOU 186 C ARG A 27 15014 13740 12412 -1869 656 146 C ATOM 187 O ARG A 27 46.528 48.088 24.558 1.00108.73 O ANISOU 187 O ARG A 27 15211 13623 12478 -1918 856 102 O ATOM 188 CB ARG A 27 46.464 46.350 22.231 1.00107.57 C ANISOU 188 CB ARG A 27 14548 13703 12618 -1521 704 105 C ATOM 189 CG ARG A 27 45.364 47.324 21.841 1.00114.09 C ANISOU 189 CG ARG A 27 15414 14398 13536 -1518 901 68 C ATOM 190 CD ARG A 27 44.448 46.757 20.764 1.00112.88 C ANISOU 190 CD ARG A 27 15091 14229 13569 -1337 946 49 C ATOM 191 NE ARG A 27 45.157 46.451 19.514 1.00110.96 N ANISOU 191 NE ARG A 27 14621 14177 13360 -1247 818 69 N ATOM 192 CZ ARG A 27 45.578 47.351 18.627 1.00105.20 C ANISOU 192 CZ ARG A 27 13810 13538 12621 -1289 799 82 C ATOM 193 NH1 ARG A 27 45.387 48.649 18.833 1.00114.70 N ANISOU 193 NH1 ARG A 27 15137 14649 13792 -1406 877 86 N ATOM 194 NH2 ARG A 27 46.206 46.954 17.527 1.00102.42 N ANISOU 194 NH2 ARG A 27 13262 13365 12287 -1228 703 83 N ATOM 195 N GLN A 28 48.499 47.102 25.080 1.00108.82 N ANISOU 195 N GLN A 28 15163 13845 12338 -1977 484 194 N ATOM 196 CA GLN A 28 48.534 47.514 26.488 1.00112.85 C ANISOU 196 CA GLN A 28 15986 14223 12668 -2197 510 210 C ATOM 197 C GLN A 28 47.414 46.953 27.337 1.00113.45 C ANISOU 197 C GLN A 28 16276 14105 12723 -2232 650 175 C ATOM 198 O GLN A 28 47.092 47.514 28.377 1.00120.67 O ANISOU 198 O GLN A 28 17466 14880 13500 -2425 770 152 O ATOM 199 CB GLN A 28 48.536 49.046 26.618 1.00117.80 C ANISOU 199 CB GLN A 28 16734 14807 13216 -2347 646 190 C ATOM 200 CG GLN A 28 49.572 49.759 25.764 1.00118.35 C ANISOU 200 CG GLN A 28 16618 15063 13285 -2350 537 220 C ATOM 201 CD GLN A 28 50.995 49.426 26.171 1.00120.33 C ANISOU 201 CD GLN A 28 16828 15460 13430 -2437 282 285 C ATOM 202 OE1 GLN A 28 51.261 48.378 26.767 1.00121.22 O ANISOU 202 OE1 GLN A 28 16969 15560 13526 -2421 133 317 O ATOM 203 NE2 GLN A 28 51.922 50.321 25.850 1.00120.33 N ANISOU 203 NE2 GLN A 28 16761 15590 13368 -2536 217 307 N ATOM 204 N LEU A 29 46.834 45.838 26.918 1.00113.45 N ANISOU 204 N LEU A 29 16160 14097 12848 -2065 640 162 N ATOM 205 CA LEU A 29 45.776 45.199 27.692 1.00112.05 C ANISOU 205 CA LEU A 29 16176 13748 12648 -2110 769 126 C ATOM 206 C LEU A 29 46.386 44.136 28.586 1.00106.98 C ANISOU 206 C LEU A 29 15680 13091 11875 -2194 544 196 C ATOM 207 O LEU A 29 47.571 43.823 28.472 1.00103.34 O ANISOU 207 O LEU A 29 15117 12752 11393 -2170 282 265 O ATOM 208 CB LEU A 29 44.733 44.595 26.758 1.00111.94 C ANISOU 208 CB LEU A 29 15973 13718 12839 -1899 881 79 C ATOM 209 CG LEU A 29 44.207 45.610 25.738 1.00114.70 C ANISOU 209 CG LEU A 29 16158 14080 13340 -1803 1042 29 C ATOM 210 CD1 LEU A 29 43.601 44.907 24.533 1.00114.37 C ANISOU 210 CD1 LEU A 29 15870 14085 13501 -1576 1044 17 C ATOM 211 CD2 LEU A 29 43.215 46.559 26.401 1.00115.18 C ANISOU 211 CD2 LEU A 29 16409 13957 13396 -1929 1311 -55 C ATOM 212 N ASP A 30 45.573 43.605 29.491 1.00111.02 N ANISOU 212 N ASP A 30 16434 13444 12303 -2307 643 174 N ATOM 213 CA ASP A 30 45.991 42.502 30.364 1.00114.90 C ANISOU 213 CA ASP A 30 17106 13885 12665 -2403 419 248 C ATOM 214 C ASP A 30 45.907 41.172 29.611 1.00115.26 C ANISOU 214 C ASP A 30 16942 13982 12870 -2171 269 270 C ATOM 215 O ASP A 30 44.967 40.957 28.836 1.00115.24 O ANISOU 215 O ASP A 30 16788 13975 13024 -2013 439 209 O ATOM 216 CB ASP A 30 45.148 42.460 31.656 1.00118.25 C ANISOU 216 CB ASP A 30 17909 14115 12904 -2658 593 210 C ATOM 217 CG ASP A 30 43.639 42.447 31.397 1.00116.40 C ANISOU 217 CG ASP A 30 17651 13787 12787 -2600 924 93 C ATOM 218 OD1 ASP A 30 43.190 43.004 30.365 1.00115.58 O ANISOU 218 OD1 ASP A 30 17292 13738 12883 -2416 1072 34 O ATOM 219 OD2 ASP A 30 42.902 41.894 32.243 1.00105.33 O ANISOU 219 OD2 ASP A 30 16493 12251 11277 -2755 1031 61 O ATOM 220 N ILE A 31 46.882 40.287 29.838 1.00116.28 N ANISOU 220 N ILE A 31 17060 14148 12971 -2150 -58 356 N ATOM 221 CA ILE A 31 46.952 38.998 29.120 1.00115.77 C ANISOU 221 CA ILE A 31 16790 14128 13067 -1921 -232 372 C ATOM 222 C ILE A 31 45.840 38.047 29.575 1.00115.37 C ANISOU 222 C ILE A 31 16929 13922 12984 -1957 -149 361 C ATOM 223 O ILE A 31 45.458 37.134 28.837 1.00121.28 O ANISOU 223 O ILE A 31 17511 14688 13881 -1761 -180 346 O ATOM 224 CB ILE A 31 48.325 38.281 29.282 1.00119.40 C ANISOU 224 CB ILE A 31 17177 14647 13540 -1880 -628 455 C ATOM 225 CG1 ILE A 31 49.499 39.188 28.867 1.00122.00 C ANISOU 225 CG1 ILE A 31 17306 15145 13903 -1866 -716 460 C ATOM 226 CG2 ILE A 31 48.362 36.974 28.482 1.00117.92 C ANISOU 226 CG2 ILE A 31 16766 14493 13543 -1627 -787 449 C ATOM 227 CD1 ILE A 31 49.612 39.468 27.378 1.00121.14 C ANISOU 227 CD1 ILE A 31 16818 15215 13991 -1636 -617 389 C ATOM 228 N SER A 32 45.312 38.266 30.779 1.00110.45 N ANISOU 228 N SER A 32 16660 13148 12157 -2224 -32 361 N ATOM 229 CA SER A 32 44.231 37.429 31.297 1.00109.21 C ANISOU 229 CA SER A 32 16709 12844 11940 -2308 74 340 C ATOM 230 C SER A 32 42.903 37.719 30.597 1.00100.04 C ANISOU 230 C SER A 32 15407 11676 10927 -2199 425 226 C ATOM 231 O SER A 32 41.945 36.958 30.748 1.00 99.74 O ANISOU 231 O SER A 32 15454 11546 10896 -2217 527 196 O ATOM 232 CB SER A 32 44.075 37.609 32.812 1.00108.33 C ANISOU 232 CB SER A 32 17036 12577 11546 -2664 115 358 C ATOM 233 OG SER A 32 43.205 38.684 33.102 1.00107.34 O ANISOU 233 OG SER A 32 17011 12402 11370 -2803 496 246 O ATOM 234 N ARG A 33 42.852 38.817 29.846 1.00 95.66 N ANISOU 234 N ARG A 33 14642 11210 10492 -2099 593 168 N ATOM 235 CA ARG A 33 41.656 39.192 29.092 1.00 96.95 C ANISOU 235 CA ARG A 33 14641 11360 10832 -1980 887 69 C ATOM 236 C ARG A 33 41.289 38.173 28.020 1.00 87.94 C ANISOU 236 C ARG A 33 13255 10273 9882 -1731 814 76 C ATOM 237 O ARG A 33 40.203 37.587 28.046 1.00 78.70 O ANISOU 237 O ARG A 33 12121 9018 8763 -1725 955 31 O ATOM 238 CB ARG A 33 41.823 40.571 28.435 1.00104.29 C ANISOU 238 CB ARG A 33 15401 12367 11857 -1919 1013 27 C ATOM 239 CG ARG A 33 40.515 41.325 28.311 1.00111.41 C ANISOU 239 CG ARG A 33 16286 13171 12873 -1930 1354 -89 C ATOM 240 CD ARG A 33 40.062 41.815 29.686 1.00122.47 C ANISOU 240 CD ARG A 33 18015 14422 14095 -2213 1559 -158 C ATOM 241 NE ARG A 33 38.606 41.825 29.826 1.00125.23 N ANISOU 241 NE ARG A 33 18381 14646 14554 -2238 1869 -284 N ATOM 242 CZ ARG A 33 37.846 40.769 30.122 1.00125.81 C ANISOU 242 CZ ARG A 33 18527 14653 14619 -2271 1920 -306 C ATOM 243 NH1 ARG A 33 36.533 40.928 30.214 1.00128.66 N ANISOU 243 NH1 ARG A 33 18869 14910 15104 -2298 2225 -439 N ATOM 244 NH2 ARG A 33 38.368 39.559 30.318 1.00128.48 N ANISOU 244 NH2 ARG A 33 18950 15023 14844 -2277 1668 -203 N ATOM 245 N PHE A 34 42.201 37.950 27.085 1.00 73.48 N ANISOU 245 N PHE A 34 9984 8987 8946 -302 -355 -10 N ATOM 246 CA PHE A 34 41.900 37.050 25.986 1.00 80.07 C ANISOU 246 CA PHE A 34 10718 9864 9838 -266 -326 -17 C ATOM 247 C PHE A 34 41.792 35.609 26.483 1.00 81.06 C ANISOU 247 C PHE A 34 10817 9997 9984 -257 -335 -11 C ATOM 248 O PHE A 34 40.957 34.847 25.978 1.00 65.72 O ANISOU 248 O PHE A 34 8828 8071 8068 -219 -297 -21 O ATOM 249 CB PHE A 34 42.875 37.255 24.805 1.00 75.82 C ANISOU 249 CB PHE A 34 10101 9363 9344 -275 -353 -9 C ATOM 250 CG PHE A 34 42.809 38.647 24.227 1.00 75.18 C ANISOU 250 CG PHE A 34 10043 9276 9244 -282 -340 -14 C ATOM 251 CD1 PHE A 34 41.582 39.287 24.057 1.00 80.93 C ANISOU 251 CD1 PHE A 34 10811 9988 9949 -252 -283 -36 C ATOM 252 CD2 PHE A 34 43.956 39.337 23.896 1.00 79.38 C ANISOU 252 CD2 PHE A 34 10559 9817 9783 -321 -388 6 C ATOM 253 CE1 PHE A 34 41.506 40.577 23.556 1.00 79.71 C ANISOU 253 CE1 PHE A 34 10683 9824 9778 -259 -275 -40 C ATOM 254 CE2 PHE A 34 43.892 40.633 23.396 1.00 80.54 C ANISOU 254 CE2 PHE A 34 10732 9955 9913 -333 -383 6 C ATOM 255 CZ PHE A 34 42.665 41.252 23.224 1.00 82.09 C ANISOU 255 CZ PHE A 34 10972 10132 10086 -301 -328 -19 C ATOM 256 N ASP A 35 42.592 35.278 27.505 1.00 87.21 N ANISOU 256 N ASP A 35 11630 10757 10748 -293 -388 6 N ATOM 257 CA ASP A 35 42.496 33.994 28.232 1.00 89.46 C ANISOU 257 CA ASP A 35 11909 11038 11043 -292 -404 16 C ATOM 258 C ASP A 35 41.095 33.782 28.817 1.00 81.45 C ANISOU 258 C ASP A 35 10941 10010 9996 -267 -349 9 C ATOM 259 O ASP A 35 40.457 32.748 28.584 1.00 72.87 O ANISOU 259 O ASP A 35 9809 8938 8939 -242 -329 9 O ATOM 260 CB ASP A 35 43.533 33.937 29.372 1.00 98.37 C ANISOU 260 CB ASP A 35 13087 12141 12148 -341 -471 39 C ATOM 261 CG ASP A 35 44.976 33.826 28.866 1.00107.22 C ANISOU 261 CG ASP A 35 14144 13282 13310 -366 -532 56 C ATOM 262 OD1 ASP A 35 45.221 33.109 27.864 1.00 98.70 O ANISOU 262 OD1 ASP A 35 12973 12241 12287 -338 -530 53 O ATOM 263 OD2 ASP A 35 45.870 34.454 29.487 1.00119.92 O ANISOU 263 OD2 ASP A 35 15797 14870 14895 -412 -583 75 O ATOM 264 N ASN A 36 40.621 34.773 29.567 1.00 77.11 N ANISOU 264 N ASN A 36 10481 9432 9384 -274 -325 4 N ATOM 265 CA ASN A 36 39.285 34.733 30.152 1.00 76.92 C ANISOU 265 CA ASN A 36 10503 9400 9322 -246 -266 0 C ATOM 266 C ASN A 36 38.155 34.576 29.119 1.00 74.28 C ANISOU 266 C ASN A 36 10108 9092 9019 -199 -202 -11 C ATOM 267 O ASN A 36 37.082 34.075 29.432 1.00 71.00 O ANISOU 267 O ASN A 36 9696 8685 8596 -176 -159 -5 O ATOM 268 CB ASN A 36 39.074 36.000 30.968 1.00 85.65 C ANISOU 268 CB ASN A 36 11717 10472 10353 -253 -252 -7 C ATOM 269 CG ASN A 36 37.683 36.097 31.537 1.00 94.02 C ANISOU 269 CG ASN A 36 12823 11529 11368 -216 -182 -11 C ATOM 270 OD1 ASN A 36 36.826 36.789 30.988 1.00102.42 O ANISOU 270 OD1 ASN A 36 13889 12600 12426 -180 -127 -27 O ATOM 271 ND2 ASN A 36 37.443 35.391 32.634 1.00 99.98 N ANISOU 271 ND2 ASN A 36 13615 12279 12093 -224 -184 5 N ATOM 272 N LEU A 37 38.397 35.018 27.890 1.00 70.83 N ANISOU 272 N LEU A 37 9618 8674 8619 -188 -199 -25 N ATOM 273 CA LEU A 37 37.391 34.975 26.832 1.00 69.36 C ANISOU 273 CA LEU A 37 9378 8511 8464 -146 -145 -36 C ATOM 274 C LEU A 37 37.566 33.772 25.927 1.00 62.46 C ANISOU 274 C LEU A 37 8409 7665 7655 -134 -162 -34 C ATOM 275 O LEU A 37 36.728 33.514 25.058 1.00 58.60 O ANISOU 275 O LEU A 37 7872 7195 7197 -102 -125 -41 O ATOM 276 CB LEU A 37 37.477 36.252 26.008 1.00 67.01 C ANISOU 276 CB LEU A 37 9085 8214 8162 -140 -129 -53 C ATOM 277 CG LEU A 37 37.255 37.509 26.867 1.00 71.08 C ANISOU 277 CG LEU A 37 9703 8694 8609 -147 -115 -59 C ATOM 278 CD1 LEU A 37 37.683 38.781 26.139 1.00 68.37 C ANISOU 278 CD1 LEU A 37 9370 8343 8262 -155 -124 -70 C ATOM 279 CD2 LEU A 37 35.806 37.602 27.316 1.00 68.61 C ANISOU 279 CD2 LEU A 37 9425 8377 8264 -108 -47 -62 C ATOM 280 N MET A 38 38.675 33.068 26.136 1.00 57.96 N ANISOU 280 N MET A 38 7817 7097 7107 -159 -221 -24 N ATOM 281 CA MET A 38 39.013 31.835 25.450 1.00 59.17 C ANISOU 281 CA MET A 38 7892 7272 7318 -146 -249 -23 C ATOM 282 C MET A 38 39.394 32.085 24.004 1.00 60.73 C ANISOU 282 C MET A 38 8022 7498 7554 -125 -246 -39 C ATOM 283 O MET A 38 39.136 31.253 23.165 1.00 60.51 O ANISOU 283 O MET A 38 7933 7488 7568 -96 -244 -46 O ATOM 284 CB MET A 38 37.891 30.771 25.558 1.00 62.01 C ANISOU 284 CB MET A 38 8234 7631 7694 -123 -226 -16 C ATOM 285 CG MET A 38 37.394 30.525 26.980 1.00 62.45 C ANISOU 285 CG MET A 38 8354 7665 7708 -142 -221 3 C ATOM 286 SD MET A 38 36.043 29.318 27.129 1.00 75.12 S ANISOU 286 SD MET A 38 9933 9274 9332 -123 -195 23 S ATOM 287 CE MET A 38 36.740 27.963 26.193 1.00 75.35 C ANISOU 287 CE MET A 38 9881 9312 9434 -113 -254 18 C ATOM 288 N MET A 39 40.034 33.218 23.727 1.00 62.56 N ANISOU 288 N MET A 39 8266 7732 7769 -141 -251 -42 N ATOM 289 CA MET A 39 40.568 33.499 22.403 1.00 66.79 C ANISOU 289 CA MET A 39 8737 8301 8337 -127 -253 -51 C ATOM 290 C MET A 39 42.093 33.256 22.374 1.00 64.34 C ANISOU 290 C MET A 39 8391 8008 8045 -150 -312 -37 C ATOM 291 O MET A 39 42.803 33.781 23.199 1.00 67.57 O ANISOU 291 O MET A 39 8844 8399 8427 -190 -345 -21 O ATOM 292 CB MET A 39 40.303 34.964 22.026 1.00 68.93 C ANISOU 292 CB MET A 39 9039 8568 8580 -133 -222 -58 C ATOM 293 CG MET A 39 38.879 35.464 22.161 1.00 69.76 C ANISOU 293 CG MET A 39 9188 8655 8661 -111 -164 -69 C ATOM 294 SD MET A 39 38.828 37.247 21.818 1.00 76.42 S ANISOU 294 SD MET A 39 10076 9487 9470 -121 -144 -76 S ATOM 295 CE MET A 39 37.417 37.748 22.778 1.00 79.37 C ANISOU 295 CE MET A 39 10534 9825 9795 -103 -91 -83 C ATOM 296 N LYS A 40 42.585 32.480 21.416 1.00 67.07 N ANISOU 296 N LYS A 40 8659 8387 8435 -124 -325 -42 N ATOM 297 CA LYS A 40 44.007 32.187 21.304 1.00 64.55 C ANISOU 297 CA LYS A 40 8295 8093 8138 -137 -376 -27 C ATOM 298 C LYS A 40 44.576 32.833 20.053 1.00 65.88 C ANISOU 298 C LYS A 40 8406 8305 8321 -126 -367 -27 C ATOM 299 O LYS A 40 45.541 33.609 20.137 1.00 61.06 O ANISOU 299 O LYS A 40 7793 7706 7701 -160 -394 -6 O ATOM 300 CB LYS A 40 44.259 30.684 21.225 1.00 68.81 C ANISOU 300 CB LYS A 40 8788 8641 8715 -108 -404 -30 C ATOM 301 CG LYS A 40 43.673 29.853 22.347 1.00 80.20 C ANISOU 301 CG LYS A 40 10276 10044 10149 -116 -416 -27 C ATOM 302 CD LYS A 40 43.975 28.362 22.127 1.00 94.40 C ANISOU 302 CD LYS A 40 12026 11850 11991 -85 -451 -31 C ATOM 303 CE LYS A 40 44.281 27.622 23.436 1.00100.35 C ANISOU 303 CE LYS A 40 12816 12572 12739 -114 -498 -12 C ATOM 304 NZ LYS A 40 44.677 26.183 23.295 1.00 98.04 N ANISOU 304 NZ LYS A 40 12480 12281 12488 -86 -541 -14 N ATOM 305 N GLU A 41 44.000 32.483 18.891 1.00 60.33 N ANISOU 305 N GLU A 41 7655 7626 7641 -80 -333 -49 N ATOM 306 CA GLU A 41 44.473 32.980 17.599 1.00 61.91 C ANISOU 306 CA GLU A 41 7795 7872 7853 -64 -319 -51 C ATOM 307 C GLU A 41 43.334 33.388 16.683 1.00 59.16 C ANISOU 307 C GLU A 41 7446 7526 7503 -36 -267 -73 C ATOM 308 O GLU A 41 42.192 32.938 16.829 1.00 55.74 O ANISOU 308 O GLU A 41 7038 7067 7071 -16 -242 -89 O ATOM 309 CB GLU A 41 45.271 31.924 16.873 1.00 65.65 C ANISOU 309 CB GLU A 41 8192 8387 8363 -25 -341 -54 C ATOM 310 CG GLU A 41 46.477 31.424 17.640 1.00 71.10 C ANISOU 310 CG GLU A 41 8869 9082 9063 -45 -395 -30 C ATOM 311 CD GLU A 41 46.767 29.979 17.340 1.00 76.87 C ANISOU 311 CD GLU A 41 9552 9827 9829 2 -416 -43 C ATOM 312 OE1 GLU A 41 45.842 29.248 16.927 1.00 85.25 O ANISOU 312 OE1 GLU A 41 10614 10874 10902 41 -396 -70 O ATOM 313 OE2 GLU A 41 47.920 29.568 17.525 1.00 85.00 O ANISOU 313 OE2 GLU A 41 10543 10878 10873 1 -456 -24 O ATOM 314 N LYS A 42 43.650 34.258 15.736 1.00 53.90 N ANISOU 314 N LYS A 42 6750 6893 6835 -37 -252 -69 N ATOM 315 CA LYS A 42 42.700 34.533 14.669 1.00 55.24 C ANISOU 315 CA LYS A 42 6907 7073 7008 -7 -207 -89 C ATOM 316 C LYS A 42 43.347 34.369 13.315 1.00 53.88 C ANISOU 316 C LYS A 42 6658 6957 6855 23 -204 -92 C ATOM 317 O LYS A 42 44.497 34.798 13.109 1.00 52.77 O ANISOU 317 O LYS A 42 6482 6852 6712 3 -225 -68 O ATOM 318 CB LYS A 42 42.071 35.911 14.810 1.00 53.50 C ANISOU 318 CB LYS A 42 6739 6828 6758 -34 -180 -86 C ATOM 319 CG LYS A 42 43.011 37.088 14.646 1.00 54.92 C ANISOU 319 CG LYS A 42 6917 7026 6922 -74 -199 -61 C ATOM 320 CD LYS A 42 42.179 38.327 14.413 1.00 56.61 C ANISOU 320 CD LYS A 42 7176 7219 7114 -85 -167 -66 C ATOM 321 CE LYS A 42 43.032 39.571 14.376 1.00 58.98 C ANISOU 321 CE LYS A 42 7486 7525 7395 -132 -193 -39 C ATOM 322 NZ LYS A 42 42.138 40.727 14.084 1.00 60.70 N ANISOU 322 NZ LYS A 42 7750 7719 7594 -136 -163 -47 N ATOM 323 N ALA A 43 42.592 33.775 12.388 1.00 50.38 N ANISOU 323 N ALA A 43 6190 6523 6429 69 -178 -117 N ATOM 324 CA ALA A 43 43.000 33.765 10.985 1.00 48.70 C ANISOU 324 CA ALA A 43 5914 6363 6225 102 -166 -123 C ATOM 325 C ALA A 43 42.935 35.166 10.454 1.00 50.45 C ANISOU 325 C ALA A 43 6141 6600 6428 75 -143 -110 C ATOM 326 O ALA A 43 41.996 35.927 10.774 1.00 51.18 O ANISOU 326 O ALA A 43 6285 6654 6505 55 -121 -113 O ATOM 327 CB ALA A 43 42.106 32.863 10.149 1.00 47.04 C ANISOU 327 CB ALA A 43 5689 6150 6032 155 -148 -154 C ATOM 328 N VAL A 44 43.913 35.489 9.611 1.00 50.07 N ANISOU 328 N VAL A 44 6036 6608 6378 78 -147 -95 N ATOM 329 CA VAL A 44 43.970 36.778 8.949 1.00 52.35 C ANISOU 329 CA VAL A 44 6320 6918 6651 52 -130 -78 C ATOM 330 C VAL A 44 44.129 36.596 7.431 1.00 50.17 C ANISOU 330 C VAL A 44 5980 6701 6380 94 -107 -86 C ATOM 331 O VAL A 44 44.990 35.855 6.968 1.00 52.51 O ANISOU 331 O VAL A 44 6219 7045 6686 126 -117 -84 O ATOM 332 CB VAL A 44 45.149 37.597 9.475 1.00 53.43 C ANISOU 332 CB VAL A 44 6452 7072 6776 -1 -162 -36 C ATOM 333 CG1 VAL A 44 45.109 38.998 8.896 1.00 57.07 C ANISOU 333 CG1 VAL A 44 6919 7544 7220 -36 -151 -16 C ATOM 334 CG2 VAL A 44 45.109 37.635 10.976 1.00 55.07 C ANISOU 334 CG2 VAL A 44 6723 7223 6976 -39 -190 -30 C ATOM 335 N SER A 45 43.282 37.291 6.697 1.00 51.06 N ANISOU 335 N SER A 45 6106 6807 6484 95 -77 -95 N ATOM 336 CA SER A 45 43.237 37.291 5.254 1.00 51.09 C ANISOU 336 CA SER A 45 6063 6860 6486 130 -53 -103 C ATOM 337 C SER A 45 44.327 38.179 4.657 1.00 51.32 C ANISOU 337 C SER A 45 6046 6951 6503 103 -57 -65 C ATOM 338 O SER A 45 44.549 39.308 5.100 1.00 52.71 O ANISOU 338 O SER A 45 6246 7113 6666 47 -68 -36 O ATOM 339 CB SER A 45 41.877 37.840 4.809 1.00 51.62 C ANISOU 339 CB SER A 45 6169 6892 6551 132 -23 -121 C ATOM 340 OG SER A 45 41.666 37.596 3.423 1.00 60.97 O ANISOU 340 OG SER A 45 7314 8114 7734 173 -2 -136 O ATOM 341 N LEU A 46 44.998 37.682 3.627 1.00 50.51 N ANISOU 341 N LEU A 46 5876 6914 6399 144 -48 -64 N ATOM 342 CA LEU A 46 45.955 38.515 2.892 1.00 49.61 C ANISOU 342 CA LEU A 46 5709 6869 6270 122 -46 -23 C ATOM 343 C LEU A 46 45.209 39.405 1.897 1.00 47.56 C ANISOU 343 C LEU A 46 5459 6613 5996 114 -18 -26 C ATOM 344 O LEU A 46 44.078 39.121 1.548 1.00 43.27 O ANISOU 344 O LEU A 46 4947 6035 5456 143 2 -62 O ATOM 345 CB LEU A 46 46.974 37.644 2.178 1.00 50.40 C ANISOU 345 CB LEU A 46 5731 7045 6370 174 -43 -19 C ATOM 346 CG LEU A 46 48.105 37.050 3.031 1.00 54.93 C ANISOU 346 CG LEU A 46 6276 7637 6957 171 -75 1 C ATOM 347 CD1 LEU A 46 49.108 38.133 3.415 1.00 58.19 C ANISOU 347 CD1 LEU A 46 6665 8080 7364 101 -99 63 C ATOM 348 CD2 LEU A 46 47.626 36.352 4.279 1.00 53.11 C ANISOU 348 CD2 LEU A 46 6102 7333 6744 168 -99 -23 C ATOM 349 N PRO A 47 45.858 40.459 1.382 1.00 48.67 N ANISOU 349 N PRO A 47 5569 6800 6122 75 -19 16 N ATOM 350 CA PRO A 47 45.186 41.286 0.356 1.00 47.47 C ANISOU 350 CA PRO A 47 5423 6655 5956 69 5 16 C ATOM 351 C PRO A 47 44.863 40.548 -0.932 1.00 46.89 C ANISOU 351 C PRO A 47 5314 6623 5877 136 36 -13 C ATOM 352 O PRO A 47 43.939 40.939 -1.656 1.00 46.10 O ANISOU 352 O PRO A 47 5236 6508 5771 142 57 -29 O ATOM 353 CB PRO A 47 46.208 42.397 0.073 1.00 50.21 C ANISOU 353 CB PRO A 47 5732 7055 6289 14 -9 76 C ATOM 354 CG PRO A 47 46.989 42.501 1.348 1.00 51.75 C ANISOU 354 CG PRO A 47 5938 7230 6493 -29 -49 105 C ATOM 355 CD PRO A 47 47.134 41.056 1.812 1.00 51.63 C ANISOU 355 CD PRO A 47 5909 7212 6493 24 -49 72 C ATOM 356 N TYR A 48 45.618 39.490 -1.233 1.00 43.80 N ANISOU 356 N TYR A 48 4871 6284 5485 188 39 -21 N ATOM 357 CA TYR A 48 45.331 38.702 -2.438 1.00 44.26 C ANISOU 357 CA TYR A 48 4903 6378 5533 259 65 -54 C ATOM 358 C TYR A 48 44.400 37.536 -2.099 1.00 44.04 C ANISOU 358 C TYR A 48 4920 6288 5524 305 61 -108 C ATOM 359 O TYR A 48 44.453 36.493 -2.750 1.00 43.94 O ANISOU 359 O TYR A 48 4887 6298 5507 372 67 -139 O ATOM 360 CB TYR A 48 46.624 38.205 -3.134 1.00 43.45 C ANISOU 360 CB TYR A 48 4721 6372 5414 301 74 -35 C ATOM 361 CG TYR A 48 47.649 37.654 -2.169 1.00 43.40 C ANISOU 361 CG TYR A 48 4687 6378 5423 300 48 -17 C ATOM 362 CD1 TYR A 48 47.530 36.370 -1.673 1.00 42.57 C ANISOU 362 CD1 TYR A 48 4597 6241 5335 351 35 -57 C ATOM 363 CD2 TYR A 48 48.720 38.438 -1.730 1.00 44.94 C ANISOU 363 CD2 TYR A 48 4843 6613 5617 243 31 42 C ATOM 364 CE1 TYR A 48 48.449 35.856 -0.793 1.00 44.60 C ANISOU 364 CE1 TYR A 48 4830 6507 5607 350 9 -41 C ATOM 365 CE2 TYR A 48 49.676 37.933 -0.841 1.00 45.35 C ANISOU 365 CE2 TYR A 48 4869 6676 5685 240 4 61 C ATOM 366 CZ TYR A 48 49.534 36.638 -0.386 1.00 47.65 C ANISOU 366 CZ TYR A 48 5175 6937 5993 295 -4 18 C ATOM 367 OH TYR A 48 50.404 36.124 0.529 1.00 50.61 O ANISOU 367 OH TYR A 48 5527 7315 6385 292 -34 36 O ATOM 368 N GLU A 49 43.539 37.720 -1.097 1.00 43.18 N ANISOU 368 N GLU A 49 4872 6100 5433 272 49 -118 N ATOM 369 CA GLU A 49 42.519 36.729 -0.765 1.00 42.47 C ANISOU 369 CA GLU A 49 4825 5950 5363 306 44 -162 C ATOM 370 C GLU A 49 41.231 37.466 -0.521 1.00 43.47 C ANISOU 370 C GLU A 49 5006 6013 5495 272 54 -167 C ATOM 371 O GLU A 49 41.253 38.616 -0.106 1.00 42.22 O ANISOU 371 O GLU A 49 4866 5843 5331 218 55 -139 O ATOM 372 CB GLU A 49 42.895 35.970 0.482 1.00 46.29 C ANISOU 372 CB GLU A 49 5320 6403 5863 304 17 -165 C ATOM 373 CG GLU A 49 44.093 35.047 0.312 1.00 47.70 C ANISOU 373 CG GLU A 49 5445 6636 6040 348 5 -164 C ATOM 374 CD GLU A 49 44.294 34.211 1.562 1.00 50.84 C ANISOU 374 CD GLU A 49 5863 6993 6460 347 -25 -171 C ATOM 375 OE1 GLU A 49 44.735 34.781 2.597 1.00 52.07 O ANISOU 375 OE1 GLU A 49 6029 7134 6618 293 -42 -141 O ATOM 376 OE2 GLU A 49 43.966 32.996 1.523 1.00 50.77 O ANISOU 376 OE2 GLU A 49 5863 6962 6463 397 -37 -205 O ATOM 377 N ASP A 50 40.114 36.829 -0.815 1.00 42.72 N ANISOU 377 N ASP A 50 4939 5880 5413 304 59 -199 N ATOM 378 CA ASP A 50 38.807 37.441 -0.564 1.00 43.36 C ANISOU 378 CA ASP A 50 5069 5902 5504 279 71 -202 C ATOM 379 C ASP A 50 37.810 36.296 -0.277 1.00 42.80 C ANISOU 379 C ASP A 50 5025 5780 5455 311 62 -232 C ATOM 380 O ASP A 50 38.226 35.133 -0.181 1.00 42.63 O ANISOU 380 O ASP A 50 4990 5766 5441 347 43 -249 O ATOM 381 CB ASP A 50 38.422 38.346 -1.764 1.00 43.18 C ANISOU 381 CB ASP A 50 5036 5902 5465 273 92 -196 C ATOM 382 CG ASP A 50 37.970 37.572 -2.990 1.00 43.91 C ANISOU 382 CG ASP A 50 5114 6011 5556 326 98 -223 C ATOM 383 OD1 ASP A 50 37.870 36.315 -2.961 1.00 44.13 O ANISOU 383 OD1 ASP A 50 5143 6028 5596 370 83 -250 O ATOM 384 OD2 ASP A 50 37.732 38.223 -4.031 1.00 46.06 O ANISOU 384 OD2 ASP A 50 5378 6307 5815 325 113 -218 O ATOM 385 N PRO A 51 36.511 36.615 -0.136 1.00 42.11 N ANISOU 385 N PRO A 51 4975 5644 5380 299 73 -236 N ATOM 386 CA PRO A 51 35.591 35.559 0.234 1.00 41.18 C ANISOU 386 CA PRO A 51 4879 5480 5286 322 61 -254 C ATOM 387 C PRO A 51 35.443 34.470 -0.807 1.00 41.10 C ANISOU 387 C PRO A 51 4852 5482 5282 373 47 -280 C ATOM 388 O PRO A 51 35.174 33.345 -0.443 1.00 40.67 O ANISOU 388 O PRO A 51 4808 5398 5244 395 23 -294 O ATOM 389 CB PRO A 51 34.276 36.315 0.470 1.00 41.61 C ANISOU 389 CB PRO A 51 4968 5490 5351 298 81 -245 C ATOM 390 CG PRO A 51 34.721 37.633 0.985 1.00 43.82 C ANISOU 390 CG PRO A 51 5259 5775 5613 255 95 -223 C ATOM 391 CD PRO A 51 35.960 37.949 0.170 1.00 43.80 C ANISOU 391 CD PRO A 51 5217 5834 5590 256 92 -216 C ATOM 392 N VAL A 52 35.629 34.820 -2.087 1.00 40.52 N ANISOU 392 N VAL A 52 4756 5448 5190 391 58 -285 N ATOM 393 CA VAL A 52 35.588 33.877 -3.182 1.00 41.92 C ANISOU 393 CA VAL A 52 4923 5641 5363 444 44 -312 C ATOM 394 C VAL A 52 36.762 32.887 -3.072 1.00 41.01 C ANISOU 394 C VAL A 52 4784 5558 5240 482 24 -327 C ATOM 395 O VAL A 52 36.559 31.669 -3.112 1.00 40.89 O ANISOU 395 O VAL A 52 4781 5518 5237 522 -3 -351 O ATOM 396 CB VAL A 52 35.600 34.586 -4.573 1.00 43.61 C ANISOU 396 CB VAL A 52 5118 5897 5552 453 65 -311 C ATOM 397 CG1 VAL A 52 35.741 33.576 -5.690 1.00 43.62 C ANISOU 397 CG1 VAL A 52 5113 5920 5541 514 49 -342 C ATOM 398 CG2 VAL A 52 34.344 35.414 -4.801 1.00 45.29 C ANISOU 398 CG2 VAL A 52 5355 6073 5777 423 79 -300 C ATOM 399 N SER A 53 37.970 33.404 -2.901 1.00 39.22 N ANISOU 399 N SER A 53 4523 5381 4994 471 35 -309 N ATOM 400 CA SER A 53 39.139 32.539 -2.841 1.00 41.94 C ANISOU 400 CA SER A 53 4838 5763 5331 510 19 -318 C ATOM 401 C SER A 53 39.060 31.682 -1.587 1.00 42.68 C ANISOU 401 C SER A 53 4955 5808 5452 506 -9 -323 C ATOM 402 O SER A 53 39.371 30.489 -1.629 1.00 43.56 O ANISOU 402 O SER A 53 5064 5915 5569 553 -36 -347 O ATOM 403 CB SER A 53 40.440 33.353 -2.893 1.00 39.91 C ANISOU 403 CB SER A 53 4535 5576 5053 492 37 -288 C ATOM 404 OG SER A 53 40.666 34.045 -1.684 1.00 40.72 O ANISOU 404 OG SER A 53 4646 5659 5166 433 34 -259 O ATOM 405 N TYR A 54 38.591 32.269 -0.485 1.00 41.47 N ANISOU 405 N TYR A 54 4827 5614 5313 451 -6 -303 N ATOM 406 CA TYR A 54 38.369 31.474 0.727 1.00 39.76 C ANISOU 406 CA TYR A 54 4637 5348 5120 443 -33 -305 C ATOM 407 C TYR A 54 37.411 30.323 0.454 1.00 40.34 C ANISOU 407 C TYR A 54 4736 5377 5213 478 -57 -331 C ATOM 408 O TYR A 54 37.694 29.163 0.798 1.00 40.44 O ANISOU 408 O TYR A 54 4753 5373 5238 506 -91 -345 O ATOM 409 CB TYR A 54 37.904 32.363 1.899 1.00 40.85 C ANISOU 409 CB TYR A 54 4807 5451 5264 382 -21 -279 C ATOM 410 CG TYR A 54 38.992 32.801 2.854 1.00 40.29 C ANISOU 410 CG TYR A 54 4726 5397 5184 349 -27 -256 C ATOM 411 CD1 TYR A 54 39.968 33.706 2.470 1.00 43.26 C ANISOU 411 CD1 TYR A 54 5069 5826 5539 332 -14 -236 C ATOM 412 CD2 TYR A 54 39.046 32.315 4.149 1.00 44.28 C ANISOU 412 CD2 TYR A 54 5255 5866 5701 330 -48 -250 C ATOM 413 CE1 TYR A 54 40.990 34.089 3.323 1.00 44.20 C ANISOU 413 CE1 TYR A 54 5179 5960 5652 299 -27 -211 C ATOM 414 CE2 TYR A 54 40.056 32.704 5.024 1.00 44.45 C ANISOU 414 CE2 TYR A 54 5272 5901 5715 298 -59 -228 C ATOM 415 CZ TYR A 54 41.013 33.600 4.611 1.00 44.74 C ANISOU 415 CZ TYR A 54 5277 5989 5734 281 -50 -208 C ATOM 416 OH TYR A 54 41.985 33.980 5.499 1.00 45.49 O ANISOU 416 OH TYR A 54 5368 6093 5823 244 -67 -181 O ATOM 417 N ALA A 55 36.283 30.625 -0.187 1.00 39.82 N ANISOU 417 N ALA A 55 4688 5290 5152 474 -45 -334 N ATOM 418 CA ALA A 55 35.254 29.606 -0.424 1.00 39.25 C ANISOU 418 CA ALA A 55 4641 5169 5101 498 -73 -351 C ATOM 419 C ALA A 55 35.701 28.486 -1.319 1.00 41.71 C ANISOU 419 C ALA A 55 4946 5493 5406 560 -104 -384 C ATOM 420 O ALA A 55 35.321 27.320 -1.113 1.00 41.70 O ANISOU 420 O ALA A 55 4968 5451 5425 582 -145 -398 O ATOM 421 CB ALA A 55 34.023 30.254 -1.037 1.00 40.65 C ANISOU 421 CB ALA A 55 4833 5327 5284 481 -54 -344 C ATOM 422 N VAL A 56 36.426 28.845 -2.384 1.00 43.07 N ANISOU 422 N VAL A 56 5092 5723 5550 591 -85 -395 N ATOM 423 CA VAL A 56 36.900 27.847 -3.344 1.00 44.83 C ANISOU 423 CA VAL A 56 5310 5964 5757 660 -109 -429 C ATOM 424 C VAL A 56 37.911 26.919 -2.677 1.00 42.58 C ANISOU 424 C VAL A 56 5015 5685 5476 690 -137 -439 C ATOM 425 O VAL A 56 37.885 25.713 -2.902 1.00 42.01 O ANISOU 425 O VAL A 56 4962 5587 5410 739 -177 -467 O ATOM 426 CB VAL A 56 37.547 28.491 -4.599 1.00 46.11 C ANISOU 426 CB VAL A 56 5442 6197 5881 688 -77 -435 C ATOM 427 CG1 VAL A 56 38.284 27.444 -5.408 1.00 48.23 C ANISOU 427 CG1 VAL A 56 5703 6493 6126 768 -97 -470 C ATOM 428 CG2 VAL A 56 36.486 29.170 -5.465 1.00 48.48 C ANISOU 428 CG2 VAL A 56 5758 6485 6176 671 -60 -432 C ATOM 429 N ASN A 57 38.791 27.486 -1.863 1.00 43.08 N ANISOU 429 N ASN A 57 5049 5779 5537 660 -119 -414 N ATOM 430 CA ASN A 57 39.776 26.683 -1.133 1.00 45.37 C ANISOU 430 CA ASN A 57 5326 6075 5835 682 -145 -418 C ATOM 431 C ASN A 57 39.113 25.787 -0.106 1.00 46.19 C ANISOU 431 C ASN A 57 5470 6107 5972 666 -187 -420 C ATOM 432 O ASN A 57 39.561 24.671 0.118 1.00 47.45 O ANISOU 432 O ASN A 57 5634 6251 6141 705 -226 -437 O ATOM 433 CB ASN A 57 40.829 27.559 -0.446 1.00 43.70 C ANISOU 433 CB ASN A 57 5076 5910 5615 644 -121 -385 C ATOM 434 CG ASN A 57 41.764 28.209 -1.431 1.00 44.85 C ANISOU 434 CG ASN A 57 5173 6138 5729 667 -88 -378 C ATOM 435 OD1 ASN A 57 42.124 27.612 -2.420 1.00 48.43 O ANISOU 435 OD1 ASN A 57 5612 6624 6164 733 -90 -404 O ATOM 436 ND2 ASN A 57 42.151 29.434 -1.173 1.00 44.00 N ANISOU 436 ND2 ASN A 57 5042 6063 5612 614 -60 -342 N ATOM 437 N ALA A 58 38.028 26.234 0.498 1.00 42.42 N ANISOU 437 N ALA A 58 5020 5585 5512 611 -180 -400 N ATOM 438 CA ALA A 58 37.278 25.332 1.386 1.00 42.25 C ANISOU 438 CA ALA A 58 5034 5497 5521 597 -220 -398 C ATOM 439 C ALA A 58 36.649 24.188 0.600 1.00 45.51 C ANISOU 439 C ALA A 58 5473 5873 5944 643 -263 -426 C ATOM 440 O ALA A 58 36.587 23.048 1.078 1.00 45.28 O ANISOU 440 O ALA A 58 5466 5803 5936 658 -312 -434 O ATOM 441 CB ALA A 58 36.180 26.104 2.161 1.00 41.60 C ANISOU 441 CB ALA A 58 4972 5380 5451 532 -197 -367 C ATOM 442 N ALA A 59 36.156 24.489 -0.604 1.00 46.29 N ANISOU 442 N ALA A 59 5574 5984 6030 664 -248 -440 N ATOM 443 CA ALA A 59 35.367 23.509 -1.367 1.00 45.40 C ANISOU 443 CA ALA A 59 5495 5827 5926 699 -293 -464 C ATOM 444 C ALA A 59 36.169 22.581 -2.250 1.00 46.85 C ANISOU 444 C ALA A 59 5681 6027 6090 778 -324 -505 C ATOM 445 O ALA A 59 35.669 21.525 -2.599 1.00 43.42 O ANISOU 445 O ALA A 59 5284 5545 5667 809 -377 -527 O ATOM 446 CB ALA A 59 34.347 24.197 -2.230 1.00 45.62 C ANISOU 446 CB ALA A 59 5530 5851 5950 683 -271 -459 C ATOM 447 N LYS A 60 37.364 23.008 -2.642 1.00 45.85 N ANISOU 447 N LYS A 60 5516 5969 5932 810 -290 -515 N ATOM 448 CA LYS A 60 38.196 22.273 -3.593 1.00 50.75 C ANISOU 448 CA LYS A 60 6135 6621 6526 894 -306 -554 C ATOM 449 C LYS A 60 38.393 20.766 -3.255 1.00 50.61 C ANISOU 449 C LYS A 60 6149 6554 6525 941 -374 -580 C ATOM 450 O LYS A 60 38.271 19.913 -4.146 1.00 50.38 O ANISOU 450 O LYS A 60 6152 6505 6482 1005 -410 -617 O ATOM 451 CB LYS A 60 39.549 22.993 -3.751 1.00 52.18 C ANISOU 451 CB LYS A 60 6258 6890 6677 911 -257 -545 C ATOM 452 CG LYS A 60 40.549 22.366 -4.735 1.00 52.91 C ANISOU 452 CG LYS A 60 6335 7032 6734 1004 -260 -581 C ATOM 453 CD LYS A 60 39.948 22.248 -6.124 1.00 57.09 C ANISOU 453 CD LYS A 60 6894 7560 7235 1047 -262 -611 C ATOM 454 CE LYS A 60 40.991 22.217 -7.249 1.00 60.79 C ANISOU 454 CE LYS A 60 7333 8109 7654 1129 -233 -635 C ATOM 455 NZ LYS A 60 41.931 21.076 -7.051 1.00 66.58 N ANISOU 455 NZ LYS A 60 8065 8847 8384 1204 -265 -662 N ATOM 456 N PRO A 61 38.674 20.425 -1.985 1.00 50.00 N ANISOU 456 N PRO A 61 6069 6453 6476 911 -394 -561 N ATOM 457 CA PRO A 61 38.844 18.984 -1.634 1.00 50.07 C ANISOU 457 CA PRO A 61 6110 6410 6503 953 -464 -584 C ATOM 458 C PRO A 61 37.578 18.154 -1.800 1.00 53.74 C ANISOU 458 C PRO A 61 6633 6793 6991 946 -523 -592 C ATOM 459 O PRO A 61 37.648 16.959 -2.069 1.00 53.54 O ANISOU 459 O PRO A 61 6646 6727 6970 1000 -585 -623 O ATOM 460 CB PRO A 61 39.246 19.036 -0.166 1.00 51.48 C ANISOU 460 CB PRO A 61 6270 6580 6707 903 -466 -551 C ATOM 461 CG PRO A 61 39.814 20.413 0.029 1.00 49.42 C ANISOU 461 CG PRO A 61 5959 6388 6429 864 -397 -523 C ATOM 462 CD PRO A 61 38.961 21.287 -0.834 1.00 50.76 C ANISOU 462 CD PRO A 61 6133 6568 6584 844 -360 -521 C ATOM 463 N ILE A 62 36.408 18.791 -1.691 1.00 50.59 N ANISOU 463 N ILE A 62 6243 6370 6607 881 -507 -564 N ATOM 464 CA ILE A 62 35.171 18.060 -1.817 1.00 48.68 C ANISOU 464 CA ILE A 62 6049 6054 6391 866 -563 -561 C ATOM 465 C ILE A 62 35.038 17.672 -3.265 1.00 51.51 C ANISOU 465 C ILE A 62 6437 6409 6724 930 -586 -602 C ATOM 466 O ILE A 62 34.765 16.517 -3.602 1.00 56.01 O ANISOU 466 O ILE A 62 7055 6923 7301 968 -658 -626 O ATOM 467 CB ILE A 62 33.988 18.928 -1.380 1.00 52.77 C ANISOU 467 CB ILE A 62 6562 6558 6930 786 -532 -517 C ATOM 468 CG1 ILE A 62 34.066 19.159 0.138 1.00 53.11 C ANISOU 468 CG1 ILE A 62 6587 6596 6996 727 -518 -478 C ATOM 469 CG2 ILE A 62 32.676 18.301 -1.788 1.00 53.78 C ANISOU 469 CG2 ILE A 62 6732 6620 7082 773 -586 -510 C ATOM 470 CD1 ILE A 62 32.929 20.007 0.688 1.00 51.44 C ANISOU 470 CD1 ILE A 62 6370 6372 6802 654 -484 -434 C ATOM 471 N ILE A 63 35.271 18.652 -4.117 1.00 48.76 N ANISOU 471 N ILE A 63 6062 6121 6341 942 -526 -609 N ATOM 472 CA ILE A 63 35.140 18.484 -5.536 1.00 51.22 C ANISOU 472 CA ILE A 63 6399 6439 6621 999 -536 -645 C ATOM 473 C ILE A 63 36.237 17.536 -6.090 1.00 53.87 C ANISOU 473 C ILE A 63 6749 6791 6926 1096 -565 -694 C ATOM 474 O ILE A 63 35.941 16.719 -6.921 1.00 54.08 O ANISOU 474 O ILE A 63 6827 6779 6939 1149 -616 -729 O ATOM 475 CB ILE A 63 35.207 19.847 -6.262 1.00 51.17 C ANISOU 475 CB ILE A 63 6356 6502 6585 984 -461 -635 C ATOM 476 CG1 ILE A 63 34.124 20.824 -5.739 1.00 50.46 C ANISOU 476 CG1 ILE A 63 6253 6395 6524 896 -431 -588 C ATOM 477 CG2 ILE A 63 35.047 19.654 -7.756 1.00 54.66 C ANISOU 477 CG2 ILE A 63 6828 6951 6989 1043 -472 -672 C ATOM 478 CD1 ILE A 63 32.707 20.280 -5.640 1.00 48.32 C ANISOU 478 CD1 ILE A 63 6025 6045 6289 860 -485 -573 C ATOM 479 N ASP A 64 37.482 17.664 -5.639 1.00 55.51 N ANISOU 479 N ASP A 64 6914 7055 7123 1122 -533 -696 N ATOM 480 CA ASP A 64 38.563 16.749 -6.065 1.00 59.25 C ANISOU 480 CA ASP A 64 7395 7547 7569 1219 -558 -740 C ATOM 481 C ASP A 64 38.160 15.278 -5.917 1.00 59.99 C ANISOU 481 C ASP A 64 7556 7551 7684 1253 -652 -767 C ATOM 482 O ASP A 64 38.454 14.494 -6.770 1.00 65.65 O ANISOU 482 O ASP A 64 8311 8258 8373 1337 -687 -813 O ATOM 483 CB ASP A 64 39.844 16.984 -5.257 1.00 57.98 C ANISOU 483 CB ASP A 64 7174 7444 7409 1225 -523 -725 C ATOM 484 CG ASP A 64 40.557 18.287 -5.616 1.00 62.44 C ANISOU 484 CG ASP A 64 7672 8107 7942 1215 -437 -705 C ATOM 485 OD1 ASP A 64 40.306 18.863 -6.702 1.00 60.85 O ANISOU 485 OD1 ASP A 64 7471 7941 7708 1230 -404 -714 O ATOM 486 OD2 ASP A 64 41.396 18.740 -4.803 1.00 65.75 O ANISOU 486 OD2 ASP A 64 8040 8570 8370 1190 -407 -677 O ATOM 487 N ARG A 65 37.461 14.925 -4.848 1.00 66.94 N ANISOU 487 N ARG A 65 8454 8366 8614 1186 -694 -736 N ATOM 488 CA ARG A 65 37.096 13.526 -4.568 1.00 66.97 C ANISOU 488 CA ARG A 65 8519 8281 8643 1207 -791 -753 C ATOM 489 C ARG A 65 35.940 12.964 -5.405 1.00 66.67 C ANISOU 489 C ARG A 65 8550 8174 8608 1212 -853 -768 C ATOM 490 O ARG A 65 35.790 11.765 -5.516 1.00 65.85 O ANISOU 490 O ARG A 65 8505 8000 8513 1251 -938 -793 O ATOM 491 CB ARG A 65 36.716 13.391 -3.099 1.00 70.26 C ANISOU 491 CB ARG A 65 8927 8657 9111 1126 -812 -706 C ATOM 492 CG ARG A 65 37.286 12.150 -2.446 1.00 84.32 C ANISOU 492 CG ARG A 65 10734 10393 10911 1163 -883 -721 C ATOM 493 CD ARG A 65 37.497 12.365 -0.956 1.00 85.85 C ANISOU 493 CD ARG A 65 10892 10588 11137 1094 -870 -676 C ATOM 494 NE ARG A 65 36.399 13.173 -0.446 1.00 78.06 N ANISOU 494 NE ARG A 65 9893 9592 10172 998 -839 -627 N ATOM 495 CZ ARG A 65 36.498 14.239 0.357 1.00 74.70 C ANISOU 495 CZ ARG A 65 9418 9211 9750 935 -772 -588 C ATOM 496 NH1 ARG A 65 37.677 14.654 0.854 1.00 63.18 N ANISOU 496 NH1 ARG A 65 7915 7808 8279 947 -731 -587 N ATOM 497 NH2 ARG A 65 35.369 14.877 0.695 1.00 65.12 N ANISOU 497 NH2 ARG A 65 8203 7983 8555 859 -750 -548 N ATOM 498 N LEU A 66 35.111 13.814 -5.988 1.00 60.31 N ANISOU 498 N LEU A 66 7738 7381 7796 1171 -818 -751 N ATOM 499 CA LEU A 66 33.906 13.341 -6.658 1.00 63.19 C ANISOU 499 CA LEU A 66 8163 7675 8170 1159 -881 -754 C ATOM 500 C LEU A 66 34.176 12.743 -8.041 1.00 65.87 C ANISOU 500 C LEU A 66 8558 8007 8463 1255 -916 -814 C ATOM 501 O LEU A 66 35.011 13.242 -8.785 1.00 67.86 O ANISOU 501 O LEU A 66 8785 8332 8665 1314 -857 -843 O ATOM 502 CB LEU A 66 32.915 14.506 -6.817 1.00 62.29 C ANISOU 502 CB LEU A 66 8021 7579 8066 1083 -829 -713 C ATOM 503 CG LEU A 66 32.328 15.070 -5.519 1.00 59.15 C ANISOU 503 CG LEU A 66 7584 7176 7715 987 -803 -651 C ATOM 504 CD1 LEU A 66 31.353 16.191 -5.839 1.00 54.63 C ANISOU 504 CD1 LEU A 66 6989 6620 7147 927 -754 -617 C ATOM 505 CD2 LEU A 66 31.634 13.962 -4.740 1.00 58.83 C ANISOU 505 CD2 LEU A 66 7582 7050 7721 954 -890 -629 C ATOM 506 N SER A 67 33.444 11.697 -8.406 1.00 64.65 N ANISOU 506 N SER A 67 8478 7764 8320 1269 -1012 -829 N ATOM 507 CA SER A 67 33.478 11.236 -9.783 1.00 67.15 C ANISOU 507 CA SER A 67 8857 8066 8588 1350 -1048 -884 C ATOM 508 C SER A 67 32.917 12.349 -10.673 1.00 69.20 C ANISOU 508 C SER A 67 9098 8370 8824 1323 -989 -872 C ATOM 509 O SER A 67 32.269 13.272 -10.181 1.00 68.78 O ANISOU 509 O SER A 67 8997 8333 8802 1236 -943 -820 O ATOM 510 CB SER A 67 32.638 9.980 -9.941 1.00 67.73 C ANISOU 510 CB SER A 67 9021 8027 8686 1353 -1172 -893 C ATOM 511 OG SER A 67 31.268 10.317 -9.970 1.00 69.96 O ANISOU 511 OG SER A 67 9311 8268 9003 1265 -1194 -846 O ATOM 512 N ASP A 68 33.141 12.265 -11.978 1.00 68.42 N ANISOU 512 N ASP A 68 9039 8287 8669 1398 -991 -920 N ATOM 513 CA ASP A 68 32.585 13.263 -12.875 1.00 74.01 C ANISOU 513 CA ASP A 68 9734 9031 9352 1373 -943 -909 C ATOM 514 C ASP A 68 31.081 13.256 -12.781 1.00 73.47 C ANISOU 514 C ASP A 68 9694 8888 9332 1287 -998 -866 C ATOM 515 O ASP A 68 30.466 14.311 -12.711 1.00 72.61 O ANISOU 515 O ASP A 68 9540 8808 9241 1216 -944 -823 O ATOM 516 CB ASP A 68 33.004 13.029 -14.327 1.00 81.72 C ANISOU 516 CB ASP A 68 10762 10028 10256 1471 -949 -968 C ATOM 517 CG ASP A 68 34.466 13.363 -14.579 1.00 87.71 C ANISOU 517 CG ASP A 68 11473 10889 10961 1552 -869 -1000 C ATOM 518 OD1 ASP A 68 35.142 13.868 -13.661 1.00 95.47 O ANISOU 518 OD1 ASP A 68 12381 11927 11965 1525 -810 -972 O ATOM 519 OD2 ASP A 68 34.948 13.106 -15.700 1.00100.20 O ANISOU 519 OD2 ASP A 68 13095 12498 12479 1644 -868 -1050 O ATOM 520 N ALA A 69 30.483 12.070 -12.778 1.00 69.24 N ANISOU 520 N ALA A 69 9233 8255 8819 1292 -1106 -875 N ATOM 521 CA ALA A 69 29.022 11.965 -12.650 1.00 69.35 C ANISOU 521 CA ALA A 69 9270 8195 8885 1207 -1168 -826 C ATOM 522 C ALA A 69 28.509 12.700 -11.395 1.00 63.60 C ANISOU 522 C ALA A 69 8466 7485 8215 1105 -1119 -755 C ATOM 523 O ALA A 69 27.531 13.440 -11.457 1.00 61.54 O ANISOU 523 O ALA A 69 8179 7224 7978 1036 -1097 -710 O ATOM 524 CB ALA A 69 28.584 10.505 -12.612 1.00 67.18 C ANISOU 524 CB ALA A 69 9080 7812 8631 1222 -1298 -839 C ATOM 525 N ASP A 70 29.174 12.489 -10.268 1.00 60.71 N ANISOU 525 N ASP A 70 8065 7133 7869 1100 -1102 -746 N ATOM 526 CA ASP A 70 28.719 13.079 -9.012 1.00 62.52 C ANISOU 526 CA ASP A 70 8231 7373 8148 1009 -1061 -682 C ATOM 527 C ASP A 70 28.909 14.595 -9.014 1.00 59.00 C ANISOU 527 C ASP A 70 7713 7015 7686 981 -946 -663 C ATOM 528 O ASP A 70 28.067 15.317 -8.523 1.00 56.13 O ANISOU 528 O ASP A 70 7313 6654 7357 905 -915 -611 O ATOM 529 CB ASP A 70 29.447 12.461 -7.828 1.00 64.24 C ANISOU 529 CB ASP A 70 8436 7584 8387 1014 -1075 -680 C ATOM 530 CG ASP A 70 28.773 11.202 -7.316 1.00 68.37 C ANISOU 530 CG ASP A 70 9011 8010 8954 988 -1186 -660 C ATOM 531 OD1 ASP A 70 27.669 10.831 -7.790 1.00 66.84 O ANISOU 531 OD1 ASP A 70 8860 7755 8781 957 -1253 -640 O ATOM 532 OD2 ASP A 70 29.369 10.585 -6.413 1.00 69.31 O ANISOU 532 OD2 ASP A 70 9129 8117 9089 995 -1208 -661 O ATOM 533 N LYS A 71 30.014 15.050 -9.581 1.00 59.53 N ANISOU 533 N LYS A 71 7762 7153 7703 1044 -887 -705 N ATOM 534 CA LYS A 71 30.266 16.455 -9.722 1.00 58.73 C ANISOU 534 CA LYS A 71 7599 7133 7581 1022 -787 -690 C ATOM 535 C LYS A 71 29.151 17.112 -10.528 1.00 59.01 C ANISOU 535 C LYS A 71 7642 7157 7619 983 -782 -669 C ATOM 536 O LYS A 71 28.721 18.210 -10.185 1.00 56.02 O ANISOU 536 O LYS A 71 7216 6811 7257 922 -721 -628 O ATOM 537 CB LYS A 71 31.619 16.705 -10.362 1.00 58.41 C ANISOU 537 CB LYS A 71 7542 7168 7482 1101 -735 -736 C ATOM 538 CG LYS A 71 31.965 18.173 -10.502 1.00 61.15 C ANISOU 538 CG LYS A 71 7823 7601 7807 1075 -636 -717 C ATOM 539 CD LYS A 71 33.253 18.339 -11.285 1.00 63.82 C ANISOU 539 CD LYS A 71 8146 8017 8085 1156 -592 -758 C ATOM 540 CE LYS A 71 33.820 19.738 -11.117 1.00 69.95 C ANISOU 540 CE LYS A 71 8849 8880 8846 1123 -497 -730 C ATOM 541 NZ LYS A 71 35.223 19.904 -11.613 1.00 70.04 N ANISOU 541 NZ LYS A 71 8828 8977 8805 1194 -450 -757 N ATOM 542 N GLN A 72 28.661 16.434 -11.560 1.00 57.66 N ANISOU 542 N GLN A 72 7535 6937 7432 1017 -850 -695 N ATOM 543 CA GLN A 72 27.613 16.985 -12.405 1.00 57.87 C ANISOU 543 CA GLN A 72 7575 6951 7461 984 -854 -676 C ATOM 544 C GLN A 72 26.269 16.993 -11.719 1.00 54.92 C ANISOU 544 C GLN A 72 7192 6521 7152 896 -887 -614 C ATOM 545 O GLN A 72 25.367 17.704 -12.164 1.00 51.83 O ANISOU 545 O GLN A 72 6789 6129 6772 853 -873 -583 O ATOM 546 CB GLN A 72 27.460 16.201 -13.715 1.00 65.30 C ANISOU 546 CB GLN A 72 8595 7849 8364 1045 -926 -722 C ATOM 547 CG GLN A 72 28.665 16.220 -14.624 1.00 69.49 C ANISOU 547 CG GLN A 72 9139 8440 8821 1140 -891 -784 C ATOM 548 CD GLN A 72 29.154 17.622 -14.928 1.00 76.20 C ANISOU 548 CD GLN A 72 9924 9387 9641 1131 -784 -775 C ATOM 549 OE1 GLN A 72 28.384 18.491 -15.339 1.00 73.53 O ANISOU 549 OE1 GLN A 72 9570 9058 9310 1082 -758 -745 O ATOM 550 NE2 GLN A 72 30.451 17.845 -14.732 1.00 77.97 N ANISOU 550 NE2 GLN A 72 10109 9685 9832 1179 -723 -798 N ATOM 551 N ARG A 73 26.122 16.204 -10.657 1.00 54.30 N ANISOU 551 N ARG A 73 7118 6397 7116 870 -933 -592 N ATOM 552 CA ARG A 73 24.886 16.207 -9.877 1.00 55.74 C ANISOU 552 CA ARG A 73 7283 6535 7360 786 -959 -525 C ATOM 553 C ARG A 73 24.704 17.429 -8.952 1.00 51.93 C ANISOU 553 C ARG A 73 6725 6107 6899 726 -865 -477 C ATOM 554 O ARG A 73 23.624 17.626 -8.418 1.00 49.84 O ANISOU 554 O ARG A 73 6438 5817 6679 660 -871 -419 O ATOM 555 CB ARG A 73 24.782 14.946 -9.041 1.00 58.53 C ANISOU 555 CB ARG A 73 7666 6823 7748 776 -1041 -512 C ATOM 556 CG ARG A 73 24.411 13.707 -9.850 1.00 63.62 C ANISOU 556 CG ARG A 73 8393 7387 8391 808 -1157 -537 C ATOM 557 CD ARG A 73 24.366 12.502 -8.928 1.00 67.75 C ANISOU 557 CD ARG A 73 8943 7846 8951 794 -1239 -521 C ATOM 558 NE ARG A 73 23.834 11.325 -9.613 1.00 76.02 N ANISOU 558 NE ARG A 73 10073 8804 10006 811 -1362 -533 N ATOM 559 CZ ARG A 73 24.564 10.327 -10.103 1.00 82.31 C ANISOU 559 CZ ARG A 73 10940 9564 10770 888 -1429 -595 C ATOM 560 NH1 ARG A 73 25.902 10.304 -9.993 1.00 85.53 N ANISOU 560 NH1 ARG A 73 11340 10019 11138 960 -1382 -650 N ATOM 561 NH2 ARG A 73 23.945 9.331 -10.715 1.00 87.28 N ANISOU 561 NH2 ARG A 73 11648 10105 11408 894 -1546 -600 N ATOM 562 N ILE A 74 25.751 18.212 -8.737 1.00 46.91 N ANISOU 562 N ILE A 74 6049 5542 6231 749 -783 -499 N ATOM 563 CA ILE A 74 25.588 19.446 -7.982 1.00 48.67 C ANISOU 563 CA ILE A 74 6211 5813 6468 696 -697 -458 C ATOM 564 C ILE A 74 24.773 20.424 -8.829 1.00 46.64 C ANISOU 564 C ILE A 74 5942 5571 6209 673 -666 -440 C ATOM 565 O ILE A 74 25.235 20.896 -9.868 1.00 49.96 O ANISOU 565 O ILE A 74 6368 6027 6586 711 -641 -474 O ATOM 566 CB ILE A 74 26.928 20.060 -7.612 1.00 48.51 C ANISOU 566 CB ILE A 74 6156 5862 6413 724 -625 -484 C ATOM 567 CG1 ILE A 74 27.674 19.099 -6.699 1.00 47.25 C ANISOU 567 CG1 ILE A 74 6005 5685 6261 743 -659 -496 C ATOM 568 CG2 ILE A 74 26.687 21.415 -6.946 1.00 50.00 C ANISOU 568 CG2 ILE A 74 6291 6093 6612 669 -543 -444 C ATOM 569 CD1 ILE A 74 29.154 19.353 -6.573 1.00 48.46 C ANISOU 569 CD1 ILE A 74 6135 5900 6377 789 -611 -531 C ATOM 570 N GLU A 75 23.547 20.667 -8.402 1.00 44.78 N ANISOU 570 N GLU A 75 5689 5306 6017 612 -672 -385 N ATOM 571 CA GLU A 75 22.597 21.548 -9.120 1.00 47.58 C ANISOU 571 CA GLU A 75 6031 5666 6381 583 -651 -358 C ATOM 572 C GLU A 75 22.190 22.801 -8.337 1.00 44.76 C ANISOU 572 C