HEADER MEMBRANE PROTEIN 10-DEC-19 6LI2 TITLE CRYSTAL STRUCTURE OF GPR52 LIGAND FREE FORM WITH RUBREDOXIN FUSION COMPND MOL_ID: 1; COMPND 2 MOLECULE: CHIMERA OF G-PROTEIN COUPLED RECEPTOR 52 AND RUBREDOXIN; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: RD; COMPND 5 ENGINEERED: YES; COMPND 6 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, CLOSTRIDIUM PASTEURIANUM; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606, 1501; SOURCE 5 GENE: GPR52; SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: F9 KEYWDS HUMAN GPR52 RECEPTOR, CLASS A, ORPHAN GPCR, MEMBRANE PROTEIN, APO KEYWDS 2 FORM, RUBREDOXIN, LCP EXPDTA X-RAY DIFFRACTION AUTHOR Z.P.LUO,X.LIN,F.XU,G.W.HAN REVDAT 3 18-MAR-20 6LI2 1 JRNL REVDAT 2 04-MAR-20 6LI2 1 JRNL REVDAT 1 26-FEB-20 6LI2 0 JRNL AUTH X.LIN,M.LI,N.WANG,Y.WU,Z.LUO,S.GUO,G.W.HAN,S.LI,Y.YUE,X.WEI, JRNL AUTH 2 X.XIE,Y.CHEN,S.ZHAO,J.WU,M.LEI,F.XU JRNL TITL STRUCTURAL BASIS OF LIGAND RECOGNITION AND SELF-ACTIVATION JRNL TITL 2 OF ORPHAN GPR52. JRNL REF NATURE V. 579 152 2020 JRNL REFN ESSN 1476-4687 JRNL PMID 32076264 JRNL DOI 10.1038/S41586-020-2019-0 REMARK 2 REMARK 2 RESOLUTION. 2.80 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.8.0253 REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER, REMARK 3 : NICHOLLS,WINN,LONG,VAGIN REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.25 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 81.1 REMARK 3 NUMBER OF REFLECTIONS : 11830 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) : 0.242 REMARK 3 R VALUE (WORKING SET) : 0.241 REMARK 3 FREE R VALUE : 0.263 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900 REMARK 3 FREE R VALUE TEST SET COUNT : 612 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) : 2.80 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.87 REMARK 3 REFLECTION IN BIN (WORKING SET) : 566 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 53.00 REMARK 3 BIN R VALUE (WORKING SET) : 0.2580 REMARK 3 BIN FREE R VALUE SET COUNT : 26 REMARK 3 BIN FREE R VALUE : 0.2720 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 2761 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 177 REMARK 3 SOLVENT ATOMS : 18 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 47.78 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 61.37 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 2.26000 REMARK 3 B22 (A**2) : -3.97000 REMARK 3 B33 (A**2) : 1.71000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 16.343 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.401 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.315 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 32.117 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.889 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.892 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3015 ; 0.008 ; 0.013 REMARK 3 BOND LENGTHS OTHERS (A): 2798 ; 0.007 ; 0.017 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4069 ; 1.440 ; 1.689 REMARK 3 BOND ANGLES OTHERS (DEGREES): 6475 ; 0.805 ; 1.666 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 345 ; 4.494 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 123 ;34.237 ;21.545 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 433 ;16.099 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 10 ;14.948 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 393 ; 0.073 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3178 ; 0.042 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 660 ; 0.036 ; 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): 1386 ; 8.562 ; 9.930 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1385 ; 8.537 ; 9.933 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1729 ;11.818 ;18.623 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1730 ;11.827 ;18.625 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1629 ; 9.052 ;11.456 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1630 ; 9.049 ;11.455 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 2341 ;12.484 ;20.757 REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 49693 ;18.218 ; NULL REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 49688 ;18.218 ; 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 : 3 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 23 A 235 REMARK 3 ORIGIN FOR THE GROUP (A): 5.7104 20.6519 37.6473 REMARK 3 T TENSOR REMARK 3 T11: 0.0684 T22: 0.3205 REMARK 3 T33: 0.0062 T12: -0.0378 REMARK 3 T13: 0.0011 T23: -0.0056 REMARK 3 L TENSOR REMARK 3 L11: 0.4022 L22: 0.4206 REMARK 3 L33: 1.0024 L12: -0.2062 REMARK 3 L13: -0.1189 L23: 0.4029 REMARK 3 S TENSOR REMARK 3 S11: -0.0350 S12: 0.0063 S13: 0.0030 REMARK 3 S21: 0.0847 S22: -0.0273 S23: 0.0019 REMARK 3 S31: 0.1184 S32: -0.1444 S33: 0.0623 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 1001 A 1054 REMARK 3 ORIGIN FOR THE GROUP (A): 23.0352 34.5562 69.9635 REMARK 3 T TENSOR REMARK 3 T11: 0.0563 T22: 0.3297 REMARK 3 T33: 0.0306 T12: -0.0306 REMARK 3 T13: -0.0266 T23: 0.0171 REMARK 3 L TENSOR REMARK 3 L11: 1.3930 L22: 0.2524 REMARK 3 L33: 3.9739 L12: 0.3127 REMARK 3 L13: -1.1322 L23: 0.1753 REMARK 3 S TENSOR REMARK 3 S11: 0.0520 S12: 0.0569 S13: -0.0037 REMARK 3 S21: -0.0188 S22: -0.0510 S23: 0.0491 REMARK 3 S31: -0.0281 S32: 0.0843 S33: -0.0010 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 263 A 605 REMARK 3 ORIGIN FOR THE GROUP (A): 16.6934 26.2174 41.3018 REMARK 3 T TENSOR REMARK 3 T11: 0.0812 T22: 0.3231 REMARK 3 T33: 0.0796 T12: -0.0079 REMARK 3 T13: 0.0327 T23: 0.0263 REMARK 3 L TENSOR REMARK 3 L11: 1.0906 L22: 0.1786 REMARK 3 L33: 2.0785 L12: 0.3888 REMARK 3 L13: 1.0534 L23: 0.3703 REMARK 3 S TENSOR REMARK 3 S11: -0.0525 S12: -0.0652 S13: -0.0372 REMARK 3 S21: -0.0156 S22: -0.0662 S23: -0.0616 REMARK 3 S31: 0.2166 S32: -0.2529 S33: 0.1187 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : BABINET MODEL WITH MASK 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: REMARK 3 HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS REMARK 3 REMARK 3 REMARK 3 AUTHORS ANISO-CORRECTED THE OBSERVED DATA BY STARANISO WHICH REMARK 3 REMOVE WEAK REFLECTIONS. REMARK 4 REMARK 4 6LI2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 11-DEC-19. REMARK 100 THE DEPOSITION ID IS D_1300013683. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 01-JUL-19 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SPRING-8 REMARK 200 BEAMLINE : BL41XU REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.000 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15032 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 96.9 REMARK 200 DATA REDUNDANCY : 8.200 REMARK 200 R MERGE (I) : 0.16400 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 13.2000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90 REMARK 200 COMPLETENESS FOR SHELL (%) : 96.1 REMARK 200 DATA REDUNDANCY IN SHELL : 8.00 REMARK 200 R MERGE FOR SHELL (I) : 0.96700 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.700 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: ROSETTA MODELLING REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 67.90 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.83 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.08-0.1 M MAGNESIUM SULPHATE, 0.1 M REMARK 280 SODIUM CACODYLATE TRIHYDRATE PH 6.2, AND 28-31% PEG300, LIPIDIC REMARK 280 CUBIC PHASE, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z REMARK 290 3555 -X,Y,-Z REMARK 290 4555 X,-Y,-Z REMARK 290 5555 X+1/2,Y+1/2,Z+1/2 REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2 REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2 REMARK 290 8555 X+1/2,-Y+1/2,-Z+1/2 REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 38.61150 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 56.61450 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 69.30750 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 38.61150 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 56.61450 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 69.30750 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 38.61150 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 56.61450 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 69.30750 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 38.61150 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 56.61450 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 69.30750 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 300 REMARK: AUTHORS STATE THAT THE BIOLOGICAL UNIT IS UNKNOWN. 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 110 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19130 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 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 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 GLY A 16 REMARK 465 GLY A 17 REMARK 465 ILE A 18 REMARK 465 VAL A 19 REMARK 465 ASN A 20 REMARK 465 VAL A 21 REMARK 465 SER A 22 REMARK 465 ALA A 68 REMARK 465 PRO A 69 REMARK 465 LEU A 70 REMARK 465 LEU A 606 REMARK 465 PHE A 607 REMARK 465 GLN A 608 REMARK 465 GLY A 609 REMARK 465 PRO A 610 REMARK 465 HIS A 611 REMARK 465 HIS A 612 REMARK 465 HIS A 613 REMARK 465 HIS A 614 REMARK 465 HIS A 615 REMARK 465 HIS A 616 REMARK 465 HIS A 617 REMARK 465 HIS A 618 REMARK 465 HIS A 619 REMARK 465 HIS A 620 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 VAL A 36 CG1 CG2 REMARK 470 LEU A 71 CG CD1 CD2 REMARK 470 SER A 105 OG REMARK 470 LYS A 145 CG CD CE NZ REMARK 470 LYS A1002 CG CD CE NZ REMARK 470 ASP A1036 CG OD1 OD2 REMARK 470 GLU A 601 CG CD OE1 OE2 REMARK 470 PHE A 602 CG CD1 CD2 CE1 CE2 CZ 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 PHE A 31 109.90 -38.65 REMARK 500 HIS A 72 -113.51 -139.54 REMARK 500 TYR A 74 -63.91 72.11 REMARK 500 ASP A 188 4.07 -68.53 REMARK 500 LEU A 211 -63.85 -139.86 REMARK 500 CYS A1042 -13.01 -146.81 REMARK 500 REMARK 500 REMARK: NULL REMARK 610 REMARK 610 MISSING HETEROATOM REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 610 I=INSERTION CODE): REMARK 610 M RES C SSEQI REMARK 610 OLC A 1202 REMARK 610 OLC A 1203 REMARK 610 OLC A 1204 REMARK 610 OLC A 1205 REMARK 610 OLC A 1206 REMARK 610 OLC A 1207 REMARK 610 OLC A 1208 REMARK 610 OLC A 1209 REMARK 610 OLC A 1210 REMARK 610 OLC A 1211 REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN A1201 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A1006 SG REMARK 620 2 CYS A1009 SG 103.7 REMARK 620 3 CYS A1039 SG 106.4 114.6 REMARK 620 4 CYS A1042 SG 111.8 114.5 105.6 REMARK 620 N 1 2 3 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1201 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1202 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1203 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1204 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1205 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1206 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1207 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1208 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1210 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1211 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1212 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 1213 DBREF 6LI2 A 17 235 UNP Q9Y2T5 GPR52_HUMAN 17 235 DBREF 6LI2 A 1002 1054 UNP P00268 RUBR_CLOPA 2 54 DBREF 6LI2 A 265 340 UNP Q9Y2T5 GPR52_HUMAN 265 340 SEQADV 6LI2 GLY A 16 UNP Q9Y2T5 EXPRESSION TAG SEQADV 6LI2 TRP A 130 UNP Q9Y2T5 ALA 130 CONFLICT SEQADV 6LI2 MET A 1001 UNP Q9Y2T5 LINKER SEQADV 6LI2 TYR A 263 UNP P00268 LINKER SEQADV 6LI2 LEU A 264 UNP P00268 LINKER SEQADV 6LI2 GLN A 278 UNP Q9Y2T5 TRP 278 ENGINEERED MUTATION SEQADV 6LI2 PRO A 314 UNP Q9Y2T5 CYS 314 ENGINEERED MUTATION SEQADV 6LI2 ALA A 318 UNP Q9Y2T5 SER 318 ENGINEERED MUTATION SEQADV 6LI2 ASP A 321 UNP Q9Y2T5 ASN 321 ENGINEERED MUTATION SEQADV 6LI2 THR A 323 UNP Q9Y2T5 VAL 323 ENGINEERED MUTATION SEQADV 6LI2 GLU A 601 UNP Q9Y2T5 EXPRESSION TAG SEQADV 6LI2 PHE A 602 UNP Q9Y2T5 EXPRESSION TAG SEQADV 6LI2 LEU A 603 UNP Q9Y2T5 EXPRESSION TAG SEQADV 6LI2 GLU A 604 UNP Q9Y2T5 EXPRESSION TAG SEQADV 6LI2 VAL A 605 UNP Q9Y2T5 EXPRESSION TAG SEQADV 6LI2 LEU A 606 UNP Q9Y2T5 EXPRESSION TAG SEQADV 6LI2 PHE A 607 UNP Q9Y2T5 EXPRESSION TAG SEQADV 6LI2 GLN A 608 UNP Q9Y2T5 EXPRESSION TAG SEQADV 6LI2 GLY A 609 UNP Q9Y2T5 EXPRESSION TAG SEQADV 6LI2 PRO A 610 UNP Q9Y2T5 EXPRESSION TAG SEQADV 6LI2 HIS A 611 UNP Q9Y2T5 EXPRESSION TAG SEQADV 6LI2 HIS A 612 UNP Q9Y2T5 EXPRESSION TAG SEQADV 6LI2 HIS A 613 UNP Q9Y2T5 EXPRESSION TAG SEQADV 6LI2 HIS A 614 UNP Q9Y2T5 EXPRESSION TAG SEQADV 6LI2 HIS A 615 UNP Q9Y2T5 EXPRESSION TAG SEQADV 6LI2 HIS A 616 UNP Q9Y2T5 EXPRESSION TAG SEQADV 6LI2 HIS A 617 UNP Q9Y2T5 EXPRESSION TAG SEQADV 6LI2 HIS A 618 UNP Q9Y2T5 EXPRESSION TAG SEQADV 6LI2 HIS A 619 UNP Q9Y2T5 EXPRESSION TAG SEQADV 6LI2 HIS A 620 UNP Q9Y2T5 EXPRESSION TAG SEQRES 1 A 372 GLY GLY ILE VAL ASN VAL SER GLU ARG HIS SER CYS PRO SEQRES 2 A 372 LEU GLY PHE GLY HIS TYR SER VAL VAL ASP VAL CYS ILE SEQRES 3 A 372 PHE GLU THR VAL VAL ILE VAL LEU LEU THR PHE LEU ILE SEQRES 4 A 372 ILE ALA GLY ASN LEU THR VAL ILE PHE VAL PHE HIS CYS SEQRES 5 A 372 ALA PRO LEU LEU HIS HIS TYR THR THR SER TYR PHE ILE SEQRES 6 A 372 GLN THR MET ALA TYR ALA ASP LEU PHE VAL GLY VAL SER SEQRES 7 A 372 CYS LEU VAL PRO THR LEU SER LEU LEU HIS TYR SER THR SEQRES 8 A 372 GLY VAL HIS GLU SER LEU THR CYS GLN VAL PHE GLY TYR SEQRES 9 A 372 ILE ILE SER VAL LEU LYS SER VAL SER MET TRP CYS LEU SEQRES 10 A 372 ALA CYS ILE SER VAL ASP ARG TYR LEU ALA ILE THR LYS SEQRES 11 A 372 PRO LEU SER TYR ASN GLN LEU VAL THR PRO CYS ARG LEU SEQRES 12 A 372 ARG ILE CYS ILE ILE LEU ILE TRP ILE TYR SER CYS LEU SEQRES 13 A 372 ILE PHE LEU PRO SER PHE PHE GLY TRP GLY LYS PRO GLY SEQRES 14 A 372 TYR HIS GLY ASP ILE PHE GLU TRP CYS ALA THR SER TRP SEQRES 15 A 372 LEU THR SER ALA TYR PHE THR GLY PHE ILE VAL CYS LEU SEQRES 16 A 372 LEU TYR ALA PRO ALA ALA PHE VAL VAL CYS PHE THR TYR SEQRES 17 A 372 PHE HIS ILE PHE LYS ILE CYS ARG GLN HIS THR LYS MET SEQRES 18 A 372 LYS LYS TYR THR CYS THR VAL CYS GLY TYR ILE TYR ASN SEQRES 19 A 372 PRO GLU ASP GLY ASP PRO ASP ASN GLY VAL ASN PRO GLY SEQRES 20 A 372 THR ASP PHE LYS ASP ILE PRO ASP ASP TRP VAL CYS PRO SEQRES 21 A 372 LEU CYS GLY VAL GLY LYS ASP GLN PHE GLU GLU VAL GLU SEQRES 22 A 372 GLU TYR LEU MET VAL LEU PHE ARG ILE THR SER VAL PHE SEQRES 23 A 372 TYR MET LEU GLN LEU PRO TYR ILE ILE TYR PHE LEU LEU SEQRES 24 A 372 GLU SER SER ARG VAL LEU ASP ASN PRO THR LEU SER PHE SEQRES 25 A 372 LEU THR THR TRP LEU ALA ILE SER ASN SER PHE CYS ASN SEQRES 26 A 372 PRO VAL ILE TYR ALA LEU SER ASP SER THR PHE ARG LEU SEQRES 27 A 372 GLY LEU ARG ARG LEU SER GLU THR MET CYS THR SER CYS SEQRES 28 A 372 MET GLU PHE LEU GLU VAL LEU PHE GLN GLY PRO HIS HIS SEQRES 29 A 372 HIS HIS HIS HIS HIS HIS HIS HIS HET ZN A1201 1 HET OLC A1202 14 HET OLC A1203 15 HET OLC A1204 15 HET OLC A1205 21 HET OLC A1206 12 HET OLC A1207 15 HET OLC A1208 12 HET OLC A1209 15 HET OLC A1210 13 HET OLC A1211 12 HET OLC A1212 25 HET PEG A1213 7 HETNAM ZN ZINC ION HETNAM OLC (2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE HETNAM PEG DI(HYDROXYETHYL)ETHER HETSYN OLC 1-OLEOYL-R-GLYCEROL FORMUL 2 ZN ZN 2+ FORMUL 3 OLC 11(C21 H40 O4) FORMUL 14 PEG C4 H10 O3 FORMUL 15 HOH *18(H2 O) HELIX 1 AA1 CYS A 40 PHE A 65 1 26 HELIX 2 AA2 TYR A 74 CYS A 94 1 21 HELIX 3 AA3 CYS A 94 LEU A 101 1 8 HELIX 4 AA4 HIS A 109 LYS A 145 1 37 HELIX 5 AA5 SER A 148 VAL A 153 1 6 HELIX 6 AA6 CYS A 156 PHE A 173 1 18 HELIX 7 AA7 LEU A 174 GLY A 179 5 6 HELIX 8 AA8 PHE A 190 SER A 196 1 7 HELIX 9 AA9 SER A 200 LEU A 211 1 12 HELIX 10 AB1 LEU A 211 ARG A 231 1 21 HELIX 11 AB2 ASP A 1019 GLY A 1023 5 5 HELIX 12 AB3 ASP A 1029 ILE A 1033 5 5 HELIX 13 AB4 GLY A 1045 ASP A 1047 5 3 HELIX 14 AB5 GLU A 1054 GLN A 278 1 17 HELIX 15 AB6 GLN A 278 SER A 290 1 13 HELIX 16 AB7 ASN A 295 SER A 308 1 14 HELIX 17 AB8 SER A 308 ASP A 321 1 14 HELIX 18 AB9 ASP A 321 LEU A 603 1 23 SHEET 1 AA1 3 ILE A1012 TYR A1013 0 SHEET 2 AA1 3 TYR A1004 CYS A1006 -1 N TYR A1004 O TYR A1013 SHEET 3 AA1 3 PHE A1049 GLU A1051 -1 O GLU A1050 N THR A1005 SSBOND 1 CYS A 27 CYS A 40 1555 1555 2.03 SSBOND 2 CYS A 114 CYS A 193 1555 1555 2.05 LINK SG CYS A1006 ZN ZN A1201 1555 1555 2.28 LINK SG CYS A1009 ZN ZN A1201 1555 1555 2.35 LINK SG CYS A1039 ZN ZN A1201 1555 1555 2.36 LINK SG CYS A1042 ZN ZN A1201 1555 1555 2.34 SITE 1 AC1 4 CYS A1006 CYS A1009 CYS A1039 CYS A1042 SITE 1 AC2 4 SER A 272 VAL A 273 MET A 276 LEU A 277 SITE 1 AC3 2 ILE A 316 HOH A1301 SITE 1 AC4 5 VAL A 37 VAL A 39 ILE A 41 THR A 44 SITE 2 AC4 5 HIS A 103 SITE 1 AC5 5 TYR A 202 SER A 289 LEU A 328 ARG A 329 SITE 2 AC5 5 SER A 332 SITE 1 AC6 5 THR A 60 VAL A 64 THR A 323 PHE A 324 SITE 2 AC6 5 GLY A 327 SITE 1 AC7 3 THR A 60 VAL A 64 OLC A1208 SITE 1 AC8 1 OLC A1207 SITE 1 AC9 3 TRP A 180 TYR A 202 CYS A 209 SITE 1 AD1 3 HIS A 33 ASP A 38 PHE A 42 SITE 1 AD2 2 THR A 297 LEU A 301 SITE 1 AD3 3 ARG A 24 GLU A 191 ASP A1036 CRYST1 77.223 113.229 138.615 90.00 90.00 90.00 I 2 2 2 8 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.012950 0.000000 0.000000 0.00000 SCALE2 0.000000 0.008832 0.000000 0.00000 SCALE3 0.000000 0.000000 0.007214 0.00000 ATOM 1 N GLU A 23 16.394 9.222 16.256 1.00 68.73 N ANISOU 1 N GLU A 23 8093 10641 7380 -183 77 -142 N ATOM 2 CA GLU A 23 15.234 10.101 16.580 1.00 55.69 C ANISOU 2 CA GLU A 23 6420 9007 5731 -216 77 -128 C ATOM 3 C GLU A 23 15.588 11.537 16.193 1.00 48.17 C ANISOU 3 C GLU A 23 5419 8092 4789 -199 81 -94 C ATOM 4 O GLU A 23 16.599 12.024 16.637 1.00 63.27 O ANISOU 4 O GLU A 23 7320 9992 6724 -181 80 -74 O ATOM 5 CB GLU A 23 14.849 9.982 18.056 1.00 70.62 C ANISOU 5 CB GLU A 23 8341 10852 7638 -241 70 -125 C ATOM 6 CG GLU A 23 14.179 8.660 18.407 1.00 87.23 C ANISOU 6 CG GLU A 23 10499 12916 9726 -272 74 -158 C ATOM 7 CD GLU A 23 14.019 8.370 19.895 1.00 91.94 C ANISOU 7 CD GLU A 23 11139 13459 10332 -290 72 -152 C ATOM 8 OE1 GLU A 23 13.600 9.271 20.631 1.00117.47 O ANISOU 8 OE1 GLU A 23 14352 16702 13580 -303 69 -133 O ATOM 9 OE2 GLU A 23 14.304 7.234 20.323 1.00 82.79 O ANISOU 9 OE2 GLU A 23 10042 12247 9165 -288 74 -167 O ATOM 10 N ARG A 24 14.784 12.173 15.353 1.00 53.15 N ANISOU 10 N ARG A 24 6025 8767 5401 -204 85 -89 N ATOM 11 CA ARG A 24 15.056 13.542 14.852 1.00 58.43 C ANISOU 11 CA ARG A 24 6660 9467 6073 -185 94 -53 C ATOM 12 C ARG A 24 14.721 14.577 15.923 1.00 53.67 C ANISOU 12 C ARG A 24 6050 8847 5494 -198 88 -29 C ATOM 13 O ARG A 24 13.721 14.408 16.638 1.00 56.66 O ANISOU 13 O ARG A 24 6438 9217 5872 -222 78 -42 O ATOM 14 CB ARG A 24 14.244 13.823 13.584 1.00 65.76 C ANISOU 14 CB ARG A 24 7573 10448 6964 -176 98 -58 C ATOM 15 CG ARG A 24 14.879 13.316 12.289 1.00 60.18 C ANISOU 15 CG ARG A 24 6863 9768 6231 -151 110 -68 C ATOM 16 CD ARG A 24 13.830 13.195 11.193 1.00 58.79 C ANISOU 16 CD ARG A 24 6680 9644 6013 -144 106 -89 C ATOM 17 NE ARG A 24 13.315 14.503 10.812 1.00 54.50 N ANISOU 17 NE ARG A 24 6119 9133 5454 -127 108 -57 N ATOM 18 CZ ARG A 24 12.104 14.762 10.344 1.00 49.77 C ANISOU 18 CZ ARG A 24 5509 8577 4822 -120 96 -72 C ATOM 19 NH1 ARG A 24 11.812 16.011 10.013 1.00 51.67 N ANISOU 19 NH1 ARG A 24 5743 8840 5047 -93 99 -37 N ATOM 20 NH2 ARG A 24 11.208 13.796 10.207 1.00 58.00 N ANISOU 20 NH2 ARG A 24 6549 9640 5847 -139 83 -122 N ATOM 21 N HIS A 25 15.517 15.628 16.025 1.00 44.71 N ANISOU 21 N HIS A 25 4899 7708 4380 -186 96 2 N ATOM 22 CA HIS A 25 15.277 16.647 17.066 1.00 46.18 C ANISOU 22 CA HIS A 25 5080 7874 4590 -197 90 24 C ATOM 23 C HIS A 25 15.159 18.015 16.431 1.00 44.64 C ANISOU 23 C HIS A 25 4872 7699 4390 -185 103 56 C ATOM 24 O HIS A 25 15.622 18.190 15.321 1.00 49.26 O ANISOU 24 O HIS A 25 5451 8308 4959 -169 120 67 O ATOM 25 CB HIS A 25 16.378 16.633 18.110 1.00 42.40 C ANISOU 25 CB HIS A 25 4602 7359 4147 -199 86 27 C ATOM 26 CG HIS A 25 16.545 15.322 18.781 1.00 41.17 C ANISOU 26 CG HIS A 25 4473 7177 3992 -201 73 0 C ATOM 27 ND1 HIS A 25 17.622 14.505 18.536 1.00 52.06 N ANISOU 27 ND1 HIS A 25 5857 8551 5373 -181 75 -15 N ATOM 28 CD2 HIS A 25 15.796 14.699 19.705 1.00 48.41 C ANISOU 28 CD2 HIS A 25 5417 8069 4907 -219 61 -15 C ATOM 29 CE1 HIS A 25 17.531 13.425 19.279 1.00 58.41 C ANISOU 29 CE1 HIS A 25 6696 9322 6173 -182 62 -36 C ATOM 30 NE2 HIS A 25 16.419 13.523 20.011 1.00 59.95 N ANISOU 30 NE2 HIS A 25 6908 9504 6367 -209 56 -35 N ATOM 31 N SER A 26 14.520 18.927 17.144 1.00 51.61 N ANISOU 31 N SER A 26 5754 8571 5282 -191 95 70 N ATOM 32 CA SER A 26 14.437 20.347 16.742 1.00 57.13 C ANISOU 32 CA SER A 26 6452 9275 5979 -177 107 105 C ATOM 33 C SER A 26 15.538 21.041 17.519 1.00 51.90 C ANISOU 33 C SER A 26 5785 8575 5358 -189 115 122 C ATOM 34 O SER A 26 15.412 21.073 18.739 1.00 39.66 O ANISOU 34 O SER A 26 4236 7000 3832 -202 99 113 O ATOM 35 CB SER A 26 13.082 20.928 17.051 1.00 62.71 C ANISOU 35 CB SER A 26 7161 9994 6670 -170 91 105 C ATOM 36 OG SER A 26 12.967 22.263 16.566 1.00 54.43 O ANISOU 36 OG SER A 26 6121 8946 5611 -148 102 138 O ATOM 37 N CYS A 27 16.587 21.489 16.823 1.00 56.69 N ANISOU 37 N CYS A 27 6385 9181 5970 -187 142 140 N ATOM 38 CA CYS A 27 17.766 22.091 17.494 1.00 53.32 C ANISOU 38 CA CYS A 27 5946 8726 5586 -205 153 147 C ATOM 39 C CYS A 27 18.008 23.480 16.929 1.00 51.30 C ANISOU 39 C CYS A 27 5699 8460 5331 -208 183 183 C ATOM 40 O CYS A 27 18.898 23.659 16.091 1.00 48.38 O ANISOU 40 O CYS A 27 5323 8100 4958 -213 215 194 O ATOM 41 CB CYS A 27 18.952 21.170 17.302 1.00 61.61 C ANISOU 41 CB CYS A 27 6976 9787 6645 -206 160 126 C ATOM 42 SG CYS A 27 18.647 19.584 18.116 1.00 74.49 S ANISOU 42 SG CYS A 27 8615 11414 8274 -200 125 87 S ATOM 43 N PRO A 28 17.246 24.493 17.406 1.00 43.35 N ANISOU 43 N PRO A 28 4712 7431 4327 -206 176 201 N ATOM 44 CA PRO A 28 17.331 25.850 16.885 1.00 43.40 C ANISOU 44 CA PRO A 28 4742 7417 4328 -205 205 238 C ATOM 45 C PRO A 28 18.457 26.737 17.422 1.00 49.75 C ANISOU 45 C PRO A 28 5540 8184 5178 -240 229 245 C ATOM 46 O PRO A 28 18.615 27.810 16.902 1.00 56.26 O ANISOU 46 O PRO A 28 6391 8985 5997 -245 260 276 O ATOM 47 CB PRO A 28 16.027 26.429 17.415 1.00 40.91 C ANISOU 47 CB PRO A 28 4449 7093 4002 -185 180 244 C ATOM 48 CG PRO A 28 15.910 25.827 18.762 1.00 34.72 C ANISOU 48 CG PRO A 28 3644 6301 3247 -200 149 212 C ATOM 49 CD PRO A 28 16.258 24.387 18.483 1.00 37.86 C ANISOU 49 CD PRO A 28 4020 6726 3636 -203 143 186 C ATOM 50 N LEU A 29 19.201 26.297 18.437 1.00 48.32 N ANISOU 50 N LEU A 29 5327 7995 5035 -262 214 215 N ATOM 51 CA LEU A 29 20.240 27.177 19.043 1.00 53.91 C ANISOU 51 CA LEU A 29 6022 8672 5787 -298 234 213 C ATOM 52 C LEU A 29 21.482 27.196 18.158 1.00 61.57 C ANISOU 52 C LEU A 29 6971 9658 6762 -321 276 214 C ATOM 53 O LEU A 29 21.605 26.326 17.269 1.00 83.14 O ANISOU 53 O LEU A 29 9694 12427 9467 -304 283 211 O ATOM 54 CB LEU A 29 20.566 26.704 20.464 1.00 56.93 C ANISOU 54 CB LEU A 29 6376 9049 6204 -306 199 176 C ATOM 55 CG LEU A 29 19.401 26.768 21.447 1.00 53.60 C ANISOU 55 CG LEU A 29 5974 8612 5779 -290 162 173 C ATOM 56 CD1 LEU A 29 19.703 25.976 22.695 1.00 54.81 C ANISOU 56 CD1 LEU A 29 6105 8767 5953 -290 128 137 C ATOM 57 CD2 LEU A 29 19.077 28.207 21.797 1.00 55.80 C ANISOU 57 CD2 LEU A 29 6278 8850 6072 -300 171 193 C ATOM 58 N GLY A 30 22.380 28.146 18.385 1.00 59.09 N ANISOU 58 N GLY A 30 6648 9320 6483 -361 307 215 N ATOM 59 CA GLY A 30 23.534 28.319 17.481 1.00 90.97 C ANISOU 59 CA GLY A 30 10665 13373 10523 -390 357 217 C ATOM 60 C GLY A 30 23.077 28.425 16.032 1.00 68.37 C ANISOU 60 C GLY A 30 7842 10521 7612 -371 389 257 C ATOM 61 O GLY A 30 23.635 27.713 15.196 1.00 53.21 O ANISOU 61 O GLY A 30 5900 8642 5674 -366 407 250 O ATOM 62 N PHE A 31 22.094 29.302 15.817 1.00 58.16 N ANISOU 62 N PHE A 31 6607 9194 6297 -355 393 296 N ATOM 63 CA PHE A 31 21.350 29.611 14.567 1.00 69.36 C ANISOU 63 CA PHE A 31 8076 10615 7659 -321 413 339 C ATOM 64 C PHE A 31 22.230 29.605 13.312 1.00 75.32 C ANISOU 64 C PHE A 31 8832 11392 8393 -338 469 355 C ATOM 65 O PHE A 31 23.019 30.541 13.149 1.00 69.02 O ANISOU 65 O PHE A 31 8046 10562 7613 -382 520 371 O ATOM 66 CB PHE A 31 20.726 31.000 14.738 1.00 80.31 C ANISOU 66 CB PHE A 31 9525 11945 9043 -319 425 375 C ATOM 67 CG PHE A 31 20.671 31.468 16.174 1.00 80.13 C ANISOU 67 CG PHE A 31 9492 11885 9069 -340 397 353 C ATOM 68 CD1 PHE A 31 21.806 31.955 16.804 1.00 67.70 C ANISOU 68 CD1 PHE A 31 7891 10285 7545 -398 422 334 C ATOM 69 CD2 PHE A 31 19.495 31.375 16.913 1.00 83.72 C ANISOU 69 CD2 PHE A 31 9957 12336 9515 -302 347 347 C ATOM 70 CE1 PHE A 31 21.752 32.351 18.134 1.00 76.68 C ANISOU 70 CE1 PHE A 31 9018 11392 8725 -413 393 310 C ATOM 71 CE2 PHE A 31 19.445 31.782 18.239 1.00 72.70 C ANISOU 71 CE2 PHE A 31 8551 10910 8160 -319 322 326 C ATOM 72 CZ PHE A 31 20.575 32.268 18.852 1.00 66.77 C ANISOU 72 CZ PHE A 31 7778 10131 7459 -372 344 308 C ATOM 73 N GLY A 32 22.058 28.611 12.431 1.00 62.06 N ANISOU 73 N GLY A 32 7141 9764 6674 -305 463 351 N ATOM 74 CA GLY A 32 22.705 28.593 11.111 1.00 59.17 C ANISOU 74 CA GLY A 32 6782 9423 6275 -309 515 370 C ATOM 75 C GLY A 32 24.179 28.268 11.188 1.00 62.92 C ANISOU 75 C GLY A 32 7199 9921 6786 -356 546 339 C ATOM 76 O GLY A 32 24.847 28.385 10.167 1.00 76.29 O ANISOU 76 O GLY A 32 8895 11634 8457 -371 598 353 O ATOM 77 N HIS A 33 24.694 27.874 12.347 1.00 74.40 N ANISOU 77 N HIS A 33 8601 11376 8291 -378 517 295 N ATOM 78 CA HIS A 33 26.141 27.552 12.505 1.00 69.05 C ANISOU 78 CA HIS A 33 7859 10729 7648 -417 541 255 C ATOM 79 C HIS A 33 26.339 26.052 12.679 1.00 51.82 C ANISOU 79 C HIS A 33 5628 8597 5462 -381 498 211 C ATOM 80 O HIS A 33 27.470 25.639 12.837 1.00 60.74 O ANISOU 80 O HIS A 33 6701 9759 6615 -398 508 172 O ATOM 81 CB HIS A 33 26.739 28.210 13.751 1.00 75.12 C ANISOU 81 CB HIS A 33 8598 11467 8476 -463 537 230 C ATOM 82 CG HIS A 33 27.037 29.663 13.641 1.00 80.29 C ANISOU 82 CG HIS A 33 9285 12073 9147 -517 592 258 C ATOM 83 ND1 HIS A 33 26.198 30.552 13.007 1.00 93.15 N ANISOU 83 ND1 HIS A 33 10993 13656 10742 -507 616 315 N ATOM 84 CD2 HIS A 33 28.055 30.392 14.146 1.00 92.92 C ANISOU 84 CD2 HIS A 33 10853 13658 10794 -582 626 234 C ATOM 85 CE1 HIS A 33 26.698 31.766 13.107 1.00 97.61 C ANISOU 85 CE1 HIS A 33 11581 14174 11332 -564 666 329 C ATOM 86 NE2 HIS A 33 27.843 31.692 13.797 1.00104.14 N ANISOU 86 NE2 HIS A 33 12338 15020 12211 -616 674 278 N ATOM 87 N TYR A 34 25.262 25.292 12.764 1.00 46.17 N ANISOU 87 N TYR A 34 4936 7884 4721 -334 450 212 N ATOM 88 CA TYR A 34 25.393 23.851 13.061 1.00 43.83 C ANISOU 88 CA TYR A 34 4607 7623 4424 -302 408 170 C ATOM 89 C TYR A 34 25.884 23.119 11.812 1.00 45.05 C ANISOU 89 C TYR A 34 4747 7826 4542 -283 433 163 C ATOM 90 O TYR A 34 25.591 23.573 10.690 1.00 54.61 O ANISOU 90 O TYR A 34 5989 9043 5714 -280 469 199 O ATOM 91 CB TYR A 34 24.054 23.314 13.581 1.00 49.92 C ANISOU 91 CB TYR A 34 5409 8376 5179 -268 355 171 C ATOM 92 CG TYR A 34 23.799 23.467 15.055 1.00 51.28 C ANISOU 92 CG TYR A 34 5577 8514 5389 -277 317 156 C ATOM 93 CD1 TYR A 34 24.774 23.919 15.915 1.00 55.37 C ANISOU 93 CD1 TYR A 34 6061 9023 5953 -307 322 135 C ATOM 94 CD2 TYR A 34 22.577 23.114 15.595 1.00 62.47 C ANISOU 94 CD2 TYR A 34 7023 9916 6796 -255 276 157 C ATOM 95 CE1 TYR A 34 24.535 24.033 17.266 1.00 60.07 C ANISOU 95 CE1 TYR A 34 6655 9590 6578 -310 286 120 C ATOM 96 CE2 TYR A 34 22.312 23.221 16.945 1.00 48.41 C ANISOU 96 CE2 TYR A 34 5241 8107 5044 -262 244 144 C ATOM 97 CZ TYR A 34 23.298 23.678 17.788 1.00 64.49 C ANISOU 97 CZ TYR A 34 7248 10132 7123 -287 247 126 C ATOM 98 OH TYR A 34 22.989 23.775 19.119 1.00 49.56 O ANISOU 98 OH TYR A 34 5358 8214 5255 -288 213 113 O ATOM 99 N SER A 35 26.550 21.987 12.038 1.00 45.61 N ANISOU 99 N SER A 35 4778 7930 4620 -264 412 118 N ATOM 100 CA SER A 35 27.119 21.083 11.006 1.00 42.68 C ANISOU 100 CA SER A 35 4387 7611 4218 -239 428 99 C ATOM 101 C SER A 35 26.817 19.632 11.396 1.00 46.28 C ANISOU 101 C SER A 35 4844 8075 4666 -194 375 62 C ATOM 102 O SER A 35 26.182 19.418 12.434 1.00 48.29 O ANISOU 102 O SER A 35 5115 8295 4937 -188 332 56 O ATOM 103 CB SER A 35 28.586 21.320 10.858 1.00 41.89 C ANISOU 103 CB SER A 35 4230 7545 4139 -266 468 75 C ATOM 104 OG SER A 35 29.230 21.284 12.122 1.00 62.09 O ANISOU 104 OG SER A 35 6749 10098 6745 -277 442 38 O ATOM 105 N VAL A 36 27.276 18.674 10.588 1.00 57.82 N ANISOU 105 N VAL A 36 6291 9578 6100 -164 380 38 N ATOM 106 CA VAL A 36 26.926 17.234 10.777 1.00 55.19 C ANISOU 106 CA VAL A 36 5972 9246 5750 -120 334 5 C ATOM 107 C VAL A 36 27.499 16.731 12.115 1.00 61.17 C ANISOU 107 C VAL A 36 6708 9988 6544 -110 298 -31 C ATOM 108 O VAL A 36 27.052 15.664 12.576 1.00 67.99 O ANISOU 108 O VAL A 36 7600 10834 7400 -78 257 -52 O ATOM 109 CB VAL A 36 27.415 16.385 9.584 1.00 39.63 C ANISOU 109 CB VAL A 36 3990 7324 3742 -88 351 -15 C ATOM 110 N VAL A 37 28.459 17.434 12.715 1.00 59.90 N ANISOU 110 N VAL A 37 6502 9835 6419 -134 311 -41 N ATOM 111 CA VAL A 37 29.088 16.948 13.986 1.00 65.36 C ANISOU 111 CA VAL A 37 7170 10521 7140 -115 273 -81 C ATOM 112 C VAL A 37 28.699 17.858 15.155 1.00 52.72 C ANISOU 112 C VAL A 37 5577 8879 5575 -147 258 -65 C ATOM 113 O VAL A 37 28.823 17.421 16.275 1.00 48.81 O ANISOU 113 O VAL A 37 5082 8368 5095 -127 219 -90 O ATOM 114 CB VAL A 37 30.619 16.871 13.838 1.00 75.81 C ANISOU 114 CB VAL A 37 8426 11902 8476 -107 292 -123 C ATOM 115 CG1 VAL A 37 31.027 15.863 12.783 1.00 77.80 C ANISOU 115 CG1 VAL A 37 8671 12196 8692 -66 301 -145 C ATOM 116 CG2 VAL A 37 31.227 18.221 13.513 1.00 65.73 C ANISOU 116 CG2 VAL A 37 7107 10643 7222 -166 345 -108 C ATOM 117 N ASP A 38 28.244 19.071 14.857 1.00 57.33 N ANISOU 117 N ASP A 38 6171 9445 6165 -191 290 -25 N ATOM 118 CA ASP A 38 27.955 20.159 15.818 1.00 53.93 C ANISOU 118 CA ASP A 38 5745 8976 5769 -227 285 -8 C ATOM 119 C ASP A 38 26.451 20.211 16.120 1.00 69.76 C ANISOU 119 C ASP A 38 7809 10936 7760 -222 260 23 C ATOM 120 O ASP A 38 26.065 20.915 17.073 1.00 66.55 O ANISOU 120 O ASP A 38 7412 10496 7378 -241 245 32 O ATOM 121 CB ASP A 38 28.403 21.477 15.190 1.00 50.85 C ANISOU 121 CB ASP A 38 5338 8590 5391 -278 342 15 C ATOM 122 CG ASP A 38 28.452 22.670 16.119 1.00 66.62 C ANISOU 122 CG ASP A 38 7331 10552 7428 -320 346 22 C ATOM 123 OD1 ASP A 38 28.523 22.469 17.345 1.00 76.59 O ANISOU 123 OD1 ASP A 38 8582 11802 8716 -311 305 -4 O ATOM 124 OD2 ASP A 38 28.453 23.794 15.591 1.00 64.88 O ANISOU 124 OD2 ASP A 38 7122 10315 7211 -362 392 53 O ATOM 125 N VAL A 39 25.618 19.519 15.336 1.00 64.22 N ANISOU 125 N VAL A 39 7141 10239 7019 -198 254 35 N ATOM 126 CA VAL A 39 24.136 19.652 15.458 1.00 49.73 C ANISOU 126 CA VAL A 39 5353 8373 5166 -197 236 62 C ATOM 127 C VAL A 39 23.695 19.209 16.872 1.00 55.03 C ANISOU 127 C VAL A 39 6038 9013 5856 -190 191 44 C ATOM 128 O VAL A 39 24.249 18.238 17.388 1.00 68.18 O ANISOU 128 O VAL A 39 7696 10682 7526 -167 169 12 O ATOM 129 CB VAL A 39 23.393 18.868 14.360 1.00 43.16 C ANISOU 129 CB VAL A 39 4548 7562 4290 -172 236 66 C ATOM 130 CG1 VAL A 39 23.213 17.398 14.703 1.00 48.74 C ANISOU 130 CG1 VAL A 39 5267 8266 4985 -144 201 31 C ATOM 131 CG2 VAL A 39 22.042 19.463 14.079 1.00 41.05 C ANISOU 131 CG2 VAL A 39 4315 7281 4001 -176 234 97 C ATOM 132 N CYS A 40 22.734 19.928 17.451 1.00 44.50 N ANISOU 132 N CYS A 40 4728 7650 4530 -205 181 66 N ATOM 133 CA CYS A 40 22.078 19.639 18.745 1.00 51.71 C ANISOU 133 CA CYS A 40 5660 8532 5453 -202 144 56 C ATOM 134 C CYS A 40 23.094 19.585 19.883 1.00 67.88 C ANISOU 134 C CYS A 40 7683 10572 7534 -201 128 30 C ATOM 135 O CYS A 40 22.985 18.668 20.722 1.00 53.26 O ANISOU 135 O CYS A 40 5848 8708 5679 -180 97 9 O ATOM 136 CB CYS A 40 21.323 18.317 18.698 1.00 64.20 C ANISOU 136 CB CYS A 40 7272 10113 7007 -182 122 40 C ATOM 137 SG CYS A 40 20.027 18.270 17.429 1.00 69.90 S ANISOU 137 SG CYS A 40 8017 10855 7687 -181 134 59 S ATOM 138 N ILE A 41 24.044 20.515 19.936 1.00 67.44 N ANISOU 138 N ILE A 41 7592 10525 7507 -221 148 29 N ATOM 139 CA ILE A 41 25.057 20.452 21.024 1.00 55.35 C ANISOU 139 CA ILE A 41 6028 8996 6005 -216 128 -5 C ATOM 140 C ILE A 41 24.629 21.372 22.170 1.00 51.75 C ANISOU 140 C ILE A 41 5580 8507 5574 -236 113 1 C ATOM 141 O ILE A 41 24.645 20.901 23.304 1.00 54.09 O ANISOU 141 O ILE A 41 5882 8792 5875 -217 78 -19 O ATOM 142 CB ILE A 41 26.478 20.694 20.484 1.00 56.39 C ANISOU 142 CB ILE A 41 6104 9166 6153 -226 156 -27 C ATOM 143 CG1 ILE A 41 27.550 20.422 21.542 1.00 60.05 C ANISOU 143 CG1 ILE A 41 6528 9646 6640 -209 129 -73 C ATOM 144 CG2 ILE A 41 26.631 22.066 19.861 1.00 62.32 C ANISOU 144 CG2 ILE A 41 6843 9914 6921 -273 201 -1 C ATOM 145 CD1 ILE A 41 27.789 18.947 21.789 1.00 60.13 C ANISOU 145 CD1 ILE A 41 6550 9670 6627 -153 95 -102 C ATOM 146 N PHE A 42 24.214 22.603 21.892 1.00 48.43 N ANISOU 146 N PHE A 42 5166 8068 5164 -269 138 31 N ATOM 147 CA PHE A 42 23.781 23.559 22.941 1.00 46.74 C ANISOU 147 CA PHE A 42 4962 7821 4973 -286 124 36 C ATOM 148 C PHE A 42 22.505 23.032 23.613 1.00 46.76 C ANISOU 148 C PHE A 42 5005 7804 4955 -265 92 44 C ATOM 149 O PHE A 42 22.295 23.265 24.794 1.00 49.90 O ANISOU 149 O PHE A 42 5409 8183 5367 -265 67 34 O ATOM 150 CB PHE A 42 23.619 24.974 22.375 1.00 44.42 C ANISOU 150 CB PHE A 42 4677 7508 4691 -321 161 67 C ATOM 151 CG PHE A 42 24.913 25.587 21.911 1.00 48.60 C ANISOU 151 CG PHE A 42 5167 8052 5246 -354 199 55 C ATOM 152 CD1 PHE A 42 25.779 26.178 22.804 1.00 54.30 C ANISOU 152 CD1 PHE A 42 5854 8770 6007 -380 196 24 C ATOM 153 CD2 PHE A 42 25.282 25.560 20.574 1.00 67.76 C ANISOU 153 CD2 PHE A 42 7589 10500 7655 -363 240 71 C ATOM 154 CE1 PHE A 42 26.992 26.704 22.376 1.00 58.11 C ANISOU 154 CE1 PHE A 42 6292 9271 6514 -418 234 6 C ATOM 155 CE2 PHE A 42 26.480 26.110 20.141 1.00 60.79 C ANISOU 155 CE2 PHE A 42 6668 9634 6794 -400 281 58 C ATOM 156 CZ PHE A 42 27.340 26.670 21.048 1.00 57.06 C ANISOU 156 CZ PHE A 42 6155 9159 6364 -430 279 23 C ATOM 157 N GLU A 43 21.635 22.412 22.834 1.00 57.06 N ANISOU 157 N GLU A 43 6336 9115 6226 -252 95 61 N ATOM 158 CA GLU A 43 20.401 21.801 23.377 1.00 53.17 C ANISOU 158 CA GLU A 43 5878 8611 5711 -240 70 63 C ATOM 159 C GLU A 43 20.806 20.608 24.241 1.00 49.85 C ANISOU 159 C GLU A 43 5463 8188 5288 -219 42 33 C ATOM 160 O GLU A 43 20.230 20.474 25.318 1.00 69.40 O ANISOU 160 O GLU A 43 7961 10645 7764 -216 20 29 O ATOM 161 CB GLU A 43 19.459 21.378 22.247 1.00 48.07 C ANISOU 161 CB GLU A 43 5252 7981 5030 -234 81 78 C ATOM 162 CG GLU A 43 19.100 22.515 21.322 1.00 51.38 C ANISOU 162 CG GLU A 43 5674 8404 5443 -242 107 109 C ATOM 163 CD GLU A 43 20.178 22.863 20.296 1.00 65.88 C ANISOU 163 CD GLU A 43 7489 10255 7284 -249 141 117 C ATOM 164 OE1 GLU A 43 19.922 23.730 19.453 1.00 61.69 O ANISOU 164 OE1 GLU A 43 6971 9725 6743 -254 166 146 O ATOM 165 OE2 GLU A 43 21.289 22.278 20.339 1.00 55.17 O ANISOU 165 OE2 GLU A 43 6108 8912 5941 -248 142 95 O ATOM 166 N THR A 44 21.775 19.802 23.809 1.00 47.30 N ANISOU 166 N THR A 44 5125 7884 4962 -201 44 14 N ATOM 167 CA THR A 44 22.160 18.588 24.567 1.00 52.03 C ANISOU 167 CA THR A 44 5741 8477 5550 -170 17 -12 C ATOM 168 C THR A 44 22.842 18.961 25.886 1.00 56.31 C ANISOU 168 C THR A 44 6267 9011 6116 -162 -5 -31 C ATOM 169 O THR A 44 22.622 18.223 26.866 1.00 50.99 O ANISOU 169 O THR A 44 5626 8317 5428 -139 -32 -42 O ATOM 170 CB THR A 44 23.015 17.625 23.746 1.00 55.67 C ANISOU 170 CB THR A 44 6192 8962 5998 -144 23 -30 C ATOM 171 OG1 THR A 44 22.231 17.279 22.609 1.00 61.33 O ANISOU 171 OG1 THR A 44 6927 9684 6690 -153 41 -14 O ATOM 172 CG2 THR A 44 23.355 16.357 24.489 1.00 54.03 C ANISOU 172 CG2 THR A 44 6013 8740 5774 -105 -5 -56 C ATOM 173 N VAL A 45 23.651 20.020 25.933 1.00 46.34 N ANISOU 173 N VAL A 45 4959 7761 4885 -179 3 -38 N ATOM 174 CA VAL A 45 24.298 20.356 27.232 1.00 50.77 C ANISOU 174 CA VAL A 45 5502 8320 5467 -169 -22 -64 C ATOM 175 C VAL A 45 23.209 20.817 28.215 1.00 49.16 C ANISOU 175 C VAL A 45 5332 8084 5263 -180 -37 -48 C ATOM 176 O VAL A 45 23.221 20.365 29.364 1.00 52.68 O ANISOU 176 O VAL A 45 5797 8519 5700 -155 -67 -64 O ATOM 177 CB VAL A 45 25.491 21.325 27.105 1.00 54.25 C ANISOU 177 CB VAL A 45 5881 8786 5944 -191 -7 -85 C ATOM 178 CG1 VAL A 45 26.497 20.805 26.096 1.00 56.78 C ANISOU 178 CG1 VAL A 45 6165 9145 6260 -180 10 -103 C ATOM 179 CG2 VAL A 45 25.104 22.762 26.786 1.00 58.46 C ANISOU 179 CG2 VAL A 45 6407 9302 6501 -240 21 -60 C ATOM 180 N VAL A 46 22.261 21.630 27.776 1.00 38.97 N ANISOU 180 N VAL A 46 4053 6779 3974 -210 -17 -18 N ATOM 181 CA VAL A 46 21.213 22.177 28.676 1.00 43.98 C ANISOU 181 CA VAL A 46 4713 7389 4608 -219 -29 -6 C ATOM 182 C VAL A 46 20.385 21.033 29.264 1.00 48.36 C ANISOU 182 C VAL A 46 5312 7931 5129 -199 -48 -7 C ATOM 183 O VAL A 46 20.104 21.069 30.472 1.00 35.78 O ANISOU 183 O VAL A 46 3736 6324 3534 -191 -69 -14 O ATOM 184 CB VAL A 46 20.294 23.136 27.904 1.00 45.37 C ANISOU 184 CB VAL A 46 4896 7556 4783 -244 -5 24 C ATOM 185 CG1 VAL A 46 19.018 23.445 28.702 1.00 43.99 C ANISOU 185 CG1 VAL A 46 4750 7364 4598 -245 -19 34 C ATOM 186 CG2 VAL A 46 21.049 24.401 27.503 1.00 42.28 C ANISOU 186 CG2 VAL A 46 4475 7164 4425 -268 16 27 C ATOM 187 N ILE A 47 19.987 20.072 28.428 1.00 45.52 N ANISOU 187 N ILE A 47 4973 7578 4744 -195 -37 0 N ATOM 188 CA ILE A 47 19.075 18.980 28.864 1.00 41.81 C ANISOU 188 CA ILE A 47 4551 7092 4242 -188 -45 0 C ATOM 189 C ILE A 47 19.842 18.025 29.765 1.00 37.79 C ANISOU 189 C ILE A 47 4065 6570 3723 -155 -68 -21 C ATOM 190 O ILE A 47 19.360 17.695 30.817 1.00 44.20 O ANISOU 190 O ILE A 47 4912 7361 4519 -149 -82 -22 O ATOM 191 CB ILE A 47 18.493 18.273 27.638 1.00 40.79 C ANISOU 191 CB ILE A 47 4435 6973 4091 -197 -26 7 C ATOM 192 CG1 ILE A 47 17.608 19.231 26.851 1.00 50.68 C ANISOU 192 CG1 ILE A 47 5670 8240 5344 -221 -8 28 C ATOM 193 CG2 ILE A 47 17.740 17.029 28.052 1.00 43.15 C ANISOU 193 CG2 ILE A 47 4784 7252 4359 -197 -30 1 C ATOM 194 CD1 ILE A 47 16.729 18.551 25.822 1.00 55.42 C ANISOU 194 CD1 ILE A 47 6285 8855 5917 -229 4 30 C ATOM 195 N VAL A 48 21.022 17.615 29.335 1.00 53.43 N ANISOU 195 N VAL A 48 6024 8566 5708 -129 -72 -37 N ATOM 196 CA VAL A 48 21.838 16.629 30.093 1.00 62.70 C ANISOU 196 CA VAL A 48 7223 9732 6867 -83 -97 -60 C ATOM 197 C VAL A 48 22.225 17.220 31.455 1.00 52.17 C ANISOU 197 C VAL A 48 5880 8397 5545 -68 -124 -74 C ATOM 198 O VAL A 48 22.255 16.461 32.417 1.00 49.89 O ANISOU 198 O VAL A 48 5636 8088 5230 -34 -145 -82 O ATOM 199 CB VAL A 48 23.060 16.187 29.267 1.00 72.47 C ANISOU 199 CB VAL A 48 8429 10998 8108 -55 -97 -81 C ATOM 200 CG1 VAL A 48 24.143 15.528 30.128 1.00 78.98 C ANISOU 200 CG1 VAL A 48 9259 11827 8922 3 -129 -112 C ATOM 201 CG2 VAL A 48 22.625 15.278 28.121 1.00 64.01 C ANISOU 201 CG2 VAL A 48 7383 9922 7013 -58 -77 -72 C ATOM 202 N LEU A 49 22.513 18.516 31.524 1.00 49.04 N ANISOU 202 N LEU A 49 5432 8016 5182 -91 -121 -77 N ATOM 203 CA LEU A 49 22.854 19.136 32.826 1.00 50.95 C ANISOU 203 CA LEU A 49 5663 8257 5436 -79 -147 -95 