GLU A 75 5616 5345 6042 534 -570 -314 C ATOM 573 O GLU A 75 21.303 23.575 -8.765 1.00 42.59 O ANISOU 573 O GLU A 75 5325 5073 5782 506 -550 -284 O ATOM 574 CB GLU A 75 21.352 20.770 -9.469 1.00 50.69 C ANISOU 574 CB GLU A 75 6454 5991 6814 556 -734 -326 C ATOM 575 CG GLU A 75 21.693 19.565 -10.346 1.00 64.87 C ANISOU 575 CG GLU A 75 8317 7743 8587 607 -822 -373 C ATOM 576 CD GLU A 75 20.531 19.039 -11.173 1.00 68.63 C ANISOU 576 CD GLU A 75 8832 8156 9087 588 -906 -351 C ATOM 577 OE1 GLU A 75 19.353 19.437 -10.950 1.00 67.42 O ANISOU 577 OE1 GLU A 75 8649 7988 8979 528 -905 -289 O ATOM 578 OE2 GLU A 75 20.823 18.206 -12.051 1.00 77.34 O ANISOU 578 OE2 GLU A 75 9998 9224 10162 635 -974 -395 O ATOM 579 N MET A 76 22.831 23.007 -7.198 1.00 43.82 N ANISOU 579 N MET A 76 5472 5254 5923 526 -526 -310 N ATOM 580 CA MET A 76 22.624 24.249 -6.447 1.00 44.20 C ANISOU 580 CA MET A 76 5475 5339 5978 489 -447 -277 C ATOM 581 C MET A 76 23.916 24.622 -5.761 1.00 41.72 C ANISOU 581 C MET A 76 5146 5070 5634 505 -397 -302 C ATOM 582 O MET A 76 24.559 23.778 -5.148 1.00 45.06 O ANISOU 582 O MET A 76 5580 5482 6056 520 -424 -316 O ATOM 583 CB MET A 76 21.474 24.096 -5.439 1.00 43.39 C ANISOU 583 CB MET A 76 5354 5205 5926 438 -455 -216 C ATOM 584 CG MET A 76 21.181 25.367 -4.653 1.00 47.24 C ANISOU 584 CG MET A 76 5803 5728 6418 407 -373 -183 C ATOM 585 SD MET A 76 19.515 25.445 -3.944 1.00 51.45 S ANISOU 585 SD MET A 76 6308 6233 7006 355 -373 -106 S ATOM 586 CE MET A 76 19.639 24.153 -2.745 1.00 53.21 C ANISOU 586 CE MET A 76 6540 6426 7250 340 -420 -87 C ATOM 587 N VAL A 77 24.289 25.885 -5.879 1.00 40.85 N ANISOU 587 N VAL A 77 5011 5008 5500 501 -328 -305 N ATOM 588 CA VAL A 77 25.391 26.463 -5.100 1.00 39.78 C ANISOU 588 CA VAL A 77 4856 4917 5341 502 -277 -316 C ATOM 589 C VAL A 77 24.901 27.675 -4.338 1.00 39.69 C ANISOU 589 C VAL A 77 4820 4921 5340 460 -216 -280 C ATOM 590 O VAL A 77 24.538 28.673 -4.958 1.00 40.05 O ANISOU 590 O VAL A 77 4855 4984 5379 452 -183 -273 O ATOM 591 CB VAL A 77 26.540 26.898 -6.034 1.00 41.65 C ANISOU 591 CB VAL A 77 5090 5204 5530 542 -254 -357 C ATOM 592 CG1 VAL A 77 27.606 27.673 -5.284 1.00 41.03 C ANISOU 592 CG1 VAL A 77 4986 5173 5430 534 -200 -359 C ATOM 593 CG2 VAL A 77 27.147 25.684 -6.710 1.00 45.74 C ANISOU 593 CG2 VAL A 77 5636 5712 6031 595 -309 -398 C ATOM 594 N ILE A 78 24.906 27.597 -3.007 1.00 38.33 N ANISOU 594 N ILE A 78 4640 4740 5181 436 -202 -258 N ATOM 595 CA ILE A 78 24.496 28.686 -2.156 1.00 38.71 C ANISOU 595 CA ILE A 78 4673 4801 5235 402 -145 -226 C ATOM 596 C ILE A 78 25.724 29.188 -1.396 1.00 39.91 C ANISOU 596 C ILE A 78 4820 4986 5356 402 -110 -242 C ATOM 597 O ILE A 78 26.393 28.426 -0.666 1.00 42.00 O ANISOU 597 O ILE A 78 5091 5246 5620 407 -132 -250 O ATOM 598 CB ILE A 78 23.473 28.263 -1.104 1.00 39.37 C ANISOU 598 CB ILE A 78 4753 4851 5353 373 -153 -182 C ATOM 599 CG1 ILE A 78 22.266 27.567 -1.748 1.00 43.37 C ANISOU 599 CG1 ILE A 78 5261 5320 5895 367 -201 -159 C ATOM 600 CG2 ILE A 78 22.984 29.473 -0.346 1.00 41.40 C ANISOU 600 CG2 ILE A 78 4996 5122 5609 347 -90 -153 C ATOM 601 CD1 ILE A 78 21.192 27.160 -0.757 1.00 42.56 C ANISOU 601 CD1 ILE A 78 5148 5192 5830 335 -208 -106 C ATOM 602 N THR A 79 26.019 30.464 -1.575 1.00 37.42 N ANISOU 602 N THR A 79 4496 4703 5020 394 -62 -243 N ATOM 603 CA THR A 79 27.096 31.108 -0.844 1.00 40.43 C ANISOU 603 CA THR A 79 4873 5113 5373 386 -30 -250 C ATOM 604 C THR A 79 26.498 31.925 0.277 1.00 40.24 C ANISOU 604 C THR A 79 4854 5078 5356 354 8 -219 C ATOM 605 O THR A 79 25.600 32.735 0.041 1.00 38.33 O ANISOU 605 O THR A 79 4609 4829 5122 343 35 -201 O ATOM 606 CB THR A 79 27.922 32.020 -1.761 1.00 43.69 C ANISOU 606 CB THR A 79 5275 5569 5754 396 -7 -269 C ATOM 607 OG1 THR A 79 28.509 31.247 -2.790 1.00 46.76 O ANISOU 607 OG1 THR A 79 5659 5973 6131 433 -39 -299 O ATOM 608 CG2 THR A 79 29.051 32.634 -1.016 1.00 46.40 C ANISOU 608 CG2 THR A 79 5614 5941 6073 383 16 -271 C ATOM 609 N CYS A 80 26.978 31.694 1.504 1.00 39.72 N ANISOU 609 N CYS A 80 4797 5008 5284 341 10 -214 N ATOM 610 CA CYS A 80 26.409 32.297 2.726 1.00 39.00 C ANISOU 610 CA CYS A 80 4718 4905 5195 315 45 -185 C ATOM 611 C CYS A 80 27.431 33.213 3.301 1.00 37.78 C ANISOU 611 C CYS A 80 4574 4771 5008 303 71 -194 C ATOM 612 O CYS A 80 28.549 32.786 3.615 1.00 36.37 O ANISOU 612 O CYS A 80 4395 4606 4815 305 52 -209 O ATOM 613 CB CYS A 80 26.047 31.198 3.713 1.00 39.99 C ANISOU 613 CB CYS A 80 4850 5004 5339 308 20 -167 C ATOM 614 SG CYS A 80 24.942 29.954 2.981 1.00 42.16 S ANISOU 614 SG CYS A 80 5114 5248 5656 318 -27 -154 S ATOM 615 N SER A 81 27.096 34.491 3.394 1.00 35.60 N ANISOU 615 N SER A 81 4307 4498 4718 290 111 -184 N ATOM 616 CA SER A 81 28.114 35.475 3.701 1.00 37.78 C ANISOU 616 CA SER A 81 4596 4794 4963 276 128 -192 C ATOM 617 C SER A 81 27.510 36.800 4.117 1.00 39.76 C ANISOU 617 C SER A 81 4869 5033 5202 262 168 -177 C ATOM 618 O SER A 81 26.389 37.133 3.743 1.00 42.36 O ANISOU 618 O SER A 81 5196 5350 5548 269 186 -164 O ATOM 619 CB SER A 81 29.020 35.723 2.469 1.00 38.04 C ANISOU 619 CB SER A 81 4607 4862 4983 286 116 -212 C ATOM 620 OG SER A 81 30.144 36.512 2.823 1.00 39.76 O ANISOU 620 OG SER A 81 4831 5101 5173 268 123 -214 O ATOM 621 N GLU A 82 28.288 37.545 4.888 1.00 39.44 N ANISOU 621 N GLU A 82 4854 4996 5134 244 177 -178 N ATOM 622 CA GLU A 82 28.038 38.933 5.155 1.00 42.25 C ANISOU 622 CA GLU A 82 5239 5342 5470 232 207 -171 C ATOM 623 C GLU A 82 29.256 39.776 4.716 1.00 42.67 C ANISOU 623 C GLU A 82 5294 5419 5499 214 196 -179 C ATOM 624 O GLU A 82 29.404 40.910 5.156 1.00 45.24 O ANISOU 624 O GLU A 82 5652 5733 5802 196 209 -174 O ATOM 625 CB GLU A 82 27.689 39.155 6.631 1.00 44.04 C ANISOU 625 CB GLU A 82 5506 5543 5681 224 227 -159 C ATOM 626 CG GLU A 82 28.747 38.734 7.656 1.00 49.51 C ANISOU 626 CG GLU A 82 6218 6237 6354 207 206 -162 C ATOM 627 CD GLU A 82 28.151 38.502 9.061 1.00 58.80 C ANISOU 627 CD GLU A 82 7429 7390 7522 207 223 -148 C ATOM 628 OE1 GLU A 82 27.680 37.353 9.342 1.00 59.42 O ANISOU 628 OE1 GLU A 82 7489 7465 7621 215 215 -139 O ATOM 629 OE2 GLU A 82 28.149 39.460 9.882 1.00 55.67 O ANISOU 629 OE2 GLU A 82 7079 6977 7094 198 243 -145 O ATOM 630 N SER A 83 30.076 39.247 3.818 1.00 41.98 N ANISOU 630 N SER A 83 5170 5364 5415 219 173 -190 N ATOM 631 CA SER A 83 31.265 39.968 3.276 1.00 44.14 C ANISOU 631 CA SER A 83 5433 5671 5667 202 162 -191 C ATOM 632 C SER A 83 31.158 40.023 1.758 1.00 43.90 C ANISOU 632 C SER A 83 5368 5668 5643 217 162 -197 C ATOM 633 O SER A 83 32.147 39.842 1.051 1.00 43.06 O ANISOU 633 O SER A 83 5232 5603 5526 220 148 -202 O ATOM 634 CB SER A 83 32.587 39.226 3.590 1.00 45.51 C ANISOU 634 CB SER A 83 5588 5871 5832 198 135 -196 C ATOM 635 OG SER A 83 32.699 38.797 4.919 1.00 44.63 O ANISOU 635 OG SER A 83 5502 5736 5718 188 127 -193 O ATOM 636 N GLY A 84 29.966 40.292 1.245 1.00 42.84 N ANISOU 636 N GLY A 84 5238 5514 5524 228 179 -195 N ATOM 637 CA GLY A 84 29.734 40.323 -0.181 1.00 40.30 C ANISOU 637 CA GLY A 84 4889 5213 5208 242 177 -200 C ATOM 638 C GLY A 84 30.559 41.369 -0.930 1.00 42.43 C ANISOU 638 C GLY A 84 5149 5517 5454 223 178 -194 C ATOM 639 O GLY A 84 31.004 42.376 -0.380 1.00 41.95 O ANISOU 639 O GLY A 84 5110 5451 5376 194 181 -181 O ATOM 640 N ILE A 85 30.722 41.126 -2.220 1.00 43.17 N ANISOU 640 N ILE A 85 5213 5644 5546 238 171 -201 N ATOM 641 CA ILE A 85 31.553 41.958 -3.078 1.00 44.03 C ANISOU 641 CA ILE A 85 5303 5794 5630 222 170 -191 C ATOM 642 C ILE A 85 30.747 42.747 -4.110 1.00 44.35 C ANISOU 642 C ILE A 85 5346 5830 5674 219 180 -184 C ATOM 643 O ILE A 85 31.302 43.572 -4.808 1.00 41.28 O ANISOU 643 O ILE A 85 4945 5472 5265 201 180 -171 O ATOM 644 CB ILE A 85 32.617 41.112 -3.795 1.00 44.69 C ANISOU 644 CB ILE A 85 5347 5932 5699 244 157 -202 C ATOM 645 CG1 ILE A 85 31.983 39.976 -4.591 1.00 45.57 C ANISOU 645 CG1 ILE A 85 5449 6042 5824 286 149 -225 C ATOM 646 CG2 ILE A 85 33.610 40.580 -2.766 1.00 46.99 C ANISOU 646 CG2 ILE A 85 5634 6233 5985 240 145 -202 C ATOM 647 CD1 ILE A 85 32.966 39.314 -5.528 1.00 49.64 C ANISOU 647 CD1 ILE A 85 5929 6613 6317 316 140 -238 C ATOM 648 N ASP A 86 29.437 42.547 -4.159 1.00 43.08 N ANISOU 648 N ASP A 86 5198 5630 5538 234 187 -188 N ATOM 649 CA ASP A 86 28.591 43.265 -5.108 1.00 42.38 C ANISOU 649 CA ASP A 86 5112 5533 5457 232 194 -180 C ATOM 650 C ASP A 86 27.178 43.333 -4.539 1.00 44.36 C ANISOU 650 C ASP A 86 5384 5730 5738 240 207 -174 C ATOM 651 O ASP A 86 26.785 42.448 -3.764 1.00 42.54 O ANISOU 651 O ASP A 86 5158 5480 5525 254 206 -179 O ATOM 652 CB ASP A 86 28.583 42.472 -6.436 1.00 44.92 C ANISOU 652 CB ASP A 86 5406 5883 5776 258 181 -193 C ATOM 653 CG ASP A 86 28.096 43.296 -7.638 1.00 47.47 C ANISOU 653 CG ASP A 86 5726 6213 6095 251 183 -182 C ATOM 654 OD1 ASP A 86 28.923 44.005 -8.281 1.00 50.27 O ANISOU 654 OD1 ASP A 86 6069 6608 6423 233 183 -173 O ATOM 655 OD2 ASP A 86 26.874 43.197 -7.970 1.00 49.49 O ANISOU 655 OD2 ASP A 86 5990 6436 6378 261 182 -180 O ATOM 656 N PHE A 87 26.398 44.329 -4.966 1.00 40.07 N ANISOU 656 N PHE A 87 4852 5169 5203 232 217 -160 N ATOM 657 CA PHE A 87 25.009 44.435 -4.557 1.00 43.06 C ANISOU 657 CA PHE A 87 5244 5503 5611 244 232 -150 C ATOM 658 C PHE A 87 24.066 43.432 -5.243 1.00 42.17 C ANISOU 658 C PHE A 87 5109 5383 5528 266 221 -151 C ATOM 659 O PHE A 87 23.028 43.092 -4.685 1.00 41.47 O ANISOU 659 O PHE A 87 5022 5265 5467 278 229 -140 O ATOM 660 CB PHE A 87 24.509 45.909 -4.714 1.00 45.12 C ANISOU 660 CB PHE A 87 5526 5743 5871 231 245 -135 C ATOM 661 CG PHE A 87 24.856 46.780 -3.536 1.00 49.14 C ANISOU 661 CG PHE A 87 6074 6233 6363 217 258 -132 C ATOM 662 CD1 PHE A 87 26.138 47.306 -3.389 1.00 55.72 C ANISOU 662 CD1 PHE A 87 6918 7087 7165 189 245 -133 C ATOM 663 CD2 PHE A 87 23.923 47.015 -2.526 1.00 52.39 C ANISOU 663 CD2 PHE A 87 6511 6605 6788 233 281 -126 C ATOM 664 CE1 PHE A 87 26.483 48.064 -2.273 1.00 58.97 C ANISOU 664 CE1 PHE A 87 7372 7474 7559 174 249 -131 C ATOM 665 CE2 PHE A 87 24.252 47.784 -1.419 1.00 55.66 C ANISOU 665 CE2 PHE A 87 6969 6998 7180 224 291 -126 C ATOM 666 CZ PHE A 87 25.538 48.301 -1.280 1.00 57.11 C ANISOU 666 CZ PHE A 87 7170 7196 7333 194 271 -130 C ATOM 667 N GLY A 88 24.398 42.978 -6.448 1.00 41.24 N ANISOU 667 N GLY A 88 4972 5293 5403 272 200 -161 N ATOM 668 CA GLY A 88 23.574 41.982 -7.134 1.00 42.66 C ANISOU 668 CA GLY A 88 5139 5462 5608 292 179 -163 C ATOM 669 C GLY A 88 24.237 40.660 -7.496 1.00 42.24 C ANISOU 669 C GLY A 88 5074 5429 5544 311 152 -185 C ATOM 670 O GLY A 88 23.595 39.599 -7.476 1.00 45.60 O ANISOU 670 O GLY A 88 5497 5833 5993 326 131 -186 O ATOM 671 N LYS A 89 25.515 40.699 -7.842 1.00 43.66 N ANISOU 671 N LYS A 89 5247 5652 5688 311 150 -201 N ATOM 672 CA LYS A 89 26.199 39.505 -8.337 1.00 44.72 C ANISOU 672 CA LYS A 89 5372 5811 5808 338 125 -225 C ATOM 673 C LYS A 89 26.581 38.619 -7.152 1.00 42.66 C ANISOU 673 C LYS A 89 5113 5538 5555 345 120 -233 C ATOM 674 O LYS A 89 27.274 39.079 -6.254 1.00 45.39 O ANISOU 674 O LYS A 89 5462 5895 5890 329 136 -229 O ATOM 675 CB LYS A 89 27.443 39.903 -9.127 1.00 49.28 C ANISOU 675 CB LYS A 89 5935 6445 6343 340 130 -234 C ATOM 676 CG LYS A 89 28.150 38.755 -9.864 1.00 50.19 C ANISOU 676 CG LYS A 89 6040 6592 6436 378 108 -261 C ATOM 677 CD LYS A 89 29.491 39.267 -10.388 1.00 53.81 C ANISOU 677 CD LYS A 89 6477 7116 6851 377 122 -262 C ATOM 678 CE LYS A 89 30.258 38.195 -11.165 1.00 53.60 C ANISOU 678 CE LYS A 89 6439 7128 6796 424 107 -290 C ATOM 679 NZ LYS A 89 29.857 38.163 -12.599 1.00 55.56 N ANISOU 679 NZ LYS A 89 6693 7389 7025 443 98 -298 N ATOM 680 N SER A 90 26.104 37.370 -7.127 1.00 40.92 N ANISOU 680 N SER A 90 4897 5295 5356 366 91 -243 N ATOM 681 CA SER A 90 26.497 36.451 -6.089 1.00 41.97 C ANISOU 681 CA SER A 90 5033 5417 5495 373 80 -250 C ATOM 682 C SER A 90 27.910 35.963 -6.342 1.00 41.02 C ANISOU 682 C SER A 90 4902 5339 5343 394 70 -275 C ATOM 683 O SER A 90 28.334 35.783 -7.469 1.00 42.12 O ANISOU 683 O SER A 90 5035 5508 5460 417 60 -292 O ATOM 684 CB SER A 90 25.591 35.229 -5.956 1.00 43.86 C ANISOU 684 CB SER A 90 5280 5616 5768 386 46 -249 C ATOM 685 OG SER A 90 25.701 34.391 -7.067 1.00 50.20 O ANISOU 685 OG SER A 90 6086 6424 6563 415 10 -271 O ATOM 686 N MET A 91 28.570 35.645 -5.258 1.00 39.11 N ANISOU 686 N MET A 91 4661 5099 5100 390 72 -276 N ATOM 687 CA MET A 91 29.846 35.001 -5.330 1.00 43.83 C ANISOU 687 CA MET A 91 5246 5732 5675 414 59 -297 C ATOM 688 C MET A 91 29.773 33.599 -5.899 1.00 45.83 C ANISOU 688 C MET A 91 5505 5974 5932 455 20 -322 C ATOM 689 O MET A 91 30.814 33.042 -6.320 1.00 42.51 O ANISOU 689 O MET A 91 5073 5589 5487 489 9 -345 O ATOM 690 CB MET A 91 30.467 34.983 -3.941 1.00 44.13 C ANISOU 690 CB MET A 91 5285 5767 5715 395 65 -289 C ATOM 691 CG MET A 91 30.760 36.399 -3.509 1.00 46.05 C ANISOU 691 CG MET A 91 5528 6024 5944 358 97 -268 C ATOM 692 SD MET A 91 31.695 36.492 -1.985 1.00 52.38 S ANISOU 692 SD MET A 91 6335 6826 6739 334 100 -259 S ATOM 693 CE MET A 91 30.425 36.202 -0.785 1.00 51.01 C ANISOU 693 CE MET A 91 6192 6591 6595 321 102 -247 C ATOM 694 N SER A 92 28.566 33.031 -5.913 1.00 40.70 N ANISOU 694 N SER A 92 4873 5276 5314 455 -3 -317 N ATOM 695 CA SER A 92 28.387 31.683 -6.367 1.00 42.33 C ANISOU 695 CA SER A 92 5093 5460 5528 490 -49 -338 C ATOM 696 C SER A 92 28.808 31.505 -7.839 1.00 43.15 C ANISOU 696 C SER A 92 5198 5595 5600 529 -61 -365 C ATOM 697 O SER A 92 29.224 30.418 -8.207 1.00 41.16 O ANISOU 697 O SER A 92 4959 5341 5339 570 -97 -393 O ATOM 698 CB SER A 92 26.933 31.248 -6.206 1.00 42.78 C ANISOU 698 CB SER A 92 5167 5461 5626 474 -75 -318 C ATOM 699 OG SER A 92 26.600 31.133 -4.862 1.00 44.57 O ANISOU 699 OG SER A 92 5393 5662 5878 447 -68 -295 O ATOM 700 N THR A 93 28.668 32.549 -8.658 1.00 39.72 N ANISOU 700 N THR A 93 4755 5186 5149 517 -34 -357 N ATOM 701 CA THR A 93 29.070 32.508 -10.061 1.00 44.23 C ANISOU 701 CA THR A 93 5327 5793 5683 552 -40 -379 C ATOM 702 C THR A 93 30.581 32.300 -10.220 1.00 45.77 C ANISOU 702 C THR A 93 5502 6048 5838 586 -27 -400 C ATOM 703 O THR A 93 30.985 31.465 -11.002 1.00 44.44 O ANISOU 703 O THR A 93 5344 5893 5645 637 -50 -430 O ATOM 704 CB THR A 93 28.630 33.768 -10.838 1.00 46.20 C ANISOU 704 CB THR A 93 5569 6060 5923 526 -12 -361 C ATOM 705 OG1 THR A 93 29.235 34.939 -10.262 1.00 47.47 O ANISOU 705 OG1 THR A 93 5706 6255 6075 492 30 -339 O ATOM 706 CG2 THR A 93 27.101 33.908 -10.782 1.00 48.42 C ANISOU 706 CG2 THR A 93 5866 6284 6245 498 -26 -338 C ATOM 707 N TYR A 94 31.400 33.007 -9.440 1.00 43.92 N ANISOU 707 N TYR A 94 5242 5847 5598 562 4 -384 N ATOM 708 CA TYR A 94 32.860 32.793 -9.473 1.00 44.40 C ANISOU 708 CA TYR A 94 5276 5968 5626 592 15 -396 C ATOM 709 C TYR A 94 33.235 31.425 -8.939 1.00 44.08 C ANISOU 709 C TYR A 94 5246 5907 5595 630 -18 -421 C ATOM 710 O TYR A 94 34.158 30.789 -9.421 1.00 44.61 O ANISOU 710 O TYR A 94 5302 6012 5634 681 -25 -444 O ATOM 711 CB TYR A 94 33.619 33.841 -8.664 1.00 42.63 C ANISOU 711 CB TYR A 94 5022 5777 5398 549 49 -367 C ATOM 712 CG TYR A 94 33.640 35.233 -9.258 1.00 42.68 C ANISOU 712 CG TYR A 94 5013 5817 5386 515 80 -342 C ATOM 713 CD1 TYR A 94 34.374 35.513 -10.389 1.00 43.31 C ANISOU 713 CD1 TYR A 94 5069 5962 5425 538 95 -344 C ATOM 714 CD2 TYR A 94 32.959 36.286 -8.654 1.00 43.23 C ANISOU 714 CD2 TYR A 94 5092 5854 5476 462 95 -315 C ATOM 715 CE1 TYR A 94 34.416 36.801 -10.916 1.00 45.34 C ANISOU 715 CE1 TYR A 94 5310 6249 5665 502 120 -317 C ATOM 716 CE2 TYR A 94 33.005 37.585 -9.169 1.00 42.74 C ANISOU 716 CE2 TYR A 94 5019 5819 5398 429 119 -291 C ATOM 717 CZ TYR A 94 33.754 37.829 -10.291 1.00 43.75 C ANISOU 717 CZ TYR A 94 5122 6011 5488 447 129 -291 C ATOM 718 OH TYR A 94 33.804 39.092 -10.829 1.00 49.21 O ANISOU 718 OH TYR A 94 5803 6729 6163 412 148 -264 O ATOM 719 N ILE A 95 32.512 30.963 -7.938 1.00 42.50 N ANISOU 719 N ILE A 95 5066 5647 5434 608 -40 -413 N ATOM 720 CA ILE A 95 32.815 29.690 -7.321 1.00 41.84 C ANISOU 720 CA ILE A 95 4994 5537 5363 637 -77 -432 C ATOM 721 C ILE A 95 32.552 28.559 -8.301 1.00 43.93 C ANISOU 721 C ILE A 95 5289 5782 5620 692 -121 -466 C ATOM 722 O ILE A 95 33.382 27.677 -8.494 1.00 45.62 O ANISOU 722 O ILE A 95 5504 6013 5816 745 -141 -495 O ATOM 723 CB ILE A 95 32.015 29.514 -6.025 1.00 44.12 C ANISOU 723 CB ILE A 95 5299 5769 5696 594 -90 -410 C ATOM 724 CG1 ILE A 95 32.566 30.472 -4.970 1.00 44.07 C ANISOU 724 CG1 ILE A 95 5271 5785 5689 551 -52 -384 C ATOM 725 CG2 ILE A 95 32.074 28.092 -5.515 1.00 45.27 C ANISOU 725 CG2 ILE A 95 5465 5876 5860 621 -139 -427 C ATOM 726 CD1 ILE A 95 31.645 30.691 -3.785 1.00 44.76 C ANISOU 726 CD1 ILE A 95 5374 5822 5809 505 -49 -357 C ATOM 727 N GLN A 96 31.422 28.633 -8.968 1.00 43.29 N ANISOU 727 N GLN A 96 5230 5666 5549 682 -135 -463 N ATOM 728 CA GLN A 96 31.080 27.713 -10.033 1.00 46.14 C ANISOU 728 CA GLN A 96 5626 6005 5897 730 -180 -494 C ATOM 729 C GLN A 96 32.155 27.627 -11.119 1.00 48.14 C ANISOU 729 C GLN A 96 5873 6321 6096 791 -167 -526 C ATOM 730 O GLN A 96 32.524 26.529 -11.558 1.00 46.27 O ANISOU 730 O GLN A 96 5662 6077 5842 851 -204 -562 O ATOM 731 CB GLN A 96 29.747 28.142 -10.638 1.00 48.72 C ANISOU 731 CB GLN A 96 5972 6297 6242 699 -189 -477 C ATOM 732 CG GLN A 96 29.194 27.180 -11.685 1.00 53.36 C ANISOU 732 CG GLN A 96 6605 6846 6821 739 -246 -504 C ATOM 733 CD GLN A 96 28.531 27.870 -12.872 1.00 53.98 C ANISOU 733 CD GLN A 96 6692 6932 6884 731 -238 -499 C ATOM 734 OE1 GLN A 96 27.587 27.344 -13.467 1.00 55.04 O ANISOU 734 OE1 GLN A 96 6864 7017 7031 734 -287 -502 O ATOM 735 NE2 GLN A 96 29.035 29.040 -13.228 1.00 52.35 N ANISOU 735 NE2 GLN A 96 6454 6786 6650 719 -182 -489 N ATOM 736 N GLU A 97 32.632 28.798 -11.545 1.00 47.43 N ANISOU 736 N GLU A 97 5749 6294 5979 775 -114 -510 N ATOM 737 CA GLU A 97 33.640 28.936 -12.589 1.00 49.66 C ANISOU 737 CA GLU A 97 6013 6649 6206 825 -90 -530 C ATOM 738 C GLU A 97 34.938 28.237 -12.162 1.00 49.68 C ANISOU 738 C GLU A 97 5995 6689 6192 874 -89 -548 C ATOM 739 O GLU A 97 35.421 27.413 -12.883 1.00 49.64 O ANISOU 739 O GLU A 97 6005 6701 6154 943 -107 -583 O ATOM 740 CB GLU A 97 33.887 30.435 -12.881 1.00 53.54 C ANISOU 740 CB GLU A 97 6466 7197 6679 782 -36 -497 C ATOM 741 CG GLU A 97 34.992 30.785 -13.878 1.00 60.44 C ANISOU 741 CG GLU A 97 7309 8160 7495 823 -1 -502 C ATOM 742 CD GLU A 97 34.748 30.240 -15.284 1.00 73.23 C ANISOU 742 CD GLU A 97 8962 9786 9074 881 -20 -536 C ATOM 743 OE1 GLU A 97 33.572 30.081 -15.704 1.00 81.86 O ANISOU 743 OE1 GLU A 97 10098 10820 10183 868 -51 -542 O ATOM 744 OE2 GLU A 97 35.746 29.958 -15.998 1.00 85.79 O ANISOU 744 OE2 GLU A 97 10537 11443 10614 941 -3 -555 O ATOM 745 N TYR A 98 35.456 28.522 -10.967 1.00 45.74 N ANISOU 745 N TYR A 98 5464 6197 5716 839 -73 -524 N ATOM 746 CA TYR A 98 36.782 28.038 -10.622 1.00 46.15 C ANISOU 746 CA TYR A 98 5486 6296 5751 881 -67 -534 C ATOM 747 C TYR A 98 36.781 26.608 -10.093 1.00 47.76 C ANISOU 747 C TYR A 98 5722 6448 5976 922 -119 -564 C ATOM 748 O TYR A 98 37.817 25.974 -10.084 1.00 49.58 O ANISOU 748 O TYR A 98 5936 6713 6187 977 -123 -583 O ATOM 749 CB TYR A 98 37.479 28.997 -9.677 1.00 45.11 C ANISOU 749 CB TYR A 98 5306 6201 5629 827 -30 -495 C ATOM 750 CG TYR A 98 37.955 30.212 -10.403 1.00 44.71 C ANISOU 750 CG TYR A 98 5218 6224 5546 809 16 -470 C ATOM 751 CD1 TYR A 98 37.113 31.311 -10.568 1.00 45.43 C ANISOU 751 CD1 TYR A 98 5316 6299 5645 750 34 -445 C ATOM 752 CD2 TYR A 98 39.236 30.255 -10.981 1.00 46.31 C ANISOU 752 CD2 TYR A 98 5375 6512 5706 853 42 -469 C ATOM 753 CE1 TYR A 98 37.517 32.433 -11.265 1.00 43.88 C ANISOU 753 CE1 TYR A 98 5087 6165 5418 730 72 -420 C ATOM 754 CE2 TYR A 98 39.665 31.381 -11.677 1.00 45.05 C ANISOU 754 CE2 TYR A 98 5177 6422 5515 832 84 -440 C ATOM 755 CZ TYR A 98 38.791 32.461 -11.820 1.00 46.41 C ANISOU 755 CZ TYR A 98 5363 6572 5698 769 96 -416 C ATOM 756 OH TYR A 98 39.176 33.592 -12.495 1.00 48.29 O ANISOU 756 OH TYR A 98 5567 6874 5907 742 131 -384 O ATOM 757 N LEU A 99 35.632 26.067 -9.717 1.00 45.57 N ANISOU 757 N LEU A 99 5489 6088 5735 898 -162 -567 N ATOM 758 CA LEU A 99 35.580 24.660 -9.380 1.00 47.08 C ANISOU 758 CA LEU A 99 5717 6227 5944 939 -221 -595 C ATOM 759 C LEU A 99 35.164 23.795 -10.562 1.00 47.53 C ANISOU 759 C LEU A 99 5824 6256 5978 1000 -264 -635 C ATOM 760 O LEU A 99 35.128 22.584 -10.433 1.00 48.51 O ANISOU 760 O LEU A 99 5986 6332 6111 1041 -320 -663 O ATOM 761 CB LEU A 99 34.605 24.409 -8.219 1.00 46.30 C ANISOU 761 CB LEU A 99 5638 6052 5899 879 -252 -571 C ATOM 762 CG LEU A 99 34.946 24.988 -6.836 1.00 46.68 C ANISOU 762 CG LEU A 99 5654 6110 5973 823 -224 -536 C ATOM 763 CD1 LEU A 99 33.769 24.848 -5.887 1.00 47.48 C ANISOU 763 CD1 LEU A 99 5778 6140 6120 765 -248 -510 C ATOM 764 CD2 LEU A 99 36.146 24.278 -6.239 1.00 46.89 C ANISOU 764 CD2 LEU A 99 5663 6156 5994 860 -237 -549 C ATOM 765 N GLY A 100 34.733 24.417 -11.650 1.00 51.59 N ANISOU 765 N GLY A 100 6345 6791 6465 1000 -245 -637 N ATOM 766 CA GLY A 100 34.347 23.706 -12.859 1.00 50.87 C ANISOU 766 CA GLY A 100 6306 6677 6345 1057 -284 -675 C ATOM 767 C GLY A 100 32.995 23.016 -12.804 1.00 53.88 C ANISOU 767 C GLY A 100 6744 6963 6765 1033 -352 -675 C ATOM 768 O GLY A 100 32.828 21.985 -13.410 1.00 52.73 O ANISOU 768 O GLY A 100 6652 6777 6605 1086 -409 -711 O ATOM 769 N LEU A 101 32.008 23.584 -12.121 1.00 50.54 N ANISOU 769 N LEU A 101 6311 6502 6388 954 -348 -634 N ATOM 770 CA LEU A 101 30.727 22.892 -11.945 1.00 48.85 C ANISOU 770 CA LEU A 101 6142 6200 6217 925 -414 -624 C ATOM 771 C LEU A 101 29.819 23.044 -13.158 1.00 48.07 C ANISOU 771 C LEU A 101 6078 6080 6105 926 -436 -629 C ATOM 772 O LEU A 101 30.067 23.857 -14.015 1.00 48.46 O ANISOU 772 O LEU A 101 6113 6182 6117 936 -393 -633 O ATOM 773 CB LEU A 101 30.015 23.413 -10.700 1.00 48.39 C ANISOU 773 CB LEU A 101 6057 6116 6213 845 -398 -574 C ATOM 774 CG LEU A 101 30.823 23.370 -9.406 1.00 50.21 C ANISOU 774 CG LEU A 101 6254 6364 6457 833 -376 -564 C ATOM 775 CD1 LEU A 101 30.039 24.008 -8.270 1.00 48.22 C ANISOU 775 CD1 LEU A 101 5980 6090 6250 756 -354 -515 C ATOM 776 CD2 LEU A 101 31.213 21.939 -9.069 1.00 52.87 C ANISOU 776 CD2 LEU A 101 6623 6661 6801 878 -438 -591 C ATOM 777 N SER A 102 28.744 22.266 -13.221 1.00 48.01 N ANISOU 777 N SER A 102 6117 5993 6130 911 -507 -623 N ATOM 778 CA SER A 102 27.847 22.323 -14.362 1.00 45.74 C ANISOU 778 CA SER A 102 5868 5678 5833 910 -539 -626 C ATOM 779 C SER A 102 27.182 23.711 -14.516 1.00 48.00 C ANISOU 779 C SER A 102 6115 5991 6131 850 -484 -585 C ATOM 780 O SER A 102 26.967 24.424 -13.531 1.00 45.70 O ANISOU 780 O SER A 102 5778 5709 5875 795 -443 -546 O ATOM 781 CB SER A 102 26.750 21.285 -14.219 1.00 45.40 C ANISOU 781 CB SER A 102 5874 5541 5832 891 -630 -615 C ATOM 782 OG SER A 102 25.757 21.510 -15.221 1.00 47.30 O ANISOU 782 OG SER A 102 6144 5754 6072 874 -659 -605 O ATOM 783 N ARG A 103 26.879 24.082 -15.764 1.00 46.71 N ANISOU 783 N ARG A 103 5972 5838 5935 863 -486 -595 N ATOM 784 CA ARG A 103 26.120 25.260 -16.034 1.00 46.69 C ANISOU 784 CA ARG A 103 5943 5848 5947 810 -450 -558 C ATOM 785 C ARG A 103 24.643 25.068 -15.700 1.00 47.39 C ANISOU 785 C ARG A 103 6044 5863 6097 753 -498 -516 C ATOM 786 O ARG A 103 23.915 26.054 -15.579 1.00 49.20 O ANISOU 786 O ARG A 103 6242 6098 6354 701 -466 -476 O ATOM 787 CB ARG A 103 26.283 25.683 -17.483 1.00 48.36 C ANISOU 787 CB ARG A 103 6174 6094 6103 842 -440 -580 C ATOM 788 CG ARG A 103 27.662 26.202 -17.820 1.00 50.29 C ANISOU 788 CG ARG A 103 6389 6428 6289 885 -376 -605 C ATOM 789 CD ARG A 103 27.664 26.884 -19.183 1.00 54.45 C ANISOU 789 CD ARG A 103 6926 6995 6765 899 -356 -612 C ATOM 790 NE ARG A 103 28.846 27.712 -19.436 1.00 55.16 N ANISOU 790 NE ARG A 103 6972 7180 6806 919 -283 -616 N ATOM 791 CZ ARG A 103 28.958 28.566 -20.454 1.00 58.67 C ANISOU 791 CZ ARG A 103 7407 7674 7208 919 -250 -611 C ATOM 792 NH1 ARG A 103 27.979 28.709 -21.339 1.00 58.84 N ANISOU 792 NH1 ARG A 103 7467 7661 7229 903 -283 -606 N ATOM 793 NH2 ARG A 103 30.054 29.289 -20.598 1.00 56.85 N ANISOU 793 NH2 ARG A 103 7131 7531 6937 932 -187 -607 N ATOM 794 N ASN A 104 24.190 23.826 -15.561 1.00 46.08 N ANISOU 794 N ASN A 104 5922 5630 5955 763 -577 -523 N ATOM 795 CA ASN A 104 22.807 23.573 -15.136 1.00 48.80 C ANISOU 795 CA ASN A 104 6270 5908 6362 705 -626 -474 C ATOM 796 C ASN A 104 22.741 23.561 -13.627 1.00 50.24 C ANISOU 796 C ASN A 104 6412 6086 6591 666 -603 -440 C ATOM 797 O ASN A 104 22.636 22.511 -13.004 1.00 50.08 O ANISOU 797 O ASN A 104 6412 6020 6596 666 -657 -437 O ATOM 798 CB ASN A 104 22.291 22.251 -15.709 1.00 52.50 C ANISOU 798 CB ASN A 104 6807 6303 6836 726 -730 -490 C ATOM 799 CG ASN A 104 22.240 22.261 -17.230 1.00 51.63 C ANISOU 799 CG ASN A 104 6746 6192 6678 763 -758 -523 C ATOM 800 OD1 ASN A 104 22.903 21.467 -17.868 1.00 54.31 O ANISOU 800 OD1 ASN A 104 7138 6524 6971 828 -795 -575 O ATOM 801 ND2 ASN A 104 21.491 23.207 -17.814 1.00 52.05 N ANISOU 801 ND2 ASN A 104 6782 6256 6739 726 -736 -493 N ATOM 802 N CYS A 105 22.779 24.760 -13.043 1.00 49.06 N ANISOU 802 N CYS A 105 6208 5981 6450 631 -525 -412 N ATOM 803 CA CYS A 105 23.009 24.924 -11.618 1.00 47.83 C ANISOU 803 CA CYS A 105 6015 5837 6321 604 -487 -389 C ATOM 804 C CYS A 105 22.409 26.244 -11.143 1.00 47.55 C ANISOU 804 C CYS A 105 5933 5825 6309 553 -422 -344 C ATOM 805 O CYS A 105 22.703 27.294 -11.735 1.00 44.54 O ANISOU 805 O CYS A 105 5535 5487 5899 556 -373 -351 O ATOM 806 CB CYS A 105 24.505 24.983 -11.394 1.00 49.11 C ANISOU 806 CB CYS A 105 6167 6052 6440 645 -447 -429 C ATOM 807 SG CYS A 105 24.982 24.826 -9.683 1.00 55.19 S ANISOU 807 SG CYS A 105 6906 6826 7235 622 -423 -410 S ATOM 808 N ARG A 106 21.538 26.175 -10.134 1.00 43.76 N ANISOU 808 N ARG A 106 5433 5314 5878 509 -426 -297 N ATOM 809 CA ARG A 106 21.011 27.371 -9.497 1.00 45.99 C ANISOU 809 CA ARG A 106 5673 5618 6181 469 -362 -257 C ATOM 810 C ARG A 106 22.113 27.991 -8.636 1.00 45.40 C ANISOU 810 C ARG A 106 5577 5590 6081 474 -298 -272 C ATOM 811 O ARG A 106 22.798 27.280 -7.909 1.00 43.77 O ANISOU 811 O ARG A 106 5376 5382 5871 486 -310 -286 O ATOM 812 CB ARG A 106 19.827 27.027 -8.608 1.00 45.35 C ANISOU 812 CB ARG A 106 5578 5497 6156 428 -381 -202 C ATOM 813 CG ARG A 106 18.583 26.560 -9.353 1.00 45.91 C ANISOU 813 CG ARG A 106 5661 5521 6261 411 -443 -171 C ATOM 814 CD ARG A 106 17.537 26.314 -8.297 1.00 49.02 C ANISOU 814 CD ARG A 106 6026 5889 6707 369 -450 -109 C ATOM 815 NE ARG A 106 16.211 26.015 -8.821 1.00 50.24 N ANISOU 815 NE ARG A 106 6179 6003 6905 341 -502 -63 N ATOM 816 CZ ARG A 106 15.465 24.962 -8.487 1.00 54.32 C ANISOU 816 CZ ARG A 106 6701 6475 7462 317 -569 -24 C ATOM 817 NH1 ARG A 106 15.898 24.043 -7.620 1.00 53.31 N ANISOU 817 NH1 ARG A 106 6583 6332 7338 317 -595 -27 N ATOM 818 NH2 ARG A 106 14.259 24.821 -9.051 1.00 57.02 N ANISOU 818 NH2 ARG A 106 7036 6784 7843 289 -616 22 N ATOM 819 N MET A 107 22.270 29.305 -8.718 1.00 44.68 N ANISOU 819 N MET A 107 5463 5538 5974 462 -236 -266 N ATOM 820 CA MET A 107 23.356 30.002 -8.035 1.00 42.27 C ANISOU 820 CA MET A 107 5141 5278 5642 464 -181 -279 C ATOM 821 C MET A 107 22.833 31.284 -7.388 1.00 41.73 C ANISOU 821 C MET A 107 5047 5218 5587 428 -124 -244 C ATOM 822 O MET A 107 22.201 32.090 -8.058 1.00 41.76 O ANISOU 822 O MET A 107 5046 5225 5596 417 -109 -230 O ATOM 823 CB MET A 107 24.457 30.328 -9.034 1.00 42.79 C ANISOU 823 CB MET A 107 5209 5390 5658 497 -168 -317 C ATOM 824 CG MET A 107 25.210 29.072 -9.486 1.00 46.15 C ANISOU 824 CG MET A 107 5659 5813 6061 543 -215 -357 C ATOM 825 SD MET A 107 26.500 29.520 -10.652 1.00 51.13 S ANISOU 825 SD MET A 107 6286 6510 6629 587 -189 -397 S ATOM 826 CE MET A 107 25.570 29.864 -12.149 1.00 47.52 C ANISOU 826 CE MET A 107 5848 6041 6164 587 -207 -395 C ATOM 827 N PHE A 108 23.053 31.431 -6.079 1.00 40.74 N ANISOU 827 N PHE A 108 4913 5096 5469 411 -97 -230 N ATOM 828 CA PHE A 108 22.698 32.654 -5.355 1.00 40.30 C ANISOU 828 CA PHE A 108 4842 5049 5418 385 -42 -203 C ATOM 829 C PHE A 108 23.445 32.729 -4.015 1.00 40.47 C ANISOU 829 C PHE A 108 4864 5082 5429 376 -16 -204 C ATOM 830 O PHE A 108 24.148 31.793 -3.590 1.00 40.29 O ANISOU 830 O PHE A 108 4848 5059 5401 388 -42 -221 O ATOM 831 CB PHE A 108 21.161 32.775 -5.177 1.00 40.72 C ANISOU 831 CB PHE A 108 4886 5070 5515 364 -42 -160 C ATOM 832 CG PHE A 108 20.518 31.569 -4.523 1.00 42.58 C ANISOU 832 CG PHE A 108 5123 5271 5785 357 -81 -137 C ATOM 833 CD1 PHE A 108 20.425 31.471 -3.133 1.00 42.50 C ANISOU 833 CD1 PHE A 108 5106 5256 5783 342 -59 -114 C ATOM 834 CD2 PHE A 108 20.060 30.498 -5.295 1.00 42.93 C ANISOU 834 CD2 PHE A 108 5177 5285 5847 364 -145 -137 C ATOM 835 CE1 PHE A 108 19.872 30.347 -2.537 1.00 43.98 C ANISOU 835 CE1 PHE A 108 5292 5415 6001 332 -98 -89 C ATOM 836 CE2 PHE A 108 19.514 29.367 -4.697 1.00 41.75 C ANISOU 836 CE2 PHE A 108 5030 5103 5730 353 -188 -112 C ATOM 837 CZ PHE A 108 19.412 29.298 -3.317 1.00 42.03 C ANISOU 837 CZ PHE A 108 5054 5138 5777 336 -164 -86 C ATOM 838 N GLU A 109 23.324 33.886 -3.389 1.00 38.18 N ANISOU 838 N GLU A 109 4569 4802 5133 357 32 -188 N ATOM 839 CA GLU A 109 23.962 34.214 -2.160 1.00 39.75 C ANISOU 839 CA GLU A 109 4774 5010 5318 346 59 -186 C ATOM 840 C GLU A 109 22.891 34.559 -1.127 1.00 41.60 C ANISOU 840 C GLU A 109 5008 5221 5574 328 87 -150 C ATOM 841 O GLU A 109 21.889 35.193 -1.429 1.00 42.51 O ANISOU 841 O GLU A 109 5118 5328 5707 324 105 -128 O ATOM 842 CB GLU A 109 24.856 35.417 -2.416 1.00 41.98 C ANISOU 842 CB GLU A 109 5057 5325 5565 341 90 -200 C ATOM 843 CG GLU A 109 25.810 35.753 -1.322 1.00 46.60 C ANISOU 843 CG GLU A 109 5652 5923 6128 329 109 -204 C ATOM 844 CD GLU A 109 26.778 36.853 -1.718 1.00 46.70 C ANISOU 844 CD GLU A 109 5663 5970 6109 320 128 -214 C ATOM 845 OE1 GLU A 109 26.929 37.808 -0.928 1.00 44.81 O ANISOU 845 OE1 GLU A 109 5439 5728 5857 300 155 -203 O ATOM 846 OE2 GLU A 109 27.375 36.777 -2.810 1.00 45.06 O ANISOU 846 OE2 GLU A 109 5442 5791 5886 333 115 -231 O ATOM 847 N LEU A 110 23.155 34.213 0.110 1.00 38.74 N ANISOU 847 N LEU A 110 4656 4854 5209 320 93 -143 N ATOM 848 CA LEU A 110 22.190 34.317 1.169 1.00 39.81 C ANISOU 848 CA LEU A 110 4792 4972 5362 309 117 -108 C ATOM 849 C LEU A 110 22.828 35.082 2.322 1.00 41.41 C ANISOU 849 C LEU A 110 5015 5183 5533 299 154 -112 C ATOM 850 O LEU A 110 24.003 34.849 2.697 1.00 39.17 O ANISOU 850 O LEU A 110 4744 4912 5227 297 142 -134 O ATOM 851 CB LEU A 110 21.824 32.879 1.523 1.00 43.23 C ANISOU 851 CB LEU A 110 5218 5385 5821 307 76 -93 C ATOM 852 CG LEU A 110 20.578 32.503 2.236 1.00 48.75 C ANISOU 852 CG LEU A 110 5906 6066 6551 295 81 -47 C ATOM 853 CD1 LEU A 110 20.348 31.011 2.175 1.00 47.25 C ANISOU 853 CD1 LEU A 110 5709 5853 6388 291 22 -35 C ATOM 854 CD2 LEU A 110 20.777 32.923 3.682 1.00 54.91 C ANISOU 854 CD2 LEU A 110 6700 6852 7309 287 122 -36 C ATOM 855 N LYS A 111 22.056 36.018 2.855 1.00 40.25 N ANISOU 855 N LYS A 111 4876 5031 5386 297 197 -90 N ATOM 856 CA LYS A 111 22.452 36.961 3.893 1.00 41.91 C ANISOU 856 CA LYS A 111 5115 5244 5564 291 235 -92 C ATOM 857 C LYS A 111 21.436 36.967 5.104 1.00 42.67 C ANISOU 857 C LYS A 111 5218 5327 5665 293 268 -58 C ATOM 858 O LYS A 111 20.194 37.133 4.931 1.00 41.20 O ANISOU 858 O LYS A 111 5013 5135 5504 303 288 -28 O ATOM 859 CB LYS A 111 22.509 38.345 3.251 1.00 43.22 C ANISOU 859 CB LYS A 111 5291 5415 5715 293 259 -101 C ATOM 860 CG LYS A 111 22.689 39.473 4.236 1.00 47.99 C ANISOU 860 CG LYS A 111 5932 6012 6287 289 295 -101 C ATOM 861 CD LYS A 111 22.861 40.820 3.564 1.00 49.50 C ANISOU 861 CD LYS A 111 6137 6205 6463 288 308 -111 C ATOM 862 CE LYS A 111 21.607 41.266 2.879 1.00 50.48 C ANISOU 862 CE LYS A 111 6245 6321 6615 303 326 -93 C ATOM 863 NZ LYS A 111 21.835 42.576 2.211 1.00 47.99 N ANISOU 863 NZ LYS A 111 5944 6003 6284 300 334 -103 N ATOM 864 N GLN A 112 21.968 36.789 6.303 1.00 40.40 N ANISOU 864 N GLN A 112 4956 5039 5354 285 275 -59 N ATOM 865 CA GLN A 112 21.281 37.149 7.602 1.00 41.98 C ANISOU 865 CA GLN A 112 5177 5233 5540 290 317 -33 C ATOM 866 C GLN A 112 22.308 37.015 8.735 1.00 40.15 C ANISOU 866 C GLN A 112 4981 5000 5272 277 312 -47 C ATOM 867 O GLN A 112 22.250 36.125 9.578 1.00 41.23 O ANISOU 867 O GLN A 112 5119 5136 5411 269 303 -31 O ATOM 868 CB GLN A 112 20.013 36.317 7.874 1.00 41.55 C ANISOU 868 CB GLN A 112 5091 5177 5519 295 322 9 C ATOM 869 CG GLN A 112 19.365 36.531 9.215 1.00 43.84 C ANISOU 869 CG GLN A 112 5397 5469 5791 302 367 38 C ATOM 870 CD GLN A 112 19.438 37.967 9.723 1.00 50.21 C ANISOU 870 CD GLN A 112 6247 6273 6557 320 416 24 C ATOM 871 OE1 GLN A 112 20.002 38.242 10.786 1.00 60.64 O ANISOU 871 OE1 GLN A 112 7611 7591 7837 317 429 14 O ATOM 872 NE2 GLN A 112 18.843 38.869 9.001 1.00 49.25 N ANISOU 872 NE2 GLN A 112 6117 6149 6444 337 438 25 N ATOM 873 N ALA A 113 23.262 37.932 8.682 1.00 39.48 N ANISOU 873 N ALA A 113 4926 4916 5156 271 314 -75 N ATOM 874 CA ALA A 113 24.452 37.908 9.483 1.00 39.85 C ANISOU 874 CA ALA A 113 5005 4962 5171 254 298 -92 C ATOM 875 C ALA A 113 24.955 36.453 9.669 1.00 39.94 C ANISOU 875 C ALA A 113 4996 4978 5199 243 256 -91 C ATOM 876 O ALA A 113 24.984 35.713 8.688 1.00 42.22 O ANISOU 876 O ALA A 113 5249 5274 5518 247 226 -96 O ATOM 877 CB ALA A 113 24.201 38.664 10.773 1.00 41.45 C ANISOU 877 CB ALA A 113 5258 5152 5336 257 335 -83 C ATOM 878 N CYS A 114 25.249 36.011 10.893 1.00 40.10 N ANISOU 878 N CYS A 114 5040 4992 5201 232 253 -83 N ATOM 879 CA CYS A 114 25.867 34.693 11.130 1.00 40.60 C ANISOU 879 CA CYS A 114 5089 5056 5277 221 208 -84 C ATOM 880 C CYS A 114 24.916 33.520 11.039 1.00 41.30 C ANISOU 880 C CYS A 114 5147 5140 5403 225 194 -58 C ATOM 881 O CYS A 114 25.344 32.369 11.105 1.00 41.25 O ANISOU 881 O CYS A 114 5129 5130 5413 218 150 -59 O ATOM 882 CB CYS A 114 26.569 34.684 12.488 1.00 46.63 C ANISOU 882 CB CYS A 114 5894 5814 6008 204 205 -83 C ATOM 883 SG CYS A 114 27.838 35.981 12.622 1.00 50.40 S ANISOU 883 SG CYS A 114 6411 6293 6443 190 206 -109 S ATOM 884 N TYR A 115 23.638 33.805 10.814 1.00 39.23 N ANISOU 884 N TYR A 115 4870 4877 5157 237 225 -33 N ATOM 885 CA TYR A 115 22.664 32.765 10.567 1.00 40.40 C ANISOU 885 CA TYR A 115 4983 5021 5346 237 207 -2 C ATOM 886 C TYR A 115 22.716 32.259 9.111 1.00 40.48 C ANISOU 886 C TYR A 115 4961 5028 5389 244 166 -17 C ATOM 887 O TYR A 115 22.135 31.217 8.783 1.00 43.32 O ANISOU 887 O TYR A 115 5297 5378 5784 241 131 2 O ATOM 888 CB TYR A 115 21.263 33.311 10.925 1.00 41.31 C ANISOU 888 CB TYR A 115 5090 5140 5465 247 258 36 C ATOM 889 CG TYR A 115 20.110 32.372 10.633 1.00 44.42 C ANISOU 889 CG TYR A 115 5441 5531 5903 244 241 79 C ATOM 890 CD1 TYR A 115 19.991 31.173 11.282 1.00 44.24 C ANISOU 890 CD1 TYR A 115 5410 5504 5895 226 209 107 C ATOM 891 CD2 TYR A 115 19.124 32.714 9.708 1.00 46.62 C ANISOU 891 CD2 TYR A 115 5689 5812 6212 256 253 96 C ATOM 892 CE1 TYR A 115 18.940 30.312 11.017 1.00 46.94 C ANISOU 892 CE1 TYR A 115 5713 5840 6278 217 186 152 C ATOM 893 CE2 TYR A 115 18.052 31.875 9.443 1.00 47.13 C ANISOU 893 CE2 TYR A 115 5714 5874 6320 248 232 142 C ATOM 894 CZ TYR A 115 17.959 30.670 10.102 1.00 49.91 C ANISOU 894 CZ TYR A 115 6058 6220 6685 227 198 171 C ATOM 895 OH TYR A 115 16.921 29.812 9.801 1.00 45.41 O ANISOU 895 OH TYR A 115 5448 5644 6160 214 168 221 O ATOM 896 N SER A 116 23.411 32.981 8.228 1.00 40.82 N ANISOU 896 N SER A 116 5008 5080 5421 253 167 -52 N ATOM 897 CA SER A 116 23.381 32.691 6.795 1.00 38.63 C ANISOU 897 CA SER A 116 4705 4804 5168 264 137 -67 C ATOM 898 C SER A 116 23.701 31.220 6.486 1.00 37.72 C ANISOU 898 C SER A 116 4578 4678 5076 265 76 -73 C ATOM 899 O SER A 116 23.032 30.591 5.693 1.00 36.71 O ANISOU 899 O SER A 116 4431 4539 4978 270 47 -64 O ATOM 900 CB SER A 116 24.372 33.590 6.067 1.00 41.24 C ANISOU 900 CB SER A 116 5042 5151 5473 270 143 -103 C ATOM 901 OG SER A 116 25.730 33.303 6.507 1.00 44.73 O ANISOU 901 OG SER A 116 5498 5602 5893 264 122 -126 O ATOM 902 N GLY A 117 24.745 30.679 7.078 1.00 38.61 N ANISOU 902 N GLY A 117 4703 4791 5172 260 52 -90 N ATOM 903 CA GLY A 117 25.145 29.286 6.813 1.00 38.98 C ANISOU 903 CA GLY A 117 4745 4825 5239 266 -8 -100 C ATOM 904 C GLY A 117 24.043 28.280 7.054 1.00 40.55 C ANISOU 904 C GLY A 117 4934 4999 5473 256 -36 -62 C ATOM 905 O GLY A 117 23.759 27.446 6.203 1.00 41.54 O ANISOU 905 O GLY A 117 5049 5108 5624 265 -83 -65 O ATOM 906 N THR A 118 23.432 28.353 8.228 1.00 42.58 N ANISOU 906 N THR A 118 5196 5254 5728 236 -10 -25 N ATOM 907 CA THR A 118 22.360 27.446 8.612 1.00 42.48 C ANISOU 907 CA THR A 118 5169 5223 5747 220 -33 21 C ATOM 908 C THR A 118 21.166 27.598 7.682 1.00 42.62 C ANISOU 908 C THR A 118 5161 5236 5795 224 -31 44 C ATOM 909 O THR A 118 20.542 26.609 7.246 1.00 41.91 O ANISOU 909 O THR A 118 5057 5124 5741 216 -82 67 O ATOM 910 CB THR A 118 21.962 27.718 10.073 1.00 42.27 C ANISOU 910 CB THR A 118 5151 5204 5702 202 8 58 C ATOM 911 OG1 THR A 118 23.044 27.327 10.928 1.00 44.50 O ANISOU 911 OG1 THR A 118 5460 5485 5962 194 -10 40 O ATOM 912 CG2 THR A 118 20.685 26.988 10.468 1.00 44.22 C ANISOU 912 CG2 THR A 118 5375 5443 5981 183 -2 118 C ATOM 913 N ALA A 119 20.875 28.833 7.309 1.00 41.14 N ANISOU 913 N ALA A 119 4969 5066 5595 235 21 39 N ATOM 914 CA ALA A 119 19.750 29.041 6.383 1.00 44.08 C ANISOU 914 CA ALA A 119 5315 5435 5999 239 23 62 C ATOM 915 C ALA A 119 20.034 28.341 5.045 1.00 40.87 C ANISOU 915 C ALA A 119 4907 5011 5611 249 -38 34 C ATOM 916 O ALA A 119 19.187 27.646 4.489 1.00 41.58 O ANISOU 916 O ALA A 119 4980 5080 5736 242 -79 61 O ATOM 917 CB ALA A 119 19.469 30.517 6.179 1.00 44.15 C ANISOU 917 CB ALA A 119 5322 5462 5989 251 87 56 C ATOM 918 N GLY A 120 21.259 28.477 4.575 1.00 40.66 N ANISOU 918 N GLY A 120 4897 4992 5558 266 -47 -17 N ATOM 919 CA GLY A 120 21.691 27.824 3.345 1.00 39.13 C ANISOU 919 CA GLY A 120 4708 4787 5372 284 -102 -50 C ATOM 920 C GLY A 120 21.623 26.314 3.478 1.00 40.34 C ANISOU 920 C GLY A 120 4868 4908 5549 279 -172 -41 C ATOM 921 O GLY A 120 21.127 25.632 2.579 1.00 40.75 O ANISOU 921 O GLY A 120 4920 4936 5626 284 -224 -38 O ATOM 922 N LEU A 121 22.104 25.783 4.600 1.00 41.01 N ANISOU 922 N LEU A 121 4962 4989 5627 268 -181 -34 N ATOM 923 CA LEU A 121 22.024 24.327 4.837 1.00 43.32 C ANISOU 923 CA LEU A 121 5265 5249 5946 260 -253 -21 C ATOM 924 C LEU A 121 20.574 23.855 4.833 1.00 41.56 C ANISOU 924 C LEU A 121 5024 5002 5763 234 -277 37 C ATOM 925 O LEU A 121 20.230 22.848 4.249 1.00 44.21 O ANISOU 925 O LEU A 121 5366 5304 6126 232 -347 44 O ATOM 926 CB LEU A 121 22.668 23.970 6.168 1.00 42.16 C ANISOU 926 CB LEU A 121 5128 5103 5784 246 -250 -15 C ATOM 927 CG LEU A 121 22.544 22.528 6.654 1.00 42.79 C ANISOU 927 CG LEU A 121 5219 5148 5890 231 -322 7 C ATOM 928 CD1 LEU A 121 23.054 21.554 5.622 1.00 42.23 C ANISOU 928 CD1 LEU A 121 5167 5048 5830 259 -397 -31 C ATOM 929 CD2 LEU A 121 23.329 22.381 7.939 1.00 43.10 C ANISOU 929 CD2 LEU A 121 5271 5195 5910 219 -312 7 C ATOM 930 N GLN A 122 19.708 24.603 5.468 1.00 41.21 N ANISOU 930 N GLN A 122 4958 4977 5723 214 -220 81 N ATOM 931 CA GLN A 122 18.292 24.170 5.514 1.00 43.62 C ANISOU 931 CA GLN A 122 5237 5267 6069 188 -240 146 C ATOM 932 C GLN A 122 17.632 24.196 4.157 1.00 44.94 C ANISOU 932 C GLN A 122 5393 5418 6261 195 -270 147 C ATOM 933 O GLN A 122 16.842 23.308 3.835 1.00 47.14 O ANISOU 933 O GLN A 122 5665 5667 6578 175 -332 184 O ATOM 934 CB GLN A 122 17.534 25.013 6.515 1.00 43.04 C ANISOU 934 CB GLN A 122 5138 5223 5989 174 -165 193 C ATOM 935 CG GLN A 122 18.047 24.767 7.913 1.00 43.35 C ANISOU 935 CG GLN A 122 5192 5273 6006 161 -149 202 C ATOM 936 CD GLN A 122 17.761 23.343 8.393 1.00 47.01 C ANISOU 936 CD GLN A 122 5654 5709 6498 132 -218 243 C ATOM 937 OE1 GLN A 122 16.771 22.709 7.977 1.00 49.74 O ANISOU 937 OE1 GLN A 122 5977 6035 6884 113 -262 289 O ATOM 938 NE2 GLN A 122 18.607 22.843 9.281 1.00 45.83 N ANISOU 938 NE2 GLN A 122 5528 5555 6329 126 -233 229 N ATOM 939 N MET A 123 17.964 25.192 3.336 1.00 44.72 N ANISOU 939 N MET A 123 5369 5409 6212 220 -232 107 N ATOM 940 CA MET A 123 17.438 25.237 1.956 1.00 42.97 C ANISOU 940 CA MET A 123 5143 5172 6010 228 -263 101 C ATOM 941 C MET A 123 17.931 24.023 1.143 1.00 43.45 C ANISOU 941 C MET A 123 5235 5196 6077 240 -352 69 C ATOM 942 O MET A 123 17.195 23.448 0.345 1.00 40.89 O ANISOU 942 O MET A 123 4911 4840 5781 232 -410 88 O ATOM 943 CB MET A 123 17.862 26.535 1.259 1.00 45.48 C ANISOU 943 CB MET A 123 5462 5519 6298 252 -207 61 C ATOM 944 CG MET A 123 17.314 27.840 1.819 1.00 45.27 C ANISOU 944 CG MET A 123 5412 5522 6264 247 -125 87 C ATOM 945 SD MET A 123 15.524 27.843 2.105 1.00 49.78 S ANISOU 945 SD MET A 123 5941 6088 6883 222 -116 171 S ATOM 946 CE MET A 123 15.387 27.492 3.865 1.00 54.32 C ANISOU 946 CE MET A 123 6507 6676 7454 203 -87 214 C ATOM 947 N ALA A 124 19.173 23.608 1.383 1.00 43.53 N ANISOU 947 N ALA A 124 5271 5207 6059 261 -366 21 N ATOM 948 CA ALA A 124 19.755 22.468 0.675 1.00 43.61 C ANISOU 948 CA ALA A 124 5315 5184 6070 283 -446 -15 C ATOM 949 C ALA A 124 19.079 21.168 1.083 1.00 43.29 C ANISOU 949 C ALA A 124 5282 5097 6068 255 -524 28 C ATOM 950 O ALA A 124 18.727 20.323 0.260 1.00 46.54 O ANISOU 950 O ALA A 124 5715 5467 6499 258 -601 27 O ATOM 951 CB ALA A 124 21.237 22.408 0.935 1.00 43.14 C ANISOU 951 CB ALA A 124 5274 5142 5972 313 -435 -70 C ATOM 952 N ILE A 125 18.886 21.033 2.374 1.00 45.40 N ANISOU 952 N ILE A 125 5533 5372 6344 225 -504 69 N ATOM 953 CA ILE A 125 18.164 19.915 2.938 1.00 46.22 C ANISOU 953 CA ILE A 125 5636 5439 6486 189 -569 124 C ATOM 954 C ILE A 125 16.803 19.821 2.291 1.00 47.08 C ANISOU 954 C ILE A 125 5725 5528 6634 163 -600 177 C ATOM 955 O ILE A 125 16.420 18.747 1.839 1.00 49.61 O ANISOU 955 O ILE A 125 6065 5800 6983 151 -692 194 O ATOM 956 CB ILE A 125 18.042 20.059 4.470 1.00 47.34 C ANISOU 956 CB ILE A 125 5755 5604 6624 159 -523 169 C ATOM 957 CG1 ILE A 125 19.367 19.700 5.125 1.00 45.80 C ANISOU 957 CG1 ILE A 125 5588 5412 6400 177 -528 124 C ATOM 958 CG2 ILE A 125 16.910 19.195 5.056 1.00 50.08 C ANISOU 958 CG2 ILE A 125 6083 5927 7015 111 -571 250 C ATOM 959 CD1 ILE A 125 19.503 20.255 6.535 1.00 48.52 C ANISOU 959 CD1 ILE A 125 5917 5791 6725 158 -460 149 C ATOM 960 N ASN A 