C ATOM 204 C LEU A 49 21.615 19.121 33.708 1.00 55.28 C ANISOU 204 C LEU A 49 6261 8776 5965 -88 -151 -76 C ATOM 205 O LEU A 49 21.696 18.591 34.840 1.00 52.13 O ANISOU 205 O LEU A 49 5897 8365 5543 -55 -175 -87 O ATOM 206 CB LEU A 49 23.345 20.567 32.613 1.00 49.44 C ANISOU 206 CB LEU A 49 5411 8085 5288 -111 -137 -103 C ATOM 207 CG LEU A 49 24.833 20.680 32.299 1.00 64.54 C ANISOU 207 CG LEU A 49 7265 10033 7222 -98 -141 -138 C ATOM 208 CD1 LEU A 49 25.290 22.123 32.363 1.00 66.69 C ANISOU 208 CD1 LEU A 49 7485 10316 7538 -138 -131 -152 C ATOM 209 CD2 LEU A 49 25.657 19.835 33.260 1.00 73.27 C ANISOU 209 CD2 LEU A 49 8376 11155 8309 -39 -180 -174 C ATOM 210 N LEU A 50 20.510 19.639 33.176 1.00 46.76 N ANISOU 210 N LEU A 50 5186 7689 4890 -128 -127 -50 N ATOM 211 CA LEU A 50 19.269 19.744 33.955 1.00 38.33 C ANISOU 211 CA LEU A 50 4155 6602 3804 -142 -127 -37 C ATOM 212 C LEU A 50 18.861 18.346 34.379 1.00 39.56 C ANISOU 212 C LEU A 50 4372 6737 3919 -125 -129 -34 C ATOM 213 O LEU A 50 18.529 18.220 35.564 1.00 53.55 O ANISOU 213 O LEU A 50 6177 8494 5673 -114 -142 -37 O ATOM 214 CB LEU A 50 18.194 20.424 33.129 1.00 45.39 C ANISOU 214 CB LEU A 50 5039 7501 4705 -180 -102 -14 C ATOM 215 CG LEU A 50 17.998 21.894 33.475 1.00 57.21 C ANISOU 215 CG LEU A 50 6508 8999 6229 -195 -104 -12 C ATOM 216 CD1 LEU A 50 19.261 22.692 33.239 1.00 57.77 C ANISOU 216 CD1 LEU A 50 6535 9079 6336 -195 -107 -26 C ATOM 217 CD2 LEU A 50 16.847 22.474 32.668 1.00 78.27 C ANISOU 217 CD2 LEU A 50 9173 11671 8893 -220 -82 8 C ATOM 218 N THR A 51 18.913 17.345 33.489 1.00 35.60 N ANISOU 218 N THR A 51 3889 6232 3402 -122 -116 -31 N ATOM 219 CA THR A 51 18.512 15.957 33.888 1.00 46.54 C ANISOU 219 CA THR A 51 5346 7588 4747 -110 -114 -29 C ATOM 220 C THR A 51 19.350 15.497 35.095 1.00 51.01 C ANISOU 220 C THR A 51 5944 8140 5296 -58 -143 -44 C ATOM 221 O THR A 51 18.811 14.822 36.020 1.00 42.26 O ANISOU 221 O THR A 51 4901 7000 4153 -51 -143 -38 O ATOM 222 CB THR A 51 18.621 14.974 32.714 1.00 46.40 C ANISOU 222 CB THR A 51 5343 7567 4718 -110 -98 -30 C ATOM 223 OG1 THR A 51 17.705 15.409 31.705 1.00 49.40 O ANISOU 223 OG1 THR A 51 5698 7964 5108 -155 -74 -18 O ATOM 224 CG2 THR A 51 18.297 13.539 33.084 1.00 45.94 C ANISOU 224 CG2 THR A 51 5365 7469 4620 -99 -93 -30 C ATOM 225 N PHE A 52 20.626 15.871 35.094 1.00 52.46 N ANISOU 225 N PHE A 52 6083 8347 5500 -23 -166 -65 N ATOM 226 CA PHE A 52 21.560 15.451 36.155 1.00 49.82 C ANISOU 226 CA PHE A 52 5770 8011 5147 37 -201 -86 C ATOM 227 C PHE A 52 21.235 16.245 37.430 1.00 51.23 C ANISOU 227 C PHE A 52 5949 8189 5327 35 -216 -88 C ATOM 228 O PHE A 52 21.004 15.632 38.485 1.00 44.25 O ANISOU 228 O PHE A 52 5128 7280 4404 64 -228 -85 O ATOM 229 CB PHE A 52 23.000 15.627 35.676 1.00 51.91 C ANISOU 229 CB PHE A 52 5974 8314 5433 71 -219 -116 C ATOM 230 CG PHE A 52 24.006 15.243 36.723 1.00 60.74 C ANISOU 230 CG PHE A 52 7104 9442 6531 142 -259 -146 C ATOM 231 CD1 PHE A 52 24.200 13.907 37.043 1.00 60.78 C ANISOU 231 CD1 PHE A 52 7183 9420 6489 198 -272 -146 C ATOM 232 CD2 PHE A 52 24.682 16.219 37.435 1.00 51.72 C ANISOU 232 CD2 PHE A 52 5906 8332 5412 153 -285 -174 C ATOM 233 CE1 PHE A 52 25.085 13.548 38.038 1.00 62.37 C ANISOU 233 CE1 PHE A 52 7401 9631 6663 273 -312 -173 C ATOM 234 CE2 PHE A 52 25.576 15.853 38.419 1.00 63.29 C ANISOU 234 CE2 PHE A 52 7380 9814 6853 223 -326 -206 C ATOM 235 CZ PHE A 52 25.778 14.523 38.717 1.00 69.08 C ANISOU 235 CZ PHE A 52 8186 10523 7535 288 -341 -204 C ATOM 236 N LEU A 53 21.206 17.573 37.315 1.00 46.09 N ANISOU 236 N LEU A 53 5235 7561 4715 2 -214 -92 N ATOM 237 CA LEU A 53 21.036 18.474 38.485 1.00 49.92 C ANISOU 237 CA LEU A 53 5710 8050 5206 3 -232 -101 C ATOM 238 C LEU A 53 19.692 18.234 39.195 1.00 55.83 C ANISOU 238 C LEU A 53 6517 8770 5923 -15 -218 -77 C ATOM 239 O LEU A 53 19.632 18.372 40.440 1.00 47.50 O ANISOU 239 O LEU A 53 5486 7710 4849 7 -237 -85 O ATOM 240 CB LEU A 53 21.134 19.914 37.980 1.00 52.75 C ANISOU 240 CB LEU A 53 5998 8429 5614 -36 -224 -106 C ATOM 241 CG LEU A 53 22.514 20.336 37.491 1.00 54.17 C ANISOU 241 CG LEU A 53 6114 8640 5828 -26 -234 -136 C ATOM 242 CD1 LEU A 53 22.464 21.742 36.914 1.00 57.09 C ANISOU 242 CD1 LEU A 53 6430 9017 6243 -76 -215 -135 C ATOM 243 CD2 LEU A 53 23.521 20.259 38.613 1.00 53.27 C ANISOU 243 CD2 LEU A 53 5989 8545 5705 24 -275 -175 C ATOM 244 N ILE A 54 18.655 17.887 38.438 1.00 59.81 N ANISOU 244 N ILE A 54 7041 9261 6420 -56 -185 -53 N ATOM 245 CA ILE A 54 17.291 17.685 38.992 1.00 49.29 C ANISOU 245 CA ILE A 54 5755 7911 5060 -85 -165 -36 C ATOM 246 C ILE A 54 17.265 16.295 39.635 1.00 60.86 C ANISOU 246 C ILE A 54 7303 9343 6477 -59 -163 -30 C ATOM 247 O ILE A 54 16.716 16.189 40.758 1.00 74.04 O ANISOU 247 O ILE A 54 9016 10998 8116 -56 -162 -26 O ATOM 248 CB ILE A 54 16.206 17.886 37.916 1.00 49.33 C ANISOU 248 CB ILE A 54 5741 7923 5076 -138 -132 -20 C ATOM 249 CG1 ILE A 54 16.186 19.331 37.416 1.00 57.86 C ANISOU 249 CG1 ILE A 54 6755 9030 6198 -156 -134 -22 C ATOM 250 CG2 ILE A 54 14.835 17.486 38.432 1.00 56.08 C ANISOU 250 CG2 ILE A 54 6639 8767 5899 -170 -108 -10 C ATOM 251 CD1 ILE A 54 15.469 19.535 36.091 1.00 58.85 C ANISOU 251 CD1 ILE A 54 6856 9169 6334 -191 -108 -9 C ATOM 252 N ILE A 55 17.847 15.270 38.998 1.00 56.42 N ANISOU 252 N ILE A 55 6766 8766 5902 -38 -162 -31 N ATOM 253 CA ILE A 55 17.822 13.904 39.608 1.00 57.42 C ANISOU 253 CA ILE A 55 6987 8850 5978 -9 -158 -24 C ATOM 254 C ILE A 55 18.637 13.955 40.901 1.00 54.88 C ANISOU 254 C ILE A 55 6689 8528 5635 54 -195 -36 C ATOM 255 O ILE A 55 18.062 13.623 41.952 1.00 55.87 O ANISOU 255 O ILE A 55 6878 8628 5721 58 -188 -25 O ATOM 256 CB ILE A 55 18.312 12.816 38.633 1.00 58.76 C ANISOU 256 CB ILE A 55 7183 9002 6139 5 -151 -25 C ATOM 257 CG1 ILE A 55 17.269 12.567 37.545 1.00 55.08 C ANISOU 257 CG1 ILE A 55 6715 8532 5682 -59 -112 -14 C ATOM 258 CG2 ILE A 55 18.660 11.527 39.375 1.00 63.38 C ANISOU 258 CG2 ILE A 55 7868 9540 6672 57 -158 -22 C ATOM 259 CD1 ILE A 55 17.751 11.693 36.430 1.00 57.94 C ANISOU 259 CD1 ILE A 55 7087 8883 6042 -48 -106 -20 C ATOM 260 N ALA A 56 19.898 14.399 40.817 1.00 60.56 N ANISOU 260 N ALA A 56 7354 9279 6377 100 -231 -61 N ATOM 261 CA ALA A 56 20.840 14.504 41.960 1.00 55.43 C ANISOU 261 CA ALA A 56 6709 8641 5708 170 -273 -84 C ATOM 262 C ALA A 56 20.277 15.438 43.041 1.00 66.45 C ANISOU 262 C ALA A 56 8096 10047 7105 155 -280 -84 C ATOM 263 O ALA A 56 20.229 15.003 44.209 1.00 61.90 O ANISOU 263 O ALA A 56 7583 9452 6481 195 -293 -82 O ATOM 264 CB ALA A 56 22.174 14.997 41.485 1.00 52.90 C ANISOU 264 CB ALA A 56 6309 8366 5423 203 -304 -119 C ATOM 265 N GLY A 57 19.870 16.660 42.658 1.00 67.22 N ANISOU 265 N GLY A 57 8122 10170 7249 102 -270 -87 N ATOM 266 CA GLY A 57 19.414 17.729 43.578 1.00 49.93 C ANISOU 266 CA GLY A 57 5909 7992 5066 89 -278 -94 C ATOM 267 C GLY A 57 18.207 17.318 44.404 1.00 55.95 C ANISOU 267 C GLY A 57 6743 8728 5786 72 -255 -70 C ATOM 268 O GLY A 57 18.097 17.755 45.562 1.00 53.04 O ANISOU 268 O GLY A 57 6386 8366 5399 92 -272 -78 O ATOM 269 N ASN A 58 17.333 16.469 43.867 1.00 60.96 N ANISOU 269 N ASN A 58 7424 9335 6400 35 -216 -44 N ATOM 270 CA ASN A 58 16.131 16.031 44.624 1.00 58.72 C ANISOU 270 CA ASN A 58 7207 9028 6075 8 -186 -24 C ATOM 271 C ASN A 58 16.460 14.754 45.389 1.00 60.48 C ANISOU 271 C ASN A 58 7529 9211 6238 55 -187 -13 C ATOM 272 O ASN A 58 15.865 14.569 46.459 1.00 72.85 O ANISOU 272 O ASN A 58 9153 10762 7762 56 -175 -3 O ATOM 273 CB ASN A 58 14.918 15.809 43.723 1.00 54.18 C ANISOU 273 CB ASN A 58 6630 8448 5508 -63 -139 -7 C ATOM 274 CG ASN A 58 14.345 17.109 43.232 1.00 45.39 C ANISOU 274 CG ASN A 58 5435 7371 4438 -102 -136 -14 C ATOM 275 OD1 ASN A 58 13.808 17.870 44.023 1.00 40.76 O ANISOU 275 OD1 ASN A 58 4836 6800 3848 -108 -138 -19 O ATOM 276 ND2 ASN A 58 14.473 17.363 41.938 1.00 46.31 N ANISOU 276 ND2 ASN A 58 5501 7501 4591 -123 -131 -15 N ATOM 277 N LEU A 59 17.339 13.905 44.846 1.00 60.02 N ANISOU 277 N LEU A 59 7495 9135 6173 93 -200 -16 N ATOM 278 CA LEU A 59 17.704 12.636 45.527 1.00 72.33 C ANISOU 278 CA LEU A 59 9162 10650 7671 149 -203 -5 C ATOM 279 C LEU A 59 18.463 12.961 46.821 1.00 69.12 C ANISOU 279 C LEU A 59 8767 10259 7235 224 -248 -21 C ATOM 280 O LEU A 59 18.367 12.160 47.770 1.00 65.96 O ANISOU 280 O LEU A 59 8465 9821 6772 263 -244 -5 O ATOM 281 CB LEU A 59 18.524 11.744 44.590 1.00 62.44 C ANISOU 281 CB LEU A 59 7924 9379 6419 181 -210 -9 C ATOM 282 CG LEU A 59 17.701 10.768 43.759 1.00 63.71 C ANISOU 282 CG LEU A 59 8138 9496 6570 125 -162 11 C ATOM 283 CD1 LEU A 59 18.575 10.077 42.727 1.00 82.29 C ANISOU 283 CD1 LEU A 59 10489 11842 8933 158 -174 1 C ATOM 284 CD2 LEU A 59 17.041 9.729 44.644 1.00 77.99 C ANISOU 284 CD2 LEU A 59 10073 11244 8314 123 -130 36 C ATOM 285 N THR A 60 19.170 14.093 46.854 1.00 63.78 N ANISOU 285 N THR A 60 7997 9635 6602 243 -286 -52 N ATOM 286 CA THR A 60 19.911 14.487 48.067 1.00 69.83 C ANISOU 286 CA THR A 60 8762 10425 7343 313 -333 -76 C ATOM 287 C THR A 60 18.892 14.966 49.087 1.00 62.37 C ANISOU 287 C THR A 60 7843 9476 6376 285 -315 -63 C ATOM 288 O THR A 60 19.000 14.561 50.251 1.00 70.45 O ANISOU 288 O THR A 60 8938 10488 7342 339 -329 -60 O ATOM 289 CB THR A 60 20.986 15.525 47.758 1.00 68.10 C ANISOU 289 CB THR A 60 8433 10262 7179 333 -375 -119 C ATOM 290 OG1 THR A 60 21.856 14.886 46.825 1.00 82.84 O ANISOU 290 OG1 THR A 60 10286 12131 9056 360 -385 -129 O ATOM 291 CG2 THR A 60 21.749 15.940 48.999 1.00 80.95 C ANISOU 291 CG2 THR A 60 10053 11921 8783 403 -426 -153 C ATOM 292 N VAL A 61 17.921 15.752 48.635 1.00 51.46 N ANISOU 292 N VAL A 61 6412 8106 5034 207 -285 -56 N ATOM 293 CA VAL A 61 16.882 16.334 49.532 1.00 55.94 C ANISOU 293 CA VAL A 61 6990 8678 5584 176 -266 -48 C ATOM 294 C VAL A 61 16.019 15.203 50.119 1.00 77.55 C ANISOU 294 C VAL A 61 9838 11370 8255 165 -224 -15 C ATOM 295 O VAL A 61 15.749 15.262 51.336 1.00 85.36 O ANISOU 295 O VAL A 61 10874 12359 9199 189 -226 -12 O ATOM 296 CB VAL A 61 16.048 17.410 48.817 1.00 59.08 C ANISOU 296 CB VAL A 61 7307 9100 6038 103 -245 -51 C ATOM 297 CG1 VAL A 61 14.889 17.913 49.640 1.00 68.62 C ANISOU 297 CG1 VAL A 61 8528 10318 7227 72 -222 -45 C ATOM 298 CG2 VAL A 61 16.924 18.580 48.428 1.00 79.69 C ANISOU 298 CG2 VAL A 61 9823 11748 8708 115 -283 -83 C ATOM 299 N ILE A 62 15.644 14.185 49.338 1.00 68.24 N ANISOU 299 N ILE A 62 8707 10154 7068 131 -186 7 N ATOM 300 CA ILE A 62 14.739 13.126 49.878 1.00 67.61 C ANISOU 300 CA ILE A 62 8736 10025 6926 105 -136 38 C ATOM 301 C ILE A 62 15.508 12.152 50.780 1.00 82.12 C ANISOU 301 C ILE A 62 10682 11823 8697 188 -155 48 C ATOM 302 O ILE A 62 14.845 11.430 51.555 1.00 82.48 O ANISOU 302 O ILE A 62 10829 11828 8682 177 -117 74 O ATOM 303 CB ILE A 62 13.974 12.408 48.755 1.00 66.87 C ANISOU 303 CB ILE A 62 8657 9904 6847 30 -86 53 C ATOM 304 CG1 ILE A 62 14.913 11.707 47.778 1.00 90.13 C ANISOU 304 CG1 ILE A 62 11608 12828 9807 62 -104 50 C ATOM 305 CG2 ILE A 62 13.037 13.379 48.040 1.00 64.79 C ANISOU 305 CG2 ILE A 62 8296 9683 6635 -45 -66 43 C ATOM 306 CD1 ILE A 62 14.191 10.845 46.780 1.00109.11 C ANISOU 306 CD1 ILE A 62 14043 15199 12215 -4 -54 63 C ATOM 307 N PHE A 63 16.838 12.146 50.743 1.00 95.37 N ANISOU 307 N PHE A 63 12341 13514 10379 270 -211 28 N ATOM 308 CA PHE A 63 17.614 11.223 51.611 1.00 97.95 C ANISOU 308 CA PHE A 63 12772 13807 10635 365 -235 35 C ATOM 309 C PHE A 63 18.042 11.960 52.882 1.00 96.10 C ANISOU 309 C PHE A 63 12525 13613 10376 429 -280 15 C ATOM 310 O PHE A 63 18.420 11.289 53.862 1.00146.70 O ANISOU 310 O PHE A 63 19029 19996 16711 506 -295 25 O ATOM 311 CB PHE A 63 18.804 10.618 50.864 1.00 85.42 C ANISOU 311 CB PHE A 63 11182 12215 9057 428 -270 21 C ATOM 312 CG PHE A 63 18.437 9.446 49.993 1.00 87.77 C ANISOU 312 CG PHE A 63 11551 12452 9345 392 -226 47 C ATOM 313 CD1 PHE A 63 17.870 8.306 50.544 1.00 84.62 C ANISOU 313 CD1 PHE A 63 11292 11980 8876 391 -184 83 C ATOM 314 CD2 PHE A 63 18.654 9.484 48.623 1.00 98.86 C ANISOU 314 CD2 PHE A 63 12884 13869 10806 357 -223 35 C ATOM 315 CE1 PHE A 63 17.527 7.229 49.742 1.00 89.16 C ANISOU 315 CE1 PHE A 63 11936 12496 9445 353 -142 102 C ATOM 316 CE2 PHE A 63 18.315 8.406 47.821 1.00 89.94 C ANISOU 316 CE2 PHE A 63 11820 12685 9667 325 -184 55 C ATOM 317 CZ PHE A 63 17.750 7.282 48.383 1.00 90.80 C ANISOU 317 CZ PHE A 63 12068 12721 9711 322 -144 86 C ATOM 318 N VAL A 64 17.966 13.289 52.872 1.00 69.13 N ANISOU 318 N VAL A 64 8998 10253 7013 400 -299 -12 N ATOM 319 CA VAL A 64 18.437 14.072 54.044 1.00 66.69 C ANISOU 319 CA VAL A 64 8666 9987 6686 460 -346 -40 C ATOM 320 C VAL A 64 17.232 14.493 54.882 1.00 71.02 C ANISOU 320 C VAL A 64 9239 10533 7209 412 -309 -23 C ATOM 321 O VAL A 64 17.224 14.186 56.077 1.00 80.90 O ANISOU 321 O VAL A 64 10568 11776 8392 465 -316 -16 O ATOM 322 CB VAL A 64 19.291 15.269 53.594 1.00 67.84 C ANISOU 322 CB VAL A 64 8679 10193 6903 467 -395 -88 C ATOM 323 CG1 VAL A 64 19.427 16.314 54.689 1.00 75.97 C ANISOU 323 CG1 VAL A 64 9669 11267 7929 496 -431 -121 C ATOM 324 CG2 VAL A 64 20.661 14.814 53.113 1.00 63.18 C ANISOU 324 CG2 VAL A 64 8069 9615 6319 537 -439 -114 C ATOM 325 N PHE A 65 16.236 15.138 54.286 1.00 78.10 N ANISOU 325 N PHE A 65 10076 11442 8155 321 -272 -19 N ATOM 326 CA PHE A 65 15.090 15.670 55.064 1.00 73.10 C ANISOU 326 CA PHE A 65 9450 10821 7503 278 -240 -11 C ATOM 327 C PHE A 65 13.852 14.783 54.944 1.00 91.14 C ANISOU 327 C PHE A 65 11811 13063 9753 208 -166 27 C ATOM 328 O PHE A 65 12.949 14.931 55.788 1.00129.84 O ANISOU 328 O PHE A 65 16744 17970 14617 183 -134 36 O ATOM 329 CB PHE A 65 14.677 17.068 54.612 1.00 64.26 C ANISOU 329 CB PHE A 65 8214 9747 6454 226 -246 -37 C ATOM 330 CG PHE A 65 15.797 18.045 54.367 1.00 63.07 C ANISOU 330 CG PHE A 65 7971 9634 6357 265 -306 -78 C ATOM 331 CD1 PHE A 65 16.401 18.127 53.116 1.00 58.64 C ANISOU 331 CD1 PHE A 65 7350 9076 5855 249 -316 -86 C ATOM 332 CD2 PHE A 65 16.206 18.914 55.366 1.00 49.25 C ANISOU 332 CD2 PHE A 65 6192 7919 4601 310 -348 -111 C ATOM 333 CE1 PHE A 65 17.421 19.038 52.883 1.00 58.58 C ANISOU 333 CE1 PHE A 65 7256 9103 5897 274 -364 -126 C ATOM 334 CE2 PHE A 65 17.220 19.826 55.132 1.00 55.89 C ANISOU 334 CE2 PHE A 65 6947 8794 5495 335 -399 -154 C ATOM 335 CZ PHE A 65 17.821 19.892 53.883 1.00 62.11 C ANISOU 335 CZ PHE A 65 7675 9582 6340 313 -404 -161 C ATOM 336 N HIS A 66 13.754 13.930 53.929 1.00 99.91 N ANISOU 336 N HIS A 66 12946 14138 10877 172 -137 45 N ATOM 337 CA HIS A 66 12.512 13.132 53.735 1.00100.54 C ANISOU 337 CA HIS A 66 13088 14182 10931 90 -62 74 C ATOM 338 C HIS A 66 12.763 11.660 54.079 1.00101.03 C ANISOU 338 C HIS A 66 13289 14172 10923 121 -39 105 C ATOM 339 O HIS A 66 11.924 10.816 53.719 1.00107.79 O ANISOU 339 O HIS A 66 14204 14987 11763 52 23 127 O ATOM 340 CB HIS A 66 11.903 13.419 52.353 1.00108.65 C ANISOU 340 CB HIS A 66 14032 15226 12024 9 -38 67 C ATOM 341 CG HIS A 66 11.828 14.881 52.047 1.00 98.32 C ANISOU 341 CG HIS A 66 12600 13978 10777 -1 -68 38 C ATOM 342 ND1 HIS A 66 11.473 15.824 52.998 1.00 94.52 N ANISOU 342 ND1 HIS A 66 12090 13533 10287 7 -79 24 N ATOM 343 CD2 HIS A 66 12.079 15.574 50.917 1.00 85.71 C ANISOU 343 CD2 HIS A 66 10908 12408 9247 -19 -88 22 C ATOM 344 CE1 HIS A 66 11.510 17.026 52.464 1.00 77.59 C ANISOU 344 CE1 HIS A 66 9843 11432 8205 -3 -105 0 C ATOM 345 NE2 HIS A 66 11.883 16.902 51.195 1.00 76.40 N ANISOU 345 NE2 HIS A 66 9652 11276 8100 -20 -110 0 N ATOM 346 N CYS A 67 13.833 11.379 54.825 1.00106.29 N ANISOU 346 N CYS A 67 14011 14826 11546 222 -85 105 N ATOM 347 CA CYS A 67 14.171 10.017 55.309 1.00 89.29 C ANISOU 347 CA CYS A 67 12005 12603 9316 274 -70 136 C ATOM 348 C CYS A 67 14.815 10.149 56.689 1.00 76.47 C ANISOU 348 C CYS A 67 10435 10989 7628 375 -112 133 C ATOM 349 O CYS A 67 16.028 9.908 56.769 1.00 95.49 O ANISOU 349 O CYS A 67 12858 13399 10022 474 -170 120 O ATOM 350 CB CYS A 67 15.075 9.292 54.312 1.00107.35 C ANISOU 350 CB CYS A 67 14303 14861 11624 310 -93 133 C ATOM 351 SG CYS A 67 14.199 8.504 52.930 1.00 99.08 S ANISOU 351 SG CYS A 67 13267 13768 10611 199 -25 149 S ATOM 352 N LEU A 71 10.217 16.707 60.353 1.00 71.27 N ANISOU 352 N LEU A 71 9399 10649 7031 181 -71 24 N ATOM 353 CA LEU A 71 10.410 17.373 61.681 1.00102.40 C ANISOU 353 CA LEU A 71 13349 14625 10930 245 -104 4 C ATOM 354 C LEU A 71 10.493 18.903 61.494 1.00106.16 C ANISOU 354 C LEU A 71 13699 15159 11478 245 -150 -41 C ATOM 355 O LEU A 71 11.551 19.507 61.837 1.00102.56 O ANISOU 355 O LEU A 71 13209 14723 11035 317 -218 -73 O ATOM 356 CB LEU A 71 11.673 16.828 62.360 1.00 91.41 C ANISOU 356 CB LEU A 71 12030 13213 9487 349 -155 7 C ATOM 357 N HIS A 72 9.418 19.504 60.967 1.00146.12 N ANISOU 357 N HIS A 72 18694 20245 16579 170 -114 -48 N ATOM 358 CA HIS A 72 9.312 20.975 60.769 1.00129.30 C ANISOU 358 CA HIS A 72 16454 18161 14512 166 -149 -89 C ATOM 359 C HIS A 72 7.894 21.428 61.139 1.00129.18 C ANISOU 359 C HIS A 72 16420 18181 14480 115 -101 -94 C ATOM 360 O HIS A 72 7.556 21.356 62.333 1.00143.79 O ANISOU 360 O HIS A 72 18321 20045 16265 138 -87 -94 O ATOM 361 CB HIS A 72 9.743 21.364 59.348 1.00118.55 C ANISOU 361 CB HIS A 72 15013 16795 13235 140 -171 -98 C ATOM 362 CG HIS A 72 10.663 22.534 59.318 1.00116.16 C ANISOU 362 CG HIS A 72 14636 16513 12985 183 -237 -139 C ATOM 363 ND1 HIS A 72 11.624 22.689 58.330 1.00130.23 N ANISOU 363 ND1 HIS A 72 16370 18283 14827 189 -270 -148 N ATOM 364 CD2 HIS A 72 10.818 23.576 60.164 1.00121.20 C ANISOU 364 CD2 HIS A 72 15242 17182 13624 221 -273 -175 C ATOM 365 CE1 HIS A 72 12.314 23.791 58.550 1.00122.69 C ANISOU 365 CE1 HIS A 72 15355 17349 13909 221 -321 -188 C ATOM 366 NE2 HIS A 72 11.836 24.357 59.671 1.00133.92 N ANISOU 366 NE2 HIS A 72 16787 18797 15298 242 -326 -207 N ATOM 367 N HIS A 73 7.100 21.899 60.174 1.00 98.82 N ANISOU 367 N HIS A 73 12503 14355 10687 53 -77 -102 N ATOM 368 CA HIS A 73 5.726 22.418 60.421 1.00 99.92 C ANISOU 368 CA HIS A 73 12608 14539 10817 8 -35 -115 C ATOM 369 C HIS A 73 4.661 21.369 60.046 1.00 91.18 C ANISOU 369 C HIS A 73 11536 13425 9680 -69 41 -89 C ATOM 370 O HIS A 73 3.464 21.696 60.138 1.00 86.57 O ANISOU 370 O HIS A 73 10917 12886 9088 -114 81 -104 O ATOM 371 CB HIS A 73 5.542 23.770 59.715 1.00110.29 C ANISOU 371 CB HIS A 73 13817 15885 12202 4 -67 -149 C ATOM 372 CG HIS A 73 6.429 24.840 60.258 1.00 93.56 C ANISOU 372 CG HIS A 73 11669 13773 10106 69 -133 -180 C ATOM 373 ND1 HIS A 73 7.798 24.754 60.171 1.00 72.43 N ANISOU 373 ND1 HIS A 73 9002 11066 7449 114 -183 -182 N ATOM 374 CD2 HIS A 73 6.160 26.001 60.898 1.00 88.26 C ANISOU 374 CD2 HIS A 73 10958 13136 9439 96 -156 -215 C ATOM 375 CE1 HIS A 73 8.338 25.825 60.719 1.00 75.54 C ANISOU 375 CE1 HIS A 73 9361 11477 7862 161 -233 -219 C ATOM 376 NE2 HIS A 73 7.362 26.605 61.169 1.00 76.55 N ANISOU 376 NE2 HIS A 73 9462 11640 7982 151 -219 -239 N ATOM 377 N TYR A 74 5.090 20.170 59.632 1.00 80.66 N ANISOU 377 N TYR A 74 10270 12042 8334 -84 60 -57 N ATOM 378 CA TYR A 74 4.259 18.954 59.382 1.00 79.72 C ANISOU 378 CA TYR A 74 10208 11900 8178 -158 136 -30 C ATOM 379 C TYR A 74 3.381 19.036 58.116 1.00 77.63 C ANISOU 379 C TYR A 74 9869 11661 7965 -234 167 -42 C ATOM 380 O TYR A 74 3.550 18.153 57.251 1.00 64.24 O ANISOU 380 O TYR A 74 8199 9926 6282 -269 186 -24 O ATOM 381 CB TYR A 74 3.417 18.548 60.594 1.00 87.72 C ANISOU 381 CB TYR A 74 11288 12926 9112 -179 193 -22 C ATOM 382 CG TYR A 74 2.473 17.421 60.270 1.00 99.67 C ANISOU 382 CG TYR A 74 12850 14422 10597 -270 277 -3 C ATOM 383 CD1 TYR A 74 2.951 16.136 60.041 1.00100.26 C ANISOU 383 CD1 TYR A 74 13022 14424 10645 -281 301 32 C ATOM 384 CD2 TYR A 74 1.109 17.651 60.133 1.00 93.01 C ANISOU 384 CD2 TYR A 74 11950 13633 9754 -346 332 -26 C ATOM 385 CE1 TYR A 74 2.095 15.101 59.703 1.00100.12 C ANISOU 385 CE1 TYR A 74 13050 14385 10605 -372 381 46 C ATOM 386 CE2 TYR A 74 0.237 16.624 59.810 1.00 90.61 C ANISOU 386 CE2 TYR A 74 11682 13317 9426 -438 412 -17 C ATOM 387 CZ TYR A 74 0.737 15.351 59.589 1.00103.71 C ANISOU 387 CZ TYR A 74 13443 14897 11062 -455 437 19 C ATOM 388 OH TYR A 74 -0.108 14.338 59.259 1.00111.78 O ANISOU 388 OH TYR A 74 14505 15902 12064 -552 518 25 O ATOM 389 N THR A 75 2.403 19.930 57.993 1.00 69.74 N ANISOU 389 N THR A 75 8787 10724 6985 -262 177 -73 N ATOM 390 CA THR A 75 1.576 19.897 56.753 1.00 61.85 C ANISOU 390 CA THR A 75 7721 9750 6027 -329 205 -86 C ATOM 391 C THR A 75 2.461 20.327 55.580 1.00 60.93 C ANISOU 391 C THR A 75 7555 9615 5980 -300 150 -86 C ATOM 392 O THR A 75 2.460 19.639 54.546 1.00 57.34 O ANISOU 392 O THR A 75 7100 9138 5546 -340 167 -75 O ATOM 393 CB THR A 75 0.244 20.655 56.856 1.00 69.90 C ANISOU 393 CB THR A 75 8665 10847 7045 -362 232 -122 C ATOM 394 OG1 THR A 75 0.456 22.057 56.997 1.00 78.72 O ANISOU 394 OG1 THR A 75 9716 11996 8195 -302 176 -147 O ATOM 395 CG2 THR A 75 -0.608 20.160 58.004 1.00 90.17 C ANISOU 395 CG2 THR A 75 11283 13436 9541 -397 294 -123 C ATOM 396 N THR A 76 3.237 21.388 55.747 1.00 66.38 N ANISOU 396 N THR A 76 8208 10309 6701 -235 88 -98 N ATOM 397 CA THR A 76 4.156 21.890 54.703 1.00 54.98 C ANISOU 397 CA THR A 76 6718 8846 5323 -208 37 -99 C ATOM 398 C THR A 76 5.189 20.808 54.398 1.00 50.56 C ANISOU 398 C THR A 76 6221 8228 4758 -198 31 -71 C ATOM 399 O THR A 76 5.508 20.597 53.238 1.00 71.50 O ANISOU 399 O THR A 76 8849 10865 7451 -214 25 -64 O ATOM 400 CB THR A 76 4.816 23.180 55.175 1.00 59.63 C ANISOU 400 CB THR A 76 7269 9447 5939 -145 -20 -121 C ATOM 401 OG1 THR A 76 3.774 24.121 55.444 1.00 55.00 O ANISOU 401 OG1 THR A 76 6631 8912 5352 -152 -11 -148 O ATOM 402 CG2 THR A 76 5.752 23.747 54.139 1.00 72.77 C ANISOU 402 CG2 THR A 76 8887 11092 7668 -124 -65 -124 C ATOM 403 N SER A 77 5.661 20.122 55.426 1.00 66.83 N ANISOU 403 N SER A 77 8365 10260 6766 -168 34 -55 N ATOM 404 CA SER A 77 6.649 19.021 55.306 1.00 66.85 C ANISOU 404 CA SER A 77 8442 10206 6752 -145 27 -28 C ATOM 405 C SER A 77 6.125 17.946 54.353 1.00 58.25 C ANISOU 405 C SER A 77 7376 9091 5663 -212 77 -10 C ATOM 406 O SER A 77 6.936 17.195 53.818 1.00 69.63 O ANISOU 406 O SER A 77 8856 10489 7111 -196 66 6 O ATOM 407 CB SER A 77 7.000 18.420 56.669 1.00 69.57 C ANISOU 407 CB SER A 77 8882 10525 7024 -101 30 -13 C ATOM 408 OG SER A 77 7.729 19.341 57.475 1.00 68.00 O ANISOU 408 OG SER A 77 8661 10348 6828 -29 -27 -34 O ATOM 409 N TYR A 78 4.811 17.838 54.184 1.00 64.93 N ANISOU 409 N TYR A 78 8203 9966 6499 -283 132 -17 N ATOM 410 CA TYR A 78 4.213 16.773 53.341 1.00 64.31 C ANISOU 410 CA TYR A 78 8149 9868 6417 -355 185 -7 C ATOM 411 C TYR A 78 4.089 17.303 51.910 1.00 62.99 C ANISOU 411 C TYR A 78 7889 9729 6316 -377 167 -25 C ATOM 412 O TYR A 78 4.366 16.542 50.969 1.00 55.31 O ANISOU 412 O TYR A 78 6931 8724 5359 -399 175 -14 O ATOM 413 CB TYR A 78 2.900 16.260 53.939 1.00 72.87 C ANISOU 413 CB TYR A 78 9264 10970 7451 -426 258 -11 C ATOM 414 CG TYR A 78 3.053 14.946 54.666 1.00 97.18 C ANISOU 414 CG TYR A 78 12472 13986 10466 -439 302 20 C ATOM 415 CD1 TYR A 78 3.794 14.852 55.843 1.00105.13 C ANISOU 415 CD1 TYR A 78 13555 14961 11425 -370 280 40 C ATOM 416 CD2 TYR A 78 2.472 13.788 54.164 1.00110.41 C ANISOU 416 CD2 TYR A 78 14195 15628 12124 -517 365 28 C ATOM 417 CE1 TYR A 78 3.954 13.644 56.503 1.00105.94 C ANISOU 417 CE1 TYR A 78 13788 15001 11463 -373 320 72 C ATOM 418 CE2 TYR A 78 2.618 12.572 54.811 1.00117.40 C ANISOU 418 CE2 TYR A 78 15212 16445 12949 -529 409 59 C ATOM 419 CZ TYR A 78 3.363 12.504 55.980 1.00121.49 C ANISOU 419 CZ TYR A 78 15812 16930 13417 -453 386 84 C ATOM 420 OH TYR A 78 3.510 11.306 56.609 1.00119.64 O ANISOU 420 OH TYR A 78 15717 16623 13116 -458 430 118 O ATOM 421 N PHE A 79 3.685 18.568 51.755 1.00 63.52 N ANISOU 421 N PHE A 79 7866 9851 6416 -366 143 -50 N ATOM 422 CA PHE A 79 3.560 19.214 50.422 1.00 58.45 C ANISOU 422 CA PHE A 79 7139 9237 5832 -376 123 -65 C ATOM 423 C PHE A 79 4.967 19.318 49.808 1.00 63.93 C ANISOU 423 C PHE A 79 7833 9892 6565 -326 72 -51 C ATOM 424 O PHE A 79 5.141 19.054 48.614 1.00 66.12 O ANISOU 424 O PHE A 79 8087 10161 6873 -344 71 -48 O ATOM 425 CB PHE A 79 2.885 20.588 50.553 1.00 57.53 C ANISOU 425 CB PHE A 79 6943 9181 5734 -361 105 -93 C ATOM 426 CG PHE A 79 1.390 20.593 50.790 1.00 65.46 C ANISOU 426 CG PHE A 79 7918 10242 6709 -413 154 -117 C ATOM 427 CD1 PHE A 79 0.512 19.984 49.899 1.00 69.44 C ANISOU 427 CD1 PHE A 79 8398 10771 7215 -477 194 -129 C ATOM 428 CD2 PHE A 79 0.845 21.247 51.889 1.00 69.29 C ANISOU 428 CD2 PHE A 79 8395 10764 7168 -396 157 -134 C ATOM 429 CE1 PHE A 79 -0.861 20.001 50.118 1.00 69.11 C ANISOU 429 CE1 PHE A 79 8320 10792 7147 -526 239 -159 C ATOM 430 CE2 PHE A 79 -0.529 21.271 52.107 1.00 68.73 C ANISOU 430 CE2 PHE A 79 8290 10755 7070 -443 203 -161 C ATOM 431 CZ PHE A 79 -1.382 20.642 51.227 1.00 70.78 C ANISOU 431 CZ PHE A 79 8521 11041 7330 -509 244 -175 C ATOM 432 N ILE A 80 5.954 19.682 50.630 1.00 56.78 N ANISOU 432 N ILE A 80 6950 8966 5655 -265 32 -47 N ATOM 433 CA ILE A 80 7.390 19.763 50.227 1.00 53.49 C ANISOU 433 CA ILE A 80 6533 8519 5271 -215 -15 -40 C ATOM 434 C ILE A 80 7.878 18.353 49.857 1.00 51.76 C ANISOU 434 C ILE A 80 6382 8252 5031 -223 1 -17 C ATOM 435 O ILE A 80 8.610 18.220 48.860 1.00 46.97 O ANISOU 435 O ILE A 80 5755 7631 4460 -214 -17 -14 O ATOM 436 CB ILE A 80 8.224 20.402 51.363 1.00 47.54 C ANISOU 436 CB ILE A 80 5790 7764 4508 -150 -59 -49 C ATOM 437 CG1 ILE A 80 7.964 21.910 51.482 1.00 49.40 C ANISOU 437 CG1 ILE A 80 5952 8037 4778 -138 -85 -75 C ATOM 438 CG2 ILE A 80 9.711 20.100 51.221 1.00 50.11 C ANISOU 438 CG2 ILE A 80 6133 8058 4847 -99 -101 -45 C ATOM 439 CD1 ILE A 80 8.626 22.766 50.420 1.00 56.52 C ANISOU 439 CD1 ILE A 80 6789 8941 5745 -128 -118 -84 C ATOM 440 N GLN A 81 7.489 17.339 50.633 1.00 52.52 N ANISOU 440 N GLN A 81 6562 8322 5070 -239 39 -2 N ATOM 441 CA GLN A 81 7.911 15.933 50.400 1.00 59.98 C ANISOU 441 CA GLN A 81 7591 9211 5987 -244 60 20 C ATOM 442 C GLN A 81 7.370 15.492 49.041 1.00 54.32 C ANISOU 442 C GLN A 81 6844 8496 5299 -306 90 17 C ATOM 443 O GLN A 81 8.109 14.834 48.289 1.00 56.93 O ANISOU 443 O GLN A 81 7196 8792 5642 -293 79 27 O ATOM 444 CB GLN A 81 7.407 15.008 51.519 1.00 70.65 C ANISOU 444 CB GLN A 81 9044 10532 7267 -259 105 37 C ATOM 445 CG GLN A 81 7.820 13.542 51.368 1.00 79.40 C ANISOU 445 CG GLN A 81 10256 11572 8340 -260 129 62 C ATOM 446 CD GLN A 81 8.018 12.810 52.673 1.00 91.75 C ANISOU 446 CD GLN A 81 11936 13092 9830 -226 145 85 C ATOM 447 OE1 GLN A 81 7.530 13.226 53.726 1.00 93.83 O ANISOU 447 OE1 GLN A 81 12211 13378 10060 -223 156 84 O ATOM 448 NE2 GLN A 81 8.744 11.701 52.605 1.00 94.56 N ANISOU 448 NE2 GLN A 81 12386 13385 10157 -193 145 107 N ATOM 449 N THR A 82 6.115 15.836 48.768 1.00 57.30 N ANISOU 449 N THR A 82 7172 8916 5683 -368 124 2 N ATOM 450 CA THR A 82 5.389 15.447 47.528 1.00 58.28 C ANISOU 450 CA THR A 82 7260 9053 5827 -432 156 -8 C ATOM 451 C THR A 82 6.095 16.113 46.345 1.00 55.50 C ANISOU 451 C THR A 82 6838 8715 5533 -402 111 -13 C ATOM 452 O THR A 82 6.463 15.404 45.386 1.00 62.72 O ANISOU 452 O THR A 82 7764 9604 6460 -413 115 -7 O ATOM 453 CB THR A 82 3.905 15.854 47.615 1.00 65.37 C ANISOU 453 CB THR A 82 8108 10009 6718 -492 194 -32 C ATOM 454 OG1 THR A 82 3.331 15.323 48.803 1.00 70.03 O ANISOU 454 OG1 THR A 82 8764 10589 7254 -518 237 -27 O ATOM 455 CG2 THR A 82 3.073 15.371 46.454 1.00 69.78 C ANISOU 455 CG2 THR A 82 8632 10589 7290 -559 229 -50 C ATOM 456 N MET A 83 6.317 17.426 46.431 1.00 53.94 N ANISOU 456 N MET A 83 6575 8553 5367 -364 72 -23 N ATOM 457 CA MET A 83 6.918 18.173 45.298 1.00 48.98 C ANISOU 457 CA MET A 83 5880 7938 4792 -341 36 -27 C ATOM 458 C MET A 83 8.394 17.816 45.137 1.00 47.31 C ANISOU 458 C MET A 83 5697 7685 4593 -293 3 -14 C ATOM 459 O MET A 83 8.922 18.075 44.071 1.00 59.81 O ANISOU 459 O MET A 83 7240 9272 6214 -285 -14 -14 O ATOM 460 CB MET A 83 6.723 19.682 45.428 1.00 43.48 C ANISOU 460 CB MET A 83 5115 7282 4123 -318 9 -42 C ATOM 461 CG MET A 83 7.636 20.391 46.342 1.00 45.76 C ANISOU 461 CG MET A 83 5408 7559 4418 -263 -30 -43 C ATOM 462 SD MET A 83 7.105 22.125 46.294 1.00 52.57 S ANISOU 462 SD MET A 83 6193 8466 5314 -250 -51 -63 S ATOM 463 CE MET A 83 7.856 22.559 44.727 1.00 62.61 C ANISOU 463 CE MET A 83 7418 9729 6640 -243 -71 -57 C ATOM 464 N ALA A 84 9.000 17.175 46.132 1.00 53.93 N ANISOU 464 N ALA A 84 6605 8488 5396 -261 -2 -3 N ATOM 465 CA ALA A 84 10.353 16.593 45.995 1.00 52.33 C ANISOU 465 CA ALA A 84 6438 8249 5196 -212 -31 4 C ATOM 466 C ALA A 84 10.289 15.442 44.984 1.00 53.38 C ANISOU 466 C ALA A 84 6602 8353 5324 -243 -3 14 C ATOM 467 O ALA A 84 11.051 15.474 44.000 1.00 57.14 O ANISOU 467 O ALA A 84 7046 8830 5834 -226 -24 12 O ATOM 468 CB ALA A 84 10.878 16.139 47.335 1.00 49.80 C ANISOU 468 CB ALA A 84 6191 7901 4829 -165 -43 12 C ATOM 469 N TYR A 85 9.384 14.486 45.196 1.00 52.38 N ANISOU 469 N TYR A 85 6536 8205 5159 -291 43 21 N ATOM 470 CA TYR A 85 9.149 13.323 44.297 1.00 63.81 C ANISOU 470 CA TYR A 85 8022 9623 6600 -332 77 25 C ATOM 471 C TYR A 85 8.611 13.805 42.940 1.00 69.31 C ANISOU 471 C TYR A 85 8634 10361 7339 -373 82 10 C ATOM 472 O TYR A 85 8.969 13.207 41.890 1.00 66.01 O ANISOU 472 O TYR A 85 8218 9927 6934 -379 83 10 O ATOM 473 CB TYR A 85 8.218 12.299 44.953 1.00 59.80 C ANISOU 473 CB TYR A 85 7597 9082 6040 -385 132 33 C ATOM 474 CG TYR A 85 8.902 11.514 46.037 1.00 65.04 C ANISOU 474 CG TYR A 85 8369 9689 6655 -337 130 54 C ATOM 475 CD1 TYR A 85 9.657 10.392 45.736 1.00 70.86 C ANISOU 475 CD1 TYR A 85 9183 10366 7373 -310 129 67 C ATOM 476 CD2 TYR A 85 8.820 11.905 47.363 1.00 67.15 C ANISOU 476 CD2 TYR A 85 8663 9961 6890 -311 126 60 C ATOM 477 CE1 TYR A 85 10.309 9.669 46.724 1.00 78.93 C ANISOU 477 CE1 TYR A 85 10310 11335 8344 -254 123 87 C ATOM 478 CE2 TYR A 85 9.474 11.204 48.360 1.00 80.29 C ANISOU 478 CE2 TYR A 85 10428 11574 8502 -257 120 80 C ATOM 479 CZ TYR A 85 10.224 10.082 48.043 1.00 83.57 C ANISOU 479 CZ TYR A 85 10923 11929 8897 -226 118 94 C ATOM 480 OH TYR A 85 10.869 9.385 49.027 1.00102.16 O ANISOU 480 OH TYR A 85 13386 14234 11195 -163 110 114 O ATOM 481 N ALA A 86 7.815 14.878 42.943 1.00 61.15 N ANISOU 481 N ALA A 86 7529 9380 6323 -393 82 -3 N ATOM 482 CA ALA A 86 7.338 15.494 41.681 1.00 78.00 C ANISOU 482 CA ALA A 86 9582 11559 8493 -417 80 -17 C ATOM 483 C ALA A 86 8.542 16.023 40.884 1.00 61.51 C ANISOU 483 C ALA A 86 7455 9468 6444 -368 38 -11 C ATOM 484 O ALA A 86 8.641 15.717 39.691 1.00 59.06 O ANISOU 484 O ALA A 86 7126 9161 6151 -381 42 -13 O ATOM 485 CB ALA A 86 6.338 16.589 41.960 1.00 77.36 C ANISOU 485 CB ALA A 86 9440 11533 8418 -432 82 -33 C ATOM 486 N ASP A 87 9.420 16.787 41.533 1.00 51.20 N ANISOU 486 N ASP A 87 6140 8160 5153 -317 2 -6 N ATOM 487 CA ASP A 87 10.594 17.401 40.879 1.00 48.06 C ANISOU 487 CA ASP A 87 5700 7764 4794 -276 -33 -5 C ATOM 488 C ASP A 87 11.585 16.292 40.528 1.00 53.65 C ANISOU 488 C ASP A 87 6454 8436 5495 -254 -38 0 C ATOM 489 O ASP A 87 12.243 16.419 39.474 1.00 65.80 O ANISOU 489 O ASP A 87 7957 9981 7061 -243 -50 0 O ATOM 490 CB ASP A 87 11.267 18.472 41.731 1.00 47.40 C ANISOU 490 CB ASP A 87 5593 7688 4727 -234 -69 -10 C ATOM 491 CG ASP A 87 10.398 19.672 42.046 1.00 51.13 C ANISOU 491 CG ASP A 87 6021 8193 5210 -247 -68 -19 C ATOM 492 OD1 ASP A 87 9.516 19.988 41.201 1.00 51.23 O ANISOU 492 OD1 ASP A 87 5998 8233 5233 -278 -51 -21 O ATOM 493 OD2 ASP A 87 10.603 20.273 43.153 1.00 60.70 O ANISOU 493 OD2 ASP A 87 7237 9407 6417 -220 -88 -26 O ATOM 494 N LEU A 88 11.692 15.242 41.344 1.00 47.20 N ANISOU 494 N LEU A 88 5715 7580 4636 -244 -28 7 N ATOM 495 CA LEU A 88 12.640 14.147 40.999 1.00 53.44 C ANISOU 495 CA LEU A 88 6556 8332 5414 -213 -35 12 C ATOM 496 C LEU A 88 12.166 13.473 39.713 1.00 48.31 C ANISOU 496 C LEU A 88 5903 7679 4771 -257 -7 11 C ATOM 497 O LEU A 88 13.006 13.187 38.856 1.00 47.49 O ANISOU 497 O LEU A 88 5788 7571 4684 -232 -21 8 O ATOM 498 CB LEU A 88 12.738 13.136 42.147 1.00 51.10 C ANISOU 498 CB LEU A 88 6359 7990 5066 -191 -27 23 C ATOM 499 CG LEU A 88 13.423 11.813 41.807 1.00 47.02 C ANISOU 499 CG LEU A 88 5914 7424 4525 -164 -24 29 C ATOM 500 CD1 LEU A 88 14.857 12.005 41.352 1.00 52.17 C ANISOU 500 CD1 LEU A 88 6531 8088 5202 -99 -69 19 C ATOM 501 CD2 LEU A 88 13.385 10.908 43.004 1.00 51.13 C ANISOU 501 CD2 LEU A 88 6543 7895 4988 -142 -12 43 C ATOM 502 N PHE A 89 10.864 13.232 39.595 1.00 54.31 N ANISOU 502 N PHE A 89 6669 8447 5517 -319 31 7 N ATOM 503 CA PHE A 89 10.365 12.458 38.436 1.00 61.78 C ANISOU 503 CA PHE A 89 7619 9390 6464 -364 58 0 C ATOM 504 C PHE A 89 10.319 13.369 37.210 1.00 53.65 C ANISOU 504 C PHE A 89 6499 8410 5474 -368 45 -8 C ATOM 505 O PHE A 89 10.096 12.828 36.121 1.00 54.59 O ANISOU 505 O PHE A 89 6611 8532 5596 -393 60 -17 O ATOM 506 CB PHE A 89 9.067 11.734 38.800 1.00 66.77 C ANISOU 506 CB PHE A 89 8295 10011 7064 -431 107 -6 C ATOM 507 CG PHE A 89 9.372 10.449 39.522 1.00 71.14 C ANISOU 507 CG PHE A 89 8958 10495 7575 -425 126 5 C ATOM 508 CD1 PHE A 89 9.931 9.383 38.832 1.00 74.77 C ANISOU 508 CD1 PHE A 89 9469 10912 8028 -416 130 5 C ATOM 509 CD2 PHE A 89 9.217 10.340 40.893 1.00 65.11 C ANISOU 509 CD2 PHE A 89 8254 9707 6777 -418 136 17 C ATOM 510 CE1 PHE A 89 10.267 8.208 39.487 1.00 68.35 C ANISOU 510 CE1 PHE A 89 8768 10027 7173 -401 146 18 C ATOM 511 CE2 PHE A 89 9.575 9.173 41.548 1.00 68.58 C ANISOU 511 CE2 PHE A 89 8806 10078 7173 -402 152 32 C ATOM 512 CZ PHE A 89 10.087 8.106 40.842 1.00 72.65 C ANISOU 512 CZ PHE A 89 9375 10545 7681 -394 157 33 C ATOM 513 N VAL A 90 10.554 14.674 37.382 1.00 43.41 N ANISOU 513 N VAL A 90 5142 7146 4204 -343 19 -6 N ATOM 514 CA VAL A 90 10.665 15.578 36.201 1.00 47.41 C ANISOU 514 CA VAL A 90 5575 7692 4746 -339 6 -9 C ATOM 515 C VAL A 90 11.992 15.222 35.536 1.00 47.49 C ANISOU 515 C VAL A 90 5588 7684 4770 -301 -11 -4 C ATOM 516 O VAL A 90 12.000 14.950 34.329 1.00 69.52 O ANISOU 516 O VAL A 90 8359 10485 7568 -312 -3 -8 O ATOM 517 CB VAL A 90 10.564 17.071 36.589 1.00 49.51 C ANISOU 517 CB VAL A 90 5787 7987 5034 -323 -12 -7 C ATOM 518 CG1 VAL A 90 11.306 17.996 35.630 1.00 50.22 C ANISOU 518 CG1 VAL A 90 5823 8095 5161 -300 -31 -3 C ATOM 519 CG2 VAL A 90 9.124 17.525 36.692 1.00 53.53 C ANISOU 519 CG2 VAL A 90 6272 8533 5534 -359 6 -17 C ATOM 520 N GLY A 91 13.064 15.192 36.326 1.00 51.97 N ANISOU 520 N GLY A 91 6178 8229 5339 -256 -35 -1 N ATOM 521 CA GLY A 91 14.413 14.835 35.860 1.00 54.16 C ANISOU 521 CA GLY A 91 6455 8496 5627 -213 -55 -3 C ATOM 522 C GLY A 91 14.501 13.387 35.424 1.00 57.79 C ANISOU 522 C GLY A 91 6974 8922 6060 -214 -40 -4 C ATOM 523 O GLY A 91 15.278 13.101 34.499 1.00 74.42 O ANISOU 523 O GLY A 91 9065 11033 8178 -194 -47 -9 O ATOM 524 N VAL A 92 13.759 12.492 36.072 1.00 56.36 N ANISOU 524 N VAL A 92 6862 8707 5843 -238 -17 -2 N ATOM 525 CA VAL A 92 13.744 11.050 35.691 1.00 65.07 C ANISOU 525 CA VAL A 92 8037 9768 6919 -245 2 -4 C ATOM 526 C VAL A 92 13.124 10.932 34.288 1.00 61.36 C ANISOU 526 C VAL A 92 7528 9322 6462 -290 22 -14 C ATOM 527 O VAL A 92 13.646 10.154 33.469 1.00 55.64 O ANISOU 527 O VAL A 92 6823 8581 5734 -275 23 -21 O ATOM 528 CB VAL A 92 12.989 10.207 36.732 1.00 75.39 C ANISOU 528 CB VAL A 92 9430 11029 8183 -271 29 1 C ATOM 529 CG1 VAL A 92 12.615 8.831 36.201 1.00 81.08 C ANISOU 529 CG1 VAL A 92 10221 11705 8879 -303 62 -4 C ATOM 530 CG2 VAL A 92 13.779 10.096 38.023 1.00 80.16 C ANISOU 530 CG2 VAL A 92 10086 11604 8764 -211 5 12 C ATOM 531 N SER A 93 12.061 11.692 34.024 1.00 50.39 N ANISOU 531 N SER A 93 6087 7974 5085 -335 36 -19 N ATOM 532 CA SER A 93 11.410 11.752 32.697 1.00 50.08 C ANISOU 532 CA SER A 93 6002 7969 5056 -371 51 -32 C ATOM 533 C SER A 93 12.381 12.403 31.715 1.00 56.57 C ANISOU 533 C SER A 93 6768 8818 5906 -332 27 -27 C ATOM 534 O SER A 93 12.368 12.023 30.525 1.00 63.73 O ANISOU 534 O SER A 93 7661 9738 6814 -341 35 -36 O ATOM 535 CB SER A 93 10.130 12.525 32.748 1.00 46.96 C ANISOU 535 CB SER A 93 5560 7617 4662 -414 64 -39 C ATOM 536 OG SER A 93 9.252 11.974 33.699 1.00 60.17 O ANISOU 536 OG SER A 93 7280 9271 6309 -455 91 -45 O ATOM 537 N CYS A 94 13.183 13.356 32.194 1.00 46.75 N ANISOU 537 N CYS A 94 5493 7583 4683 -294 2 -16 N ATOM 538 CA CYS A 94 14.091 14.119 31.306 1.00 51.56 C ANISOU 538 CA CYS A 94 6046 8221 5323 -266 -13 -12 C ATOM 539 C CYS A 94 15.252 13.202 30.878 1.00 62.29 C ANISOU 539 C CYS A 94 7430 9560 6677 -229 -21 -18 C ATOM 540 O CYS A 94 16.103 13.661 30.060 1.00 58.57 O ANISOU 540 O CYS A 94 6913 9113 6227 -208 -29 -19 O ATOM 541 CB CYS A 94 14.565 15.418 31.944 1.00 46.73 C ANISOU 541 CB CYS A 94 5393 7624 4736 -245 -33 -4 C ATOM 542 SG CYS A 94 13.338 16.757 31.909 1.00 47.39 S ANISOU 542 SG CYS A 94 5431 7742 4831 -277 -26 1 S ATOM 543 N LEU A 95 15.251 11.934 31.331 1.00 56.81 N ANISOU 543 N LEU A 95 6808 8824 5954 -224 -15 -24 N ATOM 544 CA LEU A 95 16.266 10.950 30.853 1.00 47.82 C ANISOU 544 CA LEU A 95 5700 7664 4805 -184 -23 -33 C ATOM 545 C LEU A 95 15.909 10.567 29.424 1.00 54.88 C ANISOU 545 C LEU A 95 6577 8575 5699 -209 -4 -42 C ATOM 546 O LEU A 95 16.820 10.215 28.672 1.00 63.78 O ANISOU 546 O LEU A 95 7695 9707 6829 -175 -12 -50 O ATOM 547 CB LEU A 95 16.310 9.705 31.743 1.00 45.38 C ANISOU 547 CB LEU A 95 5485 7296 4460 -167 -20 -35 C ATOM 548 CG LEU A 95 17.012 9.874 33.093 1.00 47.97 C ANISOU 548 CG LEU A 95 5839 7607 4780 -118 -46 -29 C ATOM 549 CD1 LEU A 95 16.656 8.723 34.007 1.00 56.26 C ANISOU 549 CD1 LEU A 95 6994 8595 5787 -115 -34 -24 C ATOM 550 CD2 LEU A 95 18.521 9.976 32.958 1.00 44.22 C ANISOU 550 CD2 LEU A 95 5336 7150 4316 -49 -79 -40 C ATOM 551 N VAL A 96 14.621 10.635 29.072 1.00 58.66 N ANISOU 551 N VAL A 96 7049 9067 6173 -264 17 -45 N ATOM 552 CA VAL A 96 14.161 10.330 27.690 1.00 55.48 C ANISOU 552 CA VAL A 96 6624 8687 5766 -289 33 -59 C ATOM 553 C VAL A 96 14.843 11.304 26.724 1.00 58.08 C ANISOU 553 C VAL A 96 6882 9063 6119 -263 22 -51 C ATOM 554 O VAL A 96 15.705 10.864 25.965 1.00 58.70 O ANISOU 554 O VAL A 96 6960 9145 6198 -234 18 -58 O ATOM 555 CB VAL A 96 12.623 10.281 27.581 1.00 62.45 C ANISOU 555 CB VAL A 96 7504 9585 6637 -351 56 -71 C ATOM 556 CG1 VAL A 96 12.155 9.885 26.190 1.00 65.99 C ANISOU 556 CG1 VAL A 96 7933 10063 7078 -372 69 -91 C ATOM 557 CG2 VAL A 96 12.042 9.309 28.587 1.00 63.92 C ANISOU 557 CG2 VAL A 96 7765 9722 6799 -382 74 -77 C ATOM 558 N PRO A 97 14.567 12.634 26.690 1.00 57.06 N ANISOU 558 N PRO A 97 6697 8971 6010 -270 18 -37 N ATOM 559 CA PRO A 97 15.299 13.507 25.768 1.00 60.55 C ANISOU 559 CA PRO A 97 7085 9448 6471 -249 14 -28 C ATOM 560 C PRO A 97 16.829 13.302 25.777 1.00 63.22 C ANISOU 560 C PRO A 97 7420 9777 6821 -205 1 -30 C ATOM 561 O PRO A 97 17.407 13.223 24.707 1.00 92.20 O ANISOU 561 O PRO A 97 11068 13469 10492 -191 7 -33 O ATOM 562 CB PRO A 97 14.925 14.941 26.192 1.00 54.81 C ANISOU 562 CB PRO A 97 6320 8741 5764 -257 9 -11 C ATOM 563 CG PRO A 97 14.132 14.785 27.474 1.00 54.38 C ANISOU 563 CG PRO A 97 6296 8664 