126 16.074 20.927 2.236 1.00 46.85 N ANISOU 960 N ASN A 126 5659 5533 6608 156 -531 205 N ATOM 961 CA ASN A 126 14.748 20.897 1.608 1.00 48.16 C ANISOU 961 CA ASN A 126 5799 5682 6815 131 -559 261 C ATOM 962 C ASN A 126 14.724 20.594 0.112 1.00 49.26 C ANISOU 962 C ASN A 126 5967 5786 6960 149 -624 227 C ATOM 963 O ASN A 126 13.707 20.101 -0.399 1.00 49.34 O ANISOU 963 O ASN A 126 5970 5765 7010 122 -684 275 O ATOM 964 CB ASN A 126 13.971 22.179 1.900 1.00 48.01 C ANISOU 964 CB ASN A 126 5733 5709 6799 124 -467 299 C ATOM 965 CG ASN A 126 13.649 22.322 3.378 1.00 49.14 C ANISOU 965 CG ASN A 126 5846 5882 6942 102 -414 351 C ATOM 966 OD1 ASN A 126 13.824 21.387 4.157 1.00 52.58 O ANISOU 966 OD1 ASN A 126 6290 6303 7384 82 -453 371 O ATOM 967 ND2 ASN A 126 13.223 23.497 3.777 1.00 48.25 N ANISOU 967 ND2 ASN A 126 5701 5811 6817 109 -325 369 N ATOM 968 N LEU A 127 15.813 20.912 -0.597 1.00 46.90 N ANISOU 968 N LEU A 127 5702 5496 6621 194 -611 148 N ATOM 969 CA LEU A 127 15.942 20.501 -1.983 1.00 47.14 C ANISOU 969 CA LEU A 127 5770 5493 6647 218 -676 109 C ATOM 970 C LEU A 127 15.950 18.960 -2.130 1.00 46.22 C ANISOU 970 C LEU A 127 5695 5315 6550 211 -790 111 C ATOM 971 O LEU A 127 15.252 18.412 -2.973 1.00 46.18 O ANISOU 971 O LEU A 127 5709 5267 6570 200 -864 129 O ATOM 972 CB LEU A 127 17.200 21.077 -2.621 1.00 46.18 C ANISOU 972 CB LEU A 127 5673 5399 6474 269 -637 27 C ATOM 973 CG LEU A 127 17.571 20.520 -3.993 1.00 48.22 C ANISOU 973 CG LEU A 127 5980 5626 6715 305 -704 -24 C ATOM 974 CD1 LEU A 127 16.527 20.933 -5.011 1.00 53.04 C ANISOU 974 CD1 LEU A 127 6583 6224 7345 291 -719 1 C ATOM 975 CD2 LEU A 127 18.920 21.023 -4.448 1.00 49.78 C ANISOU 975 CD2 LEU A 127 6194 5860 6858 358 -660 -98 C ATOM 976 N ILE A 128 16.774 18.294 -1.332 1.00 47.50 N ANISOU 976 N ILE A 128 5876 5470 6700 220 -805 91 N ATOM 977 CA ILE A 128 16.851 16.840 -1.336 1.00 49.01 C ANISOU 977 CA ILE A 128 6110 5601 6909 215 -913 93 C ATOM 978 C ILE A 128 15.493 16.259 -0.900 1.00 52.79 C ANISOU 978 C ILE A 128 6564 6048 7443 152 -967 185 C ATOM 979 O ILE A 128 14.954 15.409 -1.582 1.00 50.13 O ANISOU 979 O ILE A 128 6258 5656 7133 139 -1064 201 O ATOM 980 CB ILE A 128 17.925 16.315 -0.365 1.00 51.22 C ANISOU 980 CB ILE A 128 6405 5884 7171 230 -912 65 C ATOM 981 CG1 ILE A 128 19.328 16.889 -0.638 1.00 50.16 C ANISOU 981 CG1 ILE A 128 6284 5788 6983 288 -856 -16 C ATOM 982 CG2 ILE A 128 17.922 14.786 -0.339 1.00 54.70 C ANISOU 982 CG2 ILE A 128 6891 6256 7633 223 -1031 71 C ATOM 983 CD1 ILE A 128 19.680 17.202 -2.057 1.00 52.36 C ANISOU 983 CD1 ILE A 128 6590 6070 7235 336 -859 -74 C ATOM 984 N LEU A 129 14.929 16.754 0.209 1.00 50.36 N ANISOU 984 N LEU A 129 6203 5779 7153 114 -904 247 N ATOM 985 CA LEU A 129 13.657 16.247 0.711 1.00 51.48 C ANISOU 985 CA LEU A 129 6311 5902 7346 53 -945 343 C ATOM 986 C LEU A 129 12.455 16.541 -0.163 1.00 55.33 C ANISOU 986 C LEU A 129 6774 6380 7867 30 -966 390 C ATOM 987 O LEU A 129 11.491 15.782 -0.134 1.00 57.10 O ANISOU 987 O LEU A 129 6988 6569 8138 -16 -1041 462 O ATOM 988 CB LEU A 129 13.354 16.788 2.088 1.00 52.13 C ANISOU 988 CB LEU A 129 6339 6036 7429 26 -862 397 C ATOM 989 CG LEU A 129 14.283 16.296 3.181 1.00 53.31 C ANISOU 989 CG LEU A 129 6507 6188 7557 30 -858 377 C ATOM 990 CD1 LEU A 129 14.012 17.098 4.437 1.00 53.09 C ANISOU 990 CD1 LEU A 129 6431 6220 7520 11 -759 421 C ATOM 991 CD2 LEU A 129 14.058 14.818 3.442 1.00 55.56 C ANISOU 991 CD2 LEU A 129 6817 6416 7876 -4 -972 416 C ATOM 992 N SER A 130 12.487 17.631 -0.924 1.00 53.56 N ANISOU 992 N SER A 130 6541 6186 7623 60 -903 355 N ATOM 993 CA SER A 130 11.434 17.883 -1.894 1.00 54.53 C ANISOU 993 CA SER A 130 6647 6294 7776 42 -931 392 C ATOM 994 C SER A 130 11.261 16.737 -2.903 1.00 57.04 C ANISOU 994 C SER A 130 7021 6537 8111 36 -1062 384 C ATOM 995 O SER A 130 10.220 16.600 -3.506 1.00 54.46 O ANISOU 995 O SER A 130 6683 6186 7823 4 -1114 437 O ATOM 996 CB SER A 130 11.716 19.162 -2.693 1.00 53.19 C ANISOU 996 CB SER A 130 6473 6162 7574 81 -854 341 C ATOM 997 OG SER A 130 12.752 18.958 -3.650 1.00 49.55 O ANISOU 997 OG SER A 130 6073 5680 7073 129 -885 253 O ATOM 998 N GLN A 131 12.326 15.993 -3.150 1.00 61.83 N ANISOU 998 N GLN A 131 7693 7112 8688 72 -1113 313 N ATOM 999 CA GLN A 131 12.367 15.003 -4.234 1.00 67.23 C ANISOU 999 CA GLN A 131 8445 7724 9373 85 -1231 284 C ATOM 1000 C GLN A 131 11.952 15.536 -5.595 1.00 63.55 C ANISOU 1000 C GLN A 131 7993 7250 8901 99 -1241 265 C ATOM 1001 O GLN A 131 11.506 14.777 -6.440 1.00 61.26 O ANISOU 1001 O GLN A 131 7748 6898 8627 89 -1346 272 O ATOM 1002 CB GLN A 131 11.589 13.727 -3.866 1.00 68.77 C ANISOU 1002 CB GLN A 131 8652 7857 9619 29 -1347 356 C ATOM 1003 CG GLN A 131 12.376 12.783 -2.949 1.00 74.32 C ANISOU 1003 CG GLN A 131 9384 8539 10315 34 -1383 339 C ATOM 1004 CD GLN A 131 13.844 12.537 -3.381 1.00 81.28 C ANISOU 1004 CD GLN A 131 10331 9410 11140 109 -1386 229 C ATOM 1005 OE1 GLN A 131 14.741 13.397 -3.212 1.00 86.75 O ANISOU 1005 OE1 GLN A 131 11007 10160 11790 152 -1286 173 O ATOM 1006 NE2 GLN A 131 14.101 11.348 -3.918 1.00 79.29 N ANISOU 1006 NE2 GLN A 131 10152 9084 10887 125 -1505 199 N ATOM 1007 N THR A 132 12.171 16.824 -5.843 1.00 58.76 N ANISOU 1007 N THR A 132 7355 6703 8267 125 -1137 238 N ATOM 1008 CA THR A 132 11.940 17.359 -7.185 1.00 57.65 C ANISOU 1008 CA THR A 132 7233 6556 8112 144 -1144 211 C ATOM 1009 C THR A 132 12.954 16.816 -8.221 1.00 58.94 C ANISOU 1009 C THR A 132 7480 6688 8227 203 -1198 119 C ATOM 1010 O THR A 132 12.629 16.697 -9.409 1.00 59.32 O ANISOU 1010 O THR A 132 7567 6702 8268 212 -1255 104 O ATOM 1011 CB THR A 132 11.927 18.906 -7.209 1.00 55.25 C ANISOU 1011 CB THR A 132 6876 6322 7792 156 -1022 205 C ATOM 1012 OG1 THR A 132 13.058 19.431 -6.504 1.00 53.67 O ANISOU 1012 OG1 THR A 132 6668 6172 7550 190 -935 155 O ATOM 1013 CG2 THR A 132 10.671 19.422 -6.572 1.00 55.05 C ANISOU 1013 CG2 THR A 132 6778 6318 7818 103 -987 299 C ATOM 1014 N PHE A 133 14.167 16.507 -7.776 1.00 56.73 N ANISOU 1014 N PHE A 133 7529 6055 7970 191 -1119 478 N ATOM 1015 CA PHE A 133 15.240 16.042 -8.662 1.00 58.10 C ANISOU 1015 CA PHE A 133 7847 6243 7982 193 -1108 456 C ATOM 1016 C PHE A 133 16.104 15.017 -7.947 1.00 57.43 C ANISOU 1016 C PHE A 133 7821 6192 7806 270 -1011 393 C ATOM 1017 O PHE A 133 17.227 15.310 -7.554 1.00 58.37 O ANISOU 1017 O PHE A 133 7928 6369 7880 340 -931 341 O ATOM 1018 CB PHE A 133 16.098 17.218 -9.145 1.00 59.03 C ANISOU 1018 CB PHE A 133 7953 6402 8071 196 -1101 448 C ATOM 1019 CG PHE A 133 15.295 18.279 -9.796 1.00 62.61 C ANISOU 1019 CG PHE A 133 8360 6807 8622 123 -1220 515 C ATOM 1020 CD1 PHE A 133 14.630 18.006 -10.998 1.00 67.71 C ANISOU 1020 CD1 PHE A 133 9097 7385 9242 20 -1346 574 C ATOM 1021 CD2 PHE A 133 15.099 19.503 -9.177 1.00 62.72 C ANISOU 1021 CD2 PHE A 133 8239 6826 8764 154 -1222 521 C ATOM 1022 CE1 PHE A 133 13.821 18.962 -11.595 1.00 69.60 C ANISOU 1022 CE1 PHE A 133 9296 7560 9587 -49 -1488 644 C ATOM 1023 CE2 PHE A 133 14.289 20.465 -9.766 1.00 65.40 C ANISOU 1023 CE2 PHE A 133 8532 7099 9217 95 -1358 583 C ATOM 1024 CZ PHE A 133 13.655 20.199 -10.975 1.00 66.27 C ANISOU 1024 CZ PHE A 133 8734 7138 9307 -6 -1498 647 C ATOM 1025 N PRO A 134 15.582 13.798 -7.795 1.00 57.43 N ANISOU 1025 N PRO A 134 7890 6148 7781 252 -1029 399 N ATOM 1026 CA PRO A 134 16.318 12.727 -7.127 1.00 57.76 C ANISOU 1026 CA PRO A 134 8006 6195 7744 320 -968 345 C ATOM 1027 C PRO A 134 17.737 12.613 -7.649 1.00 54.27 C ANISOU 1027 C PRO A 134 7633 5788 7197 384 -922 278 C ATOM 1028 O PRO A 134 17.942 12.687 -8.841 1.00 55.00 O ANISOU 1028 O PRO A 134 7792 5876 7227 340 -951 273 O ATOM 1029 CB PRO A 134 15.509 11.465 -7.485 1.00 61.36 C ANISOU 1029 CB PRO A 134 8570 6577 8164 259 -1035 373 C ATOM 1030 CG PRO A 134 14.117 11.951 -7.781 1.00 59.87 C ANISOU 1030 CG PRO A 134 8307 6361 8079 163 -1110 444 C ATOM 1031 CD PRO A 134 14.270 13.350 -8.317 1.00 60.20 C ANISOU 1031 CD PRO A 134 8263 6432 8175 158 -1127 459 C ATOM 1032 N GLY A 135 18.707 12.476 -6.757 1.00 54.67 N ANISOU 1032 N GLY A 135 7662 5876 7231 479 -852 222 N ATOM 1033 CA GLY A 135 20.113 12.391 -7.155 1.00 55.74 C ANISOU 1033 CA GLY A 135 7833 6055 7290 549 -800 141 C ATOM 1034 C GLY A 135 20.824 13.750 -7.074 1.00 57.47 C ANISOU 1034 C GLY A 135 7947 6358 7529 568 -744 127 C ATOM 1035 O GLY A 135 22.051 13.806 -7.016 1.00 52.28 O ANISOU 1035 O GLY A 135 7278 5754 6829 637 -684 54 O ATOM 1036 N ALA A 136 20.069 14.852 -7.105 1.00 53.38 N ANISOU 1036 N ALA A 136 7351 5847 7082 506 -770 190 N ATOM 1037 CA ALA A 136 20.695 16.173 -7.024 1.00 52.19 C ANISOU 1037 CA ALA A 136 7114 5764 6949 515 -730 182 C ATOM 1038 C ALA A 136 21.419 16.375 -5.698 1.00 50.51 C ANISOU 1038 C ALA A 136 6825 5599 6765 605 -657 146 C ATOM 1039 O ALA A 136 20.973 15.928 -4.644 1.00 52.98 O ANISOU 1039 O ALA A 136 7119 5886 7124 630 -651 158 O ATOM 1040 CB ALA A 136 19.664 17.265 -7.238 1.00 53.74 C ANISOU 1040 CB ALA A 136 7244 5936 7237 441 -793 256 C ATOM 1041 N LYS A 137 22.582 16.995 -5.770 1.00 48.43 N ANISOU 1041 N LYS A 137 6530 5408 6462 640 -602 99 N ATOM 1042 CA LYS A 137 23.274 17.445 -4.575 1.00 48.88 C ANISOU 1042 CA LYS A 137 6507 5514 6549 710 -544 74 C ATOM 1043 C LYS A 137 23.296 18.963 -4.540 1.00 47.36 C ANISOU 1043 C LYS A 137 6231 5364 6397 674 -531 102 C ATOM 1044 O LYS A 137 23.008 19.630 -5.547 1.00 48.99 O ANISOU 1044 O LYS A 137 6451 5566 6594 600 -571 131 O ATOM 1045 CB LYS A 137 24.701 16.956 -4.569 1.00 48.09 C ANISOU 1045 CB LYS A 137 6422 5465 6384 788 -494 -9 C ATOM 1046 CG LYS A 137 24.838 15.442 -4.735 1.00 50.90 C ANISOU 1046 CG LYS A 137 6868 5767 6702 836 -518 -53 C ATOM 1047 CD LYS A 137 26.323 15.127 -4.818 1.00 52.85 C ANISOU 1047 CD LYS A 137 7100 6068 6909 921 -470 -154 C ATOM 1048 CE LYS A 137 26.581 13.706 -5.292 1.00 54.03 C ANISOU 1048 CE LYS A 137 7341 6162 7025 972 -495 -221 C ATOM 1049 NZ LYS A 137 25.946 12.725 -4.397 1.00 51.33 N ANISOU 1049 NZ LYS A 137 7059 5726 6716 1004 -560 -180 N ATOM 1050 N ALA A 138 23.651 19.495 -3.383 1.00 44.73 N ANISOU 1050 N ALA A 138 5826 5065 6105 718 -485 94 N ATOM 1051 CA ALA A 138 23.824 20.946 -3.232 1.00 46.91 C ANISOU 1051 CA ALA A 138 6025 5379 6416 694 -468 110 C ATOM 1052 C ALA A 138 25.144 21.253 -2.568 1.00 42.98 C ANISOU 1052 C ALA A 138 5491 4959 5880 752 -403 61 C ATOM 1053 O ALA A 138 25.579 20.533 -1.712 1.00 44.78 O ANISOU 1053 O ALA A 138 5722 5191 6099 815 -378 33 O ATOM 1054 CB ALA A 138 22.681 21.536 -2.424 1.00 44.59 C ANISOU 1054 CB ALA A 138 5665 5041 6236 674 -481 152 C ATOM 1055 N LEU A 139 25.779 22.333 -2.975 1.00 43.78 N ANISOU 1055 N LEU A 139 5560 5116 5956 722 -387 56 N ATOM 1056 CA LEU A 139 27.017 22.762 -2.346 1.00 43.04 C ANISOU 1056 CA LEU A 139 5419 5102 5832 765 -328 13 C ATOM 1057 C LEU A 139 26.723 24.084 -1.598 1.00 42.41 C ANISOU 1057 C LEU A 139 5275 5022 5815 742 -322 50 C ATOM 1058 O LEU A 139 26.266 25.072 -2.197 1.00 41.06 O ANISOU 1058 O LEU A 139 5099 4833 5669 677 -360 87 O ATOM 1059 CB LEU A 139 28.070 22.927 -3.428 1.00 44.47 C ANISOU 1059 CB LEU A 139 5616 5357 5921 736 -304 -34 C ATOM 1060 CG LEU A 139 29.435 23.389 -2.987 1.00 45.87 C ANISOU 1060 CG LEU A 139 5734 5630 6063 768 -244 -88 C ATOM 1061 CD1 LEU A 139 30.113 22.257 -2.244 1.00 48.76 C ANISOU 1061 CD1 LEU A 139 6085 6004 6437 874 -224 -145 C ATOM 1062 CD2 LEU A 139 30.244 23.781 -4.190 1.00 47.26 C ANISOU 1062 CD2 LEU A 139 5923 5884 6148 698 -215 -132 C ATOM 1063 N VAL A 140 26.912 24.075 -0.283 1.00 42.15 N ANISOU 1063 N VAL A 140 5205 4997 5813 789 -285 40 N ATOM 1064 CA VAL A 140 26.633 25.238 0.549 1.00 42.25 C ANISOU 1064 CA VAL A 140 5162 5006 5885 770 -267 61 C ATOM 1065 C VAL A 140 27.950 25.701 1.125 1.00 41.71 C ANISOU 1065 C VAL A 140 5065 5016 5766 795 -222 30 C ATOM 1066 O VAL A 140 28.652 24.894 1.743 1.00 43.82 O ANISOU 1066 O VAL A 140 5340 5309 6000 850 -204 0 O ATOM 1067 CB VAL A 140 25.664 24.889 1.696 1.00 46.88 C ANISOU 1067 CB VAL A 140 5734 5536 6541 778 -251 70 C ATOM 1068 CG1 VAL A 140 25.485 26.098 2.613 1.00 50.19 C ANISOU 1068 CG1 VAL A 140 6093 5956 7017 760 -215 70 C ATOM 1069 CG2 VAL A 140 24.294 24.485 1.139 1.00 47.70 C ANISOU 1069 CG2 VAL A 140 5848 5566 6708 746 -296 98 C ATOM 1070 N ILE A 141 28.327 26.958 0.886 1.00 37.84 N ANISOU 1070 N ILE A 141 4546 4561 5269 754 -219 39 N ATOM 1071 CA ILE A 141 29.607 27.435 1.383 1.00 38.61 C ANISOU 1071 CA ILE A 141 4613 4741 5316 767 -179 11 C ATOM 1072 C ILE A 141 29.422 28.697 2.187 1.00 39.55 C ANISOU 1072 C ILE A 141 4700 4849 5478 738 -166 32 C ATOM 1073 O ILE A 141 28.961 29.716 1.662 1.00 38.24 O ANISOU 1073 O ILE A 141 4532 4654 5343 685 -197 60 O ATOM 1074 CB ILE A 141 30.633 27.706 0.272 1.00 40.69 C ANISOU 1074 CB ILE A 141 4879 5085 5495 731 -173 -15 C ATOM 1075 CG1 ILE A 141 30.747 26.507 -0.657 1.00 43.46 C ANISOU 1075 CG1 ILE A 141 5265 5441 5805 751 -179 -50 C ATOM 1076 CG2 ILE A 141 32.000 27.939 0.891 1.00 42.33 C ANISOU 1076 CG2 ILE A 141 5038 5384 5659 756 -130 -55 C ATOM 1077 CD1 ILE A 141 31.436 26.800 -1.968 1.00 45.87 C ANISOU 1077 CD1 ILE A 141 5587 5816 6023 681 -166 -80 C ATOM 1078 N ALA A 142 29.783 28.638 3.465 1.00 39.41 N ANISOU 1078 N ALA A 142 4665 4845 5463 769 -129 19 N ATOM 1079 CA ALA A 142 29.782 29.847 4.311 1.00 38.76 C ANISOU 1079 CA ALA A 142 4556 4760 5407 739 -105 26 C ATOM 1080 C ALA A 142 31.182 30.398 4.337 1.00 38.69 C ANISOU 1080 C ALA A 142 4531 4843 5326 728 -91 13 C ATOM 1081 O ALA A 142 32.147 29.657 4.623 1.00 38.34 O ANISOU 1081 O ALA A 142 4478 4854 5232 769 -81 -13 O ATOM 1082 CB ALA A 142 29.338 29.498 5.695 1.00 39.71 C ANISOU 1082 CB ALA A 142 4682 4846 5558 753 -69 18 C ATOM 1083 N THR A 143 31.302 31.668 3.977 1.00 36.76 N ANISOU 1083 N THR A 143 4280 4607 5079 672 -102 28 N ATOM 1084 CA THR A 143 32.590 32.309 3.832 1.00 40.58 C ANISOU 1084 CA THR A 143 4748 5183 5487 639 -90 18 C ATOM 1085 C THR A 143 32.489 33.752 4.269 1.00 40.68 C ANISOU 1085 C THR A 143 4763 5172 5519 586 -95 39 C ATOM 1086 O THR A 143 31.556 34.452 3.913 1.00 44.56 O ANISOU 1086 O THR A 143 5272 5585 6073 556 -132 63 O ATOM 1087 CB THR A 143 33.099 32.239 2.367 1.00 40.11 C ANISOU 1087 CB THR A 143 4698 5180 5360 596 -108 9 C ATOM 1088 OG1 THR A 143 34.343 32.924 2.253 1.00 39.21 O ANISOU 1088 OG1 THR A 143 4561 5166 5170 546 -87 -8 O ATOM 1089 CG2 THR A 143 32.129 32.856 1.404 1.00 40.98 C ANISOU 1089 CG2 THR A 143 4853 5217 5499 534 -164 50 C ATOM 1090 N ASP A 144 33.447 34.162 5.080 1.00 43.79 N ANISOU 1090 N ASP A 144 5140 5626 5869 577 -66 28 N ATOM 1091 CA ASP A 144 33.527 35.518 5.610 1.00 43.73 C ANISOU 1091 CA ASP A 144 5144 5603 5868 524 -67 42 C ATOM 1092 C ASP A 144 34.973 35.912 5.947 1.00 46.54 C ANISOU 1092 C ASP A 144 5480 6065 6136 492 -49 33 C ATOM 1093 O ASP A 144 35.803 35.060 6.335 1.00 46.52 O ANISOU 1093 O ASP A 144 5444 6131 6099 533 -30 9 O ATOM 1094 CB ASP A 144 32.621 35.646 6.835 1.00 42.55 C ANISOU 1094 CB ASP A 144 5000 5371 5796 549 -38 34 C ATOM 1095 CG ASP A 144 31.135 35.985 6.444 1.00 46.02 C ANISOU 1095 CG ASP A 144 5442 5696 6347 552 -65 39 C ATOM 1096 OD1 ASP A 144 30.879 37.027 5.803 1.00 43.14 O ANISOU 1096 OD1 ASP A 144 5090 5288 6013 512 -117 58 O ATOM 1097 OD2 ASP A 144 30.217 35.226 6.800 1.00 46.31 O ANISOU 1097 OD2 ASP A 144 5466 5682 6445 591 -44 24 O ATOM 1098 N ILE A 145 35.275 37.191 5.748 1.00 44.84 N ANISOU 1098 N ILE A 145 5285 5859 5894 416 -67 52 N ATOM 1099 CA ILE A 145 36.557 37.757 6.155 1.00 50.92 C ANISOU 1099 CA ILE A 145 6038 6723 6585 368 -52 47 C ATOM 1100 C ILE A 145 36.245 39.026 6.913 1.00 50.73 C ANISOU 1100 C ILE A 145 6055 6634 6585 323 -61 66 C ATOM 1101 O ILE A 145 35.314 39.702 6.599 1.00 49.08 O ANISOU 1101 O ILE A 145 5883 6330 6436 306 -94 83 O ATOM 1102 CB ILE A 145 37.501 38.100 4.971 1.00 50.70 C ANISOU 1102 CB ILE A 145 5999 6796 6466 288 -63 43 C ATOM 1103 CG1 ILE A 145 36.866 39.142 4.067 1.00 58.92 C ANISOU 1103 CG1 ILE A 145 7109 7771 7507 203 -117 83 C ATOM 1104 CG2 ILE A 145 37.876 36.858 4.160 1.00 52.01 C ANISOU 1104 CG2 ILE A 145 6119 7032 6609 328 -41 3 C ATOM 1105 CD1 ILE A 145 37.775 39.637 2.943 1.00 65.98 C ANISOU 1105 CD1 ILE A 145 8018 8762 8288 84 -128 84 C ATOM 1106 N SER A 146 37.050 39.359 7.895 1.00 59.27 N ANISOU 1106 N SER A 146 7131 7764 7625 304 -39 62 N ATOM 1107 CA SER A 146 36.912 40.638 8.589 1.00 66.56 C ANISOU 1107 CA SER A 146 8101 8633 8555 250 -44 74 C ATOM 1108 C SER A 146 38.003 41.592 8.099 1.00 68.58 C ANISOU 1108 C SER A 146 8367 8970 8719 152 -71 94 C ATOM 1109 O SER A 146 39.121 41.564 8.599 1.00 77.45 O ANISOU 1109 O SER A 146 9462 10190 9775 127 -55 88 O ATOM 1110 CB SER A 146 37.032 40.386 10.088 1.00 64.65 C ANISOU 1110 CB SER A 146 7864 8383 8314 274 -3 58 C ATOM 1111 OG SER A 146 36.135 39.354 10.464 1.00 68.52 O ANISOU 1111 OG SER A 146 8348 8817 8867 345 23 39 O ATOM 1112 N ARG A 147 37.693 42.418 7.111 1.00 77.97 N ANISOU 1112 N ARG A 147 9600 10119 9903 88 -121 118 N ATOM 1113 CA ARG A 147 38.686 43.350 6.544 1.00 81.04 C ANISOU 1113 CA ARG A 147 10016 10585 10190 -30 -150 141 C ATOM 1114 C ARG A 147 38.506 44.758 7.136 1.00 88.46 C ANISOU 1114 C ARG A 147 11029 11440 11140 -89 -187 163 C ATOM 1115 O ARG A 147 37.594 45.494 6.746 1.00 90.70 O ANISOU 1115 O ARG A 147 11374 11598 11487 -103 -249 181 O ATOM 1116 CB ARG A 147 38.646 43.366 4.989 1.00 79.02 C ANISOU 1116 CB ARG A 147 9783 10350 9888 -98 -192 158 C ATOM 1117 CG ARG A 147 40.059 43.244 4.394 1.00 85.11 C ANISOU 1117 CG ARG A 147 10513 11293 10531 -188 -160 140 C ATOM 1118 CD ARG A 147 40.230 43.655 2.941 1.00 81.93 C ANISOU 1118 CD ARG A 147 10165 10924 10039 -319 -197 159 C ATOM 1119 NE ARG A 147 39.739 42.674 1.967 1.00 82.62 N ANISOU 1119 NE ARG A 147 10242 11010 10140 -285 -190 141 N ATOM 1120 CZ ARG A 147 40.324 41.513 1.632 1.00 84.86 C ANISOU 1120 CZ ARG A 147 10439 11407 10395 -244 -118 81 C ATOM 1121 NH1 ARG A 147 41.459 41.069 2.204 1.00 77.72 N ANISOU 1121 NH1 ARG A 147 9432 10632 9464 -215 -50 28 N ATOM 1122 NH2 ARG A 147 39.737 40.760 0.705 1.00 88.98 N ANISOU 1122 NH2 ARG A 147 10976 11903 10926 -226 -123 71 N ATOM 1123 N PHE A 148 39.373 45.121 8.081 1.00 93.31 N ANISOU 1123 N PHE A 148 11639 12115 11699 -122 -159 158 N ATOM 1124 CA PHE A 148 39.279 46.422 8.743 1.00101.36 C ANISOU 1124 CA PHE A 148 12734 13056 12722 -179 -187 171 C ATOM 1125 C PHE A 148 39.949 47.529 7.938 1.00 99.15 C ANISOU 1125 C PHE A 148 12515 12808 12348 -317 -251 211 C ATOM 1126 O PHE A 148 41.063 47.933 8.236 1.00102.39 O ANISOU 1126 O PHE A 148 12923 13319 12660 -400 -241 220 O ATOM 1127 CB PHE A 148 39.858 46.335 10.154 1.00104.46 C ANISOU 1127 CB PHE A 148 13111 13489 13087 -168 -135 154 C ATOM 1128 CG PHE A 148 39.070 45.433 11.057 1.00108.26 C ANISOU 1128 CG PHE A 148 13568 13914 13651 -62 -81 118 C ATOM 1129 CD1 PHE A 148 37.741 45.731 11.359 1.00105.29 C ANISOU 1129 CD1 PHE A 148 13226 13393 13384 -15 -72 91 C ATOM 1130 CD2 PHE A 148 39.636 44.274 11.580 1.00103.82 C ANISOU 1130 CD2 PHE A 148 12946 13438 13061 -16 -45 108 C ATOM 1131 CE1 PHE A 148 36.997 44.901 12.173 1.00102.01 C ANISOU 1131 CE1 PHE A 148 12789 12936 13033 59 -11 53 C ATOM 1132 CE2 PHE A 148 38.895 43.441 12.397 1.00104.42 C ANISOU 1132 CE2 PHE A 148 13020 13458 13197 58 -3 82 C ATOM 1133 CZ PHE A 148 37.575 43.758 12.697 1.00105.28 C ANISOU 1133 CZ PHE A 148 13166 13437 13397 87 22 53 C ATOM 1134 N ALA A 164 36.349 43.404 19.335 1.00 70.61 N ANISOU 1134 N ALA A 164 9050 8871 8905 -81 310 -105 N ATOM 1135 CA ALA A 164 35.870 43.276 17.953 1.00 74.28 C ANISOU 1135 CA ALA A 164 9430 9327 9467 8 278 -98 C ATOM 1136 C ALA A 164 37.023 42.933 17.010 1.00 74.40 C ANISOU 1136 C ALA A 164 9392 9443 9431 33 189 -28 C ATOM 1137 O ALA A 164 37.010 41.897 16.345 1.00 68.95 O ANISOU 1137 O ALA A 164 8647 8789 8761 98 164 -10 O ATOM 1138 CB ALA A 164 35.170 44.541 17.503 1.00 71.60 C ANISOU 1138 CB ALA A 164 9085 8899 9217 14 287 -140 C ATOM 1139 N GLU A 165 38.033 43.789 16.972 1.00 72.38 N ANISOU 1139 N GLU A 165 9153 9236 9109 -24 148 2 N ATOM 1140 CA GLU A 165 39.253 43.473 16.242 1.00 73.62 C ANISOU 1140 CA GLU A 165 9252 9508 9209 -20 80 53 C ATOM 1141 C GLU A 165 39.838 42.114 16.663 1.00 69.29 C ANISOU 1141 C GLU A 165 8673 9023 8627 14 56 70 C ATOM 1142 O GLU A 165 40.189 41.311 15.810 1.00 65.48 O ANISOU 1142 O GLU A 165 8115 8601 8161 75 23 81 O ATOM 1143 CB GLU A 165 40.313 44.572 16.403 1.00 72.96 C ANISOU 1143 CB GLU A 165 9197 9477 9046 -111 45 80 C ATOM 1144 CG GLU A 165 41.728 44.076 16.125 1.00 77.68 C ANISOU 1144 CG GLU A 165 9727 10211 9577 -123 -10 117 C ATOM 1145 CD GLU A 165 42.765 45.180 16.061 1.00 79.94 C ANISOU 1145 CD GLU A 165 10024 10561 9786 -222 -45 143 C ATOM 1146 OE1 GLU A 165 42.775 46.050 16.949 1.00 86.86 O ANISOU 1146 OE1 GLU A 165 10987 11391 10625 -295 -37 145 O ATOM 1147 OE2 GLU A 165 43.596 45.155 15.137 1.00 80.79 O ANISOU 1147 OE2 GLU A 165 10056 10772 9866 -236 -77 157 O ATOM 1148 N PRO A 166 39.967 41.866 17.971 1.00 69.17 N ANISOU 1148 N PRO A 166 8726 8989 8565 -30 65 71 N ATOM 1149 CA PRO A 166 40.624 40.621 18.411 1.00 62.30 C ANISOU 1149 CA PRO A 166 7840 8165 7664 -4 10 98 C ATOM 1150 C PRO A 166 39.820 39.347 18.135 1.00 57.40 C ANISOU 1150 C PRO A 166 7200 7506 7101 77 20 84 C ATOM 1151 O PRO A 166 40.411 38.288 17.915 1.00 57.31 O ANISOU 1151 O PRO A 166 7142 7539 7094 134 -43 102 O ATOM 1152 CB PRO A 166 40.805 40.806 19.924 1.00 65.95 C ANISOU 1152 CB PRO A 166 8411 8594 8050 -99 12 107 C ATOM 1153 CG PRO A 166 40.062 42.028 20.310 1.00 69.76 C ANISOU 1153 CG PRO A 166 8964 9009 8532 -165 94 68 C ATOM 1154 CD PRO A 166 39.456 42.670 19.097 1.00 73.80 C ANISOU 1154 CD PRO A 166 9413 9500 9125 -110 123 43 C ATOM 1155 N SER A 167 38.497 39.445 18.144 1.00 52.74 N ANISOU 1155 N SER A 167 6642 6834 6563 84 95 46 N ATOM 1156 CA SER A 167 37.645 38.286 17.912 1.00 53.54 C ANISOU 1156 CA SER A 167 6732 6896 6714 147 109 33 C ATOM 1157 C SER A 167 37.324 38.020 16.445 1.00 52.40 C ANISOU 1157 C SER A 167 6498 6765 6643 235 99 28 C ATOM 1158 O SER A 167 36.730 36.990 16.135 1.00 54.30 O ANISOU 1158 O SER A 167 6726 6982 6923 291 98 22 O ATOM 1159 CB SER A 167 36.309 38.451 18.656 1.00 56.21 C ANISOU 1159 CB SER A 167 7134 7144 7078 102 204 -16 C ATOM 1160 OG SER A 167 35.650 39.619 18.226 1.00 55.93 O ANISOU 1160 OG SER A 167 7076 7068 7108 100 257 -56 O ATOM 1161 N SER A 168 37.670 38.938 15.550 1.00 51.30 N ANISOU 1161 N SER A 168 6314 6661 6515 234 88 33 N ATOM 1162 CA SER A 168 37.192 38.864 14.161 1.00 56.16 C ANISOU 1162 CA SER A 168 6871 7274 7192 290 81 28 C ATOM 1163 C SER A 168 38.120 38.136 13.185 1.00 50.78 C ANISOU 1163 C SER A 168 6119 6685 6490 336 31 42 C ATOM 1164 O SER A 168 39.152 38.655 12.815 1.00 55.05 O ANISOU 1164 O SER A 168 6625 7306 6983 303 5 53 O ATOM 1165 CB SER A 168 36.885 40.257 13.645 1.00 60.30 C ANISOU 1165 CB SER A 168 7404 7764 7742 249 88 23 C ATOM 1166 OG SER A 168 35.629 40.639 14.198 1.00 72.03 O ANISOU 1166 OG SER A 168 8925 9143 9298 245 141 -14 O ATOM 1167 N GLY A 169 37.730 36.943 12.771 1.00 45.29 N ANISOU 1167 N GLY A 169 5399 5977 5829 406 22 34 N ATOM 1168 CA GLY A 169 38.606 36.099 11.955 1.00 45.84 C ANISOU 1168 CA GLY A 169 5400 6129 5887 459 -16 29 C ATOM 1169 C GLY A 169 38.213 36.065 10.488 1.00 44.85 C ANISOU 1169 C GLY A 169 5240 6013 5789 480 -10 18 C ATOM 1170 O GLY A 169 37.441 36.900 9.990 1.00 45.37 O ANISOU 1170 O GLY A 169 5330 6028 5878 445 3 26 O ATOM 1171 N ALA A 170 38.755 35.069 9.807 1.00 46.28 N ANISOU 1171 N ALA A 170 5365 6250 5968 536 -29 -3 N ATOM 1172 CA ALA A 170 38.515 34.824 8.391 1.00 44.18 C ANISOU 1172 CA ALA A 170 5072 6002 5710 549 -23 -20 C ATOM 1173 C ALA A 170 38.515 33.314 8.188 1.00 44.41 C ANISOU 1173 C ALA A 170 5077 6027 5769 639 -40 -49 C ATOM 1174 O ALA A 170 39.356 32.610 8.721 1.00 44.23 O ANISOU 1174 O ALA A 170 5017 6040 5745 686 -68 -69 O ATOM 1175 CB ALA A 170 39.596 35.464 7.561 1.00 45.56 C ANISOU 1175 CB ALA A 170 5195 6289 5826 490 -18 -38 C ATOM 1176 N GLY A 171 37.540 32.811 7.462 1.00 42.02 N ANISOU 1176 N GLY A 171 4799 5667 5499 664 -35 -49 N ATOM 1177 CA GLY A 171 37.485 31.397 7.174 1.00 42.73 C ANISOU 1177 CA GLY A 171 4878 5743 5614 745 -53 -76 C ATOM 1178 C GLY A 171 36.283 31.062 6.350 1.00 42.86 C ANISOU 1178 C GLY A 171 4932 5690 5660 750 -48 -66 C ATOM 1179 O GLY A 171 35.386 31.910 6.161 1.00 43.89 O ANISOU 1179 O GLY A 171 5096 5770 5810 699 -39 -35 O ATOM 1180 N ALA A 172 36.260 29.815 5.888 1.00 41.95 N ANISOU 1180 N ALA A 172 4813 5565 5559 815 -64 -95 N ATOM 1181 CA ALA A 172 35.138 29.283 5.150 1.00 38.88 C ANISOU 1181 CA ALA A 172 4466 5108 5198 823 -69 -85 C ATOM 1182 C ALA A 172 35.003 27.790 5.389 1.00 39.85 C ANISOU 1182 C ALA A 172 4609 5186 5344 903 -99 -103 C ATOM 1183 O ALA A 172 36.003 27.067 5.620 1.00 41.69 O ANISOU 1183 O ALA A 172 4810 5457 5572 963 -122 -143 O ATOM 1184 CB ALA A 172 35.318 29.561 3.662 1.00 40.80 C ANISOU 1184 CB ALA A 172 4695 5400 5404 782 -57 -105 C ATOM 1185 N VAL A 173 33.772 27.334 5.324 1.00 38.37 N ANISOU 1185 N VAL A 173 4474 4914 5189 902 -107 -77 N ATOM 1186 CA VAL A 173 33.444 25.928 5.462 1.00 40.70 C ANISOU 1186 CA VAL A 173 4811 5152 5501 960 -142 -85 C ATOM 1187 C VAL A 173 32.476 25.555 4.359 1.00 41.20 C ANISOU 1187 C VAL A 173 4903 5172 5579 949 -144 -79 C ATOM 1188 O VAL A 173 31.446 26.230 4.178 1.00 39.32 O ANISOU 1188 O VAL A 173 4675 4894 5368 894 -132 -44 O ATOM 1189 CB VAL A 173 32.814 25.592 6.815 1.00 42.71 C ANISOU 1189 CB VAL A 173 5120 5335 5772 950 -155 -51 C ATOM 1190 CG1 VAL A 173 32.561 24.089 6.944 1.00 44.26 C ANISOU 1190 CG1 VAL A 173 5376 5467 5974 1000 -207 -55 C ATOM 1191 CG2 VAL A 173 33.730 26.019 7.948 1.00 45.02 C ANISOU 1191 CG2 VAL A 173 5401 5662 6041 944 -162 -48 C ATOM 1192 N ALA A 174 32.809 24.479 3.643 1.00 41.36 N ANISOU 1192 N ALA A 174 4933 5194 5587 1001 -165 -119 N ATOM 1193 CA ALA A 174 32.002 24.011 2.526 1.00 42.82 C ANISOU 1193 CA ALA A 174 5155 5340 5772 985 -174 -117 C ATOM 1194 C ALA A 174 31.325 22.719 2.879 1.00 44.10 C ANISOU 1194 C ALA A 174 5381 5417 5957 1025 -214 -108 C ATOM 1195 O ALA A 174 31.958 21.801 3.422 1.00 43.43 O ANISOU 1195 O ALA A 174 5310 5318 5872 1092 -248 -136 O ATOM 1196 CB ALA A 174 32.861 23.802 1.306 1.00 46.34 C ANISOU 1196 CB ALA A 174 5577 5854 6175 995 -156 -181 C ATOM 1197 N LEU A 175 30.037 22.654 2.560 1.00 43.01 N ANISOU 1197 N LEU A 175 5282 5216 5842 981 -222 -67 N ATOM 1198 CA LEU A 175 29.200 21.482 2.840 1.00 43.52 C ANISOU 1198 CA LEU A 175 5415 5198 5923 994 -259 -50 C ATOM 1199 C LEU A 175 28.604 20.950 1.559 1.00 44.12 C ANISOU 1199 C LEU A 175 5526 5243 5992 979 -280 -52 C ATOM 1200 O LEU A 175 28.015 21.704 0.790 1.00 44.27 O ANISOU 1200 O LEU A 175 5530 5266 6023 922 -274 -28 O ATOM 1201 CB LEU A 175 28.047 21.856 3.748 1.00 42.40 C ANISOU 1201 CB LEU A 175 5279 5006 5821 936 -245 -3 C ATOM 1202 CG LEU A 175 28.364 22.595 5.042 1.00 44.75 C ANISOU 1202 CG LEU A 175 5550 5327 6122 918 -212 3 C ATOM 1203 CD1 LEU A 175 27.070 22.837 5.803 1.00 45.31 C ANISOU 1203 CD1 LEU A 175 5628 5350 6237 851 -181 28 C ATOM 1204 CD2 LEU A 175 29.349 21.788 5.884 1.00 44.09 C ANISOU 1204 CD2 LEU A 175 5506 5245 6000 967 -247 -11 C ATOM 1205 N LEU A 176 28.794 19.666 1.312 1.00 45.76 N ANISOU 1205 N LEU A 176 5791 5415 6181 1029 -316 -82 N ATOM 1206 CA LEU A 176 28.098 18.974 0.234 1.00 47.40 C ANISOU 1206 CA LEU A 176 6056 5577 6377 1009 -342 -80 C ATOM 1207 C LEU A 176 26.904 18.285 0.867 1.00 45.62 C ANISOU 1207 C LEU A 176 5887 5264 6179 981 -377 -30 C ATOM 1208 O LEU A 176 27.060 17.494 1.795 1.00 44.74 O ANISOU 1208 O LEU A 176 5820 5114 6064 1014 -405 -31 O ATOM 1209 CB LEU A 176 29.007 17.919 -0.402 1.00 49.68 C ANISOU 1209 CB LEU A 176 6376 5869 6631 1081 -357 -155 C ATOM 1210 CG LEU A 176 28.468 17.151 -1.608 1.00 49.76 C ANISOU 1210 CG LEU A 176 6456 5835 6613 1058 -378 -169 C ATOM 1211 CD1 LEU A 176 28.164 18.119 -2.731 1.00 52.29 C ANISOU 1211 CD1 LEU A 176 6760 6200 6906 971 -351 -152 C ATOM 1212 CD2 LEU A 176 29.486 16.108 -2.070 1.00 51.43 C ANISOU 1212 CD2 LEU A 176 6688 6048 6802 1143 -384 -267 C ATOM 1213 N VAL A 177 25.722 18.585 0.361 1.00 45.13 N ANISOU 1213 N VAL A 177 5829 5172 6146 912 -384 12 N ATOM 1214 CA VAL A 177 24.467 18.123 0.958 1.00 46.23 C ANISOU 1214 CA VAL A 177 5999 5245 6321 864 -403 56 C ATOM 1215 C VAL A 177 23.756 17.174 -0.012 1.00 47.46 C ANISOU 1215 C VAL A 177 6226 5342 6463 840 -454 68 C ATOM 1216 O VAL A 177 23.598 17.499 -1.196 1.00 47.27 O ANISOU 1216 O VAL A 177 6200 5327 6434 814 -469 71 O ATOM 1217 CB VAL A 177 23.561 19.324 1.277 1.00 47.85 C ANISOU 1217 CB VAL A 177 6123 5458 6599 801 -372 88 C ATOM 1218 CG1 VAL A 177 22.233 18.875 1.881 1.00 49.27 C ANISOU 1218 CG1 VAL A 177 6311 5582 6825 741 -375 115 C ATOM 1219 CG2 VAL A 177 24.276 20.301 2.204 1.00 47.56 C ANISOU 1219 CG2 VAL A 177 6026 5475 6569 818 -320 73 C ATOM 1220 N SER A 178 23.334 16.002 0.477 1.00 47.98 N ANISOU 1220 N SER A 178 6437 5392 6399 421 -612 460 N ATOM 1221 CA SER A 178 22.768 14.978 -0.403 1.00 48.87 C ANISOU 1221 CA SER A 178 6643 5375 6550 433 -713 447 C ATOM 1222 C SER A 178 21.952 13.977 0.384 1.00 50.66 C ANISOU 1222 C SER A 178 6888 5502 6858 387 -766 518 C ATOM 1223 O SER A 178 21.871 14.071 1.598 1.00 52.68 O ANISOU 1223 O SER A 178 7084 5797 7132 356 -720 578 O ATOM 1224 CB SER A 178 23.904 14.217 -1.103 1.00 51.35 C ANISOU 1224 CB SER A 178 7035 5684 6790 548 -743 381 C ATOM 1225 OG SER A 178 24.518 13.328 -0.184 1.00 48.30 O ANISOU 1225 OG SER A 178 6663 5293 6393 599 -745 407 O ATOM 1226 N ASP A 179 21.383 12.994 -0.311 1.00 52.78 N ANISOU 1226 N ASP A 179 7244 5640 7169 384 -867 513 N ATOM 1227 CA ASP A 179 20.699 11.876 0.361 1.00 58.10 C ANISOU 1227 CA ASP A 179 7952 6204 7920 341 -930 582 C ATOM 1228 C ASP A 179 21.601 10.735 0.811 1.00 56.38 C ANISOU 1228 C ASP A 179 7803 5948 7669 426 -954 579 C ATOM 1229 O ASP A 179 21.098 9.711 1.232 1.00 61.38 O ANISOU 1229 O ASP A 179 8484 6472 8362 397 -1017 633 O ATOM 1230 CB ASP A 179 19.533 11.321 -0.492 1.00 63.50 C ANISOU 1230 CB ASP A 179 8695 6752 8677 278 -1038 588 C ATOM 1231 CG ASP A 179 19.986 10.625 -1.794 1.00 68.70 C ANISOU 1231 CG ASP A 179 9477 7329 9293 357 -1123 501 C ATOM 1232 OD1 ASP A 179 21.200 10.516 -2.069 1.00 67.25 O ANISOU 1232 OD1 ASP A 179 9333 7194 9022 468 -1097 439 O ATOM 1233 OD2 ASP A 179 19.091 10.192 -2.561 1.00 74.84 O ANISOU 1233 OD2 ASP A 179 10311 7998 10124 307 -1219 496 O ATOM 1234 N THR A 180 22.916 10.902 0.740 1.00 56.51 N ANISOU 1234 N THR A 180 7824 6055 7593 530 -905 523 N ATOM 1235 CA THR A 180 23.849 9.961 1.389 1.00 58.52 C ANISOU 1235 CA THR A 180 8121 6303 7809 619 -909 530 C ATOM 1236 C THR A 180 24.754 10.705 2.372 1.00 57.02 C ANISOU 1236 C THR A 180 7833 6270 7559 647 -803 542 C ATOM 1237 O THR A 180 25.906 11.025 2.074 1.00 59.91 O ANISOU 1237 O THR A 180 8187 6736 7839 734 -761 484 O ATOM 1238 CB THR A 180 24.717 9.232 0.353 1.00 59.24 C ANISOU 1238 CB THR A 180 8320 6353 7833 742 -962 448 C ATOM 1239 OG1 THR A 180 25.404 10.213 -0.440 1.00 60.00 O ANISOU 1239 OG1 THR A 180 8377 6567 7853 787 -906 378 O ATOM 1240 CG2 THR A 180 23.833 8.373 -0.535 1.00 59.55 C ANISOU 1240 CG2 THR A 180 8473 6222 7931 716 -1080 434 C ATOM 1241 N PRO A 181 24.230 10.984 3.557 1.00 56.18 N ANISOU 1241 N PRO A 181 7654 6193 7497 573 -761 620 N ATOM 1242 CA PRO A 181 24.924 11.893 4.466 1.00 58.55 C ANISOU 1242 CA PRO A 181 7855 6645 7743 580 -663 627 C ATOM 1243 C PRO A 181 26.052 11.237 5.250 1.00 57.38 C ANISOU 1243 C PRO A 181 7717 6546 7537 674 -646 634 C ATOM 1244 O PRO A 181 25.892 11.020 6.431 1.00 59.01 O ANISOU 1244 O PRO A 181 7891 6766 7762 651 -624 702 O ATOM 1245 CB PRO A 181 23.802 12.346 5.404 1.00 58.21 C ANISOU 1245 CB PRO A 181 7743 6602 7770 471 -633 709 C ATOM 1246 CG PRO A 181 22.813 11.245 5.400 1.00 57.88 C ANISOU 1246 CG PRO A 181 7765 6412 7813 427 -715 768 C ATOM 1247 CD PRO A 181 22.907 10.581 4.060 1.00 58.29 C ANISOU 1247 CD PRO A 181 7919 6362 7863 472 -800 703 C ATOM 1248 N HIS A 182 27.174 10.953 4.592 1.00 55.73 N ANISOU 1248 N HIS A 182 7548 6373 7253 782 -655 566 N ATOM 1249 CA HIS A 182 28.305 10.235 5.208 1.00 58.03 C ANISOU 1249 CA HIS A 182 7854 6711 7483 890 -647 568 C ATOM 1250 C HIS A 182 28.843 10.898 6.449 1.00 56.61 C ANISOU 1250 C HIS A 182 7571 6672 7265 878 -567 601 C ATOM 1251 O HIS A 182 29.400 10.228 7.280 1.00 59.06 O ANISOU 1251 O HIS A 182 7889 7000 7550 938 -568 632 O ATOM 1252 CB HIS A 182 29.482 10.072 4.238 1.00 59.19 C ANISOU 1252 CB HIS A 182 8037 6910 7543 1012 -653 485 C ATOM 1253 CG HIS A 182 29.115 9.434 2.941 1.00 61.86 C ANISOU 1253 CG HIS A 182 8485 7121 7897 1045 -732 438 C ATOM 1254 ND1 HIS A 182 28.237 8.372 2.860 1.00 64.59 N ANISOU 1254 ND1 HIS A 182 8932 7293 8316 1023 -820 469 N ATOM 1255 CD2 HIS A 182 29.506 9.699 1.672 1.00 62.98 C ANISOU 1255 CD2 HIS A 182 8655 7285 7989 1098 -740 362 C ATOM 1256 CE1 HIS A 182 28.092 8.018 1.596 1.00 64.40 C ANISOU 1256 CE1 HIS A 182 8997 7185 8285 1060 -883 409 C ATOM 1257 NE2 HIS A 182 28.847 8.810 0.855 1.00 66.86 N ANISOU 1257 NE2 HIS A 182 9267 7616 8520 1110 -834 343 N ATOM 1258 N ILE A 183 28.684 12.213 6.587 1.00 52.48 N ANISOU 1258 N ILE A 183 6958 6245 6737 803 -502 592 N ATOM 1259 CA ILE A 183 29.258 12.921 7.738 1.00 53.32 C ANISOU 1259 CA ILE A 183 6971 6489 6798 791 -430 612 C ATOM 1260 C ILE A 183 28.252 13.254 8.835 1.00 50.26 C ANISOU 1260 C ILE A 183 6540 6087 6467 697 -404 686 C ATOM 1261 O ILE A 183 28.505 13.002 10.009 1.00 50.14 O ANISOU 1261 O ILE A 183 6497 6118 6434 712 -382 733 O ATOM 1262 CB ILE A 183 29.986 14.221 7.296 1.00 54.31 C ANISOU 1262 CB ILE A 183 7022 6748 6862 781 -370 550 C ATOM 1263 CG1 ILE A 183 31.078 13.932 6.251 1.00 52.57 C ANISOU 1263 CG1 ILE A 183 6830 6568 6574 881 -384 483 C ATOM 1264 CG2 ILE A 183 30.578 14.919 8.500 1.00 55.41 C ANISOU 1264 CG2 ILE A 183 7073 7022 6956 764 -306 567 C ATOM 1265 CD1 ILE A 183 32.239 13.097 6.773 1.00 56.62 C ANISOU 1265 CD1 ILE A 183 7346 7144 7023 996 -389 484 C ATOM 1266 N PHE A 184 27.123 13.858 8.475 1.00 52.50 N ANISOU 1266 N PHE A 184 6814 6320 6813 605 -403 698 N ATOM 1267 CA PHE A 184 26.167 14.304 9.475 1.00 49.02 C ANISOU 1267 CA PHE A 184 6322 5885 6418 522 -369 766 C ATOM 1268 C PHE A 184 24.796 13.990 8.962 1.00 47.99 C ANISOU 1268 C PHE A 184 6226 5627 6379 453 -417 804 C ATOM 1269 O PHE A 184 24.382 14.567 7.983 1.00 50.32 O ANISOU 1269 O PHE A 184 6525 5900 6694 419 -426 764 O ATOM 1270 CB PHE A 184 26.335 15.804 9.717 1.00 49.65 C ANISOU 1270 CB PHE A 184 6321 6082 6460 478 -294 734 C ATOM 1271 CG PHE A 184 25.579 16.359 10.910 1.00 50.16 C ANISOU 1271 CG PHE A 184 6330 6182 6547 416 -247 796 C ATOM 1272 CD1 PHE A 184 25.819 15.908 12.186 1.00 51.80 C ANISOU 1272 CD1 PHE A 184 6519 6431 6731 440 -228 849 C ATOM 1273 CD2 PHE A 184 24.671 17.415 10.744 1.00 54.98 C ANISOU 1273 CD2 PHE A 184 6905 6795 7190 342 -215 796 C ATOM 1274 CE1 PHE A 184 25.162 16.443 13.280 1.00 53.07 C ANISOU 1274 CE1 PHE A 184 6629 6633 6900 393 -180 903 C ATOM 1275 CE2 PHE A 184 24.015 17.978 11.837 1.00 54.26 C ANISOU 1275 CE2 PHE A 184 6763 6745 7107 298 -166 848 C ATOM 1276 CZ PHE A 184 24.265 17.490 13.112 1.00 55.85 C ANISOU 1276 CZ PHE A 184 6947 6990 7283 324 -148 900 C ATOM 1277 N GLN A 185 24.103 13.069 9.620 1.00 49.17 N ANISOU 1277 N GLN A 185 6400 5697 6584 430 -449 884 N ATOM 1278 CA GLN A 185 22.758 12.698 9.222 1.00 52.85 C ANISOU 1278 CA GLN A 185 6891 6046 7144 353 -500 933 C ATOM 1279 C GLN A 185 21.759 13.574 9.971 1.00 49.65 C ANISOU 1279 C GLN A 185 6400 5690 6773 270 -443 992 C ATOM 1280 O GLN A 185 21.703 13.540 11.192 1.00 49.22 O ANISOU 1280 O GLN A 185 6305 5686 6709 265 -400 1054 O ATOM 1281 CB GLN A 185 22.477 11.214 9.495 1.00 55.53 C ANISOU 1281 CB GLN A 185 7303 6264 7531 362 -570 997 C ATOM 1282 CG GLN A 185 21.020 10.898 9.140 1.00 66.72 C ANISOU 1282 CG GLN A 185 8731 7568 9051 264 -624 1056 C ATOM 1283 CD GLN A 185 20.734 9.431 8.807 1.00 70.69 C ANISOU 1283 CD GLN A 185 9336 7912 9608 264 -724 1089 C ATOM 1284 OE1 GLN A 185 21.603 8.569 8.909 1.00 75.39 O ANISOU 1284 OE1 GLN A 185 10003 8474 10166 347 -753 1074 O ATOM 1285 NE2 GLN A 185 19.500 9.156 8.406 1.00 71.45 N ANISOU 1285 NE2 GLN A 185 9441 7911 9795 171 -781 1135 N ATOM 1286 N ILE A 186 20.989 14.370 9.243 1.00 50.19 N ANISOU 1286 N ILE A 186 6444 5749 6876 213 -440 971 N ATOM 1287 CA ILE A 186 20.080 15.327 9.861 1.00 51.09 C ANISOU 1287 CA ILE A 186 6477 5920 7013 149 -381 1017 C ATOM 1288 C ILE A 186 18.852 14.634 10.451 1.00 53.86 C ANISOU 1288 C ILE A 186 6812 6206 7446 85 -405 1126 C ATOM 1289 O ILE A 186 18.273 13.769 9.828 1.00 57.18 O ANISOU 1289 O ILE A 186 7279 6515 7931 53 -482 1150 O ATOM 1290 CB ILE A 186 19.606 16.368 8.835 1.00 52.67 C ANISOU 1290 CB ILE A 186 6660 6125 7225 115 -376 964 C ATOM 1291 CG1 ILE A 186 20.728 17.374 8.567 1.00 53.20 C ANISOU 1291 CG1 ILE A 186 6717 6287 7208 160 -325 875 C ATOM 1292 CG2 ILE A 186 18.325 17.088 9.278 1.00 52.72 C ANISOU 1292 CG2 ILE A 186 6596 6153 7280 46 -339 1025 C ATOM 1293 CD1 ILE A 186 20.965 18.344 9.706 1.00 53.81 C ANISOU 1293 CD1 ILE A 186 6729 6478 7238 157 -239 885 C ATOM 1294 N ASP A 187 18.474 15.054 11.655 1.00 54.14 N ANISOU 1294 N ASP A 187 6780 6318 7474 65 -339 1190 N ATOM 1295 CA ASP A 187 17.184 14.740 12.248 1.00 55.20 C ANISOU 1295 CA ASP A 187 6868 6423 7678 -2 -339 1300 C ATOM 1296 C ASP A 187 16.112 15.579 11.546 1.00 57.38 C ANISOU 1296 C ASP A 187 7100 6697 8002 -60 -337 1295 C ATOM 1297 O ASP A 187 15.964 16.770 11.820 1.00 56.99 O ANISOU 1297 O ASP A 187 6995 6737 7919 -57 -267 1275 O ATOM 1298 CB ASP A 187 17.195 15.084 13.745 1.00 55.91 C ANISOU 1298 CB ASP A 187 6898 6618 7727 10 -256 1361 C ATOM 1299 CG ASP A 187 18.184 14.231 14.558 1.00 56.25 C ANISOU 1299 CG ASP A 187 6979 6671 7722 68 -258 1379 C ATOM 1300 OD1 ASP A 187 18.347 13.020 14.254 1.00 54.58 O ANISOU 1300 OD1 ASP A 187 6834 6359 7544 75 -328 1401 O ATOM 1301 OD2 ASP A 187 18.777 14.785 15.526 1.00 55.95 O ANISOU 1301 OD2 ASP A 187 6907 6741 7610 110 -190 1371 O ATOM 1302 N VAL A 188 15.367 14.953 10.645 1.00 55.57 N ANISOU 1302 N VAL A 188 6900 6364 7850 -110 -417 1313 N ATOM 1303 CA VAL A 188 14.413 15.654 9.780 1.00 55.59 C ANISOU 1303 CA VAL A 188 6868 6355 7896 -159 -431 1300 C ATOM 1304 C VAL A 188 13.202 16.220 10.552 1.00 56.13 C ANISOU 1304 C VAL A 188 6837 6488 8001 -210 -376 1391 C ATOM 1305 O VAL A 188 12.564 15.535 11.352 1.00 54.45 O ANISOU 1305 O VAL A 188 6591 6265 7833 -250 -377 1496 O ATOM 1306 CB VAL A 188 13.951 14.713 8.637 1.00 56.15 C ANISOU 1306 CB VAL A 188 7001 6294 8037 -201 -544 1297 C ATOM 1307 CG1 VAL A 188 12.815 15.315 7.829 1.00 55.88 C ANISOU 1307 CG1 VAL A 188 6923 6251 8057 -259 -568 1302 C ATOM 1308 CG2 VAL A 188 15.125 14.383 7.714 1.00 55.64 C ANISOU 1308 CG2 VAL A 188 7034 6182 7923 -135 -590 1191 C ATOM 1309 N GLY A 189 12.890 17.487 10.324 1.00 55.67 N ANISOU 1309 N GLY A 189 6732 6498 7921 -203 -325 1355 N ATOM 1310 CA GLY A 189 11.776 18.130 11.037 1.00 56.33 C ANISOU 1310 CA GLY A 189 6720 6653 8027 -233 -265 1433 C ATOM 1311 C GLY A 189 12.081 18.511 12.485 1.00 57.26 C ANISOU 1311 C GLY A 189 6798 6872 8084 -193 -172 1469 C ATOM 1312 O GLY A 189 11.245 19.089 13.157 1.00 57.85 O ANISOU 1312 O GLY A 189 6798 7018 8163 -201 -113 1529 O ATOM 1313 N CYS A 190 13.290 18.227 12.967 1.00 56.71 N ANISOU 1313 N CYS A 190 6777 6818 7952 -144 -158 1429 N ATOM 1314 CA CYS A 190 13.677 18.594 14.329 1.00 53.10 C ANISOU 1314 CA CYS A 190 6288 6459 7426 -102 -75 1453 C ATOM 1315 C CYS A 190 14.347 19.976 14.307 1.00 52.81 C ANISOU 1315 C CYS A 190 6254 6499 7310 -55 -16 1355 C ATOM 1316 O CYS A 190 15.587 20.116 14.253 1.00 50.65 O ANISOU 1316 O CYS A 190 6027 6243 6973 -13 -14 1276 O ATOM 1317 CB CYS A 190 14.559 17.498 14.893 1.00 56.51 C ANISOU 1317 CB CYS A 190 6767 6867 7836 -77 -99 1472 C ATOM 1318 SG CYS A 190 13.663 15.904 14.917 1.00 57.66 S ANISOU 1318 SG CYS A 190 6918 6906 8084 -145 -173 1597 S ATOM 1319 N ASN A 191 13.500 21.002 14.273 1.00 50.46 N ANISOU 1319 N ASN A 191 5909 6244 7019 -63 26 1360 N ATOM 1320 CA ASN A 191 13.973 22.369 14.111 1.00 53.21 C ANISOU 1320 CA ASN A 191 6268 6645 7303 -29 74 1269 C ATOM 1321 C ASN A 191 13.146 23.315 14.963 1.00 51.28 C ANISOU 1321 C ASN A 191 5965 6481 7037 -12 150 1308 C ATOM 1322 O ASN A 191 11.929 23.233 14.966 1.00 53.93 O ANISOU 1322 O ASN A 191 6246 6816 7428 -38 153 1385 O ATOM 1323 CB ASN A 191 13.885 22.851 12.639 1.00 54.41 C ANISOU 1323 CB ASN A 191 6450 6739 7484 -47 30 1201 C ATOM 1324 CG ASN A 191 14.676 21.989 11.665 1.00 55.93 C ANISOU 1324 CG ASN A 191 6705 6854 7690 -53 -45 1154 C ATOM 1325 OD1 ASN A 191 15.802 22.356 11.260 1.00 53.83 O ANISOU 1325 OD1 ASN A 191 6484 6598 7368 -23 -43 1067 O ATOM 1326 ND2 ASN A 191 14.098 20.847 11.265 1.00 50.66 N ANISOU 1326 ND2 ASN A 191 6043 6109 7096 -90 -113 1210 N ATOM 1327 N GLY A 192 13.807 24.227 15.656 1.00 47.99 N ANISOU 1327 N GLY A 192 5561 6135 6536 31 210 1254 N ATOM 1328 CA GLY A 192 13.129 25.385 16.243 1.00 46.91 C ANISOU 1328 CA GLY A 192 5390 6065 6365 60 280 1260 C ATOM 1329 C GLY A 192 13.855 26.643 15.818 1.00 45.49 C ANISOU 1329 C GLY A 192 5261 5894 6128 81 299 1148 C ATOM 1330 O GLY A 192 15.076 26.630 15.667 1.00 43.79 O ANISOU 1330 O GLY A 192 5092 5674 5870 84 281 1077 O ATOM 1331 N TYR A 193 13.111 27.717 15.602 1.00 45.32 N ANISOU 1331 N TYR A 193 5228 5884 6106 95 332 1135 N ATOM 1332 CA TYR A 193 13.680 28.974 15.171 1.00 47.37 C ANISOU 1332 CA TYR A 193 5541 6140 6316 110 348 1037 C ATOM 1333 C TYR A 193 13.026 30.136 15.861 1.00 47.39 C ANISOU 1333 C TYR A 193 5534 6193 6276 155 415 1037 C ATOM 1334 O TYR A 193 11.894 30.030 16.319 1.00 47.40 O ANISOU 1334 O TYR A 193 5479 6227 6303 175 444 1116 O ATOM 1335 CB TYR A 193 13.603 29.135 13.632 1.00 50.79 C ANISOU 1335 CB TYR A 193 6000 6498 6800 78 296 998 C ATOM 1336 CG TYR A 193 12.541 28.313 12.887 1.00 52.55 C ANISOU 1336 CG TYR A 193 6180 6672 7114 46 248 1069 C ATOM 1337 CD1 TYR A 193 11.265 28.812 12.692 1.00 51.81 C ANISOU 1337 CD1 TYR A 193 6042 6584 7056 54 264 1114 C ATOM 1338 CD2 TYR A 193 12.852 27.064 12.319 1.00 52.34 C ANISOU 1338 CD2 TYR A 193 6161 6590 7133 10 180 1086 C ATOM 1339 CE1 TYR A 193 10.310 28.086 12.008 1.00 55.17 C ANISOU 1339 CE1 TYR A 193 6424 6971 7565 18 213 1179 C ATOM 1340 CE2 TYR A 193 11.899 26.335 11.614 1.00 52.45 C ANISOU 1340 CE2 TYR A 193 6144 6554 7230 -26 126 1145 C ATOM 1341 CZ TYR A 193 10.635 26.853 11.468 1.00 55.12 C ANISOU 1341 CZ TYR A 193 6431 6906 7606 -27 141 1192 C ATOM 1342 OH TYR A 193 9.675 26.138 10.803 1.00 62.11 O ANISOU 1342 OH TYR A 193 7278 7747 8574 -70 82 1253 O ATOM 1343 N TYR A 194 13.741 31.261 15.910 1.00 45.47 N ANISOU 1343 N TYR A 194 5349 5958 5968 173 438 948 N ATOM 1344 CA TYR A 194 13.290 32.417 16.628 1.00 45.31 C ANISOU 1344 CA TYR A 194 5342 5979 5893 224 498 932 C ATOM 1345 C TYR A 194 14.066 33.643 16.157 1.00 46.70 C ANISOU 1345 C TYR A 194 5596 6123 6022 219 499 827 C ATOM 1346 O TYR A 194 15.307 33.629 16.071 1.00 45.65 O ANISOU 1346 O TYR A 194 5503 5986 5855 188 476 765 O ATOM 1347 CB TYR A 194 13.503 32.204 18.151 1.00 47.53 C ANISOU 1347 CB TYR A 194 5608 6340 6108 262 543 957 C ATOM 1348 CG TYR A 194 12.753 33.149 19.092 1.00 46.34 C ANISOU 1348 CG TYR A 194 5458 6246 5903 332 611 966 C ATOM 1349 CD1 TYR A 194 11.396 32.966 19.368 1.00 50.12 C ANISOU 1349 CD1 TYR A 194 5869 6760 6415 368 645 1059 C ATOM 1350 CD2 TYR A 194 13.409 34.213 19.711 1.00 48.64 C ANISOU 1350 CD2 TYR A 194 5818 6558 6105 364 639 882 C ATOM 1351 CE1 TYR A 194 10.702 33.825 20.229 1.00 51.65 C ANISOU 1351 CE1 TYR A 194 6061 7012 6550 446 712 1068 C ATOM 1352 CE2 TYR A 194 12.736 35.069 20.582 1.00 48.87 C ANISOU 1352 CE2 TYR A 194 5858 6633 6075 438 699 884 C ATOM 1353 CZ TYR A 194 11.382 34.876 20.819 1.00 50.81 C ANISOU 1353 CZ TYR A 194 6035 6917 6351 485 738 976 C ATOM 1354 OH TYR A 194 10.739 35.702 21.684 1.00 53.89 O ANISOU 1354 OH TYR A 194 6436 7361 6676 571 801 978 O ATOM 1355 N GLY A 195 13.343 34.721 15.873 1.00 43.91 N ANISOU 1355 N GLY A 195 5265 5751 5666 250 525 811 N ATOM 1356 CA GLY A 195 14.001 35.996 15.579 1.00 43.99 C ANISOU 1356 CA GLY A 195 5358 5728 5626 247 530 718 C ATOM 1357 C GLY A 195 13.033 37.144 15.696 1.00 44.34 C ANISOU 1357 C GLY A 195 5428 5765 5654 306 573 715 C ATOM 1358 O GLY A 195 11.811 36.939 15.785 1.00 43.59 O ANISOU 1358 O GLY A 195 5274 5692 5594 347 594 788 O ATOM 1359 N TYR A 196 13.591 38.342 15.678 1.00 43.30 N ANISOU 1359 N TYR A 196 5381 5602 5468 309 583 634 N ATOM 1360 CA TYR A 196 12.833 39.589 15.796 1.00 44.14 C ANISOU 1360 CA TYR A 196 5535 5688 5545 373 621 615 C ATOM 1361 C TYR A 196 13.819 40.708 15.482 1.00 47.34 C ANISOU 1361 C TYR A 196 6046 6034 5904 339 608 517 C ATOM 1362 O TYR A 196 15.056 40.496 15.520 1.00 45.02 O ANISOU 1362 O TYR A 196 5773 5744 5588 275 580 471 O ATOM 1363 CB TYR A 196 12.261 39.763 17.199 1.00 48.68 C ANISOU 1363 CB TYR A 196 6098 6334 6064 453 677 639 C ATOM 1364 CG TYR A 196 13.277 39.630 18.317 1.00 47.83 C ANISOU 1364 CG TYR A 196 6016 6273 5883 443 683 597 C ATOM 1365 CD1 TYR A 196 13.584 38.397 18.847 1.00 49.50 C ANISOU 1365 CD1 TYR A 196 6159 6543 6103 421 675 646 C ATOM 1366 CD2 TYR A 196 13.929 40.737 18.830 1.00 52.19 C ANISOU 1366 CD2 TYR A 196 6665 6807 6356 454 693 509 C ATOM 1367 CE1 TYR A 196 14.503 38.260 19.870 1.00 50.51 C ANISOU 1367 CE1 TYR A 196 6308 6720 6162 417 678 611 C ATOM 1368 CE2 TYR A 196 14.868 40.612 19.846 1.00 54.21 C ANISOU 1368 CE2 TYR A 196 6942 7110 6542 442 691 469 C ATOM 1369 CZ TYR A 196 15.152 39.361 20.363 1.00 53.75 C ANISOU 1369 CZ TYR A 196 6809 7120 6493 426 685 521 C ATOM 1370 OH TYR A 196 16.077 39.215 21.386 1.00 53.75 O ANISOU 1370 OH TYR A 196 6826 7174 6420 420 682 485 O ATOM 1371 N GLU A 197 13.297 41.878 15.134 1.00 43.36 N ANISOU 1371 N GLU A 197 5606 5478 5388 377 624 490 N ATOM 1372 CA GLU A 197 14.158 43.005 14.763 1.00 46.38 C ANISOU 1372 CA GLU A 197 6097 5792 5734 338 609 405 C ATOM 1373 C GLU A 197 14.813 43.616 16.014 1.00 48.42 C ANISOU 1373 C GLU A 197 6419 6072 5904 351 628 342 C ATOM 1374 O GLU A 197 14.144 43.986 16.932 1.00 47.18 O ANISOU 1374 O GLU A 197 6276 5944 5704 433 668 347 O ATOM 1375 CB GLU A 197 13.400 44.061 13.990 1.00 46.60 C ANISOU 1375 CB GLU A 197 6183 5747 5775 377 618 398 C ATOM 1376 CG GLU A 197 14.314 44.986 13.186 1.00 49.22 C ANISOU 1376 CG GLU A 197 6612 5995 6094 310 590 329 C ATOM 1377 CD GLU A 197 14.926 46.105 14.028 1.00 54.55 C ANISOU 1377 CD GLU A 197 7394 6640 6689 312 602 251 C ATOM 1378 OE1 GLU A 197 14.126 46.842 14.622 1.00 56.45 O ANISOU 1378 OE1 GLU A 197 7683 6868 6895 401 636 244 O ATOM 1379 OE2 GLU A 197 16.185 46.261 14.100 1.00 51.76 O ANISOU 1379 OE2 GLU A 197 7080 6278 6309 227 575 196 O ATOM 1380 N VAL A 198 16.140 43.696 16.006 1.00 50.46 N ANISOU 1380 N VAL A 198 6714 6323 6136 269 597 283 N ATOM 1381 CA VAL A 198 16.932 44.228 17.098 1.00 50.94 C ANISOU 1381 CA VAL A 198 6835 6405 6115 262 599 217 C ATOM 1382 C VAL A 198 18.260 44.765 16.526 1.00 51.87 C ANISOU 1382 C VAL A 198 7010 6475 6220 157 557 149 C ATOM 1383 O VAL A 198 18.837 44.175 15.612 1.00 50.19 O ANISOU 1383 O VAL A 198 6753 6262 6054 89 528 165 O ATOM 1384 CB VAL A 198 17.189 43.125 18.168 1.00 55.34 C ANISOU 1384 CB VAL A 198 7315 7062 6648 276 607 248 C ATOM 1385 CG1 VAL A 198 17.889 41.899 17.558 1.00 51.35 C ANISOU 1385 CG1 VAL A 198 6728 6587 6193 206 571 281 C ATOM 1386 CG2 VAL A 198 17.967 43.702 19.359 1.00 54.13 C ANISOU 1386 CG2 VAL A 198 7227 6938 6402 275 606 177 C ATOM 1387 N MET A 199 18.735 45.885 17.055 1.00 55.15 N ANISOU 1387 N MET A 199 7527 6854 6573 144 553 76 N ATOM 1388 CA MET A 199 20.001 46.477 16.625 1.00 55.51 C ANISOU 1388 CA MET A 199 7627 6860 6603 36 513 15 C ATOM 1389 C MET A 199 21.199 46.032 17.473 1.00 57.02 C ANISOU 1389 C MET A 199 7790 7129 6746 -19 487 -19 C ATOM 1390 O MET A 199 21.956 46.859 17.980 1.00 60.10 O ANISOU 1390 O MET A 199 8255 7500 7079 -67 465 -88 O ATOM 1391 CB MET A 199 19.875 47.998 16.651 1.00 60.31 C ANISOU 1391 CB MET A 199 8370 7369 7173 39 513 -45 C ATOM 1392 CG MET A 199 18.865 48.522 15.643 1.00 63.63 C ANISOU 1392 CG MET A 199 8826 7708 7642 84 531 -14 C ATOM 1393 SD MET A 199 19.299 48.181 13.908 1.00 63.53 S ANISOU 1393 SD MET A 199 8768 7661 7706 -5 503 22 S ATOM 1394 CE MET A 199 20.792 49.172 13.771 1.00 66.04 C ANISOU 1394 CE MET A 199 9178 7929 7986 -135 464 -53 C ATOM 1395 N ASP A 200 21.402 44.724 17.596 1.00 59.17 N ANISOU 1395 N ASP A 200 7955 7484 7039 -17 485 28 N ATOM 1396 CA ASP A 200 22.508 44.232 18.410 1.00 63.43 C ANISOU 1396 CA ASP A 200 8461 8107 7531 -59 460 2 C ATOM 1397 C ASP A 200 23.847 44.461 17.696 1.00 66.37 C ANISOU 1397 C ASP A 200 8835 8473 7907 -174 418 -35 C ATOM 1398 O ASP A 200 24.753 45.087 18.259 1.00 71.83 O ANISOU 1398 O ASP A 200 9571 9177 8543 -231 391 -97 O ATOM 1399 CB ASP A 200 22.309 42.781 18.885 1.00 61.70 C ANISOU 1399 CB ASP A 200 8138 7978 7327 -12 472 67 C ATOM 1400 CG ASP A 200 22.145 41.775 17.750 1.00 60.96 C ANISOU 1400 CG ASP A 200 7965 7881 7314 -26 464 130 C ATOM 1401 OD1 ASP A 200 21.474 42.099 16.741 1.00 55.57 O ANISOU 1401 OD1 ASP A 200 7300 7128 6684 -22 471 148 O ATOM 1402 OD2 ASP A 200 22.699 40.654 17.895 1.00 64.62 O ANISOU 1402 OD2 ASP A 200 8354 8410 7785 -36 448 158 O ATOM 1403 N THR A 201 23.958 43.989 16.462 1.00 64.34 N ANISOU 1403 N THR A 201 8531 8200 7713 -209 410 1 N ATOM 1404 CA THR A 201 25.045 44.417 15.577 1.00 69.08 C ANISOU 1404 CA THR A 201 9142 8783 8320 -312 379 -27 C ATOM 1405 C THR A 201 24.504 44.486 14.136 1.00 66.64 C ANISOU 1405 C THR A 201 8837 8405 8077 -315 387 9 C ATOM 1406 O THR A 201 23.484 43.861 13.795 1.00 73.05 O ANISOU 1406 O THR A 201 9613 9205 8934 -246 406 62 O ATOM 1407 CB THR A 201 26.349 43.531 15.641 1.00 66.56 C ANISOU 1407 CB THR A 201 8737 8564 7987 -368 350 -26 C ATOM 1408 OG1 THR A 201 26.175 42.338 14.890 1.00 71.35 O ANISOU 1408 OG1 THR A 201 9263 9199 8647 -339 353 31 O ATOM 1409 CG2 THR A 201 26.764 43.145 17.047 1.00 64.18 C ANISOU 1409 CG2 THR A 201 8412 8347 7626 -346 342 -46 C ATOM 1410 N CYS A 202 25.183 45.272 13.309 1.00 64.76 N ANISOU 1410 N CYS A 202 8640 8122 7840 -399 370 -15 N ATOM 1411 CA CYS A 202 24.846 45.394 11.900 1.00 65.72 C ANISOU 1411 CA CYS A 202 8769 8186 8014 -410 375 16 C ATOM 1412 C CYS A 202 26.088 45.885 11.137 1.00 65.39 C ANISOU 1412 C CYS A 202 8735 8145 7962 -521 352 -4 C ATOM 1413 O CYS A 202 27.081 46.273 11.759 1.00 56.99 O ANISOU 1413 O CYS A 202 7681 7118 6855 -590 333 -46 O ATOM 1414 CB CYS A 202 23.673 46.376 11.731 1.00 64.27 C ANISOU 1414 CB CYS A 202 8677 7899 7843 -359 396 15 C ATOM 1415 SG CYS A 202 24.083 48.073 12.200 1.00 69.91 S ANISOU 1415 SG CYS A 202 9527 8531 8504 -418 387 -54 S ATOM 1416 N ARG A 203 26.019 45.865 9.803 1.00 64.28 N ANISOU 1416 N ARG A 203 8589 7972 7860 -538 354 26 N ATOM 1417 CA ARG A 203 27.131 46.308 8.931 1.00 63.45 C ANISOU 1417 CA ARG A 203 8486 7875 7748 -640 340 20 C ATOM 1418 C ARG A 203 26.598 47.288 7.887 1.00 59.85 C ANISOU 1418 C ARG A 203 8112 7312 7314 -654 350 33 C ATOM 1419 O ARG A 203 26.415 46.958 6.718 1.00 55.34 O ANISOU 1419 O ARG A 203 7518 6733 6774 -643 355 71 O ATOM 1420 CB ARG A 203 27.783 45.124 8.240 1.00 62.95 C ANISOU 1420 CB ARG A 203 8319 7900 7698 -643 333 52 C ATOM 1421 CG ARG A 203 28.292 44.053 9.176 1.00 66.51 C ANISOU 1421 CG ARG A 203 8686 8454 8128 -618 323 48 C ATOM 1422 CD ARG A 203 28.648 42.810 8.383 1.00 68.97 C ANISOU 1422 CD ARG A 203 8912 8832 8461 -591 317 84 C ATOM 1423 NE ARG A 203 29.227 41.792 9.246 1.00 73.74 N ANISOU 1423 NE ARG A 203 9441 9534 9043 -566 305 81 N ATOM 1424 CZ ARG A 203 30.474 41.821 9.716 1.00 76.27 C ANISOU 1424 CZ ARG A 203 9720 9940 9319 -625 290 57 C ATOM 1425 NH1 ARG A 203 31.289 42.826 9.410 1.00 81.59 N ANISOU 1425 NH1 ARG A 203 10416 10614 9968 -722 285 35 N ATOM 1426 NH2 ARG A 203 30.908 40.845 10.505 1.00 72.80 N ANISOU 1426 NH2 ARG A 203 9214 9588 8859 -588 279 59 N ATOM 1427 N PRO A 204 26.339 48.513 8.323 1.00 63.80 N ANISOU 1427 N PRO A 204 8717 7728 7796 -674 351 0 N ATOM 1428 CA PRO A 204 25.642 49.475 7.484 1.00 62.03 C ANISOU 1428 CA PRO A 204 8585 7391 7591 -666 362 13 C ATOM 1429 C PRO A 204 26.546 50.117 6.432 1.00 61.97 C ANISOU 1429 C PRO A 204 8602 7361 7582 -774 354 24 C ATOM 1430 O PRO A 204 26.028 50.743 5.515 1.00 58.33 O ANISOU 1430 O PRO A 204 8204 6817 7139 -766 363 48 O ATOM 1431 CB PRO A 204 25.190 50.521 8.492 1.00 63.40 C ANISOU 1431 CB PRO A 204 8867 7488 7735 -648 362 -32 C ATOM 1432 CG PRO A 204 26.287 50.510 9.516 1.00 65.78 C ANISOU 1432 CG PRO A 204 9147 7853 7991 -721 339 -78 C ATOM 1433 CD PRO A 204 26.733 49.086 9.629 1.00 63.21 C ANISOU 1433 CD PRO A 204 8687 7655 7673 -704 338 -54 C ATOM 1434 N ASN A 205 27.864 49.983 6.608 1.00 62.55 N ANISOU 1434 N ASN A 205 8624 7512 7629 -871 336 10 N ATOM 1435 CA ASN A 205 28.888 50.440 5.676 1.00 69.08 C ANISOU 1435 CA ASN A 205 9447 8349 8451 -982 331 28 C ATOM 1436 C ASN A 205 29.811 49.289 5.242 1.00 72.71 C ANISOU 1436 C ASN A 205 9774 8944 8907 -999 330 54 C ATOM 1437 O ASN A 205 29.948 48.288 5.980 1.00 64.44 O ANISOU 1437 O ASN A 205 8648 7983 7853 -953 324 43 O ATOM 1438 CB ASN A 205 29.786 51.490 6.332 1.00 73.20 C ANISOU 1438 CB ASN A 205 10027 8846 8938 -1101 306 -12 C ATOM 1439 CG ASN A 205 29.046 52.759 6.664 1.00 77.82 C ANISOU 1439 CG ASN A 205 10761 9287 9520 -1095 302 -41 C ATOM 1440 OD1 ASN A 205 28.675 53.520 5.778 1.00 82.14 O ANISOU 1440 OD1 ASN A 205 11386 9738 10084 -1107 312 -16 O ATOM 1441 ND2 ASN A 205 28.831 52.998 7.948 1.00 82.95 N ANISOU 1441 ND2 ASN A 205 11454 9918 10142 -1069 288 -95 N ATOM 1442 N PRO A 206 30.481 49.449 4.068 1.00 80.84 N ANISOU 1442 N PRO A 206 10782 9994 9937 -1064 337 90 N ATOM 1443 CA PRO A 206 31.472 48.451 3.604 1.00 82.84 C ANISOU 1443 CA PRO A 206 10913 10382 10177 -1080 339 114 C ATOM 1444 C PRO A 206 32.703 48.360 4.529 1.00 77.54 C ANISOU 1444 C PRO A 206 10177 9811 9470 -1160 318 85 C ATOM 1445 O PRO A 206 33.124 49.381 5.104 1.00 72.74 O ANISOU 1445 O PRO A 206 9626 9166 8845 -1254 301 57 O ATOM 1446 CB PRO A 206 31.881 48.954 2.197 1.00 84.11 C ANISOU 1446 CB PRO A 206 11088 10531 10338 -1139 355 159 C ATOM 1447 CG PRO A 206 30.962 50.096 1.855 1.00 86.34 C ANISOU 1447 CG PRO A 206 11499 10665 10640 -1140 361 163 C ATOM 1448 CD PRO A 206 30.398 50.615 3.154 1.00 83.66 C ANISOU 1448 CD PRO A 206 11231 10253 10300 -1125 346 113 C ATOM 1449 N ASP A 207 33.219 47.136 4.687 1.00 74.00 N ANISOU 1449 N ASP A 207 9617 9486 9011 -1116 316 91 N ATOM 1450 CA ASP A 207 34.469 46.845 5.418 1.00 80.41 C ANISOU 1450 CA ASP A 207 10343 10421 9786 -1178 296 73 C ATOM 1451 C ASP A 207 34.430 47.435 6.844 1.00 81.92 C ANISOU 1451 C ASP A 207 10584 10581 9959 -1213 269 20 C ATOM 1452 O ASP A 207 35.398 48.021 7.334 1.00 82.09 O ANISOU 1452 O ASP A 207 10593 10644 9950 -1320 245 0 O ATOM 1453 CB ASP A 207 35.702 47.351 4.613 1.00 81.34 C ANISOU 1453 CB ASP A 207 10416 10605 9882 -1296 300 102 C ATOM 1454 CG ASP A 207 35.615 47.025 3.085 1.00 81.42 C ANISOU 1454 CG ASP A 207 10405 10624 9904 -1262 331 155 C ATOM 1455 OD1 ASP A 207 35.521 45.832 2.702 1.00 75.76 O ANISOU 1455 OD1 ASP A 207 9622 9973 9189 -1164 341 170 O ATOM 1456 OD2 ASP A 207 35.634 47.972 2.267 1.00 75.07 O ANISOU 1456 OD2 ASP A 207 9660 9757 9105 -1331 344 181 O ATOM 1457 N SER A 208 33.292 47.260 7.498 1.00 83.59 N ANISOU 1457 N SER A 208 10850 10723 10185 -1119 273 1 N ATOM 1458 CA SER A 208 32.969 47.981 8.731 1.00 87.90 C ANISOU 1458 CA SER A 208 11474 11210 10712 -1132 254 -49 C ATOM 1459 C SER A 208 31.925 47.197 9.558 1.00 84.79 C ANISOU 1459 C SER A 208 11079 10809 10325 -1003 263 -58 C ATOM 1460 O SER A 208 31.316 46.250 9.063 1.00 83.59 O ANISOU 1460 O SER A 208 10883 10671 10204 -913 282 -22 O ATOM 1461 CB SER A 208 32.438 49.363 8.355 1.00 85.02 C ANISOU 1461 CB SER A 208 11241 10703 10360 -1179 257 -59 C ATOM 1462 OG SER A 208 32.239 50.164 9.495 1.00 92.17 O ANISOU 1462 OG SER A 208 12234 11547 11239 -1198 234 -114 O ATOM 1463 N GLU A 209 31.730 47.583 10.817 1.00 85.71 N ANISOU 1463 N GLU A 209 11245 10908 10412 -995 248 -104 N ATOM 1464 CA GLU A 209 30.687 46.963 11.665 1.00 87.87 C ANISOU 1464 CA GLU A 209 11523 11174 10688 -874 262 -106 C ATOM 1465 C GLU A 209 30.278 47.873 12.831 1.00 79.55 C ANISOU 1465 C GLU A 209 10569 10058 9597 -869 252 -161 C ATOM 1466 O GLU A 209 31.123 48.530 13.415 1.00 77.59 O ANISOU 1466 O GLU A 209 10347 9824 9308 -955 219 -205 O ATOM 1467 CB GLU A 209 31.147 45.601 12.203 1.00 86.48 C ANISOU 1467 CB GLU A 209 11233 11125 10499 -828 256 -92 C ATOM 1468 CG GLU A 209 30.110 44.915 13.076 1.00 91.03 C ANISOU 1468 CG GLU A 209 11808 11700 11077 -712 272 -84 C ATOM 1469 CD GLU A 209 30.465 43.477 13.391 1.00 95.37 C ANISOU 1469 CD GLU A 209 12251 12360 11625 -660 269 -55 C ATOM 1470 OE1 GLU A 209 31.462 43.247 14.098 1.00100.60 O ANISOU 1470 OE1 GLU A 209 12866 13114 12243 -695 245 -77 O ATOM 1471 OE2 GLU A 209 29.739 42.574 12.940 1.00 97.74 O ANISOU 1471 OE2 GLU A 209 12517 12652 11965 -583 286 -10 O ATOM 1472 N ALA A 210 28.984 47.903 13.153 1.00 73.51 N ANISOU 1472 N ALA A 210 9856 9228 8844 -765 277 -156 N ATOM 1473 CA ALA A 210 28.457 48.696 14.277 1.00 75.68 C ANISOU 1473 CA ALA A 210 10229 9447 9078 -732 274 -207 C ATOM 1474 C ALA A 210 27.615 47.777 15.186 1.00 78.12 C ANISOU 1474 C ALA A 210 10495 9807 9378 -608 298 -190 C ATOM 1475 O ALA A 210 26.984 46.811 14.716 1.00 73.19 O ANISOU 1475 O ALA A 210 9802 9208 8798 -539 323 -133 O ATOM 1476 CB ALA A 210 27.635 49.887 13.771 1.00 69.64 C ANISOU 1476 CB ALA A 210 9589 8541 8329 -722 287 -216 C ATOM 1477 N GLY A 211 27.617 48.062 16.484 1.00 81.54 N ANISOU 1477 N GLY A 211 10970 10258 9752 -584 289 -236 N ATOM 1478 CA GLY A 211 26.874 47.223 17.435 1.00 88.87 C ANISOU 1478 CA GLY A 211 11857 11244 10663 -470 314 -216 C ATOM 1479 C GLY A 211 27.168 47.472 18.897 1.00 85.44 C ANISOU 1479 C GLY A 211 11458 10853 10150 -455 297 -271 C ATOM 1480 O GLY A 211 28.152 48.119 19.238 1.00 78.95 O ANISOU 1480 O GLY A 211 10675 10036 9285 -545 254 -328 O ATOM 1481 N ASP A 212 26.288 46.957 19.752 1.00 87.59 N ANISOU 1481 N ASP A 212 11719 11159 10402 -342 329 -250 N ATOM 1482 CA ASP A 212 26.447 47.037 21.194 1.00 85.46 C ANISOU 1482 CA ASP A 212 11476 10943 10050 -305 319 -294 C ATOM 1483 C ASP A 212 26.669 45.622 21.746 1.00 82.21 C ANISOU 1483 C ASP A 212 10946 10657 9633 -263 325 -245 C ATOM 1484 O ASP A 212 25.794 44.749 21.627 1.00 70.37 O ANISOU 1484 O ASP A 212 9387 9177 8172 -182 365 -176 O ATOM 1485 CB ASP A 212 25.217 47.691 21.836 1.00 91.14 C ANISOU 1485 CB ASP A 212 12288 11603 10737 -197 356 -309 C ATOM 1486 CG ASP A 212 25.194 47.534 23.362 1.00 93.80 C ANISOU 1486 CG ASP A 212 12638 12014 10985 -129 357 -339 C ATOM 1487 OD1 ASP A 212 24.134 47.172 23.901 1.00101.93 O ANISOU 1487 OD1 ASP A 212 13657 13067 12002 -11 406 -301 O ATOM 1488 OD2 ASP A 212 26.235 47.730 24.025 1.00 99.70 O ANISOU 1488 OD2 ASP A 212 13400 12805 11673 -193 310 -396 O ATOM 1489 N ALA A 213 27.835 45.419 22.359 1.00 77.49 N ANISOU 1489 N ALA A 213 10316 10140 8984 -322 283 -279 N ATOM 1490 CA ALA A 213 28.223 44.109 22.896 1.00 79.00 C ANISOU 1490 CA ALA A 213 10400 10451 9162 -288 282 -236 C ATOM 1491 C ALA A 213 27.238 43.583 23.952 1.00 76.74 C ANISOU 1491 C ALA A 213 10112 10203 8842 -164 323 -203 C ATOM 1492 O ALA A 213 26.928 42.393 23.960 1.00 77.27 O ANISOU 1492 O ALA A 213 10093 10326 8939 -110 345 -132 O ATOM 1493 CB ALA A 213 29.642 44.160 23.464 1.00 76.07 C ANISOU 1493 CB ALA A 213 10006 10164 8733 -368 225 -286 C ATOM 1494 N ASP A 214 26.737 44.464 24.819 1.00 71.59 N ANISOU 1494 N ASP A 214 9554 9519 8125 -117 332 -253 N ATOM 1495 CA ASP A 214 25.772 44.059 25.858 1.00 75.46 C ANISOU 1495 CA ASP A 214 10044 10052 8572 6 377 -220 C ATOM 1496 C ASP A 214 24.411 43.658 25.278 1.00 69.61 C ANISOU 1496 C ASP A 214 9275 9271 7902 84 437 -141 C ATOM 1497 O ASP A 214 23.815 42.673 25.711 1.00 62.34 O ANISOU 1497 O ASP A 214 8285 8412 6988 158 471 -69 O ATOM 1498 CB ASP A 214 25.611 45.162 26.915 1.00 83.49 C ANISOU 1498 CB ASP A 214 11179 11047 9494 43 372 -300 C ATOM 1499 CG ASP A 214 26.931 45.471 27.659 1.00 93.02 C ANISOU 1499 CG ASP A 214 12411 12309 10623 -31 306 -377 C ATOM 1500 OD1 ASP A 214 27.967 44.811 27.392 1.00 93.47 O ANISOU 1500 OD1 ASP A 214 12383 12432 10699 -106 269 -363 O ATOM 1501 OD2 ASP A 214 26.934 46.383 28.514 1.00 99.70 O ANISOU 1501 OD2 ASP A 214 13361 13134 11385 -11 288 -453 O ATOM 1502 N LEU A 215 23.937 44.394 24.272 1.00 65.28 N ANISOU 1502 N LEU A 215 8775 8620 7409 63 445 -149 N ATOM 1503 CA LEU A 215 22.688 44.020 23.588 1.00 62.95 C ANISOU 1503 CA LEU A 215 8443 8287 7185 127 492 -74 C ATOM 1504 C LEU A 215 22.886 42.756 22.731 1.00 58.39 C ANISOU 1504 C LEU A 215 7754 7742 6689 92 485 0 C ATOM 1505 O LEU A 215 22.002 41.904 22.681 1.00 54.83 O ANISOU 1505 O LEU A 215 7238 7313 6279 154 519 77 O ATOM 1506 CB LEU A 215 22.125 45.196 22.785 1.00 63.68 C ANISOU 1506 CB LEU A 215 8625 8263 7305 122 500 -104 C ATOM 1507 CG LEU A 215 20.830 44.978 21.972 1.00 66.92 C ANISOU 1507 CG LEU A 215 9004 8630 7790 184 542 -32 C ATOM 1508 CD1 LEU A 215 19.643 44.514 22.818 1.00 61.53 C ANISOU 1508 CD1 LEU A 215 8285 8003 7088 306 597 25 C ATOM 1509 CD2 LEU A 215 20.489 46.268 21.216 1.00 69.73 C ANISOU 1509 CD2 LEU A 215 9463 8870 8161 173 541 -74 C ATOM 1510 N SER A 216 24.064 42.619 22.111 1.00 59.97 N ANISOU 1510 N SER A 216 7929 7948 6906 -4 441 -25 N ATOM 1511 CA SER A 216 24.455 41.370 21.417 1.00 60.75 C ANISOU 1511 CA SER A 216 7928 8089 7065 -30 428 32 C ATOM 1512 C SER A 216 24.297 40.158 22.313 1.00 58.70 C ANISOU 1512 C SER A 216 7597 7918 6787 32 441 89 C ATOM 1513 O SER A 216 23.704 39.152 21.911 1.00 56.92 O ANISOU 1513 O SER A 216 7307 7697 6622 65 457 164 O ATOM 1514 CB SER A 216 25.918 41.410 20.940 1.00 66.19 C ANISOU 1514 CB SER A 216 8598 8803 7747 -131 379 -9 C ATOM 1515 OG SER A 216 26.117 42.344 19.891 1.00 75.38 O ANISOU 1515 OG SER A 216 9813 9886 8941 -201 366 -43 O ATOM 1516 N LEU A 217 24.827 40.266 23.530 1.00 59.08 N ANISOU 1516 N LEU A 217 7660 8034 6751 46 432 53 N ATOM 1517 CA LEU A 217 24.771 39.170 24.493 1.00 59.49 C ANISOU 1517 CA LEU A 217 7652 8177 6774 107 444 107 C ATOM 1518 C LEU A 217 23.340 38.826 24.912 1.00 57.06 C ANISOU 1518 C LEU A 217 7332 7866 6481 201 500 178 C ATOM 1519 O LEU A 217 22.950 37.635 24.896 1.00 54.60 O ANISOU 1519 O LEU A 217 6947 7586 6211 233 514 262 O ATOM 1520 CB LEU A 217 25.614 39.490 25.741 1.00 62.45 C ANISOU 1520 CB LEU A 217 8054 8627 7044 106 420 48 C ATOM 1521 CG LEU A 217 25.459 38.512 26.912 1.00 66.20 C ANISOU 1521 CG LEU A 217 8483 9197 7471 182 438 102 C ATOM 1522 CD1 LEU A 217 25.777 37.101 26.465 1.00 67.62 C ANISOU 1522 CD1 LEU A 217 8569 9414 7708 176 427 176 C ATOM 1523 CD2 LEU A 217 26.358 38.898 28.070 1.00 69.04 C ANISOU 1523 CD2 LEU A 217 8876 9633 7724 177 407 36 C ATOM 1524 N LEU A 218 22.562 39.845 25.283 1.00 55.82 N ANISOU 1524 N LEU A 218 7246 7672 6290 247 531 148 N ATOM 1525 CA LEU A 218 21.155 39.622 25.634 1.00 59.39 C ANISOU 1525 CA LEU A 218 7681 8129 6754 341 589 218 C ATOM 1526 C LEU A 218 20.402 38.909 24.533 1.00 53.13 C ANISOU 1526 C LEU A 218 6823 7294 6070 333 600 298 C ATOM 1527 O LEU A 218 19.670 37.988 24.802 1.00 50.63 O ANISOU 1527 O LEU A 218 6441 7015 5780 380 628 385 O ATOM 1528 CB LEU A 218 20.434 40.939 25.943 1.00 67.22 C ANISOU 1528 CB LEU A 218 8764 9074 7700 394 619 168 C ATOM 1529 CG LEU A 218 20.881 41.644 27.230 1.00 74.88 C ANISOU 1529 CG LEU A 218 9810 10087 8551 428 615 94 C ATOM 1530 CD1 LEU A 218 20.150 42.977 27.416 1.00 76.18 C ANISOU 1530 CD1 LEU A 218 10080 10190 8674 486 642 39 C ATOM 1531 CD2 LEU A 218 20.687 40.732 28.438 1.00 72.96 C ANISOU 1531 CD2 LEU A 218 9512 9955 8253 500 644 153 C ATOM 1532 N SER A 219 20.594 39.321 23.281 1.00 52.76 N ANISOU 1532 N SER A 219 6794 7168 6083 271 575 270 N ATOM 1533 CA SER A 219 19.781 38.766 22.199 1.00 51.91 C ANISOU 1533 CA SER A 219 6636 7014 6072 269 582 339 C ATOM 1534 C SER A 219 20.176 37.334 21.907 1.00 49.59 C ANISOU 1534 C SER A 219 6260 6754 5828 242 557 399 C ATOM 1535 O SER A 219 19.322 36.494 21.604 1.00 47.24 O ANISOU 1535 O SER A 219 5904 6451 5592 265 569 480 O ATOM 1536 CB SER A 219 19.910 39.610 20.936 1.00 54.76 C ANISOU 1536 CB SER A 219 7045 7284 6476 214 561 292 C ATOM 1537 OG SER A 219 19.746 40.982 21.255 1.00 60.54 O ANISOU 1537 OG SER A 219 7869 7976 7155 234 575 227 O ATOM 1538 N TYR A 220 21.479 37.057 21.973 1.00 49.82 N ANISOU 1538 N TYR A 220 6284 6815 5827 191 518 358 N ATOM 1539 CA TYR A 220 21.976 35.700 21.758 1.00 49.12 C ANISOU 1539 CA TYR A 220 6127 6760 5774 175 492 408 C ATOM 1540 C TYR A 220 21.334 34.724 22.767 1.00 46.84 C ANISOU 1540 C TYR A 220 5790 6530 5476 239 519 490 C ATOM 1541 O TYR A 220 20.880 33.664 22.380 1.00 46.24 O ANISOU 1541 O TYR A 220 5663 6442 5464 245 515 565 O ATOM 1542 CB TYR A 220 23.508 35.670 21.872 1.00 49.66 C ANISOU 1542 CB TYR A 220 6198 6875 5796 125 450 348 C ATOM 1543 CG TYR A 220 24.167 34.331 21.592 1.00 48.44 C ANISOU 1543 CG TYR A 220 5981 6754 5669 117 420 389 C ATOM 1544 CD1 TYR A 220 24.145 33.294 22.525 1.00 51.36 C ANISOU 1544 CD1 TYR A 220 6310 7185 6017 164 425 447 C ATOM 1545 CD2 TYR A 220 24.861 34.116 20.401 1.00 51.19 C ANISOU 1545 CD2 TYR A 220 6316 7073 6060 66 385 370 C ATOM 1546 CE1 TYR A 220 24.767 32.067 22.256 1.00 51.15 C ANISOU 1546 CE1 TYR A 220 6237 7181 6015 164 394 483 C ATOM 1547 CE2 TYR A 220 25.496 32.907 20.134 1.00 50.32 C ANISOU 1547 CE2 TYR A 220 6156 6992 5969 70 356 402 C ATOM 1548 CZ TYR A 220 25.446 31.887 21.066 1.00 52.25 C ANISOU 1548 CZ TYR A 220 6368 7290 6195 119 359 457 C ATOM 1549 OH TYR A 220 26.084 30.716 20.769 1.00 49.22 O ANISOU 1549 OH TYR A 220 5946 6925 5829 129 328 487 O ATOM 1550 N LEU A 221 21.289 35.107 24.039 1.00 51.54 N ANISOU 1550 N LEU A 221 6408 7186 5989 286 546 477 N ATOM 1551 CA LEU A 221 20.708 34.264 25.111 1.00 55.37 C ANISOU 1551 CA LEU A 221 6850 7737 6450 350 579 559 C ATOM 1552 C LEU A 221 19.216 34.106 24.968 1.00 53.09 C ANISOU 1552 C LEU A 221 6531 7424 6216 392 623 640 C ATOM 1553 O LEU A 221 18.683 33.016 25.117 1.00 53.77 O ANISOU 1553 O LEU A 221 6557 7529 6343 409 633 734 O ATOM 1554 CB LEU A 221 20.990 34.831 26.515 1.00 59.19 C ANISOU 1554 CB LEU A 221 7372 8295 6820 398 600 519 C ATOM 1555 CG LEU A 221 22.462 34.978 26.913 1.00 65.24 C ANISOU 1555 CG LEU A 221 8161 9107 7517 361 554 443 C ATOM 1556 CD1 LEU A 221 22.633 35.835 28.166 1.00 65.37 C ANISOU 1556 CD1 LEU A 221 8236 9180 7420 403 569 384 C ATOM 1557 CD2 LEU A 221 23.123 33.612 27.084 1.00 63.42 C ANISOU 1557 CD2 LEU A 221 7868 8929 7298 357 528 498 C ATOM 1558 N ASP A 222 18.540 35.205 24.691 1.00 52.54 N ANISOU 1558 N ASP A 222 6502 7313 6145 410 648 606 N ATOM 1559 CA ASP A 222 17.119 35.159 24.405 1.00 50.21 C ANISOU 1559 CA ASP A 222 6173 6998 5907 448 687 679 C ATOM 1560 C ASP A 222 16.827 34.176 23.248 1.00 49.18 C ANISOU 1560 C ASP A 222 5983 6814 5886 398 655 742 C ATOM 1561 O ASP A 222 15.966 33.328 23.350 1.00 46.25 O ANISOU 1561 O ASP A 222 5549 6459 5563 415 671 839 O ATOM 1562 CB ASP A 222 16.642 36.575 24.097 1.00 53.94 C ANISOU 1562 CB ASP A 222 6711 7422 6361 472 708 617 C ATOM 1563 CG ASP A 222 15.133 36.653 23.810 1.00 58.60 C ANISOU 1563 CG ASP A 222 7262 8001 7002 522 750 690 C ATOM 1564 OD1 ASP A 222 14.719 37.432 22.931 1.00 60.03 O ANISOU 1564 OD1 ASP A 222 7474 8115 7218 517 747 660 O ATOM 1565 OD2 ASP A 222 14.361 35.910 24.432 1.00 61.40 O ANISOU 1565 OD2 ASP A 222 7548 8415 7363 565 785 784 O ATOM 1566 N CYS A 223 17.586 34.242 22.169 1.00 46.72 N ANISOU 1566 N CYS A 223 5694 6443 5613 334 606 689 N ATOM 1567 CA CYS A 223 17.350 33.323 21.057 1.00 47.77 C ANISOU 1567 CA CYS A 223 5783 6523 5842 292 571 739 C ATOM 1568 C CYS A 223 17.752 31.883 21.401 1.00 48.45 C ANISOU 1568 C CYS A 223 5822 6642 5945 283 547 800 C ATOM 1569 O CYS A 223 17.090 30.933 20.992 1.00 45.48 O ANISOU 1569 O CYS A 223 5399 6239 5642 273 534 879 O ATOM 1570 CB CYS A 223 18.102 33.770 19.803 1.00 49.17 C ANISOU 1570 CB CYS A 223 5999 6635 6045 234 528 666 C ATOM 1571 SG CYS A 223 17.364 35.198 18.968 1.00 47.51 S ANISOU 1571 SG CYS A 223 5839 6357 5853 237 545 622 S ATOM 1572 N CYS A 224 18.836 31.718 22.149 1.00 48.09 N ANISOU 1572 N CYS A 224 5791 6649 5831 286 538 765 N ATOM 1573 CA CYS A 224 19.291 30.389 22.506 1.00 49.84 C ANISOU 1573 CA CYS A 224 5976 6900 6061 287 515 820 C ATOM 1574 C CYS A 224 18.187 29.666 23.276 1.00 51.28 C ANISOU 1574 C CYS A 224 6110 7112 6261 326 551 931 C ATOM 1575 O CYS A 224 17.897 28.492 23.063 1.00 53.72 O ANISOU 1575 O CYS A 224 6381 7398 6631 312 530 1010 O ATOM 1576 CB CYS A 224 20.547 30.496 23.378 1.00 57.07 C ANISOU 1576 CB CYS A 224 6912 7885 6885 297 506 765 C ATOM 1577 SG CYS A 224 21.442 28.941 23.588 1.00 63.45 S ANISOU 1577 SG CYS A 224 7687 8721 7697 298 465 812 S ATOM 1578 N GLU A 225 17.535 30.393 24.156 1.00 50.53 N ANISOU 1578 N GLU A 225 6017 7066 6113 374 606 940 N ATOM 1579 CA GLU A 225 16.463 29.800 24.956 1.00 53.71 C ANISOU 1579 CA GLU A 225 6367 7514 6523 415 650 1051 C ATOM 1580 C GLU A 225 15.203 29.563 24.108 1.00 51.90 C ANISOU 1580 C GLU A 225 6093 7232 6394 395 653 1122 C ATOM 1581 O GLU A 225 14.583 28.501 24.165 1.00 52.02 O ANISOU 1581 O GLU A 225 6052 7245 6466 382 649 1226 O ATOM 1582 CB GLU A 225 16.187 30.700 26.158 1.00 56.68 C ANISOU 1582 CB GLU A 225 6765 7970 6801 485 711 1033 C ATOM 1583 CG GLU A 225 14.803 30.567 26.760 1.00 70.88 C ANISOU 1583 CG GLU A 225 8509 9815 8606 536 772 1136 C ATOM 1584 CD GLU A 225 14.589 31.432 28.002 1.00 79.95 C ANISOU 1584 CD GLU A 225 9685 11049 9642 620 834 1114 C ATOM 1585 OE1 GLU A 225 15.566 32.010 28.526 1.00 81.68 O ANISOU 1585 OE1 GLU A 225 9967 11292 9775 634 823 1022 O ATOM 1586 OE2 GLU A 225 13.424 31.534 28.449 1.00 88.25 O ANISOU 1586 OE2 GLU A 225 10693 12145 10690 673 893 1189 O ATOM 1587 N ASN A 226 14.805 30.552 23.320 1.00 51.56 N ANISOU 1587 N ASN A 226 6072 7144 6372 389 656 1069 N ATOM 1588 CA ASN A 226 13.521 30.430 22.603 1.00 50.80 C ANISOU 1588 CA ASN A 226 5927 7012 6362 379 661 1138 C ATOM 1589 C ASN A 226 13.556 29.548 21.371 1.00 48.22 C ANISOU 1589 C ASN A 226 5582 6604 6134 310 596 1160 C ATOM 1590 O ASN A 226 12.578 28.883 21.067 1.00 49.31 O ANISOU 1590 O ASN A 226 5663 6726 6347 291 588 1250 O ATOM 1591 CB ASN A 226 12.940 31.798 22.316 1.00 49.62 C ANISOU 1591 CB ASN A 226 5805 6852 6193 413 693 1087 C ATOM 1592 CG ASN A 226 12.403 32.431 23.579 1.00 53.94 C ANISOU 1592 CG ASN A 226 6351 7486 6659 496 766 1104 C ATOM 1593 OD1 ASN A 226 11.350 32.033 24.053 1.00 53.75 O ANISOU 1593 OD1 ASN A 226 6258 7512 6651 529 806 1204 O ATOM 1594 ND2 ASN A 226 13.158 33.355 24.168 1.00 54.47 N ANISOU 1594 ND2 ASN A 226 6491 7573 6632 529 780 1010 N ATOM 1595 N ALA A 227 14.688 29.516 20.677 1.00 48.54 N ANISOU 1595 N ALA A 227 5671 6597 6174 273 546 1081 N ATOM 1596 CA ALA A 227 14.824 28.579 19.575 1.00 47.52 C ANISOU 1596 CA ALA A 227 5534 6394 6126 219 482 1098 C ATOM 1597 C ALA A 227 14.784 27.148 20.089 1.00 47.07 C ANISOU 1597 C ALA A 227 5440 6347 6098 210 464 1188 C ATOM 1598 O ALA A 227 14.135 26.293 19.500 1.00 46.87 O ANISOU 1598 O ALA A 227 5384 6270 6155 174 428 1255 O ATOM 1599 CB ALA A 227 16.097 28.847 18.784 1.00 47.01 C ANISOU 1599 CB ALA A 227 5526 6292 6043 192 439 996 C ATOM 1600 N TYR A 228 15.436 26.901 21.219 1.00 51.92 N ANISOU 1600 N TYR A 228 6060 7025 6642 241 486 1194 N ATOM 1601 CA TYR A 228 15.414 25.573 21.829 1.00 51.86 C ANISOU 1601 CA TYR A 228 6023 7027 6652 239 474 1286 C ATOM 1602 C TYR A 228 14.019 25.215 22.302 1.00 51.81 C ANISOU 1602 C TYR A 228 5952 7044 6688 240 510 1406 C ATOM 1603 O TYR A 228 13.585 24.080 22.135 1.00 50.79 O ANISOU 1603 O TYR A 228 5794 6875 6629 204 478 1494 O ATOM 1604 CB TYR A 228 16.416 25.420 22.996 1.00 52.67 C ANISOU 1604 CB TYR A 228 6146 7203 6661 279 492 1269 C ATOM 1605 CG TYR A 228 16.364 23.997 23.556 1.00 51.83 C ANISOU 1605 CG TYR A 228 6016 7098 6578 278 477 1373 C ATOM 1606 CD1 TYR A 228 16.860 22.934 22.828 1.00 52.24 C ANISOU 1606 CD1 TYR A 228 6086 7075 6686 246 410 1381 C ATOM 1607 CD2 TYR A 228 15.752 23.719 24.766 1.00 53.94 C ANISOU 1607 CD2 TYR A 228 6245 7435 6814 310 528 1466 C ATOM 1608 CE1 TYR A 228 16.773 21.636 23.293 1.00 53.13 C ANISOU 1608 CE1 TYR A 228 6188 7172 6824 243 392 1478 C ATOM 1609 CE2 TYR A 228 15.653 22.415 25.238 1.00 54.34 C ANISOU 1609 CE2 TYR A 228 6277 7478 6891 303 513 1571 C ATOM 1610 CZ TYR A 228 16.167 21.385 24.496 1.00 52.96 C ANISOU 1610 CZ TYR A 228 6129 7218 6775 267 443 1575 C ATOM 1611 OH TYR A 228 16.101 20.095 24.952 1.00 58.71 O ANISOU 1611 OH TYR A 228 6851 7926 7530 260 423 1676 O ATOM 1612 N ARG A 229 13.314 26.166 22.899 1.00 54.34 N ANISOU 1612 N ARG A 229 6250 7428 6966 283 575 1413 N ATOM 1613 CA ARG A 229 11.946 25.892 23.349 1.00 54.15 C ANISOU 1613 CA ARG A 229 6152 7443 6979 289 616 1533 C ATOM 1614 C ARG A 229 11.071 25.454 22.185 1.00 53.89 C ANISOU 1614 C ARG A 229 6081 7334 7060 228 570 1580 C ATOM 1615 O ARG A 229 10.265 24.549 22.340 1.00 53.89 O ANISOU 1615 O ARG A 229 6021 7334 7121 196 565 1695 O ATOM 1616 CB ARG A 229 11.356 27.118 24.027 1.00 60.71 C ANISOU 1616 CB ARG A 229 6972 8354 7741 358 693 1516 C ATOM 1617 CG ARG A 229 9.859 27.012 24.320 1.00 73.70 C ANISOU 1617 CG ARG A 229 8530 10048 9424 371 740 1635 C ATOM 1618 CD ARG A 229 9.389 28.068 25.317 1.00 83.56 C ANISOU 1618 CD ARG A 229 9771 11396 10579 462 826 1629 C ATOM 1619 NE ARG A 229 10.143 27.930 26.562 1.00 90.22 N ANISOU 1619 NE ARG A 229 10645 12309 11324 508 857 1621 N ATOM 1620 CZ ARG A 229 10.810 28.903 27.185 1.00 91.36 C ANISOU 1620 CZ ARG A 229 10855 12493 11361 570 886 1523 C ATOM 1621 NH1 ARG A 229 10.793 30.160 26.743 1.00 89.14 N ANISOU 1621 NH1 ARG A 229 10623 12189 11056 597 894 1425 N ATOM 1622 NH2 ARG A 229 11.484 28.613 28.291 1.00 96.41 N ANISOU 1622 NH2 ARG A 229 11516 13197 11917 604 904 1526 N ATOM 1623 N HIS A 230 11.252 26.074 21.009 1.00 53.11 N ANISOU 1623 N HIS A 230 6018 7171 6990 207 533 1493 N ATOM 1624 CA HIS A 230 10.437 25.759 19.817 1.00 51.17 C ANISOU 1624 CA HIS A 230 5742 6853 6846 152 483 1525 C ATOM 1625 C HIS A 230 10.743 24.343 19.343 1.00 52.01 C ANISOU 1625 C HIS A 230 5856 6884 7021 91 408 1566 C ATOM 1626 O HIS A 230 9.833 23.560 19.024 1.00 50.43 O ANISOU 1626 O HIS A 230 5606 6651 6904 41 377 1658 O ATOM 1627 CB HIS A 230 10.709 26.794 18.727 1.00 54.27 C ANISOU 1627 CB HIS A 230 6183 7198 7237 154 463 1416 C ATOM 1628 CG HIS A 230 9.760 26.753 17.566 1.00 58.98 C ANISOU 1628 CG HIS A 230 6748 7739 7921 113 422 1442 C ATOM 1629 ND1 HIS A 230 10.148 27.083 16.282 1.00 52.44 N ANISOU 1629 ND1 HIS A 230 5969 6836 7118 89 369 1361 N ATOM 1630 CD2 HIS A 230 8.440 26.457 17.490 1.00 57.50 C ANISOU 1630 CD2 HIS A 230 6480 7565 7799 94 424 1542 C ATOM 1631 CE1 HIS A 230 9.121 26.970 15.464 1.00 53.46 C ANISOU 1631 CE1 HIS A 230 6056 6933 7323 58 337 1405 C ATOM 1632 NE2 HIS A 230 8.069 26.597 16.170 1.00 56.77 N ANISOU 1632 NE2 HIS A 230 6394 7406 7770 58 368 1515 N ATOM 1633 N TYR A 231 12.027 23.989 19.357 1.00 48.99 N ANISOU 1633 N TYR A 231 5537 6477 6600 96 379 1502 N ATOM 1634 CA TYR A 231 12.441 22.632 19.035 1.00 51.62 C ANISOU 1634 CA TYR A 231 5890 6739 6982 55 312 1536 C ATOM 1635 C TYR A 231 11.797 21.628 19.972 1.00 54.95 C ANISOU 1635 C TYR A 231 6263 7186 7430 41 326 1669 C ATOM 1636 O TYR A 231 11.301 20.600 19.521 1.00 54.17 O ANISOU 1636 O TYR A 231 6151 7017 7415 -15 270 1740 O ATOM 1637 CB TYR A 231 13.945 22.519 19.154 1.00 53.31 C ANISOU 1637 CB TYR A 231 6170 6952 7131 84 295 1451 C ATOM 1638 CG TYR A 231 14.579 21.173 18.896 1.00 52.62 C ANISOU 1638 CG TYR A 231 6119 6797 7075 65 229 1472 C ATOM 1639 CD1 TYR A 231 14.608 20.194 19.882 1.00 53.70 C ANISOU 1639 CD1 TYR A 231 6245 6953 7206 72 235 1560 C ATOM 1640 CD2 TYR A 231 15.243 20.920 17.699 1.00 52.90 C ANISOU 1640 CD2 TYR A 231 6207 6754 7135 49 163 1397 C ATOM 1641 CE1 TYR A 231 15.260 18.994 19.670 1.00 52.67 C ANISOU 1641 CE1 TYR A 231 6159 6755 7097 65 174 1573 C ATOM 1642 CE2 TYR A 231 15.909 19.730 17.483 1.00 52.74 C ANISOU 1642 CE2 TYR A 231 6231 6674 7134 48 104 1406 C ATOM 1643 CZ TYR A 231 15.902 18.767 18.476 1.00 53.81 C ANISOU 1643 CZ TYR A 231 6358 6820 7265 56 108 1494 C ATOM 1644 OH TYR A 231 16.559 17.585 18.268 1.00 51.75 O ANISOU 1644 OH TYR A 231 6149 6492 7020 63 48 1503 O ATOM 1645 N GLN A 232 11.834 21.946 21.264 1.00 57.07 N ANISOU 1645 N GLN A 232 6507 7551 7623 91 398 1701 N ATOM 1646 CA GLN A 232 11.227 21.140 22.332 1.00 61.26 C ANISOU 1646 CA GLN A 232 6986 8128 8160 88 430 1834 C ATOM 1647 C GLN A 232 9.746 20.881 22.093 1.00 65.01 C ANISOU 1647 C GLN A 232 7379 8598 8721 37 432 1946 C ATOM 1648 O GLN A 232 9.302 19.744 22.219 1.00 61.56 O ANISOU 1648 O GLN A 232 6916 8125 8348 -14 401 2054 O ATOM 1649 CB GLN A 232 11.390 21.851 23.675 1.00 66.25 C ANISOU 1649 CB GLN A 232 7605 8881 8684 163 517 1835 C ATOM 1650 CG GLN A 232 11.448 20.951 24.877 1.00 75.05 C ANISOU 1650 CG GLN A 232 8701 10046 9767 178 544 1939 C ATOM 1651 CD GLN A 232 11.586 21.740 26.164 1.00 77.27 C ANISOU 1651 CD GLN A 232 8974 10451 9931 260 628 1930 C ATOM 1652 OE1 GLN A 232 12.584 21.633 26.871 1.00 73.57 O ANISOU 1652 OE1 GLN A 232 8549 10018 9384 301 634 1893 O ATOM 1653 NE2 GLN A 232 10.573 22.541 26.471 1.00 82.94 N ANISOU 1653 NE2 GLN A 232 9637 11240 10636 288 693 1962 N ATOM 1654 N ASN A 233 8.995 21.925 21.727 1.00 62.91 N ANISOU 1654 N ASN A 233 7075 8366 8459 52 465 1921 N ATOM 1655 CA ASN A 233 7.570 21.775 21.426 1.00 67.28 C ANISOU 1655 CA ASN A 233 7541 8927 9095 7 465 2023 C ATOM 1656 C ASN A 233 7.356 20.841 20.249 1.00 66.15 C ANISOU 1656 C ASN A 233 7407 8664 9061 -82 364 2041 C ATOM 1657 O ASN A 233 6.314 20.203 20.148 1.00 66.06 O ANISOU 1657 O ASN A 233 7326 8644 9130 -145 344 2154 O ATOM 1658 CB ASN A 233 6.906 23.131 21.097 1.00 65.52 C ANISOU 1658 CB ASN A 233 7287 8755 8853 49 510 1976 C ATOM 1659 CG ASN A 233 6.893 24.077 22.282 1.00 72.23 C ANISOU 1659 CG ASN A 233 8124 9723 9596 142 610 1967 C ATOM 1660 OD1 ASN A 233 7.160 23.679 23.416 1.00 75.83 O ANISOU 1660 OD1 ASN A 233 8574 10238 9997 171 652 2019 O ATOM 1661 ND2 ASN A 233 6.615 25.343 22.023 1.00 79.24 N ANISOU 1661 ND2 ASN A 233 9017 10640 10449 195 646 1898 N ATOM 1662 N ARG A 234 8.326 20.786 19.343 1.00 62.35 N ANISOU 1662 N ARG A 234 7013 8095 8582 -90 301 1931 N ATOM 1663 CA ARG A 234 8.210 19.918 18.181 1.00 64.22 C ANISOU 1663 CA ARG A 234 7275 8214 8912 -165 200 1933 C ATOM 1664 C ARG A 234 8.777 18.511 18.360 1.00 61.63 C ANISOU 1664 C ARG A 234 6994 7810 8611 -200 143 1976 C ATOM 1665 O ARG A 234 8.501 17.648 17.562 1.00 65.04 O ANISOU 1665 O ARG A 234 7444 8142 9125 -267 59 2001 O ATOM 1666 CB ARG A 234 8.887 20.568 16.986 1.00 66.04 C ANISOU 1666 CB ARG A 234 7574 8386 9131 -150 159 1795 C ATOM 1667 CG ARG A 234 8.159 21.812 16.525 1.00 66.04 C ANISOU 1667 CG ARG A 234 7534 8429 9128 -131 193 1762 C ATOM 1668 CD ARG A 234 8.882 22.463 15.371 1.00 64.27 C ANISOU 1668 CD ARG A 234 7382 8149 8887 -117 156 1631 C ATOM 1669 NE ARG A 234 7.942 23.255 14.598 1.00 63.61 N ANISOU 1669 NE ARG A 234 7260 8070 8838 -124 154 1625 N ATOM 1670 CZ ARG A 234 8.264 24.051 13.596 1.00 63.67 C ANISOU 1670 CZ ARG A 234 7314 8044 8832 -109 135 1527 C ATOM 1671 NH1 ARG A 234 9.543 24.197 13.229 1.00 61.30 N ANISOU 1671 NH1 ARG A 234 7098 7709 8483 -89 119 1425 N ATOM 1672 NH2 ARG A 234 7.298 24.736 12.978 1.00 62.65 N ANISOU 1672 NH2 ARG A 234 7143 7924 8735 -111 135 1537 N ATOM 1673 N VAL A 235 9.607 18.291 19.357 1.00 62.74 N ANISOU 1673 N VAL A 235 7164 7992 8680 -152 181 1978 N ATOM 1674 CA VAL A 235 10.303 17.020 19.494 1.00 64.91 C ANISOU 1674 CA VAL A 235 7499 8192 8970 -169 126 2004 C ATOM 1675 C VAL A 235 9.983 16.545 20.898 1.00 68.32 C ANISOU 1675 C VAL A 235 7884 8696 9376 -160 185 2128 C ATOM 1676 O VAL A 235 10.649 16.906 21.870 1.00 71.48 O ANISOU 1676 O VAL A 235 8294 9179 9684 -91 246 2108 O ATOM 1677 CB VAL A 235 11.818 17.195 19.303 1.00 62.33 C ANISOU 1677 CB VAL A 235 7260 7850 8569 -108 112 1878 C ATOM 1678 CG1 VAL A 235 12.528 15.853 19.342 1.00 64.77 C ANISOU 1678 CG1 VAL A 235 7636 8076 8895 -114 49 1902 C ATOM 1679 CG2 VAL A 235 12.129 17.910 17.995 1.00 64.45 C ANISOU 1679 CG2 VAL A 235 7566 8075 8846 -107 75 1755 C ATOM 1680 N GLU A 236 8.947 15.736 21.017 1.00 76.51 N ANISOU 1680 N GLU A 236 8868 9706 10496 -233 164 2260 N ATOM 1681 CA GLU A 236 8.402 15.440 22.337 1.00 79.97 C ANISOU 1681 CA GLU A 236 9240 10232 10911 -229 233 2395 C ATOM 1682 C GLU A 236 9.361 14.622 23.191 1.00 72.90 C ANISOU 1682 C GLU A 236 8406 9327 9963 -193 234 2419 C ATOM 1683 O GLU A 236 10.021 13.713 22.702 1.00 72.28 O ANISOU 1683 O GLU A 236 8408 9137 9917 -213 156 2396 O ATOM 1684 CB GLU A 236 7.067 14.722 22.212 1.00 90.50 C ANISOU 1684 CB GLU A 236 10497 11538 12351 -328 206 2540 C ATOM 1685 CG GLU A 236 6.111 15.059 23.339 1.00 94.93 C ANISOU 1685 CG GLU A 236 10946 12236 12884 -315 305 2665 C ATOM 1686 CD GLU A 236 4.817 14.327 23.170 1.00 98.88 C ANISOU 1686 CD GLU A 236 11361 12714 13494 -423 274 2814 C ATOM 1687 OE1 GLU A 236 3.776 14.987 22.985 1.00106.14 O ANISOU 1687 OE1 GLU A 236 12182 13705 14440 -437 308 2849 O ATOM 1688 OE2 GLU A 236 4.861 13.083 23.187 1.00104.22 O ANISOU 1688 OE2 GLU A 236 12071 13295 14231 -494 211 2894 O ATOM 1689 N GLY A 237 9.457 14.991 24.463 1.00 70.98 N ANISOU 1689 N GLY A 237 8130 9207 9633 -130 323 2461 N ATOM 1690 CA GLY A 237 10.305 14.291 25.414 1.00 67.37 C ANISOU 1690 CA GLY A 237 7721 8761 9113 -87 334 2494 C ATOM 1691 C GLY A 237 11.791 14.523 25.249 1.00 65.44 C ANISOU 1691 C GLY A 237 7566 8502 8794 -16 311 2353 C ATOM 1692 O GLY A 237 12.579 13.788 25.797 1.00 66.53 O ANISOU 1692 O GLY A 237 7755 8627 8895 14 296 2372 O ATOM 1693 N VAL A 238 12.199 15.546 24.506 1.00 63.39 N ANISOU 1693 N VAL A 238 7324 8250 8510 9 308 2215 N ATOM 1694 CA VAL A 238 13.615 15.803 24.352 1.00 60.02 C ANISOU 1694 CA VAL A 238 6970 7821 8011 70 288 2087 C ATOM 1695 C VAL A 238 14.194 16.404 25.631 1.00 58.50 C ANISOU 1695 C VAL A 238 6770 7758 7697 150 364 2072 C ATOM 1696 O VAL A 238 13.534 17.179 26.307 1.00 58.48 O ANISOU 1696 O VAL A 238 6711 7853 7656 171 438 2102 O ATOM 1697 CB VAL A 238 13.893 16.701 23.150 1.00 62.02 C ANISOU 1697 CB VAL A 238 7246 8042 8276 66 261 1952 C ATOM 1698 CG1 VAL A 238 13.503 18.148 23.440 1.00 62.70 C ANISOU 1698 CG1 VAL A 238 7286 8229 8308 97 336 1906 C ATOM 1699 CG2 VAL A 238 15.363 16.598 22.774 1.00 64.23 C ANISOU 1699 CG2 VAL A 238 7602 8294 8507 110 219 1840 C ATOM 1700 N ASP A 239 15.428 16.045 25.962 1.00 58.23 N ANISOU 1700 N ASP A 239 6793 7731 7601 200 344 2024 N ATOM 1701 CA ASP A 239 16.057 16.551 27.178 1.00 60.97 C ANISOU 1701 CA ASP A 239 7137 8200 7828 275 404 2005 C ATOM 1702 C ASP A 239 17.392 17.239 26.907 1.00 57.54 C ANISOU 1702 C ASP A 239 6749 7793 7320 322 387 1856 C ATOM 1703 O ASP A 239 18.268 16.667 26.270 1.00 61.90 O ANISOU 1703 O ASP A 239 7349 8279 7888 325 324 1807 O ATOM 1704 CB ASP A 239 16.275 15.406 28.150 1.00 64.44 C ANISOU 1704 CB ASP A 239 7589 8648 8244 298 403 2115 C ATOM 1705 CG ASP A 239 16.893 15.865 29.453 1.00 68.39 C ANISOU 1705 CG ASP A 239 8087 9280 8615 378 462 2103 C ATOM 1706 OD1 ASP A 239 16.135 16.117 30.397 1.00 77.56 O ANISOU 1706 OD1 ASP A 239 9201 10527 9741 393 531 2184 O ATOM 1707 OD2 ASP A 239 18.123 16.014 29.532 1.00 67.55 O ANISOU 1707 OD2 ASP A 239 8023 9200 8440 427 439 2010 O ATOM 1708 N TYR A 240 17.582 18.430 27.466 1.00 59.53 N ANISOU 1708 N TYR A 240 6986 8146 7486 362 442 1790 N ATOM 1709 CA TYR A 240 18.773 19.227 27.137 1.00 58.51 C ANISOU 1709 CA TYR A 240 6893 8044 7294 390 425 1647 C ATOM 1710 C TYR A 240 20.088 18.554 27.520 1.00 58.54 C ANISOU 1710 C TYR A 240 6933 8068 7239 435 389 1623 C ATOM 1711 O TYR A 240 21.072 18.731 26.799 1.00 55.37 O ANISOU 1711 O TYR A 240 6561 7646 6829 438 346 1525 O ATOM 1712 CB TYR A 240 18.724 20.626 27.743 1.00 57.94 C ANISOU 1712 CB TYR A 240 6807 8070 7137 422 485 1581 C ATOM 1713 CG TYR A 240 19.778 21.579 27.173 1.00 56.14 C ANISOU 1713 CG TYR A 240 6613 7852 6866 425 462 1434 C ATOM 1714 CD1 TYR A 240 19.707 22.035 25.857 1.00 55.79 C ANISOU 1714 CD1 TYR A 240 6579 7731 6885 379 432 1366 C ATOM 1715 CD2 TYR A 240 20.839 22.025 27.955 1.00 57.88 C ANISOU 1715 CD2 TYR A 240 6851 8159 6979 469 469 1368 C ATOM 1716 CE1 TYR A 240 20.660 22.917 25.343 