5701 -276 7 -14 C ATOM 564 CD PRO A 97 13.561 13.380 27.458 1.00 54.19 C ANISOU 564 CD PRO A 97 6324 8617 5649 -298 20 -31 C ATOM 565 N THR A 98 17.460 13.220 26.954 1.00 64.62 N ANISOU 565 N THR A 98 7618 9930 7004 -181 -15 -31 N ATOM 566 CA THR A 98 18.948 13.101 27.019 1.00 70.00 C ANISOU 566 CA THR A 98 8286 10615 7696 -135 -31 -40 C ATOM 567 C THR A 98 19.424 11.856 26.262 1.00 64.10 C ANISOU 567 C THR A 98 7567 9858 6928 -110 -28 -57 C ATOM 568 O THR A 98 20.419 11.970 25.551 1.00 76.34 O ANISOU 568 O THR A 98 9080 11436 8487 -84 -30 -65 O ATOM 569 CB THR A 98 19.478 13.044 28.463 1.00 70.75 C ANISOU 569 CB THR A 98 8404 10686 7791 -105 -55 -45 C ATOM 570 OG1 THR A 98 18.807 12.006 29.167 1.00 83.05 O ANISOU 570 OG1 THR A 98 10036 12200 9318 -109 -53 -46 O ATOM 571 CG2 THR A 98 19.281 14.323 29.244 1.00 54.22 C ANISOU 571 CG2 THR A 98 6276 8602 5720 -121 -62 -34 C ATOM 572 N LEU A 99 18.752 10.711 26.425 1.00 66.53 N ANISOU 572 N LEU A 99 7941 10128 7208 -119 -22 -63 N ATOM 573 CA LEU A 99 19.169 9.433 25.786 1.00 67.03 C ANISOU 573 CA LEU A 99 8045 10173 7248 -93 -19 -82 C ATOM 574 C LEU A 99 18.864 9.492 24.283 1.00 71.74 C ANISOU 574 C LEU A 99 8606 10804 7845 -115 -1 -87 C ATOM 575 O LEU A 99 19.665 8.956 23.500 1.00 78.19 O ANISOU 575 O LEU A 99 9420 11632 8656 -82 -2 -101 O ATOM 576 CB LEU A 99 18.470 8.245 26.452 1.00 64.90 C ANISOU 576 CB LEU A 99 7865 9843 6948 -106 -13 -87 C ATOM 577 CG LEU A 99 19.023 7.843 27.814 1.00 68.84 C ANISOU 577 CG LEU A 99 8419 10301 7434 -64 -32 -84 C ATOM 578 CD1 LEU A 99 17.961 7.109 28.610 1.00 83.81 C ANISOU 578 CD1 LEU A 99 10396 12141 9304 -101 -14 -79 C ATOM 579 CD2 LEU A 99 20.283 6.999 27.691 1.00 69.53 C ANISOU 579 CD2 LEU A 99 8534 10375 7507 7 -51 -102 C ATOM 580 N SER A 100 17.769 10.133 23.873 1.00 72.00 N ANISOU 580 N SER A 100 8613 10860 7882 -162 13 -77 N ATOM 581 CA SER A 100 17.479 10.273 22.417 1.00 74.93 C ANISOU 581 CA SER A 100 8950 11272 8249 -175 28 -82 C ATOM 582 C SER A 100 18.536 11.182 21.790 1.00 67.07 C ANISOU 582 C SER A 100 7894 10317 7272 -148 27 -71 C ATOM 583 O SER A 100 19.024 10.843 20.708 1.00 87.35 O ANISOU 583 O SER A 100 10449 12907 9831 -131 34 -82 O ATOM 584 CB SER A 100 16.093 10.786 22.148 1.00 72.30 C ANISOU 584 CB SER A 100 8600 10959 7910 -222 39 -77 C ATOM 585 OG SER A 100 16.045 12.203 22.251 1.00 70.44 O ANISOU 585 OG SER A 100 8315 10753 7695 -225 37 -54 O ATOM 586 N LEU A 101 18.866 12.272 22.478 1.00 59.76 N ANISOU 586 N LEU A 101 6936 9398 6371 -147 20 -54 N ATOM 587 CA LEU A 101 19.880 13.275 22.078 1.00 66.12 C ANISOU 587 CA LEU A 101 7686 10237 7200 -133 23 -45 C ATOM 588 C LEU A 101 21.274 12.640 22.124 1.00 78.66 C ANISOU 588 C LEU A 101 9268 11827 8789 -89 13 -66 C ATOM 589 O LEU A 101 22.227 13.215 21.546 1.00 80.51 O ANISOU 589 O LEU A 101 9454 12097 9038 -78 22 -67 O ATOM 590 CB LEU A 101 19.841 14.451 23.055 1.00 65.12 C ANISOU 590 CB LEU A 101 7536 10105 7099 -146 16 -29 C ATOM 591 CG LEU A 101 18.794 15.524 22.773 1.00 57.99 C ANISOU 591 CG LEU A 101 6617 9215 6200 -179 28 -6 C ATOM 592 CD1 LEU A 101 18.734 16.485 23.942 1.00 69.15 C ANISOU 592 CD1 LEU A 101 8021 10614 7636 -188 17 3 C ATOM 593 CD2 LEU A 101 19.102 16.297 21.517 1.00 61.04 C ANISOU 593 CD2 LEU A 101 6966 9635 6589 -182 49 7 C ATOM 594 N LEU A 102 21.382 11.513 22.822 1.00 69.13 N ANISOU 594 N LEU A 102 8114 10585 7566 -63 -2 -82 N ATOM 595 CA LEU A 102 22.664 10.784 22.959 1.00 68.93 C ANISOU 595 CA LEU A 102 8092 10561 7535 -8 -18 -107 C ATOM 596 C LEU A 102 22.652 9.591 22.004 1.00 68.03 C ANISOU 596 C LEU A 102 8012 10441 7393 9 -11 -125 C ATOM 597 O LEU A 102 23.435 8.669 22.220 1.00 75.70 O ANISOU 597 O LEU A 102 9013 11399 8350 60 -26 -147 O ATOM 598 CB LEU A 102 22.833 10.368 24.421 1.00 65.08 C ANISOU 598 CB LEU A 102 7649 10035 7042 18 -44 -113 C ATOM 599 CG LEU A 102 23.105 11.531 25.375 1.00 63.12 C ANISOU 599 CG LEU A 102 7360 9799 6821 11 -56 -104 C ATOM 600 CD1 LEU A 102 23.243 11.028 26.795 1.00 61.42 C ANISOU 600 CD1 LEU A 102 7195 9547 6592 44 -83 -111 C ATOM 601 CD2 LEU A 102 24.341 12.317 24.983 1.00 58.73 C ANISOU 601 CD2 LEU A 102 6728 9295 6292 26 -56 -118 C ATOM 602 N HIS A 103 21.777 9.642 20.993 1.00 74.15 N ANISOU 602 N HIS A 103 8784 11228 8159 -26 9 -117 N ATOM 603 CA HIS A 103 21.652 8.683 19.858 1.00 77.46 C ANISOU 603 CA HIS A 103 9226 11651 8553 -18 20 -136 C ATOM 604 C HIS A 103 21.212 7.300 20.353 1.00 77.29 C ANISOU 604 C HIS A 103 9288 11570 8507 -10 12 -153 C ATOM 605 O HIS A 103 21.320 6.337 19.580 1.00101.02 O ANISOU 605 O HIS A 103 12322 14569 11491 6 16 -176 O ATOM 606 CB HIS A 103 22.948 8.618 19.031 1.00 76.48 C ANISOU 606 CB HIS A 103 9060 11570 8429 25 23 -152 C ATOM 607 CG HIS A 103 23.532 9.959 18.760 1.00 75.54 C ANISOU 607 CG HIS A 103 8866 11499 8335 14 35 -136 C ATOM 608 ND1 HIS A 103 24.779 10.329 19.219 1.00 96.02 N ANISOU 608 ND1 HIS A 103 11418 14115 10947 44 26 -146 N ATOM 609 CD2 HIS A 103 23.013 11.043 18.152 1.00 82.34 C ANISOU 609 CD2 HIS A 103 9691 12388 9206 -24 56 -110 C ATOM 610 CE1 HIS A 103 25.025 11.569 18.862 1.00103.03 C ANISOU 610 CE1 HIS A 103 12248 15040 11857 16 46 -129 C ATOM 611 NE2 HIS A 103 23.953 12.030 18.211 1.00 92.07 N ANISOU 611 NE2 HIS A 103 10867 13652 10463 -23 64 -104 N ATOM 612 N TYR A 104 20.720 7.197 21.584 1.00 79.49 N ANISOU 612 N TYR A 104 9610 11805 8787 -24 3 -144 N ATOM 613 CA TYR A 104 20.132 5.909 22.038 1.00 92.57 C ANISOU 613 CA TYR A 104 11357 13397 10417 -30 5 -157 C ATOM 614 C TYR A 104 18.651 5.945 21.661 1.00 94.17 C ANISOU 614 C TYR A 104 11566 13598 10614 -100 26 -156 C ATOM 615 O TYR A 104 18.016 6.992 21.826 1.00 97.43 O ANISOU 615 O TYR A 104 11933 14040 11043 -136 31 -137 O ATOM 616 CB TYR A 104 20.390 5.666 23.532 1.00 96.24 C ANISOU 616 CB TYR A 104 11874 13814 10878 -5 -11 -149 C ATOM 617 CG TYR A 104 21.843 5.796 23.927 1.00103.10 C ANISOU 617 CG TYR A 104 12720 14700 11751 66 -38 -156 C ATOM 618 CD1 TYR A 104 22.791 4.899 23.450 1.00101.37 C ANISOU 618 CD1 TYR A 104 12522 14477 11514 127 -48 -181 C ATOM 619 CD2 TYR A 104 22.278 6.829 24.749 1.00 87.95 C ANISOU 619 CD2 TYR A 104 10754 12806 9856 75 -53 -143 C ATOM 620 CE1 TYR A 104 24.132 5.024 23.777 1.00115.86 C ANISOU 620 CE1 TYR A 104 14327 16340 13353 197 -73 -195 C ATOM 621 CE2 TYR A 104 23.614 6.962 25.093 1.00103.61 C ANISOU 621 CE2 TYR A 104 12706 14815 11844 138 -77 -158 C ATOM 622 CZ TYR A 104 24.545 6.056 24.604 1.00115.03 C ANISOU 622 CZ TYR A 104 14170 16265 13272 201 -88 -185 C ATOM 623 OH TYR A 104 25.870 6.177 24.915 1.00 95.29 O ANISOU 623 OH TYR A 104 11630 13800 10774 267 -114 -207 O ATOM 624 N SER A 105 18.134 4.841 21.129 1.00 85.37 N ANISOU 624 N SER A 105 10504 12455 9477 -117 39 -179 N ATOM 625 CA SER A 105 16.734 4.783 20.642 1.00 80.39 C ANISOU 625 CA SER A 105 9871 11833 8839 -185 59 -190 C ATOM 626 C SER A 105 16.136 3.399 20.913 1.00 91.31 C ANISOU 626 C SER A 105 11345 13149 10199 -213 73 -215 C ATOM 627 O SER A 105 16.889 2.409 21.029 1.00113.96 O ANISOU 627 O SER A 105 14278 15969 13053 -171 68 -226 O ATOM 628 CB SER A 105 16.637 5.154 19.179 1.00 67.87 C ANISOU 628 CB SER A 105 8225 10310 7252 -188 64 -201 C ATOM 629 N THR A 106 14.810 3.370 21.040 1.00 90.34 N ANISOU 629 N THR A 106 11227 13024 10072 -284 93 -225 N ATOM 630 CA THR A 106 13.975 2.142 21.020 1.00 86.30 C ANISOU 630 CA THR A 106 10790 12460 9540 -335 117 -257 C ATOM 631 C THR A 106 13.105 2.184 19.759 1.00 86.87 C ANISOU 631 C THR A 106 10811 12587 9607 -379 127 -290 C ATOM 632 O THR A 106 12.874 3.296 19.249 1.00 99.66 O ANISOU 632 O THR A 106 12346 14280 11237 -377 118 -279 O ATOM 633 CB THR A 106 13.119 2.083 22.289 1.00 88.84 C ANISOU 633 CB THR A 106 11153 12740 9858 -388 134 -248 C ATOM 634 OG1 THR A 106 12.486 3.354 22.436 1.00 85.46 O ANISOU 634 OG1 THR A 106 10645 12377 9449 -413 131 -232 O ATOM 635 CG2 THR A 106 13.926 1.796 23.537 1.00 89.86 C ANISOU 635 CG2 THR A 106 11352 12806 9982 -343 125 -220 C ATOM 636 N GLY A 107 12.635 1.037 19.266 1.00102.53 N ANISOU 636 N GLY A 107 12847 14537 11572 -414 145 -331 N ATOM 637 CA GLY A 107 11.814 0.968 18.036 1.00108.63 C ANISOU 637 CA GLY A 107 13572 15365 12335 -453 152 -371 C ATOM 638 C GLY A 107 10.392 1.469 18.259 1.00107.25 C ANISOU 638 C GLY A 107 13354 15232 12163 -526 167 -386 C ATOM 639 O GLY A 107 9.446 0.683 18.035 1.00117.96 O ANISOU 639 O GLY A 107 14734 16576 13507 -593 189 -433 O ATOM 640 N VAL A 108 10.255 2.726 18.696 1.00 89.55 N ANISOU 640 N VAL A 108 11051 13037 9937 -516 155 -352 N ATOM 641 CA VAL A 108 8.946 3.365 19.027 1.00 89.54 C ANISOU 641 CA VAL A 108 11000 13081 9937 -574 165 -363 C ATOM 642 C VAL A 108 8.879 4.714 18.290 1.00 90.26 C ANISOU 642 C VAL A 108 10997 13262 10033 -538 143 -347 C ATOM 643 O VAL A 108 9.878 5.470 18.353 1.00 81.45 O ANISOU 643 O VAL A 108 9865 12151 8931 -478 126 -304 O ATOM 644 CB VAL A 108 8.775 3.515 20.559 1.00 88.28 C ANISOU 644 CB VAL A 108 10878 12876 9787 -596 176 -336 C ATOM 645 CG1 VAL A 108 7.565 4.359 20.937 1.00 77.08 C ANISOU 645 CG1 VAL A 108 9400 11515 8372 -642 182 -343 C ATOM 646 CG2 VAL A 108 8.685 2.167 21.263 1.00 94.77 C ANISOU 646 CG2 VAL A 108 11803 13607 10597 -637 204 -352 C ATOM 647 N HIS A 109 7.749 5.009 17.628 1.00 93.45 N ANISOU 647 N HIS A 109 11346 13736 10425 -571 145 -382 N ATOM 648 CA HIS A 109 7.488 6.310 16.956 1.00 94.09 C ANISOU 648 CA HIS A 109 11346 13901 10502 -536 125 -368 C ATOM 649 C HIS A 109 7.869 7.457 17.895 1.00 85.93 C ANISOU 649 C HIS A 109 10297 12861 9490 -507 116 -314 C ATOM 650 O HIS A 109 7.494 7.416 19.078 1.00 94.57 O ANISOU 650 O HIS A 109 11413 13922 10594 -541 126 -308 O ATOM 651 CB HIS A 109 6.011 6.470 16.579 1.00105.80 C ANISOU 651 CB HIS A 109 12776 15455 11968 -582 128 -416 C ATOM 652 CG HIS A 109 5.539 5.655 15.422 1.00126.63 C ANISOU 652 CG HIS A 109 15404 18126 14581 -603 131 -475 C ATOM 653 ND1 HIS A 109 4.334 4.962 15.465 1.00114.21 N ANISOU 653 ND1 HIS A 109 13823 16573 12997 -677 148 -538 N ATOM 654 CD2 HIS A 109 6.048 5.455 14.183 1.00105.76 C ANISOU 654 CD2 HIS A 109 12753 15508 11922 -563 120 -485 C ATOM 655 CE1 HIS A 109 4.126 4.361 14.307 1.00 92.53 C ANISOU 655 CE1 HIS A 109 11065 13861 10229 -681 145 -588 C ATOM 656 NE2 HIS A 109 5.164 4.642 13.503 1.00 93.72 N ANISOU 656 NE2 HIS A 109 11218 14015 10376 -609 127 -554 N ATOM 657 N GLU A 110 8.540 8.472 17.366 1.00 86.51 N ANISOU 657 N GLU A 110 10334 12966 9569 -450 99 -278 N ATOM 658 CA GLU A 110 8.873 9.698 18.130 1.00 79.23 C ANISOU 658 CA GLU A 110 9391 12043 8667 -423 89 -231 C ATOM 659 C GLU A 110 7.589 10.422 18.573 1.00 69.96 C ANISOU 659 C GLU A 110 8180 10913 7489 -450 88 -241 C ATOM 660 O GLU A 110 7.581 10.992 19.685 1.00 76.19 O ANISOU 660 O GLU A 110 8972 11680 8295 -453 87 -217 O ATOM 661 CB GLU A 110 9.733 10.586 17.237 1.00 78.18 C ANISOU 661 CB GLU A 110 9228 11940 8536 -366 79 -198 C ATOM 662 CG GLU A 110 10.190 11.832 17.935 1.00 79.53 C ANISOU 662 CG GLU A 110 9383 12105 8730 -341 72 -153 C ATOM 663 CD GLU A 110 11.084 12.683 17.068 1.00 68.65 C ANISOU 663 CD GLU A 110 7981 10748 7353 -294 69 -121 C ATOM 664 OE1 GLU A 110 12.286 12.358 16.985 1.00 63.57 O ANISOU 664 OE1 GLU A 110 7354 10077 6722 -273 72 -109 O ATOM 665 OE2 GLU A 110 10.560 13.643 16.476 1.00 57.85 O ANISOU 665 OE2 GLU A 110 6580 9426 5972 -277 66 -110 O ATOM 666 N SER A 111 6.553 10.408 17.727 1.00 67.49 N ANISOU 666 N SER A 111 7827 10663 7150 -464 87 -280 N ATOM 667 CA SER A 111 5.249 11.070 17.995 1.00 64.40 C ANISOU 667 CA SER A 111 7390 10330 6749 -483 83 -301 C ATOM 668 C SER A 111 4.676 10.612 19.341 1.00 66.25 C ANISOU 668 C SER A 111 7647 10529 6994 -541 100 -315 C ATOM 669 O SER A 111 3.920 11.389 19.950 1.00 66.45 O ANISOU 669 O SER A 111 7641 10587 7020 -546 97 -315 O ATOM 670 CB SER A 111 4.282 10.822 16.878 1.00 61.33 C ANISOU 670 CB SER A 111 6958 10014 6327 -492 78 -354 C ATOM 671 OG SER A 111 4.399 9.493 16.411 1.00 88.26 O ANISOU 671 OG SER A 111 10400 13402 9731 -528 91 -393 O ATOM 672 N LEU A 112 5.031 9.403 19.785 1.00 71.12 N ANISOU 672 N LEU A 112 8324 11080 7617 -580 120 -326 N ATOM 673 CA LEU A 112 4.445 8.792 21.010 1.00 76.40 C ANISOU 673 CA LEU A 112 9027 11710 8289 -643 144 -342 C ATOM 674 C LEU A 112 5.277 9.193 22.233 1.00 87.43 C ANISOU 674 C LEU A 112 10464 13047 9708 -618 141 -290 C ATOM 675 O LEU A 112 4.676 9.574 23.260 1.00 85.80 O ANISOU 675 O LEU A 112 10252 12843 9504 -642 149 -287 O ATOM 676 CB LEU A 112 4.410 7.268 20.848 1.00 86.76 C ANISOU 676 CB LEU A 112 10397 12975 9593 -695 169 -379 C ATOM 677 CG LEU A 112 3.583 6.517 21.888 1.00 94.54 C ANISOU 677 CG LEU A 112 11420 13926 10574 -775 204 -407 C ATOM 678 CD1 LEU A 112 2.118 6.451 21.473 1.00105.51 C ANISOU 678 CD1 LEU A 112 12749 15393 11947 -835 217 -471 C ATOM 679 CD2 LEU A 112 4.141 5.119 22.096 1.00102.57 C ANISOU 679 CD2 LEU A 112 12531 14851 11588 -803 227 -412 C ATOM 680 N THR A 113 6.611 9.091 22.129 1.00 90.68 N ANISOU 680 N THR A 113 10910 13412 10132 -571 130 -254 N ATOM 681 CA THR A 113 7.507 9.393 23.275 1.00 66.64 C ANISOU 681 CA THR A 113 7902 10313 7106 -543 123 -211 C ATOM 682 C THR A 113 7.491 10.898 23.545 1.00 62.80 C ANISOU 682 C THR A 113 7361 9865 6633 -509 104 -181 C ATOM 683 O THR A 113 7.672 11.269 24.717 1.00 69.79 O ANISOU 683 O THR A 113 8263 10722 7530 -505 103 -159 O ATOM 684 CB THR A 113 8.920 8.838 23.064 1.00 60.04 C ANISOU 684 CB THR A 113 7108 9425 6276 -499 115 -191 C ATOM 685 OG1 THR A 113 9.593 9.590 22.060 1.00 68.75 O ANISOU 685 OG1 THR A 113 8166 10568 7388 -450 97 -175 O ATOM 686 CG2 THR A 113 8.915 7.377 22.677 1.00 59.11 C ANISOU 686 CG2 THR A 113 7047 9268 6142 -527 132 -223 C ATOM 687 N CYS A 114 7.258 11.737 22.534 1.00 58.15 N ANISOU 687 N CYS A 114 6716 9336 6041 -483 92 -182 N ATOM 688 CA CYS A 114 7.240 13.192 22.839 1.00 63.04 C ANISOU 688 CA CYS A 114 7296 9982 6672 -449 76 -152 C ATOM 689 C CYS A 114 5.839 13.594 23.291 1.00 59.92 C ANISOU 689 C CYS A 114 6868 9631 6264 -479 80 -177 C ATOM 690 O CYS A 114 5.684 14.716 23.811 1.00 52.84 O ANISOU 690 O CYS A 114 5950 8750 5378 -456 68 -156 O ATOM 691 CB CYS A 114 7.781 14.041 21.688 1.00 71.36 C ANISOU 691 CB CYS A 114 8317 11068 7727 -400 62 -131 C ATOM 692 SG CYS A 114 6.692 14.260 20.255 1.00 59.86 S ANISOU 692 SG CYS A 114 6812 9694 6237 -394 58 -163 S ATOM 693 N GLN A 115 4.872 12.700 23.105 1.00 63.63 N ANISOU 693 N GLN A 115 7337 10124 6716 -530 96 -222 N ATOM 694 CA GLN A 115 3.462 12.961 23.475 1.00 63.45 C ANISOU 694 CA GLN A 115 7274 10155 6677 -564 103 -258 C ATOM 695 C GLN A 115 3.281 12.602 24.954 1.00 61.60 C ANISOU 695 C GLN A 115 7078 9876 6450 -606 123 -255 C ATOM 696 O GLN A 115 2.555 13.315 25.659 1.00 54.05 O ANISOU 696 O GLN A 115 6092 8951 5491 -610 122 -259 O ATOM 697 CB GLN A 115 2.554 12.161 22.545 1.00 77.73 C ANISOU 697 CB GLN A 115 9057 12013 8461 -604 114 -315 C ATOM 698 CG GLN A 115 1.126 12.001 23.047 1.00 99.43 C ANISOU 698 CG GLN A 115 11772 14812 11195 -661 131 -366 C ATOM 699 CD GLN A 115 0.159 11.530 21.986 1.00 98.44 C ANISOU 699 CD GLN A 115 11598 14760 11044 -689 134 -430 C ATOM 700 OE1 GLN A 115 0.514 11.312 20.818 1.00 93.53 O ANISOU 700 OE1 GLN A 115 10971 14152 10413 -663 121 -437 O ATOM 701 NE2 GLN A 115 -1.088 11.381 22.407 1.00 66.60 N ANISOU 701 NE2 GLN A 115 7527 10779 6998 -743 151 -482 N ATOM 702 N VAL A 116 3.976 11.554 25.389 1.00 56.15 N ANISOU 702 N VAL A 116 6455 9114 5764 -628 139 -246 N ATOM 703 CA VAL A 116 3.884 10.965 26.755 1.00 59.63 C ANISOU 703 CA VAL A 116 6951 9500 6203 -668 163 -241 C ATOM 704 C VAL A 116 4.725 11.827 27.705 1.00 64.53 C ANISOU 704 C VAL A 116 7585 10089 6842 -618 143 -194 C ATOM 705 O VAL A 116 4.224 12.249 28.769 1.00 66.98 O ANISOU 705 O VAL A 116 7894 10404 7151 -632 150 -190 O ATOM 706 CB VAL A 116 4.343 9.488 26.744 1.00 63.83 C ANISOU 706 CB VAL A 116 7560 9963 6728 -700 185 -250 C ATOM 707 CG1 VAL A 116 4.576 8.940 28.148 1.00 62.86 C ANISOU 707 CG1 VAL A 116 7512 9769 6600 -720 206 -231 C ATOM 708 CG2 VAL A 116 3.360 8.593 25.996 1.00 62.81 C ANISOU 708 CG2 VAL A 116 7421 9862 6582 -765 211 -306 C ATOM 709 N PHE A 117 5.966 12.090 27.319 1.00 55.98 N ANISOU 709 N PHE A 117 6512 8980 5776 -564 121 -162 N ATOM 710 CA PHE A 117 6.930 12.915 28.078 1.00 59.05 C ANISOU 710 CA PHE A 117 6908 9342 6185 -515 100 -122 C ATOM 711 C PHE A 117 6.347 14.313 28.334 1.00 50.04 C ANISOU 711 C PHE A 117 5712 8249 5052 -499 86 -115 C ATOM 712 O PHE A 117 6.477 14.822 29.434 1.00 54.55 O ANISOU 712 O PHE A 117 6293 8802 5630 -489 81 -100 O ATOM 713 CB PHE A 117 8.251 12.980 27.305 1.00 65.03 C ANISOU 713 CB PHE A 117 7667 10081 6958 -467 81 -101 C ATOM 714 CG PHE A 117 9.224 13.986 27.850 1.00 58.65 C ANISOU 714 CG PHE A 117 6849 9261 6175 -421 59 -68 C ATOM 715 CD1 PHE A 117 9.973 13.692 28.972 1.00 56.96 C ANISOU 715 CD1 PHE A 117 6679 8998 5965 -406 54 -54 C ATOM 716 CD2 PHE A 117 9.362 15.227 27.253 1.00 54.74 C ANISOU 716 CD2 PHE A 117 6302 8801 5693 -392 45 -54 C ATOM 717 CE1 PHE A 117 10.870 14.618 29.487 1.00 64.77 C ANISOU 717 CE1 PHE A 117 7652 9980 6977 -367 32 -33 C ATOM 718 CE2 PHE A 117 10.243 16.155 27.782 1.00 61.03 C ANISOU 718 CE2 PHE A 117 7090 9582 6514 -358 29 -29 C ATOM 719 CZ PHE A 117 10.996 15.851 28.896 1.00 57.53 C ANISOU 719 CZ PHE A 117 6682 9097 6079 -348 21 -21 C ATOM 720 N GLY A 118 5.792 14.955 27.313 1.00 51.14 N ANISOU 720 N GLY A 118 5797 8446 5188 -487 78 -127 N ATOM 721 CA GLY A 118 5.297 16.340 27.408 1.00 52.05 C ANISOU 721 CA GLY A 118 5866 8604 5307 -459 63 -119 C ATOM 722 C GLY A 118 4.099 16.410 28.311 1.00 57.22 C ANISOU 722 C GLY A 118 6507 9287 5947 -493 74 -144 C ATOM 723 O GLY A 118 3.919 17.456 28.966 1.00 63.96 O ANISOU 723 O GLY A 118 7343 10152 6808 -468 62 -133 O ATOM 724 N TYR A 119 3.326 15.316 28.350 1.00 70.33 N ANISOU 724 N TYR A 119 8177 10957 7588 -549 100 -180 N ATOM 725 CA TYR A 119 2.136 15.133 29.229 1.00 60.24 C ANISOU 725 CA TYR A 119 6888 9707 6293 -598 122 -212 C ATOM 726 C TYR A 119 2.639 14.995 30.666 1.00 75.11 C ANISOU 726 C TYR A 119 8824 11529 8181 -604 131 -186 C ATOM 727 O TYR A 119 2.224 15.814 31.516 1.00 71.74 O ANISOU 727 O TYR A 119 8379 11123 7754 -592 126 -183 O ATOM 728 CB TYR A 119 1.309 13.910 28.806 1.00 61.77 C ANISOU 728 CB TYR A 119 7084 9919 6466 -666 153 -259 C ATOM 729 CG TYR A 119 0.247 13.481 29.791 1.00 62.18 C ANISOU 729 CG TYR A 119 7138 9987 6500 -731 187 -292 C ATOM 730 CD1 TYR A 119 -0.943 14.178 29.911 1.00 66.72 C ANISOU 730 CD1 TYR A 119 7644 10643 7062 -738 187 -326 C ATOM 731 CD2 TYR A 119 0.436 12.386 30.615 1.00 61.44 C ANISOU 731 CD2 TYR A 119 7116 9828 6400 -782 221 -288 C ATOM 732 CE1 TYR A 119 -1.918 13.808 30.826 1.00 72.20 C ANISOU 732 CE1 TYR A 119 8335 11359 7739 -800 223 -359 C ATOM 733 CE2 TYR A 119 -0.523 12.006 31.540 1.00 66.32 C ANISOU 733 CE2 TYR A 119 7741 10458 7000 -846 259 -315 C ATOM 734 CZ TYR A 119 -1.709 12.717 31.645 1.00 71.58 C ANISOU 734 CZ TYR A 119 8330 11210 7654 -859 261 -353 C ATOM 735 OH TYR A 119 -2.675 12.374 32.549 1.00 66.32 O ANISOU 735 OH TYR A 119 7663 10565 6969 -925 302 -383 O ATOM 736 N ILE A 120 3.531 14.016 30.897 1.00 61.87 N ANISOU 736 N ILE A 120 7215 9784 6508 -613 140 -169 N ATOM 737 CA ILE A 120 4.074 13.649 32.236 1.00 50.52 C ANISOU 737 CA ILE A 120 5842 8284 5068 -615 149 -146 C ATOM 738 C ILE A 120 4.675 14.908 32.856 1.00 46.33 C ANISOU 738 C ILE A 120 5293 7753 4557 -558 118 -116 C ATOM 739 O ILE A 120 4.398 15.182 34.001 1.00 56.39 O ANISOU 739 O ILE A 120 6579 9022 5823 -563 123 -113 O ATOM 740 CB ILE A 120 5.093 12.495 32.134 1.00 51.87 C ANISOU 740 CB ILE A 120 6084 8384 5237 -612 154 -131 C ATOM 741 CG1 ILE A 120 4.411 11.156 31.836 1.00 54.22 C ANISOU 741 CG1 ILE A 120 6420 8668 5513 -679 193 -162 C ATOM 742 CG2 ILE A 120 5.947 12.416 33.388 1.00 48.89 C ANISOU 742 CG2 ILE A 120 5767 7948 4858 -583 147 -101 C ATOM 743 CD1 ILE A 120 5.358 9.999 31.591 1.00 56.42 C ANISOU 743 CD1 ILE A 120 6772 8875 5787 -671 197 -152 C ATOM 744 N ILE A 121 5.462 15.662 32.112 1.00 43.84 N ANISOU 744 N ILE A 121 4948 7443 4264 -509 89 -97 N ATOM 745 CA ILE A 121 6.179 16.849 32.660 1.00 47.58 C ANISOU 745 CA ILE A 121 5409 7907 4759 -459 61 -71 C ATOM 746 C ILE A 121 5.128 17.895 33.027 1.00 43.91 C ANISOU 746 C ILE A 121 4900 7493 4290 -458 58 -84 C ATOM 747 O ILE A 121 5.188 18.443 34.128 1.00 59.98 O ANISOU 747 O ILE A 121 6943 9517 6328 -445 51 -76 O ATOM 748 CB ILE A 121 7.234 17.385 31.665 1.00 50.92 C ANISOU 748 CB ILE A 121 5813 8326 5208 -417 39 -52 C ATOM 749 CG1 ILE A 121 8.379 16.387 31.441 1.00 53.74 C ANISOU 749 CG1 ILE A 121 6212 8636 5568 -410 39 -42 C ATOM 750 CG2 ILE A 121 7.751 18.744 32.107 1.00 50.00 C ANISOU 750 CG2 ILE A 121 5674 8207 5115 -378 16 -33 C ATOM 751 CD1 ILE A 121 9.205 16.050 32.662 1.00 53.20 C ANISOU 751 CD1 ILE A 121 6191 8519 5500 -393 32 -30 C ATOM 752 N SER A 122 4.230 18.191 32.110 1.00 46.17 N ANISOU 752 N SER A 122 5138 7834 4567 -465 60 -105 N ATOM 753 CA SER A 122 3.203 19.220 32.363 1.00 55.15 C ANISOU 753 CA SER A 122 6230 9026 5697 -453 54 -120 C ATOM 754 C SER A 122 2.455 18.854 33.649 1.00 57.39 C ANISOU 754 C SER A 122 6528 9314 5962 -490 75 -139 C ATOM 755 O SER A 122 2.188 19.774 34.455 1.00 43.29 O ANISOU 755 O SER A 122 4728 7542 4178 -467 65 -137 O ATOM 756 CB SER A 122 2.280 19.343 31.185 1.00 58.24 C ANISOU 756 CB SER A 122 6572 9482 6073 -454 54 -148 C ATOM 757 OG SER A 122 2.834 20.235 30.236 1.00 60.66 O ANISOU 757 OG SER A 122 6862 9791 6393 -402 30 -125 O ATOM 758 N VAL A 123 2.124 17.567 33.824 1.00 56.62 N ANISOU 758 N VAL A 123 6461 9205 5847 -547 107 -156 N ATOM 759 CA VAL A 123 1.357 17.085 35.013 1.00 46.77 C ANISOU 759 CA VAL A 123 5233 7960 4576 -594 138 -174 C ATOM 760 C VAL A 123 2.202 17.294 36.261 1.00 43.74 C ANISOU 760 C VAL A 123 4899 7520 4197 -567 129 -142 C ATOM 761 O VAL A 123 1.695 17.854 37.216 1.00 49.44 O ANISOU 761 O VAL A 123 5612 8263 4910 -564 131 -148 O ATOM 762 CB VAL A 123 0.950 15.608 34.860 1.00 47.56 C ANISOU 762 CB VAL A 123 5369 8045 4656 -664 179 -196 C ATOM 763 CG1 VAL A 123 0.626 14.985 36.201 1.00 63.89 C ANISOU 763 CG1 VAL A 123 7489 10084 6701 -708 214 -198 C ATOM 764 CG2 VAL A 123 -0.221 15.447 33.909 1.00 48.73 C ANISOU 764 CG2 VAL A 123 5455 8266 4791 -702 193 -244 C ATOM 765 N LEU A 124 3.446 16.827 36.242 1.00 49.03 N ANISOU 765 N LEU A 124 5619 8128 4880 -546 117 -113 N ATOM 766 CA LEU A 124 4.376 16.942 37.391 1.00 47.27 C ANISOU 766 CA LEU A 124 5445 7854 4660 -514 104 -86 C ATOM 767 C LEU A 124 4.592 18.426 37.705 1.00 48.78 C ANISOU 767 C LEU A 124 5594 8066 4873 -465 70 -78 C ATOM 768 O LEU A 124 4.705 18.775 38.883 1.00 45.94 O ANISOU 768 O LEU A 124 5254 7695 4506 -450 65 -73 O ATOM 769 CB LEU A 124 5.688 16.245 37.020 1.00 50.48 C ANISOU 769 CB LEU A 124 5896 8204 5077 -491 91 -64 C ATOM 770 CG LEU A 124 5.573 14.734 36.840 1.00 53.86 C ANISOU 770 CG LEU A 124 6383 8597 5483 -535 124 -70 C ATOM 771 CD1 LEU A 124 6.781 14.170 36.127 1.00 59.84 C ANISOU 771 CD1 LEU A 124 7168 9314 6253 -504 107 -55 C ATOM 772 CD2 LEU A 124 5.411 14.058 38.181 1.00 59.37 C ANISOU 772 CD2 LEU A 124 7151 9257 6148 -554 148 -64 C ATOM 773 N LYS A 125 4.655 19.259 36.668 1.00 45.27 N ANISOU 773 N LYS A 125 5099 7649 4450 -439 50 -78 N ATOM 774 CA LYS A 125 4.829 20.732 36.796 1.00 47.73 C ANISOU 774 CA LYS A 125 5376 7975 4783 -394 21 -70 C ATOM 775 C LYS A 125 3.587 21.360 37.441 1.00 48.50 C ANISOU 775 C LYS A 125 5444 8120 4863 -399 28 -93 C ATOM 776 O LYS A 125 3.680 22.467 37.940 1.00 56.90 O ANISOU 776 O LYS A 125 6494 9186 5937 -363 7 -90 O ATOM 777 CB LYS A 125 5.091 21.356 35.419 1.00 55.64 C ANISOU 777 CB LYS A 125 6343 8992 5806 -369 6 -63 C ATOM 778 CG LYS A 125 6.549 21.415 34.986 1.00 61.02 C ANISOU 778 CG LYS A 125 7039 9628 6515 -344 -9 -38 C ATOM 779 CD LYS A 125 7.224 22.709 35.366 1.00 60.22 C ANISOU 779 CD LYS A 125 6928 9510 6441 -307 -33 -25 C ATOM 780 CE LYS A 125 8.725 22.566 35.409 1.00 73.42 C ANISOU 780 CE LYS A 125 8618 11139 8137 -292 -46 -9 C ATOM 781 NZ LYS A 125 9.159 21.360 36.166 1.00 76.55 N ANISOU 781 NZ LYS A 125 9057 11509 8519 -303 -41 -11 N ATOM 782 N SER A 126 2.436 20.719 37.321 1.00 54.43 N ANISOU 782 N SER A 126 6180 8913 5586 -442 56 -121 N ATOM 783 CA SER A 126 1.174 21.205 37.921 1.00 55.81 C ANISOU 783 CA SER A 126 6320 9145 5739 -451 67 -150 C ATOM 784 C SER A 126 1.162 20.754 39.382 1.00 59.78 C ANISOU 784 C SER A 126 6866 9624 6223 -473 86 -148 C ATOM 785 O SER A 126 0.773 21.540 40.268 1.00 43.89 O ANISOU 785 O SER A 126 4840 7631 4202 -453 80 -157 O ATOM 786 CB SER A 126 -0.003 20.654 37.190 1.00 56.88 C ANISOU 786 CB SER A 126 6416 9341 5853 -493 92 -187 C ATOM 787 OG SER A 126 -1.205 21.150 37.757 1.00 55.61 O ANISOU 787 OG SER A 126 6212 9244 5670 -498 101 -221 O ATOM 788 N VAL A 127 1.641 19.534 39.615 1.00 47.66 N ANISOU 788 N VAL A 127 5388 8041 4678 -508 108 -136 N ATOM 789 CA VAL A 127 1.694 18.963 40.982 1.00 47.34 C ANISOU 789 CA VAL A 127 5404 7969 4611 -527 130 -129 C ATOM 790 C VAL A 127 2.570 19.848 41.879 1.00 49.01 C ANISOU 790 C VAL A 127 5632 8153 4836 -469 95 -109 C ATOM 791 O VAL A 127 2.171 20.107 43.014 1.00 52.35 O ANISOU 791 O VAL A 127 6065 8587 5238 -468 103 -115 O ATOM 792 CB VAL A 127 2.256 17.538 40.960 1.00 44.35 C ANISOU 792 CB VAL A 127 5097 7532 4220 -560 154 -114 C ATOM 793 CG1 VAL A 127 2.564 17.085 42.377 1.00 51.68 C ANISOU 793 CG1 VAL A 127 6097 8417 5120 -559 168 -98 C ATOM 794 CG2 VAL A 127 1.328 16.568 40.274 1.00 39.56 C ANISOU 794 CG2 VAL A 127 4485 6948 3597 -628 195 -140 C ATOM 795 N SER A 128 3.751 20.231 41.401 1.00 49.54 N ANISOU 795 N SER A 128 5701 8185 4935 -426 60 -87 N ATOM 796 CA SER A 128 4.671 21.123 42.145 1.00 54.45 C ANISOU 796 CA SER A 128 6329 8783 5575 -374 24 -75 C ATOM 797 C SER A 128 4.068 22.525 42.253 1.00 55.86 C ANISOU 797 C SER A 128 6455 9002 5764 -348 7 -90 C ATOM 798 O SER A 128 4.141 23.128 43.328 1.00 54.53 O ANISOU 798 O SER A 128 6295 8832 5592 -324 -5 -94 O ATOM 799 CB SER A 128 6.029 21.137 41.508 1.00 58.71 C ANISOU 799 CB SER A 128 6876 9283 6146 -344 -2 -56 C ATOM 800 OG SER A 128 6.613 19.845 41.583 1.00 60.34 O ANISOU 800 OG SER A 128 7138 9450 6337 -357 9 -44 O ATOM 801 N MET A 129 3.480 23.026 41.173 1.00 47.96 N ANISOU 801 N MET A 129 5407 8039 4777 -348 5 -100 N ATOM 802 CA MET A 129 2.872 24.375 41.188 1.00 54.60 C ANISOU 802 CA MET A 129 6203 8915 5624 -315 -12 -114 C ATOM 803 C MET A 129 1.734 24.425 42.226 1.00 64.73 C ANISOU 803 C MET A 129 7477 10242 6873 -328 6 -140 C ATOM 804 O MET A 129 1.561 25.474 42.882 1.00 50.34 O ANISOU 804 O MET A 129 5642 8431 5053 -293 -11 -149 O ATOM 805 CB MET A 129 2.326 24.704 39.811 1.00 58.19 C ANISOU 805 CB MET A 129 6615 9406 6086 -310 -13 -121 C ATOM 806 CG MET A 129 2.221 26.171 39.556 1.00 66.34 C ANISOU 806 CG MET A 129 7621 10450 7135 -259 -40 -122 C ATOM 807 SD MET A 129 1.077 26.458 38.186 1.00 70.57 S ANISOU 807 SD MET A 129 8105 11051 7656 -248 -38 -141 S ATOM 808 CE MET A 129 1.351 28.212 37.928 1.00 69.65 C ANISOU 808 CE MET A 129 7984 10917 7561 -179 -71 -129 C ATOM 809 N TRP A 130 0.964 23.342 42.350 1.00 57.13 N ANISOU 809 N TRP A 130 6522 9304 5880 -381 45 -154 N ATOM 810 CA TRP A 130 -0.199 23.307 43.270 1.00 57.03 C ANISOU 810 CA TRP A 130 6495 9342 5832 -404 72 -183 C ATOM 811 C TRP A 130 0.305 23.156 44.690 1.00 65.08 C ANISOU 811 C TRP A 130 7567 10324 6836 -398 74 -170 C ATOM 812 O TRP A 130 -0.170 23.938 45.558 1.00 57.17 O ANISOU 812 O TRP A 130 6549 9350 5820 -374 68 -187 O ATOM 813 CB TRP A 130 -1.182 22.189 42.889 1.00 65.99 C ANISOU 813 CB TRP A 130 7619 10515 6940 -472 117 -206 C ATOM 814 CG TRP A 130 -2.182 22.640 41.873 1.00 60.59 C ANISOU 814 CG TRP A 130 6862 9903 6256 -470 115 -239 C ATOM 815 CD1 TRP A 130 -2.344 22.182 40.601 1.00 62.20 C ANISOU 815 CD1 TRP A 130 7042 10123 6466 -490 118 -247 C ATOM 816 CD2 TRP A 130 -3.121 23.710 42.031 1.00 57.32 C ANISOU 816 CD2 TRP A 130 6390 9557 5832 -435 102 -271 C ATOM 817 NE1 TRP A 130 -3.341 22.871 39.968 1.00 51.57 N ANISOU 817 NE1 TRP A 130 5626 8854 5112 -469 109 -283 N ATOM 818 CE2 TRP A 130 -3.817 23.827 40.810 1.00 53.73 C ANISOU 818 CE2 TRP A 130 5878 9159 5376 -432 98 -297 C ATOM 819 CE3 TRP A 130 -3.450 24.559 43.089 1.00 56.91 C ANISOU 819 CE3 TRP A 130 6330 9526 5768 -402 94 -283 C ATOM 820 CZ2 TRP A 130 -4.839 24.748 40.632 1.00 65.39 C ANISOU 820 CZ2 TRP A 130 7291 10714 6838 -394 84 -334 C ATOM 821 CZ3 TRP A 130 -4.441 25.494 42.905 1.00 64.19 C ANISOU 821 CZ3 TRP A 130 7189 10521 6679 -366 81 -318 C ATOM 822 CH2 TRP A 130 -5.124 25.583 41.689 1.00 72.83 C ANISOU 822 CH2 TRP A 130 8228 11672 7770 -360 75 -344 C ATOM 823 N CYS A 131 1.215 22.188 44.896 1.00 57.87 N ANISOU 823 N CYS A 131 6715 9351 5920 -412 81 -144 N ATOM 824 CA CYS A 131 1.917 21.957 46.191 1.00 44.50 C ANISOU 824 CA CYS A 131 5082 7616 4209 -395 77 -127 C ATOM 825 C CYS A 131 2.354 23.309 46.750 1.00 38.02 C ANISOU 825 C CYS A 131 4240 6797 3408 -335 34 -131 C ATOM 826 O CYS A 131 2.188 23.506 47.924 1.00 58.32 O ANISOU 826 O CYS A 131 6830 9373 5953 -323 36 -138 O ATOM 827 CB CYS A 131 3.112 21.026 46.051 1.00 45.91 C ANISOU 827 CB CYS A 131 5321 7730 4393 -392 71 -99 C ATOM 828 SG CYS A 131 2.644 19.282 45.938 1.00 63.13 S ANISOU 828 SG CYS A 131 7560 9889 6535 -461 128 -93 S ATOM 829 N LEU A 132 2.825 24.232 45.922 1.00 40.68 N ANISOU 829 N LEU A 132 4539 7129 3786 -302 0 -129 N ATOM 830 CA LEU A 132 3.309 25.546 46.421 1.00 44.23 C ANISOU 830 CA LEU A 132 4974 7571 4258 -250 -39 -135 C ATOM 831 C LEU A 132 2.108 26.455 46.702 1.00 42.86 C ANISOU 831 C LEU A 132 4760 7452 4071 -238 -35 -163 C ATOM 832 O LEU A 132 2.222 27.333 47.576 1.00 61.79 O ANISOU 832 O LEU A 132 7158 9849 6470 -202 -56 -174 O ATOM 833 CB LEU A 132 4.315 26.187 45.448 1.00 45.95 C ANISOU 833 CB LEU A 132 5177 7757 4525 -224 -70 -121 C ATOM 834 CG LEU A 132 5.742 25.598 45.435 1.00 45.15 C ANISOU 834 CG LEU A 132 5110 7604 4440 -218 -85 -101 C ATOM 835 CD1 LEU A 132 6.604 26.208 44.324 1.00 52.48 C ANISOU 835 CD1 LEU A 132 6014 8509 5414 -204 -107 -91 C ATOM 836 CD2 LEU A 132 6.438 25.770 46.748 1.00 44.18 C ANISOU 836 CD2 LEU A 132 5017 7460 4308 -190 -106 -107 C ATOM 837 N ALA A 133 0.990 26.207 46.044 1.00 49.58 N ANISOU 837 N ALA A 133 5575 8353 4907 -265 -9 -178 N ATOM 838 CA ALA A 133 -0.281 26.932 46.277 1.00 55.37 C ANISOU 838 CA ALA A 133 6263 9152 5620 -253 -3 -212 C ATOM 839 C ALA A 133 -0.971 26.415 47.549 1.00 59.95 C ANISOU 839 C ALA A 133 6859 9762 6156 -280 29 -229 C ATOM 840 O ALA A 133 -1.719 27.181 48.173 1.00 60.82 O ANISOU 840 O ALA A 133 6941 9917 6248 -256 26 -256 O ATOM 841 CB ALA A 133 -1.163 26.784 45.063 1.00 59.54 C ANISOU 841 CB ALA A 133 6743 9730 6147 -271 9 -227 C ATOM 842 N CYS A 134 -0.720 25.173 47.953 1.00 53.82 N ANISOU 842 N CYS A 134 6130 8959 5357 -326 60 -213 N ATOM 843 CA CYS A 134 -1.386 24.567 49.130 1.00 49.19 C ANISOU 843 CA CYS A 134 5570 8397 4722 -359 101 -224 C ATOM 844 C CYS A 134 -0.627 24.935 50.398 1.00 45.97 C ANISOU 844 C CYS A 134 5207 7953 4304 -318 79 -213 C ATOM 845 O CYS A 134 -1.232 25.090 51.437 1.00 54.74 O ANISOU 845 O CYS A 134 6322 9096 5379 -317 96 -230 O ATOM 846 CB CYS A 134 -1.486 23.055 48.974 1.00 56.94 C ANISOU 846 CB CYS A 134 6594 9359 5680 -427 148 -211 C ATOM 847 SG CYS A 134 -2.787 22.546 47.808 1.00 72.95 S ANISOU 847 SG CYS A 134 8560 11454 7704 -491 188 -244 S ATOM 848 N ILE A 135 0.684 25.004 50.294 1.00 50.58 N ANISOU 848 N ILE A 135 5824 8476 4916 -286 42 -187 N ATOM 849 CA ILE A 135 1.599 25.480 51.368 1.00 51.29 C ANISOU 849 CA ILE A 135 5949 8533 5004 -237 9 -181 C ATOM 850 C ILE A 135 1.235 26.938 51.690 1.00 51.02 C ANISOU 850 C ILE A 135 5869 8531 4984 -192 -19 -210 C ATOM 851 O ILE A 135 1.186 27.273 52.881 1.00 70.83 O ANISOU 851 O ILE A 135 8396 11049 7466 -168 -25 -222 O ATOM 852 CB ILE A 135 3.052 25.301 50.864 1.00 50.92 C ANISOU 852 CB ILE A 135 5927 8426 4994 -216 -24 -157 C ATOM 853 CG1 ILE A 135 3.536 23.862 51.081 1.00 45.75 C ANISOU 853 CG1 ILE A 135 5339 7733 4310 -241 -1 -131 C ATOM 854 CG2 ILE A 135 3.996 26.333 51.476 1.00 51.17 C ANISOU 854 CG2 ILE A 135 5957 8436 5049 -159 -74 -165 C ATOM 855 CD1 ILE A 135 4.754 23.470 50.238 1.00 47.45 C ANISOU 855 CD1 ILE A 135 5566 7900 4559 -230 -25 -110 C ATOM 856 N SER A 136 1.001 27.750 50.649 1.00 44.83 N ANISOU 856 N SER A 136 5034 7760 4236 -179 -37 -218 N ATOM 857 CA SER A 136 0.714 29.205 50.733 1.00 43.79 C ANISOU 857 CA SER A 136 4866 7648 4123 -131 -68 -243 C ATOM 858 C SER A 136 -0.592 29.425 51.511 1.00 52.36 C ANISOU 858 C SER A 136 5928 8800 5166 -130 -44 -275 C ATOM 859 O SER A 136 -0.656 30.370 52.313 1.00 40.50 O ANISOU 859 O SER A 136 4422 7305 3658 -87 -66 -296 O ATOM 860 CB SER A 136 0.613 29.781 49.343 1.00 41.13 C ANISOU 860 CB SER A 136 4491 7311 3823 -121 -82 -240 C ATOM 861 OG SER A 136 -0.586 29.342 48.704 1.00 42.07 O ANISOU 861 OG SER A 136 4573 7489 3920 -151 -50 -254 O ATOM 862 N VAL A 137 -1.598 28.586 51.240 1.00 56.31 N ANISOU 862 N VAL A 137 6409 9348 5635 -179 0 -283 N ATOM 863 CA VAL A 137 -2.948 28.618 51.885 1.00 49.95 C ANISOU 863 CA VAL A 137 5573 8620 4785 -191 33 -319 C ATOM 864 C VAL A 137 -2.804 28.131 53.333 1.00 50.10 C ANISOU 864 C VAL A 137 5642 8631 4762 -202 54 -315 C ATOM 865 O VAL A 137 -3.401 28.751 54.235 1.00 39.96 O ANISOU 865 O VAL A 137 4343 7389 3451 -176 56 -343 O ATOM 866 CB VAL A 137 -3.954 27.758 51.092 1.00 45.69 C ANISOU 866 CB VAL A 137 4997 8133 4229 -251 78 -332 C ATOM 867 CG1 VAL A 137 -5.170 27.351 51.908 1.00 44.96 C ANISOU 867 CG1 VAL A 137 4884 8113 4083 -289 128 -365 C ATOM 868 CG2 VAL A 137 -4.346 28.457 49.800 1.00 50.04 C ANISOU 868 CG2 VAL A 137 5489 8713 4809 -225 54 -346 C ATOM 869 N ASP A 138 -2.036 27.062 53.535 1.00 48.59 N ANISOU 869 N ASP A 138 5511 8388 4562 -233 69 -282 N ATOM 870 CA ASP A 138 -1.821 26.429 54.862 1.00 52.98 C ANISOU 870 CA ASP A 138 6130 8928 5070 -241 92 -271 C ATOM 871 C ASP A 138 -1.163 27.447 55.800 1.00 43.81 C ANISOU 871 C ASP A 138 4980 7750 3912 -173 45 -279 C ATOM 872 O ASP A 138 -1.545 27.556 56.950 1.00 42.97 O ANISOU 872 O ASP A 138 4891 7671 3764 -161 59 -294 O ATOM 873 CB ASP A 138 -0.986 25.161 54.700 1.00 61.93 C ANISOU 873 CB ASP A 138 7331 9999 6199 -273 107 -231 C ATOM 874 CG ASP A 138 -0.767 24.384 55.982 1.00 65.80 C ANISOU 874 CG ASP A 138 7899 10467 6633 -279 134 -215 C ATOM 875 OD1 ASP A 138 -1.731 23.787 56.462 1.00 60.31 O ANISOU 875 OD1 ASP A 138 7216 9807 5890 -327 191 -223 O ATOM 876 OD2 ASP A 138 0.389 24.360 56.472 1.00 99.87 O ANISOU 876 OD2 ASP A 138 12264 14732 10950 -235 98 -195 O ATOM 877 N ARG A 139 -0.216 28.200 55.285 1.00 46.84 N ANISOU 877 N ARG A 139 5354 8093 4348 -131 -7 -274 N ATOM 878 CA ARG A 139 0.515 29.235 56.057 1.00 58.74 C ANISOU 878 CA ARG A 139 6869 9579 5868 -70 -56 -288 C ATOM 879 C ARG A 139 -0.416 30.445 56.225 1.00 46.53 C ANISOU 879 C ARG A 139 5272 8084 4322 -38 -65 -327 C ATOM 880 O ARG A 139 -0.296 31.133 57.246 1.00 41.96 O ANISOU 880 O ARG A 139 4703 7510 3728 2 -86 -348 O ATOM 881 CB ARG A 139 1.855 29.571 55.358 1.00 56.58 C ANISOU 881 CB ARG A 139 6599 9245 5651 -48 -102 -272 C ATOM 882 CG ARG A 139 2.871 28.430 55.338 1.00 52.84 C ANISOU 882 CG ARG A 139 6177 8725 5173 -64 -100 -240 C ATOM 883 CD ARG A 139 3.665 28.286 56.641 1.00 88.51 C ANISOU 883 CD ARG A 139 10745 13224 9659 -28 -121 -242 C ATOM 884 NE ARG A 139 2.877 27.989 57.851 1.00103.60 N ANISOU 884 NE ARG A 139 12685 15170 11505 -29 -90 -251 N ATOM 885 CZ ARG A 139 2.471 26.776 58.251 1.00 83.87 C ANISOU 885 CZ ARG A 139 10237 12675 8953 -63 -42 -229 C ATOM 886 NH1 ARG A 139 2.756 25.687 57.558 1.00 96.39 N ANISOU 886 NH1 ARG A 139 11853 14229 10542 -100 -20 -198 N ATOM 887 NH2 ARG A 139 1.769 26.647 59.357 1.00 84.14 N ANISOU 887 NH2 ARG A 139 10295 12743 8929 -63 -13 -239 N ATOM 888 N TYR A 140 -1.312 30.676 55.261 1.00 44.64 N ANISOU 888 N TYR A 140 4981 7882 4095 -53 -51 -338 N ATOM 889 CA TYR A 140 -2.333 31.760 55.337 1.00 50.57 C ANISOU 889 CA TYR A 140 5683 8690 4841 -17 -58 -377 C ATOM 890 C TYR A 140 -3.298 31.463 56.498 1.00 53.09 C ANISOU 890 C TYR A 140 6000 9072 5098 -28 -20 -402 C ATOM 891 O TYR A 140 -3.524 32.344 57.351 1.00 45.30 O ANISOU 891 O TYR A 140 5007 8106 4096 18 -38 -432 O ATOM 892 CB TYR A 140 -3.102 31.891 54.018 1.00 53.48 C ANISOU 892 CB TYR A 140 5998 9092 5227 -28 -50 -384 C ATOM 893 CG TYR A 140 -4.124 32.999 53.997 1.00 47.25 C ANISOU 893 CG TYR A 140 5160 8362 4430 19 -62 -426 C ATOM 894 CD1 TYR A 140 -3.733 34.313 53.801 1.00 49.24 C ANISOU 894 CD1 TYR A 140 5412 8580 4716 83 -109 -435 C ATOM 895 CD2 TYR A 140 -5.472 32.741 54.183 1.00 47.67 C ANISOU 895 CD2 TYR A 140 5168 8504 4440 2 -24 -460 C ATOM 896 CE1 TYR A 140 -4.657 35.343 53.791 1.00 50.60 C ANISOU 896 CE1 TYR A 140 5547 8801 4877 136 -122 -473 C ATOM 897 CE2 TYR A 140 -6.413 33.762 54.167 1.00 48.68 C ANISOU 897 CE2 TYR A 140 5246 8691 4556 56 -38 -502 C ATOM 898 CZ TYR A 140 -6.006 35.074 53.965 1.00 48.86 C ANISOU 898 CZ TYR A 140 5276 8674 4611 128 -89 -508 C ATOM 899 OH TYR A 140 -6.885 36.129 53.926 1.00 42.24 O ANISOU 899 OH TYR A 140 4400 7887 3761 192 -107 -549 O ATOM 900 N LEU A 141 -3.799 30.226 56.551 1.00 51.13 N ANISOU 900 N LEU A 141 5762 8848 4814 -91 33 -391 N ATOM 901 CA LEU A 141 -4.817 29.773 57.531 1.00 55.89 C ANISOU 901 CA LEU A 141 6363 9517 5355 -120 85 -413 C ATOM 902 C LEU A 141 -4.225 29.719 58.951 1.00 57.88 C ANISOU 902 C LEU A 141 6676 9743 5571 -96 80 -405 C ATOM 903 O LEU A 141 -4.957 30.012 59.936 1.00 48.69 O ANISOU 903 O LEU A 141 5504 8634 4362 -83 100 -434 O ATOM 904 CB LEU A 141 -5.324 28.394 57.097 1.00 61.88 C ANISOU 904 CB LEU A 141 7129 10291 6092 -204 146 -399 C ATOM 905 CG LEU A 141 -6.259 28.380 55.882 1.00 63.17 C ANISOU 905 CG LEU A 141 7219 10508 6272 -234 162 -422 C ATOM 906 CD1 LEU A 141 -6.514 26.937 55.459 1.00 64.07 C ANISOU 906 CD1 LEU A 141 7353 10619 6370 -322 219 -406 C ATOM 907 CD2 LEU A 141 -7.576 29.104 56.176 1.00 57.05 C ANISOU 907 CD2 LEU A 141 6373 9833 5469 -215 175 -478 C ATOM 908 N ALA A 142 -2.955 29.338 59.066 1.00 53.74 N ANISOU 908 N ALA A 142 6211 9143 5062 -87 54 -370 N ATOM 909 CA ALA A 142 -2.260 29.277 60.365 1.00 46.61 C ANISOU 909 CA ALA A 142 5369 8215 4125 -54 41 -363 C ATOM 910 C ALA A 142 -2.190 30.685 60.951 1.00 47.08 C ANISOU 910 C ALA A 142 5402 8290 4196 14 -6 -400 C ATOM 911 O ALA A 142 -2.489 30.825 62.159 1.00 58.39 O ANISOU 911 O ALA A 142 6854 9753 5578 36 3 -418 O ATOM 912 CB ALA A 142 -0.906 28.681 60.188 1.00 43.81 C ANISOU 912 CB ALA A 142 5069 7784 3790 -49 15 -325 C ATOM 913 N ILE A 143 -1.900 31.681 60.111 1.00 42.91 N ANISOU 913 N ILE A 143 4833 7742 3727 46 -51 -412 N ATOM 914 CA ILE A 143 -1.716 33.100 60.545 1.00 50.39 C ANISOU 914 CA ILE A 143 5762 8687 4695 112 -101 -447 C ATOM 915 C ILE A 143 -3.082 33.797 60.720 1.00 55.79 C ANISOU 915 C ILE A 143 6395 9447 5355 130 -84 -489 C ATOM 916 O ILE A 143 -3.197 34.610 61.628 1.00 62.74 O ANISOU 916 O ILE A 143 7276 10344 6217 178 -104 -521 O ATOM 917 CB ILE A 143 -0.792 33.858 59.562 1.00 60.42 C ANISOU 917 CB ILE A 143 7021 9897 6038 133 -150 -441 C ATOM 918 CG1 ILE A 143 0.653 33.336 59.569 1.00 64.68 C ANISOU 918 CG1 ILE A 143 7604 10370 6599 127 -175 -412 C ATOM 919 CG2 ILE A 143 -0.843 35.357 59.810 1.00 57.50 C ANISOU 919 CG2 ILE A 143 6631 9525 5691 192 -192 -480 C ATOM 920 CD1 ILE A 143 1.274 33.140 60.959 1.00 81.09 C ANISOU 920 CD1 ILE A 143 9729 12443 8639 153 -189 -420 C ATOM 921 N THR A 144 -4.096 33.505 59.901 1.00 53.58 N ANISOU 921 N THR A 144 6069 9215 5071 97 -49 -493 N ATOM 922 CA THR A 144 -5.393 34.247 59.902 1.00 52.47 C ANISOU 922 CA THR A 144 5869 9153 4912 123 -39 -539 C ATOM 923 C THR A 144 -6.398 33.636 60.900 1.00 61.47 C ANISOU 923 C THR A 144 7002 10371 5981 94 16 -560 C ATOM 924 O THR A 144 -7.144 34.412 61.532 1.00 48.17 O ANISOU 924 O THR A 144 5287 8745 4270 137 14 -603 O ATOM 925 CB THR A 144 -6.018 34.290 58.505 1.00 51.33 C ANISOU 925 CB THR A 144 5672 9035 4796 109 -34 -541 C ATOM 926 OG1 THR A 144 -6.070 32.954 57.997 1.00 50.88 O ANISOU 926 OG1 THR A 144 5622 8979 4731 33 10 -512 O ATOM 927 CG2 THR A 144 -5.253 35.179 57.548 1.00 51.15 C ANISOU 927 CG2 THR A 144 5652 8946 4835 150 -87 -529 C ATOM 928 N LYS A 145 -6.441 32.303 61.027 1.00 59.40 N ANISOU 928 N LYS A 145 6769 10111 5689 23 69 -531 N ATOM 929 CA LYS A 145 -7.312 31.583 61.990 1.00 52.92 C ANISOU 929 CA LYS A 145 5954 9354 4798 -17 133 -544 C ATOM 930 C LYS A 145 -6.418 30.729 62.895 1.00 59.62 C ANISOU 930 C LYS A 145 6892 10145 5616 -35 147 -504 C ATOM 931 O LYS A 145 -6.414 29.499 62.774 1.00 56.56 O ANISOU 931 O LYS A 145 6541 9741 5207 -102 196 -472 O ATOM 932 CB LYS A 145 -8.376 30.782 61.222 1.00 49.42 C ANISOU 932 CB LYS A 145 5462 8970 4343 -91 192 -554 C ATOM 933 N PRO A 146 -5.611 31.346 63.800 1.00 64.83 N ANISOU 933 N PRO A 146 7591 10770 6270 26 102 -505 N ATOM 934 CA PRO A 146 -4.705 30.600 64.679 1.00 71.50 C ANISOU 934 CA PRO A 146 8521 11564 7080 25 105 -471 C ATOM 935 C PRO A 146 -5.421 29.703 65.703 1.00 89.49 C ANISOU 935 C PRO A 146 10839 13885 9275 -15 178 -466 C ATOM 936 O PRO A 146 -4.781 28.769 66.175 1.00 77.02 O ANISOU 936 O PRO A 146 9339 12260 7664 -32 195 -426 O ATOM 937 CB PRO A 146 -3.914 31.677 65.444 1.00 60.02 C ANISOU 937 CB PRO A 146 7081 10087 5636 107 39 -492 C ATOM 938 CG PRO A 146 -4.134 32.951 64.646 1.00 56.03 C ANISOU 938 CG PRO A 146 6506 9591 5191 145 -4 -526 C ATOM 939 CD PRO A 146 -5.500 32.798 64.022 1.00 59.75 C ANISOU 939 CD PRO A 146 6915 10133 5651 105 43 -544 C ATOM 940 N LEU A 147 -6.691 30.001 66.023 1.00 90.71 N ANISOU 940 N LEU A 147 10941 14127 9396 -29 218 -506 N ATOM 941 CA LEU A 147 -7.533 29.194 66.953 1.00 95.97 C ANISOU 941 CA LEU A 147 11636 14846 9982 -79 299 -507 C ATOM 942 C LEU A 147 -8.001 27.908 66.245 1.00 88.05 C ANISOU 942 C LEU A 147 10642 13840 8973 -179 369 -480 C ATOM 943 O LEU A 147 -7.988 26.814 66.844 1.00 85.61 O ANISOU 943 O LEU A 147 10409 13509 8608 -229 428 -448 O ATOM 944 CB LEU A 147 -8.732 30.039 67.403 1.00105.42 C ANISOU 944 CB LEU A 147 12758 16143 11151 -58 316 -567 C ATOM 945 CG LEU A 147 -8.486 31.021 68.551 1.00109.94 C ANISOU 945 CG LEU A 147 13344 16731 11697 25 274 -594 C ATOM 946 CD1 LEU A 147 -8.025 32.396 68.059 1.00100.32 C ANISOU 946 CD1 LEU A 147 12081 15491 10545 105 187 -622 C ATOM 947 CD2 LEU A 147 -9.746 31.149 69.408 1.00105.42 C ANISOU 947 CD2 LEU A 147 12735 16261 11057 15 332 -638 C ATOM 948 N SER A 148 -8.398 28.043 64.983 1.00 89.38 N ANISOU 948 N SER A 148 10739 14025 9194 -205 362 -495 N ATOM 949 CA SER A 148 -9.102 26.979 64.229 1.00 87.01 C ANISOU 949 CA SER A 148 10423 13744 8891 -303 430 -489 C ATOM 950 C SER A 148 -8.112 26.127 63.428 1.00 81.10 C ANISOU 950 C SER A 148 9733 12902 8180 -331 417 -436 C ATOM 951 O SER A 148 -8.511 25.022 63.041 1.00 87.28 O ANISOU 951 O SER A 148 10533 13680 8948 -416 479 -422 O ATOM 952 CB SER A 148 -10.160 27.580 63.331 1.00103.17 C ANISOU 952 CB SER A 148 12355 15875 10967 -311 429 -542 C ATOM 953 OG SER A 148 -11.049 28.412 64.066 1.00 95.69 O ANISOU 953 OG SER A 148 11352 15018 9985 -275 436 -594 O ATOM 954 N TYR A 149 -6.878 26.595 63.217 1.00 76.92 N ANISOU 954 N TYR A 149 9231 12299 7693 -265 342 -411 N ATOM 955 CA TYR A 149 -5.894 25.964 62.296 1.00 94.28 C ANISOU 955 CA TYR A 149 11468 14416 9936 -279 319 -368 C ATOM 956 C TYR A 149 -5.769 24.436 62.480 1.00110.24 C ANISOU 956 C TYR A 149 13576 16392 11916 -350 383 -327 C ATOM 957 O TYR A 149 -5.844 23.715 61.452 1.00127.19 O ANISOU 957 O TYR A 149 15716 18518 14091 -408 404 -314 O ATOM 958 CB TYR A 149 -4.520 26.611 62.452 1.00102.08 C ANISOU 958 CB TYR A 149 12487 15339 10958 -198 239 -351 C ATOM 959 CG TYR A 149 -3.480 26.027 61.526 1.00114.30 C ANISOU 959 CG TYR A 149 14068 16810 12552 -207 214 -312 C ATOM 960 CD1 TYR A 149 -3.656 26.033 60.147 1.00107.57 C ANISOU 960 CD1 TYR A 149 13161 15958 11753 -236 208 -314 C ATOM 961 CD2 TYR A 149 -2.324 25.457 62.034 1.00111.81 C ANISOU 961 CD2 TYR A 149 13836 16426 12220 -182 195 -275 C ATOM 962 CE1 TYR A 149 -2.710 25.489 59.296 1.00108.47 C ANISOU 962 CE1 TYR A 149 13303 16005 11905 -244 187 -280 C ATOM 963 CE2 TYR A 149 -1.364 24.918 61.194 1.00114.97 C ANISOU 963 CE2 TYR A 149 14263 16761 12659 -185 171 -243 C ATOM 964 CZ TYR A 149 -1.559 24.932 59.825 1.00106.89 C ANISOU 964 CZ TYR A 149 13183 15738 11690 -219 168 -245 C ATOM 965 OH TYR A 149 -0.612 24.398 58.999 1.00132.63 O ANISOU 965 OH TYR A 149 16468 18937 14986 -222 147 -216 O ATOM 966 N ASN A 150 -5.532 23.952 63.710 1.00104.18 N ANISOU 966 N ASN A 150 12893 15603 11084 -343 409 -305 N ATOM 967 CA ASN A 150 -5.352 22.490 63.984 1.00 95.98 C ANISOU 967 CA ASN A 150 11958 14509 9998 -402 471 -260 C ATOM 968 C ASN A 150 -6.691 21.725 63.822 1.00 93.15 C ANISOU 968 C ASN A 150 11581 14202 9608 -510 567 -277 C ATOM 969 O ASN A 150 -6.664 20.478 63.634 1.00 74.29 O ANISOU 969 O ASN A 150 9264 11763 7197 -579 623 -245 O ATOM 970 CB ASN A 150 -4.707 22.260 65.359 1.00 97.24 C ANISOU 970 CB ASN A 150 12220 14633 10092 -353 469 -232 C ATOM 971 CG ASN A 150 -5.425 22.951 66.508 1.00115.20 C ANISOU 971 CG ASN A 150 14473 16980 12315 -329 487 -265 C ATOM 972 OD1 ASN A 150 -5.661 24.162 66.460 1.00116.89 O ANISOU 972 OD1 ASN A 150 14602 17249 12562 -281 441 -308 O ATOM 973 ND2 ASN A 150 -5.763 22.196 67.553 1.00 97.79 N ANISOU 973 ND2 ASN A 150 12351 14774 10028 -358 554 -246 N ATOM 974 N GLN A 151 -7.830 22.432 63.870 1.00 93.39 N ANISOU 974 N GLN A 151 11516 14331 9636 -525 587 -330 N ATOM 975 CA GLN A 151 -9.194 21.833 63.763 1.00104.67 C ANISOU 975 CA GLN A 151 12906 15828 11034 -628 678 -361 C ATOM 976 C GLN A 151 -9.628 21.766 62.292 1.00107.14 C ANISOU 976 C GLN A 151 13133 16165 11407 -674 673 -386 C ATOM 977 O GLN A 151 -10.570 21.009 61.999 1.00106.42 O ANISOU 977 O GLN A 151 13021 16115 11299 -772 749 -408 O ATOM 978 CB GLN A 151 -10.205 22.639 64.587 1.00118.91 C ANISOU 978 CB GLN A 151 14643 17735 12799 -614 700 -413 C ATOM 979 CG GLN A 151 -9.996 22.512 66.093 1.00130.61 C ANISOU 979 CG GLN A 151 16214 19204 14206 -588 726 -391 C ATOM 980 CD GLN A 151 -10.563 23.672 66.875 1.00128.84 C ANISOU 980 CD GLN A 151 15924 19067 13960 -528 707 -439 C ATOM 981 OE1 GLN A 151 -10.005 24.768 66.880 1.00132.78 O ANISOU 981 OE1 GLN A 151 16391 19564 14495 -433 623 -451 O ATOM 982 NE2 GLN A 151 -11.672 23.433 67.559 1.00120.77 N ANISOU 982 NE2 GLN A 151 14884 18124 12878 -586 788 -469 N ATOM 983 N LEU A 152 -8.974 22.533 61.408 1.00 95.47 N ANISOU 983 N LEU A 152 11609 14667 9996 -608 590 -386 N ATOM 984 CA LEU A 152 -9.236 22.536 59.942 1.00 97.05 C ANISOU 984 CA LEU A 152 11734 14884 10253 -635 575 -406 C ATOM 985 C LEU A 152 -8.301 21.522 59.257 1.00103.51 C ANISOU 985 C LEU A 152 12628 15603 11096 -664 572 -355 C ATOM 986 O LEU A 152 -8.743 20.872 58.292 1.00 82.87 O ANISOU 986 O LEU A 152 9986 12998 8501 -734 603 -366 O ATOM 987 CB LEU A 152 -9.040 23.949 59.367 1.00105.08 C ANISOU 987 CB LEU A 152 12669 15929 11324 -545 490 -430 C ATOM 988 CG LEU A 152 -9.906 25.081 59.941 1.00102.76 C ANISOU 988 CG LEU A 152 12300 15731 11013 -499 480 -484 C ATOM 989 CD1 LEU A 152 -9.351 26.438 59.521 1.00 97.35 C ANISOU 989 CD1 LEU A 152 11573 15034 10378 -398 390 -492 C ATOM 990 CD2 LEU A 152 -11.379 24.972 59.540 1.00 96.34 C ANISOU 990 CD2 LEU A 152 11393 15028 10183 -560 533 -543 C ATOM 991 N VAL A 153 -7.050 21.400 59.724 1.00112.26 N ANISOU 991 N VAL A 153 13825 16624 12203 -610 533 -306 N ATOM 992 CA VAL A 153 -6.004 20.554 59.066 1.00119.75 C ANISOU 992 CA VAL A 153 14843 17477 13176 -616 517 -259 C ATOM 993 C VAL A 153 -5.767 19.281 59.892 1.00112.59 C ANISOU 993 C VAL A 153 14062 16507 12208 -659 577 -218 C ATOM 994 O VAL A 153 -5.498 19.407 61.099 1.00131.50 O ANISOU 994 O VAL A 153 16516 18893 14555 -619 578 -203 O ATOM 995 CB VAL A 153 -4.699 21.347 58.834 1.00123.73 C ANISOU 995 CB VAL A 153 15350 17932 13728 -519 425 -239 C ATOM 996 CG1 VAL A 153 -4.917 22.507 57.866 1.00105.44 C ANISOU 996 CG1 VAL A 153 12925 15664 11473 -484 372 -273 C ATOM 997 CG2 VAL A 153 -4.069 21.838 60.133 1.00126.35 C ANISOU 997 CG2 VAL A 153 15732 18247 14026 -447 394 -227 C ATOM 998 N THR A 154 -5.848 18.107 59.243 1.00113.19 N ANISOU 998 N THR A 154 14181 16541 12285 -735 625 -201 N ATOM 999 CA THR A 154 -5.762 16.756 59.880 1.00112.36 C ANISOU 999 CA THR A 154 14204 16367 12118 -791 696 -163 C ATOM 1000 C THR A 154 -4.963 15.801 58.984 1.00108.89 C ANISOU 1000 C THR A 154 13826 15839 11705 -806 687 -128 C ATOM 1001 O THR A 154 -4.735 16.105 57.824 1.00 93.30 O ANISOU 1001 O THR A 154 11783 13872 9794 -796 643 -141 O ATOM 1002 CB THR A 154 -7.175 16.238 60.194 1.00121.24 C ANISOU 1002 CB THR A 154 15314 17551 13200 -900 795 -194 C ATOM 1003 OG1 THR A 154 -8.065 16.591 59.133 1.00109.72 O ANISOU 1003 OG1 THR A 154 13729 16170 11787 -949 799 -248 O ATOM 1004 CG2 THR A 154 -7.725 16.800 61.489 1.00139.15 C ANISOU 1004 CG2 THR A 154 17578 19877 15413 -882 820 -209 C ATOM 1005 N PRO A 155 -4.492 14.621 59.466 1.00127.30 N ANISOU 1005 N PRO A 155 16294 18084 13990 -826 728 -83 N ATOM 1006 CA PRO A 155 -3.706 13.700 58.631 1.00107.08 C ANISOU 1006 CA PRO A 155 13797 15437 11451 -833 718 -52 C ATOM 1007 C PRO A 155 -4.479 12.971 57.517 1.00104.03 C ANISOU 1007 C PRO A 155 13376 15056 11091 -940 771 -76 C ATOM 1008 O PRO A 155 -3.853 12.359 56.661 1.00 83.47 O ANISOU 1008 O PRO A 155 10804 12392 8516 -940 754 -58 O ATOM 1009 CB PRO A 155 -3.184 12.653 59.632 1.00116.00 C ANISOU 1009 CB PRO A 155 15089 16476 12507 -824 757 0 C ATOM 1010 CG PRO A 155 -4.204 12.672 60.752 1.00136.51 C ANISOU 1010 CG PRO A 155 17705 19120 15041 -874 830 -11 C ATOM 1011 CD PRO A 155 -4.656 14.118 60.841 1.00144.04 C ANISOU 1011 CD PRO A 155 18521 20180 16026 -835 785 -57 C ATOM 1012 N CYS A 156 -5.814 13.041 57.545 1.00116.05 N ANISOU 1012 N CYS A 156 14832 16657 12603 -1027 835 -120 N ATOM 1013 CA CYS A 156 -6.659 12.458 56.465 1.00118.48 C ANISOU 1013 CA CYS A 156 15087 16991 12938 -1132 883 -158 C ATOM 1014 C CYS A 156 -6.937 13.549 55.425 1.00103.20 C ANISOU 1014 C CYS A 156 12997 15142 11068 -1100 820 -204 C ATOM 1015 O CYS A 156 -6.894 13.214 54.232 1.00103.83 O ANISOU 1015 O CYS A 156 13044 15214 11190 -1129 809 -216 O ATOM 1016 CB CYS A 156 -7.956 11.876 57.030 1.00124.85 C ANISOU 1016 CB CYS A 156 15902 17839 13695 -1249 990 -187 C ATOM 1017 SG CYS A 156 -9.061 11.127 55.797 1.00110.91 S ANISOU 1017 SG CYS A 156 14066 16115 11958 -1388 1055 -245 S ATOM 1018 N ARG A 157 -7.199 14.785 55.880 1.00 98.23 N ANISOU 1018 N ARG A 157 12287 14590 10444 -1041 782 -227 N ATOM 1019 CA ARG A 157 -7.504 15.945 55.000 1.00 95.84 C ANISOU 1019 CA ARG A 157 11846 14370 10196 -999 721 -270 C ATOM 1020 C ARG A 157 -6.286 16.251 54.121 1.00111.98 C ANISOU 1020 C ARG A 157 13893 16358 12295 -922 639 -240 C ATOM 1021 O ARG A 157 -6.437 16.357 52.893 1.00104.97 O ANISOU 1021 O ARG A 157 12936 15494 11452 -934 618 -262 O ATOM 1022 CB ARG A 157 -7.893 17.171 55.832 1.00 93.32 C ANISOU 1022 CB ARG A 157 11466 14127 9864 -940 696 -293 C ATOM 1023 CG ARG A 157 -7.532 18.500 55.186 1.00101.40 C ANISOU 1023 CG ARG A 157 12399 15186 10942 -847 607 -308 C ATOM 1024 CD ARG A 157 -8.523 19.604 55.485 1.00110.02 C ANISOU 1024 CD ARG A 157 13388 16385 12027 -825 601 -361 C ATOM 1025 NE ARG A 157 -8.012 20.902 55.060 1.00123.09 N ANISOU 1025 NE ARG A 157 14986 18052 13728 -726 514 -365 N ATOM 1026 CZ ARG A 157 -8.753 21.991 54.887 1.00117.58 C ANISOU 1026 CZ ARG A 157 14190 17441 13041 -688 490 -411 C ATOM 1027 NH1 ARG A 157 -10.055 21.950 55.100 1.00129.20 N ANISOU 1027 NH1 ARG A 157 15599 19007 14481 -740 541 -463 N ATOM 1028 NH2 ARG A 157 -8.193 23.122 54.501 1.00111.16 N ANISOU 1028 NH2 ARG A 157 13344 16621 12269 -600 414 -408 N ATOM 1029 N LEU A 158 -5.117 16.382 54.740 1.00119.65 N ANISOU 1029 N LEU A 158 14939 17260 13260 -845 595 -194 N ATOM 1030 CA LEU A 158 -3.859 16.616 53.981 1.00110.19 C ANISOU 1030 CA LEU A 158 13748 16006 12111 -774 521 -166 C ATOM 1031 C LEU A 158 -3.623 15.449 53.006 1.00114.14 C ANISOU 1031 C LEU A 158 14291 16451 12626 -828 546 -152 C ATOM 1032 O LEU A 158 -3.165 15.731 51.890 1.00129.74 O ANISOU 1032 O LEU A 158 16219 18424 14653 -802 499 -155 O ATOM 1033 CB LEU A 158 -2.718 16.806 54.989 1.00117.44 C ANISOU 1033 CB LEU A 158 14745 16867 13009 -691 481 -127 C ATOM 1034 CG LEU A 158 -1.289 16.502 54.536 1.00109.20 C ANISOU 1034 CG LEU A 158 13754 15744 11992 -634 428 -89 C ATOM 1035 CD1 LEU A 158 -0.776 17.530 53.537 1.00101.31 C ANISOU 1035 CD1 LEU A 158 12664 14767 11060 -581 357 -103 C ATOM 1036 CD2 LEU A 158 -0.374 16.452 55.756 1.00121.04 C ANISOU 1036 CD2 LEU A 158 15341 17195 13450 -565 405 -58 C ATOM 1037 N ARG A 159 -3.984 14.210 53.378 1.00116.53 N ANISOU 1037 N ARG A 159 14679 16711 12883 -905 619 -141 N ATOM 1038 CA ARG A 159 -3.733 13.011 52.521 1.00103.45 C ANISOU 1038 CA ARG A 159 13079 14990 11236 -958 646 -128 C ATOM 1039 C ARG A 159 -4.715 12.966 51.341 1.00 89.05 C ANISOU 1039 C ARG A 159 11157 13231 9445 -1033 669 -178 C ATOM 1040 O ARG A 159 -4.292 12.498 50.249 1.00 94.17 O ANISOU 1040 O ARG A 159 11807 13845 10127 -1040 652 -175 O ATOM 1041 CB ARG A 159 -3.771 11.710 53.335 1.00120.62 C ANISOU 1041 CB ARG A 159 15392 17088 13349 -1014 720 -98 C ATOM 1042 CG ARG A 159 -2.427 11.297 53.934 1.00137.48 C ANISOU 1042 CG ARG A 159 17648 19126 15460 -933 686 -41 C ATOM 1043 CD ARG A 159 -1.245 11.210 52.964 1.00145.24 C ANISOU 1043 CD ARG A 159 18634 20059 16489 -871 619 -22 C ATOM 1044 NE ARG A 159 -1.495 10.377 51.785 1.00139.24 N ANISOU 1044 NE ARG A 159 17871 19277 15754 -940 647 -36 N ATOM 1045 CZ ARG A 159 -0.579 10.019 50.887 1.00127.15 C ANISOU 1045 CZ ARG A 159 16358 17696 14256 -903 607 -21 C ATOM 1046 NH1 ARG A 159 -0.924 9.259 49.860 1.00110.43 N ANISOU 1046 NH1 ARG A 159 14237 15563 12157 -972 637 -39 N ATOM 1047 NH2 ARG A 159 0.676 10.413 51.016 1.00140.60 N ANISOU 1047 NH2 ARG A 159 18080 19370 15973 -800 537 6 N ATOM 1048 N ILE A 160 -5.955 13.442 51.520 1.00 73.73 N ANISOU 1048 N ILE A 160 9131 11386 7494 -1080 703 -227 N ATOM 1049 CA ILE A 160 -6.940 13.506 50.389 1.00 76.74 C ANISOU 1049 CA ILE A 160 9405 11848 7906 -1141 717 -285 C ATOM 1050 C ILE A 160 -6.609 14.723 49.506 1.00 78.43 C ANISOU 1050 C ILE A 160 9518 12109 8172 -1055 631 -296 C ATOM 1051 O ILE A 160 -6.907 14.684 48.292 1.00 65.65 O ANISOU 1051 O ILE A 160 7833 10524 6584 -1075 620 -326 O ATOM 1052 CB ILE A 160 -8.422 13.481 50.849 1.00 86.78 C ANISOU 1052 CB ILE A 160 10617 13211 9144 -1228 787 -340 C ATOM 1053 CG1 ILE A 160 -8.790 14.618 51.814 1.00101.17 C ANISOU 1053 CG1 ILE A 160 12388 15102 10947 -1173 770 -353 C ATOM 1054 CG2 ILE A 160 -8.773 12.116 51.439 1.00 99.10 C ANISOU 1054 CG2 ILE A 160 12280 14715 10656 -1334 882 -332 C ATOM 1055 CD1 ILE A 160 -10.283 14.749 52.140 1.00 86.65 C ANISOU 1055 CD1 ILE A 160 10466 13375 9080 -1248 832 -418 C ATOM 1056 N CYS A 161 -5.973 15.751 50.073 1.00 85.15 N ANISOU 1056 N CYS A 161 10364 12957 9030 -960 574 -273 N ATOM 1057 CA CYS A 161 -5.551 16.988 49.354 1.00 78.77 C ANISOU 1057 CA CYS A 161 9477 12180 8270 -873 495 -277 C ATOM 1058 C CYS A 161 -4.422 16.662 48.365 1.00 83.47 C ANISOU 1058 C CYS A 161 10104 12705 8904 -843 453 -244 C ATOM 1059 O CYS A 161 -4.376 17.271 47.266 1.00 68.21 O ANISOU 1059 O CYS A 161 8099 10804 7010 -812 411 -259 O ATOM 1060 CB CYS A 161 -5.087 18.041 50.351 1.00 72.84 C ANISOU 1060 CB CYS A 161 8731 11431 7514 -791 453 -261 C ATOM 1061 SG CYS A 161 -4.854 19.698 49.668 1.00 82.56 S ANISOU 1061 SG CYS A 161 9865 12708 8795 -696 370 -275 S ATOM 1062 N ILE A 162 -3.563 15.706 48.733 1.00 84.79 N ANISOU 1062 N ILE A 162 10377 12782 9055 -849 467 -203 N ATOM 1063 CA ILE A 162 -2.407 15.272 47.893 1.00 86.29 C ANISOU 1063 CA ILE A 162 10607 12901 9276 -817 431 -171 C ATOM 1064 C ILE A 162 -2.954 14.563 46.648 1.00 78.58 C ANISOU 1064 C ILE A 162 9599 11940 8315 -884 458 -198 C ATOM 1065 O ILE A 162 -2.544 14.942 45.534 1.00 84.66 O ANISOU 1065 O ILE A 162 10320 12718 9125 -850 414 -200 O ATOM 1066 CB ILE A 162 -1.421 14.388 48.695 1.00 77.39 C ANISOU 1066 CB ILE A 162 9605 11678 8119 -800 440 -124 C ATOM 1067 CG1 ILE A 162 -0.676 15.169 49.786 1.00 81.58 C ANISOU 1067 CG1 ILE A 162 10159 12195 8639 -717 397 -101 C ATOM 1068 CG2 ILE A 162 -0.458 13.653 47.769 1.00 75.34 C ANISOU 1068 CG2 ILE A 162 9388 11352 7883 -787 419 -102 C ATOM 1069 CD1 ILE A 162 -0.007 16.444 49.330 1.00 91.70 C ANISOU 1069 CD1 ILE A 162 11368 13502 9971 -638 323 -103 C ATOM 1070 N ILE A 163 -3.857 13.593 46.820 1.00 74.43 N ANISOU 1070 N ILE A 163 9099 11420 7758 -979 529 -220 N ATOM 1071 CA ILE A 163 -4.331 12.778 45.665 1.00 80.75 C ANISOU 1071 CA ILE A 163 9880 12229 8572 -1050 558 -250 C ATOM 1072 C ILE A 163 -5.189 13.677 44.766 1.00 73.31 C ANISOU 1072 C ILE A 163 8805 11394 7656 -1047 534 -301 C ATOM 1073 O ILE A 163 -5.228 13.392 43.553 1.00 85.60 O ANISOU 1073 O ILE A 163 10325 12961 9235 -1063 524 -320 O ATOM 1074 CB ILE A 163 -5.071 11.491 46.099 1.00102.78 C ANISOU 1074 CB ILE A 163 12736 14993 11321 -1161 646 -265 C ATOM 1075 CG1 ILE A 163 -4.134 10.475 46.766 1.00111.24 C ANISOU 1075 CG1 ILE A 163 13955 15945 12365 -1156 666 -211 C ATOM 1076 CG2 ILE A 163 -5.785 10.865 44.906 1.00114.35 C ANISOU 1076 CG2 ILE A 163 14152 16492 12803 -1239 674 -314 C ATOM 1077 CD1 ILE A 163 -4.835 9.298 47.420 1.00 99.83 C ANISOU 1077 CD1 ILE A 163 12596 14463 10873 -1261 758 -218 C ATOM 1078 N LEU A 164 -5.828 14.726 45.304 1.00 61.17 N ANISOU 1078 N LEU A 164 7197 9933 6111 -1019 523 -324 N ATOM 1079 CA LEU A 164 -6.682 15.597 44.437 1.00 66.27 C ANISOU 1079 CA LEU A 164 7719 10684 6776 -1005 498 -375 C ATOM 1080 C LEU A 164 -5.798 16.487 43.558 1.00 68.13 C ANISOU 1080 C LEU A 164 7925 10907 7053 -912 421 -351 C ATOM 1081 O LEU A 164 -6.230 16.839 42.442 1.00 87.56 O ANISOU 1081 O LEU A 164 10310 13427 9532 -903 400 -382 O ATOM 1082 CB LEU A 164 -7.684 16.419 45.260 1.00 66.84 C ANISOU 1082 CB LEU A 164 7727 10844 6824 -1001 510 -411 C ATOM 1083 CG LEU A 164 -8.956 15.667 45.662 1.00 58.57 C ANISOU 1083 CG LEU A 164 6659 9854 5741 -1109 589 -463 C ATOM 1084 CD1 LEU A 164 -9.613 16.309 46.858 1.00 63.52 C ANISOU 1084 CD1 LEU A 164 7260 10536 6335 -1100 609 -480 C ATOM 1085 CD2 LEU A 164 -9.946 15.571 44.524 1.00 65.83 C ANISOU 1085 CD2 LEU A 164 7478 10864 6669 -1153 598 -529 C ATOM 1086 N ILE A 165 -4.581 16.788 43.989 1.00 74.07 N ANISOU 1086 N ILE A 165 8738 11586 7819 -847 384 -298 N ATOM 1087 CA ILE A 165 -3.604 17.499 43.106 1.00 71.57 C ANISOU 1087 CA ILE A 165 8404 11245 7543 -770 320 -272 C ATOM 1088 C ILE A 165 -3.207 16.570 41.956 1.00 67.53 C ANISOU 1088 C ILE A 165 7913 10698 7047 -800 324 -267 C ATOM 1089 O ILE A 165 -3.291 17.016 40.813 1.00 55.47 O ANISOU 1089 O ILE A 165 6326 9208 5542 -776 295 -282 O ATOM 1090 CB ILE A 165 -2.374 17.953 43.898 1.00 57.69 C ANISOU 1090 CB ILE A 165 6704 9420 5794 -703 283 -224 C ATOM 1091 CG1 ILE A 165 -2.776 18.840 45.078 1.00 61.20 C ANISOU 1091 CG1 ILE A 165 7132 9898 6221 -674 279 -232 C ATOM 1092 CG2 ILE A 165 -1.410 18.634 42.952 1.00 56.29 C ANISOU 1092 CG2 ILE A 165 6506 9221 5659 -637 226 -203 C ATOM 1093 CD1 ILE A 165 -1.745 18.964 46.156 1.00 63.86 C ANISOU 1093 CD1 ILE A 165 7539 10172 6553 -629 259 -194 C ATOM 1094 N TRP A 166 -2.839 15.324 42.289 1.00 68.74 N ANISOU 1094 N TRP A 166 8151 10782 7183 -848 362 -249 N ATOM 1095 CA TRP A 166 -2.475 14.242 41.329 1.00 62.51 C ANISOU 1095 CA TRP A 166 7398 9949 6403 -884 375 -246 C ATOM 1096 C TRP A 166 -3.623 13.922 40.360 1.00 68.43 C ANISOU 1096 C TRP A 166 8078 10770 7150 -948 401 -302 C ATOM 1097 O TRP A 166 -3.333 13.532 39.236 1.00 62.35 O ANISOU 1097 O TRP A 166 7301 9990 6399 -951 389 -307 O ATOM 1098 CB TRP A 166 -2.064 12.974 42.077 1.00 51.85 C ANISOU 1098 CB TRP A 166 6162 8512 5025 -926 418 -221 C ATOM 1099 CG TRP A 166 -0.688 13.071 42.616 1.00 50.21 C ANISOU 1099 CG TRP A 166 6024 8229 4822 -853 381 -169 C ATOM 1100 CD1 TRP A 166 -0.329 13.331 43.899 1.00 59.98 C ANISOU 1100 CD1 TRP A 166 7310 9441 6039 -819 377 -143 C ATOM 1101 CD2 TRP A 166 0.527 12.970 41.863 1.00 63.79 C ANISOU 1101 CD2 TRP A 166 7764 9901 6570 -798 338 -142 C ATOM 1102 NE1 TRP A 166 1.032 13.369 44.008 1.00 55.92 N ANISOU 1102 NE1 TRP A 166 6843 8865 5536 -748 334 -104 N ATOM 1103 CE2 TRP A 166 1.586 13.157 42.773 1.00 61.48 C ANISOU 1103 CE2 TRP A 166 7530 9556 6271 -735 310 -103 C ATOM 1104 CE3 TRP A 166 0.831 12.728 40.516 1.00 61.65 C ANISOU 1104 CE3 TRP A 166 7467 9630 6326 -796 321 -149 C ATOM 1105 CZ2 TRP A 166 2.925 13.106 42.378 1.00 61.45 C ANISOU 1105 CZ2 TRP A 166 7553 9504 6289 -673 267 -75 C ATOM 1106 CZ3 TRP A 166 2.153 12.679 40.132 1.00 57.98 C ANISOU 1106 CZ3 TRP A 166 7033 9114 5881 -735 281 -117 C ATOM 1107 CH2 TRP A 166 3.184 12.869 41.050 1.00 52.01 C ANISOU 1107 CH2 TRP A 166 6329 8311 5121 -675 255 -83 C ATOM 1108 N ILE A 167 -4.877 14.017 40.804 1.00 72.10 N ANISOU 1108 N ILE A 167 8495 11307 7592 -1001 439 -347 N ATOM 1109 CA ILE A 167 -6.032 13.733 39.911 1.00 63.67 C ANISOU 1109 CA ILE A 167 7348 10321 6520 -1064 464 -411 C ATOM 1110 C ILE A 167 -6.228 14.976 39.046 1.00 68.08 C ANISOU 1110 C ILE A 167 7808 10957 7099 -989 405 -429 C ATOM 1111 O ILE A 167 -6.235 14.831 37.805 1.00 80.55 O ANISOU 1111 O ILE A 167 9353 12559 8694 -985 387 -447 O ATOM 1112 CB ILE A 167 -7.299 13.346 40.706 1.00 74.76 C ANISOU 1112 CB ILE A 167 8733 11780 7891 -1152 529 -459 C ATOM 1113 CG1 ILE A 167 -7.181 11.953 41.338 1.00 91.02 C ANISOU 1113 CG1 ILE A 167 10899 13756 9927 -1239 596 -444 C ATOM 1114 CG2 ILE A 167 -8.545 13.445 39.836 1.00 64.53 C ANISOU 1114 CG2 ILE A 167 7325 10598 6592 -1194 540 -536 C ATOM 1115 CD1 ILE A 167 -6.844 10.841 40.357 1.00102.55 C ANISOU 1115 CD1 ILE A 167 12402 15161 11398 -1285 610 -448 C ATOM 1116 N TYR A 168 -6.358 16.138 39.683 1.00 56.40 N ANISOU 1116 N TYR A 168 6294 9515 5619 -929 378 -422 N ATOM 1117 CA TYR A 168 -6.593 17.401 38.943 1.00 59.16 C ANISOU 1117 CA TYR A 168 6561 9934 5983 -851 324 -438 C ATOM 1118 C TYR A 168 -5.498 17.646 37.903 1.00 60.88 C ANISOU 1118 C TYR A 168 6796 10102 6231 -791 276 -398 C ATOM 1119 O TYR A 168 -5.810 18.058 36.795 1.00 75.41 O ANISOU 1119 O TYR A 168 8577 11996 8078 -762 250 -421 O ATOM 1120 CB TYR A 168 -6.584 18.572 39.913 1.00 64.48 C ANISOU 1120 CB TYR A 168 7222 10622 6653 -789 300 -423 C ATOM 1121 CG TYR A 168 -7.077 19.864 39.319 1.00 66.68 C ANISOU 1121 CG TYR A 168 7419 10978 6937 -714 255 -447 C ATOM 1122 CD1 TYR A 168 -8.338 19.941 38.754 1.00 61.11 C ANISOU 1122 CD1 TYR A 168 6627 10380 6213 -733 264 -512 C ATOM 1123 CD2 TYR A 168 -6.309 21.019 39.389 1.00 71.07 C ANISOU 1123 CD2 TYR A 168 7987 11501 7514 -625 204 -408 C ATOM 1124 CE1 TYR A 168 -8.810 21.136 38.251 1.00 65.99 C ANISOU 1124 CE1 TYR A 168 7176 11067 6827 -654 220 -534 C ATOM 1125 CE2 TYR A 168 -6.770 22.219 38.887 1.00 59.14 C ANISOU 1125 CE2 TYR A 168 6414 10052 6004 -554 165 -427 C ATOM 1126 CZ TYR A 168 -8.019 22.269 38.320 1.00 58.18 C ANISOU 1126 CZ TYR A 168 6211 10034 5858 -564 171 -488 C ATOM 1127 OH TYR A 168 -8.458 23.455 37.845 1.00 72.22 O ANISOU 1127 OH TYR A 168 7937 11870 7632 -482 130 -505 O ATOM 1128 N SER A 169 -4.232 17.436 38.259 1.00 66.36 N ANISOU 1128 N SER A 169 7569 10700 6942 -768 265 -342 N ATOM 1129 CA SER A 169 -3.168 17.729 37.275 1.00 60.19 C ANISOU 1129 CA SER A 169 6799 9878 6190 -711 222 -307 C ATOM 1130 C SER A 169 -3.371 16.823 36.052 1.00 67.65 C ANISOU 1130 C SER A 169 7732 10835 7135 -753 235 -332 C ATOM 1131 O SER A 169 -3.458 17.372 34.942 1.00 72.36 O ANISOU 1131 O SER A 169 8277 11474 7740 -714 205 -342 O ATOM 1132 CB SER A 169 -1.826 17.584 37.888 1.00 53.18 C ANISOU 1132 CB SER A 169 5989 8897 5318 -683 209 -253 C ATOM 1133 OG SER A 169 -1.839 16.521 38.807 1.00 69.26 O ANISOU 1133 OG SER A 169 8091 10889 7333 -740 252 -249 O ATOM 1134 N CYS A 170 -3.523 15.509 36.263 1.00 60.07 N ANISOU 1134 N CYS A 170 6819 9843 6162 -831 281 -344 N ATOM 1135 CA CYS A 170 -3.727 14.542 35.145 1.00 61.96 C ANISOU 1135 CA CYS A 170 7053 10089 6400 -879 298 -373 C ATOM 1136 C CYS A 170 -4.899 14.968 34.250 1.00 60.04 C ANISOU 1136 C CYS A 170 6709 9956 6147 -884 290 -432 C ATOM 1137 O CYS A 170 -4.779 14.835 33.024 1.00 60.10 O ANISOU 1137 O CYS A 170 6692 9981 6162 -871 271 -444 O ATOM 1138 CB CYS A 170 -3.964 13.129 35.663 1.00 61.80 C ANISOU 1138 CB CYS A 170 7098 10022 6361 -972 357 -386 C ATOM 1139 SG CYS A 170 -2.538 12.458 36.555 1.00 66.87 S ANISOU 1139 SG CYS A 170 7868 10532 7007 -954 362 -318 S ATOM 1140 N LEU A 171 -5.977 15.481 34.839 1.00 60.10 N ANISOU 1140 N LEU A 171 6659 10039 6136 -898 303 -471 N ATOM 1141 CA LEU A 171 -7.224 15.726 34.072 1.00 64.96 C ANISOU 1141 CA LEU A 171 7175 10771 6736 -910 301 -541 C ATOM 1142 C LEU A 171 -7.139 17.049 33.310 1.00 62.80 C ANISOU 1142 C LEU A 171 6846 10546 6468 -807 241 -532 C ATOM 1143 O LEU A 171 -7.922 17.232 32.373 1.00 73.13 O ANISOU 1143 O LEU A 171 8081 11942 7763 -796 227 -582 O ATOM 1144 CB LEU A 171 -8.424 15.725 35.025 1.00 70.91 C ANISOU 1144 CB LEU A 171 7885 11592 7463 -965 341 -590 C ATOM 1145 CG LEU A 171 -8.751 14.409 35.736 1.00 66.92 C ANISOU 1145 CG LEU A 171 7429 11051 6944 -1080 412 -609 C ATOM 1146 CD1 LEU A 171 -10.140 14.502 36.340 1.00 76.63 C ANISOU 1146 CD1 LEU A 171 8587 12381 8146 -1136 451 -676 C ATOM 1147 CD2 LEU A 171 -8.652 13.194 34.816 1.00 67.73 C ANISOU 1147 CD2 LEU A 171 7557 11125 7052 -1146 435 -631 C ATOM 1148 N ILE A 172 -6.220 17.937 33.653 1.00 71.27 N ANISOU 1148 N ILE A 172 7955 11564 7560 -732 207 -473 N ATOM 1149 CA ILE A 172 -6.096 19.216 32.891 1.00 87.28 C ANISOU 1149 CA ILE A 172 9943 13626 9592 -635 154 -460 C ATOM 1150 C ILE A 172 -5.222 18.992 31.650 1.00 79.76 C ANISOU 1150 C ILE A 172 9014 12634 8655 -610 132 -432 C ATOM 1151 O ILE A 172 -5.213 19.858 30.777 1.00 72.59 O ANISOU 1151 O ILE A 172 8075 11759 7745 -539 95 -427 O ATOM 1152 CB ILE A 172 -5.551 20.330 33.794 1.00 92.28 C ANISOU 1152 CB ILE A 172 10602 14220 10238 -573 130 -416 C ATOM 1153 CG1 ILE A 172 -6.423 20.491 35.034 1.00 95.87 C ANISOU 1153 CG1 ILE A 172 11034 14717 10674 -599 154 -446 C ATOM 1154 CG2 ILE A 172 -5.439 21.638 33.031 1.00 97.39 C ANISOU 1154 CG2 ILE A 172 11220 14892 10889 -478 81 -402 C ATOM 1155 CD1 ILE A 172 -7.884 20.735 34.715 1.00 90.77 C ANISOU 1155 CD1 ILE A 172 10297 14192 9998 -603 157 -518 C ATOM 1156 N PHE A 173 -4.531 17.859 31.578 1.00 65.33 N ANISOU 1156 N PHE A 173 7242 10738 6839 -662 155 -415 N ATOM 1157 CA PHE A 173 -3.621 17.550 30.457 1.00 70.24 C ANISOU 1157 CA PHE A 173 7891 11319 7475 -640 138 -388 C ATOM 1158 C PHE A 173 -4.040 16.226 29.815 1.00 79.13 C ANISOU 1158 C PHE A 173 9014 12460 8589 -713 168 -432 C ATOM 1159 O PHE A 173 -3.257 15.629 29.064 1.00 89.07 O ANISOU 1159 O PHE A 173 10310 13674 9860 -714 165 -413 O ATOM 1160 CB PHE A 173 -2.177 17.518 30.956 1.00 60.33 C ANISOU 1160 CB PHE A 173 6713 9962 6248 -619 132 -323 C ATOM 1161 CG PHE A 173 -1.691 18.840 31.480 1.00 59.07 C ANISOU 1161 CG PHE A 173 6554 9785 6102 -550 101 -285 C ATOM 1162 CD1 PHE A 173 -1.489 19.905 30.623 1.00 51.79 C ANISOU 1162 CD1 PHE A 173 5606 8885 5186 -480 66 -269 C ATOM 1163 CD2 PHE A 173 -1.447 19.021 32.833 1.00 62.66 C ANISOU 1163 CD2 PHE A 173 7042 10200 6563 -555 109 -265 C ATOM 1164 CE1 PHE A 173 -1.043 21.124 31.112 1.00 55.02 C ANISOU 1164 CE1 PHE A 173 6023 9272 5610 -422 42 -236 C ATOM 1165 CE2 PHE A 173 -1.009 20.245 33.320 1.00 56.38 C ANISOU 1165 CE2 PHE A 173 6247 9389 5782 -494 81 -236 C ATOM 1166 CZ PHE A 173 -0.803 21.296 32.456 1.00 52.30 C ANISOU 1166 CZ PHE A 173 5706 8890 5275 -431 48 -222 C ATOM 1167 N LEU A 174 -5.262 15.790 30.099 1.00 68.36 N ANISOU 1167 N LEU A 174 7606 11162 7204 -776 198 -493 N ATOM 1168 CA LEU A 174 -5.826 14.543 29.533 1.00 73.96 C ANISOU 1168 CA LEU A 174 8306 11892 7901 -858 231 -547 C ATOM 1169 C LEU A 174 -6.346 14.803 28.120 1.00 73.30 C ANISOU 1169 C LEU A 174 8150 11894 7803 -825 202 -590 C ATOM 1170 O LEU A 174 -6.198 13.931 27.260 1.00 69.09 O ANISOU 1170 O LEU A 174 7629 11352 7270 -857 210 -610 O ATOM 1171 CB LEU A 174 -6.929 14.031 30.466 1.00 78.37 C ANISOU 1171 CB LEU A 174 8844 12490 8443 -944 280 -599 C ATOM 1172 CG LEU A 174 -7.312 12.566 30.278 1.00 78.40 C ANISOU 1172 CG LEU A 174 8869 12478 8438 -1052 331 -644 C ATOM 1173 CD1 LEU A 174 -6.075 11.679 30.211 1.00 80.80 C ANISOU 1173 CD1 LEU A 174 9278 12661 8760 -1062 340 -592 C ATOM 1174 CD2 LEU A 174 -8.229 12.111 31.399 1.00 80.67 C ANISOU 1174 CD2 LEU A 174 9153 12785 8710 -1141 387 -682 C ATOM 1175 N PRO A 175 -6.960 15.982 27.829 1.00 66.09 N ANISOU 1175 N PRO A 175 7167 11067 6875 -755 167 -607 N ATOM 1176 CA PRO A 175 -7.431 16.298 26.478 1.00 76.24 C ANISOU 1176 CA PRO A 175 8390 12436 8141 -708 134 -645 C ATOM 1177 C PRO A 175 -6.387 16.126 25.363 1.00 71.07 C ANISOU 1177 C PRO A 175 7776 11730 7496 -668 112 -604 C ATOM 1178 O PRO A 175 -6.758 15.737 24.274 1.00 66.33 O ANISOU 1178 O PRO A 175 7140 11184 6878 -671 103 -647 O ATOM 1179 CB PRO A 175 -7.854 17.771 26.585 1.00 67.78 C ANISOU 1179 CB PRO A 175 7271 11425 7055 -615 95 -639 C ATOM 1180 CG PRO A 175 -8.293 17.907 28.013 1.00 54.24 C ANISOU 1180 CG PRO A 175 5555 9708 5343 -652 122 -644 C ATOM 1181 CD PRO A 175 -7.314 17.050 28.778 1.00 60.38 C ANISOU 1181 CD PRO A 175 6422 10368 6148 -713 156 -596 C ATOM 1182 N SER A 176 -5.124 16.410 25.660 1.00 72.14 N ANISOU 1182 N SER A 176 7982 11769 7658 -634 104 -528 N ATOM 1183 CA SER A 176 -4.019 16.265 24.683 1.00 69.77 C ANISOU 1183 CA SER A 176 7722 11416 7368 -597 87 -486 C ATOM 1184 C SER A 176 -4.095 14.862 24.073 1.00 77.34 C ANISOU 1184 C SER A 176 8692 12369 8322 -667 112 -527 C ATOM 1185 O SER A 176 -3.777 14.741 22.887 1.00 91.29 O ANISOU 1185 O SER A 176 10454 14149 10081 -637 94 -528 O ATOM 1186 CB SER A 176 -2.688 16.531 25.333 1.00 65.74 C ANISOU 1186 CB SER A 176 7283 10803 6890 -574 85 -411 C ATOM 1187 OG SER A 176 -2.214 15.394 26.035 1.00 55.08 O ANISOU 1187 OG SER A 176 5992 9380 5555 -641 118 -404 O ATOM 1188 N PHE A 177 -4.579 13.873 24.845 1.00 69.46 N ANISOU 1188 N PHE A 177 7708 11357 7327 -758 153 -562 N ATOM 1189 CA PHE A 177 -4.699 12.469 24.364 1.00 64.56 C ANISOU 1189 CA PHE A 177 7107 10720 6702 -836 183 -604 C ATOM 1190 C PHE A 177 -6.003 12.261 23.586 1.00 68.80 C ANISOU 1190 C PHE A 177 7558 11371 7211 -867 183 -693 C ATOM 1191 O PHE A 177 -6.194 11.153 23.049 1.00 75.10 O ANISOU 1191 O PHE A 177 8363 12167 8004 -931 205 -739 O ATOM 1192 CB PHE A 177 -4.665 11.452 25.504 1.00 67.56 C ANISOU 1192 CB PHE A 177 7550 11027 7092 -925 233 -604 C ATOM 1193 CG PHE A 177 -3.299 11.189 26.080 1.00 80.08 C ANISOU 1193 CG PHE A 177 9231 12493 8701 -906 236 -531 C ATOM 1194 CD1 PHE A 177 -2.288 10.658 25.296 1.00 84.24 C ANISOU 1194 CD1 PHE A 177 9804 12964 9237 -883 225 -506 C ATOM 1195 CD2 PHE A 177 -3.030 11.447 27.415 1.00 85.46 C ANISOU 1195 CD2 PHE A 177 9953 13124 9391 -908 249 -492 C ATOM 1196 CE1 PHE A 177 -1.036 10.397 25.830 1.00 74.68 C ANISOU 1196 CE1 PHE A 177 8676 11654 8045 -861 226 -446 C ATOM 1197 CE2 PHE A 177 -1.769 11.206 27.944 1.00 93.75 C ANISOU 1197 CE2 PHE A 177 11087 14073 10458 -884 247 -430 C ATOM 1198 CZ PHE A 177 -0.778 10.674 27.149 1.00 79.08 C ANISOU 1198 CZ PHE A 177 9270 12165 8610 -860 235 -409 C ATOM 1199 N PHE A 178 -6.876 13.271 23.528 1.00 69.27 N ANISOU 1199 N PHE A 178 7539 11528 7250 -821 158 -721 N ATOM 1200 CA PHE A 178 -8.191 13.211 22.824 1.00 71.96 C ANISOU 1200 CA PHE A 178 7784 11998 7560 -837 152 -813 C ATOM 1201 C PHE A 178 -8.317 14.455 21.947 1.00 74.42 C ANISOU 1201 C PHE A 178 8045 12384 7848 -720 96 -804 C ATOM 1202 O PHE A 178 -9.332 15.201 22.069 1.00 93.40 O ANISOU 1202 O PHE A 178 10372 14886 10226 -688 78 -847 O ATOM 1203 CB PHE A 178 -9.369 13.083 23.807 1.00 77.41 C ANISOU 1203 CB PHE A 178 8423 12748 8241 -909 185 -872 C ATOM 1204 CG PHE A 178 -9.253 11.915 24.759 1.00 81.12 C ANISOU 1204 CG PHE A 178 8955 13136 8729 -1023 246 -874 C ATOM 1205 CD1 PHE A 178 -9.091 10.619 24.280 1.00 91.62 C ANISOU 1205 CD1 PHE A 178 10323 14424 10064 -1101 277 -902 C ATOM 1206 CD2 PHE A 178 -9.242 12.116 26.132 1.00 68.54 C ANISOU 1206 CD2 PHE A 178 7394 11500 7145 -1048 274 -842 C ATOM 1207 CE1 PHE A 178 -8.929 9.551 25.150 1.00 90.68 C ANISOU 1207 CE1 PHE A 178 10277 14217 9958 -1201 334 -897 C ATOM 1208 CE2 PHE A 178 -9.089 11.046 26.996 1.00 79.25 C ANISOU 1208 CE2 PHE A 178 8822 12776 8514 -1146 331 -837 C ATOM 1209 CZ PHE A 178 -8.929 9.768 26.507 1.00 81.22 C ANISOU 1209 CZ PHE A 178 9113 12978 8766 -1222 362 -862 C ATOM 1210 N GLY A 179 -7.274 14.695 21.148 1.00 77.14 N ANISOU 1210 N GLY A 179 8435 12675 8197 -656 70 -747 N ATOM 1211 CA GLY A 179 -7.278 15.594 19.977 1.00 85.49 C ANISOU 1211 CA GLY A 179 9460 13793 9226 -552 23 -740 C ATOM 1212 C GLY A 179 -7.661 17.036 20.291 1.00 75.79 C ANISOU 1212 C GLY A 179 8202 12610 7983 -465 -7 -719 C ATOM 1213 O GLY A 179 -8.161 17.730 19.362 1.00 56.52 O ANISOU 1213 O GLY A 179 5715 10253 5504 -384 -45 -742 O ATOM 1214 N TRP A 180 -7.388 17.520 21.506 1.00 74.81 N ANISOU 1214 N TRP A 180 8109 12430 7884 -470 4 -676 N ATOM 1215 CA TRP A 180 -7.682 18.937 21.840 1.00 73.59 C ANISOU 1215 CA TRP A 180 7935 12307 7716 -382 -25 -653 C ATOM 1216 C TRP A 180 -6.495 19.827 21.467 1.00 62.99 C ANISOU 1216 C TRP A 180 6657 10887 6386 -301 -48 -566 C ATOM 1217 O TRP A 180 -6.654 21.057 21.507 1.00 58.73 O ANISOU 1217 O TRP A 180 6113 10367 5834 -219 -75 -543 O ATOM 1218 CB TRP A 180 -8.099 19.091 23.303 1.00 73.51 C ANISOU 1218 CB TRP A 180 7919 12289 7723 -423 -3 -660 C ATOM 1219 CG TRP A 180 -9.587 19.123 23.453 1.00 79.26 C ANISOU 1219 CG TRP A 180 8555 13142 8418 -438 -3 -748 C ATOM 1220 CD1 TRP A 180 -10.371 18.203 24.082 1.00 77.61 C ANISOU 1220 CD1 TRP A 180 8308 12970 8210 -539 36 -812 C ATOM 1221 CD2 TRP A 180 -10.483 20.106 22.897 1.00 93.92 C ANISOU 1221 CD2 TRP A 180 10344 15107 10233 -346 -44 -787 C ATOM 1222 NE1 TRP A 180 -11.686 18.565 23.988 1.00 85.45 N ANISOU 1222 NE1 TRP A 180 9205 14093 9167 -521 23 -892 N ATOM 1223 CE2 TRP A 180 -11.788 19.725 23.269 1.00 88.63 C ANISOU 1223 CE2 TRP A 180 9587 14544 9542 -398 -29 -879 C ATOM 1224 CE3 TRP A 180 -10.314 21.267 22.129 1.00 96.99 C ANISOU 1224 CE3 TRP A 180 10740 15514 10598 -224 -91 -754 C ATOM 1225 CZ2 TRP A 180 -12.909 20.469 22.905 1.00 97.91 C ANISOU 1225 CZ2 TRP A 180 10678 15850 10673 -325 -64 -942 C ATOM 1226 CZ3 TRP A 180 -11.422 21.999 21.764 1.00 83.87 C ANISOU 1226 CZ3 TRP A 180 9005 13971 8889 -148 -126 -810 C ATOM 1227 CH2 TRP A 180 -12.702 21.602 22.150 1.00 99.61 C ANISOU 1227 CH2 TRP A 180 10907 16077 10863 -195 -115 -905 C ATOM 1228 N GLY A 181 -5.366 19.239 21.072 1.00 50.44 N ANISOU 1228 N GLY A 181 5127 9218 4821 -323 -36 -522 N ATOM 1229 CA GLY A 181 -4.224 20.092 20.720 1.00 54.51 C ANISOU 1229 CA GLY A 181 5698 9664 5349 -254 -52 -443 C ATOM 1230 C GLY A 181 -2.998 19.811 21.579 1.00 61.36 C ANISOU 1230 C GLY A 181 6633 10418 6264 -294 -29 -385 C ATOM 1231 O GLY A 181 -2.957 18.763 22.239 1.00 58.84 O ANISOU 1231 O GLY A 181 6325 10068 5962 -373 -1 -403 O ATOM 1232 N LYS A 182 -2.029 20.728 21.561 1.00 68.80 N ANISOU 1232 N LYS A 182 7618 11299 7222 -240 -40 -318 N ATOM 1233 CA LYS A 182 -0.714 20.597 22.235 1.00 61.19 C ANISOU 1233 CA LYS A 182 6715 10233 6302 -263 -24 -262 C ATOM 1234 C LYS A 182 -0.787 21.302 23.572 1.00 52.77 C ANISOU 1234 C LYS A 182 5655 9138 5253 -262 -24 -246 C ATOM 1235 O LYS A 182 -1.124 22.475 23.585 1.00 56.45 O ANISOU 1235 O LYS A 182 6111 9626 5708 -202 -44 -235 O ATOM 1236 CB LYS A 182 0.369 21.271 21.394 1.00 68.54 C ANISOU 1236 CB LYS A 182 7681 11122 7238 -208 -34 -206 C ATOM 1237 CG LYS A 182 1.795 20.813 21.681 1.00 70.98 C ANISOU 1237 CG LYS A 182 8039 11342 7585 -236 -17 -163 C ATOM 1238 CD LYS A 182 2.782 21.025 20.546 1.00 70.05 C ANISOU 1238 CD LYS A 182 7945 11202 7466 -201 -18 -126 C ATOM 1239 CE LYS A 182 3.152 22.479 20.318 1.00 75.56 C ANISOU 1239 CE LYS A 182 8661 11884 8164 -139 -28 -80 C ATOM 1240 NZ LYS A 182 3.807 22.669 18.997 1.00 86.21 N ANISOU 1240 NZ LYS A 182 10027 13232 9497 -104 -25 -53 N ATOM 1241 N PRO A 183 -0.429 20.631 24.690 1.00 47.36 N ANISOU 1241 N PRO A 183 4997 8402 4595 -320 -3 -242 N ATOM 1242 CA PRO A 183 -0.540 21.202 26.029 1.00 50.93 C ANISOU 1242 CA PRO A 183 5457 8832 5062 -322 -2 -231 C ATOM 1243 C PRO A 183 0.720 21.943 26.496 1.00 57.04 C ANISOU 1243 C PRO A 183 6276 9525 5868 -292 -10 -172 C ATOM 1244 O PRO A 183 0.773 22.411 27.635 1.00 63.44 O ANISOU 1244 O PRO A 183 7098 10311 6693 -292 -10 -162 O ATOM 1245 CB PRO A 183 -0.696 19.923 26.858 1.00 56.32 C ANISOU 1245 CB PRO A 183 6152 9495 5750 -402 27 -256 C ATOM 1246 CG PRO A 183 0.290 18.985 26.208 1.00 54.91 C ANISOU 1246 CG PRO A 183 6011 9266 5584 -423 36 -238 C ATOM 1247 CD PRO A 183 0.117 19.267 24.728 1.00 49.33 C ANISOU 1247 CD PRO A 183 5276 8609 4858 -382 19 -246 C ATOM 1248 N GLY A 184 1.743 21.997 25.648 1.00 45.09 N ANISOU 1248 N GLY A 184 4789 7976 4367 -271 -13 -138 N ATOM 1249 CA GLY A 184 2.976 22.704 26.014 1.00 41.72 C ANISOU 1249 CA GLY A 184 4398 7478 3972 -248 -17 -88 C ATOM 1250 C GLY A 184 4.052 22.462 25.011 1.00 42.71 C ANISOU 1250 C GLY A 184 4545 7574 4108 -240 -13 -61 C ATOM 1251 O GLY A 184 3.754 21.870 23.973 1.00 44.38 O ANISOU 1251 O GLY A 184 4742 7822 4297 -242 -11 -78 O ATOM 1252 N TYR A 185 5.277 22.869 25.328 1.00 44.18 N ANISOU 1252 N TYR A 185 4759 7699 4325 -233 -12 -23 N ATOM 1253 CA TYR A 185 6.426 22.703 24.396 1.00 40.60 C ANISOU 1253 CA TYR A 185 4323 7219 3883 -225 -5 2 C ATOM 1254 C TYR A 185 7.467 21.790 25.023 1.00 39.92 C ANISOU 1254 C TYR A 185 4259 7085 3823 -258 2 6 C ATOM 1255 O TYR A 185 8.582 21.793 24.566 1.00 55.00 O ANISOU 1255 O TYR A 185 6181 8967 5748 -251 7 27 O ATOM 1256 CB TYR A 185 7.010 24.085 24.117 1.00 43.96 C ANISOU 1256 CB TYR A 185 4761 7620 4322 -186 -9 39 C ATOM 1257 CG TYR A 185 5.959 25.110 23.765 1.00 48.75 C ANISOU 1257 CG TYR A 185 5356 8264 4900 -143 -20 37 C ATOM 1258 CD1 TYR A 185 5.368 25.125 22.514 1.00 48.83 C ANISOU 1258 CD1 TYR A 185 5355 8323 4873 -113 -23 31 C ATOM 1259 CD2 TYR A 185 5.544 26.047 24.686 1.00 52.29 C ANISOU 1259 CD2 TYR A 185 5807 8703 5356 -126 -31 38 C ATOM 1260 CE1 TYR A 185 4.409 26.055 22.183 1.00 53.35 C ANISOU 1260 CE1 TYR A 185 5921 8934 5415 -63 -37 27 C ATOM 1261 CE2 TYR A 185 4.584 26.985 24.370 1.00 50.52 C ANISOU 1261 CE2 TYR A 185 5577 8514 5104 -78 -44 34 C ATOM 1262 CZ TYR A 185 4.020 26.992 23.118 1.00 51.42 C ANISOU 1262 CZ TYR A 185 5681 8676 5179 -44 -48 29 C ATOM 1263 OH TYR A 185 3.065 27.918 22.808 1.00 57.14 O ANISOU 1263 OH TYR A 185 6402 9439 5870 14 -64 23 O ATOM 1264 N HIS A 186 7.077 21.037 26.043 1.00 46.50 N ANISOU 1264 N HIS A 186 5100 7912 4656 -290 4 -15 N ATOM 1265 CA HIS A 186 7.997 20.171 26.820 1.00 49.15 C ANISOU 1265 CA HIS A 186 5465 8199 5009 -313 9 -12 C ATOM 1266 C HIS A 186 8.593 19.069 25.929 1.00 47.35 C ANISOU 1266 C HIS A 186 5250 7963 4775 -322 18 -16 C ATOM 1267 O HIS A 186 9.712 18.621 26.223 1.00 66.72 O ANISOU 1267 O HIS A 186 7726 10377 7246 -319 18 -6 O ATOM 1268 CB HIS A 186 7.268 19.628 28.062 1.00 58.83 C ANISOU 1268 CB HIS A 186 6704 9421 6227 -344 13 -33 C ATOM 1269 CG HIS A 186 6.781 20.699 28.984 1.00 68.40 C ANISOU 1269 CG HIS A 186 7904 10639 7444 -330 4 -30 C ATOM 1270 ND1 HIS A 186 7.602 21.322 29.907 1.00 74.16 N ANISOU 1270 ND1 HIS A 186 8648 11330 8198 -315 -6 -11 N ATOM 1271 CD2 HIS A 186 5.563 21.275 29.122 1.00 75.59 C ANISOU 1271 CD2 HIS A 186 8787 11595 8337 -327 1 -47 C ATOM 1272 CE1 HIS A 186 6.909 22.226 30.583 1.00 80.13 C ANISOU 1272 CE1 HIS A 186 9391 12101 8952 -304 -14 -15 C ATOM 1273 NE2 HIS A 186 5.653 22.227 30.104 1.00 66.42 N ANISOU 1273 NE2 HIS A 186 7628 10417 7190 -309 -9 -37 N ATOM 1274 N GLY A 187 7.934 18.710 24.835 1.00 41.59 N ANISOU 1274 N GLY A 187 4504 7274 4022 -326 24 -33 N ATOM 1275 CA GLY A 187 8.445 17.664 23.926 1.00 51.22 C ANISOU 1275 CA GLY A 187 5736 8490 5234 -333 32 -42 C ATOM 1276 C GLY A 187 8.919 18.232 22.600 1.00 45.60 C ANISOU 1276 C GLY A 187 5008 7800 4518 -299 31 -24 C ATOM 1277 O GLY A 187 9.313 17.459 21.757 1.00 45.07 O ANISOU 1277 O GLY A 187 4946 7736 4441 -300 38 -32 O ATOM 1278 N ASP A 188 8.930 19.559 22.458 1.00 51.58 N ANISOU 1278 N ASP A 188 5750 8566 5280 -270 25 0 N ATOM 1279 CA ASP A 188 9.333 20.221 21.192 1.00 49.00 C ANISOU 1279 CA ASP A 188 5415 8257 4944 -237 29 21 C ATOM 1280 C ASP A 188 10.835 20.023 20.939 1.00 48.51 C ANISOU 1280 C ASP A 188 5366 8160 4905 -234 40 41 C ATOM 1281 O ASP A 188 11.355 20.593 19.978 1.00 55.90 O ANISOU 1281 O ASP A 188 6299 9104 5836 -212 49 63 O ATOM 1282 CB ASP A 188 8.950 21.704 21.184 1.00 53.39 C ANISOU 1282 CB ASP A 188 5964 8821 5498 -206 23 44 C ATOM 1283 CG ASP A 188 7.471 21.920 20.931 1.00 57.96 C ANISOU 1283 CG ASP A 188 6524 9455 6042 -192 12 21 C ATOM 1284 OD1 ASP A 188 6.686 20.949 21.147 1.00 45.91 O ANISOU 1284 OD1 ASP A 188 4985 7956 4503 -220 10 -17 O ATOM 1285 OD2 ASP A 188 7.120 23.048 20.522 1.00 57.58 O ANISOU 1285 OD2 ASP A 188 6475 9422 5980 -152 7 39 O ATOM 1286 N ILE A 189 11.527 19.264 21.777 1.00 61.85 N ANISOU 1286 N ILE A 189 7069 9814 6615 -252 38 33 N ATOM 1287 CA ILE A 189 12.956 18.963 21.484 1.00 58.30 C ANISOU 1287 CA ILE A 189 6625 9343 6183 -245 46 43 C ATOM 1288 C ILE A 189 12.927 17.842 20.458 1.00 57.10 C ANISOU 1288 C ILE A 189 6477 9211 6006 -245 53 24 C ATOM 1289 O ILE A 189 13.814 17.788 19.597 1.00 68.26 O ANISOU 1289 O ILE A 189 7885 10630 7419 -230 63 33 O ATOM 1290 CB ILE A 189 13.764 18.598 22.752 1.00 59.68 C ANISOU 1290 CB ILE A 189 6813 9477 6385 -252 38 39 C ATOM 1291 CG1 ILE A 189 15.219 18.298 22.410 1.00 58.41 C ANISOU 1291 CG1 ILE A 189 6647 9305 6238 -238 43 42 C ATOM 1292 CG2 ILE A 189 13.135 17.449 23.513 1.00 71.52 C ANISOU 1292 CG2 ILE A 189 8339 10963 7871 -271 31 15 C ATOM 1293 CD1 ILE A 189 15.925 19.428 21.675 1.00 53.17 C ANISOU 1293 CD1 ILE A 189 5960 8652 5588 -228 57 65 C ATOM 1294 N PHE A 190 11.900 17.005 20.542 1.00 48.57 N ANISOU 1294 N PHE A 190 5405 8143 4905 -265 49 -3 N ATOM 1295 CA PHE A 190 11.623 15.980 19.510 1.00 53.74 C ANISOU 1295 CA PHE A 190 6063 8821 5533 -269 55 -28 C ATOM 1296 C PHE A 190 11.037 16.683 18.293 1.00 55.42 C ANISOU 1296 C PHE A 190 6251 9085 5719 -248 57 -23 C ATOM 1297 O PHE A 190 10.243 17.620 18.492 1.00 45.68 O ANISOU 1297 O PHE A 190 5002 7871 4480 -241 50 -15 O ATOM 1298 CB PHE A 190 10.645 14.940 20.041 1.00 50.69 C ANISOU 1298 CB PHE A 190 5695 8431 5134 -306 54 -64 C ATOM 1299 CG PHE A 190 11.181 14.166 21.214 1.00 55.51 C ANISOU 1299 CG PHE A 190 6342 8986 5760 -321 55 -67 C ATOM 1300 CD1 PHE A 190 11.029 14.648 22.506 1.00 45.58 C ANISOU 1300 CD1 PHE A 190 5092 7706 4519 -330 49 -55 C ATOM 1301 CD2 PHE A 190 11.839 12.961 21.016 1.00 50.32 C ANISOU 1301 CD2 PHE A 190 5719 8300 5099 -321 59 -81 C ATOM 1302 CE1 PHE A 190 11.527 13.932 23.577 1.00 57.70 C ANISOU 1302 CE1 PHE A 190 6668 9192 6063 -337 48 -57 C ATOM 1303 CE2 PHE A 190 12.320 12.242 22.095 1.00 52.03 C ANISOU 1303 CE2 PHE A 190 5980 8464 5325 -326 58 -83 C ATOM 1304 CZ PHE A 190 12.180 12.738 23.368 1.00 61.16 C ANISOU 1304 CZ PHE A 190 7142 9599 6494 -333 52 -69 C ATOM 1305 N GLU A 191 11.405 16.240 17.085 1.00 52.28 N ANISOU 1305 N GLU A 191 5851 8710 5302 -233 64 -29 N ATOM 1306 CA GLU A 191 10.945 16.888 15.836 1.00 47.46 C ANISOU 1306 CA GLU A 191 5222 8149 4659 -205 66 -22 C ATOM 1307 C GLU A 191 9.422 16.789 15.700 1.00 47.69 C ANISOU 1307 C GLU A 191 5235 8225 4659 -212 53 -55 C ATOM 1308 O GLU A 191 8.822 17.810 15.345 1.00 59.83 O ANISOU 1308 O GLU A 191 6759 9796 6178 -184 47 -41 O ATOM 1309 CB GLU A 191 11.593 16.227 14.623 1.00 59.51 C ANISOU 1309 CB GLU A 191 6751 9692 6166 -189 76 -29 C ATOM 1310 CG GLU A 191 11.035 16.727 13.291 1.00 56.20 C ANISOU 1310 CG GLU A 191 6318 9329 5703 -157 77 -27 C ATOM 1311 CD GLU A 191 9.802 16.028 12.780 1.00 57.40 C ANISOU 1311 CD GLU A 191 6457 9530 5821 -164 63 -74 C ATOM 1312 OE1 GLU A 191 8.925 16.726 12.254 1.00 63.17 O ANISOU 1312 OE1 GLU A 191 7171 10308 6519 -137 54 -75 O ATOM 1313 OE2 GLU A 191 9.736 14.789 12.905 1.00 76.37 O ANISOU 1313 OE2 GLU A 191 8867 11923 8226 -194 63 -113 O ATOM 1314 N TRP A 192 8.826 15.607 15.887 1.00 41.84 N ANISOU 1314 N TRP A 192 4496 7488 3911 -247 51 -99 N ATOM 1315 CA TRP A 192 7.375 15.469 15.603 1.00 50.35 C ANISOU 1315 CA TRP A 192 5547 8623 4958 -258 41 -141 C ATOM 1316 C TRP A 192 6.572 16.480 16.410 1.00 52.43 C ANISOU 1316 C TRP A 192 5793 8901 5226 -254 32 -132 C ATOM 1317 O TRP A 192 5.673 17.085 15.844 1.00 53.79 O ANISOU 1317 O TRP A 192 5938 9132 5368 -227 20 -145 O ATOM 1318 CB TRP A 192 6.866 14.066 15.893 1.00 55.76 C ANISOU 1318 CB TRP A 192 6241 9301 5641 -311 47 -192 C ATOM 1319 CG TRP A 192 5.447 13.919 15.436 1.00 57.75 C ANISOU 1319 CG TRP A 192 6457 9623 5861 -325 39 -243 C ATOM 1320 CD1 TRP A 192 5.006 13.663 14.173 1.00 58.07 C ANISOU 1320 CD1 TRP A 192 6475 9724 5865 -308 32 -276 C ATOM 1321 CD2 TRP A 192 4.272 14.048 16.250 1.00 67.73 C ANISOU 1321 CD2 TRP A 192 7696 10913 7123 -358 36 -273 C ATOM 1322 NE1 TRP A 192 3.642 13.611 14.141 1.00 64.51 N ANISOU 1322 NE1 TRP A 192 7250 10603 6658 -327 23 -327 N ATOM 1323 CE2 TRP A 192 3.161 13.847 15.401 1.00 73.79 C ANISOU 1323 CE2 TRP A 192 8422 11760 7854 -359 27 -327 C ATOM 1324 CE3 TRP A 192 4.049 14.314 17.606 1.00 56.85 C ANISOU 1324 CE3 TRP A 192 6325 9504 5769 -384 41 -262 C ATOM 1325 CZ2 TRP A 192 1.852 13.911 15.872 1.00 66.34 C ANISOU 1325 CZ2 TRP A 192 7438 10868 6898 -388 24 -372 C ATOM 1326 CZ3 TRP A 192 2.759 14.370 18.076 1.00 60.39 C ANISOU 1326 CZ3 TRP A 192 6739 9999 6205 -413 41 -303 C ATOM 1327 CH2 TRP A 192 1.678 14.163 17.217 1.00 77.60 C ANISOU 1327 CH2 TRP A 192 8873 12261 8350 -417 32 -359 C ATOM 1328 N CYS A 193 6.895 16.668 17.679 1.00 52.86 N ANISOU 1328 N CYS A 193 5863 8905 5313 -274 35 -114 N ATOM 1329 CA CYS A 193 6.097 17.565 18.553 1.00 69.32 C ANISOU 1329 CA CYS A 193 7932 11002 7402 -271 26 -110 C ATOM 1330 C CYS A 193 6.278 19.041 18.170 1.00 60.09 C ANISOU 1330 C CYS A 193 6758 9843 6229 -217 18 -70 C ATOM 1331 O CYS A 193 5.379 19.838 18.459 1.00 55.51 O ANISOU 1331 O CYS A 193 6160 9294 5637 -198 6 -75 O ATOM 1332 CB CYS A 193 6.449 17.336 20.018 1.00 60.54 C ANISOU 1332 CB CYS A 193 6842 9834 6324 -304 31 -102 C ATOM 1333 SG CYS A 193 5.574 15.916 20.722 1.00 73.32 S ANISOU 1333 SG CYS A 193 8468 11452 7936 -371 43 -154 S ATOM 1334 N ALA A 194 7.400 19.406 17.569 1.00 48.80 N ANISOU 1334 N ALA A 194 5346 8386 4807 -192 26 -32 N ATOM 1335 CA ALA A 194 7.680 20.832 17.296 1.00 56.93 C ANISOU 1335 CA ALA A 194 6384 9410 5836 -149 26 10 C ATOM 1336 C ALA A 194 7.135 21.249 15.926 1.00 51.63 C ANISOU 1336 C ALA A 194 5705 8793 5117 -102 21 10 C ATOM 1337 O ALA A 194 6.995 22.455 15.691 1.00 51.73 O ANISOU 1337 O ALA A 194 5730 8808 5117 -60 19 40 O ATOM 1338 CB ALA A 194 9.163 21.100 17.394 1.00 64.25 C ANISOU 1338 CB ALA A 194 7333 10282 6796 -152 43 48 C ATOM 1339 N THR A 195 6.842 20.305 15.039 1.00 54.65 N ANISOU 1339 N THR A 195 6074 9217 5471 -106 20 -21 N ATOM 1340 CA THR A 195 6.324 20.741 13.709 1.00 63.60 C ANISOU 1340 CA THR A 195 7201 10408 6552 -53 13 -22 C ATOM 1341 C THR A 195 4.954 20.121 13.400 1.00 63.90 C ANISOU 1341 C THR A 195 7202 10522 6554 -54 -7 -83 C ATOM 1342 O THR A 195 4.229 20.736 12.594 1.00 56.15 O ANISOU 1342 O THR A 195 6210 9598 5526 0 -22 -89 O ATOM 1343 CB THR A 195 7.328 20.471 12.580 1.00 57.87 C ANISOU 1343 CB THR A 195 6494 9677 5814 -38 31 -1 C ATOM 1344 OG1 THR A 195 7.552 19.065 12.459 1.00 55.59 O ANISOU 1344 OG1 THR A 195 6197 9391 5532 -78 34 -38 O ATOM 1345 CG2 THR A 195 8.653 21.167 12.801 1.00 60.22 C ANISOU 1345 CG2 THR A 195 6823 9913 6146 -39 54 53 C ATOM 1346 N SER A 196 4.613 18.968 13.981 1.00 62.13 N ANISOU 1346 N SER A 196 6960 10299 6346 -111 -6 -130 N ATOM 1347 CA SER A 196 3.349 18.273 13.621 1.00 60.68 C ANISOU 1347 CA SER A 196 6736 10189 6130 -124 -20 -197 C ATOM 1348 C SER A 196 2.203 18.564 14.613 1.00 53.13 C ANISOU 1348 C SER A 196 5748 9262 5176 -141 -32 -228 C ATOM 1349 O SER A 196 1.122 18.887 14.171 1.00 73.87 O ANISOU 1349 O SER A 196 8336 11965 7764 -110 -51 -264 O ATOM 1350 CB SER A 196 3.593 16.811 13.456 1.00 66.94 C ANISOU 1350 CB SER A 196 7532 10970 6931 -179 -8 -235 C ATOM 1351 OG SER A 196 4.769 16.590 12.686 1.00 66.99 O ANISOU 1351 OG SER A 196 7567 10944 6938 -161 2 -203 O ATOM 1352 N TRP A 197 2.398 18.405 15.905 1.00 64.94 N ANISOU 1352 N TRP A 197 7256 10705 6713 -187 -20 -220 N ATOM 1353 CA TRP A 197 1.338 18.713 16.901 1.00 56.08 C ANISOU 1353 CA TRP A 197 6104 9611 5592 -204 -27 -248 C ATOM 1354 C TRP A 197 1.207 20.231 17.026 1.00 62.75 C ANISOU 1354 C TRP A 197 6951 10462 6428 -137 -43 -210 C ATOM 1355 O TRP A 197 2.243 20.895 17.073 1.00 93.92 O ANISOU 1355 O TRP A 197 10938 14350 10397 -113 -37 -152 O ATOM 1356 CB TRP A 197 1.759 18.128 18.243 1.00 56.85 C ANISOU 1356 CB TRP A 197 6226 9641 5733 -267 -8 -241 C ATOM 1357 CG TRP A 197 0.634 17.631 19.080 1.00 59.14 C ANISOU 1357 CG TRP A 197 6485 9964 6019 -319 -2 -294 C ATOM 1358 CD1 TRP A 197 -0.672 17.511 18.713 1.00 55.92 C ANISOU 1358 CD1 TRP A 197 6023 9645 5578 -324 -11 -355 C ATOM 1359 CD2 TRP A 197 0.734 17.118 20.420 1.00 53.61 C ANISOU 1359 CD2 TRP A 197 5807 9213 5349 -377 17 -294 C ATOM 1360 NE1 TRP A 197 -1.399 16.979 19.741 1.00 60.31 N ANISOU 1360 NE1 TRP A 197 6562 10207 6142 -387 5 -394 N ATOM 1361 CE2 TRP A 197 -0.572 16.734 20.804 1.00 55.63 C ANISOU 1361 CE2 TRP A 197 6021 9528 5587 -420 23 -354 C ATOM 1362 CE3 TRP A 197 1.785 16.960 21.328 1.00 45.10 C ANISOU 1362 CE3 TRP A 197 4780 8049 4306 -394 29 -251 C ATOM 1363 CZ2 TRP A 197 -0.852 16.190 22.054 1.00 50.72 C ANISOU 1363 CZ2 TRP A 197 5413 8877 4982 -483 47 -368 C ATOM 1364 CZ3 TRP A 197 1.506 16.425 22.568 1.00 52.26 C ANISOU 1364 CZ3 TRP A 197 5702 8928 5227 -448 47 -264 C ATOM 1365 CH2 TRP A 197 0.209 16.049 22.926 1.00 56.28 C ANISOU 1365 CH2 TRP A 197 6175 9491 5717 -494 58 -319 C ATOM 1366 N LEU A 198 -0.001 20.766 17.092 1.00 62.25 N ANISOU 1366 N LEU A 198 6846 10468 6335 -108 -62 -245 N ATOM 1367 CA LEU A 198 -0.172 22.245 17.157 1.00 59.75 C ANISOU 1367 CA LEU A 198 6540 10155 6005 -35 -79 -210 C ATOM 1368 C LEU A 198 -1.002 22.614 18.386 1.00 65.62 C ANISOU 1368 C LEU A 198 7257 10915 6759 -47 -85 -234 C ATOM 1369 O LEU A 198 -1.972 21.930 18.696 1.00 49.55 O ANISOU 1369 O LEU A 198 5174 8938 4713 -87 -85 -295 O ATOM 1370 CB LEU A 198 -0.849 22.721 15.869 1.00 55.90 C ANISOU 1370 CB LEU A 198 6033 9747 5459 40 -103 -227 C ATOM 1371 CG LEU A 198 0.084 22.833 14.654 1.00 64.45 C ANISOU 1371 CG LEU A 198 7156 10804 6526 76 -97 -183 C ATOM 1372 CD1 LEU A 198 -0.527 23.705 13.591 1.00 61.66 C ANISOU 1372 CD1 LEU A 198 6801 10513 6111 169 -122 -182 C ATOM 1373 CD2 LEU A 198 1.435 23.417 15.023 1.00 69.92 C ANISOU 1373 CD2 LEU A 198 7907 11397 7259 71 -76 -110 C ATOM 1374 N THR A 199 -0.601 23.663 19.080 1.00 65.00 N ANISOU 1374 N THR A 199 7210 10786 6701 -19 -87 -189 N ATOM 1375 CA THR A 199 -1.329 24.188 20.252 1.00 57.96 C ANISOU 1375 CA THR A 199 6298 9906 5816 -19 -94 -206 C ATOM 1376 C THR A 199 -2.644 24.815 19.781 1.00 61.57 C ANISOU 1376 C THR A 199 6711 10460 6222 46 -122 -248 C ATOM 1377 O THR A 199 -2.618 25.515 18.767 1.00 74.33 O ANISOU 1377 O THR A 199 8343 12093 7804 120 -139 -227 O ATOM 1378 CB THR A 199 -0.475 25.240 20.965 1.00 65.06 C ANISOU 1378 CB THR A 199 7248 10724 6748 2 -91 -146 C ATOM 1379 OG1 THR A 199 -0.178 26.259 20.011 1.00 60.99 O ANISOU 1379 OG1 THR A 199 6764 10198 6209 77 -102 -107 O ATOM 1380 CG2 THR A 199 0.814 24.679 21.519 1.00 68.80 C ANISOU 1380 CG2 THR A 199 7757 11111 7270 -55 -68 -112 C ATOM 1381 N SER A 200 -3.761 24.552 20.458 1.00 62.43 N ANISOU 1381 N SER A 200 6764 10634 6320 23 -126 -307 N ATOM 1382 CA SER A 200 -5.026 25.237 20.115 1.00 56.98 C ANISOU 1382 CA SER A 200 6026 10044 5580 95 -157 -353 C ATOM 1383 C SER A 200 -5.313 26.245 21.203 1.00 58.51 C ANISOU 1383 C SER A 200 6225 10221 5782 126 -164 -341 C ATOM 1384 O SER A 200 -5.145 25.876 22.354 1.00 65.25 O ANISOU 1384 O SER A 200 7080 11038 6673 61 -144 -342 O ATOM 1385 CB SER A 200 -6.175 24.289 19.923 1.00 52.20 C ANISOU 1385 CB SER A 200 5342 9543 4948 55 -158 -439 C ATOM 1386 OG SER A 200 -6.405 23.500 21.050 1.00 50.64 O ANISOU 1386 OG SER A 200 5122 9336 4780 -36 -130 -469 O ATOM 1387 N ALA A 201 -5.778 27.432 20.831 1.00 61.59 N ANISOU 1387 N ALA A 201 6621 10642 6137 226 -194 -335 N ATOM 1388 CA ALA A 201 -6.073 28.517 21.791 1.00 61.54 C ANISOU 1388 CA ALA A 201 6626 10620 6134 270 -205 -325 C ATOM 1389 C ALA A 201 -7.122 28.046 22.807 1.00 62.68 C ANISOU 1389 C ALA A 201 6700 10836 6279 224 -201 -393 C ATOM 1390 O ALA A 201 -7.003 28.414 23.990 1.00 54.27 O ANISOU 1390 O ALA A 201 5649 9730 5242 206 -192 -381 O ATOM 1391 CB ALA A 201 -6.529 29.737 21.035 1.00 67.32 C ANISOU 1391 CB ALA A 201 7377 11385 6817 392 -239 -315 C ATOM 1392 N TYR A 202 -8.114 27.274 22.370 1.00 70.17 N ANISOU 1392 N TYR A 202 7574 11892 7196 204 -205 -467 N ATOM 1393 CA TYR A 202 -9.144 26.724 23.279 1.00 73.06 C ANISOU 1393 CA TYR A 202 7866 12333 7560 147 -192 -539 C ATOM 1394 C TYR A 202 -8.469 25.912 24.381 1.00 68.27 C ANISOU 1394 C TYR A 202 7287 11646 7006 37 -151 -517 C ATOM 1395 O TYR A 202 -8.779 26.138 25.561 1.00 59.97 O ANISOU 1395 O TYR A 202 6225 10592 5967 17 -140 -528 O ATOM 1396 CB TYR A 202 -10.094 25.785 22.542 1.00 72.14 C ANISOU 1396 CB TYR A 202 7669 12330 7409 116 -194 -621 C ATOM 1397 CG TYR A 202 -10.864 26.383 21.397 1.00 69.45 C ANISOU 1397 CG TYR A 202 7290 12089 7008 222 -237 -658 C ATOM 1398 CD1 TYR A 202 -11.614 27.536 21.553 1.00 69.49 C ANISOU 1398 CD1 TYR A 202 7275 12152 6976 324 -271 -675 C ATOM 1399 CD2 TYR A 202 -10.873 25.755 20.157 1.00 79.31 C ANISOU 1399 CD2 TYR A 202 8521 13378 8231 223 -245 -680 C ATOM 1400 CE1 TYR A 202 -12.371 28.031 20.504 1.00 86.95 C ANISOU 1400 CE1 TYR A 202 9450 14461 9125 429 -314 -714 C ATOM 1401 CE2 TYR A 202 -11.577 26.265 19.081 1.00 68.06 C ANISOU 1401 CE2 TYR A 202 7063 12051 6746 325 -287 -716 C ATOM 1402 CZ TYR A 202 -12.345 27.401 19.264 1.00 86.22 C ANISOU 1402 CZ TYR A 202 9342 14409 9006 430 -322 -734 C ATOM 1403 OH TYR A 202 -13.087 27.879 18.219 1.00 83.23 O ANISOU 1403 OH TYR A 202 8930 14133 8560 540 -367 -773 O ATOM 1404 N PHE A 203 -7.565 25.004 23.999 1.00 64.97 N ANISOU 1404 N PHE A 203 6905 11164 6614 -23 -129 -488 N ATOM 1405 CA PHE A 203 -6.881 24.100 24.963 1.00 55.30 C ANISOU 1405 CA PHE A 203 5714 9862 5435 -123 -91 -468 C ATOM 1406 C PHE A 203 -5.936 24.902 25.857 1.00 51.89 C ANISOU 1406 C PHE A 203 5345 9331 5037 -102 -91 -400 C ATOM 1407 O PHE A 203 -5.899 24.668 27.057 1.00 55.51 O ANISOU 1407 O PHE A 203 5811 9760 5517 -152 -70 -401 O ATOM 1408 CB PHE A 203 -6.118 22.988 24.256 1.00 45.57 C ANISOU 1408 CB PHE A 203 4509 8586 4218 -179 -73 -454 C ATOM 1409 CG PHE A 203 -5.706 21.881 25.184 1.00 49.95 C ANISOU 1409 CG PHE A 203 5089 9083 4806 -279 -34 -452 C ATOM 1410 CD1 PHE A 203 -6.184 21.820 26.476 1.00 50.62 C ANISOU 1410 CD1 PHE A 203 5163 9172 4898 -321 -14 -471 C ATOM 1411 CD2 PHE A 203 -4.858 20.870 24.756 1.00 61.74 C ANISOU 1411 CD2 PHE A 203 6621 10517 6317 -328 -15 -432 C ATOM 1412 CE1 PHE A 203 -5.795 20.796 27.324 1.00 60.63 C ANISOU 1412 CE1 PHE A 203 6465 10380 6189 -407 22 -465 C ATOM 1413 CE2 PHE A 203 -4.480 19.836 25.600 1.00 56.66 C ANISOU 1413 CE2 PHE A 203 6012 9816 5699 -412 18 -429 C ATOM 1414 CZ PHE A 203 -4.948 19.802 26.888 1.00 57.07 C ANISOU 1414 CZ PHE A 203 6059 9868 5756 -451 38 -444 C ATOM 1415 N THR A 204 -5.208 25.839 25.276 1.00 48.25 N ANISOU 1415 N THR A 204 4929 8822 4579 -31 -111 -346 N ATOM 1416 CA THR A 204 -4.259 26.678 26.025 1.00 53.73 C ANISOU 1416 CA THR A 204 5683 9422 5307 -12 -112 -286 C ATOM 1417 C THR A 204 -5.054 27.531 27.007 1.00 53.82 C ANISOU 1417 C THR A 204 5673 9465 5309 22 -124 -309 C ATOM 1418 O THR A 204 -4.655 27.609 28.175 1.00 51.73 O ANISOU 1418 O THR A 204 5432 9149 5074 -8 -112 -292 O ATOM 1419 CB THR A 204 -3.398 27.509 25.067 1.00 68.72 C ANISOU 1419 CB THR A 204 7633 11268 7207 51 -126 -230 C ATOM 1420 OG1 THR A 204 -2.687 26.566 24.264 1.00 60.97 O ANISOU 1420 OG1 THR A 204 6664 10264 6235 9 -111 -216 O ATOM 1421 CG2 THR A 204 -2.421 28.431 25.770 1.00 73.36 C ANISOU 1421 CG2 THR A 204 8279 11761 7831 67 -125 -174 C ATOM 1422 N GLY A 205 -6.156 28.124 26.556 1.00 56.71 N ANISOU 1422 N GLY A 205 5994 9919 5631 89 -148 -349 N ATOM 1423 CA GLY A 205 -6.984 28.979 27.435 1.00 58.43 C ANISOU 1423 CA GLY A 205 6188 10177 5834 133 -163 -377 C ATOM 1424 C GLY A 205 -7.541 28.180 28.585 1.00 48.87 C ANISOU 1424 C GLY A 205 4935 9001 4632 53 -136 -421 C ATOM 1425 O GLY A 205 -7.607 28.704 29.669 1.00 44.93 O ANISOU 1425 O GLY A 205 4445 8483 4144 59 -135 -418 O ATOM 1426 N PHE A 206 -7.952 26.947 28.306 1.00 52.36 N ANISOU 1426 N PHE A 206 5334 9493 5067 -19 -114 -464 N ATOM 1427 CA PHE A 206 -8.492 25.993 29.304 1.00 49.37 C ANISOU 1427 CA PHE A 206 4920 9144 4693 -111 -78 -508 C ATOM 1428 C PHE A 206 -7.453 25.770 30.395 1.00 52.90 C ANISOU 1428 C PHE A 206 5432 9483 5181 -161 -55 -455 C ATOM 1429 O PHE A 206 -7.761 26.008 31.565 1.00 51.97 O ANISOU 1429 O PHE A 206 5311 9369 5067 -173 -45 -466 O ATOM 1430 CB PHE A 206 -8.816 24.697 28.572 1.00 53.42 C ANISOU 1430 CB PHE A 206 5398 9701 5196 -182 -57 -549 C ATOM 1431 CG PHE A 206 -9.341 23.561 29.399 1.00 52.03 C ANISOU 1431 CG PHE A 206 5195 9550 5024 -289 -12 -594 C ATOM 1432 CD1 PHE A 206 -10.560 23.655 30.034 1.00 56.67 C ANISOU 1432 CD1 PHE A 206 5713 10231 5585 -303 -2 -660 C ATOM 1433 CD2 PHE A 206 -8.643 22.369 29.480 1.00 61.12 C ANISOU 1433 CD2 PHE A 206 6390 10631 6199 -376 21 -574 C ATOM 1434 CE1 PHE A 206 -11.058 22.586 30.759 1.00 61.37 C ANISOU 1434 CE1 PHE A 206 6287 10847 6181 -409 46 -702 C ATOM 1435 CE2 PHE A 206 -9.138 21.303 30.210 1.00 66.75 C ANISOU 1435 CE2 PHE A 206 7090 11360 6912 -477 67 -614 C ATOM 1436 CZ PHE A 206 -10.345 21.413 30.849 1.00 59.14 C ANISOU 1436 CZ PHE A 206 6059 10486 5923 -497 82 -677 C ATOM 1437 N ILE A 207 -6.258 25.333 29.995 1.00 61.59 N ANISOU 1437 N ILE A 207 6591 10498 6312 -184 -49 -403 N ATOM 1438 CA ILE A 207 -5.123 25.060 30.931 1.00 57.89 C ANISOU 1438 CA ILE A 207 6187 9926 5882 -225 -31 -353 C ATOM 1439 C ILE A 207 -4.824 26.312 31.751 1.00 59.46 C ANISOU 1439 C ILE A 207 6411 10086 6092 -169 -51 -324 C ATOM 1440 O ILE A 207 -4.751 26.191 32.976 1.00 64.33 O ANISOU 1440 O ILE A 207 7042 10679 6720 -201 -35 -323 O ATOM 1441 CB ILE A 207 -3.865 24.635 30.163 1.00 55.78 C ANISOU 1441 CB ILE A 207 5969 9583 5640 -235 -31 -304 C ATOM 1442 CG1 ILE A 207 -4.064 23.329 29.399 1.00 61.26 C ANISOU 1442 CG1 ILE A 207 6647 10304 6324 -294 -11 -333 C ATOM 1443 CG2 ILE A 207 -2.699 24.535 31.123 1.00 64.50 C ANISOU 1443 CG2 ILE A 207 7134 10591 6780 -259 -21 -258 C ATOM 1444 CD1 ILE A 207 -3.018 23.078 28.351 1.00 63.57 C ANISOU 1444 CD1 ILE A 207 6976 10545 6631 -283 -17 -294 C ATOM 1445 N VAL A 208 -4.640 27.459 31.093 1.00 54.20 N ANISOU 1445 N VAL A 208 5757 9412 5423 -87 -81 -301 N ATOM 1446 CA VAL A 208 -4.247 28.719 31.790 1.00 49.04 C ANISOU 1446 CA VAL A 208 5138 8709 4785 -33 -100 -271 C ATOM 1447 C VAL A 208 -5.306 29.106 32.822 1.00 54.00 C ANISOU 1447 C VAL A 208 5728 9397 5392 -20 -101 -315 C ATOM 1448 O VAL A 208 -4.944 29.380 33.961 1.00 58.28 O ANISOU 1448 O VAL A 208 6296 9894 5953 -31 -97 -302 O ATOM 1449 CB VAL A 208 -4.053 29.850 30.788 1.00 57.88 C ANISOU 1449 CB VAL A 208 6279 9814 5896 51 -128 -244 C ATOM 1450 CG1 VAL A 208 -3.879 31.186 31.486 1.00 61.20 C ANISOU 1450 CG1 VAL A 208 6733 10192 6326 109 -146 -225 C ATOM 1451 CG2 VAL A 208 -2.896 29.539 29.851 1.00 69.35 C ANISOU 1451 CG2 VAL A 208 7774 11203 7371 36 -122 -197 C ATOM 1452 N CYS A 209 -6.571 29.075 32.432 1.00 58.15 N ANISOU 1452 N CYS A 209 6189 10024 5878 0 -107 -370 N ATOM 1453 CA CYS A 209 -7.680 29.477 33.329 1.00 62.96 C ANISOU 1453 CA CYS A 209 6752 10707 6462 19 -108 -420 C ATOM 1454 C CYS A 209 -7.899 28.457 34.455 1.00 69.97 C ANISOU 1454 C CYS A 209 7625 11605 7355 -73 -69 -444 C ATOM 1455 O CYS A 209 -8.352 28.895 35.529 1.00 68.42 O ANISOU 1455 O CYS A 209 7416 11428 7150 -64 -66 -464 O ATOM 1456 CB CYS A 209 -8.973 29.676 32.547 1.00 68.41 C ANISOU 1456 CB CYS A 209 7370 11516 7106 68 -126 -480 C ATOM 1457 SG CYS A 209 -8.911 31.075 31.387 1.00 79.31 S ANISOU 1457 SG CYS A 209 8777 12890 8465 199 -175 -455 S ATOM 1458 N LEU A 210 -7.681 27.158 34.210 1.00 61.57 N ANISOU 1458 N LEU A 210 6562 10532 6299 -157 -38 -446 N ATOM 1459 CA LEU A 210 -7.997 26.114 35.220 1.00 57.73 C ANISOU 1459 CA LEU A 210 6067 10055 5809 -249 5 -471 C ATOM 1460 C LEU A 210 -6.760 25.653 35.984 1.00 63.32 C ANISOU 1460 C LEU A 210 6852 10654 6551 -291 21 -416 C ATOM 1461 O LEU A 210 -6.923 24.819 36.907 1.00 57.08 O ANISOU 1461 O LEU A 210 6072 9859 5756 -361 58 -427 O ATOM 1462 CB LEU A 210 -8.650 24.921 34.527 1.00 66.21 C ANISOU 1462 CB LEU A 210 7098 11191 6867 -318 32 -517 C ATOM 1463 CG LEU A 210 -10.163 25.037 34.360 1.00 83.80 C ANISOU 1463 CG LEU A 210 9232 13551 9054 -311 34 -597 C ATOM 1464 CD1 LEU A 210 -10.523 26.071 33.301 1.00 88.19 C ANISOU 1464 CD1 LEU A 210 9754 14162 9592 -207 -15 -609 C ATOM 1465 CD2 LEU A 210 -10.768 23.690 34.005 1.00 96.71 C ANISOU 1465 CD2 LEU A 210 10829 15238 10678 -408 74 -648 C ATOM 1466 N LEU A 211 -5.570 26.151 35.658 1.00 74.87 N ANISOU 1466 N LEU A 211 8368 12033 8043 -252 -2 -360 N ATOM 1467 CA LEU A 211 -4.348 25.698 36.373 1.00 63.11 C ANISOU 1467 CA LEU A 211 6946 10448 6584 -286 8 -313 C ATOM 1468 C LEU A 211 -3.407 26.876 36.636 1.00 61.31 C ANISOU 1468 C LEU A 211 6757 10153 6382 -223 -23 -271 C ATOM 1469 O LEU A 211 -3.152 27.156 37.804 1.00 58.91 O ANISOU 1469 O LEU A 211 6476 9820 6084 -223 -22 -263 O ATOM 1470 CB LEU A 211 -3.677 24.592 35.554 1.00 72.70 C ANISOU 1470 CB LEU A 211 8185 11624 7811 -333 22 -294 C ATOM 1471 CG LEU A 211 -2.204 24.330 35.868 1.00 83.28 C ANISOU 1471 CG LEU A 211 9592 12865 9183 -341 20 -242 C ATOM 1472 CD1 LEU A 211 -1.965 24.243 37.359 1.00 78.95 C ANISOU 1472 CD1 LEU A 211 9078 12283 8636 -359 32 -234 C ATOM 1473 CD2 LEU A 211 -1.738 23.053 35.195 1.00 84.91 C ANISOU 1473 CD2 LEU A 211 9821 13045 9395 -392 40 -234 C ATOM 1474 N TYR A 212 -2.875 27.510 35.593 1.00 59.25 N ANISOU 1474 N TYR A 212 6506 9868 6136 -176 -47 -245 N ATOM 1475 CA TYR A 212 -1.894 28.611 35.744 1.00 61.02 C ANISOU 1475 CA TYR A 212 6772 10022 6389 -127 -72 -205 C ATOM 1476 C TYR A 212 -2.513 29.830 36.434 1.00 57.54 C ANISOU 1476 C TYR A 212 6321 9603 5938 -70 -91 -222 C ATOM 1477 O TYR A 212 -1.848 30.386 37.318 1.00 52.61 O ANISOU 1477 O TYR A 212 5729 8923 5334 -60 -99 -204 O ATOM 1478 CB TYR A 212 -1.286 28.971 34.394 1.00 59.94 C ANISOU 1478 CB TYR A 212 6649 9858 6264 -95 -86 -175 C ATOM 1479 CG TYR A 212 -0.447 27.873 33.789 1.00 71.15 C ANISOU 1479 CG TYR A 212 8087 11244 7699 -144 -70 -153 C ATOM 1480 CD1 TYR A 212 0.529 27.224 34.530 1.00 75.36 C ANISOU 1480 CD1 TYR A 212 8656 11720 8258 -186 -58 -134 C ATOM 1481 CD2 TYR A 212 -0.584 27.510 32.456 1.00 71.39 C ANISOU 1481 CD2 TYR A 212 8103 11302 7719 -140 -69 -154 C ATOM 1482 CE1 TYR A 212 1.326 26.230 33.984 1.00 87.14 C ANISOU 1482 CE1 TYR A 212 10166 13180 9762 -223 -46 -116 C ATOM 1483 CE2 TYR A 212 0.205 26.520 31.891 1.00 68.75 C ANISOU 1483 CE2 TYR A 212 7787 10937 7398 -181 -55 -137 C ATOM 1484 CZ TYR A 212 1.168 25.878 32.654 1.00 86.15 C ANISOU 1484 CZ TYR A 212 10025 13080 9626 -221 -43 -118 C ATOM 1485 OH TYR A 212 1.965 24.912 32.112 1.00 64.10 O ANISOU 1485 OH TYR A 212 7252 10256 6844 -253 -32 -102 O ATOM 1486 N ALA A 213 -3.707 30.261 36.040 1.00 56.18 N ANISOU 1486 N ALA A 213 6103 9508 5732 -30 -100 -258 N ATOM 1487 CA ALA A 213 -4.327 31.471 36.633 1.00 54.89 C ANISOU 1487 CA ALA A 213 5931 9368 5555 34 -121 -278 C ATOM 1488 C ALA A 213 -4.747 31.237 38.088 1.00 60.97 C ANISOU 1488 C ALA A 213 6688 10159 6316 3 -105 -305 C ATOM 1489 O ALA A 213 -4.504 32.097 38.931 1.00 61.46 O ANISOU 1489 O ALA A 213 6775 10188 6388 37 -120 -299 O ATOM 1490 CB ALA A 213 -5.480 31.949 35.804 1.00 43.77 C ANISOU 1490 CB ALA A 213 4477 8044 4109 93 -137 -313 C ATOM 1491 N PRO A 214 -5.406 30.117 38.451 1.00 51.17 N ANISOU 1491 N PRO A 214 5411 8975 5055 -60 -74 -337 N ATOM 1492 CA PRO A 214 -5.791 29.887 39.848 1.00 57.38 C ANISOU 1492 CA PRO A 214 6192 9780 5828 -91 -54 -360 C ATOM 1493 C PRO A 214 -4.614 29.800 40.844 1.00 56.59 C ANISOU 1493 C PRO A 214 6154 9589 5756 -113 -51 -321 C ATOM 1494 O PRO A 214 -4.645 30.473 41.843 1.00 42.47 O ANISOU 1494 O PRO A 214 4376 7794 3966 -85 -61 -327 O ATOM 1495 CB PRO A 214 -6.536 28.540 39.798 1.00 52.26 C ANISOU 1495 CB PRO A 214 5506 9192 5156 -170 -13 -393 C ATOM 1496 CG PRO A 214 -6.965 28.407 38.370 1.00 48.51 C ANISOU 1496 CG PRO A 214 4993 8764 4672 -156 -23 -409 C ATOM 1497 CD PRO A 214 -5.850 29.039 37.568 1.00 46.75 C ANISOU 1497 CD PRO A 214 4818 8463 4480 -108 -54 -356 C ATOM 1498 N ALA A 215 -3.585 29.007 40.537 1.00 52.87 N ANISOU 1498 N ALA A 215 5723 9056 5310 -155 -42 -284 N ATOM 1499 CA ALA A 215 -2.427 28.857 41.436 1.00 58.23 C ANISOU 1499 CA ALA A 215 6456 9656 6011 -170 -43 -252 C ATOM 1500 C ALA A 215 -1.741 30.219 41.576 1.00 57.98 C ANISOU 1500 C ALA A 215 6447 9575 6006 -108 -80 -234 C ATOM 1501 O ALA A 215 -1.440 30.624 42.701 1.00 53.32 O ANISOU 1501 O ALA A 215 5879 8961 5420 -96 -87 -235 O ATOM 1502 CB ALA A 215 -1.497 27.798 40.909 1.00 50.28 C ANISOU 1502 CB ALA A 215 5481 8600 5023 -216 -31 -221 C ATOM 1503 N ALA A 216 -1.552 30.930 40.468 1.00 53.59 N ANISOU 1503 N ALA A 216 5889 9006 5466 -68 -100 -220 N ATOM 1504 CA ALA A 216 -0.835 32.219 40.543 1.00 52.64 C ANISOU 1504 CA ALA A 216 5799 8827 5373 -17 -128 -201 C ATOM 1505 C ALA A 216 -1.598 33.196 41.445 1.00 60.63 C ANISOU 1505 C ALA A 216 6801 9867 6367 29 -142 -232 C ATOM 1506 O ALA A 216 -0.954 33.888 42.238 1.00 59.36 O ANISOU 1506 O ALA A 216 6671 9656 6227 46 -157 -226 O ATOM 1507 CB ALA A 216 -0.643 32.772 39.177 1.00 52.93 C ANISOU 1507 CB ALA A 216 5841 8848 5421 15 -140 -181 C ATOM 1508 N PHE A 217 -2.925 33.225 41.370 1.00 65.91 N ANISOU 1508 N PHE A 217 7424 10618 6998 48 -137 -269 N ATOM 1509 CA PHE A 217 -3.738 34.151 42.198 1.00 57.16 C ANISOU 1509 CA PHE A 217 6301 9546 5868 100 -150 -303 C ATOM 1510 C PHE A 217 -3.735 33.650 43.635 1.00 55.40 C ANISOU 1510 C PHE A 217 6081 9330 5636 61 -133 -317 C ATOM 1511 O PHE A 217 -3.621 34.485 44.552 1.00 54.12 O ANISOU 1511 O PHE A 217 5938 9148 5477 97 -149 -327 O ATOM 1512 CB PHE A 217 -5.160 34.262 41.661 1.00 71.80 C ANISOU 1512 CB PHE A 217 8099 11499 7683 134 -150 -344 C ATOM 1513 CG PHE A 217 -5.995 35.318 42.337 1.00 85.56 C ANISOU 1513 CG PHE A 217 9825 13282 9401 201 -168 -381 C ATOM 1514 CD1 PHE A 217 -5.785 36.665 42.073 1.00 87.53 C ANISOU 1514 CD1 PHE A 217 10108 13487 9660 279 -201 -371 C ATOM 1515 CD2 PHE A 217 -6.981 34.959 43.247 1.00 97.27 C ANISOU 1515 CD2 PHE A 217 11261 14845 10849 185 -150 -427 C ATOM 1516 CE1 PHE A 217 -6.561 37.631 42.694 1.00100.75 C ANISOU 1516 CE1 PHE A 217 11772 15196 11310 347 -219 -407 C ATOM 1517 CE2 PHE A 217 -7.750 35.928 43.875 1.00 99.97 C ANISOU 1517 CE2 PHE A 217 11585 15230 11167 251 -167 -465 C ATOM 1518 CZ PHE A 217 -7.544 37.261 43.589 1.00105.36 C ANISOU 1518 CZ PHE A 217 12304 15868 11860 336 -204 -456 C ATOM 1519 N VAL A 218 -3.834 32.330 43.821 1.00 53.35 N ANISOU 1519 N VAL A 218 5811 9094 5364 -7 -100 -318 N ATOM 1520 CA VAL A 218 -3.794 31.740 45.195 1.00 49.02 C ANISOU 1520 CA VAL A 218 5277 8546 4799 -45 -79 -327 C ATOM 1521 C VAL A 218 -2.514 32.229 45.881 1.00 48.13 C ANISOU 1521 C VAL A 218 5218 8349 4718 -29 -102 -299 C ATOM 1522 O VAL A 218 -2.655 32.837 46.936 1.00 60.09 O ANISOU 1522 O VAL A 218 6739 9868 6222 -2 -111 -317 O ATOM 1523 CB VAL A 218 -3.896 30.201 45.162 1.00 55.80 C ANISOU 1523 CB VAL A 218 6136 9422 5643 -125 -38 -322 C ATOM 1524 CG1 VAL A 218 -3.380 29.560 46.446 1.00 55.09 C ANISOU 1524 CG1 VAL A 218 6090 9298 5544 -160 -19 -311 C ATOM 1525 CG2 VAL A 218 -5.313 29.723 44.857 1.00 53.57 C ANISOU 1525 CG2 VAL A 218 5793 9236 5324 -151 -9 -365 C ATOM 1526 N VAL A 219 -1.328 32.021 45.280 1.00 50.19 N ANISOU 1526 N VAL A 219 5512 8543 5016 -43 -112 -262 N ATOM 1527 CA VAL A 219 -0.015 32.372 45.912 1.00 52.49 C ANISOU 1527 CA VAL A 219 5846 8758 5337 -35 -133 -242 C ATOM 1528 C VAL A 219 0.148 33.894 45.965 1.00 51.63 C ANISOU 1528 C VAL A 219 5745 8621 5250 23 -165 -250 C ATOM 1529 O VAL A 219 0.870 34.366 46.823 1.00 67.60 O ANISOU 1529 O VAL A 219 7793 10603 7288 35 -182 -252 O ATOM 1530 CB VAL A 219 1.226 31.706 45.273 1.00 54.40 C ANISOU 1530 CB VAL A 219 6114 8943 5611 -66 -133 -207 C ATOM 1531 CG1 VAL A 219 1.234 30.191 45.484 1.00 61.46 C ANISOU 1531 CG1 VAL A 219 7019 9849 6483 -121 -103 -198 C ATOM 1532 CG2 VAL A 219 1.401 32.054 43.807 1.00 65.73 C ANISOU 1532 CG2 VAL A 219 7539 10364 7069 -55 -139 -188 C ATOM 1533 N CYS A 220 -0.526 34.649 45.116 1.00 55.83 N ANISOU 1533 N CYS A 220 6258 9175 5780 62 -173 -257 N ATOM 1534 CA CYS A 220 -0.373 36.126 45.152 1.00 51.97 C ANISOU 1534 CA CYS A 220 5788 8647 5308 120 -202 -263 C ATOM 1535 C CYS A 220 -1.196 36.689 46.298 1.00 53.93 C ANISOU 1535 C CYS A 220 6025 8936 5528 156 -209 -302 C ATOM 1536 O CYS A 220 -0.734 37.636 46.923 1.00 53.59 O ANISOU 1536 O CYS A 220 6010 8848 5503 186 -230 -310 O ATOM 1537 CB CYS A 220 -0.765 36.761 43.829 1.00 52.00 C ANISOU 1537 CB CYS A 220 5788 8654 5314 159 -209 -253 C ATOM 1538 SG CYS A 220 0.571 36.506 42.646 1.00 56.67 S ANISOU 1538 SG CYS A 220 6409 9173 5949 126 -206 -205 S ATOM 1539 N PHE A 221 -2.371 36.123 46.548 1.00 57.30 N ANISOU 1539 N PHE A 221 6411 9446 5912 149 -189 -329 N ATOM 1540 CA PHE A 221 -3.290 36.598 47.615 1.00 55.80 C ANISOU 1540 CA PHE A 221 6202 9310 5689 183 -191 -370 C ATOM 1541 C PHE A 221 -2.739 36.200 48.993 1.00 58.64 C ANISOU 1541 C PHE A 221 6585 9650 6045 154 -185 -373 C ATOM 1542 O PHE A 221 -2.765 37.043 49.913 1.00 66.59 O ANISOU 1542 O PHE A 221 7603 10648 7046 194 -203 -396 O ATOM 1543 CB PHE A 221 -4.689 36.044 47.353 1.00 60.25 C ANISOU 1543 CB PHE A 221 6707 9975 6208 177 -168 -401 C ATOM 1544 CG PHE A 221 -5.737 36.344 48.389 1.00 61.82 C ANISOU 1544 CG PHE A 221 6875 10247 6366 204 -161 -449 C ATOM 1545 CD1 PHE A 221 -6.451 37.530 48.347 1.00 65.36 C ANISOU 1545 CD1 PHE A 221 7307 10724 6800 283 -187 -480 C ATOM 1546 CD2 PHE A 221 -6.025 35.427 49.387 1.00 69.92 C ANISOU 1546 CD2 PHE A 221 7889 11312 7363 151 -128 -462 C ATOM 1547 CE1 PHE A 221 -7.416 37.807 49.305 1.00 75.66 C ANISOU 1547 CE1 PHE A 221 8579 12100 8065 311 -181 -528 C ATOM 1548 CE2 PHE A 221 -6.979 35.708 50.353 1.00 70.45 C ANISOU 1548 CE2 PHE A 221 7926 11449 7390 173 -118 -506 C ATOM 1549 CZ PHE A 221 -7.687 36.890 50.297 1.00 71.97 C ANISOU 1549 CZ PHE A 221 8096 11678 7571 253 -145 -541 C ATOM 1550 N THR A 222 -2.297 34.947 49.150 1.00 49.90 N ANISOU 1550 N THR A 222 5486 8538 4934 91 -160 -352 N ATOM 1551 CA THR A 222 -1.810 34.434 50.457 1.00 48.52 C ANISOU 1551 CA THR A 222 5339 8349 4746 68 -153 -353 C ATOM 1552 C THR A 222 -0.534 35.187 50.857 1.00 53.48 C ANISOU 1552 C THR A 222 6007 8900 5412 92 -188 -343 C ATOM 1553 O THR A 222 -0.526 35.777 51.922 1.00 62.97 O ANISOU 1553 O THR A 222 7220 10102 6603 121 -202 -367 O ATOM 1554 CB THR A 222 -1.558 32.922 50.408 1.00 51.78 C ANISOU 1554 CB THR A 222 5764 8763 5146 1 -119 -329 C ATOM 1555 OG1 THR A 222 -0.577 32.660 49.395 1.00 43.83 O ANISOU 1555 OG1 THR A 222 4773 7700 4179 -14 -130 -295 O ATOM 1556 CG2 THR A 222 -2.819 32.119 50.154 1.00 48.80 C ANISOU 1556 CG2 THR A 222 5347 8462 4729 -34 -78 -346 C ATOM 1557 N TYR A 223 0.506 35.186 50.023 1.00 58.33 N ANISOU 1557 N TYR A 223 6639 9454 6069 79 -201 -314 N ATOM 1558 CA TYR A 223 1.785 35.860 50.371 1.00 54.32 C ANISOU 1558 CA TYR A 223 6162 8876 5600 93 -231 -310 C ATOM 1559 C TYR A 223 1.612 37.385 50.479 1.00 54.92 C ANISOU 1559 C TYR A 223 6242 8930 5692 146 -258 -334 C ATOM 1560 O TYR A 223 2.340 37.973 51.284 1.00 69.33 O ANISOU 1560 O TYR A 223 8089 10717 7534 159 -280 -350 O ATOM 1561 CB TYR A 223 2.907 35.411 49.426 1.00 43.98 C ANISOU 1561 CB TYR A 223 4864 7516 4330 61 -232 -277 C ATOM 1562 CG TYR A 223 3.370 34.012 49.750 1.00 43.85 C ANISOU 1562 CG TYR A 223 4858 7505 4297 20 -215 -260 C ATOM 1563 CD1 TYR A 223 3.980 33.731 50.960 1.00 44.53 C ANISOU 1563 CD1 TYR A 223 4967 7581 4370 22 -226 -270 C ATOM 1564 CD2 TYR A 223 3.154 32.953 48.881 1.00 45.88 C ANISOU 1564 CD2 TYR A 223 5107 7778 4546 -16 -189 -236 C ATOM 1565 CE1 TYR A 223 4.361 32.443 51.293 1.00 43.94 C ANISOU 1565 CE1 TYR A 223 4913 7508 4273 -6 -210 -253 C ATOM 1566 CE2 TYR A 223 3.561 31.659 49.179 1.00 47.29 C ANISOU 1566 CE2 TYR A 223 5306 7954 4707 -50 -173 -221 C ATOM 1567 CZ TYR A 223 4.154 31.406 50.402 1.00 49.91 C ANISOU 1567 CZ TYR A 223 5666 8273 5023 -43 -183 -228 C ATOM 1568 OH TYR A 223 4.527 30.141 50.749 1.00 56.82 O ANISOU 1568 OH TYR A 223 6572 9142 5874 -68 -167 -211 O ATOM 1569 N PHE A 224 0.694 38.016 49.759 1.00 53.24 N ANISOU 1569 N PHE A 224 6013 8741 5473 179 -257 -341 N ATOM 1570 CA PHE A 224 0.398 39.459 49.955 1.00 54.25 C ANISOU 1570 CA PHE A 224 6155 8849 5608 238 -281 -366 C ATOM 1571 C PHE A 224 -0.104 39.686 51.386 1.00 66.72 C ANISOU 1571 C PHE A 224 7729 10464 7154 263 -287 -405 C ATOM 1572 O PHE A 224 0.453 40.553 52.089 1.00 88.13 O ANISOU 1572 O PHE A 224 10468 13132 9885 287 -312 -425 O ATOM 1573 CB PHE A 224 -0.653 39.992 48.976 1.00 59.54 C ANISOU 1573 CB PHE A 224 6809 9550 6263 281 -280 -369 C ATOM 1574 CG PHE A 224 -1.007 41.438 49.217 1.00 65.60 C ANISOU 1574 CG PHE A 224 7599 10295 7032 350 -304 -395 C ATOM 1575 CD1 PHE A 224 -0.117 42.463 48.911 1.00 71.05 C ANISOU 1575 CD1 PHE A 224 8336 10894 7764 364 -323 -385 C ATOM 1576 CD2 PHE A 224 -2.215 41.779 49.787 1.00 73.60 C ANISOU 1576 CD2 PHE A 224 8587 11376 8002 399 -307 -434 C ATOM 1577 CE1 PHE A 224 -0.436 43.795 49.149 1.00 69.76 C ANISOU 1577 CE1 PHE A 224 8203 10700 7601 427 -344 -409 C ATOM 1578 CE2 PHE A 224 -2.535 43.108 50.031 1.00 87.90 C ANISOU 1578 CE2 PHE A 224 10423 13162 9811 469 -332 -460 C ATOM 1579 CZ PHE A 224 -1.646 44.114 49.715 1.00 82.82 C ANISOU 1579 CZ PHE A 224 9836 12421 9211 484 -350 -447 C ATOM 1580 N HIS A 225 -1.129 38.943 51.811 1.00 58.03 N ANISOU 1580 N HIS A 225 6597 9445 6007 255 -264 -419 N ATOM 1581 CA HIS A 225 -1.798 39.133 53.127 1.00 60.14 C ANISOU 1581 CA HIS A 225 6855 9761 6233 281 -263 -458 C ATOM 1582 C HIS A 225 -0.922 38.630 54.283 1.00 62.69 C ANISOU 1582 C HIS A 225 7204 10061 6552 254 -266 -457 C ATOM 1583 O HIS A 225 -0.969 39.263 55.355 1.00 65.94 O ANISOU 1583 O HIS A 225 7626 10476 6949 288 -282 -489 O ATOM 1584 CB HIS A 225 -3.196 38.508 53.129 1.00 58.42 C ANISOU 1584 CB HIS A 225 6591 9641 5964 275 -231 -476 C ATOM 1585 CG HIS A 225 -4.184 39.386 52.450 1.00 63.51 C ANISOU 1585 CG HIS A 225 7207 10321 6599 332 -242 -499 C ATOM 1586 ND1 HIS A 225 -4.692 39.099 51.205 1.00 55.77 N ANISOU 1586 ND1 HIS A 225 6199 9369 5619 327 -232 -487 N ATOM 1587 CD2 HIS A 225 -4.695 40.582 52.819 1.00 71.32 C ANISOU 1587 CD2 HIS A 225 8198 11318 7579 403 -266 -534 C ATOM 1588 CE1 HIS A 225 -5.506 40.078 50.845 1.00 73.30 C ANISOU 1588 CE1 HIS A 225 8404 11618 7826 397 -250 -514 C ATOM 1589 NE2 HIS A 225 -5.522 41.003 51.820 1.00 69.01 N ANISOU 1589 NE2 HIS A 225 7880 11061 7278 445 -271 -542 N ATOM 1590 N ILE A 226 -0.172 37.540 54.099 1.00 57.64 N ANISOU 1590 N ILE A 226 6577 9401 5921 201 -252 -424 N ATOM 1591 CA ILE A 226 0.760 36.994 55.138 1.00 53.14 C ANISOU 1591 CA ILE A 226 6037 8808 5345 184 -258 -421 C ATOM 1592 C ILE A 226 1.808 38.064 55.505 1.00 46.49 C ANISOU 1592 C ILE A 226 5217 7903 4542 213 -300 -439 C ATOM 1593 O ILE A 226 1.989 38.327 56.688 1.00 61.58 O ANISOU 1593 O ILE A 226 7142 9820 6435 235 -315 -466 O ATOM 1594 CB ILE A 226 1.383 35.660 54.679 1.00 52.09 C ANISOU 1594 CB ILE A 226 5915 8661 5215 130 -238 -383 C ATOM 1595 CG1 ILE A 226 0.352 34.522 54.690 1.00 56.17 C ANISOU 1595 CG1 ILE A 226 6417 9239 5683 94 -192 -374 C ATOM 1596 CG2 ILE A 226 2.579 35.328 55.547 1.00 50.07 C ANISOU 1596 CG2 ILE A 226 5693 8369 4962 128 -257 -380 C ATOM 1597 CD1 ILE A 226 0.805 33.265 53.984 1.00 54.72 C ANISOU 1597 CD1 ILE A 226 6246 9038 5506 43 -169 -337 C ATOM 1598 N PHE A 227 2.385 38.742 54.521 1.00 57.14 N ANISOU 1598 N PHE A 227 6570 9198 5943 214 -316 -428 N ATOM 1599 CA PHE A 227 3.384 39.821 54.740 1.00 60.95 C ANISOU 1599 CA PHE A 227 7073 9615 6469 231 -350 -447 C ATOM 1600 C PHE A 227 2.672 41.113 55.164 1.00 61.17 C ANISOU 1600 C PHE A 227 7106 9644 6491 285 -366 -485 C ATOM 1601 O PHE A 227 3.332 41.988 55.737 1.00 62.13 O ANISOU 1601 O PHE A 227 7248 9721 6636 302 -394 -514 O ATOM 1602 CB PHE A 227 4.272 39.982 53.495 1.00 57.02 C ANISOU 1602 CB PHE A 227 6581 9057 6026 204 -352 -419 C ATOM 1603 