1.00 55.38 C ANISOU 1716 CE1 TYR A 240 6555 7692 6794 376 414 1242 C ATOM 1717 CE2 TYR A 240 21.804 22.897 27.450 1.00 57.42 C ANISOU 1717 CE2 TYR A 240 6817 8113 6884 460 447 1242 C ATOM 1718 CZ TYR A 240 21.703 23.349 26.148 1.00 55.95 C ANISOU 1718 CZ TYR A 240 6641 7851 6765 412 422 1182 C ATOM 1719 OH TYR A 240 22.660 24.216 25.648 1.00 57.90 O ANISOU 1719 OH TYR A 240 6911 8113 6976 397 402 1066 O ATOM 1720 N ARG A 241 20.128 17.794 28.616 1.00 60.82 N ANISOU 1720 N ARG A 241 7219 8402 7487 472 406 1715 N ATOM 1721 CA ARG A 241 21.347 17.052 28.927 1.00 65.32 C ANISOU 1721 CA ARG A 241 7824 8986 8007 520 366 1702 C ATOM 1722 C ARG A 241 21.377 15.711 28.222 1.00 64.42 C ANISOU 1722 C ARG A 241 7744 8752 7980 499 303 1758 C ATOM 1723 O ARG A 241 22.358 15.402 27.553 1.00 70.06 O ANISOU 1723 O ARG A 241 8495 9429 8694 518 249 1688 O ATOM 1724 CB ARG A 241 21.594 16.839 30.425 1.00 77.15 C ANISOU 1724 CB ARG A 241 9315 10589 9407 581 405 1763 C ATOM 1725 CG ARG A 241 22.963 16.160 30.660 1.00 87.31 C ANISOU 1725 CG ARG A 241 10637 11898 10638 638 358 1735 C ATOM 1726 CD ARG A 241 23.389 16.004 32.117 1.00 96.39 C ANISOU 1726 CD ARG A 241 11784 13163 11677 707 389 1780 C ATOM 1727 NE ARG A 241 22.320 15.430 32.930 1.00100.32 N ANISOU 1727 NE ARG A 241 12264 13663 12188 705 434 1925 N ATOM 1728 CZ ARG A 241 21.480 16.123 33.701 1.00107.14 C ANISOU 1728 CZ ARG A 241 13093 14605 13011 709 504 1962 C ATOM 1729 NH1 ARG A 241 21.573 17.446 33.807 1.00108.76 N ANISOU 1729 NH1 ARG A 241 13284 14882 13155 717 535 1859 N ATOM 1730 NH2 ARG A 241 20.534 15.483 34.383 1.00108.02 N ANISOU 1730 NH2 ARG A 241 13182 14720 13139 705 544 2106 N ATOM 1731 N GLU A 242 20.315 14.929 28.347 1.00 63.65 N ANISOU 1731 N GLU A 242 7636 8593 7954 461 307 1883 N ATOM 1732 CA GLU A 242 20.345 13.515 27.933 1.00 66.29 C ANISOU 1732 CA GLU A 242 8015 8810 8360 447 244 1954 C ATOM 1733 C GLU A 242 20.241 13.249 26.438 1.00 61.44 C ANISOU 1733 C GLU A 242 7432 8067 7842 397 177 1903 C ATOM 1734 O GLU A 242 20.791 12.272 25.976 1.00 63.39 O ANISOU 1734 O GLU A 242 7737 8229 8118 412 114 1904 O ATOM 1735 CB GLU A 242 19.228 12.717 28.623 1.00 71.17 C ANISOU 1735 CB GLU A 242 8611 9403 9024 412 267 2117 C ATOM 1736 CG GLU A 242 19.246 12.806 30.140 1.00 80.66 C ANISOU 1736 CG GLU A 242 9786 10730 10130 465 333 2189 C ATOM 1737 CD GLU A 242 20.608 12.457 30.723 1.00 87.30 C ANISOU 1737 CD GLU A 242 10670 11621 10877 550 313 2150 C ATOM 1738 OE1 GLU A 242 21.181 11.423 30.319 1.00 91.88 O ANISOU 1738 OE1 GLU A 242 11307 12113 11490 564 249 2163 O ATOM 1739 OE2 GLU A 242 21.116 13.215 31.579 1.00 93.60 O ANISOU 1739 OE2 GLU A 242 11448 12547 11566 606 358 2105 O ATOM 1740 N SER A 243 19.508 14.065 25.686 1.00 59.50 N ANISOU 1740 N SER A 243 7642 7310 7655 522 -71 1562 N ATOM 1741 CA SER A 243 19.320 13.801 24.256 1.00 57.56 C ANISOU 1741 CA SER A 243 7394 7030 7447 493 -90 1541 C ATOM 1742 C SER A 243 20.515 14.227 23.373 1.00 56.93 C ANISOU 1742 C SER A 243 7311 6932 7386 545 -105 1462 C ATOM 1743 O SER A 243 20.604 13.829 22.220 1.00 56.54 O ANISOU 1743 O SER A 243 7272 6844 7364 530 -129 1439 O ATOM 1744 CB SER A 243 18.032 14.474 23.751 1.00 59.68 C ANISOU 1744 CB SER A 243 7602 7349 7723 446 -55 1567 C ATOM 1745 OG SER A 243 16.974 14.316 24.684 1.00 62.83 O ANISOU 1745 OG SER A 243 7988 7786 8096 406 -33 1636 O ATOM 1746 N PHE A 244 21.435 15.023 23.901 1.00 54.65 N ANISOU 1746 N PHE A 244 7009 6675 7078 601 -91 1422 N ATOM 1747 CA PHE A 244 22.544 15.528 23.092 1.00 53.53 C ANISOU 1747 CA PHE A 244 6857 6530 6950 644 -101 1349 C ATOM 1748 C PHE A 244 23.891 15.157 23.679 1.00 52.52 C ANISOU 1748 C PHE A 244 6763 6390 6801 701 -128 1318 C ATOM 1749 O PHE A 244 24.229 15.607 24.760 1.00 55.68 O ANISOU 1749 O PHE A 244 7157 6828 7169 727 -111 1320 O ATOM 1750 CB PHE A 244 22.415 17.046 22.940 1.00 53.00 C ANISOU 1750 CB PHE A 244 6735 6522 6879 654 -55 1319 C ATOM 1751 CG PHE A 244 21.067 17.475 22.433 1.00 50.49 C ANISOU 1751 CG PHE A 244 6379 6226 6576 608 -26 1353 C ATOM 1752 CD1 PHE A 244 20.698 17.239 21.103 1.00 49.59 C ANISOU 1752 CD1 PHE A 244 6256 6089 6496 578 -40 1343 C ATOM 1753 CD2 PHE A 244 20.151 18.091 23.278 1.00 51.97 C ANISOU 1753 CD2 PHE A 244 6540 6464 6741 596 15 1395 C ATOM 1754 CE1 PHE A 244 19.446 17.597 20.644 1.00 50.21 C ANISOU 1754 CE1 PHE A 244 6296 6196 6583 537 -14 1377 C ATOM 1755 CE2 PHE A 244 18.893 18.464 22.812 1.00 50.55 C ANISOU 1755 CE2 PHE A 244 6321 6315 6570 559 42 1429 C ATOM 1756 CZ PHE A 244 18.540 18.235 21.495 1.00 47.26 C ANISOU 1756 CZ PHE A 244 5892 5877 6185 530 28 1420 C ATOM 1757 N ASP A 245 24.656 14.334 22.963 1.00 52.40 N ANISOU 1757 N ASP A 245 6783 6326 6800 723 -170 1288 N ATOM 1758 CA ASP A 245 25.992 13.933 23.423 1.00 52.60 C ANISOU 1758 CA ASP A 245 6838 6346 6802 785 -199 1257 C ATOM 1759 C ASP A 245 26.964 15.100 23.356 1.00 55.05 C ANISOU 1759 C ASP A 245 7104 6715 7099 824 -181 1194 C ATOM 1760 O ASP A 245 27.835 15.219 24.205 1.00 52.68 O ANISOU 1760 O ASP A 245 6806 6444 6764 866 -185 1179 O ATOM 1761 CB ASP A 245 26.517 12.806 22.562 1.00 54.92 C ANISOU 1761 CB ASP A 245 7179 6574 7112 803 -246 1240 C ATOM 1762 CG ASP A 245 25.642 11.556 22.654 1.00 56.23 C ANISOU 1762 CG ASP A 245 7404 6673 7287 761 -267 1300 C ATOM 1763 OD1 ASP A 245 25.554 11.037 23.772 1.00 60.86 O ANISOU 1763 OD1 ASP A 245 8024 7251 7847 766 -271 1344 O ATOM 1764 OD2 ASP A 245 25.038 11.106 21.645 1.00 56.28 O ANISOU 1764 OD2 ASP A 245 7425 6637 7323 719 -279 1306 O ATOM 1765 N TYR A 246 26.827 15.953 22.332 1.00 52.05 N ANISOU 1765 N TYR A 246 6683 6351 6742 806 -163 1158 N ATOM 1766 CA TYR A 246 27.600 17.190 22.239 1.00 49.30 C ANISOU 1766 CA TYR A 246 6293 6058 6378 829 -140 1102 C ATOM 1767 C TYR A 246 26.721 18.344 21.825 1.00 51.31 C ANISOU 1767 C TYR A 246 6509 6338 6647 791 -96 1103 C ATOM 1768 O TYR A 246 25.623 18.131 21.303 1.00 52.37 O ANISOU 1768 O TYR A 246 6639 6449 6807 752 -89 1138 O ATOM 1769 CB TYR A 246 28.714 17.030 21.227 1.00 52.17 C ANISOU 1769 CB TYR A 246 6655 6416 6751 860 -170 1041 C ATOM 1770 CG TYR A 246 29.654 15.923 21.600 1.00 52.47 C ANISOU 1770 CG TYR A 246 6731 6432 6770 910 -213 1037 C ATOM 1771 CD1 TYR A 246 30.714 16.144 22.487 1.00 53.56 C ANISOU 1771 CD1 TYR A 246 6864 6619 6867 955 -217 1014 C ATOM 1772 CD2 TYR A 246 29.456 14.654 21.125 1.00 54.95 C ANISOU 1772 CD2 TYR A 246 7092 6680 7103 912 -249 1059 C ATOM 1773 CE1 TYR A 246 31.566 15.099 22.879 1.00 56.83 C ANISOU 1773 CE1 TYR A 246 7314 7018 7259 1009 -257 1015 C ATOM 1774 CE2 TYR A 246 30.291 13.610 21.506 1.00 57.27 C ANISOU 1774 CE2 TYR A 246 7432 6951 7377 966 -288 1058 C ATOM 1775 CZ TYR A 246 31.335 13.833 22.380 1.00 55.33 C ANISOU 1775 CZ TYR A 246 7175 6757 7090 1017 -292 1038 C ATOM 1776 OH TYR A 246 32.151 12.776 22.706 1.00 57.01 O ANISOU 1776 OH TYR A 246 7432 6949 7280 1077 -331 1039 O ATOM 1777 N LEU A 247 27.212 19.560 22.074 1.00 48.93 N ANISOU 1777 N LEU A 247 6180 6086 6324 804 -66 1065 N ATOM 1778 CA LEU A 247 26.570 20.765 21.620 1.00 49.35 C ANISOU 1778 CA LEU A 247 6201 6162 6385 780 -24 1056 C ATOM 1779 C LEU A 247 27.557 21.645 20.856 1.00 50.61 C ANISOU 1779 C LEU A 247 6342 6344 6541 792 -20 987 C ATOM 1780 O LEU A 247 28.720 21.872 21.302 1.00 48.08 O ANISOU 1780 O LEU A 247 6022 6053 6191 818 -29 947 O ATOM 1781 CB LEU A 247 25.983 21.532 22.788 1.00 50.65 C ANISOU 1781 CB LEU A 247 6360 6362 6520 775 17 1085 C ATOM 1782 CG LEU A 247 24.922 20.753 23.589 1.00 54.11 C ANISOU 1782 CG LEU A 247 6813 6789 6957 758 18 1158 C ATOM 1783 CD1 LEU A 247 24.650 21.419 24.935 1.00 53.71 C ANISOU 1783 CD1 LEU A 247 6759 6779 6866 766 54 1179 C ATOM 1784 CD2 LEU A 247 23.641 20.583 22.811 1.00 51.94 C ANISOU 1784 CD2 LEU A 247 6523 6497 6714 720 28 1196 C ATOM 1785 N SER A 248 27.099 22.130 19.695 1.00 48.38 N ANISOU 1785 N SER A 248 6041 6053 6288 771 -7 974 N ATOM 1786 CA SER A 248 27.856 23.117 18.923 1.00 47.02 C ANISOU 1786 CA SER A 248 5850 5903 6112 774 4 914 C ATOM 1787 C SER A 248 27.042 24.383 18.796 1.00 48.48 C ANISOU 1787 C SER A 248 6021 6104 6294 755 54 920 C ATOM 1788 O SER A 248 25.809 24.323 18.620 1.00 47.45 O ANISOU 1788 O SER A 248 5885 5962 6183 737 71 966 O ATOM 1789 CB SER A 248 28.258 22.546 17.571 1.00 50.27 C ANISOU 1789 CB SER A 248 6256 6289 6554 774 -28 885 C ATOM 1790 OG SER A 248 29.451 21.771 17.679 1.00 56.03 O ANISOU 1790 OG SER A 248 6997 7021 7271 806 -69 856 O ATOM 1791 N PHE A 249 27.733 25.518 18.919 1.00 48.31 N ANISOU 1791 N PHE A 249 5997 6112 6245 759 78 876 N ATOM 1792 CA PHE A 249 27.128 26.850 18.928 1.00 47.90 C ANISOU 1792 CA PHE A 249 5944 6073 6181 748 129 875 C ATOM 1793 C PHE A 249 27.826 27.755 17.930 1.00 49.74 C ANISOU 1793 C PHE A 249 6172 6314 6413 739 137 818 C ATOM 1794 O PHE A 249 29.019 27.599 17.658 1.00 46.16 O ANISOU 1794 O PHE A 249 5715 5873 5951 741 111 772 O ATOM 1795 CB PHE A 249 27.304 27.542 20.293 1.00 48.47 C ANISOU 1795 CB PHE A 249 6034 6174 6207 756 157 875 C ATOM 1796 CG PHE A 249 26.624 26.850 21.478 1.00 48.64 C ANISOU 1796 CG PHE A 249 6063 6197 6219 765 157 931 C ATOM 1797 CD1 PHE A 249 27.173 25.702 22.056 1.00 49.33 C ANISOU 1797 CD1 PHE A 249 6157 6282 6304 777 116 942 C ATOM 1798 CD2 PHE A 249 25.501 27.393 22.058 1.00 50.49 C ANISOU 1798 CD2 PHE A 249 6300 6440 6442 765 198 973 C ATOM 1799 CE1 PHE A 249 26.588 25.092 23.149 1.00 47.63 C ANISOU 1799 CE1 PHE A 249 5950 6068 6076 783 117 994 C ATOM 1800 CE2 PHE A 249 24.901 26.796 23.168 1.00 50.22 C ANISOU 1800 CE2 PHE A 249 6270 6413 6395 771 199 1024 C ATOM 1801 CZ PHE A 249 25.448 25.650 23.716 1.00 49.45 C ANISOU 1801 CZ PHE A 249 6181 6310 6297 777 158 1035 C ATOM 1802 N HIS A 250 27.092 28.737 17.411 1.00 47.67 N ANISOU 1802 N HIS A 250 5910 6047 6155 729 176 823 N ATOM 1803 CA HIS A 250 27.721 29.905 16.856 1.00 47.19 C ANISOU 1803 CA HIS A 250 5857 5994 6076 719 197 772 C ATOM 1804 C HIS A 250 28.582 30.495 17.975 1.00 47.98 C ANISOU 1804 C HIS A 250 5978 6121 6128 719 209 743 C ATOM 1805 O HIS A 250 28.094 30.730 19.072 1.00 45.86 O ANISOU 1805 O HIS A 250 5726 5860 5836 728 233 770 O ATOM 1806 CB HIS A 250 26.714 30.958 16.415 1.00 48.99 C ANISOU 1806 CB HIS A 250 6094 6213 6307 717 244 789 C ATOM 1807 CG HIS A 250 27.364 32.230 15.987 1.00 51.27 C ANISOU 1807 CG HIS A 250 6403 6505 6571 704 269 739 C ATOM 1808 ND1 HIS A 250 28.344 32.265 15.013 1.00 52.65 N ANISOU 1808 ND1 HIS A 250 6567 6683 6752 686 247 691 N ATOM 1809 CD2 HIS A 250 27.219 33.498 16.421 1.00 51.22 C ANISOU 1809 CD2 HIS A 250 6433 6499 6529 704 315 729 C ATOM 1810 CE1 HIS A 250 28.775 33.502 14.875 1.00 50.49 C ANISOU 1810 CE1 HIS A 250 6322 6412 6449 670 278 654 C ATOM 1811 NE2 HIS A 250 28.100 34.270 15.706 1.00 51.61 N ANISOU 1811 NE2 HIS A 250 6495 6548 6565 681 319 676 N ATOM 1812 N THR A 251 29.854 30.738 17.671 1.00 47.14 N ANISOU 1812 N THR A 251 5870 6036 6004 706 192 687 N ATOM 1813 CA THR A 251 30.854 31.041 18.675 1.00 47.53 C ANISOU 1813 CA THR A 251 5931 6120 6005 702 191 656 C ATOM 1814 C THR A 251 31.565 32.352 18.366 1.00 50.63 C ANISOU 1814 C THR A 251 6342 6529 6365 671 217 603 C ATOM 1815 O THR A 251 32.603 32.360 17.692 1.00 48.40 O ANISOU 1815 O THR A 251 6043 6270 6077 655 195 557 O ATOM 1816 CB THR A 251 31.884 29.885 18.740 1.00 49.08 C ANISOU 1816 CB THR A 251 6103 6341 6204 716 138 639 C ATOM 1817 OG1 THR A 251 31.222 28.663 19.118 1.00 46.53 O ANISOU 1817 OG1 THR A 251 5775 5996 5907 741 115 691 O ATOM 1818 CG2 THR A 251 32.951 30.198 19.760 1.00 49.80 C ANISOU 1818 CG2 THR A 251 6199 6480 6241 711 135 607 C ATOM 1819 N PRO A 252 30.999 33.474 18.825 1.00 51.95 N ANISOU 1819 N PRO A 252 6546 6684 6507 663 264 608 N ATOM 1820 CA PRO A 252 31.683 34.758 18.642 1.00 52.58 C ANISOU 1820 CA PRO A 252 6657 6773 6548 629 290 558 C ATOM 1821 C PRO A 252 33.045 34.739 19.332 1.00 50.74 C ANISOU 1821 C PRO A 252 6419 6591 6270 607 269 514 C ATOM 1822 O PRO A 252 33.999 35.283 18.815 1.00 49.15 O ANISOU 1822 O PRO A 252 6216 6411 6045 572 265 464 O ATOM 1823 CB PRO A 252 30.748 35.771 19.338 1.00 52.48 C ANISOU 1823 CB PRO A 252 6693 6736 6511 636 344 580 C ATOM 1824 CG PRO A 252 29.405 35.142 19.298 1.00 53.46 C ANISOU 1824 CG PRO A 252 6800 6836 6675 673 348 642 C ATOM 1825 CD PRO A 252 29.649 33.641 19.380 1.00 53.83 C ANISOU 1825 CD PRO A 252 6802 6898 6752 686 297 661 C ATOM 1826 N PHE A 253 33.084 34.127 20.514 1.00 50.00 N ANISOU 1826 N PHE A 253 6319 6516 6159 627 256 534 N ATOM 1827 CA PHE A 253 34.311 33.777 21.250 1.00 48.46 C ANISOU 1827 CA PHE A 253 6108 6379 5926 619 227 503 C ATOM 1828 C PHE A 253 33.849 32.791 22.321 1.00 46.16 C ANISOU 1828 C PHE A 253 5808 6089 5639 658 211 551 C ATOM 1829 O PHE A 253 32.675 32.780 22.689 1.00 45.70 O ANISOU 1829 O PHE A 253 5768 5996 5599 677 235 597 O ATOM 1830 CB PHE A 253 34.979 35.008 21.870 1.00 50.75 C ANISOU 1830 CB PHE A 253 6433 6696 6152 576 255 459 C ATOM 1831 CG PHE A 253 34.053 35.861 22.715 1.00 54.34 C ANISOU 1831 CG PHE A 253 6940 7119 6585 579 303 482 C ATOM 1832 CD1 PHE A 253 33.308 36.900 22.140 1.00 56.90 C ANISOU 1832 CD1 PHE A 253 7307 7395 6915 569 347 483 C ATOM 1833 CD2 PHE A 253 33.950 35.656 24.088 1.00 58.25 C ANISOU 1833 CD2 PHE A 253 7446 7634 7050 594 306 501 C ATOM 1834 CE1 PHE A 253 32.465 37.697 22.920 1.00 57.92 C ANISOU 1834 CE1 PHE A 253 7488 7497 7020 579 393 503 C ATOM 1835 CE2 PHE A 253 33.103 36.449 24.882 1.00 59.45 C ANISOU 1835 CE2 PHE A 253 7648 7760 7179 601 352 520 C ATOM 1836 CZ PHE A 253 32.356 37.462 24.301 1.00 58.52 C ANISOU 1836 CZ PHE A 253 7572 7595 7067 596 396 521 C ATOM 1837 N GLY A 254 34.745 31.934 22.784 1.00 48.21 N ANISOU 1837 N GLY A 254 6040 6392 5883 672 171 541 N ATOM 1838 CA GLY A 254 34.385 30.830 23.673 1.00 51.77 C ANISOU 1838 CA GLY A 254 6484 6842 6342 711 150 588 C ATOM 1839 C GLY A 254 33.697 31.191 24.987 1.00 52.34 C ANISOU 1839 C GLY A 254 6587 6912 6388 716 181 619 C ATOM 1840 O GLY A 254 32.761 30.508 25.408 1.00 50.60 O ANISOU 1840 O GLY A 254 6369 6665 6192 742 181 674 O ATOM 1841 N GLY A 255 34.159 32.265 25.635 1.00 56.93 N ANISOU 1841 N GLY A 255 7192 7522 6916 687 208 585 N ATOM 1842 CA GLY A 255 33.586 32.741 26.907 1.00 53.68 C ANISOU 1842 CA GLY A 255 6814 7111 6470 691 240 607 C ATOM 1843 C GLY A 255 32.092 32.930 26.855 1.00 57.29 C ANISOU 1843 C GLY A 255 7291 7516 6958 709 276 657 C ATOM 1844 O GLY A 255 31.377 32.589 27.785 1.00 60.20 O ANISOU 1844 O GLY A 255 7666 7883 7321 732 286 701 O ATOM 1845 N MET A 256 31.616 33.445 25.732 1.00 57.78 N ANISOU 1845 N MET A 256 7359 7542 7051 699 295 651 N ATOM 1846 CA MET A 256 30.214 33.689 25.550 1.00 57.24 C ANISOU 1846 CA MET A 256 7305 7434 7009 718 329 697 C ATOM 1847 C MET A 256 29.409 32.409 25.391 1.00 52.81 C ANISOU 1847 C MET A 256 6711 6857 6496 745 304 755 C ATOM 1848 O MET A 256 28.299 32.324 25.859 1.00 51.93 O ANISOU 1848 O MET A 256 6605 6735 6391 764 327 804 O ATOM 1849 CB MET A 256 30.025 34.570 24.331 1.00 66.29 C ANISOU 1849 CB MET A 256 8465 8550 8172 701 352 673 C ATOM 1850 CG MET A 256 28.615 34.535 23.785 1.00 73.91 C ANISOU 1850 CG MET A 256 9426 9478 9175 725 375 723 C ATOM 1851 SD MET A 256 28.282 35.996 22.817 1.00 83.16 S ANISOU 1851 SD MET A 256 10637 10618 10342 714 421 697 S ATOM 1852 CE MET A 256 26.517 35.998 23.018 1.00 88.87 C ANISOU 1852 CE MET A 256 11360 11323 11082 758 458 767 C ATOM 1853 N VAL A 257 29.955 31.422 24.696 1.00 51.64 N ANISOU 1853 N VAL A 257 6531 6709 6380 746 259 749 N ATOM 1854 CA VAL A 257 29.309 30.111 24.603 1.00 48.25 C ANISOU 1854 CA VAL A 257 6078 6262 5991 766 230 802 C ATOM 1855 C VAL A 257 29.230 29.451 25.982 1.00 47.11 C ANISOU 1855 C VAL A 257 5939 6137 5823 784 221 837 C ATOM 1856 O VAL A 257 28.211 28.872 26.340 1.00 48.79 O ANISOU 1856 O VAL A 257 6150 6336 6053 795 225 894 O ATOM 1857 CB VAL A 257 30.033 29.214 23.594 1.00 46.92 C ANISOU 1857 CB VAL A 257 5884 6086 5855 766 182 782 C ATOM 1858 CG1 VAL A 257 29.476 27.789 23.580 1.00 45.48 C ANISOU 1858 CG1 VAL A 257 5690 5880 5709 784 149 833 C ATOM 1859 CG2 VAL A 257 29.914 29.849 22.218 1.00 49.32 C ANISOU 1859 CG2 VAL A 257 6183 6370 6186 749 195 756 C ATOM 1860 N LYS A 258 30.297 29.564 26.752 1.00 48.63 N ANISOU 1860 N LYS A 258 6137 6367 5972 783 209 804 N ATOM 1861 CA LYS A 258 30.306 29.075 28.127 1.00 51.41 C ANISOU 1861 CA LYS A 258 6495 6743 6292 800 203 833 C ATOM 1862 C LYS A 258 29.193 29.718 28.968 1.00 55.08 C ANISOU 1862 C LYS A 258 6982 7204 6739 803 250 869 C ATOM 1863 O LYS A 258 28.437 29.018 29.643 1.00 54.54 O ANISOU 1863 O LYS A 258 6912 7133 6676 818 249 924 O ATOM 1864 CB LYS A 258 31.665 29.330 28.746 1.00 52.02 C ANISOU 1864 CB LYS A 258 6573 6870 6319 795 187 784 C ATOM 1865 CG LYS A 258 31.839 28.706 30.141 1.00 56.84 C ANISOU 1865 CG LYS A 258 7187 7511 6895 816 174 811 C ATOM 1866 CD LYS A 258 33.313 28.655 30.526 1.00 56.94 C ANISOU 1866 CD LYS A 258 7187 7581 6864 816 144 764 C ATOM 1867 CE LYS A 258 33.501 28.219 31.965 1.00 62.88 C ANISOU 1867 CE LYS A 258 7945 8370 7574 836 136 788 C ATOM 1868 NZ LYS A 258 34.938 28.027 32.274 1.00 62.73 N ANISOU 1868 NZ LYS A 258 7906 8413 7512 841 102 746 N ATOM 1869 N GLY A 259 29.081 31.048 28.894 1.00 57.00 N ANISOU 1869 N GLY A 259 7249 7448 6959 789 293 838 N ATOM 1870 CA GLY A 259 27.958 31.769 29.504 1.00 56.43 C ANISOU 1870 CA GLY A 259 7200 7369 6868 799 343 870 C ATOM 1871 C GLY A 259 26.592 31.254 29.074 1.00 56.90 C ANISOU 1871 C GLY A 259 7242 7405 6971 814 352 931 C ATOM 1872 O GLY A 259 25.729 30.997 29.904 1.00 57.05 O ANISOU 1872 O GLY A 259 7260 7434 6980 829 368 981 O ATOM 1873 N ALA A 260 26.389 31.069 27.776 1.00 55.93 N ANISOU 1873 N ALA A 260 7101 7255 6895 806 340 929 N ATOM 1874 CA ALA A 260 25.082 30.626 27.283 1.00 54.26 C ANISOU 1874 CA ALA A 260 6868 7025 6720 814 349 986 C ATOM 1875 C ALA A 260 24.738 29.206 27.731 1.00 52.91 C ANISOU 1875 C ALA A 260 6677 6856 6568 816 314 1039 C ATOM 1876 O ALA A 260 23.600 28.893 28.094 1.00 52.26 O ANISOU 1876 O ALA A 260 6584 6780 6490 821 330 1097 O ATOM 1877 CB ALA A 260 25.053 30.712 25.762 1.00 55.27 C ANISOU 1877 CB ALA A 260 6982 7126 6890 802 340 967 C ATOM 1878 N HIS A 261 25.717 28.324 27.664 1.00 50.49 N ANISOU 1878 N HIS A 261 6365 6545 6270 812 267 1021 N ATOM 1879 CA HIS A 261 25.508 26.963 28.128 1.00 51.40 C ANISOU 1879 CA HIS A 261 6473 6655 6398 815 233 1069 C ATOM 1880 C HIS A 261 25.213 26.974 29.616 1.00 51.38 C ANISOU 1880 C HIS A 261 6483 6682 6355 827 251 1102 C ATOM 1881 O HIS A 261 24.305 26.274 30.066 1.00 52.89 O ANISOU 1881 O HIS A 261 6670 6873 6553 825 251 1162 O ATOM 1882 CB HIS A 261 26.742 26.148 27.848 1.00 52.84 C ANISOU 1882 CB HIS A 261 6655 6830 6589 819 182 1037 C ATOM 1883 CG HIS A 261 26.801 24.849 28.577 1.00 54.14 C ANISOU 1883 CG HIS A 261 6828 6991 6753 830 147 1078 C ATOM 1884 ND1 HIS A 261 27.489 24.696 29.768 1.00 54.68 N ANISOU 1884 ND1 HIS A 261 6908 7089 6778 847 138 1075 N ATOM 1885 CD2 HIS A 261 26.299 23.632 28.269 1.00 53.30 C ANISOU 1885 CD2 HIS A 261 6721 6850 6678 825 118 1123 C ATOM 1886 CE1 HIS A 261 27.404 23.437 30.157 1.00 53.54 C ANISOU 1886 CE1 HIS A 261 6772 6928 6640 857 105 1118 C ATOM 1887 NE2 HIS A 261 26.689 22.770 29.270 1.00 52.73 N ANISOU 1887 NE2 HIS A 261 6666 6784 6583 842 92 1147 N ATOM 1888 N ARG A 262 25.956 27.774 30.376 1.00 52.54 N ANISOU 1888 N ARG A 262 6648 6858 6456 834 267 1063 N ATOM 1889 CA ARG A 262 25.672 27.902 31.816 1.00 57.79 C ANISOU 1889 CA ARG A 262 7325 7553 7076 846 288 1090 C ATOM 1890 C ARG A 262 24.222 28.332 32.063 1.00 59.23 C ANISOU 1890 C ARG A 262 7505 7741 7256 851 333 1139 C ATOM 1891 O ARG A 262 23.521 27.757 32.890 1.00 55.96 O ANISOU 1891 O ARG A 262 7087 7343 6832 856 337 1194 O ATOM 1892 CB ARG A 262 26.607 28.896 32.496 1.00 60.11 C ANISOU 1892 CB ARG A 262 7641 7878 7318 848 304 1035 C ATOM 1893 CG ARG A 262 26.376 29.031 34.010 1.00 65.94 C ANISOU 1893 CG ARG A 262 8395 8650 8006 861 325 1060 C ATOM 1894 CD ARG A 262 26.914 30.351 34.555 1.00 68.79 C ANISOU 1894 CD ARG A 262 8786 9036 8315 857 358 1007 C ATOM 1895 NE ARG A 262 28.214 30.672 33.965 1.00 78.21 N ANISOU 1895 NE ARG A 262 9980 10232 9502 839 335 940 N ATOM 1896 CZ ARG A 262 28.515 31.749 33.225 1.00 83.96 C ANISOU 1896 CZ ARG A 262 10724 10948 10227 820 357 889 C ATOM 1897 NH1 ARG A 262 27.620 32.709 32.968 1.00 88.17 N ANISOU 1897 NH1 ARG A 262 11280 11459 10760 824 404 893 N ATOM 1898 NH2 ARG A 262 29.749 31.870 32.733 1.00 84.06 N ANISOU 1898 NH2 ARG A 262 10732 10973 10233 800 330 833 N ATOM 1899 N ASN A 263 23.783 29.339 31.331 1.00 57.73 N ANISOU 1899 N ASN A 263 7318 7543 7074 851 368 1119 N ATOM 1900 CA ASN A 263 22.416 29.827 31.451 1.00 61.09 C ANISOU 1900 CA ASN A 263 7738 7979 7494 863 413 1163 C ATOM 1901 C ASN A 263 21.376 28.769 31.095 1.00 58.23 C ANISOU 1901 C ASN A 263 7341 7612 7168 853 398 1229 C ATOM 1902 O ASN A 263 20.381 28.599 31.783 1.00 57.36 O ANISOU 1902 O ASN A 263 7220 7530 7043 859 420 1284 O ATOM 1903 CB ASN A 263 22.264 31.035 30.545 1.00 69.61 C ANISOU 1903 CB ASN A 263 8828 9043 8577 869 447 1126 C ATOM 1904 CG ASN A 263 21.153 31.937 30.969 1.00 79.03 C ANISOU 1904 CG ASN A 263 10030 10256 9741 896 503 1153 C ATOM 1905 OD1 ASN A 263 21.394 32.986 31.566 1.00 91.76 O ANISOU 1905 OD1 ASN A 263 11680 11875 11309 912 538 1121 O ATOM 1906 ND2 ASN A 263 19.924 31.532 30.683 1.00 78.19 N ANISOU 1906 ND2 ASN A 263 9891 10162 9655 902 513 1211 N ATOM 1907 N MET A 264 21.596 28.039 30.014 1.00 58.16 N ANISOU 1907 N MET A 264 7317 7573 7207 833 360 1225 N ATOM 1908 CA MET A 264 20.638 27.002 29.625 1.00 60.21 C ANISOU 1908 CA MET A 264 7550 7826 7500 814 343 1285 C ATOM 1909 C MET A 264 20.535 25.947 30.703 1.00 57.97 C ANISOU 1909 C MET A 264 7270 7553 7201 807 322 1332 C ATOM 1910 O MET A 264 19.446 25.503 31.054 1.00 58.96 O ANISOU 1910 O MET A 264 7378 7698 7325 796 333 1394 O ATOM 1911 CB MET A 264 21.017 26.336 28.288 1.00 58.47 C ANISOU 1911 CB MET A 264 7319 7565 7329 793 302 1266 C ATOM 1912 CG MET A 264 20.926 27.283 27.105 1.00 62.83 C ANISOU 1912 CG MET A 264 7863 8108 7900 796 323 1230 C ATOM 1913 SD MET A 264 19.223 27.608 26.598 1.00 62.83 S ANISOU 1913 SD MET A 264 7830 8132 7911 793 361 1285 S ATOM 1914 CE MET A 264 18.930 26.132 25.639 1.00 63.92 C ANISOU 1914 CE MET A 264 7945 8240 8099 753 310 1317 C ATOM 1915 N MET A 265 21.677 25.532 31.215 1.00 57.43 N ANISOU 1915 N MET A 265 7223 7475 7120 813 291 1304 N ATOM 1916 CA MET A 265 21.699 24.446 32.191 1.00 61.30 C ANISOU 1916 CA MET A 265 7724 7970 7597 810 266 1349 C ATOM 1917 C MET A 265 21.011 24.853 33.508 1.00 63.82 C ANISOU 1917 C MET A 265 8043 8334 7869 821 304 1387 C ATOM 1918 O MET A 265 20.236 24.087 34.071 1.00 62.32 O ANISOU 1918 O MET A 265 7847 8156 7675 807 302 1449 O ATOM 1919 CB MET A 265 23.120 23.970 32.444 1.00 55.68 C ANISOU 1919 CB MET A 265 7033 7245 6876 823 224 1309 C ATOM 1920 CG MET A 265 23.717 23.192 31.292 1.00 57.04 C ANISOU 1920 CG MET A 265 7206 7372 7091 815 179 1287 C ATOM 1921 SD MET A 265 22.928 21.594 30.986 1.00 63.01 S ANISOU 1921 SD MET A 265 7968 8087 7882 787 143 1355 S ATOM 1922 CE MET A 265 23.617 20.537 32.276 1.00 62.61 C ANISOU 1922 CE MET A 265 7951 8036 7799 806 109 1381 C ATOM 1923 N ARG A 266 21.280 26.070 33.953 1.00 67.35 N ANISOU 1923 N ARG A 266 8500 8807 8281 844 341 1348 N ATOM 1924 CA ARG A 266 20.696 26.593 35.167 1.00 72.17 C ANISOU 1924 CA ARG A 266 9115 9462 8844 860 381 1375 C ATOM 1925 C ARG A 266 19.179 26.596 35.035 1.00 73.38 C ANISOU 1925 C ARG A 266 9239 9637 9003 854 413 1435 C ATOM 1926 O ARG A 266 18.477 26.052 35.876 1.00 71.81 O ANISOU 1926 O ARG A 266 9030 9467 8785 849 419 1494 O ATOM 1927 CB ARG A 266 21.229 27.992 35.442 1.00 76.19 C ANISOU 1927 CB ARG A 266 9646 9985 9316 883 416 1315 C ATOM 1928 CG ARG A 266 20.820 28.552 36.791 1.00 90.03 C ANISOU 1928 CG ARG A 266 11412 11781 11012 904 456 1334 C ATOM 1929 CD ARG A 266 22.018 29.127 37.531 1.00 97.37 C ANISOU 1929 CD ARG A 266 12375 12722 11899 913 454 1276 C ATOM 1930 NE ARG A 266 22.613 30.263 36.827 1.00102.06 N ANISOU 1930 NE ARG A 266 12990 13297 12491 913 470 1208 N ATOM 1931 CZ ARG A 266 23.916 30.551 36.790 1.00106.37 C ANISOU 1931 CZ ARG A 266 13554 13838 13023 903 449 1146 C ATOM 1932 NH1 ARG A 266 24.814 29.772 37.398 1.00104.89 N ANISOU 1932 NH1 ARG A 266 13364 13665 12822 898 410 1142 N ATOM 1933 NH2 ARG A 266 24.331 31.628 36.120 1.00104.61 N ANISOU 1933 NH2 ARG A 266 13352 13597 12795 897 468 1088 N ATOM 1934 N ARG A 267 18.681 27.157 33.945 1.00 73.74 N ANISOU 1934 N ARG A 267 9268 9672 9075 854 430 1424 N ATOM 1935 CA ARG A 267 17.249 27.288 33.750 1.00 73.88 C ANISOU 1935 CA ARG A 267 9253 9723 9094 853 463 1478 C ATOM 1936 C ARG A 267 16.564 25.956 33.451 1.00 75.36 C ANISOU 1936 C ARG A 267 9414 9907 9313 812 431 1540 C ATOM 1937 O ARG A 267 15.558 25.624 34.065 1.00 72.31 O ANISOU 1937 O ARG A 267 9004 9562 8905 803 448 1602 O ATOM 1938 CB ARG A 267 16.967 28.268 32.632 1.00 76.94 C ANISOU 1938 CB ARG A 267 9632 10101 9498 868 489 1447 C ATOM 1939 CG ARG A 267 15.516 28.726 32.600 1.00 85.75 C ANISOU 1939 CG ARG A 267 10715 11265 10598 885 534 1496 C ATOM 1940 CD ARG A 267 15.295 29.775 31.526 1.00 90.04 C ANISOU 1940 CD ARG A 267 11257 11799 11153 908 562 1464 C ATOM 1941 NE ARG A 267 16.011 29.394 30.311 1.00 97.87 N ANISOU 1941 NE ARG A 267 12250 12740 12196 880 521 1428 N ATOM 1942 CZ ARG A 267 15.603 28.461 29.446 1.00 99.02 C ANISOU 1942 CZ ARG A 267 12363 12875 12383 844 489 1457 C ATOM 1943 NH1 ARG A 267 14.448 27.816 29.621 1.00101.29 N ANISOU 1943 NH1 ARG A 267 12611 13203 12669 825 493 1526 N ATOM 1944 NH2 ARG A 267 16.355 28.173 28.388 1.00 97.63 N ANISOU 1944 NH2 ARG A 267 12193 12651 12248 824 453 1418 N ATOM 1945 N LEU A 268 17.102 25.184 32.518 1.00 73.13 N ANISOU 1945 N LEU A 268 9134 9575 9074 785 385 1524 N ATOM 1946 CA LEU A 268 16.419 23.958 32.112 1.00 72.26 C ANISOU 1946 CA LEU A 268 9006 9455 8993 741 356 1579 C ATOM 1947 C LEU A 268 16.577 22.796 33.089 1.00 76.42 C ANISOU 1947 C LEU A 268 9553 9976 9506 720 326 1621 C ATOM 1948 O LEU A 268 15.731 21.911 33.128 1.00 72.96 O ANISOU 1948 O LEU A 268 9102 9545 9074 681 315 1682 O ATOM 1949 CB LEU A 268 16.896 23.506 30.736 1.00 73.72 C ANISOU 1949 CB LEU A 268 9193 9586 9229 720 317 1547 C ATOM 1950 CG LEU A 268 16.512 24.408 29.558 1.00 76.73 C ANISOU 1950 CG LEU A 268 9550 9972 9631 728 341 1521 C ATOM 1951 CD1 LEU A 268 17.352 24.046 28.342 1.00 80.37 C ANISOU 1951 CD1 LEU A 268 10022 10377 10136 715 300 1474 C ATOM 1952 CD2 LEU A 268 15.030 24.301 29.232 1.00 70.89 C ANISOU 1952 CD2 LEU A 268 8766 9274 8893 705 363 1581 C ATOM 1953 N LYS A 269 17.666 22.766 33.848 1.00 72.92 N ANISOU 1953 N LYS A 269 9143 9520 9043 744 311 1590 N ATOM 1954 CA LYS A 269 17.947 21.599 34.676 1.00 76.39 C ANISOU 1954 CA LYS A 269 9607 9944 9470 729 277 1626 C ATOM 1955 C LYS A 269 18.181 21.871 36.166 1.00 74.57 C ANISOU 1955 C LYS A 269 9391 9754 9188 755 296 1636 C ATOM 1956 O LYS A 269 18.389 20.927 36.925 1.00 77.86 O ANISOU 1956 O LYS A 269 9829 10161 9590 746 270 1670 O ATOM 1957 CB LYS A 269 19.160 20.870 34.105 1.00 77.08 C ANISOU 1957 CB LYS A 269 9726 9972 9586 732 224 1586 C ATOM 1958 CG LYS A 269 19.016 20.454 32.654 1.00 79.31 C ANISOU 1958 CG LYS A 269 10001 10210 9920 705 200 1576 C ATOM 1959 CD LYS A 269 17.966 19.376 32.460 1.00 80.25 C ANISOU 1959 CD LYS A 269 10117 10317 10055 654 185 1645 C ATOM 1960 CE LYS A 269 18.478 18.027 32.929 1.00 82.61 C ANISOU 1960 CE LYS A 269 10463 10571 10352 642 138 1670 C ATOM 1961 NZ LYS A 269 17.499 16.942 32.672 1.00 85.89 N ANISOU 1961 NZ LYS A 269 10884 10966 10783 583 121 1735 N ATOM 1962 N ARG A 270 18.142 23.139 36.580 1.00 76.46 N ANISOU 1962 N ARG A 270 9622 10033 9396 788 341 1607 N ATOM 1963 CA ARG A 270 18.492 23.525 37.948 1.00 80.08 C ANISOU 1963 CA ARG A 270 10097 10528 9802 815 359 1604 C ATOM 1964 C ARG A 270 19.867 22.996 38.343 1.00 77.70 C ANISOU 1964 C ARG A 270 9827 10200 9492 826 317 1571 C ATOM 1965 O ARG A 270 20.090 22.631 39.487 1.00 79.06 O ANISOU 1965 O ARG A 270 10015 10394 9629 835 312 1594 O ATOM 1966 CB ARG A 270 17.446 22.997 38.949 1.00 84.70 C ANISOU 1966 CB ARG A 270 10669 11156 10357 800 376 1682 C ATOM 1967 CG ARG A 270 15.987 23.231 38.576 1.00 90.32 C ANISOU 1967 CG ARG A 270 11340 11904 11072 783 411 1730 C ATOM 1968 CD ARG A 270 15.717 24.654 38.103 1.00 98.60 C ANISOU 1968 CD ARG A 270 12373 12974 12114 817 457 1688 C ATOM 1969 NE ARG A 270 16.497 25.668 38.824 1.00107.93 N ANISOU 1969 NE ARG A 270 13583 14166 13257 860 480 1634 N ATOM 1970 CZ ARG A 270 16.651 26.939 38.432 1.00117.77 C ANISOU 1970 CZ ARG A 270 14837 15413 14496 891 514 1582 C ATOM 1971 NH1 ARG A 270 17.401 27.764 39.163 1.00122.13 N ANISOU 1971 NH1 ARG A 270 15422 15972 15007 920 531 1534 N ATOM 1972 NH2 ARG A 270 16.063 27.401 37.323 1.00116.24 N ANISOU 1972 NH2 ARG A 270 14622 15212 14330 892 530 1576 N ATOM 1973 N ALA A 271 20.796 22.940 37.402 1.00 73.33 N ANISOU 1973 N ALA A 271 9283 9605 8971 829 286 1518 N ATOM 1974 CA ALA A 271 22.085 22.333 37.688 1.00 73.02 C ANISOU 1974 CA ALA A 271 9269 9548 8925 843 243 1490 C ATOM 1975 C ALA A 271 22.955 23.275 38.507 1.00 73.48 C ANISOU 1975 C ALA A 271 9337 9643 8936 872 260 1439 C ATOM 1976 O ALA A 271 22.806 24.497 38.428 1.00 70.86 O ANISOU 1976 O ALA A 271 9000 9333 8590 879 300 1405 O ATOM 1977 CB ALA A 271 22.783 21.964 36.401 1.00 76.43 C ANISOU 1977 CB ALA A 271 9704 9931 9403 839 205 1450 C ATOM 1978 N LYS A 272 23.857 22.689 39.288 1.00 73.03 N ANISOU 1978 N LYS A 272 9299 9595 8853 888 229 1436 N ATOM 1979 CA LYS A 272 24.747 23.443 40.156 1.00 77.04 C ANISOU 1979 CA LYS A 272 9815 10144 9309 910 240 1391 C ATOM 1980 C LYS A 272 26.052 23.774 39.450 1.00 72.97 C ANISOU 1980 C LYS A 272 9301 9622 8801 918 215 1317 C ATOM 1981 O LYS A 272 26.425 23.097 38.508 1.00 67.49 O ANISOU 1981 O LYS A 272 8604 8890 8146 916 179 1309 O ATOM 1982 CB LYS A 272 25.033 22.626 41.417 1.00 83.08 C ANISOU 1982 CB LYS A 272 10596 10932 10036 924 219 1430 C ATOM 1983 CG LYS A 272 23.768 22.198 42.156 1.00 91.16 C ANISOU 1983 CG LYS A 272 11619 11968 11049 911 241 1508 C ATOM 1984 CD LYS A 272 22.811 23.376 42.350 1.00 98.17 C ANISOU 1984 CD LYS A 272 12491 12889 11919 907 300 1508 C ATOM 1985 CE LYS A 272 21.577 23.006 43.156 1.00105.02 C ANISOU 1985 CE LYS A 272 13350 13783 12768 897 324 1585 C ATOM 1986 NZ LYS A 272 20.561 24.093 43.056 1.00107.21 N ANISOU 1986 NZ LYS A 272 13609 14090 13037 899 381 1586 N ATOM 1987 N PRO A 273 26.772 24.789 39.939 1.00 70.78 N ANISOU 1987 N PRO A 273 9029 9384 8481 926 233 1264 N ATOM 1988 CA PRO A 273 27.929 25.261 39.196 1.00 70.27 C ANISOU 1988 CA PRO A 273 8959 9319 8419 925 216 1192 C ATOM 1989 C PRO A 273 28.950 24.176 38.832 1.00 69.21 C ANISOU 1989 C PRO A 273 8820 9174 8299 941 158 1183 C ATOM 1990 O PRO A 273 29.423 24.151 37.697 1.00 64.39 O ANISOU 1990 O PRO A 273 8200 8540 7723 936 139 1147 O ATOM 1991 CB PRO A 273 28.531 26.321 40.130 1.00 69.31 C ANISOU 1991 CB PRO A 273 8849 9250 8235 926 240 1147 C ATOM 1992 CG PRO A 273 27.347 26.855 40.872 1.00 69.84 C ANISOU 1992 CG PRO A 273 8926 9326 8282 926 289 1185 C ATOM 1993 CD PRO A 273 26.510 25.627 41.127 1.00 70.83 C ANISOU 1993 CD PRO A 273 9044 9435 8430 931 273 1264 C ATOM 1994 N ALA A 274 29.275 23.279 39.751 1.00 62.45 N ANISOU 1994 N ALA A 274 7973 8336 7418 962 131 1216 N ATOM 1995 CA ALA A 274 30.301 22.274 39.449 1.00 65.97 C ANISOU 1995 CA ALA A 274 8419 8774 7870 988 77 1206 C ATOM 1996 C ALA A 274 29.807 21.301 38.381 1.00 62.80 C ANISOU 1996 C ALA A 274 8024 8306 7529 985 52 1237 C ATOM 1997 O ALA A 274 30.556 20.950 37.477 1.00 58.30 O ANISOU 1997 O ALA A 274 7449 7720 6982 997 20 1204 O ATOM 1998 CB ALA A 274 30.734 21.516 40.700 1.00 64.16 C ANISOU 1998 CB ALA A 274 8204 8578 7596 1018 54 1239 C ATOM 1999 N GLU A 275 28.551 20.883 38.480 1.00 61.07 N ANISOU 1999 N GLU A 275 7815 8054 7333 966 68 1300 N ATOM 2000 CA GLU A 275 27.963 20.001 37.475 1.00 65.85 C ANISOU 2000 CA GLU A 275 8428 8596 7993 952 47 1331 C ATOM 2001 C GLU A 275 27.965 20.695 36.085 1.00 60.59 C ANISOU 2001 C GLU A 275 7741 7911 7368 935 57 1282 C ATOM 2002 O GLU A 275 28.287 20.086 35.065 1.00 53.46 O ANISOU 2002 O GLU A 275 6841 6968 6501 938 25 1269 O ATOM 2003 CB GLU A 275 26.527 19.667 37.839 1.00 71.66 C ANISOU 2003 CB GLU A 275 9171 9315 8741 924 70 1403 C ATOM 2004 CG GLU A 275 26.389 18.933 39.160 1.00 87.79 C ANISOU 2004 CG GLU A 275 11236 11373 10745 935 62 1459 C ATOM 2005 CD GLU A 275 24.996 19.050 39.781 1.00 97.99 C ANISOU 2005 CD GLU A 275 12522 12677 12029 904 100 1522 C ATOM 2006 OE1 GLU A 275 24.137 19.863 39.315 1.00 91.74 O ANISOU 2006 OE1 GLU A 275 11706 11895 11254 881 139 1519 O ATOM 2007 OE2 GLU A 275 24.778 18.311 40.767 1.00107.17 O ANISOU 2007 OE2 GLU A 275 13706 13846 13165 907 92 1576 O ATOM 2008 N ILE A 276 27.599 21.971 36.077 1.00 55.25 N ANISOU 2008 N ILE A 276 7048 7261 6682 919 102 1257 N ATOM 2009 CA ILE A 276 27.540 22.738 34.874 1.00 57.01 C ANISOU 2009 CA ILE A 276 7255 7468 6937 903 117 1214 C ATOM 2010 C ILE A 276 28.926 22.783 34.219 1.00 55.70 C ANISOU 2010 C ILE A 276 7082 7308 6770 918 85 1149 C ATOM 2011 O ILE A 276 29.035 22.611 33.012 1.00 54.10 O ANISOU 2011 O ILE A 276 6871 7074 6608 911 69 1128 O ATOM 2012 CB ILE A 276 26.999 24.166 35.141 1.00 57.32 C ANISOU 2012 CB ILE A 276 7287 7536 6954 890 173 1196 C ATOM 2013 CG1 ILE A 276 25.484 24.101 35.423 1.00 60.24 C ANISOU 2013 CG1 ILE A 276 7653 7899 7333 876 205 1262 C ATOM 2014 CG2 ILE A 276 27.313 25.082 33.958 1.00 58.11 C ANISOU 2014 CG2 ILE A 276 7376 7625 7075 878 185 1138 C ATOM 2015 CD1 ILE A 276 24.803 25.436 35.750 1.00 60.50 C ANISOU 2015 CD1 ILE A 276 7685 7961 7341 875 262 1253 C ATOM 2016 N GLU A 277 29.967 23.028 35.004 1.00 54.93 N ANISOU 2016 N GLU A 277 6986 7259 6626 936 76 1116 N ATOM 2017 CA GLU A 277 31.308 23.133 34.451 1.00 55.37 C ANISOU 2017 CA GLU A 277 7028 7337 6673 949 48 1054 C ATOM 2018 C GLU A 277 31.822 21.805 33.892 1.00 56.97 C ANISOU 2018 C GLU A 277 7234 7509 6900 978 -3 1065 C ATOM 2019 O GLU A 277 32.515 21.789 32.867 1.00 53.32 O ANISOU 2019 O GLU A 277 6758 7043 6456 983 -24 1021 O ATOM 2020 CB GLU A 277 32.276 23.715 35.481 1.00 56.76 C ANISOU 2020 CB GLU A 277 7199 7581 6784 958 51 1019 C ATOM 2021 CG GLU A 277 33.756 23.686 35.083 1.00 60.79 C ANISOU 2021 CG GLU A 277 7690 8133 7275 973 17 959 C ATOM 2022 CD GLU A 277 34.108 24.368 33.750 1.00 63.56 C ANISOU 2022 CD GLU A 277 8022 8474 7651 950 22 904 C ATOM 2023 OE1 GLU A 277 33.289 25.163 33.206 1.00 65.15 O ANISOU 2023 OE1 GLU A 277 8230 8645 7879 918 58 902 O ATOM 2024 OE2 GLU A 277 35.227 24.105 33.247 1.00 59.26 O ANISOU 2024 OE2 GLU A 277 7458 7958 7098 966 -11 864 O ATOM 2025 N ALA A 278 31.500 20.695 34.548 1.00 55.99 N ANISOU 2025 N ALA A 278 7133 7365 6774 998 -24 1122 N ATOM 2026 CA ALA A 278 31.863 19.360 34.023 1.00 53.13 C ANISOU 2026 CA ALA A 278 6789 6961 6435 1028 -73 1138 C ATOM 2027 C ALA A 278 31.129 19.071 32.698 1.00 53.34 C ANISOU 2027 C ALA A 278 6819 6923 6523 1003 -75 1146 C ATOM 2028 O ALA A 278 31.686 18.485 31.784 1.00 54.51 O ANISOU 2028 O ALA A 278 6970 7045 6693 1022 -108 1124 O ATOM 2029 CB ALA A 278 31.523 18.275 35.049 1.00 53.70 C ANISOU 2029 CB ALA A 278 6895 7016 6491 1048 -90 1204 C ATOM 2030 N ASP A 279 29.867 19.482 32.609 1.00 52.86 N ANISOU 2030 N ASP A 279 6756 6842 6485 963 -39 1179 N ATOM 2031 CA ASP A 279 29.072 19.273 31.409 1.00 54.61 C ANISOU 2031 CA ASP A 279 6976 7010 6760 935 -39 1190 C ATOM 2032 C ASP A 279 29.617 20.128 30.258 1.00 51.06 C ANISOU 2032 C ASP A 279 6499 6571 6328 929 -32 1124 C ATOM 2033 O ASP A 279 29.682 19.670 29.132 1.00 54.07 O ANISOU 2033 O ASP A 279 6881 6914 6746 927 -55 1111 O ATOM 2034 CB ASP A 279 27.608 19.637 31.685 1.00 56.14 C ANISOU 2034 CB ASP A 279 7166 7199 6965 896 1 1240 C ATOM 2035 CG ASP A 279 26.690 19.284 30.531 1.00 59.29 C ANISOU 2035 CG ASP A 279 7562 7549 7415 864 0 1261 C ATOM 2036 OD1 ASP A 279 26.475 18.080 30.277 1.00 62.80 O ANISOU 2036 OD1 ASP A 279 8033 7946 7879 859 -33 1296 O ATOM 2037 OD2 ASP A 279 26.193 20.210 29.854 1.00 59.88 O ANISOU 2037 OD2 ASP A 279 7611 7632 7507 843 30 1243 O ATOM 2038 N PHE A 280 30.016 21.362 30.566 1.00 49.79 N ANISOU 2038 N PHE A 280 6319 6460 6138 924 -2 1082 N ATOM 2039 CA PHE A 280 30.671 22.245 29.601 1.00 49.53 C ANISOU 2039 CA PHE A 280 6263 6443 6111 916 3 1017 C ATOM 2040 C PHE A 280 31.911 21.576 29.014 1.00 49.42 C ANISOU 2040 C PHE A 280 6245 6434 6098 947 -42 978 C ATOM 2041 O PHE A 280 32.108 21.559 27.801 1.00 48.49 O ANISOU 2041 O PHE A 280 6115 6295 6011 942 -54 949 O ATOM 2042 CB PHE A 280 31.060 23.586 30.247 1.00 49.58 C ANISOU 2042 CB PHE A 280 6260 6503 6073 905 39 978 C ATOM 2043 CG PHE A 280 31.845 24.484 29.332 1.00 50.92 C ANISOU 2043 CG PHE A 280 6411 6692 6242 892 44 911 C ATOM 2044 CD1 PHE A 280 31.211 25.197 28.332 1.00 51.68 C ANISOU 2044 CD1 PHE A 280 6503 6761 6371 865 71 900 C ATOM 2045 CD2 PHE A 280 33.218 24.581 29.447 1.00 52.06 C ANISOU 2045 CD2 PHE A 280 6543 6886 6351 905 21 860 C ATOM 2046 CE1 PHE A 280 31.939 26.018 27.486 1.00 53.73 C ANISOU 2046 CE1 PHE A 280 6749 7036 6627 849 76 839 C ATOM 2047 CE2 PHE A 280 33.959 25.390 28.600 1.00 52.00 C ANISOU 2047 CE2 PHE A 280 6517 6900 6339 886 25 799 C ATOM 2048 CZ PHE A 280 33.318 26.103 27.614 1.00 52.13 C ANISOU 2048 CZ PHE A 280 6534 6883 6389 857 53 789 C ATOM 2049 N GLN A 281 32.752 21.026 29.874 1.00 48.21 N ANISOU 2049 N GLN A 281 6098 6313 5907 982 -68 978 N ATOM 2050 CA GLN A 281 33.982 20.427 29.403 1.00 50.94 C ANISOU 2050 CA GLN A 281 6435 6675 6244 1020 -111 941 C ATOM 2051 C GLN A 281 33.730 19.206 28.538 1.00 50.72 C ANISOU 2051 C GLN A 281 6429 6581 6259 1039 -145 965 C ATOM 2052 O GLN A 281 34.381 19.023 27.491 1.00 50.17 O ANISOU 2052 O GLN A 281 6347 6508 6204 1054 -168 926 O ATOM 2053 CB GLN A 281 34.911 20.081 30.552 1.00 49.75 C ANISOU 2053 CB GLN A 281 6285 6578 6037 1060 -132 940 C ATOM 2054 CG GLN A 281 36.318 19.862 30.055 1.00 52.63 C ANISOU 2054 CG GLN A 281 6626 6988 6380 1098 -167 888 C ATOM 2055 CD GLN A 281 37.299 19.555 31.153 1.00 53.02 C ANISOU 2055 CD GLN A 281 6670 7104 6371 1141 -188 884 C ATOM 2056 OE1 GLN A 281 38.015 20.427 31.621 1.00 56.73 O ANISOU 2056 OE1 GLN A 281 7111 7649 6795 1129 -176 845 O ATOM 2057 NE2 GLN A 281 37.335 18.316 31.569 1.00 56.75 N ANISOU 2057 NE2 GLN A 281 7173 7549 6840 1190 -220 927 N ATOM 2058 N ARG A 282 32.756 18.405 28.943 1.00 48.57 N ANISOU 2058 N ARG A 282 6190 6257 6004 1033 -148 1028 N ATOM 2059 CA ARG A 282 32.434 17.184 28.222 1.00 51.13 C ANISOU 2059 CA ARG A 282 6547 6512 6365 1043 -180 1056 C ATOM 2060 C ARG A 282 31.723 17.442 26.872 1.00 53.33 C ANISOU 2060 C ARG A 282 6816 6750 6696 1004 -169 1046 C ATOM 2061 O ARG A 282 32.098 16.856 25.854 1.00 50.58 O ANISOU 2061 O ARG A 282 6476 6370 6371 1020 -198 1024 O ATOM 2062 CB ARG A 282 31.582 16.261 29.107 1.00 56.47 C ANISOU 2062 CB ARG A 282 7267 7148 7041 1039 -185 1130 C ATOM 2063 CG ARG A 282 31.255 14.914 28.459 1.00 63.54 C ANISOU 2063 CG ARG A 282 8209 7963 7967 1045 -221 1161 C ATOM 2064 CD ARG A 282 30.484 13.965 29.384 1.00 73.54 C ANISOU 2064 CD ARG A 282 9524 9189 9226 1036 -228 1235 C ATOM 2065 NE ARG A 282 29.274 14.569 29.988 1.00 81.08 N ANISOU 2065 NE ARG A 282 10464 10158 10184 982 -186 1278 N ATOM 2066 CZ ARG A 282 28.021 14.530 29.493 1.00 79.81 C ANISOU 2066 CZ ARG A 282 10303 9963 10058 925 -168 1313 C ATOM 2067 NH1 ARG A 282 27.035 15.128 30.169 1.00 80.02 N ANISOU 2067 NH1 ARG A 282 10309 10018 10075 888 -129 1350 N ATOM 2068 NH2 ARG A 282 27.731 13.922 28.339 1.00 76.55 N ANISOU 2068 NH2 ARG A 282 9908 9493 9684 907 -189 1312 N ATOM 2069 N ARG A 283 30.704 18.307 26.855 1.00 49.98 N ANISOU 2069 N ARG A 283 6375 6328 6287 957 -127 1061 N ATOM 2070 CA ARG A 283 29.820 18.392 25.697 1.00 48.73 C ANISOU 2070 CA ARG A 283 6210 6129 6175 919 -117 1067 C ATOM 2071 C ARG A 283 30.095 19.576 24.761 1.00 47.92 C ANISOU 2071 C ARG A 283 6070 6053 6083 904 -94 1011 C ATOM 2072 O ARG A 283 29.673 19.561 23.611 1.00 48.83 O ANISOU 2072 O ARG A 283 6178 6138 6236 884 -96 1004 O ATOM 2073 CB ARG A 283 28.368 18.449 26.182 1.00 48.59 C ANISOU 2073 CB ARG A 283 6197 6095 6168 879 -87 1130 C ATOM 2074 CG ARG A 283 27.948 17.170 26.917 1.00 50.87 C ANISOU 2074 CG ARG A 283 6528 6348 6452 881 -111 1191 C ATOM 2075 CD ARG A 283 26.447 16.963 26.863 1.00 49.98 C ANISOU 2075 CD ARG A 283 6418 6209 6362 830 -92 1252 C ATOM 2076 NE ARG A 283 25.748 18.031 27.572 1.00 51.70 N ANISOU 2076 NE ARG A 283 6606 6475 6560 812 -43 1268 N ATOM 2077 CZ ARG A 283 24.514 18.446 27.291 1.00 52.05 C ANISOU 2077 CZ ARG A 283 6630 6524 6622 773 -11 1299 C ATOM 2078 NH1 ARG A 283 23.996 19.436 27.990 1.00 53.62 N ANISOU 2078 NH1 ARG A 283 6805 6770 6797 769 32 1310 N ATOM 2079 NH2 ARG A 283 23.807 17.912 26.296 1.00 52.55 N ANISOU 2079 NH2 ARG A 283 6693 6550 6722 739 -23 1319 N ATOM 2080 N VAL A 284 30.764 20.609 25.267 1.00 48.52 N ANISOU 2080 N VAL A 284 6125 6186 6124 910 -73 973 N ATOM 2081 CA VAL A 284 30.878 21.880 24.568 1.00 47.50 C ANISOU 2081 CA VAL A 284 5969 6080 5998 887 -43 927 C ATOM 2082 C VAL A 284 32.316 22.210 24.175 1.00 49.35 C ANISOU 2082 C VAL A 284 6184 6357 6209 906 -61 860 C ATOM 2083 O VAL A 284 32.595 22.673 23.068 1.00 47.99 O ANISOU 2083 O VAL A 284 5993 6184 6053 893 -59 820 O ATOM 2084 CB VAL A 284 30.289 23.012 25.422 1.00 48.52 C ANISOU 2084 CB VAL A 284 6094 6237 6101 866 5 938 C ATOM 2085 CG1 VAL A 284 30.388 24.348 24.679 1.00 49.44 C ANISOU 2085 CG1 VAL A 284 6195 6371 6219 843 38 892 C ATOM 2086 CG2 VAL A 284 28.833 22.694 25.761 1.00 49.99 C ANISOU 2086 CG2 VAL A 284 6292 6394 6307 848 24 1006 C ATOM 2087 N MET A 285 33.241 21.933 25.075 1.00 49.56 N ANISOU 2087 N MET A 285 6211 6423 6193 936 -80 850 N ATOM 2088 CA MET A 285 34.630 22.239 24.841 1.00 50.14 C ANISOU 2088 CA MET A 285 6261 6552 6236 953 -97 789 C ATOM 2089 C MET A 285 35.211 21.595 23.584 1.00 49.36 C ANISOU 2089 C MET A 285 6152 6438 6163 974 -132 761 C ATOM 2090 O MET A 285 36.068 22.188 22.911 1.00 50.08 O ANISOU 2090 O MET A 285 6215 6571 6242 968 -133 706 O ATOM 2091 CB MET A 285 35.432 21.857 26.078 1.00 51.06 C ANISOU 2091 CB MET A 285 6381 6717 6302 988 -115 792 C ATOM 2092 CG MET