CG PHE A 227 5.115 38.765 53.200 1.00 59.44 C ANISOU 1603 CG PHE A 227 6883 9360 6339 158 -341 -390 C ATOM 1604 CD1 PHE A 227 5.728 38.052 54.222 1.00 63.38 C ANISOU 1604 CD1 PHE A 227 7390 9872 6819 150 -350 -399 C ATOM 1605 CD2 PHE A 227 5.304 38.323 51.901 1.00 74.41 C ANISOU 1605 CD2 PHE A 227 8772 11241 8256 128 -324 -353 C ATOM 1606 CE1 PHE A 227 6.490 36.922 53.964 1.00 63.71 C ANISOU 1606 CE1 PHE A 227 7434 9910 6862 117 -342 -373 C ATOM 1607 CE2 PHE A 227 6.070 37.194 51.640 1.00 72.22 C ANISOU 1607 CE2 PHE A 227 8493 10961 7983 91 -315 -329 C ATOM 1608 CZ PHE A 227 6.659 36.496 52.672 1.00 70.35 C ANISOU 1608 CZ PHE A 227 8266 10735 7727 87 -325 -339 C ATOM 1609 N LYS A 228 1.371 41.244 54.894 1.00 65.98 N ANISOU 1609 N LYS A 228 7697 10304 7068 313 -351 -489 N ATOM 1610 CA LYS A 228 0.593 42.429 55.351 1.00 67.36 C ANISOU 1610 CA LYS A 228 7876 10488 7228 374 -367 -529 C ATOM 1611 C LYS A 228 0.461 42.380 56.887 1.00 74.82 C ANISOU 1611 C LYS A 228 8821 11469 8135 391 -375 -566 C ATOM 1612 O LYS A 228 0.630 43.439 57.537 1.00 64.84 O ANISOU 1612 O LYS A 228 7578 10176 6881 431 -403 -603 O ATOM 1613 CB LYS A 228 -0.757 42.465 54.639 1.00 66.14 C ANISOU 1613 CB LYS A 228 7693 10391 7044 403 -350 -528 C ATOM 1614 CG LYS A 228 -1.387 43.847 54.519 1.00 80.89 C ANISOU 1614 CG LYS A 228 9575 12245 8912 474 -371 -557 C ATOM 1615 CD LYS A 228 -2.668 43.859 53.688 1.00101.01 C ANISOU 1615 CD LYS A 228 12092 14857 11430 510 -358 -558 C ATOM 1616 CE LYS A 228 -3.935 43.741 54.518 1.00 89.92 C ANISOU 1616 CE LYS A 228 10646 13551 9967 544 -348 -599 C ATOM 1617 NZ LYS A 228 -5.147 43.749 53.669 1.00104.52 N ANISOU 1617 NZ LYS A 228 12456 15470 11787 580 -339 -607 N ATOM 1618 N ILE A 229 0.208 41.175 57.425 1.00 74.51 N ANISOU 1618 N ILE A 229 8767 11487 8056 361 -350 -555 N ATOM 1619 CA ILE A 229 -0.009 40.864 58.877 1.00 75.47 C ANISOU 1619 CA ILE A 229 8891 11655 8128 372 -348 -582 C ATOM 1620 C ILE A 229 1.338 40.932 59.619 1.00 76.95 C ANISOU 1620 C ILE A 229 9108 11790 8336 366 -377 -591 C ATOM 1621 O ILE A 229 1.395 41.501 60.748 1.00 77.37 O ANISOU 1621 O ILE A 229 9174 11851 8371 401 -398 -631 O ATOM 1622 CB ILE A 229 -0.675 39.470 59.039 1.00 68.97 C ANISOU 1622 CB ILE A 229 8051 10899 7254 333 -303 -561 C ATOM 1623 CG1 ILE A 229 -2.151 39.495 58.653 1.00 72.91 C ANISOU 1623 CG1 ILE A 229 8510 11471 7721 345 -275 -573 C ATOM 1624 CG2 ILE A 229 -0.502 38.907 60.441 1.00 80.10 C ANISOU 1624 CG2 ILE A 229 9481 12336 8617 331 -297 -572 C ATOM 1625 CD1 ILE A 229 -2.738 38.133 58.367 1.00 77.47 C ANISOU 1625 CD1 ILE A 229 9067 12102 8266 289 -227 -548 C ATOM 1626 N CYS A 230 2.376 40.345 59.026 1.00 66.01 N ANISOU 1626 N CYS A 230 7732 10362 6985 325 -379 -559 N ATOM 1627 CA CYS A 230 3.722 40.215 59.640 1.00 65.61 C ANISOU 1627 CA CYS A 230 7701 10274 6953 316 -407 -568 C ATOM 1628 C CYS A 230 4.369 41.602 59.798 1.00 60.46 C ANISOU 1628 C CYS A 230 7059 9566 6346 341 -446 -608 C ATOM 1629 O CYS A 230 5.009 41.843 60.837 1.00 58.73 O ANISOU 1629 O CYS A 230 6851 9341 6120 357 -473 -643 O ATOM 1630 CB CYS A 230 4.572 39.237 58.835 1.00 60.83 C ANISOU 1630 CB CYS A 230 7096 9643 6371 269 -397 -526 C ATOM 1631 SG CYS A 230 4.086 37.503 59.104 1.00 68.26 S ANISOU 1631 SG CYS A 230 8044 10639 7250 240 -356 -489 S ATOM 1632 N ARG A 231 4.164 42.493 58.826 1.00 67.46 N ANISOU 1632 N ARG A 231 7945 10412 7273 345 -446 -604 N ATOM 1633 CA ARG A 231 4.728 43.877 58.808 1.00 82.13 C ANISOU 1633 CA ARG A 231 9822 12203 9179 362 -476 -639 C ATOM 1634 C ARG A 231 4.344 44.644 60.088 1.00 82.53 C ANISOU 1634 C ARG A 231 9884 12272 9201 411 -499 -694 C ATOM 1635 O ARG A 231 5.089 45.554 60.462 1.00 97.75 O ANISOU 1635 O ARG A 231 11829 14148 11163 417 -527 -733 O ATOM 1636 CB ARG A 231 4.251 44.609 57.546 1.00 99.59 C ANISOU 1636 CB ARG A 231 12042 14376 11420 369 -464 -619 C ATOM 1637 CG ARG A 231 5.014 45.874 57.168 1.00 98.92 C ANISOU 1637 CG ARG A 231 11988 14203 11394 367 -483 -639 C ATOM 1638 CD ARG A 231 4.630 46.371 55.770 1.00114.77 C ANISOU 1638 CD ARG A 231 14011 16169 13424 370 -465 -604 C ATOM 1639 NE ARG A 231 3.183 46.503 55.587 1.00126.43 N ANISOU 1639 NE ARG A 231 15482 17696 14857 423 -455 -601 N ATOM 1640 CZ ARG A 231 2.438 47.545 55.975 1.00125.52 C ANISOU 1640 CZ ARG A 231 15388 17575 14727 483 -469 -635 C ATOM 1641 NH1 ARG A 231 2.994 48.592 56.566 1.00131.54 N ANISOU 1641 NH1 ARG A 231 16186 18277 15516 497 -493 -675 N ATOM 1642 NH2 ARG A 231 1.130 47.527 55.778 1.00109.14 N ANISOU 1642 NH2 ARG A 231 13298 15561 12609 532 -460 -634 N ATOM 1643 N GLN A 232 3.221 44.312 60.729 1.00 83.22 N ANISOU 1643 N GLN A 232 9960 12430 9228 443 -484 -701 N ATOM 1644 CA GLN A 232 2.816 44.953 62.011 1.00 98.78 C ANISOU 1644 CA GLN A 232 11939 14428 11164 493 -504 -754 C ATOM 1645 C GLN A 232 3.586 44.292 63.163 1.00101.94 C ANISOU 1645 C GLN A 232 12344 14851 11538 484 -518 -769 C ATOM 1646 O GLN A 232 4.263 45.029 63.909 1.00102.57 O ANISOU 1646 O GLN A 232 12436 14901 11632 503 -553 -816 O ATOM 1647 CB GLN A 232 1.300 44.872 62.217 1.00109.74 C ANISOU 1647 CB GLN A 232 13309 15890 12496 530 -480 -758 C ATOM 1648 CG GLN A 232 0.511 45.871 61.370 1.00107.92 C ANISOU 1648 CG GLN A 232 13080 15640 12284 567 -480 -764 C ATOM 1649 CD GLN A 232 -0.283 45.217 60.265 1.00113.50 C ANISOU 1649 CD GLN A 232 13759 16383 12980 550 -447 -721 C ATOM 1650 OE1 GLN A 232 -1.027 44.266 60.506 1.00105.38 O ANISOU 1650 OE1 GLN A 232 12701 15432 11903 537 -417 -710 O ATOM 1651 NE2 GLN A 232 -0.136 45.730 59.046 1.00107.75 N ANISOU 1651 NE2 GLN A 232 13043 15601 12296 548 -449 -699 N ATOM 1652 N HIS A 233 3.510 42.958 63.262 1.00 99.70 N ANISOU 1652 N HIS A 233 12052 14613 11216 458 -493 -732 N ATOM 1653 CA HIS A 233 4.165 42.138 64.319 1.00 95.33 C ANISOU 1653 CA HIS A 233 11511 14086 10625 456 -502 -738 C ATOM 1654 C HIS A 233 5.675 41.983 64.061 1.00 87.53 C ANISOU 1654 C HIS A 233 10526 13046 9684 429 -530 -737 C ATOM 1655 O HIS A 233 6.030 41.008 63.388 1.00 82.45 O ANISOU 1655 O HIS A 233 9880 12399 9048 392 -512 -692 O ATOM 1656 CB HIS A 233 3.505 40.751 64.375 1.00 88.03 C ANISOU 1656 CB HIS A 233 10585 13217 9642 435 -458 -694 C ATOM 1657 CG HIS A 233 2.036 40.773 64.637 1.00111.29 C ANISOU 1657 CG HIS A 233 13520 16226 12539 453 -425 -699 C ATOM 1658 ND1 HIS A 233 1.119 41.153 63.664 1.00128.64 N ANISOU 1658 ND1 HIS A 233 15691 18430 14754 451 -405 -689 N ATOM 1659 CD2 HIS A 233 1.318 40.432 65.731 1.00106.86 C ANISOU 1659 CD2 HIS A 233 12966 15728 11908 475 -406 -713 C ATOM 1660 CE1 HIS A 233 -0.101 41.054 64.154 1.00127.93 C ANISOU 1660 CE1 HIS A 233 15586 18411 14610 469 -377 -703 C ATOM 1661 NE2 HIS A 233 -0.006 40.612 65.423 1.00118.24 N ANISOU 1661 NE2 HIS A 233 14380 17218 13329 481 -374 -717 N ATOM 1662 N THR A 234 6.527 42.851 64.629 1.00 92.63 N ANISOU 1662 N THR A 234 11177 13660 10358 446 -572 -788 N ATOM 1663 CA THR A 234 8.006 42.865 64.399 1.00107.92 C ANISOU 1663 CA THR A 234 13107 15553 12344 418 -601 -802 C ATOM 1664 C THR A 234 8.721 41.900 65.364 1.00 82.40 C ANISOU 1664 C THR A 234 9880 12360 9065 432 -619 -809 C ATOM 1665 O THR A 234 9.313 42.380 66.337 1.00 71.30 O ANISOU 1665 O THR A 234 8477 10960 7653 461 -658 -864 O ATOM 1666 CB THR A 234 8.596 44.287 64.466 1.00122.70 C ANISOU 1666 CB THR A 234 14977 17369 14271 421 -634 -859 C ATOM 1667 OG1 THR A 234 8.283 44.899 65.716 1.00133.21 O ANISOU 1667 OG1 THR A 234 16319 18725 15567 469 -659 -914 O ATOM 1668 CG2 THR A 234 8.102 45.194 63.359 1.00119.46 C ANISOU 1668 CG2 THR A 234 14572 16905 13911 406 -617 -845 C ATOM 1669 N LYS A 235 8.737 40.606 65.022 1.00 77.33 N ANISOU 1669 N LYS A 235 9245 11740 8398 413 -594 -756 N ATOM 1670 CA LYS A 235 9.411 39.514 65.777 1.00 78.31 C ANISOU 1670 CA LYS A 235 9386 11895 8472 430 -606 -750 C ATOM 1671 C LYS A 235 10.947 39.687 65.771 1.00 73.51 C ANISOU 1671 C LYS A 235 8759 11264 7907 426 -651 -786 C ATOM 1672 O LYS A 235 11.508 40.125 64.757 1.00 78.97 O ANISOU 1672 O LYS A 235 9424 11910 8668 387 -653 -786 O ATOM 1673 CB LYS A 235 8.999 38.166 65.169 1.00 76.80 C ANISOU 1673 CB LYS A 235 9209 11717 8252 404 -562 -681 C ATOM 1674 CG LYS A 235 9.171 36.971 66.098 1.00 97.01 C ANISOU 1674 CG LYS A 235 11807 14314 10735 431 -559 -665 C ATOM 1675 CD LYS A 235 9.259 35.637 65.388 1.00107.36 C ANISOU 1675 CD LYS A 235 13137 15619 12035 400 -526 -605 C ATOM 1676 CE LYS A 235 9.782 34.527 66.283 1.00108.28 C ANISOU 1676 CE LYS A 235 13301 15758 12083 435 -534 -593 C ATOM 1677 NZ LYS A 235 9.934 33.249 65.549 1.00116.11 N ANISOU 1677 NZ LYS A 235 14316 16734 13066 407 -504 -537 N ATOM 1678 N MET A1001 11.616 39.297 66.861 1.00 68.73 N ANISOU 1678 N MET A1001 7427 11389 7297 452 -279 330 N ATOM 1679 CA MET A1001 13.094 39.376 67.010 1.00 71.49 C ANISOU 1679 CA MET A1001 7931 11497 7734 361 -261 331 C ATOM 1680 C MET A1001 13.747 38.158 66.346 1.00 72.31 C ANISOU 1680 C MET A1001 8003 11627 7845 207 -305 280 C ATOM 1681 O MET A1001 13.243 37.021 66.549 1.00 87.50 O ANISOU 1681 O MET A1001 9837 13654 9753 95 -330 207 O ATOM 1682 CB MET A1001 13.502 39.420 68.484 1.00 80.10 C ANISOU 1682 CB MET A1001 9097 12434 8903 287 -226 290 C ATOM 1683 CG MET A1001 13.448 40.807 69.073 1.00 79.65 C ANISOU 1683 CG MET A1001 9153 12251 8857 413 -156 338 C ATOM 1684 SD MET A1001 14.183 40.852 70.713 1.00 77.74 S ANISOU 1684 SD MET A1001 9004 11836 8694 285 -114 281 S ATOM 1685 CE MET A1001 12.932 40.026 71.698 1.00 73.56 C ANISOU 1685 CE MET A1001 8331 11464 8154 256 -137 217 C ATOM 1686 N LYS A1002 14.852 38.376 65.623 1.00 53.34 N ANISOU 1686 N LYS A1002 5683 9123 5460 192 -304 311 N ATOM 1687 CA LYS A1002 15.489 37.325 64.786 1.00 60.03 C ANISOU 1687 CA LYS A1002 6504 10002 6300 81 -338 269 C ATOM 1688 C LYS A1002 16.357 36.370 65.638 1.00 68.00 C ANISOU 1688 C LYS A1002 7562 10895 7380 -50 -333 207 C ATOM 1689 O LYS A1002 17.201 36.855 66.444 1.00 68.62 O ANISOU 1689 O LYS A1002 7725 10835 7511 -58 -306 223 O ATOM 1690 CB LYS A1002 16.295 37.994 63.667 1.00 59.16 C ANISOU 1690 CB LYS A1002 6455 9855 6167 130 -335 330 C ATOM 1691 N LYS A1003 16.186 35.050 65.456 1.00 61.24 N ANISOU 1691 N LYS A1003 6662 10096 6511 -152 -349 139 N ATOM 1692 CA LYS A1003 17.086 33.989 65.999 1.00 50.90 C ANISOU 1692 CA LYS A1003 5414 8676 5248 -247 -338 93 C ATOM 1693 C LYS A1003 18.430 34.014 65.251 1.00 49.26 C ANISOU 1693 C LYS A1003 5258 8407 5050 -238 -338 112 C ATOM 1694 O LYS A1003 18.450 34.439 64.084 1.00 58.78 O ANISOU 1694 O LYS A1003 6440 9679 6214 -203 -352 136 O ATOM 1695 CB LYS A1003 16.443 32.604 65.852 1.00 48.44 C ANISOU 1695 CB LYS A1003 5076 8424 4902 -355 -334 16 C ATOM 1696 CG LYS A1003 15.162 32.407 66.629 1.00 56.99 C ANISOU 1696 CG LYS A1003 6101 9591 5959 -401 -329 -17 C ATOM 1697 CD LYS A1003 14.494 31.074 66.355 1.00 78.10 C ANISOU 1697 CD LYS A1003 8763 12336 8576 -546 -311 -105 C ATOM 1698 CE LYS A1003 14.655 30.101 67.500 1.00 95.65 C ANISOU 1698 CE LYS A1003 11079 14428 10834 -639 -273 -140 C ATOM 1699 NZ LYS A1003 14.335 28.718 67.079 1.00108.97 N ANISOU 1699 NZ LYS A1003 12821 16118 12464 -792 -232 -227 N ATOM 1700 N TYR A1004 19.520 33.578 65.889 1.00 48.89 N ANISOU 1700 N TYR A1004 5268 8261 5043 -264 -323 106 N ATOM 1701 CA TYR A1004 20.852 33.497 65.235 1.00 41.33 C ANISOU 1701 CA TYR A1004 4340 7281 4080 -255 -321 116 C ATOM 1702 C TYR A1004 21.490 32.161 65.558 1.00 41.99 C ANISOU 1702 C TYR A1004 4461 7317 4174 -279 -304 78 C ATOM 1703 O TYR A1004 21.283 31.644 66.649 1.00 56.03 O ANISOU 1703 O TYR A1004 6266 9044 5978 -297 -290 70 O ATOM 1704 CB TYR A1004 21.768 34.609 65.706 1.00 41.00 C ANISOU 1704 CB TYR A1004 4327 7199 4051 -236 -310 163 C ATOM 1705 CG TYR A1004 21.482 35.943 65.087 1.00 42.78 C ANISOU 1705 CG TYR A1004 4563 7436 4251 -199 -307 210 C ATOM 1706 CD1 TYR A1004 20.392 36.692 65.470 1.00 49.62 C ANISOU 1706 CD1 TYR A1004 5432 8298 5122 -154 -299 234 C ATOM 1707 CD2 TYR A1004 22.340 36.486 64.154 1.00 55.84 C ANISOU 1707 CD2 TYR A1004 6240 9106 5871 -201 -302 236 C ATOM 1708 CE1 TYR A1004 20.143 37.940 64.924 1.00 52.91 C ANISOU 1708 CE1 TYR A1004 5889 8705 5508 -89 -280 292 C ATOM 1709 CE2 TYR A1004 22.103 37.728 63.585 1.00 63.64 C ANISOU 1709 CE2 TYR A1004 7271 10080 6827 -163 -285 291 C ATOM 1710 CZ TYR A1004 20.996 38.461 63.973 1.00 60.94 C ANISOU 1710 CZ TYR A1004 6949 9714 6490 -96 -271 324 C ATOM 1711 OH TYR A1004 20.740 39.686 63.425 1.00 73.86 O ANISOU 1711 OH TYR A1004 8655 11320 8089 -26 -241 392 O ATOM 1712 N THR A1005 22.226 31.605 64.622 1.00 39.45 N ANISOU 1712 N THR A1005 4151 7009 3828 -270 -299 60 N ATOM 1713 CA THR A1005 22.778 30.263 64.863 1.00 42.64 C ANISOU 1713 CA THR A1005 4615 7352 4233 -262 -266 27 C ATOM 1714 C THR A1005 24.298 30.386 64.882 1.00 53.51 C ANISOU 1714 C THR A1005 5987 8743 5599 -196 -262 58 C ATOM 1715 O THR A1005 24.837 31.380 64.362 1.00 56.87 O ANISOU 1715 O THR A1005 6367 9235 6006 -194 -281 84 O ATOM 1716 CB THR A1005 22.176 29.270 63.870 1.00 48.22 C ANISOU 1716 CB THR A1005 5351 8063 4906 -312 -244 -40 C ATOM 1717 OG1 THR A1005 22.820 28.014 64.059 1.00 53.90 O ANISOU 1717 OG1 THR A1005 6166 8690 5622 -285 -194 -66 O ATOM 1718 CG2 THR A1005 22.321 29.726 62.432 1.00 51.31 C ANISOU 1718 CG2 THR A1005 5690 8547 5255 -314 -265 -49 C ATOM 1719 N CYS A1006 24.946 29.457 65.569 1.00 56.01 N ANISOU 1719 N CYS A1006 6352 9013 5916 -143 -232 63 N ATOM 1720 CA CYS A1006 26.414 29.384 65.609 1.00 54.28 C ANISOU 1720 CA CYS A1006 6108 8852 5663 -59 -224 91 C ATOM 1721 C CYS A1006 26.849 28.636 64.373 1.00 55.85 C ANISOU 1721 C CYS A1006 6332 9059 5829 -18 -199 51 C ATOM 1722 O CYS A1006 26.344 27.544 64.183 1.00 65.19 O ANISOU 1722 O CYS A1006 7606 10147 7016 -15 -159 10 O ATOM 1723 CB CYS A1006 26.895 28.660 66.843 1.00 65.35 C ANISOU 1723 CB CYS A1006 7546 10222 7061 14 -200 125 C ATOM 1724 SG CYS A1006 28.649 28.305 66.734 1.00 73.92 S ANISOU 1724 SG CYS A1006 8582 11427 8074 152 -184 157 S ATOM 1725 N THR A1007 27.707 29.245 63.560 1.00 58.67 N ANISOU 1725 N THR A1007 6619 9523 6147 -7 -215 56 N ATOM 1726 CA THR A1007 28.223 28.624 62.315 1.00 56.05 C ANISOU 1726 CA THR A1007 6298 9222 5774 32 -191 14 C ATOM 1727 C THR A1007 29.142 27.439 62.628 1.00 58.23 C ANISOU 1727 C THR A1007 6625 9478 6022 171 -139 14 C ATOM 1728 O THR A1007 29.314 26.602 61.707 1.00 57.17 O ANISOU 1728 O THR A1007 6545 9313 5861 214 -96 -35 O ATOM 1729 CB THR A1007 28.899 29.675 61.438 1.00 58.34 C ANISOU 1729 CB THR A1007 6498 9646 6021 -2 -220 24 C ATOM 1730 OG1 THR A1007 29.956 30.247 62.199 1.00 66.46 O ANISOU 1730 OG1 THR A1007 7460 10773 7019 22 -228 67 O ATOM 1731 CG2 THR A1007 27.924 30.744 60.991 1.00 67.03 C ANISOU 1731 CG2 THR A1007 7582 10744 7140 -104 -256 34 C ATOM 1732 N VAL A1008 29.688 27.348 63.855 1.00 53.57 N ANISOU 1732 N VAL A1008 6022 8907 5426 248 -136 70 N ATOM 1733 CA VAL A1008 30.656 26.267 64.220 1.00 56.32 C ANISOU 1733 CA VAL A1008 6410 9261 5727 427 -85 94 C ATOM 1734 C VAL A1008 29.910 25.023 64.743 1.00 53.98 C ANISOU 1734 C VAL A1008 6287 8759 5463 471 -23 88 C ATOM 1735 O VAL A1008 30.136 23.927 64.210 1.00 61.79 O ANISOU 1735 O VAL A1008 7392 9657 6428 568 48 59 O ATOM 1736 CB VAL A1008 31.729 26.768 65.204 1.00 67.28 C ANISOU 1736 CB VAL A1008 7679 10822 7060 499 -110 163 C ATOM 1737 CG1 VAL A1008 32.783 25.704 65.469 1.00 64.04 C ANISOU 1737 CG1 VAL A1008 7286 10466 6580 722 -59 201 C ATOM 1738 CG2 VAL A1008 32.399 28.060 64.745 1.00 66.80 C ANISOU 1738 CG2 VAL A1008 7469 10955 6956 405 -157 157 C ATOM 1739 N CYS A1009 29.035 25.160 65.740 1.00 70.43 N ANISOU 1739 N CYS A1009 8405 10761 7592 394 -38 110 N ATOM 1740 CA CYS A1009 28.419 23.988 66.440 1.00 78.29 C ANISOU 1740 CA CYS A1009 9574 11568 8602 425 28 115 C ATOM 1741 C CYS A1009 26.896 23.959 66.244 1.00 67.86 C ANISOU 1741 C CYS A1009 8320 10133 7329 236 30 49 C ATOM 1742 O CYS A1009 26.333 22.846 66.291 1.00 66.39 O ANISOU 1742 O CYS A1009 8305 9781 7137 216 107 14 O ATOM 1743 CB CYS A1009 28.775 23.984 67.926 1.00 72.96 C ANISOU 1743 CB CYS A1009 8885 10921 7916 508 19 204 C ATOM 1744 SG CYS A1009 28.086 25.388 68.842 1.00 66.10 S ANISOU 1744 SG CYS A1009 7883 10138 7091 345 -64 220 S ATOM 1745 N GLY A1010 26.266 25.125 66.039 1.00 66.47 N ANISOU 1745 N GLY A1010 8021 10050 7182 107 -41 33 N ATOM 1746 CA GLY A1010 24.843 25.206 65.636 1.00 66.91 C ANISOU 1746 CA GLY A1010 8095 10067 7259 -56 -46 -31 C ATOM 1747 C GLY A1010 23.957 25.657 66.775 1.00 63.98 C ANISOU 1747 C GLY A1010 7699 9687 6921 -131 -74 -6 C ATOM 1748 O GLY A1010 22.751 25.425 66.709 1.00 56.46 O ANISOU 1748 O GLY A1010 6778 8703 5969 -254 -63 -58 O ATOM 1749 N TYR A1011 24.561 26.293 67.782 1.00 67.45 N ANISOU 1749 N TYR A1011 8074 10178 7373 -68 -108 63 N ATOM 1750 CA TYR A1011 23.831 26.863 68.941 1.00 65.83 C ANISOU 1750 CA TYR A1011 7834 9978 7197 -132 -134 87 C ATOM 1751 C TYR A1011 22.871 27.936 68.426 1.00 52.56 C ANISOU 1751 C TYR A1011 6064 8369 5536 -230 -180 56 C ATOM 1752 O TYR A1011 23.323 28.830 67.724 1.00 54.95 O ANISOU 1752 O TYR A1011 6291 8751 5834 -211 -212 66 O ATOM 1753 CB TYR A1011 24.794 27.463 69.980 1.00 66.70 C ANISOU 1753 CB TYR A1011 7878 10161 7300 -58 -159 158 C ATOM 1754 CG TYR A1011 24.144 28.397 70.978 1.00 55.84 C ANISOU 1754 CG TYR A1011 6444 8818 5952 -134 -190 171 C ATOM 1755 CD1 TYR A1011 23.463 27.911 72.098 1.00 48.02 C ANISOU 1755 CD1 TYR A1011 5508 7766 4971 -168 -171 181 C ATOM 1756 CD2 TYR A1011 24.211 29.769 70.790 1.00 47.04 C ANISOU 1756 CD2 TYR A1011 5238 7786 4846 -174 -228 171 C ATOM 1757 CE1 TYR A1011 22.866 28.762 73.012 1.00 41.02 C ANISOU 1757 CE1 TYR A1011 4565 6915 4104 -234 -194 185 C ATOM 1758 CE2 TYR A1011 23.592 30.632 71.676 1.00 49.48 C ANISOU 1758 CE2 TYR A1011 5514 8107 5176 -234 -241 175 C ATOM 1759 CZ TYR A1011 22.921 30.126 72.784 1.00 48.01 C ANISOU 1759 CZ TYR A1011 5363 7875 5002 -261 -227 179 C ATOM 1760 OH TYR A1011 22.300 30.982 73.644 1.00 48.06 O ANISOU 1760 OH TYR A1011 5335 7899 5025 -316 -235 175 O ATOM 1761 N ILE A1012 21.612 27.883 68.834 1.00 42.08 N ANISOU 1761 N ILE A1012 4744 7025 4218 -321 -177 27 N ATOM 1762 CA ILE A1012 20.639 28.937 68.453 1.00 46.67 C ANISOU 1762 CA ILE A1012 5230 7698 4804 -376 -217 11 C ATOM 1763 C ILE A1012 20.505 29.930 69.603 1.00 48.82 C ANISOU 1763 C ILE A1012 5454 7990 5105 -365 -239 53 C ATOM 1764 O ILE A1012 20.050 29.547 70.709 1.00 43.81 O ANISOU 1764 O ILE A1012 4847 7319 4479 -400 -223 53 O ATOM 1765 CB ILE A1012 19.268 28.360 68.043 1.00 47.87 C ANISOU 1765 CB ILE A1012 5385 7877 4924 -484 -201 -55 C ATOM 1766 CG1 ILE A1012 19.373 27.149 67.096 1.00 53.25 C ANISOU 1766 CG1 ILE A1012 6153 8512 5566 -530 -155 -116 C ATOM 1767 CG2 ILE A1012 18.435 29.467 67.438 1.00 45.33 C ANISOU 1767 CG2 ILE A1012 4947 7688 4586 -490 -245 -56 C ATOM 1768 CD1 ILE A1012 19.229 25.781 67.768 1.00 57.10 C ANISOU 1768 CD1 ILE A1012 6790 8865 6040 -589 -83 -147 C ATOM 1769 N TYR A1013 20.916 31.166 69.352 1.00 48.69 N ANISOU 1769 N TYR A1013 5381 8022 5096 -328 -265 84 N ATOM 1770 CA TYR A1013 20.554 32.247 70.296 1.00 43.44 C ANISOU 1770 CA TYR A1013 4685 7368 4449 -332 -271 106 C ATOM 1771 C TYR A1013 19.096 32.617 70.037 1.00 49.20 C ANISOU 1771 C TYR A1013 5371 8148 5172 -351 -279 83 C ATOM 1772 O TYR A1013 18.820 33.187 68.955 1.00 57.05 O ANISOU 1772 O TYR A1013 6333 9197 6146 -320 -293 89 O ATOM 1773 CB TYR A1013 21.441 33.464 70.096 1.00 42.70 C ANISOU 1773 CB TYR A1013 4580 7290 4352 -304 -275 139 C ATOM 1774 CG TYR A1013 20.961 34.625 70.904 1.00 39.73 C ANISOU 1774 CG TYR A1013 4201 6903 3988 -313 -262 150 C ATOM 1775 CD1 TYR A1013 21.179 34.633 72.264 1.00 48.77 C ANISOU 1775 CD1 TYR A1013 5354 8033 5142 -345 -248 151 C ATOM 1776 CD2 TYR A1013 20.241 35.661 70.340 1.00 47.85 C ANISOU 1776 CD2 TYR A1013 5228 7938 5012 -279 -258 161 C ATOM 1777 CE1 TYR A1013 20.723 35.672 73.053 1.00 50.44 C ANISOU 1777 CE1 TYR A1013 5575 8227 5362 -359 -225 148 C ATOM 1778 CE2 TYR A1013 19.791 36.721 71.103 1.00 50.68 C ANISOU 1778 CE2 TYR A1013 5611 8265 5379 -268 -229 169 C ATOM 1779 CZ TYR A1013 20.038 36.725 72.465 1.00 58.41 C ANISOU 1779 CZ TYR A1013 6601 9220 6371 -317 -210 155 C ATOM 1780 OH TYR A1013 19.595 37.764 73.233 1.00 59.34 O ANISOU 1780 OH TYR A1013 6752 9299 6492 -313 -171 151 O ATOM 1781 N ASN A1014 18.198 32.234 70.942 1.00 50.92 N ANISOU 1781 N ASN A1014 5583 8371 5392 -396 -269 60 N ATOM 1782 CA ASN A1014 16.754 32.575 70.871 1.00 43.33 C ANISOU 1782 CA ASN A1014 4554 7502 4406 -410 -274 35 C ATOM 1783 C ASN A1014 16.548 33.789 71.772 1.00 46.94 C ANISOU 1783 C ASN A1014 4995 7953 4884 -359 -266 63 C ATOM 1784 O ASN A1014 16.723 33.673 72.982 1.00 37.91 O ANISOU 1784 O ASN A1014 3877 6764 3762 -393 -251 62 O ATOM 1785 CB ASN A1014 15.923 31.353 71.237 1.00 44.55 C ANISOU 1785 CB ASN A1014 4714 7680 4532 -514 -257 -18 C ATOM 1786 CG ASN A1014 14.431 31.624 71.345 1.00 57.54 C ANISOU 1786 CG ASN A1014 6264 9467 6132 -544 -261 -52 C ATOM 1787 OD1 ASN A1014 13.825 32.232 70.469 1.00 64.05 O ANISOU 1787 OD1 ASN A1014 7005 10413 6916 -493 -281 -50 O ATOM 1788 ND2 ASN A1014 13.802 31.130 72.404 1.00 65.61 N ANISOU 1788 ND2 ASN A1014 7287 10497 7143 -625 -240 -82 N ATOM 1789 N PRO A1015 16.245 34.994 71.221 1.00 53.54 N ANISOU 1789 N PRO A1015 5808 8824 5710 -273 -267 92 N ATOM 1790 CA PRO A1015 16.139 36.212 72.034 1.00 53.70 C ANISOU 1790 CA PRO A1015 5853 8803 5747 -218 -238 114 C ATOM 1791 C PRO A1015 15.042 36.188 73.116 1.00 56.43 C ANISOU 1791 C PRO A1015 6153 9201 6087 -229 -223 85 C ATOM 1792 O PRO A1015 15.113 37.001 74.021 1.00 60.47 O ANISOU 1792 O PRO A1015 6701 9658 6616 -208 -190 89 O ATOM 1793 CB PRO A1015 15.798 37.318 71.016 1.00 62.01 C ANISOU 1793 CB PRO A1015 6907 9883 6771 -102 -231 157 C ATOM 1794 CG PRO A1015 16.211 36.759 69.670 1.00 60.60 C ANISOU 1794 CG PRO A1015 6710 9744 6569 -114 -264 165 C ATOM 1795 CD PRO A1015 16.032 35.262 69.790 1.00 52.14 C ANISOU 1795 CD PRO A1015 5598 8717 5495 -217 -286 109 C ATOM 1796 N GLU A1016 14.063 35.282 73.005 1.00 57.89 N ANISOU 1796 N GLU A1016 6261 9498 6235 -279 -241 46 N ATOM 1797 CA GLU A1016 12.985 35.050 74.019 1.00 54.76 C ANISOU 1797 CA GLU A1016 5806 9183 5817 -320 -228 7 C ATOM 1798 C GLU A1016 13.581 34.445 75.314 1.00 50.98 C ANISOU 1798 C GLU A1016 5389 8606 5374 -418 -213 -5 C ATOM 1799 O GLU A1016 13.041 34.728 76.408 1.00 46.35 O ANISOU 1799 O GLU A1016 4781 8044 4785 -431 -192 -23 O ATOM 1800 CB GLU A1016 11.902 34.109 73.475 1.00 58.61 C ANISOU 1800 CB GLU A1016 6200 9833 6235 -395 -244 -41 C ATOM 1801 CG GLU A1016 11.195 34.613 72.229 1.00 79.98 C ANISOU 1801 CG GLU A1016 8812 12697 8878 -300 -264 -28 C ATOM 1802 CD GLU A1016 10.103 35.647 72.451 1.00103.75 C ANISOU 1802 CD GLU A1016 11728 15850 11841 -164 -253 -11 C ATOM 1803 OE1 GLU A1016 9.079 35.307 73.117 1.00 87.95 O ANISOU 1803 OE1 GLU A1016 9634 13993 9789 -219 -245 -60 O ATOM 1804 OE2 GLU A1016 10.275 36.791 71.941 1.00136.04 O ANISOU 1804 OE2 GLU A1016 15844 19909 15936 1 -244 52 O ATOM 1805 N ASP A1017 14.627 33.623 75.185 1.00 45.15 N ANISOU 1805 N ASP A1017 4719 7777 4658 -472 -221 6 N ATOM 1806 CA ASP A1017 15.398 33.005 76.294 1.00 48.53 C ANISOU 1806 CA ASP A1017 5210 8122 5105 -532 -208 17 C ATOM 1807 C ASP A1017 16.604 33.882 76.680 1.00 49.29 C ANISOU 1807 C ASP A1017 5343 8154 5229 -487 -203 54 C ATOM 1808 O ASP A1017 16.838 34.126 77.878 1.00 70.62 O ANISOU 1808 O ASP A1017 8055 10844 7932 -517 -186 56 O ATOM 1809 CB ASP A1017 15.954 31.624 75.924 1.00 45.17 C ANISOU 1809 CB ASP A1017 4849 7641 4671 -582 -209 20 C ATOM 1810 CG ASP A1017 14.939 30.559 75.598 1.00 46.81 C ANISOU 1810 CG ASP A1017 5059 7890 4837 -677 -195 -29 C ATOM 1811 OD1 ASP A1017 13.877 30.554 76.247 1.00 55.71 O ANISOU 1811 OD1 ASP A1017 6138 9093 5935 -740 -184 -63 O ATOM 1812 OD2 ASP A1017 15.240 29.738 74.688 1.00 52.94 O ANISOU 1812 OD2 ASP A1017 5886 8628 5598 -698 -189 -41 O ATOM 1813 N GLY A1018 17.396 34.280 75.704 1.00 55.79 N ANISOU 1813 N GLY A1018 6184 8952 6059 -439 -213 76 N ATOM 1814 CA GLY A1018 18.674 34.952 75.958 1.00 54.75 C ANISOU 1814 CA GLY A1018 6086 8783 5930 -433 -203 102 C ATOM 1815 C GLY A1018 19.699 33.978 76.520 1.00 59.97 C ANISOU 1815 C GLY A1018 6763 9442 6578 -461 -210 123 C ATOM 1816 O GLY A1018 19.531 32.720 76.390 1.00 48.03 O ANISOU 1816 O GLY A1018 5269 7916 5061 -465 -218 126 O ATOM 1817 N ASP A1019 20.730 34.547 77.145 1.00 57.42 N ANISOU 1817 N ASP A1019 6441 9141 6235 -481 -199 137 N ATOM 1818 CA ASP A1019 21.790 33.772 77.834 1.00 63.36 C ANISOU 1818 CA ASP A1019 7185 9938 6950 -484 -205 170 C ATOM 1819 C ASP A1019 21.844 34.291 79.263 1.00 54.02 C ANISOU 1819 C ASP A1019 5983 8798 5741 -546 -186 162 C ATOM 1820 O ASP A1019 22.647 35.162 79.565 1.00 56.22 O ANISOU 1820 O ASP A1019 6245 9132 5984 -592 -170 152 O ATOM 1821 CB ASP A1019 23.114 33.907 77.071 1.00 63.66 C ANISOU 1821 CB ASP A1019 7206 10024 6955 -455 -214 190 C ATOM 1822 CG ASP A1019 24.126 32.793 77.308 1.00 64.33 C ANISOU 1822 CG ASP A1019 7278 10169 6995 -396 -224 236 C ATOM 1823 OD1 ASP A1019 23.730 31.700 77.764 1.00 73.07 O ANISOU 1823 OD1 ASP A1019 8422 11233 8106 -361 -221 260 O ATOM 1824 OD2 ASP A1019 25.314 33.031 77.032 1.00 67.71 O ANISOU 1824 OD2 ASP A1019 7662 10692 7372 -381 -228 251 O ATOM 1825 N PRO A1020 20.921 33.877 80.155 1.00 61.98 N ANISOU 1825 N PRO A1020 6997 9793 6760 -572 -179 154 N ATOM 1826 CA PRO A1020 20.824 34.505 81.480 1.00 58.24 C ANISOU 1826 CA PRO A1020 6503 9363 6261 -640 -156 134 C ATOM 1827 C PRO A1020 22.011 34.168 82.401 1.00 49.22 C ANISOU 1827 C PRO A1020 5327 8325 5048 -660 -160 173 C ATOM 1828 O PRO A1020 22.296 34.938 83.301 1.00 56.21 O ANISOU 1828 O PRO A1020 6185 9277 5893 -736 -138 147 O ATOM 1829 CB PRO A1020 19.484 33.994 82.013 1.00 61.93 C ANISOU 1829 CB PRO A1020 6976 9802 6750 -658 -151 117 C ATOM 1830 CG PRO A1020 19.288 32.665 81.293 1.00 74.66 C ANISOU 1830 CG PRO A1020 8622 11371 8373 -619 -170 145 C ATOM 1831 CD PRO A1020 19.881 32.870 79.914 1.00 64.46 C ANISOU 1831 CD PRO A1020 7335 10056 7097 -561 -186 151 C ATOM 1832 N ASP A1021 22.664 33.036 82.158 1.00 42.38 N ANISOU 1832 N ASP A1021 4464 7480 4157 -587 -182 233 N ATOM 1833 CA ASP A1021 23.878 32.597 82.874 1.00 41.63 C ANISOU 1833 CA ASP A1021 4323 7519 3976 -558 -191 290 C ATOM 1834 C ASP A1021 24.984 33.625 82.638 1.00 47.38 C ANISOU 1834 C ASP A1021 4983 8367 4650 -606 -188 265 C ATOM 1835 O ASP A1021 25.735 33.906 83.588 1.00 68.90 O ANISOU 1835 O ASP A1021 7640 11251 7287 -659 -182 272 O ATOM 1836 CB ASP A1021 24.350 31.223 82.391 1.00 46.55 C ANISOU 1836 CB ASP A1021 4985 8116 4583 -428 -202 363 C ATOM 1837 CG ASP A1021 23.421 30.057 82.683 1.00 54.92 C ANISOU 1837 CG ASP A1021 6141 9053 5670 -402 -186 391 C ATOM 1838 OD1 ASP A1021 22.279 30.308 83.156 1.00 54.20 O ANISOU 1838 OD1 ASP A1021 6067 8909 5615 -493 -176 348 O ATOM 1839 OD2 ASP A1021 23.874 28.887 82.442 1.00 49.93 O ANISOU 1839 OD2 ASP A1021 5576 8381 5011 -291 -176 456 O ATOM 1840 N ASN A1022 25.092 34.143 81.413 1.00 45.73 N ANISOU 1840 N ASN A1022 4794 8102 4479 -601 -187 235 N ATOM 1841 CA ASN A1022 26.196 35.020 80.950 1.00 44.22 C ANISOU 1841 CA ASN A1022 4556 8016 4228 -657 -177 211 C ATOM 1842 C ASN A1022 25.680 36.458 80.781 1.00 41.41 C ANISOU 1842 C ASN A1022 4256 7572 3903 -768 -134 139 C ATOM 1843 O ASN A1022 26.240 37.203 79.930 1.00 44.10 O ANISOU 1843 O ASN A1022 4612 7915 4225 -810 -116 115 O ATOM 1844 CB ASN A1022 26.867 34.400 79.719 1.00 42.68 C ANISOU 1844 CB ASN A1022 4351 7834 4031 -555 -201 245 C ATOM 1845 CG ASN A1022 27.243 32.947 79.954 1.00 51.56 C ANISOU 1845 CG ASN A1022 5460 9003 5126 -417 -224 320 C ATOM 1846 OD1 ASN A1022 28.126 32.620 80.769 1.00 71.63 O ANISOU 1846 OD1 ASN A1022 7927 11717 7572 -386 -229 364 O ATOM 1847 ND2 ASN A1022 26.553 32.052 79.273 1.00 41.79 N ANISOU 1847 ND2 ASN A1022 4302 7616 3959 -331 -228 337 N ATOM 1848 N GLY A1023 24.687 36.842 81.586 1.00 41.42 N ANISOU 1848 N GLY A1023 4296 7502 3940 -811 -109 107 N ATOM 1849 CA GLY A1023 24.287 38.245 81.778 1.00 45.76 C ANISOU 1849 CA GLY A1023 4912 7978 4495 -909 -47 39 C ATOM 1850 C GLY A1023 23.403 38.747 80.661 1.00 51.91 C ANISOU 1850 C GLY A1023 5773 8596 5352 -841 -33 31 C ATOM 1851 O GLY A1023 23.061 39.956 80.687 1.00 56.47 O ANISOU 1851 O GLY A1023 6436 9086 5933 -888 31 -13 O ATOM 1852 N VAL A1024 23.012 37.870 79.732 1.00 48.04 N ANISOU 1852 N VAL A1024 5268 8070 4913 -731 -83 73 N ATOM 1853 CA VAL A1024 22.216 38.338 78.564 1.00 58.46 C ANISOU 1853 CA VAL A1024 6643 9280 6287 -660 -76 73 C ATOM 1854 C VAL A1024 20.752 38.164 78.924 1.00 51.30 C ANISOU 1854 C VAL A1024 5736 8326 5427 -607 -76 62 C ATOM 1855 O VAL A1024 20.320 36.989 79.010 1.00 51.49 O ANISOU 1855 O VAL A1024 5713 8379 5468 -577 -118 79 O ATOM 1856 CB VAL A1024 22.559 37.620 77.244 1.00 59.21 C ANISOU 1856 CB VAL A1024 6717 9384 6395 -590 -121 109 C ATOM 1857 CG1 VAL A1024 21.831 38.268 76.075 1.00 58.52 C ANISOU 1857 CG1 VAL A1024 6680 9215 6339 -527 -111 113 C ATOM 1858 CG2 VAL A1024 24.060 37.598 76.977 1.00 55.02 C ANISOU 1858 CG2 VAL A1024 6158 8943 5803 -635 -126 120 C ATOM 1859 N ASN A1025 20.062 39.297 79.127 1.00 50.72 N ANISOU 1859 N ASN A1025 5722 8185 5362 -599 -21 32 N ATOM 1860 CA ASN A1025 18.628 39.313 79.518 1.00 56.33 C ANISOU 1860 CA ASN A1025 6417 8884 6100 -538 -12 15 C ATOM 1861 C ASN A1025 17.781 38.763 78.373 1.00 63.95 C ANISOU 1861 C ASN A1025 7341 9866 7091 -438 -55 42 C ATOM 1862 O ASN A1025 18.031 39.062 77.197 1.00 64.29 O ANISOU 1862 O ASN A1025 7410 9881 7133 -386 -62 68 O ATOM 1863 CB ASN A1025 18.151 40.731 79.852 1.00 62.70 C ANISOU 1863 CB ASN A1025 7312 9609 6901 -514 70 -17 C ATOM 1864 CG ASN A1025 18.392 41.141 81.288 1.00 64.51 C ANISOU 1864 CG ASN A1025 7564 9845 7103 -620 121 -68 C ATOM 1865 OD1 ASN A1025 18.829 40.338 82.110 1.00 70.85 O ANISOU 1865 OD1 ASN A1025 8298 10735 7887 -704 86 -72 O ATOM 1866 ND2 ASN A1025 18.117 42.399 81.594 1.00 66.72 N ANISOU 1866 ND2 ASN A1025 7950 10029 7369 -612 212 -107 N ATOM 1867 N PRO A1026 16.720 37.987 78.680 1.00 59.51 N ANISOU 1867 N PRO A1026 6711 9366 6534 -424 -80 30 N ATOM 1868 CA PRO A1026 15.749 37.606 77.658 1.00 60.19 C ANISOU 1868 CA PRO A1026 6744 9506 6618 -351 -110 38 C ATOM 1869 C PRO A1026 15.058 38.882 77.162 1.00 62.26 C ANISOU 1869 C PRO A1026 7031 9753 6871 -229 -70 47 C ATOM 1870 O PRO A1026 14.847 39.789 77.944 1.00 56.59 O ANISOU 1870 O PRO A1026 6359 8990 6150 -206 -14 29 O ATOM 1871 CB PRO A1026 14.788 36.644 78.374 1.00 61.75 C ANISOU 1871 CB PRO A1026 6871 9787 6803 -403 -125 8 C ATOM 1872 CG PRO A1026 15.456 36.294 79.702 1.00 52.62 C ANISOU 1872 CG PRO A1026 5740 8602 5648 -497 -115 1 C ATOM 1873 CD PRO A1026 16.372 37.463 80.007 1.00 55.85 C ANISOU 1873 CD PRO A1026 6213 8945 6063 -494 -77 4 C ATOM 1874 N GLY A1027 14.763 38.933 75.864 1.00 79.42 N ANISOU 1874 N GLY A1027 9184 11961 9031 -145 -93 78 N ATOM 1875 CA GLY A1027 14.147 40.124 75.250 1.00 84.93 C ANISOU 1875 CA GLY A1027 9915 12648 9704 6 -53 111 C ATOM 1876 C GLY A1027 15.203 41.078 74.723 1.00 68.88 C ANISOU 1876 C GLY A1027 8016 10475 7678 21 -13 147 C ATOM 1877 O GLY A1027 14.893 42.265 74.532 1.00 63.78 O ANISOU 1877 O GLY A1027 7462 9756 7014 137 51 176 O ATOM 1878 N THR A1028 16.427 40.591 74.512 1.00 81.36 N ANISOU 1878 N THR A1028 9619 12020 9275 -91 -39 145 N ATOM 1879 CA THR A1028 17.488 41.414 73.861 1.00 87.22 C ANISOU 1879 CA THR A1028 10474 12661 10005 -107 -3 174 C ATOM 1880 C THR A1028 17.788 40.813 72.485 1.00 84.00 C ANISOU 1880 C THR A1028 10018 12310 9586 -87 -61 208 C ATOM 1881 O THR A1028 18.084 39.602 72.421 1.00 74.84 O ANISOU 1881 O THR A1028 8775 11220 8438 -152 -119 188 O ATOM 1882 CB THR A1028 18.748 41.542 74.733 1.00 86.85 C ANISOU 1882 CB THR A1028 10480 12561 9956 -258 24 139 C ATOM 1883 OG1 THR A1028 19.349 40.251 74.850 1.00 73.68 O ANISOU 1883 OG1 THR A1028 8715 10980 8297 -333 -42 128 O ATOM 1884 CG2 THR A1028 18.458 42.129 76.104 1.00 81.57 C ANISOU 1884 CG2 THR A1028 9857 11846 9287 -296 86 94 C ATOM 1885 N ASP A1029 17.690 41.631 71.431 1.00 82.46 N ANISOU 1885 N ASP A1029 9887 12079 9363 5 -37 259 N ATOM 1886 CA ASP A1029 18.050 41.162 70.068 1.00 88.12 C ANISOU 1886 CA ASP A1029 10565 12856 10060 15 -86 290 C ATOM 1887 C ASP A1029 19.562 40.901 70.021 1.00 57.66 C ANISOU 1887 C ASP A1029 6738 8964 6206 -117 -90 271 C ATOM 1888 O ASP A1029 20.298 41.510 70.795 1.00 54.91 O ANISOU 1888 O ASP A1029 6468 8541 5854 -200 -39 252 O ATOM 1889 CB ASP A1029 17.569 42.159 69.004 1.00103.35 C ANISOU 1889 CB ASP A1029 12558 14763 11944 156 -55 361 C ATOM 1890 CG ASP A1029 17.629 41.621 67.586 1.00 98.59 C ANISOU 1890 CG ASP A1029 11887 14264 11309 181 -113 392 C ATOM 1891 OD1 ASP A1029 17.836 40.394 67.432 1.00 74.24 O ANISOU 1891 OD1 ASP A1029 8698 11268 8239 98 -173 347 O ATOM 1892 OD2 ASP A1029 17.488 42.433 66.649 1.00121.48 O ANISOU 1892 OD2 ASP A1029 14849 17145 14161 283 -88 461 O ATOM 1893 N PHE A1030 20.001 40.028 69.118 1.00 66.49 N ANISOU 1893 N PHE A1030 7790 10156 7316 -138 -144 273 N ATOM 1894 CA PHE A1030 21.429 39.653 68.953 1.00 69.52 C ANISOU 1894 CA PHE A1030 8175 10551 7689 -237 -153 257 C ATOM 1895 C PHE A1030 22.266 40.917 68.728 1.00 68.66 C ANISOU 1895 C PHE A1030 8180 10367 7540 -287 -91 277 C ATOM 1896 O PHE A1030 23.411 40.955 69.232 1.00 73.95 O ANISOU 1896 O PHE A1030 8858 11052 8187 -402 -73 248 O ATOM 1897 CB PHE A1030 21.594 38.660 67.803 1.00 60.04 C ANISOU 1897 CB PHE A1030 6901 9431 6477 -220 -207 258 C ATOM 1898 CG PHE A1030 22.941 37.988 67.737 1.00 66.69 C ANISOU 1898 CG PHE A1030 7718 10314 7306 -289 -220 236 C ATOM 1899 CD1 PHE A1030 23.245 36.933 68.589 1.00 65.65 C ANISOU 1899 CD1 PHE A1030 7540 10208 7194 -313 -238 207 C ATOM 1900 CD2 PHE A1030 23.889 38.378 66.797 1.00 64.20 C ANISOU 1900 CD2 PHE A1030 7423 10022 6947 -317 -212 251 C ATOM 1901 CE1 PHE A1030 24.478 36.300 68.519 1.00 68.95 C ANISOU 1901 CE1 PHE A1030 7927 10684 7585 -337 -246 199 C ATOM 1902 CE2 PHE A1030 25.121 37.741 66.734 1.00 78.36 C ANISOU 1902 CE2 PHE A1030 9171 11887 8714 -363 -223 231 C ATOM 1903 CZ PHE A1030 25.425 36.716 67.609 1.00 66.97 C ANISOU 1903 CZ PHE A1030 7677 10479 7288 -360 -240 207 C ATOM 1904 N LYS A1031 21.697 41.915 68.038 1.00 58.78 N ANISOU 1904 N LYS A1031 7018 9047 6266 -206 -53 327 N ATOM 1905 CA LYS A1031 22.382 43.195 67.714 1.00 67.41 C ANISOU 1905 CA LYS A1031 8266 10035 7310 -257 26 353 C ATOM 1906 C LYS A1031 22.765 43.921 69.011 1.00 68.84 C ANISOU 1906 C LYS A1031 8543 10125 7486 -364 103 308 C ATOM 1907 O LYS A1031 23.790 44.624 68.997 1.00 70.42 O ANISOU 1907 O LYS A1031 8843 10281 7633 -499 165 291 O ATOM 1908 CB LYS A1031 21.499 44.079 66.823 1.00 73.15 C ANISOU 1908 CB LYS A1031 9089 10693 8010 -108 62 431 C ATOM 1909 CG LYS A1031 20.124 44.422 67.386 1.00 89.98 C ANISOU 1909 CG LYS A1031 11233 12791 10164 42 83 451 C ATOM 1910 CD LYS A1031 19.456 45.628 66.742 1.00 95.46 C ANISOU 1910 CD LYS A1031 12073 13385 10809 205 155 540 C ATOM 1911 CE LYS A1031 18.154 46.019 67.419 1.00108.69 C ANISOU 1911 CE LYS A1031 13756 15043 12495 373 187 556 C ATOM 1912 NZ LYS A1031 17.420 47.064 66.664 1.00123.75 N ANISOU 1912 NZ LYS A1031 15788 16888 14343 589 251 662 N ATOM 1913 N ASP A1032 21.984 43.749 70.084 1.00 75.64 N ANISOU 1913 N ASP A1032 9374 10976 8389 -324 103 281 N ATOM 1914 CA ASP A1032 22.119 44.530 71.347 1.00 76.93 C ANISOU 1914 CA ASP A1032 9638 11048 8544 -412 187 234 C ATOM 1915 C ASP A1032 23.128 43.868 72.296 1.00 74.91 C ANISOU 1915 C ASP A1032 9287 10896 8277 -575 160 171 C ATOM 1916 O ASP A1032 23.642 44.588 73.169 1.00 69.44 O ANISOU 1916 O ASP A1032 8678 10159 7544 -707 235 122 O ATOM 1917 CB ASP A1032 20.764 44.718 72.033 1.00 82.97 C ANISOU 1917 CB ASP A1032 10409 11766 9347 -280 205 236 C ATOM 1918 CG ASP A1032 19.758 45.496 71.196 1.00 89.12 C ANISOU 1918 CG ASP A1032 11279 12466 10114 -88 244 309 C ATOM 1919 OD1 ASP A1032 20.020 46.677 70.923 1.00 88.88 O ANISOU 1919 OD1 ASP A1032 11443 12284 10043 -86 344 335 O ATOM 1920 OD2 ASP A1032 18.725 44.905 70.813 1.00103.47 O ANISOU 1920 OD2 ASP A1032 12976 14386 11950 54 179 340 O ATOM 1921 N ILE A1033 23.414 42.567 72.136 1.00 77.36 N ANISOU 1921 N ILE A1033 9441 11344 8607 -565 66 172 N ATOM 1922 CA ILE A1033 24.432 41.864 72.987 1.00 71.13 C ANISOU 1922 CA ILE A1033 8555 10680 7791 -680 39 132 C ATOM 1923 C ILE A1033 25.801 42.505 72.743 1.00 84.54 C ANISOU 1923 C ILE A1033 10293 12424 9403 -831 84 109 C ATOM 1924 O ILE A1033 26.172 42.728 71.591 1.00 71.37 O ANISOU 1924 O ILE A1033 8656 10750 7711 -826 86 135 O ATOM 1925 CB ILE A1033 24.489 40.347 72.696 1.00 66.62 C ANISOU 1925 CB ILE A1033 7844 10218 7249 -608 -52 149 C ATOM 1926 CG1 ILE A1033 23.113 39.716 72.474 1.00 63.23 C ANISOU 1926 CG1 ILE A1033 7385 9752 6885 -482 -92 168 C ATOM 1927 CG2 ILE A1033 25.249 39.633 73.792 1.00 71.31 C ANISOU 1927 CG2 ILE A1033 8351 10927 7814 -672 -72 127 C ATOM 1928 CD1 ILE A1033 23.181 38.283 71.988 1.00 64.80 C ANISOU 1928 CD1 ILE A1033 7493 10025 7101 -433 -158 177 C ATOM 1929 N PRO A1034 26.600 42.834 73.792 1.00 88.98 N ANISOU 1929 N PRO A1034 10848 13058 9900 -986 126 57 N ATOM 1930 CA PRO A1034 27.919 43.438 73.583 1.00 83.19 C ANISOU 1930 CA PRO A1034 10135 12413 9059 -1164 175 22 C ATOM 1931 C PRO A1034 28.874 42.472 72.868 1.00 79.49 C ANISOU 1931 C PRO A1034 9516 12131 8554 -1140 100 43 C ATOM 1932 O PRO A1034 28.714 41.250 73.011 1.00 63.53 O ANISOU 1932 O PRO A1034 7371 10188 6577 -1016 21 70 O ATOM 1933 CB PRO A1034 28.419 43.764 75.004 1.00104.21 C ANISOU 1933 CB PRO A1034 12779 15163 11651 -1327 221 -44 C ATOM 1934 CG PRO A1034 27.157 43.740 75.868 1.00 74.14 C ANISOU 1934 CG PRO A1034 9010 11229 7928 -1232 226 -44 C ATOM 1935 CD PRO A1034 26.276 42.697 75.223 1.00 68.57 C ANISOU 1935 CD PRO A1034 8232 10496 7325 -1020 135 21 C ATOM 1936 N ASP A1035 29.829 43.046 72.123 1.00 86.64 N ANISOU 1936 N ASP A1035 10450 13096 9372 -1260 138 28 N ATOM 1937 CA ASP A1035 30.773 42.304 71.231 1.00 82.94 C ANISOU 1937 CA ASP A1035 9854 12804 8855 -1236 82 45 C ATOM 1938 C ASP A1035 31.569 41.281 72.058 1.00 78.09 C ANISOU 1938 C ASP A1035 9051 12430 8189 -1221 28 34 C ATOM 1939 O ASP A1035 32.078 40.294 71.445 1.00 53.00 O ANISOU 1939 O ASP A1035 5755 9380 5002 -1113 -31 62 O ATOM 1940 CB ASP A1035 31.716 43.268 70.502 1.00 88.00 C ANISOU 1940 CB ASP A1035 10561 13490 9384 -1415 150 17 C ATOM 1941 CG ASP A1035 31.031 44.519 69.972 1.00 99.16 C ANISOU 1941 CG ASP A1035 12206 14651 10819 -1456 237 30 C ATOM 1942 OD1 ASP A1035 30.737 45.434 70.783 1.00 90.00 O ANISOU 1942 OD1 ASP A1035 11183 13367 9643 -1560 323 -5 O ATOM 1943 OD2 ASP A1035 30.786 44.562 68.756 1.00105.63 O ANISOU 1943 OD2 ASP A1035 13073 15396 11662 -1372 223 80 O ATOM 1944 N ASP A1036 31.684 41.565 73.371 1.00 70.44 N ANISOU 1944 N ASP A1036 8066 11520 7178 -1323 57 -3 N ATOM 1945 CA ASP A1036 32.372 40.753 74.403 1.00 61.48 C ANISOU 1945 CA ASP A1036 6761 10624 5974 -1314 17 -6 C ATOM 1946 C ASP A1036 31.743 39.354 74.412 1.00 71.32 C ANISOU 1946 C ASP A1036 7946 11828 7321 -1076 -62 59 C ATOM 1947 O ASP A1036 32.489 38.390 74.727 1.00 71.70 O ANISOU 1947 O ASP A1036 7854 12078 7310 -993 -106 87 O ATOM 1948 CB ASP A1036 32.270 41.455 75.766 1.00 64.53 C ANISOU 1948 CB ASP A1036 7179 11026 6312 -1469 72 -59 C ATOM 1949 N TRP A1037 30.444 39.248 74.055 1.00 61.99 N ANISOU 1949 N TRP A1037 6871 10408 6272 -971 -74 83 N ATOM 1950 CA TRP A1037 29.646 38.009 74.275 1.00 50.61 C ANISOU 1950 CA TRP A1037 5404 8903 4922 -796 -130 128 C ATOM 1951 C TRP A1037 30.170 36.886 73.389 1.00 57.38 C ANISOU 1951 C TRP A1037 6192 9836 5774 -663 -175 163 C ATOM 1952 O TRP A1037 30.631 37.171 72.253 1.00 68.67 O ANISOU 1952 O TRP A1037 7625 11286 7179 -679 -171 156 O ATOM 1953 CB TRP A1037 28.165 38.223 74.009 1.00 58.43 C ANISOU 1953 CB TRP A1037 6503 9670 6026 -740 -126 133 C ATOM 1954 CG TRP A1037 27.365 36.989 74.301 1.00 66.79 C ANISOU 1954 CG TRP A1037 7540 10682 7155 -612 -170 162 C ATOM 1955 CD1 TRP A1037 27.045 36.495 75.532 1.00 71.37 C ANISOU 1955 CD1 TRP A1037 8097 11278 7742 -602 -177 169 C ATOM 1956 CD2 TRP A1037 26.778 36.077 73.354 1.00 70.63 C ANISOU 1956 CD2 TRP A1037 8038 11097 7701 -498 -204 184 C ATOM 1957 NE1 TRP A1037 26.298 35.354 75.420 1.00 70.72 N ANISOU 1957 NE1 TRP A1037 8024 11126 7718 -496 -207 195 N ATOM 1958 CE2 TRP A1037 26.115 35.071 74.098 1.00 62.52 C ANISOU 1958 CE2 TRP A1037 7008 10033 6711 -438 -222 198 C ATOM 1959 CE3 TRP A1037 26.735 36.018 71.955 1.00 63.78 C ANISOU 1959 CE3 TRP A1037 7188 10198 6848 -456 -216 188 C ATOM 1960 CZ2 TRP A1037 25.451 34.007 73.497 1.00 60.23 C ANISOU 1960 CZ2 TRP A1037 6743 9674 6467 -357 -241 207 C ATOM 1961 CZ3 TRP A1037 26.066 34.971 71.356 1.00 64.83 C ANISOU 1961 CZ3 TRP A1037 7329 10275 7027 -368 -242 195 C ATOM 1962 CH2 TRP A1037 25.429 33.985 72.118 1.00 78.49 C ANISOU 1962 CH2 TRP A1037 9067 11964 8789 -328 -250 199 C ATOM 1963 N VAL A1038 30.075 35.651 73.872 1.00 47.33 N ANISOU 1963 N VAL A1038 4876 8588 4519 -534 -208 201 N ATOM 1964 CA VAL A1038 30.589 34.471 73.115 1.00 48.16 C ANISOU 1964 CA VAL A1038 4940 8745 4613 -386 -234 234 C ATOM 1965 C VAL A1038 29.575 33.335 73.191 1.00 46.85 C ANISOU 1965 C VAL A1038 4846 8418 4536 -266 -247 259 C ATOM 1966 O VAL A1038 28.731 33.317 74.104 1.00 47.88 O ANISOU 1966 O VAL A1038 5015 8465 4709 -290 -245 262 O ATOM 1967 CB VAL A1038 31.982 34.001 73.589 1.00 49.82 C ANISOU 1967 CB VAL A1038 5022 9209 4698 -334 -239 260 C ATOM 1968 CG1 VAL A1038 33.077 34.972 73.179 1.00 49.03 C ANISOU 1968 CG1 VAL A1038 4839 9300 4488 -466 -222 222 C ATOM 1969 CG2 VAL A1038 32.032 33.734 75.075 1.00 47.17 C ANISOU 1969 CG2 VAL A1038 4643 8957 4321 -325 -241 288 C ATOM 1970 N CYS A1039 29.678 32.426 72.222 1.00 62.04 N ANISOU 1970 N CYS A1039 6791 10306 6474 -156 -252 269 N ATOM 1971 CA CYS A1039 28.827 31.218 72.048 1.00 57.92 C ANISOU 1971 CA CYS A1039 6359 9630 6018 -62 -248 279 C ATOM 1972 C CYS A1039 28.948 30.373 73.315 1.00 47.84 C ANISOU 1972 C CYS A1039 5092 8368 4715 14 -238 328 C ATOM 1973 O CYS A1039 30.032 29.965 73.687 1.00 49.66 O ANISOU 1973 O CYS A1039 5261 8743 4864 109 -234 371 O ATOM 1974 CB CYS A1039 29.257 30.473 70.785 1.00 55.24 C ANISOU 1974 CB CYS A1039 6037 9284 5667 30 -239 271 C ATOM 1975 SG CYS A1039 28.234 29.047 70.349 1.00 59.65 S ANISOU 1975 SG CYS A1039 6734 9641 6286 97 -211 257 S ATOM 1976 N PRO A1040 27.847 30.086 74.024 1.00 49.64 N ANISOU 1976 N PRO A1040 5392 8468 4998 -18 -231 329 N ATOM 1977 CA PRO A1040 27.904 29.251 75.216 1.00 44.82 C ANISOU 1977 CA PRO A1040 4811 7859 4359 50 -217 383 C ATOM 1978 C PRO A1040 28.411 27.818 74.976 1.00 56.17 C ANISOU 1978 C PRO A1040 6325 9254 5763 222 -183 433 C ATOM 1979 O PRO A1040 28.993 27.249 75.892 1.00 79.82 O ANISOU 1979 O PRO A1040 9314 12319 8692 327 -171 503 O ATOM 1980 CB PRO A1040 26.425 29.196 75.652 1.00 45.33 C ANISOU 1980 CB PRO A1040 4955 7770 4497 -41 -210 355 C ATOM 1981 CG PRO A1040 25.828 30.449 75.077 1.00 49.84 C ANISOU 1981 CG PRO A1040 5487 8333 5114 -156 -230 296 C ATOM 1982 CD PRO A1040 26.470 30.534 73.715 1.00 55.65 C ANISOU 1982 CD PRO A1040 6206 9099 5840 -117 -235 281 C ATOM 1983 N LEU A1041 28.199 27.249 73.788 1.00 62.78 N ANISOU 1983 N LEU A1041 7240 9980 6632 257 -162 399 N ATOM 1984 CA LEU A1041 28.553 25.830 73.523 1.00 68.76 C ANISOU 1984 CA LEU A1041 8118 10646 7361 420 -106 435 C ATOM 1985 C LEU A1041 29.996 25.687 73.026 1.00 63.22 C ANISOU 1985 C LEU A1041 7335 10105 6578 579 -103 468 C ATOM 1986 O LEU A1041 30.492 24.571 73.139 1.00 73.03 O ANISOU 1986 O LEU A1041 8667 11307 7773 761 -51 523 O ATOM 1987 CB LEU A1041 27.587 25.257 72.482 1.00 74.47 C ANISOU 1987 CB LEU A1041 8972 11178 8144 356 -71 365 C ATOM 1988 CG LEU A1041 26.163 25.011 72.963 1.00 80.29 C ANISOU 1988 CG LEU A1041 9806 11766 8932 222 -54 334 C ATOM 1989 CD1 LEU A1041 25.340 24.350 71.864 1.00 75.12 C ANISOU 1989 CD1 LEU A1041 9267 10969 8303 149 -12 256 C ATOM 1990 CD2 LEU A1041 26.156 24.170 74.233 1.00 77.46 C ANISOU 1990 CD2 LEU A1041 9549 11340 8542 290 -13 405 C ATOM 1991 N CYS A1042 30.624 26.739 72.481 1.00 59.50 N ANISOU 1991 N CYS A1042 6716 9807 6083 517 -146 437 N ATOM 1992 CA CYS A1042 31.985 26.582 71.875 1.00 68.06 C ANISOU 1992 CA CYS A1042 7708 11072 7077 655 -140 455 C ATOM 1993 C CYS A1042 32.854 27.845 72.050 1.00 56.58 C ANISOU 1993 C CYS A1042 6061 9885 5551 560 -187 446 C ATOM 1994 O CYS A1042 34.043 27.718 71.843 1.00 54.39 O ANISOU 1994 O CYS A1042 5676 9818 5171 670 -184 469 O ATOM 1995 CB CYS A1042 31.890 26.148 70.409 1.00 71.56 C ANISOU 1995 CB CYS A1042 8223 11411 7553 682 -113 399 C ATOM 1996 SG CYS A1042 31.428 27.452 69.226 1.00 63.04 S ANISOU 1996 SG CYS A1042 7079 10346 6528 470 -158 313 S ATOM 1997 N GLY A1043 32.298 28.997 72.446 1.00 55.56 N ANISOU 1997 N GLY A1043 5896 9754 5460 363 -217 410 N ATOM 1998 CA GLY A1043 33.074 30.190 72.852 1.00 55.21 C ANISOU 1998 CA GLY A1043 5702 9941 5332 239 -241 395 C ATOM 1999 C GLY A1043 33.487 31.079 71.688 1.00 64.88 C ANISOU 1999 C GLY A1043 6876 11233 6539 130 -246 338 C ATOM 2000 O GLY A1043 34.237 32.066 71.933 1.00 69.80 O ANISOU 2000 O GLY A1043 7389 12055 7073 3 -250 316 O ATOM 2001 N VAL A1044 33.010 30.802 70.465 1.00 60.45 N ANISOU 2001 N VAL A1044 6397 10522 6049 153 -241 310 N ATOM 2002 CA VAL A1044 33.368 31.644 69.284 1.00 54.42 C ANISOU 2002 CA VAL A1044 5596 9817 5264 51 -244 263 C ATOM 2003 C VAL A1044 32.622 32.983 69.371 1.00 48.83 C ANISOU 2003 C VAL A1044 4931 9016 4604 -142 -248 232 C ATOM 2004 O VAL A1044 31.543 33.016 69.961 1.00 62.73 O ANISOU 2004 O VAL A1044 6770 10617 6446 -166 -251 236 O ATOM 2005 CB VAL A1044 33.122 30.916 67.957 1.00 62.31 C ANISOU 2005 CB VAL A1044 6660 10707 6306 139 -235 243 C ATOM 2006 CG1 VAL A1044 34.025 29.701 67.818 1.00 60.08 C ANISOU 2006 CG1 VAL A1044 6347 10521 5958 343 -212 270 C ATOM 2007 CG2 VAL A1044 31.656 30.545 67.765 1.00 76.53 C ANISOU 2007 CG2 VAL A1044 8597 12254 8225 124 -234 229 C ATOM 2008 N GLY A1045 33.172 34.043 68.786 1.00 44.71 N ANISOU 2008 N GLY A1045 4372 8589 4026 -273 -240 203 N ATOM 2009 CA GLY A1045 32.631 35.406 68.932 1.00 50.59 C ANISOU 2009 CA GLY A1045 5183 9245 4793 -448 -222 179 C ATOM 2010 C GLY A1045 31.303 35.587 68.192 1.00 66.52 C ANISOU 2010 C GLY A1045 7319 11033 6921 -437 -227 180 C ATOM 2011 O GLY A1045 30.899 34.688 67.392 1.00 55.53 O ANISOU 2011 O GLY A1045 5946 9576 5576 -328 -245 185 O ATOM 2012 N LYS A1046 30.642 36.723 68.434 1.00 58.26 N ANISOU 2012 N LYS A1046 6353 9878 5902 -543 -203 173 N ATOM 2013 CA LYS A1046 29.396 37.138 67.756 1.00 52.57 C ANISOU 2013 CA LYS A1046 5732 8980 5261 -526 -203 183 C ATOM 2014 C LYS A1046 29.603 37.239 66.243 1.00 52.31 C ANISOU 2014 C LYS A1046 5707 8962 5205 -515 -208 188 C ATOM 2015 O LYS A1046 28.615 37.432 65.527 1.00 60.05 O ANISOU 2015 O LYS A1046 6747 9837 6233 -477 -215 204 O ATOM 2016 CB LYS A1046 28.981 38.526 68.235 1.00 63.02 C ANISOU 2016 CB LYS A1046 7149 10211 6583 -632 -156 180 C ATOM 2017 CG LYS A1046 28.001 38.555 69.391 1.00 67.06 C ANISOU 2017 CG LYS A1046 7695 10627 7157 -612 -152 179 C ATOM 2018 CD LYS A1046 27.594 39.970 69.750 1.00 70.63 C ANISOU 2018 CD LYS A1046 8262 10969 7603 -699 -89 172 C ATOM 2019 CE LYS A1046 26.662 40.584 68.727 1.00 59.08 C ANISOU 2019 CE LYS A1046 6895 9378 6174 -632 -75 206 C ATOM 2020 NZ LYS A1046 26.123 41.870 69.205 1.00 63.98 N ANISOU 2020 NZ LYS A1046 7652 9863 6793 -670 -1 208 N ATOM 2021 N ASP A1047 30.850 37.178 65.796 1.00 65.83 N ANISOU 2021 N ASP A1047 7351 10825 6833 -551 -202 174 N ATOM 2022 CA ASP A1047 31.191 37.231 64.353 1.00 59.09 C ANISOU 2022 CA ASP A1047 6494 10012 5944 -550 -205 174 C ATOM 2023 C ASP A1047 30.699 35.951 63.687 1.00 53.20 C ANISOU 2023 C ASP A1047 5726 9238 5250 -413 -241 171 C ATOM 2024 O ASP A1047 30.288 36.033 62.535 1.00 67.19 O ANISOU 2024 O ASP A1047 7525 10975 7027 -402 -248 174 O ATOM 2025 CB ASP A1047 32.700 37.350 64.136 1.00 63.21 C ANISOU 2025 CB ASP A1047 6925 10742 6349 -622 -189 152 C ATOM 2026 CG ASP A1047 33.345 38.504 64.877 1.00 82.81 C ANISOU 2026 CG ASP A1047 9421 13292 8751 -798 -142 135 C ATOM 2027 OD1 ASP A1047 32.683 39.094 65.740 1.00 96.99 O ANISOU 2027 OD1 ASP A1047 11297 14964 10589 -846 -121 139 O ATOM 2028 OD2 ASP A1047 34.514 38.796 64.585 1.00107.65 O ANISOU 2028 OD2 ASP A1047 12495 16625 11780 -898 -121 109 O ATOM 2029 N GLN A1048 30.775 34.812 64.382 1.00 54.35 N ANISOU 2029 N GLN A1048 5832 9399 5419 -318 -253 163 N ATOM 2030 CA GLN A1048 30.520 33.482 63.769 1.00 58.47 C ANISOU 2030 CA GLN A1048 6357 9889 5970 -202 -263 147 C ATOM 2031 C GLN A1048 29.027 33.168 63.808 1.00 59.26 C ANISOU 2031 C GLN A1048 6529 9833 6153 -188 -273 143 C ATOM 2032 O GLN A1048 28.676 31.980 63.700 1.00 60.28 O ANISOU 2032 O GLN A1048 6686 9909 6307 -118 -267 121 O ATOM 2033 CB GLN A1048 31.321 32.401 64.494 1.00 58.23 C ANISOU 2033 CB GLN A1048 6281 9932 5910 -93 -253 150 C ATOM 2034 CG GLN A1048 32.748 32.830 64.793 1.00 70.60 C ANISOU 2034 CG GLN A1048 7742 11709 7373 -115 -246 157 C ATOM 2035 CD GLN A1048 33.690 32.669 63.629 1.00 84.06 C ANISOU 2035 CD GLN A1048 9384 13552 9003 -88 -238 135 C ATOM 2036 OE1 GLN A1048 33.600 33.376 62.628 1.00 79.74 O ANISOU 2036 OE1 GLN A1048 8851 13001 8444 -179 -239 119 O ATOM 2037 NE2 GLN A1048 34.634 31.750 63.777 1.00 94.00 N ANISOU 2037 NE2 GLN A1048 10571 14946 10198 49 -225 138 N ATOM 2038 N PHE A1049 28.172 34.185 63.927 1.00 62.48 N ANISOU 2038 N PHE A1049 6973 10175 6590 -252 -279 161 N ATOM 2039 CA PHE A1049 26.716 33.895 63.996 1.00 65.35 C ANISOU 2039 CA PHE A1049 7377 10440 7013 -236 -290 156 C ATOM 2040 C PHE A1049 25.972 34.518 62.817 1.00 68.18 C ANISOU 2040 C PHE A1049 7746 10799 7360 -250 -302 166 C ATOM 2041 O PHE A1049 26.049 35.756 62.628 1.00 63.84 O ANISOU 2041 O PHE A1049 7220 10246 6788 -282 -292 203 O ATOM 2042 CB PHE A1049 26.138 34.415 65.306 1.00 75.34 C ANISOU 2042 CB PHE A1049 8664 11645 8317 -260 -285 173 C ATOM 2043 CG PHE A1049 26.344 33.496 66.481 1.00 67.56 C ANISOU 2043 CG PHE A1049 7673 10647 7350 -231 -280 167 C ATOM 2044 CD1 PHE A1049 27.586 33.362 67.058 1.00 55.17 C ANISOU 2044 CD1 PHE A1049 6065 9159 5737 -219 -271 177 C ATOM 2045 CD2 PHE A1049 25.288 32.775 67.002 1.00 60.27 C ANISOU 2045 CD2 PHE A1049 6780 9650 6470 -218 -281 153 C ATOM 2046 CE1 PHE A1049 27.770 32.497 68.116 1.00 63.44 C ANISOU 2046 CE1 PHE A1049 7111 10205 6788 -168 -265 188 C ATOM 2047 CE2 PHE A1049 25.466 31.926 68.072 1.00 54.88 C ANISOU 2047 CE2 PHE A1049 6112 8942 5795 -190 -270 158 C ATOM 2048 CZ PHE A1049 26.708 31.795 68.631 1.00 74.71 C ANISOU 2048 CZ PHE A1049 8593 11527 8267 -153 -263 182 C ATOM 2049 N GLU A1050 25.257 33.653 62.088 1.00 78.39 N ANISOU 2049 N GLU A1050 9031 12096 8656 -230 -312 134 N ATOM 2050 CA GLU A1050 24.362 34.006 60.951 1.00 69.12 C ANISOU 2050 CA GLU A1050 7844 10965 7454 -234 -329 140 C ATOM 2051 C GLU A1050 22.927 34.085 61.484 1.00 72.46 C ANISOU 2051 C GLU A1050 8260 11366 7902 -228 -339 143 C ATOM 2052 O GLU A1050 22.568 33.281 62.377 1.00 62.26 O ANISOU 2052 O GLU A1050 6979 10030 6647 -241 -332 109 O ATOM 2053 CB GLU A1050 24.504 33.003 59.789 1.00 63.76 C ANISOU 2053 CB GLU A1050 7145 10343 6738 -240 -329 87 C ATOM 2054 CG GLU A1050 24.215 31.538 60.136 1.00 70.15 C ANISOU 2054 CG GLU A1050 7982 11105 7567 -247 -308 19 C ATOM 2055 CD GLU A1050 24.629 30.495 59.096 1.00 85.42 C ANISOU 2055 CD GLU A1050 9930 13065 9461 -253 -283 -44 C ATOM 2056 OE1 GLU A1050 24.638 29.275 59.421 1.00 65.72 O ANISOU 2056 OE1 GLU A1050 7499 10494 6977 -250 -242 -98 O ATOM 2057 OE2 GLU A1050 24.953 30.891 57.949 1.00114.51 O ANISOU 2057 OE2 GLU A1050 13577 16835 13096 -261 -294 -42 O ATOM 2058 N GLU A1051 22.143 35.032 60.961 1.00 72.92 N ANISOU 2058 N GLU A1051 8305 11467 7932 -199 -351 189 N ATOM 2059 CA GLU A1051 20.694 35.134 61.230 1.00 53.52 C ANISOU 2059 CA GLU A1051 5812 9050 5472 -173 -363 193 C ATOM 2060 C GLU A1051 20.035 33.841 60.755 1.00 57.27 C ANISOU 2060 C GLU A1051 6235 9605 5917 -229 -373 118 C ATOM 2061 O GLU A1051 20.348 33.418 59.600 1.00 49.59 O ANISOU 2061 O GLU A1051 5245 8698 4898 -254 -378 91 O ATOM 2062 CB GLU A1051 20.071 36.326 60.515 1.00 48.68 C ANISOU 2062 CB GLU A1051 5190 8499 4808 -96 -370 268 C ATOM 2063 CG GLU A1051 18.681 36.595 61.033 1.00 58.17 C ANISOU 2063 CG GLU A1051 6345 9755 6000 -38 -375 282 C ATOM 2064 CD GLU A1051 17.797 37.185 59.967 1.00 70.97 C ANISOU 2064 CD GLU A1051 7907 11522 7533 51 -393 339 C ATOM 2065 OE1 GLU A1051 18.329 38.120 59.302 1.00 70.27 O ANISOU 2065 OE1 GLU A1051 7882 11399 7418 109 -380 413 O ATOM 2066 OE2 GLU A1051 16.612 36.685 59.792 1.00 54.96 O ANISOU 2066 OE2 GLU A1051 5769 9660 5452 53 -417 309 O ATOM 2067 N VAL A1052 19.230 33.210 61.625 1.00 56.87 N ANISOU 2067 N VAL A1052 6174 9546 5888 -267 -367 76 N ATOM 2068 CA VAL A1052 18.381 32.047 61.244 1.00 57.58 C ANISOU 2068 CA VAL A1052 6228 9719 5931 -356 -362 -5 C ATOM 2069 C VAL A1052 17.226 32.600 60.414 1.00 58.94 C ANISOU 2069 C VAL A1052 6291 10082 6018 -335 -390 11 C ATOM 2070 O VAL A1052 16.417 33.337 60.969 1.00 78.90 O ANISOU 2070 O VAL A1052 8775 12661 8542 -274 -402 54 O ATOM 2071 CB VAL A1052 17.871 31.247 62.449 1.00 54.71 C ANISOU 2071 CB VAL A1052 5896 9291 5600 -422 -337 -53 C ATOM 2072 CG1 VAL A1052 17.005 30.076 62.012 1.00 48.00 C ANISOU 2072 CG1 VAL A1052 5031 8523 4684 -551 -315 -148 C ATOM 2073 CG2 VAL A1052 19.025 30.786 63.325 1.00 65.55 C ANISOU 2073 CG2 VAL A1052 7367 10495 7042 -408 -310 -46 C ATOM 2074 N GLU A1053 17.184 32.249 59.131 1.00 51.42 N ANISOU 2074 N GLU A1053 5298 9248 4991 -375 -399 -20 N ATOM 2075 CA GLU A1053 16.132 32.716 58.208 1.00 57.07 C ANISOU 2075 CA GLU A1053 5890 10194 5598 -350 -430 1 C ATOM 2076 C GLU A1053 14.760 32.102 58.573 1.00 60.87 C ANISOU 2076 C GLU A1053 6280 10833 6015 -439 -428 -67 C ATOM 2077 O GLU A1053 14.687 30.863 58.788 1.00 61.35 O ANISOU 2077 O GLU A1053 6382 10855 6071 -594 -392 -175 O ATOM 2078 CB GLU A1053 16.568 32.351 56.795 1.00 60.93 C ANISOU 2078 CB GLU A1053 6361 10770 6018 -397 -434 -29 C ATOM 2079 CG GLU A1053 16.009 33.291 55.762 1.00 63.65 C ANISOU 2079 CG GLU A1053 6604 11319 6261 -305 -472 50 C ATOM 2080 CD GLU A1053 16.203 32.802 54.352 1.00 69.64 C ANISOU 2080 CD GLU A1053 7317 12215 6926 -380 -477 3 C ATOM 2081 OE1 GLU A1053 17.281 32.223 54.082 1.00 61.77 O ANISOU 2081 OE1 GLU A1053 6408 11088 5974 -439 -452 -46 O ATOM 2082 OE2 GLU A1053 15.264 32.977 53.543 1.00 89.19 O ANISOU 2082 OE2 GLU A1053 9664 14949 9274 -375 -505 14 O ATOM 2083 N GLU A1054 13.701 32.928 58.592 1.00 57.27 N ANISOU 2083 N GLU A1054 5709 10559 5493 -345 -456 -9 N ATOM 2084 CA GLU A1054 12.315 32.460 58.886 1.00 65.52 C ANISOU 2084 CA GLU A1054 6627 11822 6446 -428 -457 -74 C ATOM 2085 C GLU A1054 11.785 31.515 57.788 1.00 61.55 C ANISOU 2085 C GLU A1054 6032 11546 5807 -596 -455 -177 C ATOM 2086 O GLU A1054 11.923 31.850 56.599 1.00 65.35 O ANISOU 2086 O GLU A1054 6457 12158 6215 -550 -480 -142 O ATOM 2087 CB GLU A1054 11.394 33.663 59.105 1.00 72.98 C ANISOU 2087 CB GLU A1054 7461 12928 7340 -244 -485 25 C ATOM 2088 CG GLU A1054 10.912 33.768 60.545 1.00 81.85 C ANISOU 2088 CG GLU A1054 8594 13980 8522 -230 -467 17 C ATOM 2089 CD GLU A1054 9.976 32.646 60.969 1.00 99.93 C ANISOU 2089 CD GLU A1054 10803 16421 10743 -427 -452 -105 C ATOM 2090 OE1 GLU A1054 9.068 32.224 60.147 1.00 91.09 O ANISOU 2090 OE1 GLU A1054 9531 15608 9470 -518 -465 -163 O ATOM 2091 OE2 GLU A1054 10.148 32.206 62.127 1.00 69.48 O ANISOU 2091 OE2 GLU A1054 7035 12391 6973 -501 -422 -144 O ATOM 2092 N TYR A 263 11.159 30.394 58.177 1.00 56.63 N ANISOU 2092 N TYR A 263 5314 10646 5555 -214 57 -307 N ATOM 2093 CA TYR A 263 10.710 29.296 57.271 1.00 52.14 C ANISOU 2093 CA TYR A 263 4813 10042 4955 -343 105 -237 C ATOM 2094 C TYR A 263 9.698 29.796 56.240 1.00 58.12 C ANISOU 2094 C TYR A 263 5509 10878 5695 -273 90 -343 C ATOM 2095 O TYR A 263 9.679 29.307 55.081 1.00 55.66 O ANISOU 2095 O TYR A 263 5283 10439 5427 -301 115 -290 O ATOM 2096 CB TYR A 263 10.031 28.183 58.053 1.00 57.56 C ANISOU 2096 CB TYR A 263 5464 10919 5485 -554 142 -199 C ATOM 2097 CG TYR A 263 9.791 26.917 57.283 1.00 61.06 C ANISOU 2097 CG TYR A 263 6012 11285 5901 -708 181 -101 C ATOM 2098 CD1 TYR A 263 10.837 26.228 56.681 1.00 72.12 C ANISOU 2098 CD1 TYR A 263 7582 12405 7415 -717 194 27 C ATOM 2099 CD2 TYR A 263 8.527 26.366 57.215 1.00 68.19 C ANISOU 2099 CD2 TYR A 263 6844 12409 6655 -850 200 -139 C ATOM 2100 CE1 TYR A 263 10.624 25.050 55.977 1.00 72.71 C ANISOU 2100 CE1 TYR A 263 7761 12398 7465 -850 219 108 C ATOM 2101 CE2 TYR A 263 8.294 25.184 56.527 1.00 73.55 C ANISOU 2101 CE2 TYR A 263 7630 13011 7305 -1003 228 -48 C ATOM 2102 CZ TYR A 263 9.345 24.521 55.907 1.00 79.03 C ANISOU 2102 CZ TYR A 263 8502 13403 8121 -999 234 74 C ATOM 2103 OH TYR A 263 9.131 23.346 55.247 1.00 76.14 O ANISOU 2103 OH TYR A 263 8251 12950 7727 -1140 249 155 O ATOM 2104 N LEU A 264 8.902 30.789 56.632 1.00 59.88 N ANISOU 2104 N LEU A 264 5588 11302 5859 -171 44 -498 N ATOM 2105 CA LEU A 264 7.934 31.464 55.712 1.00 68.78 C ANISOU 2105 CA LEU A 264 6647 12511 6975 -68 9 -620 C ATOM 2106 C LEU A 264 8.707 32.101 54.559 1.00 70.27 C ANISOU 2106 C LEU A 264 6951 12422 7326 66 -27 -582 C ATOM 2107 O LEU A 264 8.275 31.930 53.402 1.00 81.53 O ANISOU 2107 O LEU A 264 8409 13803 8766 63 -18 -579 O ATOM 2108 CB LEU A 264 7.138 32.503 56.517 1.00 68.52 C ANISOU 2108 CB LEU A 264 6443 12730 6861 49 -52 -803 C ATOM 2109 CG LEU A 264 6.553 33.708 55.783 1.00 66.01 C ANISOU 2109 CG LEU A 264 6071 12425 6582 248 -137 -949 C ATOM 2110 CD1 LEU A 264 5.432 33.291 54.856 1.00 80.26 C ANISOU 2110 CD1 LEU A 264 7830 14353 8312 196 -114 -990 C ATOM 2111 CD2 LEU A 264 6.022 34.732 56.767 1.00 70.19 C ANISOU 2111 CD2 LEU A 264 6448 13172 7046 384 -212 -1130 C ATOM 2112 N MET A 265 9.803 32.795 54.882 1.00 64.45 N ANISOU 2112 N MET A 265 6271 11520 6697 167 -67 -552 N ATOM 2113 CA MET A 265 10.585 33.572 53.896 1.00 62.50 C ANISOU 2113 CA MET A 265 6123 11030 6592 291 -117 -521 C ATOM 2114 C MET A 265 11.243 32.600 52.908 1.00 66.51 C ANISOU 2114 C MET A 265 6761 11349 7161 195 -51 -376 C ATOM 2115 O MET A 265 11.381 32.977 51.699 1.00 48.96 O ANISOU 2115 O MET A 265 4598 8993 5010 255 -75 -363 O ATOM 2116 CB MET A 265 11.647 34.433 54.592 1.00 60.07 C ANISOU 2116 CB MET A 265 5846 10608 6368 388 -172 -511 C ATOM 2117 CG MET A 265 11.122 35.759 55.094 1.00 59.87 C ANISOU 2117 CG MET A 265 5729 10689 6328 545 -276 -669 C ATOM 2118 SD MET A 265 10.165 36.620 53.842 1.00 85.76 S ANISOU 2118 SD MET A 265 8992 13970 9623 673 -361 -781 S ATOM 2119 CE MET A 265 11.381 36.846 52.535 1.00 74.86 C ANISOU 2119 CE MET A 265 7787 12262 8394 685 -378 -636 C ATOM 2120 N VAL A 266 11.632 31.416 53.402 1.00 61.46 N ANISOU 2120 N VAL A 266 6164 10697 6488 55 18 -275 N ATOM 2121 CA VAL A 266 12.234 30.332 52.567 1.00 61.03 C ANISOU 2121 CA VAL A 266 6234 10474 6480 -35 77 -149 C ATOM 2122 C VAL A 266 11.177 29.918 51.535 1.00 59.19 C ANISOU 2122 C VAL A 266 5988 10307 6193 -85 99 -183 C ATOM 2123 O VAL A 266 11.516 29.828 50.328 1.00 61.93 O ANISOU 2123 O VAL A 266 6413 10504 6610 -63 108 -140 O ATOM 2124 CB VAL A 266 12.697 29.138 53.427 1.00 57.24 C ANISOU 2124 CB VAL A 266 5803 9984 5961 -171 125 -51 C ATOM 2125 CG1 VAL A 266 13.176 27.977 52.576 1.00 56.85 C ANISOU 2125 CG1 VAL A 266 5880 9772 5948 -254 171 55 C ATOM 2126 CG2 VAL A 266 13.777 29.527 54.417 1.00 57.58 C ANISOU 2126 CG2 VAL A 266 5859 9961 6058 -121 105 -13 C ATOM 2127 N LEU A 267 9.943 29.685 51.997 1.00 59.71 N ANISOU 2127 N LEU A 267 5950 10606 6130 -156 107 -260 N ATOM 2128 CA LEU A 267 8.820 29.218 51.136 1.00 56.66 C ANISOU 2128 CA LEU A 267 5536 10322 5669 -225 131 -296 C ATOM 2129 C LEU A 267 8.410 30.332 50.175 1.00 61.38 C ANISOU 2129 C LEU A 267 6096 10908 6315 -75 76 -388 C ATOM 2130 O LEU A 267 8.027 29.985 49.060 1.00 76.95 O ANISOU 2130 O LEU A 267 8105 12843 8289 -105 95 -375 O ATOM 2131 CB LEU A 267 7.632 28.765 51.978 1.00 49.12 C ANISOU 2131 CB LEU A 267 4462 9652 4548 -345 149 -360 C ATOM 2132 CG LEU A 267 7.927 27.639 52.969 1.00 57.58 C ANISOU 2132 CG LEU A 267 5575 10750 5552 -520 189 -263 C ATOM 2133 CD1 LEU A 267 6.795 27.511 53.997 1.00 54.54 C ANISOU 2133 CD1 LEU A 267 5041 10690 4990 -625 192 -343 C ATOM 2134 CD2 LEU A 267 8.189 26.308 52.261 1.00 52.16 C ANISOU 2134 CD2 LEU A 267 5031 9909 4876 -662 233 -139 C ATOM 2135 N PHE A 268 8.543 31.604 50.564 1.00 58.02 N ANISOU 2135 N PHE A 268 5616 10496 5932 79 1 -472 N ATOM 2136 CA PHE A 268 8.232 32.732 49.644 1.00 59.30 C ANISOU 2136 CA PHE A 268 5767 10614 6149 229 -76 -551 C ATOM 2137 C PHE A 268 9.288 32.829 48.537 1.00 59.35 C ANISOU 2137 C PHE A 268 5910 10355 6282 256 -78 -445 C ATOM 2138 O PHE A 268 8.972 33.220 47.398 1.00 76.38 O ANISOU 2138 O PHE A 268 8090 12460 8468 305 -111 -464 O ATOM 2139 CB PHE A 268 8.141 34.065 50.384 1.00 57.89 C ANISOU 2139 CB PHE A 268 5513 10499 5984 390 -175 -670 C ATOM 2140 CG PHE A 268 7.920 35.238 49.464 1.00 61.81 C ANISOU 2140 CG PHE A 268 6026 10915 6545 545 -278 -740 C ATOM 2141 CD1 PHE A 268 6.750 35.350 48.725 1.00 57.39 C ANISOU 2141 CD1 PHE A 268 5402 10477 5926 574 -302 -829 C ATOM 2142 CD2 PHE A 268 8.891 36.213 49.319 1.00 68.67 C ANISOU 2142 CD2 PHE A 268 6980 11583 7528 652 -358 -709 C ATOM 2143 CE1 PHE A 268 6.544 36.437 47.900 1.00 55.06 C ANISOU 2143 CE1 PHE A 268 5131 10099 5688 718 -413 -890 C ATOM 2144 CE2 PHE A 268 8.693 37.291 48.471 1.00 68.58 C ANISOU 2144 CE2 PHE A 268 7001 11484 7572 780 -471 -762 C ATOM 2145 CZ PHE A 268 7.519 37.399 47.766 1.00 65.74 C ANISOU 2145 CZ PHE A 268 6582 11240 7157 817 -500 -852 C ATOM 2146 N ARG A 269 10.515 32.460 48.867 1.00 64.45 N ANISOU 2146 N ARG A 269 6640 10851 6994 219 -45 -337 N ATOM 2147 CA ARG A 269 11.606 32.482 47.865 1.00 66.50 C ANISOU 2147 CA ARG A 269 7017 10886 7361 234 -39 -237 C ATOM 2148 C ARG A 269 11.368 31.321 46.903 1.00 56.47 C ANISOU 2148 C ARG A 269 5799 9589 6067 124 35 -180 C ATOM 2149 O ARG A 269 11.503 31.555 45.702 1.00 60.44 O ANISOU 2149 O ARG A 269 6348 9997 6616 151 23 -161 O ATOM 2150 CB ARG A 269 12.994 32.417 48.529 1.00 61.35 C ANISOU 2150 CB ARG A 269 6426 10105 6777 234 -27 -149 C ATOM 2151 CG ARG A 269 14.144 32.704 47.568 1.00 69.47 C ANISOU 2151 CG ARG A 269 7550 10939 7906 266 -38 -66 C ATOM 2152 CD ARG A 269 15.390 33.360 48.153 1.00 79.14 C ANISOU 2152 CD ARG A 269 8806 12059 9201 320 -75 -20 C ATOM 2153 NE ARG A 269 15.999 32.497 49.161 1.00 88.80 N ANISOU 2153 NE ARG A 269 10038 13286 10413 259 -17 35 N ATOM 2154 CZ ARG A 269 16.066 32.757 50.474 1.00 82.66 C ANISOU 2154 CZ ARG A 269 9213 12578 9614 276 -36 8 C ATOM 2155 NH1 ARG A 269 15.628 33.906 50.964 1.00 76.98 N ANISOU 2155 NH1 ARG A 269 8433 11926 8887 364 -115 -82 N ATOM 2156 NH2 ARG A 269 16.598 31.868 51.295 1.00 80.16 N ANISOU 2156 NH2 ARG A 269 8913 12259 9282 207 14 69 N ATOM 2157 N ILE A 270 11.120 30.119 47.431 1.00 55.22 N ANISOU 2157 N ILE A 270 5641 9498 5839 -1 102 -146 N ATOM 2158 CA ILE A 270 10.915 28.908 46.582 1.00 57.40 C ANISOU 2158 CA ILE A 270 5983 9735 6090 -115 166 -90 C ATOM 2159 C ILE A 270 9.757 29.201 45.638 1.00 60.00 C ANISOU 2159 C ILE A 270 6260 10162 6373 -103 151 -166 C ATOM 2160 O ILE A 270 9.832 28.824 44.472 1.00 56.85 O ANISOU 2160 O ILE A 270 5923 9675 6000 -127 175 -131 O ATOM 2161 CB ILE A 270 10.600 27.689 47.460 1.00 56.49 C ANISOU 2161 CB ILE A 270 5874 9703 5887 -260 214 -55 C ATOM 2162 CG1 ILE A 270 11.731 27.407 48.446 1.00 56.80 C ANISOU 2162 CG1 ILE A 270 5963 9647 5969 -267 219 18 C ATOM 2163 CG2 ILE A 270 10.263 26.486 46.595 1.00 49.91 C ANISOU 2163 CG2 ILE A 270 5113 8830 5018 -379 262 -10 C ATOM 2164 CD1 ILE A 270 11.535 26.144 49.238 1.00 62.10 C ANISOU 2164 CD1 ILE A 270 6669 10367 6559 -421 251 73 C ATOM 2165 N THR A 271 8.728 29.837 46.192 1.00 70.73 N ANISOU 2165 N THR A 271 7503 11712 7659 -65 111 -272 N ATOM 2166 CA THR A 271 7.478 30.208 45.500 1.00 61.94 C ANISOU 2166 CA THR A 271 6313 10737 6485 -39 85 -367 C ATOM 2167 C THR A 271 7.758 31.278 44.432 1.00 58.66 C ANISOU 2167 C THR A 271 5931 10196 6161 92 18 -383 C ATOM 2168 O THR A 271 7.209 31.153 43.336 1.00 58.72 O ANISOU 2168 O THR A 271 5947 10207 6154 77 22 -394 O ATOM 2169 CB THR A 271 6.443 30.625 46.545 1.00 63.33 C ANISOU 2169 CB THR A 271 6343 11164 6554 -17 53 -487 C ATOM 2170 OG1 THR A 271 5.957 29.399 47.076 1.00 65.85 O ANISOU 2170 OG1 THR A 271 6643 11611 6763 -192 124 -456 O ATOM 2171 CG2 THR A 271 5.275 31.397 45.981 1.00 89.27 C ANISOU 2171 CG2 THR A 271 9531 14595 9792 72 -4 -614 C ATOM 2172 N SER A 272 8.563 32.297 44.715 1.00 45.41 N ANISOU 2172 N SER A 272 4276 8411 4567 208 -48 -381 N ATOM 2173 CA SER A 272 8.799 33.397 43.751 1.00 44.98 C ANISOU 2173 CA SER A 272 4263 8239 4589 319 -133 -391 C ATOM 2174 C SER A 272 9.716 32.918 42.626 1.00 46.51 C ANISOU 2174 C SER A 272 4568 8255 4849 261 -87 -275 C ATOM 2175 O SER A 272 9.478 33.279 41.474 1.00 49.99 O ANISOU 2175 O SER A 272 5033 8652 5306 284 -121 -276 O ATOM 2176 CB SER A 272 9.367 34.579 44.441 1.00 52.53 C ANISOU 2176 CB SER A 272 5219 9137 5604 439 -226 -419 C ATOM 2177 OG SER A 272 8.513 34.982 45.483 1.00 52.01 O ANISOU 2177 OG SER A 272 5040 9250 5468 500 -267 -541 O ATOM 2178 N VAL A 273 10.724 32.122 42.954 1.00 48.59 N ANISOU 2178 N VAL A 273 4890 8427 5143 191 -18 -183 N ATOM 2179 CA VAL A 273 11.668 31.570 41.945 1.00 54.21 C ANISOU 2179 CA VAL A 273 5696 8990 5909 142 29 -86 C ATOM 2180 C VAL A 273 10.866 30.649 41.016 1.00 54.40 C ANISOU 2180 C VAL A 273 5726 9063 5878 57 86 -92 C ATOM 2181 O VAL A 273 10.979 30.814 39.781 1.00 59.97 O ANISOU 2181 O VAL A 273 6470 9706 6610 62 79 -71 O ATOM 2182 CB VAL A 273 12.881 30.869 42.596 1.00 57.39 C ANISOU 2182 CB VAL A 273 6153 9302 6351 102 83 -3 C ATOM 2183 CG1 VAL A 273 13.723 30.118 41.565 1.00 71.29 C ANISOU 2183 CG1 VAL A 273 7994 10945 8148 55 139 72 C ATOM 2184 CG2 VAL A 273 13.741 31.869 43.364 1.00 51.20 C ANISOU 2184 CG2 VAL A 273 5367 8462 5624 184 23 7 C ATOM 2185 N PHE A 274 10.043 29.763 41.580 1.00 45.42 N ANISOU 2185 N PHE A 274 4550 8047 4659 -24 134 -121 N ATOM 2186 CA PHE A 274 9.355 28.695 40.809 1.00 44.72 C ANISOU 2186 CA PHE A 274 4482 7999 4511 -131 194 -116 C ATOM 2187 C PHE A 274 8.397 29.333 39.819 1.00 44.77 C ANISOU 2187 C PHE A 274 4440 8076 4491 -91 154 -180 C ATOM 2188 O PHE A 274 8.455 29.008 38.631 1.00 38.23 O ANISOU 2188 O PHE A 274 3662 7186 3676 -123 177 -151 O ATOM 2189 CB PHE A 274 8.627 27.730 41.735 1.00 47.08 C ANISOU 2189 CB PHE A 274 4747 8427 4714 -243 236 -130 C ATOM 2190 CG PHE A 274 7.968 26.535 41.087 1.00 53.59 C ANISOU 2190 CG PHE A 274 5608 9284 5470 -375 291 -116 C ATOM 2191 CD1 PHE A 274 6.721 26.647 40.486 1.00 57.00 C ANISOU 2191 CD1 PHE A 274 5972 9858 5826 -400 285 -184 C ATOM 2192 CD2 PHE A 274 8.558 25.276 41.147 1.00 57.68 C ANISOU 2192 CD2 PHE A 274 6228 9695 5992 -474 339 -39 C ATOM 2193 CE1 PHE A 274 6.094 25.532 39.945 1.00 62.05 C ANISOU 2193 CE1 PHE A 274 6646 10534 6395 -535 332 -169 C ATOM 2194 CE2 PHE A 274 7.942 24.162 40.591 1.00 61.35 C ANISOU 2194 CE2 PHE A 274 6739 10178 6392 -601 376 -26 C ATOM 2195 CZ PHE A 274 6.702 24.292 40.004 1.00 70.63 C ANISOU 2195 CZ PHE A 274 7846 11500 7490 -640 376 -89 C ATOM 2196 N TYR A 275 7.561 30.234 40.315 1.00 52.37 N ANISOU 2196 N TYR A 275 5309 9172 5416 -16 89 -271 N ATOM 2197 CA TYR A 275 6.479 30.873 39.531 1.00 51.12 C ANISOU 2197 CA TYR A 275 5090 9110 5220 35 36 -352 C ATOM 2198 C TYR A 275 7.102 31.883 38.564 1.00 50.97 C ANISOU 2198 C TYR A 275 5130 8943 5290 129 -36 -324 C ATOM 2199 O TYR A 275 6.459 32.145 37.529 1.00 57.39 O ANISOU 2199 O TYR A 275 5936 9782 6087 143 -66 -352 O ATOM 2200 CB TYR A 275 5.411 31.497 40.445 1.00 55.28 C ANISOU 2200 CB TYR A 275 5490 9839 5673 101 -19 -475 C ATOM 2201 CG TYR A 275 4.375 30.525 40.973 1.00 57.50 C ANISOU 2201 CG TYR A 275 5690 10328 5826 -18 44 -517 C ATOM 2202 CD1 TYR A 275 4.645 29.669 42.031 1.00 62.60 C ANISOU 2202 CD1 TYR A 275 6340 11011 6432 -123 105 -476 C ATOM 2203 CD2 TYR A 275 3.114 30.456 40.428 1.00 56.29 C ANISOU 2203 CD2 TYR A 275 5458 10343 5584 -38 39 -595 C ATOM 2204 CE1 TYR A 275 3.691 28.790 42.523 1.00 62.27 C ANISOU 2204 CE1 TYR A 275 6230 11167 6260 -257 154 -505 C ATOM 2205 CE2 TYR A 275 2.157 29.571 40.899 1.00 59.96 C ANISOU 2205 CE2 TYR A 275 5846 11017 5918 -168 95 -630 C ATOM 2206 CZ TYR A 275 2.438 28.727 41.947 1.00 58.19 C ANISOU 2206 CZ TYR A 275 5631 10827 5649 -288 152 -581 C ATOM 2207 OH TYR A 275 1.488 27.857 42.418 1.00 67.90 O ANISOU 2207 OH TYR A 275 6790 12270 6736 -441 198 -606 O ATOM 2208 N MET A 276 8.301 32.402 38.849 1.00 56.10 N ANISOU 2208 N MET A 276 5838 9450 6024 178 -64 -265 N ATOM 2209 CA MET A 276 8.950 33.365 37.912 1.00 60.51 C ANISOU 2209 CA MET A 276 6461 9873 6657 240 -140 -224 C ATOM 2210 C MET A 276 9.732 32.606 36.834 1.00 57.85 C ANISOU 2210 C MET A 276 6202 9433 6346 151 -66 -129 C ATOM 2211 O MET A 276 9.790 33.134 35.712 1.00 67.63 O ANISOU 2211 O MET A 276 7475 10619 7603 163 -112 -107 O ATOM 2212 CB MET A 276 9.866 34.353 38.641 1.00 61.59 C ANISOU 2212 CB MET A 276 6624 9916 6861 322 -216 -204 C ATOM 2213 CG MET A 276 9.083 35.365 39.473 1.00 67.65 C ANISOU 2213 CG MET A 276 7321 10771 7610 440 -322 -315 C ATOM 2214 SD MET A 276 8.196 36.609 38.503 1.00 74.49 S ANISOU 2214 SD MET A 276 8187 11639 8477 548 -470 -387 S ATOM 2215 CE MET A 276 9.566 37.659 38.011 1.00 84.11 C ANISOU 2215 CE MET A 276 9528 12635 9793 573 -568 -284 C ATOM 2216 N LEU A 277 10.281 31.423 37.143 1.00 55.18 N ANISOU 2216 N LEU A 277 5891 9069 6002 69 33 -80 N ATOM 2217 CA LEU A 277 11.040 30.613 36.146 1.00 53.78 C ANISOU 2217 CA LEU A 277 5784 8804 5846 0 102 -9 C ATOM 2218 C LEU A 277 10.116 30.069 35.045 1.00 54.57 C ANISOU 2218 C LEU A 277 5879 8964 5892 -59 133 -35 C ATOM 2219 O LEU A 277 10.638 29.769 33.961 1.00 66.85 O ANISOU 2219 O LEU A 277 7482 10455 7463 -94 163 8 O ATOM 2220 CB LEU A 277 11.738 29.440 36.832 1.00 44.39 C ANISOU 2220 CB LEU A 277 4630 7574 4661 -57 184 32 C ATOM 2221 CG LEU A 277 13.082 29.724 37.465 1.00 46.57 C ANISOU 2221 CG LEU A 277 4935 7756 5002 -16 176 87 C ATOM 2222 CD1 LEU A 277 13.820 28.422 37.734 1.00 46.91 C ANISOU 2222 CD1 LEU A 277 5029 7741 5050 -70 253 130 C ATOM 2223 CD2 LEU A 277 13.921 30.634 36.598 1.00 49.49 C ANISOU 2223 CD2 LEU A 277 5331 8052 5421 21 129 129 C ATOM 2224 N GLN A 278 8.814 29.891 35.312 1.00 66.19 N ANISOU 2224 N GLN A 278 7288 10566 7292 -77 132 -106 N ATOM 2225 CA GLN A 278 7.870 29.348 34.279 1.00 64.57 C ANISOU 2225 CA GLN A 278 7073 10430 7027 -141 162 -133 C ATOM 2226 C GLN A 278 6.986 30.477 33.717 1.00 47.76 C ANISOU 2226 C GLN A 278 4891 8371 4882 -66 71 -192 C ATOM 2227 O GLN A 278 6.277 30.211 32.741 1.00 43.95 O ANISOU 2227 O GLN A 278 4401 7940 4357 -108 83 -211 O ATOM 2228 CB GLN A 278 7.085 28.128 34.789 1.00 56.21 C ANISOU 2228 CB GLN A 278 5995 9472 5888 -245 232 -158 C ATOM 2229 CG GLN A 278 6.152 28.393 35.958 1.00 53.88 C ANISOU 2229 CG GLN A 278 5606 9334 5529 -231 204 -230 C ATOM 2230 CD GLN A 278 5.443 27.130 36.372 1.00 64.93 C ANISOU 2230 CD GLN A 278 6997 10836 6836 -368 272 -237 C ATOM 2231 OE1 GLN A 278 5.771 26.039 35.895 1.00 62.81 O ANISOU 2231 OE1 GLN A 278 6811 10488 6566 -464 331 -184 O ATOM 2232 NE2 GLN A 278 4.479 27.278 37.279 1.00 83.63 N ANISOU 2232 NE2 GLN A 278 9265 13387 9121 -379 254 -306 N ATOM 2233 N LEU A 279 7.128 31.706 34.212 1.00 42.70 N ANISOU 2233 N LEU A 279 4229 7712 4280 43 -25 -216 N ATOM 2234 CA LEU A 279 6.393 32.873 33.679 1.00 48.39 C ANISOU 2234 CA LEU A 279 4919 8469 4997 134 -140 -272 C ATOM 2235 C LEU A 279 6.743 33.106 32.211 1.00 56.52 C ANISOU 2235 C LEU A 279 6013 9409 6052 107 -161 -212 C ATOM 2236 O LEU A 279 5.828 33.290 31.409 1.00 65.82 O ANISOU 2236 O LEU A 279 7165 10653 7188 113 -196 -252 O ATOM 2237 CB LEU A 279 6.665 34.116 34.524 1.00 59.64 C ANISOU 2237 CB LEU A 279 6334 9856 6468 258 -253 -303 C ATOM 2238 CG LEU A 279 6.042 35.415 34.007 1.00 65.69 C ANISOU 2238 CG LEU A 279 7093 10622 7242 371 -402 -360 C ATOM 2239 CD1 LEU A 279 4.626 35.595 34.523 1.00 60.26 C ANISOU 2239 CD1 LEU A 279 6293 10120 6482 445 -443 -496 C ATOM 2240 CD2 LEU A 279 6.897 36.615 34.395 1.00 80.13 C ANISOU 2240 CD2 LEU A 279 8981 12315 9147 460 -519 -332 C ATOM 2241 N PRO A 280 8.026 33.124 31.770 1.00 56.23 N ANISOU 2241 N PRO A 280 6053 9238 6072 74 -144 -117 N ATOM 2242 CA PRO A 280 8.331 33.326 30.352 1.00 53.86 C ANISOU 2242 CA PRO A 280 5802 8881 5778 32 -161 -61 C ATOM 2243 C PRO A 280 7.616 32.272 29.501 1.00 49.23 C ANISOU 2243 C PRO A 280 5199 8372 5130 -52 -74 -80 C ATOM 2244 O PRO A 280 7.088 32.599 28.491 1.00 47.83 O ANISOU 2244 O PRO A 280 5023 8219 4929 -59 -115 -86 O ATOM 2245 CB PRO A 280 9.852 33.181 30.284 1.00 52.72 C ANISOU 2245 CB PRO A 280 5718 8626 5684 -7 -122 29 C ATOM 2246 CG PRO A 280 10.299 33.580 31.648 1.00 59.09 C ANISOU 2246 CG PRO A 280 6516 9402 6531 56 -151 22 C ATOM 2247 CD PRO A 280 9.247 32.992 32.568 1.00 62.17 C ANISOU 2247 CD PRO A 280 6840 9904 6877 71 -111 -62 C ATOM 2248 N TYR A 281 7.592 31.038 29.989 1.00 50.25 N ANISOU 2248 N TYR A 281 5320 8536 5234 -115 34 -90 N ATOM 2249 CA TYR A 281 7.023 29.864 29.285 1.00 46.24 C ANISOU 2249 CA TYR A 281 4812 8086 4668 -212 123 -104 C ATOM 2250 C TYR A 281 5.519 30.022 29.153 1.00 50.30 C ANISOU 2250 C TYR A 281 5257 8741 5113 -205 90 -182 C ATOM 2251 O TYR A 281 4.993 29.596 28.125 1.00 55.86 O ANISOU 2251 O TYR A 281 5963 9485 5773 -265 117 -189 O ATOM 2252 CB TYR A 281 7.365 28.573 30.019 1.00 51.72 C ANISOU 2252 CB TYR A 281 5530 8767 5353 -279 220 -94 C ATOM 2253 CG TYR A 281 6.624 27.359 29.541 1.00 46.66 C ANISOU 2253 CG TYR A 281 4896 8186 4644 -381 294 -117 C ATOM 2254 CD1 TYR A 281 7.118 26.574 28.529 1.00 53.73 C ANISOU 2254 CD1 TYR A 281 5852 9021 5541 -443 351 -87 C ATOM 2255 CD2 TYR A 281 5.440 26.981 30.123 1.00 56.24 C ANISOU 2255 CD2 TYR A 281 6055 9529 5784 -423 303 -174 C ATOM 2256 CE1 TYR A 281 6.436 25.454 28.089 1.00 55.13 C ANISOU 2256 CE1 TYR A 281 6048 9242 5656 -540 408 -111 C ATOM 2257 CE2 TYR A 281 4.748 25.862 29.697 1.00 58.02 C ANISOU 2257 CE2 TYR A 281 6294 9809 5938 -535 363 -190 C ATOM 2258 CZ TYR A 281 5.250 25.089 28.683 1.00 47.79 C ANISOU 2258 CZ TYR A 281 5073 8429 4653 -593 413 -158 C ATOM 2259 OH TYR A 281 4.577 23.978 28.282 1.00 47.06 O ANISOU 2259 OH TYR A 281 5006 8380 4492 -705 463 -175 O ATOM 2260 N ILE A 282 4.850 30.615 30.143 1.00 61.18 N ANISOU 2260 N ILE A 282 6567 10202 6474 -132 32 -247 N ATOM 2261 CA ILE A 282 3.371 30.800 29.994 1.00 63.32 C ANISOU 2261 CA ILE A 282 6753 10638 6667 -114 -4 -338 C ATOM 2262 C ILE A 282 3.122 31.963 29.029 1.00 48.81 C ANISOU 2262 C ILE A 282 4921 8774 4850 -32 -117 -346 C ATOM 2263 O ILE A 282 2.201 31.837 28.244 1.00 55.62 O ANISOU 2263 O ILE A 282 5749 9727 5655 -55 -123 -383 O ATOM 2264 CB ILE A 282 2.587 30.935 31.324 1.00 62.43 C ANISOU 2264 CB ILE A 282 6544 10670 6504 -69 -24 -425 C ATOM 2265 CG1 ILE A 282 3.028 32.126 32.173 1.00 74.94 C ANISOU 2265 CG1 ILE A 282 8119 12204 8150 67 -123 -447 C ATOM 2266 CG2 ILE A 282 2.654 29.626 32.090 1.00 62.80 C ANISOU 2266 CG2 ILE A 282 6594 10760 6508 -189 86 -407 C ATOM 2267 CD1 ILE A 282 2.157 32.367 33.400 1.00112.07 C ANISOU 2267 CD1 ILE A 282 12709 17079 12792 127 -153 -555 C ATOM 2268 N ILE A 283 3.925 33.019 29.059 1.00 47.60 N ANISOU 2268 N ILE A 283 4817 8496 4771 49 -209 -306 N ATOM 2269 CA ILE A 283 3.779 34.149 28.101 1.00 51.26 C ANISOU 2269 CA ILE A 283 5311 8909 5255 112 -337 -296 C ATOM 2270 C ILE A 283 3.959 33.584 26.686 1.00 49.51 C ANISOU 2270 C ILE A 283 5134 8661 5013 5 -279 -232 C ATOM 2271 O ILE A 283 3.136 33.897 25.811 1.00 51.94 O ANISOU 2271 O ILE A 283 5424 9025 5283 14 -334 -260 O ATOM 2272 CB ILE A 283 4.769 35.284 28.422 1.00 60.84 C ANISOU 2272 CB ILE A 283 6590 9976 6548 187 -445 -246 C ATOM 2273 CG1 ILE A 283 4.499 35.878 29.803 1.00 63.48 C ANISOU 2273 CG1 ILE A 283 6876 10345 6896 304 -511 -325 C ATOM 2274 CG2 ILE A 283 4.765 36.364 27.351 1.00 58.86 C ANISOU 2274 CG2 ILE A 283 6400 9648 6316 220 -583 -209 C ATOM 2275 CD1 ILE A 283 5.729 36.502 30.445 1.00 85.56 C ANISOU 2275 CD1 ILE A 283 9738 12999 9769 336 -557 -264 C ATOM 2276 N TYR A 284 4.963 32.744 26.457 1.00 46.76 N ANISOU 2276 N TYR A 284 4837 8243 4685 -89 -173 -159 N ATOM 2277 CA TYR A 284 5.203 32.212 25.094 1.00 50.98 C ANISOU 2277 CA TYR A 284 5409 8762 5197 -186 -118 -108 C ATOM 2278 C TYR A 284 4.047 31.279 24.744 1.00 50.17 C ANISOU 2278 C TYR A 284 5256 8786 5018 -246 -48 -169 C ATOM 2279 O TYR A 284 3.595 31.337 23.588 1.00 55.44 O ANISOU 2279 O TYR A 284 5926 9487 5650 -282 -64 -165 O ATOM 2280 CB TYR A 284 6.541 31.493 24.942 1.00 49.41 C ANISOU 2280 CB TYR A 284 5265 8477 5030 -258 -24 -35 C ATOM 2281 CG TYR A 284 6.728 30.930 23.552 1.00 54.54 C ANISOU 2281 CG TYR A 284 5940 9134 5646 -349 30 -3 C ATOM 2282 CD1 TYR A 284 7.196 31.721 22.504 1.00 55.66 C ANISOU 2282 CD1 TYR A 284 6115 9240 5793 -368 -37 57 C ATOM 2283 CD2 TYR A 284 6.429 29.605 23.274 1.00 52.20 C ANISOU 2283 CD2 TYR A 284 5640 8884 5307 -426 142 -32 C ATOM 2284 CE1 TYR A 284 7.367 31.215 21.223 1.00 52.16 C ANISOU 2284 CE1 TYR A 284 5685 8824 5309 -456 14 82 C ATOM 2285 CE2 TYR A 284 6.602 29.080 21.999 1.00 60.52 C ANISOU 2285 CE2 TYR A 284 6716 9951 6328 -503 190 -14 C ATOM 2286 CZ TYR A 284 7.050 29.890 20.967 1.00 50.90 C ANISOU 2286 CZ TYR A 284 5514 8714 5110 -516 131 39 C ATOM 2287 OH TYR A 284 7.167 29.350 19.727 1.00 44.57 O ANISOU 2287 OH TYR A 284 4723 7946 4265 -596 182 49 O ATOM 2288 N PHE A 285 3.582 30.495 25.714 1.00 41.52 N ANISOU 2288 N PHE A 285 4118 7763 3891 -264 18 -220 N ATOM 2289 CA PHE A 285 2.488 29.517 25.535 1.00 47.39 C ANISOU 2289 CA PHE A 285 4816 8638 4550 -344 87 -275 C ATOM 2290 C PHE A 285 1.205 30.249 25.154 1.00 54.50 C ANISOU 2290 C PHE A 285 5643 9666 5398 -288 1 -346 C ATOM 2291 O PHE A 285 0.366 29.667 24.450 1.00 60.66 O ANISOU 2291 O PHE A 285 6394 10544 6108 -359 40 -375 O ATOM 2292 CB PHE A 285 2.271 