A 285 36.796 22.448 26.127 1.00 57.01 C ANISOU 2092 CG MET A 285 7102 7549 7009 994 -123 732 C ATOM 2093 SD MET A 285 36.813 24.232 26.381 1.00 57.61 S ANISOU 2093 SD MET A 285 7164 7668 7054 935 -72 693 S ATOM 2094 CE MET A 285 38.279 24.478 25.408 1.00 55.56 C ANISOU 2094 CE MET A 285 6864 7471 6774 937 -97 621 C ATOM 2095 N PRO A 286 34.762 20.394 23.234 1.00 46.92 N ANISOU 2095 N PRO A 286 5868 6071 5886 996 -160 796 N ATOM 2096 CA PRO A 286 35.341 19.857 21.987 1.00 50.33 C ANISOU 2096 CA PRO A 286 6293 6489 6339 1017 -191 763 C ATOM 2097 C PRO A 286 35.064 20.717 20.721 1.00 49.02 C ANISOU 2097 C PRO A 286 6104 6317 6205 977 -169 730 C ATOM 2098 O PRO A 286 35.951 20.865 19.859 1.00 46.19 O ANISOU 2098 O PRO A 286 5720 5988 5841 988 -184 681 O ATOM 2099 CB PRO A 286 34.706 18.461 21.888 1.00 52.02 C ANISOU 2099 CB PRO A 286 6550 6629 6583 1038 -220 812 C ATOM 2100 CG PRO A 286 34.479 18.073 23.343 1.00 49.45 C ANISOU 2100 CG PRO A 286 6250 6307 6230 1052 -219 858 C ATOM 2101 CD PRO A 286 34.021 19.371 23.987 1.00 48.81 C ANISOU 2101 CD PRO A 286 6146 6263 6134 1009 -172 859 C ATOM 2102 N GLY A 287 33.871 21.299 20.644 1.00 47.49 N ANISOU 2102 N GLY A 287 5914 6091 6036 933 -134 759 N ATOM 2103 CA GLY A 287 33.514 22.209 19.562 1.00 48.75 C ANISOU 2103 CA GLY A 287 6055 6245 6221 896 -108 735 C ATOM 2104 C GLY A 287 34.324 23.502 19.490 1.00 48.75 C ANISOU 2104 C GLY A 287 6029 6305 6188 877 -85 680 C ATOM 2105 O GLY A 287 34.425 24.116 18.426 1.00 50.33 O ANISOU 2105 O GLY A 287 6213 6507 6403 856 -75 648 O ATOM 2106 N LEU A 288 34.931 23.906 20.597 1.00 46.01 N ANISOU 2106 N LEU A 288 5680 6007 5794 883 -77 670 N ATOM 2107 CA LEU A 288 35.626 25.199 20.665 1.00 46.84 C ANISOU 2107 CA LEU A 288 5768 6167 5862 854 -52 621 C ATOM 2108 C LEU A 288 37.096 25.124 20.252 1.00 49.46 C ANISOU 2108 C LEU A 288 6068 6559 6163 869 -81 565 C ATOM 2109 O LEU A 288 37.691 26.130 19.943 1.00 58.38 O ANISOU 2109 O LEU A 288 7181 7731 7268 836 -64 520 O ATOM 2110 CB LEU A 288 35.527 25.787 22.068 1.00 45.69 C ANISOU 2110 CB LEU A 288 5635 6048 5675 844 -26 634 C ATOM 2111 CG LEU A 288 34.113 26.049 22.574 1.00 48.33 C ANISOU 2111 CG LEU A 288 5996 6337 6029 829 8 686 C ATOM 2112 CD1 LEU A 288 34.105 26.559 24.011 1.00 49.38 C ANISOU 2112 CD1 LEU A 288 6143 6501 6116 826 31 697 C ATOM 2113 CD2 LEU A 288 33.402 27.032 21.659 1.00 50.19 C ANISOU 2113 CD2 LEU A 288 6233 6545 6289 795 44 678 C ATOM 2114 N VAL A 289 37.664 23.931 20.189 1.00 48.99 N ANISOU 2114 N VAL A 289 6004 6506 6105 918 -124 568 N ATOM 2115 CA VAL A 289 39.069 23.787 19.873 1.00 48.30 C ANISOU 2115 CA VAL A 289 5881 6486 5981 942 -153 518 C ATOM 2116 C VAL A 289 39.450 24.538 18.587 1.00 49.10 C ANISOU 2116 C VAL A 289 5956 6606 6091 909 -143 470 C ATOM 2117 O VAL A 289 40.312 25.410 18.632 1.00 51.06 O ANISOU 2117 O VAL A 289 6178 6923 6297 881 -133 426 O ATOM 2118 CB VAL A 289 39.473 22.308 19.782 1.00 50.24 C ANISOU 2118 CB VAL A 289 6133 6721 6233 1010 -201 532 C ATOM 2119 CG1 VAL A 289 40.955 22.160 19.483 1.00 51.30 C ANISOU 2119 CG1 VAL A 289 6227 6939 6325 1044 -230 481 C ATOM 2120 CG2 VAL A 289 39.149 21.581 21.075 1.00 51.33 C ANISOU 2120 CG2 VAL A 289 6301 6842 6358 1041 -210 581 C ATOM 2121 N TYR A 290 38.832 24.220 17.446 1.00 49.56 N ANISOU 2121 N TYR A 290 6021 6607 6199 907 -147 478 N ATOM 2122 CA TYR A 290 39.194 24.917 16.204 1.00 47.84 C ANISOU 2122 CA TYR A 290 5779 6409 5989 877 -138 434 C ATOM 2123 C TYR A 290 38.743 26.380 16.198 1.00 50.02 C ANISOU 2123 C TYR A 290 6062 6683 6259 813 -90 424 C ATOM 2124 O TYR A 290 39.443 27.234 15.648 1.00 46.78 O ANISOU 2124 O TYR A 290 5630 6318 5825 780 -79 379 O ATOM 2125 CB TYR A 290 38.664 24.201 14.957 1.00 50.98 C ANISOU 2125 CB TYR A 290 6182 6748 6439 892 -155 443 C ATOM 2126 CG TYR A 290 39.171 22.780 14.748 1.00 49.32 C ANISOU 2126 CG TYR A 290 5973 6533 6233 956 -203 445 C ATOM 2127 CD1 TYR A 290 40.393 22.360 15.236 1.00 49.54 C ANISOU 2127 CD1 TYR A 290 5980 6629 6214 1000 -231 420 C ATOM 2128 CD2 TYR A 290 38.414 21.869 14.038 1.00 51.66 C ANISOU 2128 CD2 TYR A 290 6295 6756 6577 972 -221 472 C ATOM 2129 CE1 TYR A 290 40.830 21.051 15.063 1.00 52.99 C ANISOU 2129 CE1 TYR A 290 6425 7056 6652 1068 -274 424 C ATOM 2130 CE2 TYR A 290 38.850 20.567 13.833 1.00 55.83 C ANISOU 2130 CE2 TYR A 290 6836 7269 7107 1032 -263 473 C ATOM 2131 CZ TYR A 290 40.065 20.160 14.343 1.00 54.80 C ANISOU 2131 CZ TYR A 290 6688 7202 6929 1084 -290 449 C ATOM 2132 OH TYR A 290 40.486 18.858 14.126 1.00 57.73 O ANISOU 2132 OH TYR A 290 7080 7554 7299 1153 -331 451 O ATOM 2133 N CYS A 291 37.617 26.683 16.843 1.00 49.00 N ANISOU 2133 N CYS A 291 5965 6506 6146 798 -61 467 N ATOM 2134 CA CYS A 291 37.139 28.066 16.910 1.00 50.18 C ANISOU 2134 CA CYS A 291 6130 6649 6286 747 -13 461 C ATOM 2135 C CYS A 291 38.167 29.004 17.530 1.00 51.96 C ANISOU 2135 C CYS A 291 6348 6943 6450 717 0 417 C ATOM 2136 O CYS A 291 38.349 30.103 17.039 1.00 51.72 O ANISOU 2136 O CYS A 291 6322 6924 6406 672 25 385 O ATOM 2137 CB CYS A 291 35.790 28.148 17.637 1.00 52.66 C ANISOU 2137 CB CYS A 291 6478 6910 6621 746 14 516 C ATOM 2138 SG CYS A 291 34.458 27.357 16.674 1.00 54.27 S ANISOU 2138 SG CYS A 291 6687 7037 6893 759 8 563 S ATOM 2139 N GLN A 292 38.906 28.529 18.525 1.00 49.73 N ANISOU 2139 N GLN A 292 6054 6710 6130 741 -22 413 N ATOM 2140 CA GLN A 292 39.950 29.311 19.177 1.00 52.50 C ANISOU 2140 CA GLN A 292 6393 7137 6416 710 -15 372 C ATOM 2141 C GLN A 292 41.180 29.571 18.346 1.00 53.12 C ANISOU 2141 C GLN A 292 6431 7283 6466 691 -32 315 C ATOM 2142 O GLN A 292 42.085 30.320 18.768 1.00 49.42 O ANISOU 2142 O GLN A 292 5950 6886 5941 652 -25 276 O ATOM 2143 CB GLN A 292 40.479 28.540 20.369 1.00 57.24 C ANISOU 2143 CB GLN A 292 6983 7782 6983 750 -42 384 C ATOM 2144 CG GLN A 292 39.484 28.382 21.479 1.00 65.72 C ANISOU 2144 CG GLN A 292 8093 8811 8065 762 -25 435 C ATOM 2145 CD GLN A 292 40.110 27.726 22.681 1.00 70.69 C ANISOU 2145 CD GLN A 292 8713 9492 8654 798 -50 444 C ATOM 2146 OE1 GLN A 292 40.759 26.677 22.580 1.00 77.84 O ANISOU 2146 OE1 GLN A 292 9595 10424 9556 847 -91 444 O ATOM 2147 NE2 GLN A 292 39.937 28.349 23.822 1.00 75.71 N ANISOU 2147 NE2 GLN A 292 9369 10142 9253 776 -25 452 N ATOM 2148 N GLN A 293 41.279 28.882 17.218 1.00 51.17 N ANISOU 2148 N GLN A 293 6163 7024 6255 718 -57 310 N ATOM 2149 CA GLN A 293 42.416 29.048 16.332 1.00 50.13 C ANISOU 2149 CA GLN A 293 5988 6959 6098 704 -74 259 C ATOM 2150 C GLN A 293 42.126 29.894 15.107 1.00 48.70 C ANISOU 2150 C GLN A 293 5812 6750 5939 657 -49 239 C ATOM 2151 O GLN A 293 43.046 30.271 14.392 1.00 45.42 O ANISOU 2151 O GLN A 293 5365 6395 5498 630 -56 195 O ATOM 2152 CB GLN A 293 42.913 27.671 15.889 1.00 54.83 C ANISOU 2152 CB GLN A 293 6553 7572 6707 774 -122 260 C ATOM 2153 CG GLN A 293 43.451 26.822 17.046 1.00 54.83 C ANISOU 2153 CG GLN A 293 6543 7615 6673 828 -151 274 C ATOM 2154 CD GLN A 293 43.883 25.466 16.551 1.00 57.62 C ANISOU 2154 CD GLN A 293 6877 7974 7040 903 -196 277 C ATOM 2155 OE1 GLN A 293 44.893 25.356 15.869 1.00 63.21 O ANISOU 2155 OE1 GLN A 293 7542 8750 7722 917 -216 236 O ATOM 2156 NE2 GLN A 293 43.113 24.430 16.862 1.00 56.57 N ANISOU 2156 NE2 GLN A 293 6779 7768 6944 952 -211 324 N ATOM 2157 N VAL A 294 40.850 30.158 14.845 1.00 48.06 N ANISOU 2157 N VAL A 294 5770 6583 5906 648 -22 274 N ATOM 2158 CA VAL A 294 40.446 31.014 13.746 1.00 48.00 C ANISOU 2158 CA VAL A 294 5774 6543 5920 606 4 261 C ATOM 2159 C VAL A 294 39.732 32.309 14.140 1.00 45.63 C ANISOU 2159 C VAL A 294 5522 6204 5609 557 55 270 C ATOM 2160 O VAL A 294 39.756 33.268 13.370 1.00 46.53 O ANISOU 2160 O VAL A 294 5648 6312 5719 513 80 247 O ATOM 2161 CB VAL A 294 39.595 30.218 12.707 1.00 48.94 C ANISOU 2161 CB VAL A 294 5891 6597 6103 640 -8 290 C ATOM 2162 CG1 VAL A 294 40.315 28.929 12.339 1.00 50.67 C ANISOU 2162 CG1 VAL A 294 6074 6848 6328 692 -58 279 C ATOM 2163 CG2 VAL A 294 38.233 29.860 13.229 1.00 50.35 C ANISOU 2163 CG2 VAL A 294 6105 6703 6322 661 4 347 C ATOM 2164 N GLY A 295 39.099 32.344 15.308 1.00 44.20 N ANISOU 2164 N GLY A 295 5371 5998 5423 568 71 303 N ATOM 2165 CA GLY A 295 38.346 33.521 15.758 1.00 43.31 C ANISOU 2165 CA GLY A 295 5310 5846 5299 534 120 314 C ATOM 2166 C GLY A 295 36.933 33.407 15.235 1.00 44.55 C ANISOU 2166 C GLY A 295 5488 5926 5513 556 139 360 C ATOM 2167 O GLY A 295 36.550 32.341 14.743 1.00 48.56 O ANISOU 2167 O GLY A 295 5971 6413 6065 594 111 386 O ATOM 2168 N ASN A 296 36.140 34.475 15.349 1.00 44.17 N ANISOU 2168 N ASN A 296 5485 5837 5460 534 185 372 N ATOM 2169 CA ASN A 296 34.773 34.478 14.792 1.00 44.83 C ANISOU 2169 CA ASN A 296 5583 5857 5591 555 205 416 C ATOM 2170 C ASN A 296 34.814 34.602 13.254 1.00 45.69 C ANISOU 2170 C ASN A 296 5676 5954 5729 543 201 400 C ATOM 2171 O ASN A 296 35.270 35.624 12.720 1.00 43.88 O ANISOU 2171 O ASN A 296 5465 5731 5474 503 221 365 O ATOM 2172 CB ASN A 296 33.987 35.651 15.385 1.00 47.91 C ANISOU 2172 CB ASN A 296 6029 6214 5959 544 258 431 C ATOM 2173 CG ASN A 296 32.527 35.710 14.938 1.00 47.24 C ANISOU 2173 CG ASN A 296 5957 6075 5915 571 283 481 C ATOM 2174 OD1 ASN A 296 32.012 34.861 14.223 1.00 50.31 O ANISOU 2174 OD1 ASN A 296 6313 6449 6351 594 261 507 O ATOM 2175 ND2 ASN A 296 31.861 36.745 15.369 1.00 47.86 N ANISOU 2175 ND2 ASN A 296 6083 6127 5972 569 329 493 N ATOM 2176 N ILE A 297 34.332 33.563 12.558 1.00 43.39 N ANISOU 2176 N ILE A 297 5354 5643 5487 574 173 425 N ATOM 2177 CA ILE A 297 34.267 33.567 11.107 1.00 46.00 C ANISOU 2177 CA ILE A 297 5668 5962 5847 567 167 414 C ATOM 2178 C ILE A 297 32.819 33.610 10.630 1.00 47.18 C ANISOU 2178 C ILE A 297 5828 6058 6037 584 188 462 C ATOM 2179 O ILE A 297 32.473 33.048 9.595 1.00 45.85 O ANISOU 2179 O ILE A 297 5637 5875 5907 593 170 471 O ATOM 2180 CB ILE A 297 35.040 32.390 10.494 1.00 46.19 C ANISOU 2180 CB ILE A 297 5646 6014 5888 585 116 395 C ATOM 2181 CG1 ILE A 297 34.519 31.058 11.026 1.00 47.41 C ANISOU 2181 CG1 ILE A 297 5791 6149 6073 628 86 436 C ATOM 2182 CG2 ILE A 297 36.515 32.534 10.835 1.00 46.60 C ANISOU 2182 CG2 ILE A 297 5681 6132 5892 567 99 344 C ATOM 2183 CD1 ILE A 297 35.012 29.868 10.237 1.00 48.71 C ANISOU 2183 CD1 ILE A 297 5922 6322 6261 653 39 423 C ATOM 2184 N MET A 298 31.996 34.308 11.404 1.00 49.84 N ANISOU 2184 N MET A 298 6202 6373 6362 587 227 490 N ATOM 2185 CA MET A 298 30.624 34.624 11.061 1.00 49.57 C ANISOU 2185 CA MET A 298 6181 6300 6353 603 257 535 C ATOM 2186 C MET A 298 29.755 33.402 10.770 1.00 47.76 C ANISOU 2186 C MET A 298 5918 6055 6170 630 231 579 C ATOM 2187 O MET A 298 29.621 32.506 11.612 1.00 50.27 O ANISOU 2187 O MET A 298 6227 6377 6494 647 210 604 O ATOM 2188 CB MET A 298 30.592 35.590 9.892 1.00 53.12 C ANISOU 2188 CB MET A 298 6644 6735 6801 583 280 515 C ATOM 2189 CG MET A 298 31.517 36.762 9.973 1.00 61.79 C ANISOU 2189 CG MET A 298 7779 7845 7852 546 303 467 C ATOM 2190 SD MET A 298 31.425 37.602 11.525 1.00 71.01 S ANISOU 2190 SD MET A 298 9000 9008 8970 543 341 471 S ATOM 2191 CE MET A 298 33.143 38.109 11.684 1.00 76.63 C ANISOU 2191 CE MET A 298 9719 9764 9630 487 329 402 C ATOM 2192 N GLY A 299 29.151 33.372 9.587 1.00 42.28 N ANISOU 2192 N GLY A 299 5211 5345 5509 631 231 591 N ATOM 2193 CA GLY A 299 28.190 32.363 9.263 1.00 44.25 C ANISOU 2193 CA GLY A 299 5434 5580 5799 648 212 636 C ATOM 2194 C GLY A 299 28.808 30.985 9.192 1.00 44.61 C ANISOU 2194 C GLY A 299 5454 5631 5864 652 159 626 C ATOM 2195 O GLY A 299 28.096 30.001 9.274 1.00 50.29 O ANISOU 2195 O GLY A 299 6161 6336 6610 663 139 664 O ATOM 2196 N ALA A 300 30.141 30.912 9.074 1.00 43.08 N ANISOU 2196 N ALA A 300 5254 5460 5652 645 136 575 N ATOM 2197 CA ALA A 300 30.814 29.622 9.007 1.00 44.10 C ANISOU 2197 CA ALA A 300 5364 5597 5795 659 86 563 C ATOM 2198 C ALA A 300 31.196 29.041 10.397 1.00 43.60 C ANISOU 2198 C ALA A 300 5309 5545 5710 677 72 573 C ATOM 2199 O ALA A 300 31.559 27.869 10.508 1.00 46.23 O ANISOU 2199 O ALA A 300 5633 5876 6053 697 32 575 O ATOM 2200 CB ALA A 300 32.040 29.733 8.123 1.00 45.49 C ANISOU 2200 CB ALA A 300 5522 5802 5960 650 67 506 C ATOM 2201 N THR A 301 31.060 29.831 11.451 1.00 45.31 N ANISOU 2201 N THR A 301 5547 5771 5896 671 105 582 N ATOM 2202 CA THR A 301 31.562 29.436 12.758 1.00 45.28 C ANISOU 2202 CA THR A 301 5551 5787 5865 685 93 584 C ATOM 2203 C THR A 301 30.895 28.187 13.322 1.00 45.29 C ANISOU 2203 C THR A 301 5553 5765 5890 709 69 634 C ATOM 2204 O THR A 301 31.580 27.294 13.823 1.00 45.71 O ANISOU 2204 O THR A 301 5603 5829 5934 729 35 628 O ATOM 2205 CB THR A 301 31.460 30.601 13.750 1.00 47.21 C ANISOU 2205 CB THR A 301 5822 6043 6070 673 136 584 C ATOM 2206 OG1 THR A 301 32.125 31.760 13.207 1.00 47.72 O ANISOU 2206 OG1 THR A 301 5895 6125 6110 644 158 537 O ATOM 2207 CG2 THR A 301 32.147 30.246 14.984 1.00 48.90 C ANISOU 2207 CG2 THR A 301 6040 6285 6251 683 122 578 C ATOM 2208 N LEU A 302 29.580 28.086 13.212 1.00 40.93 N ANISOU 2208 N LEU A 302 5004 5182 5364 706 86 682 N ATOM 2209 CA LEU A 302 28.868 26.886 13.695 1.00 43.41 C ANISOU 2209 CA LEU A 302 5320 5472 5698 718 64 732 C ATOM 2210 C LEU A 302 29.329 25.607 12.978 1.00 44.98 C ANISOU 2210 C LEU A 302 5513 5654 5923 729 13 722 C ATOM 2211 O LEU A 302 29.477 24.547 13.595 1.00 43.52 O ANISOU 2211 O LEU A 302 5339 5457 5738 746 -16 741 O ATOM 2212 CB LEU A 302 27.358 27.061 13.475 1.00 44.24 C ANISOU 2212 CB LEU A 302 5422 5558 5826 707 90 784 C ATOM 2213 CG LEU A 302 26.449 25.879 13.789 1.00 44.91 C ANISOU 2213 CG LEU A 302 5508 5621 5934 705 70 840 C ATOM 2214 CD1 LEU A 302 26.686 25.409 15.189 1.00 45.38 C ANISOU 2214 CD1 LEU A 302 5585 5687 5969 719 63 859 C ATOM 2215 CD2 LEU A 302 24.968 26.248 13.609 1.00 45.11 C ANISOU 2215 CD2 LEU A 302 5521 5644 5971 691 103 889 C ATOM 2216 N PHE A 303 29.547 25.705 11.667 1.00 43.92 N ANISOU 2216 N PHE A 303 5364 5516 5808 721 4 692 N ATOM 2217 CA PHE A 303 29.991 24.546 10.903 1.00 45.81 C ANISOU 2217 CA PHE A 303 5600 5736 6068 734 -41 678 C ATOM 2218 C PHE A 303 31.427 24.159 11.278 1.00 45.95 C ANISOU 2218 C PHE A 303 5617 5782 6058 763 -70 636 C ATOM 2219 O PHE A 303 31.743 22.978 11.385 1.00 44.09 O ANISOU 2219 O PHE A 303 5394 5529 5827 789 -109 642 O ATOM 2220 CB PHE A 303 29.862 24.814 9.408 1.00 47.78 C ANISOU 2220 CB PHE A 303 5831 5979 6341 718 -42 656 C ATOM 2221 CG PHE A 303 28.459 25.112 8.963 1.00 44.59 C ANISOU 2221 CG PHE A 303 5422 5555 5963 694 -17 698 C ATOM 2222 CD1 PHE A 303 27.372 24.585 9.630 1.00 46.70 C ANISOU 2222 CD1 PHE A 303 5700 5803 6241 687 -13 755 C ATOM 2223 CD2 PHE A 303 28.236 25.868 7.835 1.00 49.50 C ANISOU 2223 CD2 PHE A 303 6028 6183 6596 678 0 681 C ATOM 2224 CE1 PHE A 303 26.075 24.851 9.218 1.00 47.96 C ANISOU 2224 CE1 PHE A 303 5847 5956 6418 665 9 795 C ATOM 2225 CE2 PHE A 303 26.938 26.127 7.395 1.00 50.60 C ANISOU 2225 CE2 PHE A 303 6158 6311 6755 660 22 721 C ATOM 2226 CZ PHE A 303 25.857 25.629 8.113 1.00 49.73 C ANISOU 2226 CZ PHE A 303 6053 6189 6652 655 27 778 C ATOM 2227 N LEU A 304 32.276 25.151 11.543 1.00 44.89 N ANISOU 2227 N LEU A 304 5472 5693 5889 758 -52 597 N ATOM 2228 CA LEU A 304 33.607 24.856 12.068 1.00 47.07 C ANISOU 2228 CA LEU A 304 5742 6011 6131 785 -76 562 C ATOM 2229 C LEU A 304 33.497 24.193 13.453 1.00 46.38 C ANISOU 2229 C LEU A 304 5674 5918 6028 808 -86 597 C ATOM 2230 O LEU A 304 34.201 23.259 13.734 1.00 50.28 O ANISOU 2230 O LEU A 304 6173 6420 6511 843 -122 591 O ATOM 2231 CB LEU A 304 34.461 26.112 12.148 1.00 46.95 C ANISOU 2231 CB LEU A 304 5712 6050 6077 764 -52 516 C ATOM 2232 CG LEU A 304 35.895 25.865 12.649 1.00 51.30 C ANISOU 2232 CG LEU A 304 6246 6659 6585 787 -77 477 C ATOM 2233 CD1 LEU A 304 36.680 24.944 11.729 1.00 51.90 C ANISOU 2233 CD1 LEU A 304 6303 6747 6669 819 -120 448 C ATOM 2234 CD2 LEU A 304 36.655 27.149 12.827 1.00 53.22 C ANISOU 2234 CD2 LEU A 304 6478 6958 6786 753 -51 435 C ATOM 2235 N SER A 305 32.606 24.679 14.307 1.00 46.09 N ANISOU 2235 N SER A 305 5653 5870 5989 791 -54 636 N ATOM 2236 CA SER A 305 32.370 24.047 15.607 1.00 46.99 C ANISOU 2236 CA SER A 305 5787 5978 6090 809 -61 675 C ATOM 2237 C SER A 305 31.948 22.593 15.426 1.00 48.30 C ANISOU 2237 C SER A 305 5970 6095 6284 828 -98 710 C ATOM 2238 O SER A 305 32.423 21.711 16.155 1.00 47.88 O ANISOU 2238 O SER A 305 5934 6042 6215 860 -126 720 O ATOM 2239 CB SER A 305 31.300 24.792 16.379 1.00 48.51 C ANISOU 2239 CB SER A 305 5989 6162 6277 786 -18 715 C ATOM 2240 OG SER A 305 31.018 24.197 17.627 1.00 48.24 O ANISOU 2240 OG SER A 305 5974 6125 6230 801 -23 756 O ATOM 2241 N LEU A 306 31.054 22.337 14.468 1.00 44.57 N ANISOU 2241 N LEU A 306 5499 5583 5851 808 -98 730 N ATOM 2242 CA LEU A 306 30.653 20.947 14.204 1.00 47.40 C ANISOU 2242 CA LEU A 306 5882 5891 6236 818 -134 760 C ATOM 2243 C LEU A 306 31.882 20.071 13.868 1.00 47.32 C ANISOU 2243 C LEU A 306 5880 5884 6216 861 -179 722 C ATOM 2244 O LEU A 306 32.060 19.004 14.430 1.00 51.07 O ANISOU 2244 O LEU A 306 6385 6334 6684 890 -208 742 O ATOM 2245 CB LEU A 306 29.616 20.880 13.086 1.00 47.67 C ANISOU 2245 CB LEU A 306 5910 5890 6309 784 -129 778 C ATOM 2246 CG LEU A 306 29.234 19.483 12.562 1.00 49.49 C ANISOU 2246 CG LEU A 306 6169 6065 6566 784 -168 800 C ATOM 2247 CD1 LEU A 306 28.633 18.590 13.620 1.00 48.00 C ANISOU 2247 CD1 LEU A 306 6016 5847 6374 782 -178 856 C ATOM 2248 CD2 LEU A 306 28.237 19.634 11.423 1.00 52.90 C ANISOU 2248 CD2 LEU A 306 6588 6478 7032 745 -159 812 C ATOM 2249 N ALA A 307 32.717 20.547 12.949 1.00 44.47 N ANISOU 2249 N ALA A 307 5492 5553 5851 868 -183 667 N ATOM 2250 CA ALA A 307 33.920 19.862 12.544 1.00 47.87 C ANISOU 2250 CA ALA A 307 5922 5999 6267 913 -221 626 C ATOM 2251 C ALA A 307 34.841 19.619 13.734 1.00 47.39 C ANISOU 2251 C ALA A 307 5865 5977 6163 954 -234 621 C ATOM 2252 O ALA A 307 35.411 18.549 13.863 1.00 45.79 O ANISOU 2252 O ALA A 307 5684 5764 5950 1002 -271 620 O ATOM 2253 CB ALA A 307 34.645 20.677 11.492 1.00 47.42 C ANISOU 2253 CB ALA A 307 5826 5985 6204 905 -214 570 C ATOM 2254 N SER A 308 34.976 20.632 14.586 1.00 48.47 N ANISOU 2254 N SER A 308 5983 6159 6271 935 -203 618 N ATOM 2255 CA SER A 308 35.775 20.528 15.807 1.00 47.40 C ANISOU 2255 CA SER A 308 5849 6069 6092 967 -211 615 C ATOM 2256 C SER A 308 35.224 19.516 16.792 1.00 48.98 C ANISOU 2256 C SER A 308 6089 6225 6293 988 -226 670 C ATOM 2257 O SER A 308 35.974 18.715 17.381 1.00 47.57 O ANISOU 2257 O SER A 308 5924 6060 6088 1039 -256 670 O ATOM 2258 CB SER A 308 35.845 21.880 16.488 1.00 47.93 C ANISOU 2258 CB SER A 308 5895 6185 6129 932 -171 603 C ATOM 2259 OG SER A 308 36.809 21.865 17.519 1.00 46.68 O ANISOU 2259 OG SER A 308 5729 6085 5923 959 -181 589 O ATOM 2260 N THR A 309 33.910 19.566 16.992 1.00 46.70 N ANISOU 2260 N THR A 309 5820 5889 6033 951 -204 719 N ATOM 2261 CA THR A 309 33.238 18.588 17.831 1.00 47.27 C ANISOU 2261 CA THR A 309 5933 5917 6111 960 -217 777 C ATOM 2262 C THR A 309 33.534 17.172 17.330 1.00 50.26 C ANISOU 2262 C THR A 309 6347 6247 6501 999 -263 780 C ATOM 2263 O THR A 309 33.868 16.309 18.102 1.00 49.70 O ANISOU 2263 O THR A 309 6308 6164 6410 1038 -288 801 O ATOM 2264 CB THR A 309 31.720 18.805 17.848 1.00 47.05 C ANISOU 2264 CB THR A 309 5914 5849 6114 909 -188 827 C ATOM 2265 OG1 THR A 309 31.428 19.988 18.603 1.00 47.09 O ANISOU 2265 OG1 THR A 309 5897 5894 6099 886 -145 832 O ATOM 2266 CG2 THR A 309 31.007 17.585 18.464 1.00 48.96 C ANISOU 2266 CG2 THR A 309 6201 6037 6364 911 -208 887 C ATOM 2267 N ILE A 310 33.413 16.962 16.027 1.00 54.42 N ANISOU 2267 N ILE A 310 6872 6744 7058 990 -275 760 N ATOM 2268 CA ILE A 310 33.596 15.641 15.460 1.00 56.34 C ANISOU 2268 CA ILE A 310 7158 6934 7315 1024 -317 762 C ATOM 2269 C ILE A 310 35.023 15.133 15.657 1.00 55.11 C ANISOU 2269 C ILE A 310 7004 6812 7121 1098 -349 725 C ATOM 2270 O ILE A 310 35.188 14.068 16.173 1.00 55.24 O ANISOU 2270 O ILE A 310 7068 6795 7125 1139 -378 749 O ATOM 2271 CB ILE A 310 33.202 15.583 13.974 1.00 55.89 C ANISOU 2271 CB ILE A 310 7096 6844 7295 998 -322 742 C ATOM 2272 CG1 ILE A 310 31.691 15.684 13.865 1.00 55.76 C ANISOU 2272 CG1 ILE A 310 7088 6784 7312 933 -300 792 C ATOM 2273 CG2 ILE A 310 33.686 14.278 13.331 1.00 60.46 C ANISOU 2273 CG2 ILE A 310 7719 7374 7877 1044 -368 729 C ATOM 2274 CD1 ILE A 310 31.168 15.823 12.457 1.00 56.27 C ANISOU 2274 CD1 ILE A 310 7139 6827 7412 898 -299 776 C ATOM 2275 N ASP A 311 36.027 15.909 15.285 1.00 53.41 N ANISOU 2275 N ASP A 311 6740 6670 6884 1114 -344 670 N ATOM 2276 CA ASP A 311 37.434 15.526 15.483 1.00 53.35 C ANISOU 2276 CA ASP A 311 6721 6715 6833 1185 -373 633 C ATOM 2277 C ASP A 311 37.861 15.369 16.941 1.00 55.11 C ANISOU 2277 C ASP A 311 6952 6972 7014 1218 -376 655 C ATOM 2278 O ASP A 311 38.760 14.573 17.235 1.00 55.18 O ANISOU 2278 O ASP A 311 6976 6999 6990 1289 -408 646 O ATOM 2279 CB ASP A 311 38.378 16.557 14.842 1.00 56.38 C ANISOU 2279 CB ASP A 311 7040 7183 7196 1180 -361 571 C ATOM 2280 CG ASP A 311 38.442 16.456 13.341 1.00 58.02 C ANISOU 2280 CG ASP A 311 7239 7374 7432 1177 -371 537 C ATOM 2281 OD1 ASP A 311 37.854 15.515 12.763 1.00 59.16 O ANISOU 2281 OD1 ASP A 311 7428 7441 7607 1185 -391 557 O ATOM 2282 OD2 ASP A 311 39.100 17.323 12.720 1.00 63.09 O ANISOU 2282 OD2 ASP A 311 7830 8079 8060 1164 -359 489 O ATOM 2283 N ASN A 312 37.280 16.141 17.858 1.00 53.45 N ANISOU 2283 N ASN A 312 6731 6777 6799 1173 -343 682 N ATOM 2284 CA ASN A 312 37.829 16.190 19.229 1.00 53.47 C ANISOU 2284 CA ASN A 312 6731 6831 6755 1202 -343 693 C ATOM 2285 C ASN A 312 37.012 15.444 20.261 1.00 54.64 C ANISOU 2285 C ASN A 312 6931 6922 6907 1203 -346 758 C ATOM 2286 O ASN A 312 37.488 15.209 21.355 1.00 56.69 O ANISOU 2286 O ASN A 312 7197 7214 7127 1238 -354 772 O ATOM 2287 CB ASN A 312 38.051 17.627 19.673 1.00 50.07 C ANISOU 2287 CB ASN A 312 6249 6474 6299 1159 -306 668 C ATOM 2288 CG ASN A 312 39.057 18.340 18.806 1.00 52.97 C ANISOU 2288 CG ASN A 312 6565 6909 6650 1158 -306 603 C ATOM 2289 OD1 ASN A 312 40.241 18.093 18.903 1.00 54.05 O ANISOU 2289 OD1 ASN A 312 6680 7110 6746 1208 -330 571 O ATOM 2290 ND2 ASN A 312 38.583 19.192 17.909 1.00 53.99 N ANISOU 2290 ND2 ASN A 312 6676 7028 6809 1104 -279 584 N ATOM 2291 N GLY A 313 35.796 15.052 19.909 1.00 53.30 N ANISOU 2291 N GLY A 313 6796 6672 6780 1163 -340 799 N ATOM 2292 CA GLY A 313 34.970 14.270 20.808 1.00 55.40 C ANISOU 2292 CA GLY A 313 7114 6883 7051 1157 -344 864 C ATOM 2293 C GLY A 313 35.077 12.772 20.581 1.00 56.05 C ANISOU 2293 C GLY A 313 7262 6895 7137 1203 -387 884 C ATOM 2294 O GLY A 313 35.884 12.309 19.821 1.00 52.80 O ANISOU 2294 O GLY A 313 6856 6483 6722 1251 -415 847 O ATOM 2295 N ASP A 314 34.216 12.023 21.247 1.00 60.79 N ANISOU 2295 N ASP A 314 7916 7435 7746 1186 -391 946 N ATOM 2296 CA ASP A 314 34.239 10.562 21.205 1.00 58.39 C ANISOU 2296 CA ASP A 314 7689 7053 7440 1225 -430 973 C ATOM 2297 C ASP A 314 33.107 9.993 20.361 1.00 56.87 C ANISOU 2297 C ASP A 314 7539 6774 7293 1168 -434 1001 C ATOM 2298 O ASP A 314 31.932 10.116 20.725 1.00 60.67 O ANISOU 2298 O ASP A 314 8026 7231 7792 1101 -412 1049 O ATOM 2299 CB ASP A 314 34.136 10.020 22.629 1.00 58.37 C ANISOU 2299 CB ASP A 314 7727 7042 7406 1244 -435 1026 C ATOM 2300 CG ASP A 314 34.452 8.535 22.703 1.00 62.21 C ANISOU 2300 CG ASP A 314 8301 7457 7880 1303 -478 1049 C ATOM 2301 OD1 ASP A 314 33.753 7.763 22.008 1.00 64.53 O ANISOU 2301 OD1 ASP A 314 8649 7663 8203 1273 -492 1069 O ATOM 2302 OD2 ASP A 314 35.400 8.165 23.432 1.00 64.14 O ANISOU 2302 OD2 ASP A 314 8557 7731 8079 1378 -497 1046 O ATOM 2303 N PHE A 315 33.477 9.348 19.257 1.00 58.85 N ANISOU 2303 N PHE A 315 7818 6983 7558 1195 -463 970 N ATOM 2304 CA PHE A 315 32.530 8.758 18.308 1.00 60.49 C ANISOU 2304 CA PHE A 315 8067 7109 7805 1143 -472 987 C ATOM 2305 C PHE A 315 32.740 7.253 18.096 1.00 63.69 C ANISOU 2305 C PHE A 315 8570 7425 8204 1186 -515 1000 C ATOM 2306 O PHE A 315 32.543 6.723 16.993 1.00 67.54 O ANISOU 2306 O PHE A 315 9090 7856 8714 1174 -533 984 O ATOM 2307 CB PHE A 315 32.587 9.540 16.993 1.00 58.51 C ANISOU 2307 CB PHE A 315 7760 6888 7583 1120 -460 935 C ATOM 2308 CG PHE A 315 32.111 10.955 17.160 1.00 59.44 C ANISOU 2308 CG PHE A 315 7800 7072 7710 1066 -415 932 C ATOM 2309 CD1 PHE A 315 32.998 11.955 17.526 1.00 55.95 C ANISOU 2309 CD1 PHE A 315 7298 6717 7242 1096 -397 894 C ATOM 2310 CD2 PHE A 315 30.763 11.260 17.048 1.00 59.87 C ANISOU 2310 CD2 PHE A 315 7847 7106 7795 986 -389 972 C ATOM 2311 CE1 PHE A 315 32.566 13.237 17.748 1.00 59.41 C ANISOU 2311 CE1 PHE A 315 7679 7209 7686 1048 -355 892 C ATOM 2312 CE2 PHE A 315 30.317 12.551 17.253 1.00 59.60 C ANISOU 2312 CE2 PHE A 315 7748 7131 7765 946 -346 971 C ATOM 2313 CZ PHE A 315 31.224 13.548 17.608 1.00 58.90 C ANISOU 2313 CZ PHE A 315 7609 7118 7651 978 -329 931 C ATOM 2314 N SER A 316 33.074 6.547 19.166 1.00 62.61 N ANISOU 2314 N SER A 316 8484 7270 8033 1233 -531 1033 N ATOM 2315 CA SER A 316 33.193 5.075 19.062 1.00 67.73 C ANISOU 2315 CA SER A 316 9241 7822 8671 1273 -572 1053 C ATOM 2316 C SER A 316 31.829 4.378 18.896 1.00 67.76 C ANISOU 2316 C SER A 316 9310 7731 8702 1185 -573 1108 C ATOM 2317 O SER A 316 31.773 3.250 18.432 1.00 74.43 O ANISOU 2317 O SER A 316 10246 8485 9548 1197 -605 1115 O ATOM 2318 CB SER A 316 33.958 4.509 20.254 1.00 64.83 C ANISOU 2318 CB SER A 316 8914 7463 8256 1353 -589 1075 C ATOM 2319 OG SER A 316 33.461 5.016 21.482 1.00 64.16 O ANISOU 2319 OG SER A 316 8800 7416 8159 1315 -562 1120 O ATOM 2320 N THR A 317 30.754 5.062 19.290 1.00 65.48 N ANISOU 2320 N THR A 317 8977 7468 8432 1097 -540 1145 N ATOM 2321 CA THR A 317 29.375 4.695 18.954 1.00 67.10 C ANISOU 2321 CA THR A 317 9215 7612 8666 997 -534 1190 C ATOM 2322 C THR A 317 28.664 5.952 18.350 1.00 67.50 C ANISOU 2322 C THR A 317 9168 7727 8749 928 -496 1174 C ATOM 2323 O THR A 317 29.081 7.080 18.619 1.00 59.27 O ANISOU 2323 O THR A 317 8046 6770 7702 949 -469 1148 O ATOM 2324 CB THR A 317 28.632 4.162 20.207 1.00 70.21 C ANISOU 2324 CB THR A 317 9657 7975 9041 958 -530 1266 C ATOM 2325 OG1 THR A 317 27.283 3.853 19.873 1.00 82.55 O ANISOU 2325 OG1 THR A 317 11243 9492 10628 854 -523 1310 O ATOM 2326 CG2 THR A 317 28.588 5.172 21.329 1.00 69.42 C ANISOU 2326 CG2 THR A 317 9484 7964 8926 957 -494 1283 C ATOM 2327 N PRO A 318 27.600 5.777 17.539 1.00 63.78 N ANISOU 2327 N PRO A 318 8706 7218 8309 846 -494 1191 N ATOM 2328 CA PRO A 318 26.975 7.005 16.988 1.00 61.35 C ANISOU 2328 CA PRO A 318 8304 6977 8028 793 -457 1177 C ATOM 2329 C PRO A 318 26.570 8.015 18.059 1.00 61.08 C ANISOU 2329 C PRO A 318 8205 7018 7983 774 -416 1206 C ATOM 2330 O PRO A 318 26.249 7.628 19.165 1.00 62.30 O ANISOU 2330 O PRO A 318 8391 7163 8117 764 -413 1257 O ATOM 2331 CB PRO A 318 25.737 6.481 16.244 1.00 60.04 C ANISOU 2331 CB PRO A 318 8165 6758 7887 701 -462 1209 C ATOM 2332 CG PRO A 318 26.079 5.056 15.894 1.00 61.20 C ANISOU 2332 CG PRO A 318 8419 6806 8027 722 -508 1208 C ATOM 2333 CD PRO A 318 26.981 4.551 17.000 1.00 63.09 C ANISOU 2333 CD PRO A 318 8708 7031 8231 801 -523 1218 C ATOM 2334 N ARG A 319 26.617 9.304 17.738 1.00 57.92 N ANISOU 2334 N ARG A 319 7721 6691 7593 771 -383 1174 N ATOM 2335 CA ARG A 319 26.316 10.352 18.715 1.00 57.24 C ANISOU 2335 CA ARG A 319 7576 6676 7493 761 -342 1194 C ATOM 2336 C ARG A 319 25.365 11.382 18.149 1.00 55.97 C ANISOU 2336 C ARG A 319 7350 6560 7356 704 -305 1196 C ATOM 2337 O ARG A 319 25.417 11.677 16.964 1.00 57.25 O ANISOU 2337 O ARG A 319 7487 6721 7541 696 -307 1158 O ATOM 2338 CB ARG A 319 27.590 11.099 19.079 1.00 57.84 C ANISOU 2338 CB ARG A 319 7617 6811 7547 833 -336 1143 C ATOM 2339 CG ARG A 319 28.720 10.232 19.591 1.00 58.18 C ANISOU 2339 CG ARG A 319 7712 6830 7561 906 -372 1131 C ATOM 2340 CD ARG A 319 28.442 9.638 20.976 1.00 59.52 C ANISOU 2340 CD ARG A 319 7925 6984 7703 907 -374 1190 C ATOM 2341 NE ARG A 319 29.669 8.990 21.450 1.00 62.90 N ANISOU 2341 NE ARG A 319 8393 7404 8099 991 -406 1172 N ATOM 2342 CZ ARG A 319 29.757 8.141 22.469 1.00 64.14 C ANISOU 2342 CZ ARG A 319 8609 7530 8228 1016 -422 1215 C ATOM 2343 NH1 ARG A 319 28.688 7.821 23.181 1.00 64.32 N ANISOU 2343 NH1 ARG A 319 8659 7526 8251 958 -411 1280 N ATOM 2344 NH2 ARG A 319 30.939 7.606 22.774 1.00 64.20 N ANISOU 2344 NH2 ARG A 319 8649 7539 8205 1101 -451 1193 N ATOM 2345 N ARG A 320 24.544 11.970 19.001 1.00 54.43 N ANISOU 2345 N ARG A 320 7123 6406 7151 670 -270 1239 N ATOM 2346 CA ARG A 320 23.697 13.066 18.572 1.00 55.07 C ANISOU 2346 CA ARG A 320 7138 6538 7246 630 -230 1242 C ATOM 2347 C ARG A 320 24.284 14.414 18.978 1.00 50.92 C ANISOU 2347 C ARG A 320 6560 6079 6705 669 -196 1206 C ATOM 2348 O ARG A 320 24.721 14.612 20.107 1.00 51.87 O ANISOU 2348 O ARG A 320 6684 6225 6797 700 -187 1212 O ATOM 2349 CB ARG A 320 22.294 12.916 19.134 1.00 54.97 C ANISOU 2349 CB ARG A 320 7119 6534 7230 566 -210 1313 C ATOM 2350 CG ARG A 320 21.400 14.075 18.759 1.00 56.02 C ANISOU 2350 CG ARG A 320 7184 6727 7373 535 -167 1318 C ATOM 2351 CD ARG A 320 19.936 13.779 18.990 1.00 54.01 C ANISOU 2351 CD ARG A 320 6918 6484 7116 466 -152 1387 C ATOM 2352 NE ARG A 320 19.403 13.069 17.844 1.00 53.87 N ANISOU 2352 NE ARG A 320 6914 6428 7123 415 -177 1392 N ATOM 2353 CZ ARG A 320 19.130 11.765 17.785 1.00 59.36 C ANISOU 2353 CZ ARG A 320 7670 7063 7821 373 -213 1423 C ATOM 2354 NH1 ARG A 320 19.316 10.947 18.837 1.00 61.32 N ANISOU 2354 NH1 ARG A 320 7973 7277 8047 377 -229 1457 N ATOM 2355 NH2 ARG A 320 18.667 11.272 16.642 1.00 60.03 N ANISOU 2355 NH2 ARG A 320 7762 7117 7926 326 -233 1419 N ATOM 2356 N ILE A 321 24.270 15.348 18.044 1.00 51.28 N ANISOU 2356 N ILE A 321 6561 6155 6769 665 -177 1168 N ATOM 2357 CA ILE A 321 24.815 16.680 18.284 1.00 50.17 C ANISOU 2357 CA ILE A 321 6377 6071 6612 694 -144 1130 C ATOM 2358 C ILE A 321 23.715 17.692 18.115 1.00 49.14 C ANISOU 2358 C ILE A 321 6201 5979 6489 659 -99 1151 C ATOM 2359 O ILE A 321 23.042 17.700 17.087 1.00 47.90 O ANISOU 2359 O ILE A 321 6028 5814 6357 626 -98 1155 O ATOM 2360 CB ILE A 321 25.949 17.022 17.294 1.00 48.98 C ANISOU 2360 CB ILE A 321 6214 5925 6470 728 -158 1059 C ATOM 2361 CG1 ILE A 321 27.062 15.999 17.427 1.00 51.97 C ANISOU 2361 CG1 ILE A 321 6635 6273 6837 772 -203 1037 C ATOM 2362 CG2 ILE A 321 26.476 18.448 17.528 1.00 45.68 C ANISOU 2362 CG2 ILE A 321 5756 5566 6032 746 -122 1020 C ATOM 2363 CD1 ILE A 321 28.136 16.146 16.365 1.00 54.35 C ANISOU 2363 CD1 ILE A 321 6924 6580 7146 805 -222 970 C ATOM 2364 N GLY A 322 23.559 18.550 19.113 1.00 50.84 N ANISOU 2364 N GLY A 322 6399 6239 6679 669 -63 1164 N ATOM 2365 CA GLY A 322 22.624 19.684 19.059 1.00 51.24 C ANISOU 2365 CA GLY A 322 6408 6332 6726 651 -15 1179 C ATOM 2366 C GLY A 322 23.334 20.939 18.550 1.00 52.66 C ANISOU 2366 C GLY A 322 6566 6539 6903 676 7 1120 C ATOM 2367 O GLY A 322 24.430 21.281 19.016 1.00 52.35 O ANISOU 2367 O GLY A 322 6535 6511 6841 708 4 1080 O ATOM 2368 N MET A 323 22.690 21.628 17.612 1.00 48.25 N ANISOU 2368 N MET A 323 5978 5992 6361 660 30 1116 N ATOM 2369 CA MET A 323 23.288 22.738 16.881 1.00 49.57 C ANISOU 2369 CA MET A 323 6130 6176 6529 675 48 1061 C ATOM 2370 C MET A 323 22.501 24.026 17.144 1.00 48.52 C ANISOU 2370 C MET A 323 5976 6080 6379 677 102 1076 C ATOM 2371 O MET A 323 21.292 24.060 16.896 1.00 50.88 O ANISOU 2371 O MET A 323 6255 6390 6687 658 120 1120 O ATOM 2372 CB MET A 323 23.232 22.459 15.359 1.00 49.68 C ANISOU 2372 CB MET A 323 6132 6167 6577 659 27 1040 C ATOM 2373 CG MET A 323 23.911 21.198 14.840 1.00 52.76 C ANISOU 2373 CG MET A 323 6545 6515 6986 659 -25 1023 C ATOM 2374 SD MET A 323 25.687 21.365 14.656 1.00 56.01 S ANISOU 2374 SD MET A 323 6966 6930 7384 700 -47 948 S ATOM 2375 CE MET A 323 25.713 22.236 13.096 1.00 54.11 C ANISOU 2375 CE MET A 323 6695 6699 7163 688 -34 906 C ATOM 2376 N PHE A 324 23.166 25.083 17.611 1.00 45.76 N ANISOU 2376 N PHE A 324 5633 5751 6002 700 128 1040 N ATOM 2377 CA PHE A 324 22.506 26.376 17.781 1.00 45.63 C ANISOU 2377 CA PHE A 324 5608 5762 5966 708 181 1047 C ATOM 2378 C PHE A 324 23.158 27.443 16.917 1.00 46.34 C ANISOU 2378 C PHE A 324 5699 5852 6054 715 196 991 C ATOM 2379 O PHE A 324 24.355 27.729 17.062 1.00 43.73 O ANISOU 2379 O PHE A 324 5384 5522 5708 722 187 941 O ATOM 2380 CB PHE A 324 22.489 26.847 19.243 1.00 46.27 C ANISOU 2380 CB PHE A 324 5705 5867 6006 726 209 1062 C ATOM 2381 CG PHE A 324 21.951 28.239 19.393 1.00 43.96 C ANISOU 2381 CG PHE A 324 5415 5598 5690 742 264 1061 C ATOM 2382 CD1 PHE A 324 20.624 28.495 19.136 1.00 44.30 C ANISOU 2382 CD1 PHE A 324 5436 5657 5738 742 292 1107 C ATOM 2383 CD2 PHE A 324 22.781 29.294 19.692 1.00 44.93 C ANISOU 2383 CD2 PHE A 324 5562 5725 5783 755 285 1012 C ATOM 2384 CE1 PHE A 324 20.108 29.787 19.198 1.00 45.81 C ANISOU 2384 CE1 PHE A 324 5632 5867 5904 766 343 1106 C ATOM 2385 CE2 PHE A 324 22.282 30.590 19.774 1.00 48.08 C ANISOU 2385 CE2 PHE A 324 5974 6136 6157 772 336 1010 C ATOM 2386 CZ PHE A 324 20.932 30.838 19.535 1.00 45.89 C ANISOU 2386 CZ PHE A 324 5677 5872 5884 782 366 1058 C ATOM 2387 N SER A 325 22.353 28.017 16.017 1.00 41.74 N ANISOU 2387 N SER A 325 5099 5273 5485 711 220 1002 N ATOM 2388 CA SER A 325 22.777 29.023 15.083 1.00 44.27 C ANISOU 2388 CA SER A 325 5422 5591 5806 714 237 958 C ATOM 2389 C SER A 325 22.139 30.351 15.464 1.00 44.55 C ANISOU 2389 C SER A 325 5469 5644 5812 734 293 969 C ATOM 2390 O SER A 325 20.956 30.406 15.842 1.00 41.11 O ANISOU 2390 O SER A 325 5021 5227 5371 744 318 1021 O ATOM 2391 CB SER A 325 22.340 28.610 13.677 1.00 45.89 C ANISOU 2391 CB SER A 325 5602 5785 6049 698 218 963 C ATOM 2392 OG SER A 325 22.837 29.502 12.699 1.00 48.78 O ANISOU 2392 OG SER A 325 5970 6147 6415 699 230 918 O ATOM 2393 N TYR A 326 22.919 31.417 15.349 1.00 43.22 N ANISOU 2393 N TYR A 326 5327 5471 5620 739 313 920 N ATOM 2394 CA TYR A 326 22.451 32.772 15.656 1.00 41.99 C ANISOU 2394 CA TYR A 326 5198 5323 5433 761 368 922 C ATOM 2395 C TYR A 326 23.052 33.754 14.690 1.00 41.74 C ANISOU 2395 C TYR A 326 5186 5275 5396 755 381 874 C ATOM 2396 O TYR A 326 24.228 33.633 14.341 1.00 44.86 O ANISOU 2396 O TYR A 326 5586 5663 5794 733 354 825 O ATOM 2397 CB TYR A 326 22.906 33.178 17.049 1.00 42.56 C ANISOU 2397 CB TYR A 326 5304 5403 5463 770 385 911 C ATOM 2398 CG TYR A 326 22.563 34.619 17.398 1.00 42.27 C ANISOU 2398 CG TYR A 326 5308 5366 5387 793 441 905 C ATOM 2399 CD1 TYR A 326 21.304 34.937 17.810 1.00 41.87 C ANISOU 2399 CD1 TYR A 326 5253 5330 5323 825 478 955 C ATOM 2400 CD2 TYR A 326 23.520 35.631 17.345 1.00 43.26 C ANISOU 2400 CD2 TYR A 326 5476 5476 5483 783 457 849 C ATOM 2401 CE1 TYR A 326 20.944 36.232 18.099 1.00 43.89 C ANISOU 2401 CE1 TYR A 326 5552 5582 5540 854 530 951 C ATOM 2402 CE2 TYR A 326 23.195 36.941 17.657 1.00 45.40 C ANISOU 2402 CE2 TYR A 326 5796 5738 5716 804 508 843 C ATOM 2403 CZ TYR A 326 21.896 37.231 18.037 1.00 47.15 C ANISOU 2403 CZ TYR A 326 6017 5970 5925 844 545 894 C ATOM 2404 OH TYR A 326 21.488 38.504 18.326 1.00 48.62 O ANISOU 2404 OH TYR A 326 6256 6145 6071 875 598 892 O ATOM 2405 N GLY A 327 22.259 34.734 14.271 1.00 39.92 N ANISOU 2405 N GLY A 327 4967 5043 5155 775 423 889 N ATOM 2406 CA GLY A 327 22.757 35.831 13.515 1.00 41.83 C ANISOU 2406 CA GLY A 327 5242 5267 5384 772 444 847 C ATOM 2407 C GLY A 327 22.156 37.097 14.075 1.00 43.99 C ANISOU 2407 C GLY A 327 5560 5535 5616 804 501 859 C ATOM 2408 O GLY A 327 20.958 37.138 14.368 1.00 43.16 O ANISOU 2408 O GLY A 327 5443 5447 5507 838 526 910 O ATOM 2409 N SER A 328 22.995 38.110 14.235 1.00 42.42 N ANISOU 2409 N SER A 328 5416 5316 5383 794 522 811 N ATOM 2410 CA SER A 328 22.555 39.419 14.700 1.00 48.83 C ANISOU 2410 CA SER A 328 6288 6113 6150 824 577 814 C ATOM 2411 C SER A 328 21.478 39.955 13.818 1.00 48.71 C ANISOU 2411 C SER A 328 6271 6094 6142 861 607 846 C ATOM 2412 O SER A 328 21.471 39.699 12.598 1.00 48.22 O ANISOU 2412 O SER A 328 6178 6030 6112 848 587 844 O ATOM 2413 CB SER A 328 23.711 40.434 14.663 1.00 50.57 C ANISOU 2413 CB SER A 328 6572 6306 6336 793 590 752 C ATOM 2414 OG SER A 328 24.571 40.184 15.745 1.00 60.58 O ANISOU 2414 OG SER A 328 7851 7585 7581 769 575 725 O ATOM 2415 N GLY A 329 20.575 40.725 14.411 1.00 46.71 N ANISOU 2415 N GLY A 329 6050 5841 5854 910 655 876 N ATOM 2416 CA GLY A 329 19.624 41.472 13.598 1.00 46.13 C ANISOU 2416 CA GLY A 329 5986 5764 5775 954 690 903 C ATOM 2417 C GLY A 329 18.133 41.290 13.823 1.00 44.96 C ANISOU 2417 C GLY A 329 5800 5656 5625 1009 713 970 C ATOM 2418 O GLY A 329 17.414 42.205 13.516 1.00 48.40 O ANISOU 2418 O GLY A 329 6264 6087 6035 1059 755 988 O ATOM 2419 N CYS A 330 17.621 40.154 14.292 1.00 44.20 N ANISOU 2419 N CYS A 330 5640 5602 5552 1003 687 1009 N ATOM 2420 CA CYS A 330 18.333 38.898 14.532 1.00 43.90 C ANISOU 2420 CA CYS A 330 5562 5570 5548 950 634 997 C ATOM 2421 C CYS A 330 17.479 37.669 14.087 1.00 44.96 C ANISOU 2421 C CYS A 330 5617 5744 5722 940 602 1047 C ATOM 2422 O CYS A 330 16.267 37.783 13.887 1.00 41.87 O ANISOU 2422 O CYS A 330 5195 5387 5325 975 625 1097 O ATOM 2423 CB CYS A 330 18.629 38.779 16.027 1.00 45.94 C ANISOU 2423 CB CYS A 330 5843 5833 5777 950 639 994 C ATOM 2424 SG CYS A 330 17.244 38.221 17.087 1.00 46.47 S ANISOU 2424 SG CYS A 330 5868 5955 5832 987 656 1068 S ATOM 2425 N CYS A 331 18.104 36.501 13.947 1.00 42.71 N ANISOU 2425 N CYS A 331 5300 5455 5474 893 550 1035 N ATOM 2426 CA CYS A 331 17.379 35.236 13.722 1.00 44.07 C ANISOU 2426 CA CYS A 331 5408 5658 5679 874 517 1081 C ATOM 2427 C CYS A 331 18.284 34.102 14.185 1.00 45.13 C ANISOU 2427 C CYS A 331 5535 5776 5833 832 468 1062 C ATOM 2428 O CYS A 331 19.523 34.258 14.255 1.00 45.56 O ANISOU 2428 O CYS A 331 5622 5802 5886 816 453 1008 O ATOM 2429 CB CYS A 331 16.963 35.039 12.238 1.00 47.45 C ANISOU 2429 CB CYS A 331 5798 6092 6139 863 502 1089 C ATOM 2430 SG CYS A 331 15.689 33.746 11.896 1.00 49.90 S ANISOU 2430 SG CYS A 331 6032 6450 6477 842 475 1156 S ATOM 2431 N SER A 332 17.667 32.966 14.493 1.00 42.20 N ANISOU 2431 N SER A 332 5124 5428 5480 815 443 1106 N ATOM 2432 CA SER A 332 18.330 31.846 15.117 1.00 40.84 C ANISOU 2432 CA SER A 332 4952 5244 5322 785 401 1100 C ATOM 2433 C SER A 332 17.584 30.545 14.898 1.00 42.03 C ANISOU 2433 C SER A 332 5059 5409 5500 756 368 1148 C ATOM 2434 O SER A 332 16.385 30.547 14.640 1.00 43.29 O ANISOU 2434 O SER A 332 5184 5603 5659 760 385 1196 O ATOM 2435 CB SER A 332 18.402 32.069 16.627 1.00 43.58 C ANISOU 2435 CB SER A 332 5323 5601 5632 803 423 1110 C ATOM 2436 OG SER A 332 17.114 32.055 17.251 1.00 43.76 O ANISOU 2436 OG SER A 332 5323 5665 5637 822 451 1172 O ATOM 2437 N GLU A 333 18.286 29.433 15.076 1.00 42.99 N ANISOU 2437 N GLU A 333 5184 5506 5641 727 322 1136 N ATOM 2438 CA GLU A 333 17.706 28.113 14.849 1.00 44.04 C ANISOU 2438 CA GLU A 333 5290 5642 5801 692 286 1176 C ATOM 2439 C GLU A 333 18.462 27.065 15.654 1.00 44.87 C ANISOU 2439 C GLU A 333 5418 5722 5909 676 248 1171 C ATOM 2440 O GLU A 333 19.708 27.088 15.739 1.00 45.26 O ANISOU 2440 O GLU A 333 5494 5744 5958 684 230 1120 O ATOM 2441 CB GLU A 333 17.724 27.770 13.347 1.00 43.34 C ANISOU 2441 CB GLU A 333 5182 5538 5747 669 259 1159 C ATOM 2442 CG GLU A 333 17.086 26.425 13.008 1.00 47.51 C ANISOU 2442 CG GLU A 333 5688 6064 6300 626 221 1198 C ATOM 2443 CD GLU A 333 16.622 26.266 11.548 1.00 49.98 C ANISOU 2443 CD GLU A 333 5971 6381 6638 603 208 1197 C ATOM 2444 OE1 GLU A 333 16.285 25.107 11.196 1.00 51.47 O ANISOU 2444 OE1 GLU A 333 6150 6558 6847 561 171 1219 O ATOM 2445 OE2 GLU A 333 16.604 27.249 10.745 1.00 47.20 O ANISOU 2445 OE2 GLU A 333 5610 6039 6285 625 232 1175 O ATOM 2446 N PHE A 334 17.701 26.170 16.277 1.00 44.65 N ANISOU 2446 N PHE A 334 5377 5706 5879 655 238 1225 N ATOM 2447 CA PHE A 334 18.263 25.030 16.982 1.00 45.17 C ANISOU 2447 CA PHE A 334 5467 5745 5949 639 199 1230 C ATOM 2448 C PHE A 334 17.838 23.783 16.233 1.00 45.52 C ANISOU 2448 C PHE A 334 5502 5768 6024 595 158 1254 C ATOM 2449 O PHE A 334 16.667 23.649 15.853 1.00 49.03 O ANISOU 2449 O PHE A 334 5914 6240 6472 569 168 1299 O ATOM 2450 CB PHE A 334 17.806 24.974 18.428 1.00 46.26 C ANISOU 2450 CB PHE A 334 5611 5910 6056 646 220 1273 C ATOM 2451 CG PHE A 334 18.463 23.878 19.218 1.00 48.12 C ANISOU 2451 CG PHE A 334 5876 6117 6290 635 182 1277 C ATOM 2452 CD1 PHE A 334 17.973 22.580 19.170 1.00 49.32 C ANISOU 2452 CD1 PHE A 334 6029 6250 6457 596 148 1319 C ATOM 2453 CD2 PHE A 334 19.591 24.128 19.977 1.00 53.36 C ANISOU 2453 CD2 PHE A 334 6569 6769 6934 664 179 1239 C ATOM 2454 CE1 PHE A 334 18.589 21.557 19.862 1.00 51.03 C ANISOU 2454 CE1 PHE A 334 6283 6435 6672 591 113 1324 C ATOM 2455 CE2 PHE A 334 20.214 23.104 20.689 1.00 50.63 C ANISOU 2455 CE2 PHE A 334 6251 6400 6585 661 143 1245 C ATOM 2456 CZ PHE A 334 19.715 21.820 20.621 1.00 50.88 C ANISOU 2456 CZ PHE A 334 6289 6408 6633 627 111 1288 C ATOM 2457 N TYR A 335 18.791 22.888 15.992 1.00 44.80 N ANISOU 2457 N TYR A 335 5440 5630 5951 587 113 1224 N ATOM 2458 CA TYR A 335 18.523 21.681 15.216 1.00 45.83 C ANISOU 2458 CA TYR A 335 5574 5729 6109 546 71 1239 C ATOM 2459 C TYR A 335 19.530 20.629 15.586 1.00 45.00 C ANISOU 2459 C TYR A 335 5515 5575 6008 551 27 1220 C ATOM 2460 O TYR A 335 20.372 20.885 16.431 1.00 48.07 O ANISOU 2460 O TYR A 335 5922 5964 6377 585 31 1198 O ATOM 2461 CB TYR A 335 18.529 21.987 13.697 1.00 46.70 C ANISOU 2461 CB TYR A 335 5664 5834 6245 539 65 1206 C ATOM 2462 CG TYR A 335 19.795 22.587 13.083 1.00 45.01 C ANISOU 2462 CG TYR A 335 5461 5603 6037 572 60 1136 C ATOM 2463 CD1 TYR A 335 20.112 23.929 13.259 1.00 48.31 C ANISOU 2463 CD1 TYR A 335 5871 6047 6436 605 99 1108 C ATOM 2464 CD2 TYR A 335 20.636 21.836 12.281 1.00 47.91 C ANISOU 2464 CD2 TYR A 335 5848 5930 6426 568 17 1096 C ATOM 2465 CE1 TYR A 335 21.232 24.507 12.673 1.00 47.49 C ANISOU 2465 CE1 TYR A 335 5776 5933 6335 626 96 1046 C ATOM 2466 CE2 TYR A 335 21.783 22.395 11.688 1.00 49.67 C ANISOU 2466 CE2 TYR A 335 6073 6146 6650 596 13 1033 C ATOM 2467 CZ TYR A 335 22.079 23.740 11.881 1.00 51.09 C ANISOU 2467 CZ TYR A 335 6243 6357 6811 621 52 1008 C ATOM 2468 OH TYR A 335 23.183 24.339 11.260 1.00 49.19 O ANISOU 2468 OH TYR A 335 6004 6115 6569 639 50 947 O ATOM 2469 N SER A 336 19.466 19.453 14.968 1.00 45.86 N ANISOU 2469 N SER A 336 5643 5642 6138 519 -13 1227 N ATOM 2470 CA SER A 336 20.297 18.319 15.418 1.00 46.76 C ANISOU 2470 CA SER A 336 5808 5706 6251 527 -55 1219 C ATOM 2471 C SER A 336 20.546 17.269 14.338 1.00 47.40 C ANISOU 2471 C SER A 336 5917 5733 6358 507 -101 1201 C ATOM 2472 O SER A 336 19.865 17.212 13.303 1.00 42.98 O ANISOU 2472 O SER A 336 5338 5175 5818 471 -104 1206 O ATOM 2473 CB SER A 336 19.635 17.647 16.625 1.00 49.58 C ANISOU 2473 CB SER A 336 6184 6063 6589 504 -55 1282 C ATOM 2474 OG SER A 336 18.313 17.242 16.300 1.00 48.68 O ANISOU 2474 OG SER A 336 6052 5961 6482 446 -52 1335 O ATOM 2475 N GLY A 337 21.545 16.439 14.586 1.00 49.37 N ANISOU 2475 N GLY A 337 6215 5938 6605 534 -137 1178 N ATOM 2476 CA GLY A 337 21.823 15.290 13.743 1.00 50.37 C ANISOU 2476 CA GLY A 337 6382 6004 6749 521 -183 1164 C ATOM 2477 C GLY A 337 22.782 14.323 14.412 1.00 50.86 C ANISOU 2477 C GLY A 337 6504 6020 6798 558 -218 1155 C ATOM 2478 O GLY A 337 23.185 14.516 15.562 1.00 49.33 O ANISOU 2478 O GLY A 337 6317 5845 6581 589 -208 1165 O ATOM 2479 N VAL A 338 23.153 13.288 13.667 1.00 51.97 N ANISOU 2479 N VAL A 338 6692 6102 6951 558 -260 1137 N ATOM 2480 CA VAL A 338 23.940 12.169 14.185 1.00 53.24 C ANISOU 2480 CA VAL A 338 6922 6208 7099 594 -298 1135 C ATOM 2481 C VAL A 338 25.197 11.925 13.344 1.00 53.46 C ANISOU 2481 C VAL A 338 6967 6213 7130 651 -327 1069 C ATOM 2482 O VAL A 338 25.176 12.002 12.108 1.00 54.48 O ANISOU 2482 O VAL A 338 7082 6335 7280 639 -335 1037 O ATOM 2483 CB VAL A 338 23.093 10.888 14.191 1.00 56.07 C ANISOU 2483 CB VAL A 338 7341 6502 7461 538 -324 1186 C ATOM 2484 CG1 VAL A 338 23.900 9.687 14.679 1.00 56.16 C ANISOU 2484 CG1 VAL A 338 7435 6446 7455 580 -364 1185 C ATOM 2485 CG2 VAL A 338 21.849 11.094 15.042 1.00 56.59 C ANISOU 2485 CG2 VAL A 338 7384 6599 7517 480 -295 1254 C ATOM 2486 N VAL A 339 26.286 11.647 14.042 1.00 52.57 N ANISOU 2486 N VAL A 339 6881 6097 6993 715 -343 1050 N ATOM 2487 CA VAL A 339 27.557 11.272 13.449 1.00 52.80 C ANISOU 2487 CA VAL A 339 6931 6112 7017 780 -374 993 C ATOM 2488 C VAL A 339 27.946 9.852 13.923 1.00 55.16 C ANISOU 2488 C VAL A 339 7316 6341 7300 813 -414 1011 C ATOM 2489 O VAL A 339 27.909 9.584 15.105 1.00 53.98 O ANISOU 2489 O VAL A 339 7191 6188 7129 823 -412 1049 O ATOM 2490 CB VAL A 339 28.653 12.205 13.926 1.00 52.03 C ANISOU 2490 CB VAL A 339 6788 6083 6897 836 -358 952 C ATOM 2491 CG1 VAL A 339 30.013 11.753 13.402 1.00 53.71 C ANISOU 2491 CG1 VAL A 339 7018 6291 7097 908 -391 896 C ATOM 2492 CG2 VAL A 339 28.349 13.625 13.506 1.00 54.34 C ANISOU 2492 CG2 VAL A 339 7007 6438 7202 807 -317 933 C ATOM 2493 N THR A 340 28.322 8.976 12.992 1.00 54.16 N ANISOU 2493 N THR A 340 7239 6158 7180 834 -450 984 N ATOM 2494 CA THR A 340 28.696 7.581 13.286 1.00 56.82 C ANISOU 2494 CA THR A 340 7670 6417 7500 871 -490 998 C ATOM 2495 C THR A 340 30.220 7.513 13.399 1.00 57.10 C ANISOU 2495 C THR A 340 7708 6478 7509 974 -509 947 C ATOM 2496 O THR A 340 30.902 8.496 13.046 1.00 55.05 O ANISOU 2496 O THR A 340 7376 6291 7246 1002 -492 900 O ATOM 2497 CB THR A 340 28.257 6.675 12.120 1.00 56.07 C ANISOU 2497 CB THR A 340 7633 6245 7425 837 -518 991 C ATOM 2498 OG1 THR A 340 28.978 7.049 10.936 1.00 55.79 O ANISOU 2498 OG1 THR A 340 7563 6234 7400 873 -525 926 O ATOM 2499 CG2 THR A 340 26.751 6.844 11.813 1.00 56.23 C ANISOU 2499 CG2 THR A 340 7636 6257 7471 729 -500 1035 C ATOM 2500 N PRO A 341 30.769 6.363 13.869 1.00 57.41 N ANISOU 2500 N PRO A 341 7829 6460 7522 1031 -542 958 N ATOM 2501 CA PRO A 341 32.238 6.179 13.853 1.00 57.05 C ANISOU 2501 CA PRO A 341 7787 6442 7446 1138 -564 909 C ATOM 2502 C PRO A 341 32.843 6.284 12.459 1.00 55.87 C ANISOU 2502 C PRO A 341 7617 6302 7308 1167 -577 845 C ATOM 2503 O PRO A 341 33.903 6.866 12.280 1.00 60.38 O ANISOU 2503 O PRO A 341 8132 6946 7861 1226 -574 796 O ATOM 2504 CB PRO A 341 32.448 4.755 14.432 1.00 61.45 C ANISOU 2504 CB PRO A 341 8455 6913 7977 1186 -600 940 C ATOM 2505 CG PRO A 341 31.170 4.387 15.117 1.00 61.64 C ANISOU 2505 CG PRO A 341 8522 6885 8013 1102 -590 1012 C ATOM 2506 CD PRO A 341 30.064 5.263 14.562 1.00 59.74 C ANISOU 2506 CD PRO A 341 8215 6672 7810 1002 -559 1020 C ATOM 2507 N GLU A 342 32.135 5.772 11.468 1.00 57.96 N ANISOU 2507 N GLU A 342 7921 6501 7600 1118 -589 846 N ATOM 2508 CA GLU A 342 32.545 5.855 10.085 1.00 59.58 C ANISOU 2508 CA GLU A 342 8108 6711 7817 1135 -599 789 C ATOM 2509 C GLU A 342 32.678 7.320 9.678 1.00 61.37 C ANISOU 2509 C GLU A 342 8223 7036 8057 1111 -565 756 C ATOM 2510 O GLU A 342 33.698 7.734 9.121 1.00 59.00 O ANISOU 2510 O GLU A 342 7879 6791 7744 1166 -568 700 O ATOM 2511 CB GLU A 342 31.495 5.182 9.190 1.00 67.25 C ANISOU 2511 CB GLU A 342 9134 7597 8817 1062 -612 805 C ATOM 2512 CG GLU A 342 31.356 3.661 9.341 1.00 75.72 C ANISOU 2512 CG GLU A 342 10334 8559 9877 1077 -650 832 C ATOM 2513 CD GLU A 342 30.752 3.176 10.664 1.00 79.07 C ANISOU 2513 CD GLU A 342 10810 8944 10289 1048 -647 901 C ATOM 2514 OE1 GLU A 342 29.800 3.793 11.222 1.00 69.57 O ANISOU 2514 OE1 GLU A 342 9561 7770 9100 969 -618 945 O ATOM 2515 OE2 GLU A 342 31.247 2.127 11.144 1.00 85.91 O ANISOU 2515 OE2 GLU A 342 11768 9746 11127 1109 -676 912 O ATOM 2516 N GLY A 343 31.637 8.104 9.962 1.00 55.99 N ANISOU 2516 N GLY A 343 7497 6376 7398 1030 -531 791 N ATOM 2517 CA GLY A 343 31.657 9.528 9.638 1.00 54.32 C ANISOU 2517 CA GLY A 343 7190 6250 7198 1004 -496 765 C ATOM 2518 C GLY A 343 32.838 10.250 10.255 1.00 52.56 C ANISOU 2518 C GLY A 343 6917 6108 6943 1066 -485 732 C ATOM 2519 O GLY A 343 33.556 10.977 9.567 1.00 52.32 O ANISOU 2519 O GLY A 343 6832 6137 6910 1086 -478 681 O ATOM 2520 N ALA A 344 33.056 10.011 11.549 1.00 55.74 N ANISOU 2520 N ALA A 344 7340 6515 7320 1094 -486 763 N ATOM 2521 CA ALA A 344 34.171 10.602 12.264 1.00 56.54 C ANISOU 2521 CA ALA A 344 7399 6697 7386 1151 -479 736 C ATOM 2522 C ALA A 344 35.526 10.224 11.660 1.00 60.95 C ANISOU 2522 C ALA A 344 7956 7282 7919 1235 -508 679 C ATOM 2523 O ALA A 344 36.419 11.086 11.578 1.00 59.13 O ANISOU 2523 O ALA A 344 7659 7138 7667 1259 -496 636 O ATOM 2524 CB ALA A 344 34.108 10.245 13.730 1.00 58.09 C ANISOU 2524 CB ALA A 344 7627 6887 7558 1167 -479 782 C ATOM 2525 N ALA A 345 35.668 8.976 11.189 1.00 59.01 N ANISOU 2525 N ALA A 345 7783 6965 7672 1277 -545 677 N ATOM 2526 CA ALA A 345 36.921 8.547 10.543 1.00 59.91 C ANISOU 2526 CA ALA A 345 7899 7103 7759 1365 -573 623 C ATOM 2527 C ALA A 345 37.157 9.267 9.237 1.00 57.87 C ANISOU 2527 C ALA A 345 7581 6889 7517 1346 -564 570 C ATOM 2528 O ALA A 345 38.257 9.741 8.965 1.00 59.13 O ANISOU 2528 O ALA A 345 7685 7130 7649 1394 -564 522 O ATOM 2529 CB ALA A 345 36.938 7.034 10.308 1.00 60.41 C ANISOU 2529 CB ALA A 345 8065 7070 7817 1415 -613 634 C ATOM 2530 N ILE A 346 36.123 9.360 8.413 1.00 58.78 N ANISOU 2530 N ILE A 346 7704 6955 7674 1273 -554 581 N ATOM 2531 CA ILE A 346 36.241 10.146 7.199 1.00 58.94 C ANISOU 2531 CA ILE A 346 7664 7018 7710 1247 -541 536 C ATOM 2532 C ILE A 346 36.627 11.609 7.521 1.00 58.49 C ANISOU 2532 C ILE A 346 7516 7062 7642 1225 -505 517 C ATOM 2533 O ILE A 346 37.497 12.194 6.864 1.00 56.87 O ANISOU 2533 O ILE A 346 7258 6927 7423 1248 -502 465 O ATOM 2534 CB ILE A 346 34.931 10.151 6.405 1.00 61.56 C ANISOU 2534 CB ILE A 346 8011 7291 8087 1163 -532 558 C ATOM 2535 CG1 ILE A 346 34.591 8.721 5.943 1.00 66.13 C ANISOU 2535 CG1 ILE A 346 8683 7768 8674 1176 -569 569 C ATOM 2536 CG2 ILE A 346 35.067 11.069 5.207 1.00 54.57 C ANISOU 2536 CG2 ILE A 346 7059 6456 7216 1137 -516 513 C ATOM 2537 CD1 ILE A 346 33.164 8.543 5.465 1.00 67.45 C ANISOU 2537 CD1 ILE A 346 8875 7871 8879 1085 -563 606 C ATOM 2538 N ALA A 347 35.981 12.199 8.517 1.00 56.17 N ANISOU 2538 N ALA A 347 7209 6777 7353 1179 -478 558 N ATOM 2539 CA ALA A 347 36.294 13.586 8.895 1.00 56.99 C ANISOU 2539 CA ALA A 347 7239 6968 7444 1154 -442 542 C ATOM 2540 C ALA A 347 37.752 13.741 9.382 1.00 56.73 C ANISOU 2540 C ALA A 347 7175 7016 7362 1223 -453 503 C ATOM 2541 O ALA A 347 38.408 14.757 9.109 1.00 54.42 O ANISOU 2541 O ALA A 347 6820 6804 7053 1214 -434 463 O ATOM 2542 CB ALA A 347 35.331 14.056 9.968 1.00 54.94 C ANISOU 2542 CB ALA A 347 6982 6698 7194 1102 -413 595 C ATOM 2543 N ALA A 348 38.255 12.749 10.109 1.00 55.45 N ANISOU 2543 N ALA A 348 7057 6838 7173 1289 -481 516 N ATOM 2544 CA ALA A 348 39.631 12.815 10.612 1.00 58.62 C ANISOU 2544 CA ALA A 348 7426 7324 7522 1359 -493 483 C ATOM 2545 C ALA A 348 40.623 12.882 9.465 1.00 59.06 C ANISOU 2545 C ALA A 348 7444 7433 7562 1400 -507 422 C ATOM 2546 O ALA A 348 41.635 13.548 9.561 1.00 61.91 O ANISOU 2546 O ALA A 348 7743 7893 7885 1419 -502 385 O ATOM 2547 CB ALA A 348 39.950 11.626 11.522 1.00 60.98 C ANISOU 2547 CB ALA A 348 7785 7588 7793 1432 -524 512 C ATOM 2548 N GLN A 349 40.322 12.233 8.353 1.00 60.38 N ANISOU 2548 N GLN A 349 7645 7539 7755 1406 -525 411 N ATOM 2549 CA GLN A 349 41.244 12.219 7.237 1.00 60.53 C ANISOU 2549 CA GLN A 349 7631 7608 7758 1449 -540 354 C ATOM 2550 C GLN A 349 41.387 13.566 6.531 1.00 65.74 C ANISOU 2550 C GLN A 349 8212 8341 8423 1389 -509 318 C ATOM 2551 O GLN A 349 42.234 13.711 5.654 1.00 61.38 O ANISOU 2551 O GLN A 349 7621 7848 7852 1418 -517 269 O ATOM 2552 CB GLN A 349 40.794 11.167 6.230 1.00 68.84 C ANISOU 2552 CB GLN A 349 8747 8569 8837 1466 -565 352 C ATOM 2553 CG GLN A 349 40.955 9.747 6.752 1.00 76.30 C ANISOU 2553 CG GLN A 349 9778 9447 9765 1544 -601 375 C ATOM 2554 CD GLN A 349 40.761 8.719 5.656 1.00 86.85 C ANISOU 2554 CD GLN A 349 11180 10703 11117 1571 -629 360 C ATOM 2555 OE1 GLN A 349 41.685 7.961 5.326 1.00 93.95 O ANISOU 2555 OE1 GLN A 349 12101 11611 11982 1665 -658 329 O ATOM 2556 NE2 GLN A 349 39.560 8.703 5.061 1.00 83.95 N ANISOU 2556 NE2 GLN A 349 10840 10258 10798 1491 -621 382 N ATOM 2557 N GLN A 350 40.552 14.546 6.871 1.00 59.45 N ANISOU 2557 N GLN A 350 7395 7540 7651 1306 -473 343 N ATOM 2558 CA GLN A 350 40.664 15.857 6.261 1.00 55.48 C ANISOU 2558 CA GLN A 350 6828 7100 7152 1249 -443 313 C ATOM 2559 C GLN A 350 41.853 16.636 6.824 1.00 53.45 C ANISOU 2559 C GLN A 350 6510 6955 6841 1264 -433 280 C ATOM 2560 O GLN A 350 42.324 17.571 6.199 1.00 54.73 O ANISOU 2560 O GLN A 350 6618 7183 6991 1233 -416 243 O ATOM 2561 CB GLN A 350 39.351 16.642 6.430 1.00 58.52 C ANISOU 2561 CB GLN A 350 7217 7440 7576 1163 -407 352 C ATOM 2562 CG GLN A 350 38.104 15.862 5.992 1.00 59.68 C ANISOU 2562 CG GLN A 350 7419 7484 7770 1140 -416 390 C ATOM 2563 CD GLN A 350 38.264 15.170 4.640 1.00 65.38 C ANISOU 2563 CD GLN A 350 8156 8178 8506 1164 -442 360 C ATOM 2564 OE1 GLN A 350 38.619 15.811 3.648 1.00 63.05 O ANISOU 2564 OE1 GLN A 350 7817 7927 8211 1149 -433 321 O ATOM 2565 NE2 GLN A 350 37.967 13.863 4.585 1.00 62.27 N ANISOU 2565 NE2 GLN A 350 7828 7708 8123 1198 -474 379 N ATOM 2566 N GLY A 351 42.337 16.261 7.996 1.00 52.82 N ANISOU 2566 N GLY A 351 6440 6900 6728 1309 -445 295 N ATOM 2567 CA GLY A 351 43.522 16.872 8.572 1.00 54.24 C ANISOU 2567 CA GLY A 351 6563 7194 6851 1326 -441 264 C ATOM 2568 C GLY A 351 43.359 18.339 8.959 1.00 57.85 C ANISOU 2568 C GLY A 351 6979 7698 7302 1244 -400 260 C ATOM 2569 O GLY A 351 44.255 19.138 8.697 1.00 55.86 O ANISOU 2569 O GLY A 351 6670 7540 7014 1228 -391 218 O ATOM 2570 N ILE A 352 42.243 18.705 9.604 1.00 54.53 N ANISOU 2570 N ILE A 352 6589 7216 6912 1191 -374 304 N ATOM 2571 CA ILE A 352 42.026 20.123 9.916 1.00 52.29 C ANISOU 2571 CA ILE A 352 6277 6968 6623 1116 -333 300 C ATOM 2572 C ILE A 352 43.073 20.682 10.843 1.00 50.81 C ANISOU 2572 C ILE A 352 6051 6879 6375 1120 -329 278 C ATOM 2573 O ILE A 352 43.637 21.740 10.600 1.00 51.72 O ANISOU 2573 O ILE A 352 6124 7064 6464 1076 -309 242 O ATOM 2574 CB ILE A 352 40.630 20.429 10.489 1.00 51.70 C ANISOU 2574 CB ILE A 352 6241 6816 6587 1066 -305 352 C ATOM 2575 CG1 ILE A 352 39.542 20.188 9.423 1.00 48.56 C ANISOU 2575 CG1 ILE A 352 5867 6336 6245 1041 -301 370 C ATOM 2576 CG2 ILE A 352 40.579 21.890 10.924 1.00 50.00 C ANISOU 2576 CG2 ILE A 352 6000 6643 6353 1002 -263 343 C ATOM 2577 CD1 ILE A 352 38.167 19.901 9.981 1.00 51.00 C ANISOU 2577 CD1 ILE A 352 6221 6565 6591 1017 -289 430 C ATOM 2578 N SER A 353 43.351 19.941 11.891 1.00 55.70 N ANISOU 2578 N SER A 353 6687 7504 6970 1173 -349 299 N ATOM 2579 CA SER A 353 44.345 20.335 12.881 1.00 57.77 C ANISOU 2579 CA SER A 353 6914 7864 7170 1183 -349 281 C ATOM 2580 C SER A 353 45.702 20.671 12.274 1.00 57.92 C ANISOU 2580 C SER A 353 6869 7996 7141 1196 -361 223 C ATOM 2581 O SER A 353 46.283 21.720 12.546 1.00 60.05 O ANISOU 2581 O SER A 353 7097 8347 7370 1147 -341 195 O ATOM 2582 CB SER A 353 44.514 19.218 13.880 1.00 59.30 C ANISOU 2582 CB SER A 353 7137 8046 7346 1257 -378 313 C ATOM 2583 OG SER A 353 45.070 19.749 15.041 1.00 63.49 O ANISOU 2583 OG SER A 353 7644 8652 7827 1247 -369 310 O ATOM 2584 N ALA A 354 46.184 19.780 11.426 1.00 58.45 N ANISOU 2584 N ALA A 354 6931 8068 7209 1261 -392 205 N ATOM 2585 CA ALA A 354 47.453 19.967 10.768 1.00 58.44 C ANISOU 2585 CA ALA A 354 6867 8177 7161 1282 -405 151 C ATOM 2586 C ALA A 354 47.387 21.144 9.816 1.00 55.30 C ANISOU 2586 C ALA A 354 6436 7800 6773 1198 -376 120 C ATOM 2587 O ALA A 354 48.347 21.915 9.720 1.00 56.89 O ANISOU 2587 O ALA A 354 6580 8110 6925 1169 -369 80 O ATOM 2588 CB ALA A 354 47.867 18.686 10.022 1.00 59.41 C ANISOU 2588 CB ALA A 354 6999 8286 7284 1377 -445 141 C ATOM 2589 N GLN A 355 46.268 21.310 9.109 1.00 53.82 N ANISOU 2589 N GLN A 355 6286 7515 6647 1157 -358 138 N ATOM 2590 CA GLN A 355 46.110 22.482 8.246 1.00 53.07 C ANISOU 2590 CA GLN A 355 6168 7433 6563 1077 -328 114 C ATOM 2591 C GLN A 355 46.298 23.775 9.078 1.00 51.29 C ANISOU 2591 C GLN A 355 5925 7259 6302 1003 -294 107 C ATOM 2592 O GLN A 355 47.053 24.687 8.710 1.00 52.62 O ANISOU 2592 O GLN A 355 6049 7509 6432 955 -281 67 O ATOM 2593 CB GLN A 355 44.747 22.476 7.534 1.00 55.52 C ANISOU 2593 CB GLN A 355 6524 7627 6943 1045 -312 143 C ATOM 2594 CG GLN A 355 44.504 23.687 6.651 1.00 55.45 C ANISOU 2594 CG GLN A 355 6498 7625 6946 968 -279 123 C ATOM 2595 CD GLN A 355 43.014 23.972 6.348 1.00 60.23 C ANISOU 2595 CD GLN A 355 7147 8123 7612 925 -253 162 C ATOM 2596 OE1 GLN A 355 42.163 23.070 6.284 1.00 58.74 O ANISOU 2596 OE1 GLN A 355 6997 7854 7466 955 -267 197 O ATOM 2597 NE2 GLN A 355 42.702 25.244 6.179 1.00 55.11 N ANISOU 2597 NE2 GLN A 355 6496 7478 6963 854 -215 157 N ATOM 2598 N LEU A 356 45.659 23.822 10.228 1.00 50.30 N ANISOU 2598 N LEU A 356 5835 7090 6184 995 -282 145 N ATOM 2599 CA LEU A 356 45.674 25.050 11.037 1.00 53.72 C ANISOU 2599 CA LEU A 356 6266 7556 6588 924 -247 142 C ATOM 2600 C LEU A 356 47.053 25.320 11.656 1.00 56.68 C ANISOU 2600 C LEU A 356 6589 8059 6886 926 -259 105 C ATOM 2601 O LEU A 356 47.482 26.481 11.749 1.00 55.06 O ANISOU 2601 O LEU A 356 6363 7912 6644 854 -234 77 O ATOM 2602 CB LEU A 356 44.602 24.969 12.113 1.00 51.25 C ANISOU 2602 CB LEU A 356 6005 7166 6302 920 -232 193 C ATOM 2603 CG LEU A 356 43.154 24.958 11.597 1.00 50.48 C ANISOU 2603 CG LEU A 356 5953 6954 6273 900 -213 231 C ATOM 2604 CD1 LEU A 356 42.185 24.723 12.732 1.00 48.69 C ANISOU 2604 CD1 LEU A 356 5770 6664 6065 905 -202 283 C ATOM 2605 CD2 LEU A 356 42.791 26.253 10.893 1.00 51.83 C ANISOU 2605 CD2 LEU A 356 6123 7115 6453 825 -174 214 C ATOM 2606 N ALA A 357 47.748 24.249 12.051 1.00 55.33 N ANISOU 2606 N ALA A 357 6399 7933 6688 1007 -296 106 N ATOM 2607 CA ALA A 357 49.114 24.358 12.578 1.00 55.17 C ANISOU 2607 CA ALA A 357 6321 8049 6591 1021 -312 72 C ATOM 2608 C ALA A 357 50.121 24.805 11.535 1.00 54.49 C ANISOU 2608 C ALA A 357 6173 8060 6469 999 -316 19 C ATOM 2609 O ALA A 357 51.116 25.375 11.895 1.00 59.07 O ANISOU 2609 O ALA A 357 6704 8756 6984 969 -316 -11 O ATOM 2610 CB ALA A 357 49.572 23.028 13.199 1.00 55.12 C ANISOU 2610 CB ALA A 357 6313 8065 6565 1127 -353 89 C ATOM 2611 N ASP A 358 49.889 24.531 10.256 1.00 55.21 N ANISOU 2611 N ASP A 358 6265 8111 6599 1012 -321 9 N ATOM 2612 CA ASP A 358 50.850 24.901 9.218 1.00 58.86 C ANISOU 2612 CA ASP A 358 6668 8670 7027 994 -326 -39 C ATOM 2613 C ASP A 358 50.712 26.341 8.725 1.00 59.93 C ANISOU 2613 C ASP A 358 6798 8813 7159 881 -287 -60 C ATOM 2614 O ASP A 358 51.432 26.740 7.818 1.00 63.87 O ANISOU 2614 O ASP A 358 7251 9386 7631 853 -287 -99 O ATOM 2615 CB ASP A 358 50.747 23.925 8.011 1.00 63.12 C ANISOU 2615 CB ASP A 358 7209 9170 7603 1063 -350 -43 C ATOM 2616 CG ASP A 358 51.934 24.057 7.007 1.00 68.82 C ANISOU 2616 CG ASP A 358 7858 10012 8276 1069 -363 -95 C ATOM 2617 OD1 ASP A 358 53.101 24.287 7.416 1.00 72.19 O ANISOU 2617 OD1 ASP A 358 8223 10574 8630 1070 -372 -124 O ATOM 2618 OD2 ASP A 358 51.698 23.935 5.793 1.00 74.51 O ANISOU 2618 OD2 ASP A 358 8580 10698 9029 1072 -364 -107 O ATOM 2619 N ARG A 359 49.787 27.122 9.277 1.00 57.96 N ANISOU 2619 N ARG A 359 6599 8485 6935 817 -253 -35 N ATOM 2620 CA ARG A 359 49.598 28.502 8.812 1.00 54.75 C ANISOU 2620 CA ARG A 359 6202 8074 6527 714 -214 -52 C ATOM 2621 C ARG A 359 50.764 29.344 9.237 1.00 53.20 C ANISOU 2621 C ARG A 359 5959 8004 6249 653 -208 -92 C ATOM 2622 O ARG A 359 51.374 29.059 10.232 1.00 54.29 O ANISOU 2622 O ARG A 359 6074 8211 6342 677 -224 -93 O ATOM 2623 CB ARG A 359 48.294 29.103 9.376 1.00 52.39 C ANISOU 2623 CB ARG A 359 5974 7660 6271 671 -179 -13 C ATOM 2624 CG ARG A 359 47.040 28.470 8.774 1.00 50.38 C ANISOU 2624 CG ARG A 359 5762 7282 6096 710 -179 24 C ATOM 2625 CD ARG A 359 45.794 28.945 9.497 1.00 48.43 C ANISOU 2625 CD ARG A 359 5578 6939 5884 681 -147 66 C ATOM 2626 NE ARG A 359 45.898 28.708 10.937 1.00 47.98 N ANISOU 2626 NE ARG A 359 5530 6898 5800 701 -152 84 N ATOM 2627 CZ ARG A 359 45.088 29.224 11.857 1.00 50.61 C ANISOU 2627 CZ ARG A 359 5909 7177 6141 673 -123 114 C ATOM 2628 NH1 ARG A 359 44.066 30.052 11.528 1.00 49.86 N ANISOU 2628 NH1 ARG A 359 5856 7005 6081 627 -86 131 N ATOM 2629 NH2 ARG A 359 45.314 28.938 13.127 1.00 50.44 N ANISOU 2629 NH2 ARG A 359 5890 7183 6090 695 -132 127 N ATOM 2630 N TYR A 360 51.057 30.403 8.504 1.00 53.92 N ANISOU 2630 N TYR A 360 6038 8127 6320 569 -185 -122 N ATOM 2631 CA TYR A 360 52.155 31.310 8.879 1.00 55.53 C ANISOU 2631 CA TYR A 360 6201 8453 6441 492 -176 -161 C ATOM 2632 C TYR A 360 51.776 32.131 10.083 1.00 56.71 C ANISOU 2632 C TYR A 360 6400 8572 6573 432 -148 -148 C ATOM 2633 O TYR A 360 50.656 32.610 10.168 1.00 57.12 O ANISOU 2633 O TYR A 360 6521 8508 6673 406 -118 -120 O ATOM 2634 CB TYR A 360 52.422 32.247 7.723 1.00 59.61 C ANISOU 2634 CB TYR A 360 6707 8993 6946 411 -155 -192 C ATOM 2635 CG TYR A 360 53.579 33.212 7.885 1.00 63.52 C ANISOU 2635 CG TYR A 360 7161 9618 7356 319 -147 -235 C ATOM 2636 CD1 TYR A 360 53.387 34.462 8.454 1.00 62.55 C ANISOU 2636 CD1 TYR A 360 7087 9472 7206 216 -110 -239 C ATOM 2637 CD2 TYR A 360 54.839 32.895 7.408 1.00 64.16 C ANISOU 2637 CD2 TYR A 360 7155 9842 7379 331 -173 -271 C ATOM 2638 CE1 TYR A 360 54.425 35.353 8.577 1.00 66.34 C ANISOU 2638 CE1 TYR A 360 7534 10066 7604 121 -102 -279 C ATOM 2639 CE2 TYR A 360 55.892 33.785 7.534 1.00 66.04 C ANISOU 2639 CE2 TYR A 360 7351 10206 7534 237 -165 -310 C ATOM 2640 CZ TYR A 360 55.669 35.006 8.116 1.00 65.99 C ANISOU 2640 CZ TYR A 360 7398 10169 7503 129 -130 -313 C ATOM 2641 OH TYR A 360 56.683 35.899 8.220 1.00 68.26 O ANISOU 2641 OH TYR A 360 7652 10576 7707 26 -122 -351 O ATOM 2642 N SER A 361 52.705 32.308 11.012 1.00 59.07 N ANISOU 2642 N SER A 361 6663 8980 6801 411 -158 -167 N ATOM 2643 CA SER A 361 52.422 33.021 12.247 1.00 60.45 C ANISOU 2643 CA SER A 361 6882 9133 6951 358 -134 -158 C ATOM 2644 C SER A 361 52.943 34.442 12.151 1.00 61.37 C ANISOU 2644 C SER A 361 7007 9301 7010 232 -104 -195 C ATOM 2645 O SER A 361 54.146 34.665 12.109 1.00 62.59 O ANISOU 2645 O SER A 361 7098 9591 7093 192 -118 -233 O ATOM 2646 CB SER A 361 53.058 32.328 13.449 1.00 60.89 C ANISOU 2646 CB SER A 361 6901 9271 6960 411 -163 -153 C ATOM 2647 OG SER A 361 52.574 32.926 14.661 1.00 65.29 O ANISOU 2647 OG SER A 361 7512 9788 7506 369 -139 -137 O ATOM 2648 N LEU A 362 52.020 35.392 12.142 1.00 58.07 N ANISOU 2648 N LEU A 362 6666 8774 6620 172 -63 -182 N ATOM 2649 CA LEU A 362 52.339 36.789 11.950 1.00 59.39 C ANISOU 2649 CA LEU A 362 6863 8962 6741 51 -30 -213 C ATOM 2650 C LEU A 362 52.953 37.462 13.167 1.00 60.25 C ANISOU 2650 C LEU A 362 6978 9140 6772 -17 -22 -234 C ATOM 2651 O LEU A 362 52.512 37.259 14.301 1.00 58.91 O ANISOU 2651 O LEU A 362 6839 8935 6607 12 -20 -210 O ATOM 2652 CB LEU A 362 51.067 37.560 11.590 1.00 58.96 C ANISOU 2652 CB LEU A 362 6900 8758 6741 21 11 -189 C ATOM 2653 CG LEU A 362 50.453 37.245 10.223 1.00 58.47 C ANISOU 2653 CG LEU A 362 6840 8628 6747 58 12 -175 C ATOM 2654 CD1 LEU A 362 49.032 37.790 10.145 1.00 57.17 C ANISOU 2654 CD1 LEU A 362 6764 8315 6641 55 50 -139 C ATOM 2655 CD2 LEU A 362 51.312 37.801 9.102 1.00 57.97 C ANISOU 2655 CD2 LEU A 362 6739 8638 6646 -8 13 -215 C ATOM 2656 N SER A 363 53.947 38.303 12.921 1.00 61.94 N ANISOU 2656 N SER A 363 7167 9452 6913 -117 -16 -277 N ATOM 2657 CA SER A 363 54.404 39.215 13.958 1.00 65.29 C ANISOU 2657 CA SER A 363 7618 9923 7263 -210 0 -300 C ATOM 2658 C SER A 363 53.457 40.393 13.983 1.00 69.24 C ANISOU 2658 C SER A 363 8231 10292 7784 -279 49 -291 C ATOM 2659 O SER A 363 52.689 40.636 13.031 1.00 64.97 O ANISOU 2659 O SER A 363 7734 9651 7300 -273 69 -276 O ATOM 2660 CB SER A 363 55.796 39.728 13.661 1.00 64.63 C ANISOU 2660 CB SER A 363 7471 9995 7090 -302 -10 -349 C ATOM 2661 OG SER A 363 55.774 40.578 12.533 1.00 67.78 O ANISOU 2661 OG SER A 363 7898 10363 7490 -381 14 -367 O ATOM 2662 N MET A 364 53.530 41.143 15.064 1.00 66.17 N ANISOU 2662 N MET A 364 7892 9906 7344 -345 68 -302 N ATOM 2663 CA MET A 364 52.702 42.326 15.201 1.00 70.12 C ANISOU 2663 CA MET A 364 8506 10285 7850 -411 117 -297 C ATOM 2664 C MET A 364 52.969 43.374 14.118 1.00 71.53 C ANISOU 2664 C MET A 364 8718 10453 8006 -511 142 -325 C ATOM 2665 O MET A 364 52.051 44.033 13.622 1.00 73.38 O ANISOU 2665 O MET A 364 9036 10562 8280 -524 177 -309 O ATOM 2666 CB MET A 364 52.932 42.931 16.574 1.00 75.62 C ANISOU 2666 CB MET A 364 9244 11005 8481 -469 129 -312 C ATOM 2667 CG MET A 364 51.772 43.762 17.036 1.00 76.91 C ANISOU 2667 CG MET A 364 9528 11023 8669 -484 175 -292 C ATOM 2668 SD MET A 364 50.231 42.835 17.110 1.00 81.08 S ANISOU 2668 SD MET A 364 10080 11418 9306 -341 179 -227 S ATOM 2669 CE MET A 364 49.138 44.244 16.962 1.00 75.43 C ANISOU 2669 CE MET A 364 9504 10551 8603 -395 241 -219 C ATOM 2670 N GLU A 365 54.231 43.509 13.742 1.00 71.10 N ANISOU 2670 N GLU A 365 8593 10535 7884 -581 122 -365 N ATOM 2671 CA GLU A 365 54.635 44.427 12.694 1.00 74.57 C ANISOU 2671 CA GLU A 365 9053 10985 8294 -682 141 -393 C ATOM 2672 C GLU A 365 54.043 44.031 11.320 1.00 74.61 C ANISOU 2672 C GLU A 365 9047 10922 8376 -620 142 -371 C ATOM 2673 O GLU A 365 53.509 44.877 10.582 1.00 67.24 O ANISOU 2673 O GLU A 365 8189 9896 7461 -668 176 -368 O ATOM 2674 CB GLU A 365 56.161 44.448 12.639 1.00 81.02 C ANISOU 2674 CB GLU A 365 9777 11986 9021 -757 114 -437 C ATOM 2675 CG GLU A 365 56.762 45.346 11.577 1.00 89.78 C ANISOU 2675 CG GLU A 365 10892 13132 10086 -872 129 -469 C ATOM 2676 CD GLU A 365 58.285 45.404 11.658 1.00100.27 C ANISOU 2676 CD GLU A 365 12124 14656 11315 -956 103 -512 C ATOM 2677 OE1 GLU A 365 58.839 45.109 12.739 1.00105.70 O ANISOU 2677 OE1 GLU A 365 12770 15436 11952 -954 83 -523 O ATOM 2678 OE2 GLU A 365 58.934 45.751 10.644 1.00103.68 O ANISOU 2678 OE2 GLU A 365 12522 15156 11716 -1024 103 -535 O ATOM 2679 N GLU A 366 54.159 42.750 10.973 1.00 67.29 N ANISOU 2679 N GLU A 366 8031 10042 7491 -514 104 -357 N ATOM 2680 CA GLU A 366 53.550 42.240 9.748 1.00 64.64 C ANISOU 2680 CA GLU A 366 7685 9643 7232 -446 100 -335 C ATOM 2681 C GLU A 366 52.046 42.477 9.741 1.00 62.00 C ANISOU 2681 C GLU A 366 7447 9137 6973 -404 133 -293 C ATOM 2682 O GLU A 366 51.473 42.881 8.726 1.00 57.71 O ANISOU 2682 O GLU A 366 6942 8515 6467 -413 154 -284 O ATOM 2683 CB GLU A 366 53.843 40.762 9.580 1.00 65.99 C ANISOU 2683 CB GLU A 366 7757 9881 7433 -331 54 -325 C ATOM 2684 CG GLU A 366 55.305 40.462 9.290 1.00 67.09 C ANISOU 2684 CG GLU A 366 7790 10196 7502 -357 21 -364 C ATOM 2685 CD GLU A 366 55.624 38.985 9.388 1.00 66.82 C ANISOU 2685 CD GLU A 366 7669 10230 7488 -233 -24 -353 C ATOM 2686 OE1 GLU A 366 55.309 38.351 10.413 1.00 67.62 O ANISOU 2686 OE1 GLU A 366 7775 10310 7604 -164 -36 -331 O ATOM 2687 OE2 GLU A 366 56.191 38.463 8.428 1.00 64.86 O ANISOU 2687 OE2 GLU A 366 7351 10054 7239 -202 -46 -368 O ATOM 2688 N TYR A 367 51.424 42.281 10.898 1.00 60.54 N ANISOU 2688 N TYR A 367 7300 8898 6804 -360 138 -269 N ATOM 2689 CA TYR A 367 49.989 42.416 11.014 1.00 58.47 C ANISOU 2689 CA TYR A 367 7120 8486 6609 -311 167 -227 C ATOM 2690 C TYR A 367 49.517 43.848 10.801 1.00 61.13 C ANISOU 2690 C TYR A 367 7563 8736 6929 -396 217 -233 C ATOM 2691 O TYR A 367 48.500 44.080 10.136 1.00 56.44 O ANISOU 2691 O TYR A 367 7021 8033 6390 -367 241 -205 O ATOM 2692 CB TYR A 367 49.538 41.884 12.355 1.00 55.03 C ANISOU 2692 CB TYR A 367 6694 8029 6183 -251 161 -202 C ATOM 2693 CG TYR A 367 48.105 42.171 12.721 1.00 59.07 C ANISOU 2693 CG TYR A 367 7295 8401 6749 -212 195 -161 C ATOM 2694 CD1 TYR A 367 47.053 41.425 12.179 1.00 59.95 C ANISOU 2694 CD1 TYR A 367 7403 8432 6943 -121 191 -118 C ATOM 2695 CD2 TYR A 367 47.788 43.170 13.643 1.00 61.23 C ANISOU 2695 CD2 TYR A 367 7654 8626 6985 -264 231 -164 C ATOM 2696 CE1 TYR A 367 45.732 41.681 12.539 1.00 60.83 C ANISOU 2696 CE1 TYR A 367 7588 8427 7098 -85 223 -78 C ATOM 2697 CE2 TYR A 367 46.478 43.425 14.008 1.00 59.95 C ANISOU 2697 CE2 TYR A 367 7568 8344 6866 -221 263 -125 C ATOM 2698 CZ TYR A 367 45.454 42.677 13.463 1.00 63.15 C ANISOU 2698 CZ TYR A 367 7962 8679 7352 -131 259 -82 C ATOM 2699 OH TYR A 367 44.151 42.941 13.836 1.00 65.73 O ANISOU 2699 OH TYR A 367 8358 8898 7716 -89 292 -42 O ATOM 2700 N GLU A 368 50.234 44.817 11.349 1.00 63.90 N ANISOU 2700 N GLU A 368 7948 9130 7199 -501 233 -268 N ATOM 2701 CA GLU A 368 49.821 46.202 11.129 1.00 68.50 C ANISOU 2701 CA GLU A 368 8643 9623 7760 -583 281 -274 C ATOM 2702 C GLU A 368 50.022 46.623 9.677 1.00 65.82 C ANISOU 2702 C GLU A 368 8302 9280 7426 -627 289 -285 C ATOM 2703 O GLU A 368 49.215 47.371 9.141 1.00 66.49 O ANISOU 2703 O GLU A 368 8472 9255 7535 -638 325 -269 O ATOM 2704 CB GLU A 368 50.525 47.154 12.084 1.00 72.94 C ANISOU 2704 CB GLU A 368 9254 10227 8231 -692 297 -310 C ATOM 2705 CG GLU A 368 49.839 47.213 13.441 1.00 79.53 C ANISOU 2705 CG GLU A 368 10148 11001 9069 -655 312 -291 C ATOM 2706 CD GLU A 368 50.817 47.433 14.572 1.00 91.92 C ANISOU 2706 CD GLU A 368 11702 12670 10553 -726 300 -327 C ATOM 2707 OE1 GLU A 368 50.356 47.574 15.719 1.00100.76 O ANISOU 2707 OE1 GLU A 368 12872 13747 11662 -709 314 -316 O ATOM 2708 OE2 GLU A 368 52.050 47.467 14.324 1.00103.88 O ANISOU 2708 OE2 GLU A 368 13151 14312 12007 -801 277 -365 O ATOM 2709 N GLN A 369 51.071 46.133 9.028 1.00 62.79 N ANISOU 2709 N GLN A 369 7821 9018 7019 -647 255 -311 N ATOM 2710 CA GLN A 369 51.248 46.416 7.608 1.00 65.72 C ANISOU 2710 CA GLN A 369 8180 9390 7398 -680 260 -319 C ATOM 2711 C GLN A 369 50.121 45.793 6.773 1.00 60.85 C ANISOU 2711 C GLN A 369 7565 8679 6877 -575 261 -277 C ATOM 2712 O GLN A 369 49.620 46.388 5.828 1.00 58.78 O ANISOU 2712 O GLN A 369 7353 8343 6636 -594 286 -268 O ATOM 2713 CB GLN A 369 52.595 45.903 7.109 1.00 75.10 C ANISOU 2713 CB GLN A 369 9253 10739 8542 -711 222 -354 C ATOM 2714 CG GLN A 369 53.811 46.603 7.715 1.00 84.16 C ANISOU 2714 CG GLN A 369 10390 11999 9586 -833 221 -399 C ATOM 2715 CD GLN A 369 55.110 45.881 7.374 1.00 97.62 C ANISOU 2715 CD GLN A 369 11963 13880 11247 -839 178 -428 C ATOM 2716 OE1 GLN A 369 55.225 45.227 6.324 1.00100.73 O ANISOU 2716 OE1 GLN A 369 12290 14306 11676 -786 159 -424 O ATOM 2717 NE2 GLN A 369 56.096 45.996 8.257 1.00104.65 N ANISOU 2717 NE2 GLN A 369 12814 14890 12058 -900 164 -458 N ATOM 2718 N LEU A 370 49.731 44.586 7.130 1.00 57.53 N ANISOU 2718 N LEU A 370 7088 8260 6510 -466 232 -252 N ATOM 2719 CA LEU A 370 48.604 43.926 6.488 1.00 60.39 C ANISOU 2719 CA LEU A 370 7451 8532 6959 -368 231 -211 C ATOM 2720 C LEU A 370 47.329 44.773 6.548 1.00 57.17 C ANISOU 2720 C LEU A 370 7155 7983 6583 -365 277 -179 C ATOM 2721 O LEU A 370 46.678 44.999 5.538 1.00 58.62 O ANISOU 2721 O LEU A 370 7364 8100 6806 -350 293 -161 O ATOM 2722 CB LEU A 370 48.407 42.590 7.162 1.00 61.14 C ANISOU 2722 CB LEU A 370 7487 8648 7094 -265 195 -190 C ATOM 2723 CG LEU A 370 47.607 41.567 6.414 1.00 64.18 C ANISOU 2723 CG LEU A 370 7840 8983 7561 -166 177 -156 C ATOM 2724 CD1 LEU A 370 48.052 40.193 6.901 1.00 63.23 C ANISOU 2724 CD1 LEU A 370 7638 8934 7451 -88 131 -154 C ATOM 2725 CD2 LEU A 370 46.117 41.822 6.623 1.00 69.30 C ANISOU 2725 CD2 LEU A 370 8568 9497 8265 -124 209 -110 C ATOM 2726 N LEU A 371 47.020 45.300 7.719 1.00 57.25 N ANISOU 2726 N LEU A 371 7231 7952 6568 -382 300 -174 N ATOM 2727 CA LEU A 371 45.877 46.190 7.873 1.00 57.90 C ANISOU 2727 CA LEU A 371 7423 7907 6667 -379 347 -147 C ATOM 2728 C LEU A 371 46.034 47.390 6.952 1.00 58.74 C ANISOU 2728 C LEU A 371 7595 7980 6742 -463 379 -165 C ATOM 2729 O LEU A 371 45.140 47.703 6.175 1.00 61.43 O ANISOU 2729 O LEU A 371 7982 8234 7124 -433 402 -137 O ATOM 2730 CB LEU A 371 45.739 46.655 9.324 1.00 58.71 C ANISOU 2730 CB LEU A 371 7587 7988 6732 -397 366 -149 C ATOM 2731 CG LEU A 371 45.413 45.605 10.396 1.00 65.07 C ANISOU 2731 CG LEU A 371 8348 8808 7566 -313 342 -125 C ATOM 2732 CD1 LEU A 371 45.114 46.271 11.726 1.00 65.39 C ANISOU 2732 CD1 LEU A 371 8467 8809 7567 -334 370 -125 C ATOM 2733 CD2 LEU A 371 44.249 44.706 10.010 1.00 63.76 C ANISOU 2733 CD2 LEU A 371 8159 8578 7487 -204 334 -76 C ATOM 2734 N TYR A 372 47.191 48.041 7.017 1.00 55.58 N ANISOU 2734 N TYR A 372 7198 7654 6266 -571 379 -209 N ATOM 2735 CA TYR A 372 47.473 49.170 6.135 1.00 56.79 C ANISOU 2735 CA TYR A 372 7413 7783 6380 -663 407 -228 C ATOM 2736 C TYR A 372 47.294 48.787 4.657 1.00 56.86 C ANISOU 2736 C TYR A 372 7375 7790 6437 -629 396 -215 C ATOM 2737 O TYR A 372 46.740 49.551 3.880 1.00 57.38 O ANISOU 2737 O TYR A 372 7512 7776 6512 -646 428 -201 O ATOM 2738 CB TYR A 372 48.888 49.683 6.414 1.00 61.19 C ANISOU 2738 CB TYR A 372 7954 8448 6846 -786 398 -279 C ATOM 2739 CG TYR A 372 49.343 50.834 5.552 1.00 63.32 C ANISOU 2739 CG TYR A 372 8285 8708 7065 -899 425 -302 C ATOM 2740 CD1 TYR A 372 49.188 52.159 5.967 1.00 65.87 C ANISOU 2740 CD1 TYR A 372 8740 8951 7335 -982 468 -312 C ATOM 2741 CD2 TYR A 372 49.975 50.600 4.332 1.00 66.36 C ANISOU 2741 CD2 TYR A 372 8599 9164 7450 -925 406 -315 C ATOM 2742 CE1 TYR A 372 49.630 53.219 5.172 1.00 66.20 C ANISOU 2742 CE1 TYR A 372 8846 8980 7326 -1091 493 -332 C ATOM 2743 CE2 TYR A 372 50.410 51.649 3.534 1.00 66.88 C ANISOU 2743 CE2 TYR A 372 8721 9223 7466 -1033 430 -334 C ATOM 2744 CZ TYR A 372 50.229 52.948 3.957 1.00 68.21 C ANISOU 2744 CZ TYR A 372 9024 9307 7583 -1117 473 -341 C ATOM 2745 OH TYR A 372 50.673 53.959 3.157 1.00 74.03 O ANISOU 2745 OH TYR A 372 9823 10036 8270 -1226 496 -359 O ATOM 2746 N HIS A 373 47.714 47.592 4.259 1.00 58.96 N ANISOU 2746 N HIS A 373 7524 8142 6734 -576 352 -217 N ATOM 2747 CA HIS A 373 47.629 47.223 2.839 1.00 62.43 C ANISOU 2747 CA HIS A 373 7918 8588 7215 -549 341 -210 C ATOM 2748 C HIS A 373 46.227 46.872 2.356 1.00 63.02 C ANISOU 2748 C HIS A 373 8017 8555 7371 -451 352 -162 C ATOM 2749 O HIS A 373 45.962 46.936 1.166 1.00 60.08 O ANISOU 2749 O HIS A 373 7640 8160 7025 -443 356 -152 O ATOM 2750 CB HIS A 373 48.671 46.158 2.479 1.00 63.45 C ANISOU 2750 CB HIS A 373 7920 8851 7337 -533 292 -235 C ATOM 2751 CG HIS A 373 50.053 46.718 2.448 1.00 66.06 C ANISOU 2751 CG HIS A 373 8223 9294 7581 -646 287 -282 C ATOM 2752 ND1 HIS A 373 50.448 47.633 1.499 1.00 72.65 N ANISOU 2752 ND1 HIS A 373 9088 10135 8378 -736 307 -299 N ATOM 2753 CD2 HIS A 373 51.105 46.583 3.295 1.00 70.60 C ANISOU 2753 CD2 HIS A 373 8750 9980 8094 -690 266 -314 C ATOM 2754 CE1 HIS A 373 51.691 48.019 1.745 1.00 69.45 C ANISOU 2754 CE1 HIS A 373 8652 9842 7891 -836 299 -341 C ATOM 2755 NE2 HIS A 373 52.118 47.388 2.822 1.00 69.20 N ANISOU 2755 NE2 HIS A 373 8570 9880 7843 -809 274 -350 N ATOM 2756 N SER A 374 45.315 46.600 3.276 1.00 61.04 N ANISOU 2756 N SER A 374 7798 8239 7155 -384 360 -131 N ATOM 2757 CA SER A 374 43.997 46.124 2.917 1.00 62.73 C ANISOU 2757 CA SER A 374 8021 8368 7444 -288 365 -83 C ATOM 2758 C SER A 374 43.083 47.135 2.208 1.00 63.76 C ANISOU 2758 C SER A 374 8242 8396 7586 -296 409 -59 C ATOM 2759 O SER A 374 42.172 46.736 1.482 1.00 63.97 O ANISOU 2759 O SER A 374 8257 8376 7671 -228 409 -25 O ATOM 2760 CB SER A 374 43.335 45.525 4.157 1.00 66.72 C ANISOU 2760 CB SER A 374 8528 8844 7976 -219 361 -57 C ATOM 2761 OG SER A 374 44.093 44.374 4.537 1.00 69.65 O ANISOU 2761 OG SER A 374 8805 9308 8350 -192 314 -72 O ATOM 2762 N SER A 375 43.354 48.427 2.354 1.00 64.78 N ANISOU 2762 N SER A 375 8461 8494 7656 -378 446 -77 N ATOM 2763 CA SER A 375 42.584 49.464 1.647 1.00 69.87 C ANISOU 2763 CA SER A 375 9200 9043 8302 -387 489 -56 C ATOM 2764 C SER A 375 42.538 49.293 0.130 1.00 67.36 C ANISOU 2764 C SER A 375 8843 8734 8014 -379 480 -49 C ATOM 2765 O SER A 375 41.593 49.738 -0.525 1.00 65.89 O ANISOU 2765 O SER A 375 8710 8469 7854 -344 507 -17 O ATOM 2766 CB SER A 375 43.158 50.849 1.946 1.00 72.47 C ANISOU 2766 CB SER A 375 9632 9350 8553 -494 524 -85 C ATOM 2767 OG SER A 375 43.059 51.116 3.327 1.00 83.83 O ANISOU 2767 OG SER A 375 11121 10766 9963 -498 538 -89 O ATOM 2768 N ALA A 376 43.576 48.692 -0.430 1.00 62.65 N ANISOU 2768 N ALA A 376 8157 8239 7408 -412 444 -80 N ATOM 2769 CA ALA A 376 43.668 48.539 -1.864 1.00 64.70 C ANISOU 2769 CA ALA A 376 8376 8518 7688 -412 434 -80 C ATOM 2770 C ALA A 376 42.628 47.560 -2.413 1.00 58.08 C ANISOU 2770 C ALA A 376 7490 7647 6931 -304 417 -41 C ATOM 2771 O ALA A 376 42.287 47.640 -3.571 1.00 57.64 O ANISOU 2771 O ALA A 376 7429 7571 6897 -292 421 -28 O ATOM 2772 CB ALA A 376 45.073 48.083 -2.254 1.00 67.33 C ANISOU 2772 CB ALA A 376 8618 8978 7986 -468 398 -124 C ATOM 2773 N VAL A 377 42.155 46.622 -1.603 1.00 54.26 N ANISOU 2773 N VAL A 377 6967 7160 6486 -230 397 -22 N ATOM 2774 CA VAL A 377 41.099 45.723 -2.053 1.00 57.55 C ANISOU 2774 CA VAL A 377 7346 7541 6976 -135 383 16 C ATOM 2775 C VAL A 377 39.761 45.968 -1.336 1.00 55.96 C ANISOU 2775 C VAL A 377 7209 7248 6803 -77 412 61 C ATOM 2776 O VAL A 377 38.979 45.060 -1.174 1.00 53.67 O ANISOU 2776 O VAL A 377 6882 6943 6566 -1 395 92 O ATOM 2777 CB VAL A 377 41.532 44.251 -1.918 1.00 60.82 C ANISOU 2777 CB VAL A 377 7658 8029 7422 -87 331 6 C ATOM 2778 CG1 VAL A 377 42.669 43.961 -2.876 1.00 64.58 C ANISOU 2778 CG1 VAL A 377 8066 8594 7877 -126 303 -32 C ATOM 2779 CG2 VAL A 377 41.964 43.921 -0.493 1.00 66.21 C ANISOU 2779 CG2 VAL A 377 8331 8742 8082 -86 319 -4 C ATOM 2780 N ALA A 378 39.499 47.201 -0.923 1.00 54.89 N ANISOU 2780 N ALA A 378 7173 7052 6629 -112 457 66 N ATOM 2781 CA ALA A 378 38.217 47.553 -0.326 1.00 58.17 C ANISOU 2781 CA ALA A 378 7654 7382 7064 -53 490 109 C ATOM 2782 C ALA A 378 37.019 47.299 -1.260 1.00 54.70 C ANISOU 2782 C ALA A 378 7205 6899 6680 17 496 154 C ATOM 2783 O ALA A 378 37.137 47.294 -2.496 1.00 51.67 O ANISOU 2783 O ALA A 378 6796 6527 6307 6 488 151 O ATOM 2784 CB ALA A 378 38.239 49.026 0.091 1.00 57.08 C ANISOU 2784 CB ALA A 378 7635 7185 6866 -107 539 101 C ATOM 2785 N PHE A 379 35.853 47.151 -0.653 1.00 54.92 N ANISOU 2785 N PHE A 379 7253 6877 6737 87 511 196 N ATOM 2786 CA PHE A 379 34.595 47.051 -1.381 1.00 51.46 C ANISOU 2786 CA PHE A 379 6813 6396 6341 155 523 243 C ATOM 2787 C PHE A 379 34.463 48.183 -2.375 1.00 50.93 C ANISOU 2787 C PHE A 379 6813 6288 6250 130 557 246 C ATOM 2788 O PHE A 379 34.775 49.316 -2.068 1.00 51.37 O ANISOU 2788 O PHE A 379 6957 6307 6253 84 592 231 O ATOM 2789 CB PHE A 379 33.425 47.118 -0.413 1.00 54.30 C ANISOU 2789 CB PHE A 379 7209 6708 6714 220 548 285 C ATOM 2790 CG PHE A 379 32.119 46.957 -1.086 1.00 52.84 C ANISOU 2790 CG PHE A 379 7012 6492 6569 291 558 335 C ATOM 2791 CD1 PHE A 379 31.612 45.710 -1.306 1.00 52.80 C ANISOU 2791 CD1 PHE A 379 6923 6519 6619 337 523 359 C ATOM 2792 CD2 PHE A 379 31.441 48.061 -1.567 1.00 54.99 C ANISOU 2792 CD2 PHE A 379 7362 6709 6821 308 602 359 C ATOM 2793 CE1 PHE A 379 30.412 45.553 -1.976 1.00 54.38 C ANISOU 2793 CE1 PHE A 379 7106 6701 6853 395 531 404 C ATOM 2794 CE2 PHE A 379 30.248 47.917 -2.242 1.00 55.02 C ANISOU 2794 CE2 PHE A 379 7348 6696 6858 374 611 406 C ATOM 2795 CZ PHE A 379 29.731 46.654 -2.445 1.00 53.73 C ANISOU 2795 CZ PHE A 379 7092 6572 6750 415 575 428 C ATOM 2796 N GLY A 380 34.039 47.880 -3.595 1.00 49.26 N ANISOU 2796 N GLY A 380 6562 6081 6072 156 547 264 N ATOM 2797 CA GLY A 380 33.938 48.929 -4.605 1.00 47.97 C ANISOU 2797 CA GLY A 380 6460 5881 5883 134 578 269 C ATOM 2798 C GLY A 380 35.174 49.177 -5.440 1.00 48.52 C ANISOU 2798 C GLY A 380 6518 5994 5923 51 564 225 C ATOM 2799 O GLY A 380 35.125 49.984 -6.370 1.00 49.74 O ANISOU 2799 O GLY A 380 6719 6121 6058 29 587 229 O ATOM 2800 N THR A 381 36.285 48.493 -5.150 1.00 47.64 N ANISOU 2800 N THR A 381 6342 5953 5806 7 528 184 N ATOM 2801 CA THR A 381 37.496 48.656 -5.955 1.00 48.32 C ANISOU 2801 CA THR A 381 6403 6095 5860 -70 513 141 C ATOM 2802 C THR A 381 37.245 48.265 -7.418 1.00 46.04 C ANISOU 2802 C THR A 381 6062 5823 5605 -47 497 153 C ATOM 2803 O THR A 381 36.719 47.190 -7.703 1.00 50.49 O ANISOU 2803 O THR A 381 6553 6406 6222 14 468 171 O ATOM 2804 CB THR A 381 38.646 47.774 -5.425 1.00 54.11 C ANISOU 2804 CB THR A 381 7056 6915 6586 -102 470 100 C ATOM 2805 OG1 THR A 381 39.001 48.169 -4.092 1.00 55.64 O ANISOU 2805 OG1 THR A 381 7295 7102 6742 -133 483 85 O ATOM 2806 CG2 THR A 381 39.876 47.907 -6.330 1.00 53.75 C ANISOU 2806 CG2 THR A 381 6974 6940 6506 -178 455 58 C ATOM 2807 N ARG A 382 37.639 49.121 -8.343 1.00 45.78 N ANISOU 2807 N ARG A 382 4849 6592 5954 -186 186 301 N ATOM 2808 CA ARG A 382 37.427 48.882 -9.758 1.00 48.48 C ANISOU 2808 CA ARG A 382 5227 6998 6193 -275 105 361 C ATOM 2809 C ARG A 382 38.618 48.184 -10.479 1.00 48.07 C ANISOU 2809 C ARG A 382 5242 7076 5945 -301 149 283 C ATOM 2810 O ARG A 382 38.436 47.341 -11.370 1.00 49.09 O ANISOU 2810 O ARG A 382 5431 7258 5962 -350 119 266 O ATOM 2811 CB ARG A 382 37.149 50.231 -10.389 1.00 54.49 C ANISOU 2811 CB ARG A 382 5941 7738 7024 -353 28 496 C ATOM 2812 CG ARG A 382 36.615 50.172 -11.797 1.00 61.44 C ANISOU 2812 CG ARG A 382 6854 8660 7830 -470 -86 597 C ATOM 2813 CD ARG A 382 36.772 51.510 -12.458 1.00 65.03 C ANISOU 2813 CD ARG A 382 7270 9121 8316 -558 -156 724 C ATOM 2814 NE ARG A 382 35.893 51.571 -13.597 1.00 72.61 N ANISOU 2814 NE ARG A 382 8244 10078 9263 -675 -295 854 N ATOM 2815 CZ ARG A 382 34.829 52.360 -13.682 1.00 86.46 C ANISOU 2815 CZ ARG A 382 9921 11723 11207 -711 -403 996 C ATOM 2816 NH1 ARG A 382 34.087 52.312 -14.776 1.00 90.05 N ANISOU 2816 NH1 ARG A 382 10395 12183 11634 -833 -546 1122 N ATOM 2817 NH2 ARG A 382 34.501 53.194 -12.689 1.00 88.08 N ANISOU 2817 NH2 ARG A 382 10027 11807 11632 -633 -369 1012 N ATOM 2818 N ASN A 383 39.828 48.551 -10.093 1.00 47.49 N ANISOU 2818 N ASN A 383 5158 7047 5838 -271 224 233 N ATOM 2819 CA ASN A 383 41.041 48.027 -10.684 1.00 49.47 C ANISOU 2819 CA ASN A 383 5449 7407 5938 -289 285 159 C ATOM 2820 C ASN A 383 42.104 47.895 -9.621 1.00 47.65 C ANISOU 2820 C ASN A 383 5193 7177 5735 -204 374 74 C ATOM 2821 O ASN A 383 42.311 48.814 -8.855 1.00 46.61 O ANISOU 2821 O ASN A 383 5017 7001 5689 -181 383 106 O ATOM 2822 CB ASN A 383 41.555 48.972 -11.777 1.00 52.55 C ANISOU 2822 CB ASN A 383 5844 7876 6246 -392 259 238 C ATOM 2823 CG ASN A 383 40.704 48.920 -13.028 1.00 54.36 C ANISOU 2823 CG ASN A 383 6119 8131 6402 -505 163 319 C ATOM 2824 OD1 ASN A 383 40.648 47.889 -13.692 1.00 55.17 O ANISOU 2824 OD1 ASN A 383 6290 8285 6387 -537 173 260 O ATOM 2825 ND2 ASN A 383 40.018 50.020 -13.350 1.00 56.01 N ANISOU 2825 ND2 ASN A 383 6293 8297 6690 -572 64 459 N ATOM 2826 N VAL A 384 42.772 46.751 -9.574 1.00 47.00 N ANISOU 2826 N VAL A 384 5135 7133 5586 -163 436 -30 N ATOM 2827 CA VAL A 384 43.903 46.566 -8.679 1.00 46.26 C ANISOU 2827 CA VAL A 384 5011 7044 5520 -96 507 -98 C ATOM 2828 C VAL A 384 44.648 45.354 -9.187 1.00 45.54 C ANISOU 2828 C VAL A 384 4944 7011 5348 -81 568 -199 C ATOM 2829 O VAL A 384 44.049 44.445 -9.745 1.00 47.59 O ANISOU 2829 O VAL A 384 5249 7274 5559 -93 555 -235 O ATOM 2830 CB VAL A 384 43.481 46.409 -7.201 1.00 48.33 C ANISOU 2830 CB VAL A 384 5255 7211 5894 -22 503 -115 C ATOM 2831 CG1 VAL A 384 42.686 45.125 -6.974 1.00 49.49 C ANISOU 2831 CG1 VAL A 384 5434 7318 6051 15 490 -168 C ATOM 2832 CG2 VAL A 384 44.685 46.414 -6.270 1.00 46.16 C ANISOU 2832 CG2 VAL A 384 4952 6938 5646 22 554 -159 C ATOM 2833 N THR A 385 45.967 45.400 -9.070 1.00 46.41 N ANISOU 2833 N THR A 385 5019 7164 5449 -62 636 -239 N ATOM 2834 CA THR A 385 46.842 44.317 -9.482 1.00 49.16 C ANISOU 2834 CA THR A 385 5367 7555 5755 -39 713 -341 C ATOM 2835 C THR A 385 47.661 43.940 -8.244 1.00 50.63 C ANISOU 2835 C THR A 385 5497 7693 6046 43 738 -380 C ATOM 2836 O THR A 385 48.443 44.765 -7.737 1.00 49.23 O ANISOU 2836 O THR A 385 5274 7521 5910 46 746 -341 O ATOM 2837 CB THR A 385 47.784 44.789 -10.600 1.00 53.69 C ANISOU 2837 CB THR A 385 5935 8228 6235 -108 777 -344 C ATOM 2838 OG1 THR A 385 47.033 45.378 -11.688 1.00 56.74 O ANISOU 2838 OG1 THR A 385 6376 8660 6519 -210 731 -278 O ATOM 2839 CG2 THR A 385 48.524 43.633 -11.129 1.00 56.22 C ANISOU 2839 CG2 THR A 385 6258 8582 6520 -91 873 -462 C ATOM 2840 N LEU A 386 47.472 42.716 -7.746 1.00 49.01 N ANISOU 2840 N LEU A 386 5297 7437 5886 102 739 -447 N ATOM 2841 CA LEU A 386 48.015 42.339 -6.430 1.00 50.43 C ANISOU 2841 CA LEU A 386 5432 7555 6171 167 730 -461 C ATOM 2842 C LEU A 386 49.486 41.963 -6.529 1.00 50.69 C ANISOU 2842 C LEU A 386 5400 7615 6245 193 799 -510 C ATOM 2843 O LEU A 386 49.853 41.292 -7.456 1.00 47.51 O ANISOU 2843 O LEU A 386 4995 7249 5808 190 865 -582 O ATOM 2844 CB LEU A 386 47.272 41.144 -5.830 1.00 49.57 C ANISOU 2844 CB LEU A 386 5347 7378 6107 214 694 -502 C ATOM 2845 CG LEU A 386 45.951 41.425 -5.103 1.00 50.82 C ANISOU 2845 CG LEU A 386 5545 7478 6283 210 626 -449 C ATOM 2846 CD1 LEU A 386 46.150 42.484 -4.027 1.00 51.59 C ANISOU 2846 CD1 LEU A 386 5625 7548 6428 203 606 -387 C ATOM 2847 CD2 LEU A 386 44.860 41.860 -6.067 1.00 48.77 C ANISOU 2847 CD2 LEU A 386 5330 7241 5957 159 602 -413 C ATOM 2848 N ASP A 387 50.276 42.394 -5.542 1.00 50.44 N ANISOU 2848 N ASP A 387 5316 7556 6292 212 781 -472 N ATOM 2849 CA ASP A 387 51.662 41.977 -5.376 1.00 51.22 C ANISOU 2849 CA ASP A 387 5333 7654 6471 244 827 -502 C ATOM 2850 C ASP A 387 51.703 40.828 -4.394 1.00 49.37 C ANISOU 2850 C ASP A 387 5078 7338 6340 300 785 -530 C ATOM 2851 O ASP A 387 51.588 41.029 -3.188 1.00 52.34 O ANISOU 2851 O ASP A 387 5460 7663 6763 301 712 -476 O ATOM 2852 CB ASP A 387 52.509 43.141 -4.859 1.00 50.48 C ANISOU 2852 CB ASP A 387 5196 7575 6408 219 811 -427 C ATOM 2853 CG ASP A 387 53.963 42.743 -4.572 1.00 54.71 C ANISOU 2853 CG ASP A 387 5632 8098 7054 249 843 -439 C ATOM 2854 OD1 ASP A 387 54.389 41.652 -5.001 1.00 49.83 O ANISOU 2854 OD1 ASP A 387 4972 7470 6491 289 899 -515 O ATOM 2855 OD2 ASP A 387 54.681 43.538 -3.908 1.00 55.79 O ANISOU 2855 OD2 ASP A 387 5732 8229 7236 230 808 -371 O ATOM 2856 N TYR A 388 51.874 39.626 -4.937 1.00 50.08 N ANISOU 2856 N TYR A 388 5148 7415 6464 336 833 -615 N ATOM 2857 CA TYR A 388 51.992 38.378 -4.180 1.00 52.93 C ANISOU 2857 CA TYR A 388 5477 7694 6941 390 795 -647 C ATOM 2858 C TYR A 388 53.188 38.335 -3.227 1.00 54.59 C ANISOU 2858 C TYR A 388 5594 7857 7288 411 762 -602 C ATOM 2859 O TYR A 388 53.165 37.551 -2.291 1.00 54.10 O ANISOU 2859 O TYR A 388 5515 7719 7317 435 691 -588 O ATOM 2860 CB TYR A 388 52.107 37.157 -5.125 1.00 52.84 C ANISOU 2860 CB TYR A 388 5449 7673 6952 424 873 -759 C ATOM 2861 CG TYR A 388 50.922 36.854 -6.024 1.00 54.39 C ANISOU 2861 CG TYR A 388 5740 7897 7025 400 889 -810 C ATOM 2862 CD1 TYR A 388 49.636 37.321 -5.743 1.00 53.52 C ANISOU 2862 CD1 TYR A 388 5712 7789 6832 370 812 -752 C ATOM 2863 CD2 TYR A 388 51.092 36.076 -7.160 1.00 55.16 C ANISOU 2863 CD2 TYR A 388 5845 8014 7098 402 982 -919 C ATOM 2864 CE1 TYR A 388 48.562 37.019 -6.581 1.00 53.32 C ANISOU 2864 CE1 TYR A 388 5767 7784 6708 342 812 -785 C ATOM 2865 CE2 TYR A 388 50.033 35.776 -8.003 1.00 55.51 C ANISOU 2865 CE2 TYR A 388 5986 8083 7023 365 985 -961 C ATOM 2866 CZ TYR A 388 48.766 36.244 -7.712 1.00 54.70 C ANISOU 2866 CZ TYR A 388 5956 7981 6844 335 891 -886 C ATOM 2867 OH TYR A 388 47.717 35.936 -8.574 1.00 53.03 O ANISOU 2867 OH TYR A 388 5834 7790 6525 291 881 -915 O ATOM 2868 N GLN A 389 54.221 39.141 -3.490 1.00 54.93 N ANISOU 2868 N GLN A 389 5577 7943 7348 392 807 -574 N ATOM 2869 CA GLN A 389 55.422 39.176 -2.668 1.00 57.19 C ANISOU 2869 CA GLN A 389 5768 8188 7773 402 769 -520 C ATOM 2870 C GLN A 389 55.407 40.283 -1.617 1.00 58.58 C ANISOU 2870 C GLN A 389 5977 8360 7918 351 678 -414 C ATOM 2871 O GLN A 389 56.449 40.624 -1.076 1.00 61.85 O ANISOU 2871 O GLN A 389 6321 8758 8419 338 645 -355 O ATOM 2872 CB GLN A 389 56.659 39.360 -3.559 1.00 59.52 C ANISOU 2872 CB GLN A 389 5964 8525 8126 410 877 -550 C ATOM 2873 CG GLN A 389 56.891 38.218 -4.530 1.00 62.84 C ANISOU 2873 CG GLN A 389 6339 8934 8601 456 987 -669 C ATOM 2874 CD GLN A 389 57.139 36.903 -3.825 1.00 68.88 C ANISOU 2874 CD GLN A 389 7038 9590 9542 514 938 -689 C ATOM 2875 OE1 GLN A 389 56.521 35.890 -4.149 1.00 77.39 O ANISOU 2875 OE1 GLN A 389 8147 10633 10621 546 958 -770 O ATOM 2876 NE2 GLN A 389 58.026 36.914 -2.847 1.00 70.20 N ANISOU 2876 NE2 GLN A 389 7114 9697 9860 521 860 -607 N ATOM 2877 N LEU A 390 54.250 40.865 -1.347 1.00 57.10 N ANISOU 2877 N LEU A 390 5893 8185 7615 319 641 -393 N ATOM 2878 CA LEU A 390 54.054 41.668 -0.121 1.00 58.36 C ANISOU 2878 CA LEU A 390 6102 8317 7755 270 554 -312 C ATOM 2879 C LEU A 390 54.797 41.093 1.097 1.00 58.46 C ANISOU 2879 C LEU A 390 6072 8258 7881 262 464 -263 C ATOM 2880 O LEU A 390 55.537 41.799 1.744 1.00 57.92 O ANISOU 2880 O LEU A 390 5985 8183 7839 219 417 -194 O ATOM 2881 CB LEU A 390 52.558 41.756 0.213 1.00 56.26 C ANISOU 2881 CB LEU A 390 5940 8034 7398 254 527 -320 C ATOM 2882 CG LEU A 390 52.145 42.577 1.444 1.00 59.58 C ANISOU 2882 CG LEU A 390 6430 8422 7785 197 465 -260 C ATOM 2883 CD1 LEU A 390 52.582 44.028 1.327 1.00 60.84 C ANISOU 2883 CD1 LEU A 390 6588 8618 7910 154 480 -215 C ATOM 2884 CD2 LEU A 390 50.637 42.516 1.650 1.00 59.86 C ANISOU 2884 CD2 LEU A 390 6551 8436 7756 191 463 -281 C ATOM 2885 N PHE A 391 54.562 39.817 1.403 1.00 59.89 N ANISOU 2885 N PHE A 391 6242 8383 8128 296 430 -291 N ATOM 2886 CA PHE A 391 55.261 39.092 2.487 1.00 59.97 C ANISOU 2886 CA PHE A 391 6203 8317 8263 285 330 -236 C ATOM 2887 C PHE A 391 55.791 37.797 1.894 1.00 60.39 C ANISOU 2887 C PHE A 391 6155 8332 8457 356 363 -291 C ATOM 2888 O PHE A 391 55.042 36.822 1.757 1.00 55.13 O ANISOU 2888 O PHE A 391 5516 7635 7794 391 364 -345 O ATOM 2889 CB PHE A 391 54.331 38.738 3.651 1.00 58.56 C ANISOU 2889 CB PHE A 391 6120 8092 8038 242 239 -205 C ATOM 2890 CG PHE A 391 53.726 39.923 4.323 1.00 57.95 C ANISOU 2890 CG PHE A 391 6147 8037 7834 169 221 -168 C ATOM 2891 CD1 PHE A 391 54.530 40.936 4.815 1.00 61.05 C ANISOU 2891 CD1 PHE A 391 6534 8439 8223 111 189 -103 C ATOM 2892 CD2 PHE A 391 52.351 40.039 4.458 1.00 60.25 C ANISOU 2892 CD2 PHE A 391 6537 8332 8020 158 242 -199 C ATOM 2893 CE1 PHE A 391 53.974 42.042 5.432 1.00 60.81 C ANISOU 2893 CE1 PHE A 391 6602 8418 8082 41 183 -81 C ATOM 2894 CE2 PHE A 391 51.791 41.141 5.071 1.00 59.50 C ANISOU 2894 CE2 PHE A 391 6530 8245 7830 94 243 -176 C ATOM 2895 CZ PHE A 391 52.607 42.138 5.571 1.00 57.45 C ANISOU 2895 CZ PHE A 391 6271 7991 7564 35 216 -122 C ATOM 2896 N PRO A 392 57.078 37.786 1.529 1.00 59.03 N ANISOU 2896 N PRO A 392 5861 8153 8412 378 395 -281 N ATOM 2897 CA PRO A 392 57.677 36.619 0.882 1.00 63.32 C ANISOU 2897 CA PRO A 392 6292 8651 9114 450 453 -348 C ATOM 2898 C PRO A 392 57.529 35.337 1.694 1.00 63.63 C ANISOU 2898 C PRO A 392 6308 8588 9278 467 351 -330 C ATOM 2899 O PRO A 392 57.303 34.263 1.120 1.00 69.14 O ANISOU 2899 O PRO A 392 6975 9248 10044 527 401 -415 O ATOM 2900 CB PRO A 392 59.157 37.024 0.737 1.00 64.91 C ANISOU 2900 CB PRO A 392 6359 8849 9452 451 479 -305 C ATOM 2901 CG PRO A 392 59.124 38.518 0.648 1.00 62.59 C ANISOU 2901 CG PRO A 392 6127 8641 9010 394 495 -261 C ATOM 2902 CD PRO A 392 57.979 38.952 1.525 1.00 60.17 C ANISOU 2902 CD PRO A 392 5965 8339 8555 339 405 -221 C ATOM 2903 N GLY A 393 57.637 35.454 3.015 1.00 61.71 N ANISOU 2903 N GLY A 393 6088 8300 9059 404 206 -218 N ATOM 2904 CA GLY A 393 57.457 34.318 3.913 1.00 58.90 C ANISOU 2904 CA GLY A 393 5722 7850 8806 398 85 -176 C ATOM 2905 C GLY A 393 56.078 33.710 3.848 1.00 57.37 C ANISOU 2905 C GLY A 393 5633 7658 8504 412 93 -239 C ATOM 2906 O GLY A 393 55.938 32.498 3.767 1.00 61.97 O ANISOU 2906 O GLY A 393 6174 8173 9196 458 73 -274 O ATOM 2907 N VAL A 394 55.046 34.542 3.872 1.00 58.49 N ANISOU 2907 N VAL A 394 5905 7870 8445 375 120 -252 N ATOM 2908 CA VAL A 394 53.675 34.037 3.716 1.00 57.70 C ANISOU 2908 CA VAL A 394 5900 7775 8246 389 136 -309 C ATOM 2909 C VAL A 394 53.526 33.328 2.367 1.00 56.98 C ANISOU 2909 C VAL A 394 5768 7692 8189 473 246 -426 C ATOM 2910 O VAL A 394 52.883 32.287 2.258 1.00 59.46 O ANISOU 2910 O VAL A 394 6098 7963 8531 504 232 -471 O ATOM 2911 CB VAL A 394 52.636 35.170 3.789 1.00 60.68 C ANISOU 2911 CB VAL A 394 6402 8224 8428 342 168 -308 C ATOM 2912 CG1 VAL A 394 51.234 34.626 3.556 1.00 61.28 C ANISOU 2912 CG1 VAL A 394 6558 8300 8425 360 186 -362 C ATOM 2913 CG2 VAL A 394 52.713 35.904 5.116 1.00 60.21 C ANISOU 2913 CG2 VAL A 394 6402 8156 8317 250 79 -213 C ATOM 2914 N TRP A 395 54.134 33.883 1.329 1.00 58.18 N ANISOU 2914 N TRP A 395 5872 7899 8333 500 356 -476 N ATOM 2915 CA TRP A 395 54.032 33.258 0.022 1.00 61.96 C ANISOU 2915 CA TRP A 395 6328 8391 8823 559 472 -596 C ATOM 2916 C TRP A 395 54.646 31.845 -0.056 1.00 69.52 C ANISOU 2916 C TRP A 395 7179 9250 9984 619 470 -643 C ATOM 2917 O TRP A 395 54.099 30.973 -0.764 1.00 67.43 O ANISOU 2917 O TRP A 395 6935 8966 9719 659 523 -741 O ATOM 2918 CB TRP A 395 54.623 34.151 -1.054 1.00 61.10 C ANISOU 2918 CB TRP A 395 6191 8364 8657 559 596 -637 C ATOM 2919 CG TRP A 395 54.235 33.689 -2.408 1.00 60.67 C ANISOU 2919 CG TRP A 395 6161 8344 8544 589 717 -760 C ATOM 2920 CD1 TRP A 395 55.026 33.054 -3.301 1.00 62.25 C ANISOU 2920 CD1 TRP A 395 6278 8528 8844 631 829 -856 C ATOM 2921 CD2 TRP A 395 52.938 33.787 -3.014 1.00 59.21 C ANISOU 2921 CD2 TRP A 395 6095 8208 8191 568 736 -802 C ATOM 2922 NE1 TRP A 395 54.318 32.766 -4.439 1.00 63.77 N ANISOU 2922 NE1 TRP A 395 6545 8764 8919 629 919 -961 N ATOM 2923 CE2 TRP A 395 53.031 33.205 -4.290 1.00 61.50 C ANISOU 2923 CE2 TRP A 395 6381 8517 8468 589 854 -922 C ATOM 2924 CE3 TRP A 395 51.715 34.335 -2.610 1.00 58.50 C ANISOU 2924 CE3 TRP A 395 6113 8145 7968 529 669 -750 C ATOM 2925 CZ2 TRP A 395 51.949 33.145 -5.174 1.00 62.87 C ANISOU 2925 CZ2 TRP A 395 6660 8737 8488 563 888 -980 C ATOM 2926 CZ3 TRP A 395 50.626 34.267 -3.489 1.00 58.76 C ANISOU 2926 CZ3 TRP A 395 6234 8218 7874 515 703 -802 C ATOM 2927 CH2 TRP A 395 50.753 33.678 -4.751 1.00 61.46 C ANISOU 2927 CH2 TRP A 395 6575 8580 8195 528 802 -910 C ATOM 2928 N LYS A 396 55.754 31.616 0.661 1.00 71.52 N ANISOU 2928 N LYS A 396 7319 9434 10419 622 404 -572 N ATOM 2929 CA LYS A 396 56.379 30.272 0.716 1.00 77.22 C ANISOU 2929 CA LYS A 396 7921 10040 11378 679 384 -600 C ATOM 2930 C LYS A 396 55.393 29.235 1.199 1.00 75.71 C ANISOU 2930 C LYS A 396 7790 9786 11190 683 295 -604 C ATOM 2931 O LYS A 396 55.371 28.125 0.692 1.00 80.79 O ANISOU 2931 O LYS A 396 8385 10360 11949 741 334 -689 O ATOM 2932 CB LYS A 396 57.584 30.244 1.643 1.00 78.49 C ANISOU 2932 CB LYS A 396 7957 10126 11739 662 280 -483 C ATOM 2933 CG LYS A 396 58.785 30.977 1.093 1.00 84.79 C ANISOU 2933 CG LYS A 396 8650 10957 12609 673 374 -486 C ATOM 2934 CD LYS A 396 59.744 31.350 2.210 1.00 92.57 C ANISOU 2934 CD LYS A 396 9556 11895 13722 622 235 -332 C ATOM 2935 CE LYS A 396 60.818 32.315 1.743 1.00 96.51 C ANISOU 2935 CE LYS A 396 9970 12444 14254 618 318 -316 C ATOM 2936 NZ LYS A 396 61.877 31.590 0.988 1.00102.80 N ANISOU 2936 NZ LYS A 396 10587 13170 15302 695 427 -384 N ATOM 2937 N LYS A 397 54.582 29.620 2.178 1.00 76.73 N ANISOU 2937 N LYS A 397 8024 9937 11191 618 183 -515 N ATOM 2938 CA LYS A 397 53.557 28.757 2.739 1.00 79.85 C ANISOU 2938 CA LYS A 397 8488 10285 11565 607 93 -502 C ATOM 2939 C LYS A 397 52.366 28.497 1.806 1.00 80.60 C ANISOU 2939 C LYS A 397 8675 10421 11525 637 179 -612 C ATOM 2940 O LYS A 397 51.526 27.671 2.121 1.00 80.35 O ANISOU 2940 O LYS A 397 8689 10344 11493 637 116 -614 O ATOM 2941 CB LYS A 397 53.022 29.376 4.040 1.00 83.95 C ANISOU 2941 CB LYS A 397 9103 10827 11967 514 -26 -383 C ATOM 2942 CG LYS A 397 53.979 29.315 5.224 1.00 87.35 C ANISOU 2942 CG LYS A 397 9468 11194 12527 458 -164 -253 C ATOM 2943 CD LYS A 397 54.028 27.913 5.815 1.00 87.29 C ANISOU 2943 CD LYS A 397 9403 11071 12692 464 -284 -212 C ATOM 2944 CE LYS A 397 54.545 27.921 7.240 1.00 88.74 C ANISOU 2944 CE LYS A 397 9577 11204 12934 364 -460 -54 C ATOM 2945 NZ LYS A 397 54.452 26.554 7.812 1.00 90.33 N ANISOU 2945 NZ LYS A 397 9733 11295 13292 359 -589 -4 N ATOM 2946 N ILE A 398 52.272 29.204 0.683 1.00 78.49 N ANISOU 2946 N ILE A 398 8439 10240 11143 651 310 -692 N ATOM 2947 CA ILE A 398 51.140 29.051 -0.225 1.00 75.81 C ANISOU 2947 CA ILE A 398 8195 9944 10665 661 377 -780 C ATOM 2948 C ILE A 398 51.534 28.424 -1.566 1.00 74.22 C ANISOU 2948 C ILE A 398 7949 9734 10515 713 505 -917 C ATOM 2949 O ILE A 398 50.884 27.497 -2.027 1.00 74.32 O ANISOU 2949 O ILE A 398 7997 9709 10530 736 516 -993 O ATOM 2950 CB ILE A 398 50.479 30.410 -0.483 1.00 73.97 C ANISOU 2950 CB ILE A 398 8056 9819 10228 612 414 -755 C ATOM 2951 CG1 ILE A 398 49.919 30.967 0.820 1.00 71.44 C ANISOU 2951 CG1 ILE A 398 7795 9499 9849 555 307 -643 C ATOM 2952 CG2 ILE A 398 49.367 30.280 -1.515 1.00 78.50 C ANISOU 2952 CG2 ILE A 398 8718 10434 10671 612 472 -833 C ATOM 2953 CD1 ILE A 398 49.479 32.414 0.720 1.00 69.74 C ANISOU 2953 CD1 ILE A 398 7648 9370 9477 509 343 -610 C ATOM 2954 N ALA A 399 52.579 28.952 -2.193 1.00 74.89 N ANISOU 2954 N ALA A 399 7965 9855 10634 725 608 -952 N ATOM 2955 CA ALA A 399 53.049 28.442 -3.478 1.00 80.14 C ANISOU 2955 CA ALA A 399 8591 10518 11339 762 756 -1093 C ATOM 2956 C ALA A 399 53.163 26.915 -3.440 1.00 78.56 C ANISOU 2956 C ALA A 399 8328 10192 11326 819 743 -1163 C ATOM 2957 O ALA A 399 53.579 26.356 -2.430 1.00 83.10 O ANISOU 2957 O ALA A 399 8820 10672 12079 840 635 -1088 O ATOM 2958 CB ALA A 399 54.394 29.062 -3.843 1.00 79.80 C ANISOU 2958 CB ALA A 399 8444 10503 11373 770 854 -1101 C ATOM 2959 N GLY A 400 52.748 26.263 -4.526 1.00 72.43 N ANISOU 2959 N GLY A 400 7600 9414 10504 832 843 -1301 N ATOM 2960 CA GLY A 400 52.813 24.814 -4.652 1.00 72.31 C ANISOU 2960 CA GLY A 400 7535 9277 10663 886 850 -1391 C ATOM 2961 C GLY A 400 51.710 24.007 -3.981 1.00 72.09 C ANISOU 2961 C GLY A 400 7571 9187 10633 885 708 -1348 C ATOM 2962 O GLY A 400 51.659 22.805 -4.181 1.00 74.84 O ANISOU 2962 O GLY A 400 7890 9434 11112 925 714 -1429 O ATOM 2963 N LYS A 401 50.826 24.627 -3.200 1.00 68.91 N ANISOU 2963 N LYS A 401 7251 8837 10091 838 590 -1228 N ATOM 2964 CA LYS A 401 49.796 23.862 -2.463 1.00 68.45 C ANISOU 2964 CA LYS A 401 7246 8721 10039 831 455 -1176 C ATOM 2965 C LYS A 401 48.449 23.735 -3.189 1.00 65.07 C ANISOU 2965 C LYS A 401 6953 8340 9431 803 471 -1233 C ATOM 2966 O LYS A 401 47.518 23.142 -2.662 1.00 65.09 O ANISOU 2966 O LYS A 401 7003 8301 9428 794 368 -1192 O ATOM 2967 CB LYS A 401 49.539 24.457 -1.081 1.00 69.91 C ANISOU 2967 CB LYS A 401 7445 8921 10194 788 317 -1014 C ATOM 2968 CG LYS A 401 50.703 24.374 -0.099 1.00 76.52 C ANISOU 2968 CG LYS A 401 8161 9691 11221 796 244 -925 C ATOM 2969 CD LYS A 401 50.202 23.939 1.282 1.00 84.17 C ANISOU 2969 CD LYS A 401 9149 10604 12227 756 71 -798 C ATOM 2970 CE LYS A 401 50.858 24.672 2.453 1.00 89.96 C ANISOU 2970 CE LYS A 401 9850 11347 12983 702 -21 -659 C ATOM 2971 NZ LYS A 401 52.331 24.855 2.293 1.00 93.14 N ANISOU 2971 NZ LYS A 401 10118 11718 13550 732 17 -656 N ATOM 2972 N GLY A 402 48.351 24.269 -4.400 1.00 62.94 N ANISOU 2972 N GLY A 402 6743 8154 9017 781 592 -1321 N ATOM 2973 CA GLY A 402 47.090 24.281 -5.134 1.00 59.40 C ANISOU 2973 CA GLY A 402 6423 7755 8389 738 594 -1357 C ATOM 2974 C GLY A 402 46.023 25.158 -4.473 1.00 54.66 C ANISOU 2974 C GLY A 402 5898 7218 7653 690 497 -1228 C ATOM 2975 O GLY A 402 44.904 24.721 -4.308 1.00 51.36 O ANISOU 2975 O GLY A 402 5544 6779 7192 674 422 -1205 O ATOM 2976 N ARG A 403 46.398 26.375 -4.098 1.00 54.92 N ANISOU 2976 N ARG A 403 5914 7319 7632 668 505 -1150 N ATOM 2977 CA ARG A 403 45.509 27.357 -3.503 1.00 55.05 C ANISOU 2977 CA ARG A 403 5990 7391 7533 623 440 -1040 C ATOM 2978 C ARG A 403 45.035 28.346 -4.537 1.00 54.04 C ANISOU 2978 C ARG A 403 5934 7361 7238 575 502 -1052 C ATOM 2979 O ARG A 403 45.824 28.797 -5.376 1.00 52.64 O ANISOU 2979 O ARG A 403 5738 7235 7024 567 599 -1107 O ATOM 2980 CB ARG A 403 46.239 28.186 -2.441 1.00 60.20 C ANISOU 2980 CB ARG A 403 6587 8055 8230 618 410 -945 C ATOM 2981 CG ARG A 403 46.591 27.461 -1.158 1.00 69.08 C ANISOU 2981 CG ARG A 403 7653 9093 9500 636 313 -885 C ATOM 2982 CD ARG A 403 45.420 26.698 -0.595 1.00 69.48 C ANISOU 2982 CD ARG A 403 7757 9095 9546 625 221 -853 C ATOM 2983 NE ARG A 403 45.685 26.215 0.748 1.00 79.54 N ANISOU 2983 NE ARG A 403 8991 10301 10927 616 116 -770 N ATOM 2984 CZ ARG A 403 44.887 25.376 1.414 1.00 85.91 C ANISOU 2984 CZ ARG A 403 9826 11051 11763 603 25 -733 C ATOM 2985 NH1 ARG A 403 43.769 24.902 0.854 1.00 86.65 N ANISOU 2985 NH1 ARG A 403 9982 11143 11799 606 27 -774 N ATOM 2986 NH2 ARG A 403 45.195 25.008 2.654 1.00 82.17 N ANISOU 2986 NH2 ARG A 403 9322 10523 11375 577 -76 -646 N ATOM 2987 N LEU A 404 43.770 28.741 -4.446 1.00 46.55 N ANISOU 2987 N LEU A 404 5057 6434 6193 536 445 -992 N ATOM 2988 CA LEU A 404 43.302 29.837 -5.261 1.00 46.37 C ANISOU 2988 CA LEU A 404 5091 6497 6031 481 479 -970 C ATOM 2989 C LEU A 404 43.611 31.160 -4.573 1.00 44.27 C ANISOU 2989 C LEU A 404 4797 6272 5751 467 478 -880 C ATOM 2990 O LEU A 404 43.423 31.286 -3.395 1.00 45.34 O ANISOU 2990 O LEU A 404 4915 6372 5938 476 421 -812 O ATOM 2991 CB LEU A 404 41.798 29.718 -5.540 1.00 45.34 C ANISOU 2991 CB LEU A 404 5036 6361 5827 443 415 -936 C ATOM 2992 CG LEU A 404 41.386 30.642 -6.687 1.00 47.70 C ANISOU 2992 CG LEU A 404 5392 6740 5992 377 444 -924 C ATOM 2993 CD1 LEU A 404 41.701 30.009 -8.045 1.00 47.76 C ANISOU 2993 CD1 LEU A 404 5445 6771 5929 348 507 -1035 C ATOM 2994 CD2 LEU A 404 39.921 30.997 -6.614 1.00 46.60 C ANISOU 2994 CD2 LEU A 404 5299 6592 5813 336 364 -838 C ATOM 2995 N VAL A 405 44.061 32.150 -5.328 1.00 44.11 N ANISOU 2995 N VAL A 405 4779 6326 5652 435 540 -880 N ATOM 2996 CA VAL A 405 44.234 33.517 -4.824 1.00 42.33 C ANISOU 2996 CA VAL A 405 4537 6141 5403 412 538 -795 C ATOM 2997 C VAL A 405 43.619 34.533 -5.788 1.00 42.49 C ANISOU 2997 C VAL A 405 4607 6229 5305 351 552 -762 C ATOM 2998 O VAL A 405 43.405 34.227 -6.967 1.00 44.18 O ANISOU 2998 O VAL A 405 4866 6477 5442 318 578 -813 O ATOM 2999 CB VAL A 405 45.724 33.916 -4.634 1.00 43.38 C ANISOU 2999 CB VAL A 405 4597 6295 5587 431 593 -805 C ATOM 3000 CG1 VAL A 405 46.366 33.077 -3.541 1.00 46.34 C ANISOU 3000 CG1 VAL A 405 4912 6596 6098 480 555 -806 C ATOM 3001 CG2 VAL A 405 46.504 33.762 -5.911 1.00 45.13 C ANISOU 3001 CG2 VAL A 405 4808 6566 5772 424 689 -891 C ATOM 3002 N LEU A 406 43.345 35.729 -5.268 1.00 41.54 N ANISOU 3002 N LEU A 406 4483 6124 5175 328 530 -676 N ATOM 3003 CA LEU A 406 42.920 36.855 -6.085 1.00 42.60 C ANISOU 3003 CA LEU A 406 4645 6315 5226 268 534 -626 C ATOM 3004 C LEU A 406 44.136 37.479 -6.755 1.00 45.24 C ANISOU 3004 C LEU A 406 4952 6720 5517 249 605 -647 C ATOM 3005 O LEU A 406 45.008 38.004 -6.072 1.00 45.96 O ANISOU 3005 O LEU A 406 4993 6813 5657 270 625 -626 O ATOM 3006 CB LEU A 406 42.254 37.931 -5.222 1.00 41.81 C ANISOU 3006 CB LEU A 406 4537 6189 5158 256 495 -532 C ATOM 3007 CG LEU A 406 41.738 39.167 -5.954 1.00 42.48 C ANISOU 3007 CG LEU A 406 4635 6311 5191 196 484 -462 C ATOM 3008 CD1 LEU A 406 40.531 38.855 -6.822 1.00 45.02 C ANISOU 3008 CD1 LEU A 406 5003 6629 5473 154 433 -441 C ATOM 3009 CD2 LEU A 406 41.350 40.215 -4.927 1.00 44.99 C ANISOU 3009 CD2 LEU A 406 4930 6589 5574 197 468 -391 C ATOM 3010 N LYS A 407 44.120 37.494 -8.082 1.00 47.09 N ANISOU 3010 N LYS A 407 5226 7013 5652 196 638 -678 N ATOM 3011 CA LYS A 407 45.199 38.035 -8.898 1.00 49.00 C ANISOU 3011 CA LYS A 407 5451 7332 5834 161 717 -703 C ATOM 3012 C LYS A 407 45.016 39.514 -9.170 1.00 49.30 C ANISOU 3012 C LYS A 407 5492 7418 5819 100 693 -604 C ATOM 3013 O LYS A 407 45.983 40.284 -9.130 1.00 50.21 O ANISOU 3013 O LYS A 407 5563 7574 5940 94 737 -585 O ATOM 3014 CB LYS A 407 45.222 37.289 -10.227 1.00 51.20 C ANISOU 3014 CB LYS A 407 5786 7653 6013 114 770 -791 C ATOM 3015 CG LYS A 407 46.460 37.507 -11.088 1.00 56.14 C ANISOU 3015 CG LYS A 407 6393 8353 6582 81 884 -853 C ATOM 3016 CD LYS A 407 46.256 36.909 -12.467 1.00 59.25 C ANISOU 3016 CD LYS A 407 6873 8795 6844 4 936 -937 C ATOM 3017 CE LYS A 407 47.562 36.617 -13.213 1.00 72.00 C ANISOU 3017 CE LYS A 407 8464 10460 8431 -8 1087 -1050 C ATOM 3018 NZ LYS A 407 48.432 37.798 -13.502 1.00 73.94 N ANISOU 3018 NZ LYS A 407 8669 10786 8638 -50 1141 -999 N ATOM 3019 N ALA A 408 43.785 39.909 -9.484 1.00 45.15 N ANISOU 3019 N ALA A 408 5012 6884 5256 50 619 -534 N ATOM 3020 CA ALA A 408 43.515 41.262 -9.881 1.00 45.83 C ANISOU 3020 CA ALA A 408 5099 7006 5305 -16 585 -434 C ATOM 3021 C ALA A 408 42.018 41.533 -9.909 1.00 45.50 C ANISOU 3021 C ALA A 408 5086 6917 5283 -49 489 -350 C ATOM 3022 O ALA A 408 41.214 40.615 -9.972 1.00 48.40 O ANISOU 3022 O ALA A 408 5488 7247 5653 -41 452 -375 O ATOM 3023 CB ALA A 408 44.065 41.500 -11.294 1.00 47.57 C ANISOU 3023 CB ALA A 408 5357 7323 5393 -104 630 -451 C ATOM 3024 N ILE A 409 41.674 42.811 -9.914 1.00 45.17 N ANISOU 3024 N ILE A 409 5022 6872 5267 -89 446 -247 N ATOM 3025 CA ILE A 409 40.349 43.237 -10.337 1.00 49.30 C ANISOU 3025 CA ILE A 409 5562 7362 5807 -147 353 -150 C ATOM 3026 C ILE A 409 40.522 44.164 -11.534 1.00 51.43 C ANISOU 3026 C ILE A 409 5850 7703 5988 -255 324 -76 C ATOM 3027 O ILE A 409 41.297 45.113 -11.481 1.00 50.26 O ANISOU 3027 O ILE A 409 5667 7588 5841 -265 355 -46 O ATOM 3028 CB ILE A 409 39.598 43.919 -9.197 1.00 45.06 C ANISOU 3028 CB ILE A 409 4971 6732 5418 -101 322 -85 C ATOM 3029 CG1 ILE A 409 39.605 43.004 -7.970 1.00 44.14 C ANISOU 3029 CG1 ILE A 409 4844 6558 5366 -9 358 -161 C ATOM 3030 CG2 ILE A 409 38.180 44.240 -9.614 1.00 48.96 C ANISOU 3030 CG2 ILE A 409 5463 7172 5964 -152 227 14 C ATOM 3031 CD1 ILE A 409 39.140 43.660 -6.681 1.00 44.31 C ANISOU 3031 CD1 ILE A 409 4821 6497 5514 31 363 -125 C ATOM 3032 N LYS A 410 39.829 43.861 -12.624 1.00 54.44 N ANISOU 3032 N LYS A 410 6292 8109 6283 -345 260 -43 N ATOM 3033 CA LYS A 410 39.878 44.695 -13.819 1.00 57.87 C ANISOU 3033 CA LYS A 410 6756 8613 6618 -472 213 43 C ATOM 3034 C LYS A 410 38.474 45.099 -14.204 1.00 57.33 C ANISOU 3034 C LYS A 410 6690 8487 6603 -544 75 176 C ATOM 3035 O LYS A 410 37.648 44.244 -14.539 1.00 53.90 O ANISOU 3035 O LYS A 410 6304 8029 6144 -569 20 169 O ATOM 3036 CB LYS A 410 40.565 43.944 -14.960 1.00 67.00 C ANISOU 3036 CB LYS A 410 7999 9870 7586 -549 272 -45 C ATOM 3037 CG LYS A 410 40.653 44.739 -16.262 1.00 76.07 C ANISOU 3037 CG LYS A 410 9198 11105 8600 -706 226 42 C ATOM 3038 CD LYS A 410 41.868 44.345 -17.110 1.00 85.50 C ANISOU 3038 CD LYS A 410 10451 12413 9622 -763 347 -67 C ATOM 3039 CE LYS A 410 41.901 42.851 -17.416 1.00 87.87 C ANISOU 3039 CE LYS A 410 10824 12720 9841 -750 413 -214 C ATOM 3040 NZ LYS A 410 42.764 42.519 -18.580 1.00 90.26 N ANISOU 3040 NZ LYS A 410 11209 13133 9953 -855 517 -306 N ATOM 3041 N GLU A 411 38.187 46.398 -14.124 1.00 57.94 N ANISOU 3041 N GLU A 411 6708 8532 6775 -574 15 302 N ATOM 3042 CA GLU A 411 36.826 46.927 -14.347 1.00 56.88 C ANISOU 3042 CA GLU A 411 6543 8317 6750 -630 -121 447 C ATOM 3043 C GLU A 411 35.771 46.149 -13.575 1.00 55.83 C ANISOU 3043 C GLU A 411 6387 8084 6740 -551 -142 427 C ATOM 3044 O GLU A 411 34.719 45.796 -14.134 1.00 55.20 O ANISOU 3044 O GLU A 411 6331 7971 6672 -615 -247 498 O ATOM 3045 CB GLU A 411 36.477 46.954 -15.851 1.00 63.85 C ANISOU 3045 CB GLU A 411 7502 9264 7491 -797 -228 536 C ATOM 3046 CG GLU A 411 37.248 48.000 -16.640 1.00 70.36 C ANISOU 3046 CG GLU A 411 8335 10172 8223 -901 -238 606 C ATOM 3047 CD GLU A 411 36.951 49.415 -16.148 1.00 74.96 C ANISOU 3047 CD GLU A 411 8811 10675 8995 -885 -296 737 C ATOM 3048 OE1 GLU A 411 35.772 49.829 -16.202 1.00 82.40 O ANISOU 3048 OE1 GLU A 411 9704 11522 10080 -919 -420 867 O ATOM 3049 OE2 GLU A 411 37.884 50.097 -15.667 1.00 72.19 O ANISOU 3049 OE2 GLU A 411 8416 10344 8666 -835 -216 707 O ATOM 3050 N PHE A 412 36.068 45.896 -12.296 1.00 54.26 N ANISOU 3050 N PHE A 412 6146 7839 6629 -423 -48 337 N ATOM 3051 CA PHE A 412 35.179 45.220 -11.321 1.00 50.89 C ANISOU 3051 CA PHE A 412 5689 7316 6328 -338 -44 309 C ATOM 3052 C PHE A 412 35.131 43.706 -11.487 1.00 51.53 C ANISOU 3052 C PHE A 412 5841 7423 6312 -321 -31 210 C ATOM 3053 O PHE A 412 34.574 43.022 -10.645 1.00 50.01 O ANISOU 3053 O PHE A 412 5632 7165 6204 -249 -17 173 O ATOM 3054 CB PHE A 412 33.744 45.757 -11.353 1.00 51.52 C ANISOU 3054 CB PHE A 412 5709 7293 6570 -371 -148 443 C ATOM 3055 CG PHE A 412 33.633 47.221 -11.108 1.00 50.94 C ANISOU 3055 CG PHE A 412 5552 7164 6637 -380 -163 539 C ATOM 3056 CD1 PHE A 412 33.925 47.750 -9.869 1.00 48.49 C ANISOU 3056 CD1 PHE A 412 5186 6798 6439 -289 -68 491 C ATOM 3057 CD2 PHE A 412 33.186 48.067 -12.100 1.00 53.31 C ANISOU 3057 CD2 PHE A 412 5832 7458 6965 -487 -279 684 C ATOM 3058 CE1 PHE A 412 33.818 49.123 -9.638 1.00 51.22 C ANISOU 3058 CE1 PHE A 412 5454 7080 6924 -298 -76 571 C ATOM 3059 CE2 PHE A 412 33.042 49.433 -11.868 1.00 53.96 C ANISOU 3059 CE2 PHE A 412 5825 7471 7203 -493 -299 778 C ATOM 3060 CZ PHE A 412 33.364 49.966 -10.640 1.00 49.74 C ANISOU 3060 CZ PHE A 412 5234 6878 6783 -395 -191 716 C ATOM 3061 N HIS A 413 35.711 43.181 -12.563 1.00 53.33 N ANISOU 3061 N HIS A 413 6151 7745 6366 -392 -29 165 N ATOM 3062 CA HIS A 413 35.758 41.736 -12.772 1.00 55.67 C ANISOU 3062 CA HIS A 413 6518 8062 6572 -378 -7 57 C ATOM 3063 C HIS A 413 36.918 41.173 -11.976 1.00 48.20 C ANISOU 3063 C HIS A 413 5561 7137 5616 -275 118 -78 C ATOM 3064 O HIS A 413 38.055 41.569 -12.171 1.00 49.01 O ANISOU 3064 O HIS A 413 5662 7307 5653 -280 190 -118 O ATOM 3065 CB HIS A 413 35.959 41.389 -14.253 1.00 55.42 C ANISOU 3065 CB HIS A 413 6586 8118 6353 -505 -37 45 C ATOM 3066 CG HIS A 413 35.793 39.937 -14.559 1.00 60.62 C ANISOU 3066 CG HIS A 413 7321 8778 6932 -505 -28 -57 C ATOM 3067 ND1 HIS A 413 36.520 39.294 -15.539 1.00 70.51 N ANISOU 3067 ND1 HIS A 413 8668 10114 8007 -573 27 -158 N ATOM 3068 CD2 HIS A 413 34.962 39.001 -14.039 1.00 63.74 C ANISOU 3068 CD2 HIS A 413 7715 9098 7403 -452 -66 -77 C ATOM 3069 CE1 HIS A 413 36.133 38.030 -15.623 1.00 67.89 C ANISOU 3069 CE1 HIS A 413 8391 9753 7650 -561 19 -238 C ATOM 3070 NE2 HIS A 413 35.194 37.825 -14.718 1.00 63.77 N ANISOU 3070 NE2 HIS A 413 7812 9137 7280 -487 -43 -186 N ATOM 3071 N ARG A 414 36.630 40.232 -11.096 1.00 46.21 N ANISOU 3071 N ARG A 414 5297 6825 5433 -190 136 -140 N ATOM 3072 CA ARG A 414 37.669 39.643 -10.273 1.00 46.17 C ANISOU 3072 CA ARG A 414 5274 6826 5440 -99 232 -252 C ATOM 3073 C ARG A 414 38.278 38.472 -11.018 1.00 47.69 C ANISOU 3073 C ARG A 414 5531 7067 5522 -112 275 -366 C ATOM 3074 O ARG A 414 37.555 37.688 -11.636 1.00 47.77 O ANISOU 3074 O ARG A 414 5599 7064 5484 -155 223 -378 O ATOM 3075 CB ARG A 414 37.097 39.222 -8.932 1.00 44.45 C ANISOU 3075 CB ARG A 414 5015 6520 5351 -14 228 -256 C ATOM 3076 CG ARG A 414 36.529 40.416 -8.187 1.00 44.53 C ANISOU 3076 CG ARG A 414 4965 6477 5475 -5 211 -161 C ATOM 3077 CD ARG A 414 36.382 40.152 -6.698 1.00 46.31 C ANISOU 3077 CD ARG A 414 5155 6635 5804 72 247 -188 C ATOM 3078 NE ARG A 414 36.058 41.398 -6.024 1.00 44.14 N ANISOU 3078 NE ARG A 414 4829 6315 5627 74 260 -121 N ATOM 3079 CZ ARG A 414 36.417 41.738 -4.801 1.00 45.57 C ANISOU 3079 CZ ARG A 414 4984 6463 5864 117 317 -145 C ATOM 3080 NH1 ARG A 414 37.125 40.929 -4.029 1.00 45.86 N ANISOU 3080 NH1 ARG A 414 5038 6508 5878 162 355 -220 N ATOM 3081 NH2 ARG A 414 36.069 42.927 -4.351 1.00 47.85 N ANISOU 3081 NH2 ARG A 414 5232 6707 6239 107 334 -89 N ATOM 3082 N LYS A 415 39.607 38.393 -10.972 1.00 49.07 N ANISOU 3082 N LYS A 415 5691 7289 5664 -80 372 -449 N ATOM 3083 CA LYS A 415 40.377 37.318 -11.622 1.00 51.35 C ANISOU 3083 CA LYS A 415 6023 7613 5872 -82 444 -578 C ATOM 3084 C LYS A 415 41.211 36.616 -10.570 1.00 45.66 C ANISOU 3084 C LYS A 415 5245 6851 5252 27 507 -659 C ATOM 3085 O LYS A 415 41.847 37.259 -9.733 1.00 44.78 O ANISOU 3085 O LYS A 415 5068 6735 5209 74 533 -631 O ATOM 3086 CB LYS A 415 41.306 37.857 -12.719 1.00 57.55 C ANISOU 3086 CB LYS A 415 6836 8497 6532 -159 514 -604 C ATOM 3087 CG LYS A 415 40.778 39.082 -13.482 1.00 68.67 C ANISOU 3087 CG LYS A 415 8270 9954 7867 -269 446 -480 C ATOM 3088 CD LYS A 415 40.155 38.755 -14.833 1.00 79.46 C ANISOU 3088 CD LYS A 415 9741 11363 9086 -398 397 -475 C ATOM 3089 CE LYS A 415 39.888 40.048 -15.617 1.00 91.30 C ANISOU 3089 CE LYS A 415 11258 12919 10514 -519 329 -343 C ATOM 3090 NZ LYS A 415 39.635 39.880 -17.087 1.00 90.88 N ANISOU 3090 NZ LYS A 415 11319 12936 10274 -679 296 -339 N ATOM 3091 N TYR A 416 41.198 35.291 -10.623 1.00 43.60 N ANISOU 3091 N TYR A 416 5009 6555 5003 59 522 -753 N ATOM 3092 CA TYR A 416 41.782 34.472 -9.585 1.00 45.63 C ANISOU 3092 CA TYR A 416 5209 6752 5376 156 550 -813 C ATOM 3093 C TYR A 416 42.788 33.556 -10.255 1.00 47.63 C ANISOU 3093 C TYR A 416 5467 7019 5609 168 646 -947 C ATOM 3094 O TYR A 416 42.726 33.365 -11.448 1.00 49.63 O ANISOU 3094 O TYR A 416 5789 7319 5748 97 681 -1001 O ATOM 3095 CB TYR A 416 40.711 33.662 -8.858 1.00 43.12 C ANISOU 3095 CB TYR A 416 4901 6352 5130 192 468 -792 C ATOM 3096 CG TYR A 416 39.681 34.526 -8.175 1.00 43.46 C ANISOU 3096 CG TYR A 416 4931 6369 5211 182 394 -671 C ATOM 3097 CD1 TYR A 416 38.571 34.996 -8.867 1.00 42.71 C ANISOU 3097 CD1 TYR A 416 4878 6284 5064 111 329 -598 C ATOM 3098 CD2 TYR A 416 39.849 34.918 -6.847 1.00 42.49 C ANISOU 3098 CD2 TYR A 416 4751 6209 5182 235 392 -629 C ATOM 3099 CE1 TYR A 416 37.638 35.810 -8.228 1.00 41.84 C ANISOU 3099 CE1 TYR A 416 4738 6137 5021 108 274 -490 C ATOM 3100 CE2 TYR A 416 38.947 35.755 -6.219 1.00 41.63 C ANISOU 3100 CE2 TYR A 416 4629 6073 5115 223 349 -534 C ATOM 3101 CZ TYR A 416 37.842 36.200 -6.922 1.00 41.11 C ANISOU 3101 CZ TYR A 416 4590 6007 5020 166 296 -468 C ATOM 3102 OH TYR A 416 36.956 37.016 -6.274 1.00 43.92 O ANISOU 3102 OH TYR A 416 4917 6320 5449 161 265 -379 O ATOM 3103 N GLU A 417 43.695 32.987 -9.480 1.00 50.49 N ANISOU 3103 N GLU A 417 5758 7337 6088 249 689 -999 N ATOM 3104 CA GLU A 417 44.778 32.163 -10.029 1.00 53.22 C ANISOU 3104 CA GLU A 417 6081 7680 6458 272 796 -1129 C ATOM 3105 C GLU A 417 45.066 31.000 -9.068 1.00 53.50 C ANISOU 3105 C GLU A 417 6054 7615 6656 363 776 -1172 C ATOM 3106 O GLU A 417 45.102 31.195 -7.856 1.00 49.46 O ANISOU 3106 O GLU A 417 5487 7063 6240 409 714 -1095 O ATOM 3107 CB GLU A 417 46.008 33.067 -10.170 1.00 53.58 C ANISOU 3107 CB GLU A 417 6066 7788 6502 268 883 -1125 C ATOM 3108 CG GLU A 417 47.195 32.417 -10.812 1.00 61.21 C ANISOU 3108 CG GLU A 417 6995 8758 7502 284 1017 -1256 C ATOM 3109 CD GLU A 417 48.378 33.360 -11.017 1.00 61.62 C ANISOU 3109 CD GLU A 417 6984 8877 7550 272 1106 -1243 C ATOM 3110 OE1 GLU A 417 48.338 34.541 -10.629 1.00 58.79 O ANISOU 3110 OE1 GLU A 417 6611 8561 7164 251 1058 -1131 O ATOM 3111 OE2 GLU A 417 49.387 32.892 -11.554 1.00 68.59 O ANISOU 3111 OE2 GLU A 417 7824 9762 8472 284 1232 -1350 O ATOM 3112 N TRP A 418 45.254 29.804 -9.608 1.00 55.62 N ANISOU 3112 N TRP A 418 6337 7840 6954 379 826 -1292 N ATOM 3113 CA TRP A 418 45.747 28.647 -8.839 1.00 55.55 C ANISOU 3113 CA TRP A 418 6253 7728 7122 463 819 -1342 C ATOM 3114 C TRP A 418 47.248 28.733 -8.693 1.00 55.39 C ANISOU 3114 C TRP A 418 6125 7701 7216 509 914 -1384 C ATOM 3115 O TRP A 418 47.936 28.854 -9.673 1.00 57.72 O ANISOU 3115 O TRP A 418 6422 8043 7464 483 1037 -1472 O ATOM 3116 CB TRP A 418 45.422 27.344 -9.567 1.00 56.31 C ANISOU 3116 CB TRP A 418 6402 7771 7223 461 847 -1466 C ATOM 3117 CG TRP A 418 43.966 27.084 -9.624 1.00 54.86 C ANISOU 3117 CG TRP A 418 6311 7576 6957 421 739 -1421 C ATOM 3118 CD1 TRP A 418 43.150 27.231 -10.696 1.00 55.34 C ANISOU 3118 CD1 TRP A 418 6483 7689 6853 334 735 -1439 C ATOM 3119 CD2 TRP A 418 43.144 26.656 -8.549 1.00 51.34 C ANISOU 3119 CD2 TRP A 418 5853 7062 6592 458 615 -1339 C ATOM 3120 NE1 TRP A 418 41.867 26.915 -10.358 1.00 55.69 N ANISOU 3120 NE1 TRP A 418 6576 7696 6888 321 613 -1370 N ATOM 3121 CE2 TRP A 418 41.841 26.547 -9.042 1.00 50.75 C ANISOU 3121 CE2 TRP A 418 5874 6997 6410 399 546 -1314 C ATOM 3122 CE3 TRP A 418 43.392 26.324 -7.220 1.00 50.47 C ANISOU 3122 CE3 TRP A 418 5661 6882 6633 524 552 -1282 C ATOM 3123 CZ2 TRP A 418 40.795 26.129 -8.266 1.00 51.35 C ANISOU 3123 CZ2 TRP A 418 5959 7017 6534 412 431 -1239 C ATOM 3124 CZ3 TRP A 418 42.353 25.906 -6.446 1.00 51.22 C ANISOU 3124 CZ3 TRP A 418 5776 6926 6757 529 439 -1210 C ATOM 3125 CH2 TRP A 418 41.063 25.823 -6.961 1.00 50.26 C ANISOU 3125 CH2 TRP A 418 5744 6817 6536 478 385 -1191 C ATOM 3126 N VAL A 419 47.758 28.658 -7.479 1.00 56.05 N ANISOU 3126 N VAL A 419 6117 7726 7452 569 856 -1318 N ATOM 3127 CA VAL A 419 49.184 28.787 -7.240 1.00 61.89 C ANISOU 3127 CA VAL A 419 6741 8451 8322 609 925 -1333 C ATOM 3128 C VAL A 419 49.726 27.660 -6.355 1.00 68.27 C ANISOU 3128 C VAL A 419 7450 9136 9354 683 878 -1343 C ATOM 3129 O VAL A 419 50.951 27.555 -6.242 1.00 67.26 O ANISOU 3129 O VAL A 419 7209 8973 9373 721 937 -1365 O ATOM 3130 CB VAL A 419 49.537 30.139 -6.576 1.00 62.01 C ANISOU 3130 CB VAL A 419 6725 8525 8308 590 889 -1210 C ATOM 3131 CG1 VAL A 419 49.212 31.296 -7.514 1.00 63.49 C ANISOU 3131 CG1 VAL A 419 6989 8829 8305 517 942 -1198 C ATOM 3132 CG2 VAL A 419 48.813 30.299 -5.245 1.00 58.05 C ANISOU 3132 CG2 VAL A 419 6240 7988 7829 593 746 -1091 C ATOM 3133 OXT VAL A 419 48.989 26.873 -5.728 1.00 69.97 O ANISOU 3133 OXT VAL A 419 7686 9280 9618 701 776 -1317 O TER 3134 VAL A 419 HETATM 3135 S SO4 A 501 15.714 13.365 19.344 1.00120.73 S HETATM 3136 O1 SO4 A 501 16.314 14.723 19.403 1.00106.13 O HETATM 3137 O2 SO4 A 501 15.810 12.796 17.973 1.00100.63 O HETATM 3138 O3 SO4 A 501 16.409 12.501 20.315 1.00124.18 O HETATM 3139 O4 SO4 A 501 14.294 13.423 19.759 1.00135.03 O HETATM 3140 O HOH A 601 11.960 36.322 24.183 1.00 63.72 O HETATM 3141 O HOH A 602 32.562 41.083 -10.118 1.00 54.89 O HETATM 3142 O HOH A 603 38.577 19.490 -8.337 1.00 66.12 O HETATM 3143 O HOH A 604 17.911 31.250 32.140 1.00 88.95 O HETATM 3144 O HOH A 605 37.502 35.425 -12.958 1.00 52.70 O HETATM 3145 O HOH A 606 9.338 31.077 22.839 1.00 64.57 O HETATM 3146 O HOH A 607 31.907 10.617 -6.393 1.00 62.79 O HETATM 3147 O HOH A 608 48.714 40.090 -9.386 1.00 50.12 O HETATM 3148 O HOH A 609 14.405 19.686 26.804 1.00 62.07 O HETATM 3149 O HOH A 610 37.130 12.853 13.267 1.00 60.51 O HETATM 3150 O HOH A 611 32.117 15.949 -14.305 1.00 89.93 O HETATM 3151 O HOH A 612 44.605 33.919 5.015 1.00 55.66 O HETATM 3152 O HOH A 613 19.958 11.420 21.584 1.00 61.70 O HETATM 3153 O HOH A 614 49.550 30.237 -11.135 1.00 76.07 O HETATM 3154 O HOH A 615 23.202 12.629 -5.029 1.00 61.43 O HETATM 3155 O HOH A 616 42.323 32.361 -0.613 1.00 49.99 O HETATM 3156 O HOH A 617 25.868 38.372 1.379 1.00 44.43 O HETATM 3157 O HOH A 618 25.236 9.846 10.641 1.00 82.47 O HETATM 3158 O HOH A 619 28.909 13.504 25.871 1.00 62.34 O HETATM 3159 O HOH A 620 38.984 18.509 3.521 1.00 52.04 O HETATM 3160 O HOH A 621 51.418 35.251 15.595 1.00 57.99 O HETATM 3161 O HOH A 622 52.854 37.567 0.326 1.00 54.94 O HETATM 3162 O HOH A 623 57.376 30.968 5.360 1.00 77.55 O HETATM 3163 O HOH A 624 29.526 26.288 36.157 1.00 68.63 O HETATM 3164 O HOH A 625 25.571 12.827 -13.129 1.00 70.33 O HETATM 3165 O HOH A 626 30.937 23.497 21.169 1.00 45.17 O HETATM 3166 O HOH A 627 19.808 11.869 12.354 1.00 62.24 O HETATM 3167 O HOH A 628 39.979 15.686 -1.938 1.00 70.59 O HETATM 3168 O HOH A 629 17.262 41.355 22.434 1.00 52.99 O HETATM 3169 O HOH A 630 32.792 45.991 -5.012 1.00 52.53 O HETATM 3170 O HOH A 631 35.234 45.297 -6.533 1.00 48.75 O HETATM 3171 O HOH A 632 14.625 21.467 6.972 1.00 55.20 O HETATM 3172 O HOH A 633 34.484 43.197 -7.976 1.00 56.59 O HETATM 3173 O HOH A 634 35.646 16.794 2.553 1.00 52.04 O HETATM 3174 O HOH A 635 41.799 20.405 6.188 1.00 54.02 O HETATM 3175 O HOH A 636 22.766 9.663 21.585 1.00 71.08 O HETATM 3176 O HOH A 637 28.179 6.666 8.393 1.00 64.25 O HETATM 3177 O HOH A 638 47.389 34.317 22.086 1.00 70.11 O HETATM 3178 O HOH A 639 31.020 29.952 -14.808 1.00 52.31 O HETATM 3179 O HOH A 640 40.961 38.417 10.670 1.00 55.80 O HETATM 3180 O HOH A 641 40.176 16.665 10.334 1.00 52.47 O HETATM 3181 O HOH A 642 33.190 52.085 5.094 1.00 82.87 O HETATM 3182 O HOH A 643 15.392 24.373 -1.452 1.00 47.68 O HETATM 3183 O HOH A 644 11.187 13.289 1.315 1.00 70.20 O HETATM 3184 O HOH A 645 17.151 47.112 18.878 1.00 61.48 O HETATM 3185 O HOH A 646 25.652 10.248 -6.065 1.00 65.05 O HETATM 3186 O HOH A 647 43.760 41.810 3.697 1.00 62.87 O HETATM 3187 O HOH A 648 33.899 16.968 32.226 1.00 54.89 O HETATM 3188 O HOH A 649 31.476 20.106 21.322 1.00 45.48 O HETATM 3189 O HOH A 650 33.392 15.076 -1.745 1.00 56.43 O HETATM 3190 O HOH A 651 14.721 19.357 9.069 1.00 49.83 O HETATM 3191 O HOH A 652 34.568 41.103 0.954 1.00 53.64 O HETATM 3192 O HOH A 653 17.523 18.894 12.547 1.00 50.66 O HETATM 3193 O HOH A 654 27.513 35.267 7.198 1.00 46.40 O HETATM 3194 O HOH A 655 21.073 13.568 -3.264 1.00 51.45 O HETATM 3195 O HOH A 656 28.609 10.281 10.277 1.00 56.74 O HETATM 3196 O HOH A 657 40.505 8.317 9.609 1.00 76.53 O HETATM 3197 O HOH A 658 46.790 27.177 15.106 1.00 63.02 O HETATM 3198 O HOH A 659 27.927 17.401 34.663 1.00 69.40 O HETATM 3199 O HOH A 660 38.955 23.495 -10.333 1.00 56.59 O HETATM 3200 O HOH A 661 27.213 39.521 12.456 1.00 62.62 O HETATM 3201 O HOH A 662 23.366 10.657 -13.043 1.00 89.82 O HETATM 3202 O HOH A 663 36.044 16.878 27.031 1.00 52.99 O HETATM 3203 O HOH A 664 27.892 20.689 -11.058 1.00 51.93 O HETATM 3204 O HOH A 665 18.764 22.946 -7.895 1.00 49.80 O HETATM 3205 O HOH A 666 25.259 30.672 13.309 1.00 46.27 O HETATM 3206 O HOH A 667 35.966 17.197 11.518 1.00 55.75 O HETATM 3207 O HOH A 668 31.118 20.899 -15.300 1.00 69.42 O HETATM 3208 O HOH A 669 5.653 26.445 14.822 1.00 72.45 O HETATM 3209 O HOH A 670 34.357 9.972 -12.949 1.00 88.11 O HETATM 3210 O HOH A 671 42.777 24.918 -2.492 1.00 61.70 O HETATM 3211 O HOH A 672 29.018 26.616 31.065 1.00 50.46 O HETATM 3212 O HOH A 673 29.193 15.468 32.622 1.00 75.00 O HETATM 3213 O HOH A 674 38.904 20.434 5.644 1.00 51.56 O HETATM 3214 O HOH A 675 21.405 11.154 -10.992 1.00 83.28 O HETATM 3215 O HOH A 676 18.233 12.008 7.645 1.00 54.02 O HETATM 3216 O HOH A 677 21.715 43.778 -2.303 1.00 37.80 O HETATM 3217 O HOH A 678 43.878 21.727 16.844 1.00 59.42 O HETATM 3218 O HOH A 679 29.886 7.503 6.779 1.00 59.09 O HETATM 3219 O HOH A 680 37.518 43.085 -17.102 1.00 63.28 O HETATM 3220 O HOH A 681 30.605 25.877 19.853 1.00 49.87 O HETATM 3221 O HOH A 682 35.292 31.570 17.360 1.00 55.70 O HETATM 3222 O HOH A 683 15.364 16.691 -5.209 1.00 55.46 O HETATM 3223 O HOH A 684 34.652 16.114 6.943 1.00 58.34 O HETATM 3224 O HOH A 685 45.248 17.116 11.492 1.00 63.56 O HETATM 3225 O HOH A 686 25.168 29.619 10.456 1.00 55.80 O HETATM 3226 O HOH A 687 15.641 19.809 28.999 1.00 58.26 O HETATM 3227 O HOH A 688 18.287 12.921 -3.989 1.00 55.28 O HETATM 3228 O HOH A 689 24.878 37.085 6.147 1.00 41.69 O HETATM 3229 O HOH A 690 40.267 14.978 21.898 1.00 54.85 O HETATM 3230 O HOH A 691 17.370 20.275 10.100 1.00 51.34 O HETATM 3231 O HOH A 692 36.679 17.026 9.017 1.00 53.71 O HETATM 3232 O HOH A 693 48.294 28.582 14.037 1.00 73.26 O HETATM 3233 O HOH A 694 36.910 15.493 24.139 1.00 67.60 O HETATM 3234 O HOH A 695 31.716 9.538 -13.278 1.00 76.05 O HETATM 3235 O HOH A 696 24.040 19.884 -13.461 1.00 67.85 O HETATM 3236 O HOH A 697 13.693 22.201 -6.863 1.00 48.89 O HETATM 3237 O HOH A 698 37.046 18.994 7.072 1.00 55.93 O HETATM 3238 O HOH A 699 39.930 21.526 33.470 1.00 55.14 O HETATM 3239 O HOH A 700 27.940 30.430 12.690 1.00 41.94 O HETATM 3240 O HOH A 701 22.166 25.032 22.927 1.00 52.49 O HETATM 3241 O HOH A 702 42.573 25.374 20.422 1.00 70.82 O HETATM 3242 O HOH A 703 9.897 15.854 -9.830 1.00 70.93 O HETATM 3243 O HOH A 704 55.057 40.407 17.407 1.00 79.62 O HETATM 3244 O HOH A 705 51.133 21.361 10.280 1.00 71.19 O HETATM 3245 O HOH A 706 21.908 32.050 34.590 1.00 89.22 O HETATM 3246 O HOH A 707 34.715 5.533 7.531 1.00 69.47 O HETATM 3247 O HOH A 708 28.574 39.287 -3.641 1.00 42.58 O HETATM 3248 O HOH A 709 31.777 32.910 30.643 1.00 84.33 O HETATM 3249 O HOH A 710 55.406 31.283 10.701 1.00 67.24 O HETATM 3250 O HOH A 711 31.638 12.867 -1.531 1.00 56.73 O HETATM 3251 O HOH A 712 25.879 37.792 13.878 1.00 50.89 O HETATM 3252 O HOH A 713 9.774 29.661 20.723 1.00 49.90 O HETATM 3253 O HOH A 714 24.661 13.581 27.448 1.00 65.33 O HETATM 3254 O HOH A 715 40.307 32.977 19.087 1.00 53.01 O HETATM 3255 O HOH A 716 22.690 42.116 11.446 1.00 53.94 O HETATM 3256 O HOH A 717 15.576 12.010 10.591 1.00 62.14 O HETATM 3257 O HOH A 718 34.239 15.284 4.361 1.00 50.54 O HETATM 3258 O HOH A 719 23.900 23.834 20.818 1.00 56.56 O HETATM 3259 O HOH A 720 28.476 22.958 42.576 1.00 71.94 O HETATM 3260 O HOH A 721 27.768 22.805 -18.276 1.00 55.24 O HETATM 3261 O HOH A 722 56.408 42.687 15.573 1.00 76.16 O HETATM 3262 O HOH A 723 30.601 26.399 33.346 1.00 61.63 O HETATM 3263 O HOH A 724 40.341 51.396 -9.431 1.00 76.52 O HETATM 3264 O HOH A 725 32.494 1.485 16.143 1.00 83.77 O HETATM 3265 O HOH A 726 41.256 39.672 -19.581 1.00 66.15 O HETATM 3266 O HOH A 727 56.640 33.586 10.871 1.00 86.34 O HETATM 3267 O HOH A 728 27.505 37.142 16.271 1.00 66.99 O HETATM 3268 O HOH A 729 33.096 12.932 2.857 1.00 62.16 O HETATM 3269 O HOH A 730 41.908 17.281 -2.234 1.00 77.32 O HETATM 3270 O HOH A 731 45.324 29.414 -12.595 1.00 60.41 O HETATM 3271 O HOH A 732 37.665 21.994 -8.905 1.00 66.92 O HETATM 3272 O HOH A 733 13.801 32.436 31.307 1.00 85.01 O HETATM 3273 O HOH A 734 37.485 32.292 18.944 1.00 56.58 O HETATM 3274 O HOH A 735 24.049 47.846 16.020 1.00 80.05 O HETATM 3275 O HOH A 736 29.763 47.745 22.646 1.00 78.72 O HETATM 3276 O HOH A 737 7.740 27.999 21.059 1.00 73.36 O HETATM 3277 O HOH A 738 42.529 17.023 12.250 1.00 75.59 O HETATM 3278 O HOH A 739 46.516 49.997 0.860 1.00 78.16 O HETATM 3279 O HOH A 740 30.641 7.921 -11.804 1.00 88.68 O HETATM 3280 O HOH A 741 46.738 40.385 -13.742 1.00 58.76 O HETATM 3281 O HOH A 742 40.016 27.111 -12.883 1.00 58.09 O HETATM 3282 O HOH A 743 40.639 38.872 7.962 1.00 61.19 O HETATM 3283 O HOH A 744 52.001 33.239 -9.714 1.00 82.73 O HETATM 3284 O HOH A 745 31.229 7.058 2.833 1.00 80.08 O HETATM 3285 O HOH A 746 7.325 26.132 26.057 1.00 86.68 O HETATM 3286 O HOH A 747 28.471 11.498 31.169 1.00 81.72 O HETATM 3287 O HOH A 748 28.154 28.674 37.301 1.00 80.17 O HETATM 3288 O HOH A 749 19.319 15.104 -11.120 1.00 89.61 O HETATM 3289 O HOH A 750 49.990 25.777 -9.275 1.00 84.63 O HETATM 3290 O HOH A 751 25.470 42.318 10.688 1.00 75.64 O HETATM 3291 O HOH A 752 9.266 15.415 13.057 1.00 85.05 O HETATM 3292 O HOH A 753 9.057 13.856 17.565 1.00 80.28 O HETATM 3293 O HOH A 754 22.378 8.435 19.343 1.00 80.08 O HETATM 3294 O HOH A 755 43.741 29.040 25.979 1.00 83.17 O HETATM 3295 O HOH A 756 27.918 12.840 -15.791 1.00 85.48 O CONECT 3135 3136 3137 3138 3139 CONECT 3136 3135 CONECT 3137 3135 CONECT 3138 3135 CONECT 3139 3135 MASTER 439 0 1 18 17 0 1 6 3294 1 5 35 END If you find results from this site helpful for your research, please cite one of our papers:
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