28.699 26.808 1.00 48.53 C ANISOU 2292 CB PHE A 285 4932 8842 4666 -381 152 -307 C ATOM 2293 CG PHE A 285 1.397 27.489 26.637 1.00 51.53 C ANISOU 2293 CG PHE A 285 5292 9331 4956 -504 233 -339 C ATOM 2294 CD1 PHE A 285 1.368 26.788 25.442 1.00 47.99 C ANISOU 2294 CD1 PHE A 285 4889 8860 4483 -592 284 -316 C ATOM 2295 CD2 PHE A 285 0.633 27.016 27.687 1.00 51.75 C ANISOU 2295 CD2 PHE A 285 5258 9487 4916 -545 257 -390 C ATOM 2296 CE1 PHE A 285 0.582 25.659 25.289 1.00 43.09 C ANISOU 2296 CE1 PHE A 285 4263 8329 3778 -715 350 -342 C ATOM 2297 CE2 PHE A 285 -0.155 25.885 27.523 1.00 48.47 C ANISOU 2297 CE2 PHE A 285 4835 9172 4409 -681 323 -409 C ATOM 2298 CZ PHE A 285 -0.186 25.214 26.321 1.00 41.38 C ANISOU 2298 CZ PHE A 285 3992 8235 3492 -765 367 -385 C ATOM 2299 N LEU A 286 1.034 31.477 25.638 1.00 52.21 N ANISOU 2299 N LEU A 286 5321 9378 5138 -158 -117 -380 N ATOM 2300 CA LEU A 286 -0.174 32.266 25.297 1.00 53.03 C ANISOU 2300 CA LEU A 286 5354 9598 5195 -74 -221 -461 C ATOM 2301 C LEU A 286 0.038 32.863 23.906 1.00 48.75 C ANISOU 2301 C LEU A 286 4874 8972 4675 -75 -291 -404 C ATOM 2302 O LEU A 286 -0.854 32.728 23.098 1.00 46.49 O ANISOU 2302 O LEU A 286 4551 8783 4329 -100 -298 -437 O ATOM 2303 CB LEU A 286 -0.436 33.342 26.347 1.00 50.80 C ANISOU 2303 CB LEU A 286 5022 9343 4936 78 -338 -533 C ATOM 2304 CG LEU A 286 -0.897 32.829 27.710 1.00 60.37 C ANISOU 2304 CG LEU A 286 6145 10692 6099 79 -280 -608 C ATOM 2305 CD1 LEU A 286 -0.843 33.945 28.737 1.00 59.92 C ANISOU 2305 CD1 LEU A 286 6056 10627 6081 237 -396 -670 C ATOM 2306 CD2 LEU A 286 -2.303 32.237 27.657 1.00 74.41 C ANISOU 2306 CD2 LEU A 286 7811 12701 7760 33 -241 -701 C ATOM 2307 N LEU A 287 1.170 33.508 23.663 1.00 49.11 N ANISOU 2307 N LEU A 287 5007 8856 4797 -57 -343 -319 N ATOM 2308 CA LEU A 287 1.446 34.147 22.352 1.00 56.09 C ANISOU 2308 CA LEU A 287 5954 9662 5692 -76 -421 -251 C ATOM 2309 C LEU A 287 1.409 33.123 21.212 1.00 59.01 C ANISOU 2309 C LEU A 287 6335 10073 6013 -212 -308 -217 C ATOM 2310 O LEU A 287 0.741 33.384 20.217 1.00 52.81 O ANISOU 2310 O LEU A 287 5540 9336 5187 -223 -359 -224 O ATOM 2311 CB LEU A 287 2.816 34.812 22.410 1.00 57.44 C ANISOU 2311 CB LEU A 287 6215 9670 5940 -71 -471 -155 C ATOM 2312 CG LEU A 287 2.924 35.959 23.394 1.00 53.39 C ANISOU 2312 CG LEU A 287 5712 9092 5479 61 -605 -181 C ATOM 2313 CD1 LEU A 287 4.335 36.514 23.353 1.00 55.23 C ANISOU 2313 CD1 LEU A 287 6037 9170 5775 32 -644 -73 C ATOM 2314 CD2 LEU A 287 1.893 37.036 23.088 1.00 51.96 C ANISOU 2314 CD2 LEU A 287 5518 8941 5283 175 -777 -243 C ATOM 2315 N GLU A 288 2.124 32.008 21.335 1.00 59.27 N ANISOU 2315 N GLU A 288 6389 10080 6050 -307 -169 -184 N ATOM 2316 CA GLU A 288 2.111 31.019 20.234 1.00 57.08 C ANISOU 2316 CA GLU A 288 6126 9835 5724 -428 -69 -163 C ATOM 2317 C GLU A 288 0.684 30.467 20.055 1.00 64.34 C ANISOU 2317 C GLU A 288 6977 10907 6563 -455 -42 -244 C ATOM 2318 O GLU A 288 0.245 30.384 18.899 1.00 79.75 O ANISOU 2318 O GLU A 288 8927 12903 8469 -507 -45 -239 O ATOM 2319 CB GLU A 288 3.203 29.979 20.447 1.00 52.62 C ANISOU 2319 CB GLU A 288 5606 9200 5184 -501 53 -125 C ATOM 2320 CG GLU A 288 3.406 29.065 19.255 1.00 64.43 C ANISOU 2320 CG GLU A 288 7129 10710 6641 -609 140 -106 C ATOM 2321 CD GLU A 288 2.445 27.891 19.238 1.00 79.66 C ANISOU 2321 CD GLU A 288 9031 12731 8503 -680 224 -169 C ATOM 2322 OE1 GLU A 288 2.560 27.030 18.330 1.00 74.88 O ANISOU 2322 OE1 GLU A 288 8453 12134 7863 -768 297 -167 O ATOM 2323 OE2 GLU A 288 1.570 27.856 20.129 1.00 74.30 O ANISOU 2323 OE2 GLU A 288 8302 12126 7800 -651 212 -224 O ATOM 2324 N SER A 289 -0.037 30.149 21.130 1.00 73.36 N ANISOU 2324 N SER A 289 8055 12139 7677 -428 -20 -316 N ATOM 2325 CA SER A 289 -1.419 29.618 21.007 1.00 61.87 C ANISOU 2325 CA SER A 289 6521 10857 6128 -469 5 -395 C ATOM 2326 C SER A 289 -2.305 30.652 20.317 1.00 57.77 C ANISOU 2326 C SER A 289 5956 10411 5582 -388 -117 -433 C ATOM 2327 O SER A 289 -3.177 30.235 19.558 1.00 67.75 O ANISOU 2327 O SER A 289 7181 11786 6772 -448 -94 -465 O ATOM 2328 CB SER A 289 -1.960 29.239 22.354 1.00 70.18 C ANISOU 2328 CB SER A 289 7507 12011 7146 -458 36 -461 C ATOM 2329 OG SER A 289 -1.288 28.093 22.836 1.00 61.26 O ANISOU 2329 OG SER A 289 6429 10820 6025 -558 149 -423 O ATOM 2330 N SER A 290 -2.033 31.943 20.527 1.00 56.38 N ANISOU 2330 N SER A 290 5795 10161 5464 -259 -250 -425 N ATOM 2331 CA SER A 290 -2.793 33.070 19.930 1.00 65.05 C ANISOU 2331 CA SER A 290 6869 11296 6549 -157 -402 -459 C ATOM 2332 C SER A 290 -2.261 33.358 18.522 1.00 71.39 C ANISOU 2332 C SER A 290 7755 12000 7367 -218 -437 -365 C ATOM 2333 O SER A 290 -2.823 34.233 17.855 1.00 74.35 O ANISOU 2333 O SER A 290 8131 12389 7730 -154 -568 -375 O ATOM 2334 CB SER A 290 -2.716 34.298 20.809 1.00 79.21 C ANISOU 2334 CB SER A 290 8660 13038 8399 5 -546 -495 C ATOM 2335 OG SER A 290 -3.363 34.100 22.062 1.00 86.61 O ANISOU 2335 OG SER A 290 9499 14105 9303 67 -523 -599 O ATOM 2336 N ARG A 291 -1.189 32.666 18.114 1.00 72.79 N ANISOU 2336 N ARG A 291 8000 12088 7569 -333 -331 -281 N ATOM 2337 CA ARG A 291 -0.513 32.808 16.799 1.00 60.73 C ANISOU 2337 CA ARG A 291 6544 10486 6044 -415 -341 -188 C ATOM 2338 C ARG A 291 0.005 34.242 16.649 1.00 69.59 C ANISOU 2338 C ARG A 291 7729 11490 7220 -339 -509 -126 C ATOM 2339 O ARG A 291 0.113 34.704 15.499 1.00 98.75 O ANISOU 2339 O ARG A 291 11466 15157 10894 -386 -576 -63 O ATOM 2340 CB ARG A 291 -1.460 32.388 15.664 1.00 62.65 C ANISOU 2340 CB ARG A 291 6752 10844 6207 -483 -320 -214 C ATOM 2341 CG ARG A 291 -1.292 30.954 15.185 1.00 52.86 C ANISOU 2341 CG ARG A 291 5512 9648 4923 -622 -153 -212 C ATOM 2342 CD ARG A 291 -1.579 29.952 16.269 1.00 55.24 C ANISOU 2342 CD ARG A 291 5774 10002 5211 -639 -46 -275 C ATOM 2343 NE ARG A 291 -1.607 28.597 15.754 1.00 52.80 N ANISOU 2343 NE ARG A 291 5476 9730 4852 -769 86 -282 N ATOM 2344 CZ ARG A 291 -1.480 27.515 16.511 1.00 57.06 C ANISOU 2344 CZ ARG A 291 6024 10270 5386 -822 189 -307 C ATOM 2345 NH1 ARG A 291 -1.283 27.626 17.808 1.00 68.26 N ANISOU 2345 NH1 ARG A 291 7430 11662 6842 -763 184 -321 N ATOM 2346 NH2 ARG A 291 -1.530 26.314 15.977 1.00 56.29 N ANISOU 2346 NH2 ARG A 291 5953 10191 5243 -938 290 -316 N ATOM 2347 N VAL A 292 0.302 34.931 17.755 1.00 74.79 N ANISOU 2347 N VAL A 292 8398 12080 7938 -232 -582 -140 N ATOM 2348 CA VAL A 292 0.912 36.293 17.685 1.00 77.99 C ANISOU 2348 CA VAL A 292 8885 12348 8398 -171 -753 -73 C ATOM 2349 C VAL A 292 2.430 36.159 17.569 1.00 70.73 C ANISOU 2349 C VAL A 292 8037 11319 7517 -266 -694 35 C ATOM 2350 O VAL A 292 3.077 37.187 17.288 1.00 66.29 O ANISOU 2350 O VAL A 292 7554 10648 6985 -265 -824 116 O ATOM 2351 CB VAL A 292 0.530 37.163 18.896 1.00 73.39 C ANISOU 2351 CB VAL A 292 8286 11740 7859 -6 -874 -147 C ATOM 2352 CG1 VAL A 292 1.261 38.496 18.896 1.00 67.47 C ANISOU 2352 CG1 VAL A 292 7640 10826 7169 45 -1052 -73 C ATOM 2353 CG2 VAL A 292 -0.965 37.376 18.960 1.00 80.13 C ANISOU 2353 CG2 VAL A 292 9055 12724 8663 101 -946 -267 C ATOM 2354 N LEU A 293 2.959 34.945 17.772 1.00 75.16 N ANISOU 2354 N LEU A 293 8572 11913 8072 -347 -517 35 N ATOM 2355 CA LEU A 293 4.429 34.725 17.783 1.00 67.62 C ANISOU 2355 CA LEU A 293 7667 10876 7150 -421 -451 119 C ATOM 2356 C LEU A 293 4.750 33.249 17.559 1.00 63.38 C ANISOU 2356 C LEU A 293 7101 10395 6583 -515 -265 103 C ATOM 2357 O LEU A 293 4.057 32.406 18.155 1.00 58.66 O ANISOU 2357 O LEU A 293 6456 9862 5971 -497 -183 25 O ATOM 2358 CB LEU A 293 4.952 35.155 19.152 1.00 69.99 C ANISOU 2358 CB LEU A 293 7977 11097 7516 -333 -484 111 C ATOM 2359 CG LEU A 293 6.437 34.942 19.393 1.00 71.62 C ANISOU 2359 CG LEU A 293 8221 11231 7759 -390 -420 185 C ATOM 2360 CD1 LEU A 293 7.259 35.767 18.420 1.00100.36 C ANISOU 2360 CD1 LEU A 293 11926 14817 11390 -466 -508 293 C ATOM 2361 CD2 LEU A 293 6.789 35.320 20.815 1.00 73.86 C ANISOU 2361 CD2 LEU A 293 8507 11450 8105 -298 -450 166 C ATOM 2362 N ASP A 294 5.786 32.970 16.759 1.00 55.02 N ANISOU 2362 N ASP A 294 6073 9319 5511 -611 -212 171 N ATOM 2363 CA ASP A 294 6.385 31.615 16.614 1.00 51.38 C ANISOU 2363 CA ASP A 294 5599 8887 5034 -681 -49 154 C ATOM 2364 C ASP A 294 7.903 31.770 16.521 1.00 60.57 C ANISOU 2364 C ASP A 294 6792 9999 6220 -720 -32 226 C ATOM 2365 O ASP A 294 8.373 32.479 15.619 1.00 59.79 O ANISOU 2365 O ASP A 294 6716 9907 6094 -781 -98 298 O ATOM 2366 CB ASP A 294 5.847 30.866 15.409 1.00 60.10 C ANISOU 2366 CB ASP A 294 6686 10080 6069 -766 15 129 C ATOM 2367 CG ASP A 294 6.234 29.401 15.406 1.00 69.15 C ANISOU 2367 CG ASP A 294 7826 11245 7200 -814 166 85 C ATOM 2368 OD1 ASP A 294 5.500 28.598 15.985 1.00 77.24 O ANISOU 2368 OD1 ASP A 294 8835 12291 8219 -800 223 19 O ATOM 2369 OD2 ASP A 294 7.288 29.081 14.844 1.00 88.52 O ANISOU 2369 OD2 ASP A 294 10292 13696 9644 -865 218 115 O ATOM 2370 N ASN A 295 8.628 31.165 17.462 1.00 60.40 N ANISOU 2370 N ASN A 295 6770 9938 6241 -690 45 209 N ATOM 2371 CA ASN A 295 10.092 31.338 17.616 1.00 57.24 C ANISOU 2371 CA ASN A 295 6385 9497 5864 -709 59 268 C ATOM 2372 C ASN A 295 10.591 30.060 18.269 1.00 59.25 C ANISOU 2372 C ASN A 295 6629 9742 6140 -690 187 215 C ATOM 2373 O ASN A 295 10.297 29.820 19.422 1.00 58.13 O ANISOU 2373 O ASN A 295 6488 9558 6040 -625 199 180 O ATOM 2374 CB ASN A 295 10.406 32.575 18.464 1.00 51.64 C ANISOU 2374 CB ASN A 295 5704 8708 5209 -649 -59 318 C ATOM 2375 CG ASN A 295 11.868 32.977 18.456 1.00 53.20 C ANISOU 2375 CG ASN A 295 5917 8880 5415 -691 -68 394 C ATOM 2376 OD1 ASN A 295 12.744 32.248 18.914 1.00 54.01 O ANISOU 2376 OD1 ASN A 295 6002 8982 5534 -684 24 380 O ATOM 2377 ND2 ASN A 295 12.139 34.174 17.986 1.00 61.60 N ANISOU 2377 ND2 ASN A 295 7016 9921 6465 -734 -194 476 N ATOM 2378 N PRO A 296 11.280 29.141 17.568 1.00 64.55 N ANISOU 2378 N PRO A 296 7292 10456 6778 -742 282 199 N ATOM 2379 CA PRO A 296 11.676 27.871 18.193 1.00 54.26 C ANISOU 2379 CA PRO A 296 5994 9125 5496 -712 385 141 C ATOM 2380 C PRO A 296 12.716 28.033 19.306 1.00 49.47 C ANISOU 2380 C PRO A 296 5394 8452 4948 -653 384 166 C ATOM 2381 O PRO A 296 12.748 27.174 20.160 1.00 48.67 O ANISOU 2381 O PRO A 296 5308 8305 4877 -611 438 123 O ATOM 2382 CB PRO A 296 12.279 27.069 17.025 1.00 62.63 C ANISOU 2382 CB PRO A 296 7041 10251 6501 -769 460 114 C ATOM 2383 CG PRO A 296 11.777 27.778 15.785 1.00 56.85 C ANISOU 2383 CG PRO A 296 6293 9595 5709 -843 409 149 C ATOM 2384 CD PRO A 296 11.678 29.242 16.160 1.00 53.01 C ANISOU 2384 CD PRO A 296 5816 9074 5251 -829 287 228 C ATOM 2385 N THR A 297 13.544 29.091 19.240 1.00 51.93 N ANISOU 2385 N THR A 297 5698 8763 5268 -662 319 237 N ATOM 2386 CA THR A 297 14.614 29.387 20.225 1.00 44.85 C ANISOU 2386 CA THR A 297 4803 7816 4420 -616 310 270 C ATOM 2387 C THR A 297 13.919 29.862 21.505 1.00 49.34 C ANISOU 2387 C THR A 297 5390 8309 5046 -545 253 266 C ATOM 2388 O THR A 297 14.176 29.247 22.569 1.00 49.91 O ANISOU 2388 O THR A 297 5468 8335 5160 -491 299 238 O ATOM 2389 CB THR A 297 15.679 30.374 19.719 1.00 43.57 C ANISOU 2389 CB THR A 297 4628 7690 4236 -670 253 351 C ATOM 2390 OG1 THR A 297 15.130 31.681 19.688 1.00 53.02 O ANISOU 2390 OG1 THR A 297 5853 8854 5438 -685 128 411 O ATOM 2391 CG2 THR A 297 16.201 30.094 18.332 1.00 49.14 C ANISOU 2391 CG2 THR A 297 5301 8507 4863 -757 294 356 C ATOM 2392 N LEU A 298 13.067 30.890 21.410 1.00 44.03 N ANISOU 2392 N LEU A 298 4726 7628 4372 -540 152 288 N ATOM 2393 CA LEU A 298 12.258 31.372 22.564 1.00 49.06 C ANISOU 2393 CA LEU A 298 5367 8219 5052 -461 91 263 C ATOM 2394 C LEU A 298 11.409 30.219 23.137 1.00 53.84 C ANISOU 2394 C LEU A 298 5958 8845 5653 -440 174 184 C ATOM 2395 O LEU A 298 11.251 30.133 24.354 1.00 52.82 O ANISOU 2395 O LEU A 298 5824 8688 5558 -385 175 160 O ATOM 2396 CB LEU A 298 11.348 32.526 22.155 1.00 46.69 C ANISOU 2396 CB LEU A 298 5077 7922 4740 -449 -34 276 C ATOM 2397 CG LEU A 298 11.902 33.930 22.359 1.00 49.60 C ANISOU 2397 CG LEU A 298 5482 8226 5138 -431 -167 345 C ATOM 2398 CD1 LEU A 298 10.866 34.938 21.883 1.00 51.48 C ANISOU 2398 CD1 LEU A 298 5740 8458 5361 -408 -304 344 C ATOM 2399 CD2 LEU A 298 12.243 34.188 23.818 1.00 54.28 C ANISOU 2399 CD2 LEU A 298 6076 8756 5791 -350 -186 333 C ATOM 2400 N SER A 299 10.930 29.328 22.279 1.00 58.73 N ANISOU 2400 N SER A 299 6572 9516 6224 -495 241 149 N ATOM 2401 CA SER A 299 10.186 28.106 22.667 1.00 57.86 C ANISOU 2401 CA SER A 299 6462 9425 6096 -506 319 83 C ATOM 2402 C SER A 299 11.114 27.178 23.449 1.00 55.44 C ANISOU 2402 C SER A 299 6180 9060 5822 -491 391 78 C ATOM 2403 O SER A 299 10.656 26.564 24.428 1.00 55.59 O ANISOU 2403 O SER A 299 6208 9064 5848 -479 416 46 O ATOM 2404 CB SER A 299 9.618 27.394 21.456 1.00 52.64 C ANISOU 2404 CB SER A 299 5802 8823 5374 -577 367 52 C ATOM 2405 OG SER A 299 8.910 26.223 21.822 1.00 55.91 O ANISOU 2405 OG SER A 299 6228 9250 5765 -604 432 -3 O ATOM 2406 N PHE A 300 12.376 27.074 23.054 1.00 46.18 N ANISOU 2406 N PHE A 300 5018 7865 4663 -493 417 107 N ATOM 2407 CA PHE A 300 13.238 26.097 23.756 1.00 48.91 C ANISOU 2407 CA PHE A 300 5389 8155 5038 -465 479 91 C ATOM 2408 C PHE A 300 13.731 26.700 25.073 1.00 44.34 C ANISOU 2408 C PHE A 300 4806 7525 4515 -404 440 124 C ATOM 2409 O PHE A 300 13.776 25.975 26.076 1.00 41.73 O ANISOU 2409 O PHE A 300 4499 7148 4207 -380 470 105 O ATOM 2410 CB PHE A 300 14.402 25.675 22.871 1.00 50.59 C ANISOU 2410 CB PHE A 300 5599 8386 5236 -476 524 90 C ATOM 2411 CG PHE A 300 15.303 24.653 23.507 1.00 47.67 C ANISOU 2411 CG PHE A 300 5257 7959 4895 -429 575 61 C ATOM 2412 CD1 PHE A 300 15.037 23.301 23.381 1.00 43.36 C ANISOU 2412 CD1 PHE A 300 4758 7380 4334 -437 625 0 C ATOM 2413 CD2 PHE A 300 16.405 25.054 24.243 1.00 48.72 C ANISOU 2413 CD2 PHE A 300 5376 8065 5069 -378 561 96 C ATOM 2414 CE1 PHE A 300 15.873 22.362 23.963 1.00 46.54 C ANISOU 2414 CE1 PHE A 300 5200 7716 4766 -384 653 -28 C ATOM 2415 CE2 PHE A 300 17.235 24.115 24.832 1.00 47.40 C ANISOU 2415 CE2 PHE A 300 5235 7845 4929 -325 598 67 C ATOM 2416 CZ PHE A 300 16.970 22.770 24.693 1.00 46.62 C ANISOU 2416 CZ PHE A 300 5190 7705 4819 -323 640 4 C ATOM 2417 N LEU A 301 14.078 27.986 25.075 1.00 41.90 N ANISOU 2417 N LEU A 301 4476 7219 4223 -387 368 175 N ATOM 2418 CA LEU A 301 14.731 28.578 26.271 1.00 48.61 C ANISOU 2418 CA LEU A 301 5324 8018 5125 -331 331 208 C ATOM 2419 C LEU A 301 13.727 28.609 27.414 1.00 48.33 C ANISOU 2419 C LEU A 301 5286 7972 5104 -296 308 176 C ATOM 2420 O LEU A 301 14.063 28.153 28.518 1.00 55.34 O ANISOU 2420 O LEU A 301 6182 8821 6021 -265 333 170 O ATOM 2421 CB LEU A 301 15.239 29.987 25.968 1.00 55.39 C ANISOU 2421 CB LEU A 301 6174 8877 5992 -335 242 271 C ATOM 2422 CG LEU A 301 16.320 30.088 24.892 1.00 54.98 C ANISOU 2422 CG LEU A 301 6113 8866 5910 -389 258 313 C ATOM 2423 CD1 LEU A 301 16.834 31.521 24.818 1.00 54.01 C ANISOU 2423 CD1 LEU A 301 5995 8732 5792 -409 154 390 C ATOM 2424 CD2 LEU A 301 17.460 29.092 25.152 1.00 44.73 C ANISOU 2424 CD2 LEU A 301 4805 7569 4621 -370 344 295 C ATOM 2425 N THR A 302 12.529 29.098 27.133 1.00 45.66 N ANISOU 2425 N THR A 302 4930 7679 4739 -301 261 151 N ATOM 2426 CA THR A 302 11.469 29.264 28.156 1.00 43.98 C ANISOU 2426 CA THR A 302 4692 7494 4523 -265 230 106 C ATOM 2427 C THR A 302 11.039 27.902 28.709 1.00 47.22 C ANISOU 2427 C THR A 302 5111 7921 4907 -303 312 67 C ATOM 2428 O THR A 302 10.675 27.841 29.919 1.00 51.01 O ANISOU 2428 O THR A 302 5574 8417 5391 -281 305 46 O ATOM 2429 CB THR A 302 10.275 30.022 27.569 1.00 45.44 C ANISOU 2429 CB THR A 302 4847 7743 4673 -257 159 76 C ATOM 2430 OG1 THR A 302 9.768 29.259 26.465 1.00 47.63 O ANISOU 2430 OG1 THR A 302 5129 8067 4900 -327 213 58 O ATOM 2431 CG2 THR A 302 10.645 31.433 27.158 1.00 47.74 C ANISOU 2431 CG2 THR A 302 5150 7998 4991 -221 49 120 C ATOM 2432 N THR A 303 11.042 26.878 27.848 1.00 48.82 N ANISOU 2432 N THR A 303 5343 8126 5080 -364 378 57 N ATOM 2433 CA THR A 303 10.626 25.489 28.185 1.00 51.01 C ANISOU 2433 CA THR A 303 5654 8402 5326 -420 444 25 C ATOM 2434 C THR A 303 11.592 24.938 29.226 1.00 45.36 C ANISOU 2434 C THR A 303 4975 7606 4652 -394 467 47 C ATOM 2435 O THR A 303 11.121 24.427 30.255 1.00 47.58 O ANISOU 2435 O THR A 303 5265 7894 4918 -417 474 35 O ATOM 2436 CB THR A 303 10.562 24.596 26.932 1.00 49.80 C ANISOU 2436 CB THR A 303 5535 8250 5137 -481 495 6 C ATOM 2437 OG1 THR A 303 9.455 25.064 26.156 1.00 45.80 O ANISOU 2437 OG1 THR A 303 4989 7829 4582 -512 470 -16 O ATOM 2438 CG2 THR A 303 10.418 23.114 27.226 1.00 47.12 C ANISOU 2438 CG2 THR A 303 5258 7870 4773 -537 548 -18 C ATOM 2439 N TRP A 304 12.887 25.060 28.964 1.00 49.61 N ANISOU 2439 N TRP A 304 5529 8085 5234 -353 475 79 N ATOM 2440 CA TRP A 304 13.913 24.477 29.871 1.00 47.87 C ANISOU 2440 CA TRP A 304 5344 7788 5054 -319 496 97 C ATOM 2441 C TRP A 304 14.206 25.426 31.038 1.00 43.51 C ANISOU 2441 C TRP A 304 4759 7231 4542 -265 449 127 C ATOM 2442 O TRP A 304 14.592 24.914 32.090 1.00 43.18 O ANISOU 2442 O TRP A 304 4741 7143 4520 -251 460 136 O ATOM 2443 CB TRP A 304 15.141 24.058 29.063 1.00 48.31 C ANISOU 2443 CB TRP A 304 5421 7808 5127 -296 528 100 C ATOM 2444 CG TRP A 304 14.760 22.878 28.234 1.00 47.56 C ANISOU 2444 CG TRP A 304 5372 7705 4993 -342 571 55 C ATOM 2445 CD1 TRP A 304 14.240 22.933 26.985 1.00 41.99 C ANISOU 2445 CD1 TRP A 304 4652 7055 4246 -385 583 32 C ATOM 2446 CD2 TRP A 304 14.653 21.506 28.665 1.00 48.10 C ANISOU 2446 CD2 TRP A 304 5518 7702 5054 -363 593 27 C ATOM 2447 NE1 TRP A 304 13.884 21.679 26.587 1.00 45.04 N ANISOU 2447 NE1 TRP A 304 5098 7413 4601 -426 617 -12 N ATOM 2448 CE2 TRP A 304 14.135 20.781 27.573 1.00 42.08 C ANISOU 2448 CE2 TRP A 304 4786 6953 4247 -415 619 -16 C ATOM 2449 CE3 TRP A 304 14.989 20.809 29.834 1.00 43.81 C ANISOU 2449 CE3 TRP A 304 5029 7079 4536 -347 586 38 C ATOM 2450 CZ2 TRP A 304 13.952 19.402 27.598 1.00 44.02 C ANISOU 2450 CZ2 TRP A 304 5122 7126 4474 -449 632 -51 C ATOM 2451 CZ3 TRP A 304 14.820 19.442 29.867 1.00 45.83 C ANISOU 2451 CZ3 TRP A 304 5379 7261 4773 -384 594 9 C ATOM 2452 CH2 TRP A 304 14.302 18.752 28.766 1.00 53.96 C ANISOU 2452 CH2 TRP A 304 6446 8296 5761 -434 613 -35 C ATOM 2453 N LEU A 305 13.911 26.722 30.882 1.00 43.71 N ANISOU 2453 N LEU A 305 4737 7297 4572 -241 391 138 N ATOM 2454 CA LEU A 305 13.969 27.695 32.013 1.00 41.34 C ANISOU 2454 CA LEU A 305 4408 6996 4304 -186 333 152 C ATOM 2455 C LEU A 305 12.912 27.321 33.042 1.00 43.36 C ANISOU 2455 C LEU A 305 4646 7300 4529 -202 335 112 C ATOM 2456 O LEU A 305 13.137 27.501 34.237 1.00 55.98 O ANISOU 2456 O LEU A 305 6232 8889 6146 -171 319 118 O ATOM 2457 CB LEU A 305 13.731 29.113 31.489 1.00 39.26 C ANISOU 2457 CB LEU A 305 4114 6755 4045 -157 251 161 C ATOM 2458 CG LEU A 305 13.764 30.229 32.523 1.00 39.45 C ANISOU 2458 CG LEU A 305 4115 6770 4102 -92 172 165 C ATOM 2459 CD1 LEU A 305 15.149 30.354 33.119 1.00 46.06 C ANISOU 2459 CD1 LEU A 305 4970 7542 4987 -68 177 217 C ATOM 2460 CD2 LEU A 305 13.382 31.554 31.902 1.00 45.78 C ANISOU 2460 CD2 LEU A 305 4909 7580 4905 -64 71 168 C ATOM 2461 N ALA A 306 11.774 26.825 32.579 1.00 59.37 N ANISOU 2461 N ALA A 306 6665 9393 6499 -257 354 72 N ATOM 2462 CA ALA A 306 10.685 26.354 33.456 1.00 55.84 C ANISOU 2462 CA ALA A 306 6192 9025 5998 -299 362 32 C ATOM 2463 C ALA A 306 11.110 25.018 34.071 1.00 50.75 C ANISOU 2463 C ALA A 306 5611 8323 5349 -356 416 54 C ATOM 2464 O ALA A 306 11.049 24.908 35.298 1.00 46.92 O ANISOU 2464 O ALA A 306 5116 7856 4856 -362 408 58 O ATOM 2465 CB ALA A 306 9.413 26.249 32.669 1.00 59.35 C ANISOU 2465 CB ALA A 306 6606 9565 6376 -349 363 -13 C ATOM 2466 N ILE A 307 11.547 24.056 33.250 1.00 42.22 N ANISOU 2466 N ILE A 307 4599 7173 4270 -394 459 66 N ATOM 2467 CA ILE A 307 11.911 22.705 33.756 1.00 44.43 C ANISOU 2467 CA ILE A 307 4960 7376 4545 -445 490 82 C ATOM 2468 C ILE A 307 12.990 22.861 34.840 1.00 51.78 C ANISOU 2468 C ILE A 307 5903 8239 5532 -383 476 120 C ATOM 2469 O ILE A 307 13.045 21.988 35.750 1.00 45.69 O ANISOU 2469 O ILE A 307 5184 7428 4748 -426 479 137 O ATOM 2470 CB ILE A 307 12.326 21.792 32.595 1.00 43.01 C ANISOU 2470 CB ILE A 307 4850 7124 4367 -464 524 73 C ATOM 2471 CG1 ILE A 307 11.106 21.499 31.718 1.00 45.70 C ANISOU 2471 CG1 ILE A 307 5184 7539 4640 -545 538 36 C ATOM 2472 CG2 ILE A 307 13.004 20.506 33.068 1.00 41.59 C ANISOU 2472 CG2 ILE A 307 4771 6830 4201 -479 534 87 C ATOM 2473 CD1 ILE A 307 11.439 21.112 30.280 1.00 44.38 C ANISOU 2473 CD1 ILE A 307 5050 7338 4474 -544 565 16 C ATOM 2474 N SER A 308 13.759 23.960 34.801 1.00 43.53 N ANISOU 2474 N SER A 308 4811 7186 4539 -297 454 136 N ATOM 2475 CA SER A 308 14.911 24.173 35.715 1.00 42.87 C ANISOU 2475 CA SER A 308 4734 7041 4511 -235 441 174 C ATOM 2476 C SER A 308 14.426 24.441 37.152 1.00 47.50 C ANISOU 2476 C SER A 308 5290 7674 5082 -245 416 176 C ATOM 2477 O SER A 308 15.255 24.346 38.077 1.00 54.18 O ANISOU 2477 O SER A 308 6152 8469 5962 -213 409 208 O ATOM 2478 CB SER A 308 15.830 25.283 35.211 1.00 38.25 C ANISOU 2478 CB SER A 308 4112 6446 3974 -163 419 195 C ATOM 2479 OG SER A 308 15.255 26.578 35.359 1.00 36.70 O ANISOU 2479 OG SER A 308 3855 6312 3776 -139 367 186 O ATOM 2480 N ASN A 309 13.153 24.790 37.337 1.00 44.84 N ANISOU 2480 N ASN A 309 4900 7445 4690 -283 400 138 N ATOM 2481 CA ASN A 309 12.615 25.127 38.680 1.00 42.56 C ANISOU 2481 CA ASN A 309 4560 7237 4371 -290 375 125 C ATOM 2482 C ASN A 309 12.418 23.854 39.494 1.00 44.70 C ANISOU 2482 C ASN A 309 4885 7501 4596 -386 399 146 C ATOM 2483 O ASN A 309 12.269 23.997 40.732 1.00 42.26 O ANISOU 2483 O ASN A 309 4543 7249 4265 -398 382 149 O ATOM 2484 CB ASN A 309 11.333 25.966 38.643 1.00 47.44 C ANISOU 2484 CB ASN A 309 5089 7998 4937 -285 342 62 C ATOM 2485 CG ASN A 309 10.128 25.328 37.982 1.00 42.11 C ANISOU 2485 CG ASN A 309 4406 7409 4183 -374 366 25 C ATOM 2486 OD1 ASN A 309 9.952 24.111 37.955 1.00 43.83 O ANISOU 2486 OD1 ASN A 309 4685 7607 4361 -474 405 45 O ATOM 2487 ND2 ASN A 309 9.264 26.182 37.476 1.00 44.37 N ANISOU 2487 ND2 ASN A 309 4621 7793 4444 -338 333 -29 N ATOM 2488 N SER A 310 12.461 22.689 38.832 1.00 46.84 N ANISOU 2488 N SER A 310 5241 7701 4853 -451 428 161 N ATOM 2489 CA SER A 310 12.536 21.363 39.510 1.00 51.92 C ANISOU 2489 CA SER A 310 5976 8285 5465 -541 433 197 C ATOM 2490 C SER A 310 13.923 21.176 40.153 1.00 55.97 C ANISOU 2490 C SER A 310 6540 8674 6049 -471 421 244 C ATOM 2491 O SER A 310 14.077 20.290 41.002 1.00 57.67 O ANISOU 2491 O SER A 310 6826 8839 6246 -530 406 280 O ATOM 2492 CB SER A 310 12.224 20.243 38.552 1.00 51.55 C ANISOU 2492 CB SER A 310 6017 8181 5389 -616 450 191 C ATOM 2493 OG SER A 310 10.907 20.372 38.034 1.00 67.49 O ANISOU 2493 OG SER A 310 7983 10326 7331 -692 461 151 O ATOM 2494 N PHE A 311 14.894 21.997 39.758 1.00 48.39 N ANISOU 2494 N PHE A 311 5547 7673 5163 -356 422 245 N ATOM 2495 CA PHE A 311 16.272 21.939 40.289 1.00 57.17 C ANISOU 2495 CA PHE A 311 6690 8689 6341 -279 412 283 C ATOM 2496 C PHE A 311 16.451 23.038 41.339 1.00 58.68 C ANISOU 2496 C PHE A 311 6804 8941 6551 -234 388 294 C ATOM 2497 O PHE A 311 17.175 22.816 42.321 1.00 66.42 O ANISOU 2497 O PHE A 311 7806 9874 7554 -215 375 330 O ATOM 2498 CB PHE A 311 17.313 22.118 39.181 1.00 59.85 C ANISOU 2498 CB PHE A 311 7035 8966 6737 -194 427 276 C ATOM 2499 CG PHE A 311 18.693 22.384 39.714 1.00 59.61 C ANISOU 2499 CG PHE A 311 7001 8882 6767 -107 416 307 C ATOM 2500 CD1 PHE A 311 19.401 21.373 40.356 1.00 67.59 C ANISOU 2500 CD1 PHE A 311 8085 9799 7793 -94 405 330 C ATOM 2501 CD2 PHE A 311 19.249 23.656 39.664 1.00 67.26 C ANISOU 2501 CD2 PHE A 311 7893 9890 7770 -44 406 316 C ATOM 2502 CE1 PHE A 311 20.665 21.610 40.886 1.00 69.26 C ANISOU 2502 CE1 PHE A 311 8284 9973 8055 -11 394 355 C ATOM 2503 CE2 PHE A 311 20.514 23.898 40.197 1.00 73.83 C ANISOU 2503 CE2 PHE A 311 8716 10685 8648 23 396 346 C ATOM 2504 CZ PHE A 311 21.225 22.873 40.799 1.00 69.44 C ANISOU 2504 CZ PHE A 311 8222 10052 8108 44 394 363 C ATOM 2505 N CYS A 312 15.826 24.194 41.126 1.00 52.84 N ANISOU 2505 N CYS A 312 5979 8295 5801 -210 375 260 N ATOM 2506 CA CYS A 312 15.922 25.340 42.067 1.00 53.16 C ANISOU 2506 CA CYS A 312 5947 8392 5858 -156 340 255 C ATOM 2507 C CYS A 312 15.218 25.016 43.394 1.00 64.14 C ANISOU 2507 C CYS A 312 7315 9864 7188 -221 332 250 C ATOM 2508 O CYS A 312 15.783 25.391 44.434 1.00 68.36 O ANISOU 2508 O CYS A 312 7830 10396 7745 -185 312 269 O ATOM 2509 CB CYS A 312 15.355 26.596 41.438 1.00 48.06 C ANISOU 2509 CB CYS A 312 5232 7813 5213 -110 309 212 C ATOM 2510 SG CYS A 312 16.443 27.216 40.137 1.00 65.32 S ANISOU 2510 SG CYS A 312 7437 9914 7466 -45 303 239 S ATOM 2511 N ASN A 313 14.072 24.325 43.352 1.00 62.29 N ANISOU 2511 N ASN A 313 7084 9707 6874 -321 346 227 N ATOM 2512 CA ASN A 313 13.301 23.896 44.545 1.00 59.64 C ANISOU 2512 CA ASN A 313 6724 9480 6456 -416 340 225 C ATOM 2513 C ASN A 313 14.215 23.237 45.573 1.00 54.08 C ANISOU 2513 C ASN A 313 6085 8690 5773 -435 333 291 C ATOM 2514 O ASN A 313 14.289 23.730 46.704 1.00 50.40 O ANISOU 2514 O ASN A 313 5564 8291 5294 -423 314 290 O ATOM 2515 CB ASN A 313 12.131 22.968 44.198 1.00 65.29 C ANISOU 2515 CB ASN A 313 7459 10269 7076 -550 359 211 C ATOM 2516 CG ASN A 313 10.985 23.717 43.555 1.00 64.61 C ANISOU 2516 CG ASN A 313 7278 10326 6944 -539 357 134 C ATOM 2517 OD1 ASN A 313 10.720 24.881 43.878 1.00 48.73 O ANISOU 2517 OD1 ASN A 313 5167 8409 4936 -457 330 80 O ATOM 2518 ND2 ASN A 313 10.339 23.062 42.608 1.00 75.95 N ANISOU 2518 ND2 ASN A 313 8749 11769 8340 -613 379 124 N ATOM 2519 N PRO A 314 14.902 22.112 45.260 1.00 43.47 N ANISOU 2519 N PRO A 314 4858 7202 4456 -462 340 343 N ATOM 2520 CA PRO A 314 15.776 21.481 46.246 1.00 45.35 C ANISOU 2520 CA PRO A 314 5163 7352 4715 -471 320 404 C ATOM 2521 C PRO A 314 16.996 22.329 46.642 1.00 46.54 C ANISOU 2521 C PRO A 314 5278 7454 4949 -343 310 418 C ATOM 2522 O PRO A 314 17.536 22.128 47.709 1.00 60.19 O ANISOU 2522 O PRO A 314 7025 9160 6683 -348 290 459 O ATOM 2523 CB PRO A 314 16.230 20.175 45.584 1.00 43.65 C ANISOU 2523 CB PRO A 314 5083 6983 4518 -498 316 436 C ATOM 2524 CG PRO A 314 16.031 20.427 44.121 1.00 48.10 C ANISOU 2524 CG PRO A 314 5631 7538 5103 -454 346 389 C ATOM 2525 CD PRO A 314 14.823 21.337 44.021 1.00 44.98 C ANISOU 2525 CD PRO A 314 5125 7311 4653 -486 359 339 C ATOM 2526 N VAL A 315 17.399 23.271 45.802 1.00 50.32 N ANISOU 2526 N VAL A 315 5708 7923 5485 -243 320 388 N ATOM 2527 CA VAL A 315 18.623 24.056 46.103 1.00 48.71 C ANISOU 2527 CA VAL A 315 5477 7673 5356 -136 307 408 C ATOM 2528 C VAL A 315 18.210 25.159 47.053 1.00 44.84 C ANISOU 2528 C VAL A 315 4896 7293 4848 -121 283 384 C ATOM 2529 O VAL A 315 18.925 25.325 48.038 1.00 70.97 O ANISOU 2529 O VAL A 315 8199 10586 8178 -93 266 414 O ATOM 2530 CB VAL A 315 19.334 24.595 44.847 1.00 55.62 C ANISOU 2530 CB VAL A 315 6345 8498 6290 -55 319 398 C ATOM 2531 CG1 VAL A 315 20.336 25.695 45.172 1.00 62.93 C ANISOU 2531 CG1 VAL A 315 7221 9417 7270 29 297 413 C ATOM 2532 CG2 VAL A 315 20.026 23.472 44.098 1.00 50.54 C ANISOU 2532 CG2 VAL A 315 5785 7748 5668 -46 339 414 C ATOM 2533 N ILE A 316 17.121 25.874 46.779 1.00 45.70 N ANISOU 2533 N ILE A 316 4935 7510 4916 -129 275 324 N ATOM 2534 CA ILE A 316 16.682 26.959 47.716 1.00 49.57 C ANISOU 2534 CA ILE A 316 5334 8113 5386 -95 239 279 C ATOM 2535 C ILE A 316 16.403 26.357 49.097 1.00 47.08 C ANISOU 2535 C ILE A 316 5009 7870 5007 -173 240 296 C ATOM 2536 O ILE A 316 16.868 26.955 50.086 1.00 51.57 O ANISOU 2536 O ILE A 316 5539 8462 5591 -130 215 297 O ATOM 2537 CB ILE A 316 15.496 27.775 47.160 1.00 47.51 C ANISOU 2537 CB ILE A 316 5001 7963 5088 -77 218 198 C ATOM 2538 CG1 ILE A 316 15.774 28.264 45.725 1.00 50.99 C ANISOU 2538 CG1 ILE A 316 5465 8324 5584 -21 212 196 C ATOM 2539 CG2 ILE A 316 15.157 28.934 48.086 1.00 44.31 C ANISOU 2539 CG2 ILE A 316 4504 7660 4668 -14 167 136 C ATOM 2540 CD1 ILE A 316 14.535 28.368 44.847 1.00 59.65 C ANISOU 2540 CD1 ILE A 316 6529 9502 6630 -44 211 137 C ATOM 2541 N TYR A 317 15.758 25.191 49.153 1.00 54.35 N ANISOU 2541 N TYR A 317 5972 8817 5858 -291 262 315 N ATOM 2542 CA TYR A 317 15.282 24.543 50.406 1.00 55.65 C ANISOU 2542 CA TYR A 317 6130 9077 5936 -404 257 336 C ATOM 2543 C TYR A 317 16.463 24.159 51.308 1.00 67.67 C ANISOU 2543 C TYR A 317 7712 10498 7502 -393 243 410 C ATOM 2544 O TYR A 317 16.457 24.533 52.520 1.00 61.61 O ANISOU 2544 O TYR A 317 6886 9821 6700 -404 226 408 O ATOM 2545 CB TYR A 317 14.444 23.312 50.074 1.00 61.18 C ANISOU 2545 CB TYR A 317 6891 9798 6555 -550 273 356 C ATOM 2546 CG TYR A 317 13.787 22.623 51.244 1.00 78.50 C ANISOU 2546 CG TYR A 317 9077 12112 8634 -702 263 383 C ATOM 2547 CD1 TYR A 317 12.769 23.233 51.971 1.00 76.63 C ANISOU 2547 CD1 TYR A 317 8710 12105 8301 -743 260 315 C ATOM 2548 CD2 TYR A 317 14.148 21.327 51.584 1.00 85.04 C ANISOU 2548 CD2 TYR A 317 10033 12835 9443 -810 247 471 C ATOM 2549 CE1 TYR A 317 12.147 22.580 53.022 1.00 80.19 C ANISOU 2549 CE1 TYR A 317 9144 12695 8628 -904 251 341 C ATOM 2550 CE2 TYR A 317 13.526 20.656 52.623 1.00 92.98 C ANISOU 2550 CE2 TYR A 317 11042 13952 10331 -977 228 509 C ATOM 2551 CZ TYR A 317 12.526 21.288 53.343 1.00 86.42 C ANISOU 2551 CZ TYR A 317 10069 13370 9395 -1032 235 446 C ATOM 2552 OH TYR A 317 11.895 20.631 54.356 1.00 71.82 O ANISOU 2552 OH TYR A 317 8213 11660 7413 -1214 217 484 O ATOM 2553 N ALA A 318 17.442 23.432 50.760 1.00 61.46 N ANISOU 2553 N ALA A 318 7031 9538 6782 -365 248 468 N ATOM 2554 CA ALA A 318 18.592 22.906 51.535 1.00 57.70 C ANISOU 2554 CA ALA A 318 6621 8954 6345 -349 227 539 C ATOM 2555 C ALA A 318 19.587 24.036 51.852 1.00 56.88 C ANISOU 2555 C ALA A 318 6456 8837 6316 -222 220 532 C ATOM 2556 O ALA A 318 20.249 23.990 52.938 1.00 49.80 O ANISOU 2556 O ALA A 318 5564 7929 5427 -217 199 573 O ATOM 2557 CB ALA A 318 19.250 21.778 50.773 1.00 52.95 C ANISOU 2557 CB ALA A 318 6146 8186 5786 -343 225 581 C ATOM 2558 N LEU A 319 19.733 24.999 50.942 1.00 50.18 N ANISOU 2558 N LEU A 319 5562 7985 5520 -132 228 488 N ATOM 2559 CA LEU A 319 20.711 26.097 51.128 1.00 59.10 C ANISOU 2559 CA LEU A 319 6645 9092 6716 -26 212 488 C ATOM 2560 C LEU A 319 20.142 27.225 52.016 1.00 65.12 C ANISOU 2560 C LEU A 319 7312 9980 7448 -11 184 437 C ATOM 2561 O LEU A 319 20.909 28.104 52.411 1.00 86.67 O ANISOU 2561 O LEU A 319 10012 12694 10225 60 159 440 O ATOM 2562 CB LEU A 319 21.179 26.595 49.756 1.00 50.21 C ANISOU 2562 CB LEU A 319 5525 7903 5650 44 221 475 C ATOM 2563 CG LEU A 319 22.611 26.193 49.373 1.00 68.22 C ANISOU 2563 CG LEU A 319 7854 10072 7992 101 230 523 C ATOM 2564 CD1 LEU A 319 22.835 24.694 49.502 1.00 71.65 C ANISOU 2564 CD1 LEU A 319 8377 10430 8414 62 240 560 C ATOM 2565 CD2 LEU A 319 22.968 26.652 47.954 1.00 59.51 C ANISOU 2565 CD2 LEU A 319 6745 8940 6924 147 242 507 C ATOM 2566 N SER A 320 18.853 27.236 52.329 1.00 68.84 N ANISOU 2566 N SER A 320 7732 10582 7840 -74 183 385 N ATOM 2567 CA SER A 320 18.268 28.264 53.232 1.00 76.38 C ANISOU 2567 CA SER A 320 8586 11677 8756 -47 150 316 C ATOM 2568 C SER A 320 18.275 27.750 54.682 1.00 75.27 C ANISOU 2568 C SER A 320 8431 11613 8556 -121 149 345 C ATOM 2569 O SER A 320 18.159 28.593 55.597 1.00 54.98 O ANISOU 2569 O SER A 320 5782 9142 5965 -84 120 296 O ATOM 2570 CB SER A 320 16.890 28.658 52.769 1.00 88.81 C ANISOU 2570 CB SER A 320 10093 13379 10269 -57 144 227 C ATOM 2571 OG SER A 320 16.938 29.179 51.441 1.00 92.48 O ANISOU 2571 OG SER A 320 10578 13767 10791 9 136 208 O ATOM 2572 N ASP A 321 18.462 26.428 54.848 1.00 75.43 N ANISOU 2572 N ASP A 321 8533 11576 8550 -219 170 422 N ATOM 2573 CA ASP A 321 18.542 25.691 56.140 1.00 66.18 C ANISOU 2573 CA ASP A 321 7378 10451 7316 -316 161 476 C ATOM 2574 C ASP A 321 19.978 25.719 56.713 1.00 68.15 C ANISOU 2574 C ASP A 321 7671 10581 7641 -252 145 542 C ATOM 2575 O ASP A 321 20.925 25.226 56.042 1.00 69.24 O ANISOU 2575 O ASP A 321 7895 10559 7854 -205 150 595 O ATOM 2576 CB ASP A 321 18.051 24.252 55.955 1.00 59.96 C ANISOU 2576 CB ASP A 321 6680 9635 6464 -457 171 532 C ATOM 2577 CG ASP A 321 18.165 23.403 57.215 1.00 86.18 C ANISOU 2577 CG ASP A 321 10042 12983 9716 -577 147 606 C ATOM 2578 OD1 ASP A 321 17.417 23.667 58.182 1.00 89.64 O ANISOU 2578 OD1 ASP A 321 10392 13609 10057 -655 142 575 O ATOM 2579 OD2 ASP A 321 19.020 22.495 57.236 1.00 99.73 O ANISOU 2579 OD2 ASP A 321 11877 14539 11475 -588 128 690 O ATOM 2580 N SER A 322 20.124 26.232 57.938 1.00 68.51 N ANISOU 2580 N SER A 322 7653 10717 7659 -251 126 535 N ATOM 2581 CA SER A 322 21.413 26.424 58.651 1.00 65.76 C ANISOU 2581 CA SER A 322 7324 10291 7371 -192 107 588 C ATOM 2582 C SER A 322 22.079 25.078 58.988 1.00 58.77 C ANISOU 2582 C SER A 322 6549 9293 6485 -257 98 691 C ATOM 2583 O SER A 322 23.355 25.038 58.967 1.00 48.14 O ANISOU 2583 O SER A 322 5247 7824 5219 -175 88 739 O ATOM 2584 CB SER A 322 21.218 27.300 59.882 1.00 63.28 C ANISOU 2584 CB SER A 322 6908 10121 7012 -185 86 542 C ATOM 2585 OG SER A 322 21.060 28.670 59.506 1.00 63.16 O ANISOU 2585 OG SER A 322 6818 10144 7036 -76 72 452 O ATOM 2586 N THR A 323 21.289 24.034 59.305 1.00 54.86 N ANISOU 2586 N THR A 323 6100 8841 5900 -398 92 725 N ATOM 2587 CA THR A 323 21.868 22.712 59.702 1.00 58.00 C ANISOU 2587 CA THR A 323 6625 9117 6292 -468 59 827 C ATOM 2588 C THR A 323 22.473 21.983 58.491 1.00 54.52 C ANISOU 2588 C THR A 323 6297 8487 5931 -405 58 852 C ATOM 2589 O THR A 323 23.527 21.367 58.654 1.00 53.11 O ANISOU 2589 O THR A 323 6202 8173 5804 -359 26 912 O ATOM 2590 CB THR A 323 20.858 21.809 60.421 1.00 62.12 C ANISOU 2590 CB THR A 323 7179 9737 6686 -659 38 867 C ATOM 2591 OG1 THR A 323 19.890 21.340 59.476 1.00 83.16 O ANISOU 2591 OG1 THR A 323 9873 12413 9311 -728 55 841 O ATOM 2592 CG2 THR A 323 20.185 22.507 61.582 1.00 66.79 C ANISOU 2592 CG2 THR A 323 7642 10553 7182 -726 42 828 C ATOM 2593 N PHE A 324 21.826 22.037 57.325 1.00 60.17 N ANISOU 2593 N PHE A 324 7009 9201 6650 -398 88 801 N ATOM 2594 CA PHE A 324 22.338 21.362 56.106 1.00 55.02 C ANISOU 2594 CA PHE A 324 6452 8386 6064 -338 90 810 C ATOM 2595 C PHE A 324 23.698 21.949 55.757 1.00 47.87 C ANISOU 2595 C PHE A 324 5526 7398 5262 -179 97 805 C ATOM 2596 O PHE A 324 24.632 21.169 55.464 1.00 42.08 O ANISOU 2596 O PHE A 324 4880 6528 4578 -122 74 839 O ATOM 2597 CB PHE A 324 21.368 21.534 54.932 1.00 51.16 C ANISOU 2597 CB PHE A 324 5940 7939 5558 -356 127 748 C ATOM 2598 CG PHE A 324 21.844 20.899 53.657 1.00 48.57 C ANISOU 2598 CG PHE A 324 5698 7465 5290 -295 132 745 C ATOM 2599 CD1 PHE A 324 21.621 19.550 53.398 1.00 55.58 C ANISOU 2599 CD1 PHE A 324 6715 8251 6149 -373 101 782 C ATOM 2600 CD2 PHE A 324 22.536 21.652 52.727 1.00 44.28 C ANISOU 2600 CD2 PHE A 324 5108 6889 4825 -165 161 705 C ATOM 2601 CE1 PHE A 324 22.087 18.972 52.224 1.00 55.97 C ANISOU 2601 CE1 PHE A 324 6840 8170 6253 -302 102 764 C ATOM 2602 CE2 PHE A 324 22.985 21.075 51.553 1.00 46.06 C ANISOU 2602 CE2 PHE A 324 5400 7006 5095 -109 168 694 C ATOM 2603 CZ PHE A 324 22.764 19.738 51.305 1.00 48.86 C ANISOU 2603 CZ PHE A 324 5876 7261 5426 -168 140 716 C ATOM 2604 N ARG A 325 23.763 23.284 55.790 1.00 51.56 N ANISOU 2604 N ARG A 325 5881 7955 5753 -114 120 758 N ATOM 2605 CA ARG A 325 24.988 24.079 55.489 1.00 53.98 C ANISOU 2605 CA ARG A 325 6149 8216 6143 15 126 752 C ATOM 2606 C ARG A 325 26.145 23.615 56.382 1.00 55.06 C ANISOU 2606 C ARG A 325 6325 8289 6305 48 94 814 C ATOM 2607 O ARG A 325 27.282 23.448 55.870 1.00 70.30 O ANISOU 2607 O ARG A 325 8278 10134 8297 142 92 826 O ATOM 2608 CB ARG A 325 24.697 25.573 55.681 1.00 48.82 C ANISOU 2608 CB ARG A 325 5385 7672 5492 48 132 700 C ATOM 2609 CG ARG A 325 23.994 26.219 54.494 1.00 51.27 C ANISOU 2609 CG ARG A 325 5660 8010 5808 67 152 638 C ATOM 2610 CD ARG A 325 23.850 27.710 54.686 1.00 60.16 C ANISOU 2610 CD ARG A 325 6697 9213 6945 117 134 587 C ATOM 2611 NE ARG A 325 22.735 28.051 55.563 1.00 74.89 N ANISOU 2611 NE ARG A 325 8502 11209 8740 65 120 539 N ATOM 2612 CZ ARG A 325 22.413 29.285 55.940 1.00 76.76 C ANISOU 2612 CZ ARG A 325 8663 11529 8974 110 90 477 C ATOM 2613 NH1 ARG A 325 23.134 30.316 55.537 1.00 84.63 N ANISOU 2613 NH1 ARG A 325 9648 12472 10035 194 63 469 N ATOM 2614 NH2 ARG A 325 21.375 29.486 56.731 1.00 84.97 N ANISOU 2614 NH2 ARG A 325 9637 12708 9939 69 79 419 N ATOM 2615 N LEU A 326 25.855 23.463 57.674 1.00 62.53 N ANISOU 2615 N LEU A 326 7265 9292 7198 -26 70 848 N ATOM 2616 CA LEU A 326 26.806 23.013 58.723 1.00 72.06 C ANISOU 2616 CA LEU A 326 8509 10454 8416 -14 31 913 C ATOM 2617 C LEU A 326 27.260 21.585 58.373 1.00 76.77 C ANISOU 2617 C LEU A 326 9239 10901 9029 -10 -5 960 C ATOM 2618 O LEU A 326 28.461 21.270 58.553 1.00 79.47 O ANISOU 2618 O LEU A 326 9613 11159 9420 77 -34 991 O ATOM 2619 CB LEU A 326 26.078 23.112 60.079 1.00 80.37 C ANISOU 2619 CB LEU A 326 9526 11625 9384 -127 14 932 C ATOM 2620 CG LEU A 326 26.884 22.864 61.361 1.00 74.83 C ANISOU 2620 CG LEU A 326 8841 10913 8677 -135 -26 998 C ATOM 2621 CD1 LEU A 326 28.110 23.751 61.458 1.00 71.07 C ANISOU 2621 CD1 LEU A 326 8304 10423 8275 -7 -20 990 C ATOM 2622 CD2 LEU A 326 26.023 23.093 62.591 1.00 80.12 C ANISOU 2622 CD2 LEU A 326 9453 11737 9249 -257 -34 1002 C ATOM 2623 N GLY A 327 26.341 20.763 57.852 1.00 65.88 N ANISOU 2623 N GLY A 327 7933 9489 7607 -95 -10 958 N ATOM 2624 CA GLY A 327 26.659 19.379 57.450 1.00 68.52 C ANISOU 2624 CA GLY A 327 8412 9665 7954 -93 -60 993 C ATOM 2625 C GLY A 327 27.768 19.370 56.418 1.00 66.47 C ANISOU 2625 C GLY A 327 8158 9314 7781 67 -50 956 C ATOM 2626 O GLY A 327 28.672 18.532 56.538 1.00 71.67 O ANISOU 2626 O GLY A 327 8901 9855 8472 135 -106 983 O ATOM 2627 N LEU A 328 27.706 20.310 55.471 1.00 63.45 N ANISOU 2627 N LEU A 328 7682 8996 7427 123 11 894 N ATOM 2628 CA LEU A 328 28.671 20.453 54.346 1.00 61.74 C ANISOU 2628 CA LEU A 328 7444 8737 7276 258 32 851 C ATOM 2629 C LEU A 328 30.008 20.967 54.863 1.00 54.90 C ANISOU 2629 C LEU A 328 6519 7887 6453 359 24 866 C ATOM 2630 O LEU A 328 31.025 20.522 54.322 1.00 52.03 O ANISOU 2630 O LEU A 328 6174 7465 6128 468 10 848 O ATOM 2631 CB LEU A 328 28.145 21.462 53.325 1.00 60.76 C ANISOU 2631 CB LEU A 328 7232 8696 7155 260 94 794 C ATOM 2632 CG LEU A 328 26.947 21.036 52.496 1.00 51.30 C ANISOU 2632 CG LEU A 328 6077 7491 5921 184 111 764 C ATOM 2633 CD1 LEU A 328 26.378 22.261 51.811 1.00 51.30 C ANISOU 2633 CD1 LEU A 328 5977 7593 5920 180 160 718 C ATOM 2634 CD2 LEU A 328 27.340 19.962 51.499 1.00 49.16 C ANISOU 2634 CD2 LEU A 328 5896 7108 5674 238 97 742 C ATOM 2635 N ARG A 329 29.992 21.919 55.805 1.00 55.00 N ANISOU 2635 N ARG A 329 6452 7990 6453 329 33 887 N ATOM 2636 CA ARG A 329 31.240 22.517 56.361 1.00 56.13 C ANISOU 2636 CA ARG A 329 6532 8163 6631 411 25 905 C ATOM 2637 C ARG A 329 31.966 21.463 57.207 1.00 62.39 C ANISOU 2637 C ARG A 329 7405 8871 7429 441 -36 955 C ATOM 2638 O ARG A 329 33.220 21.491 57.270 1.00 79.29 O ANISOU 2638 O ARG A 329 9517 11002 9605 546 -51 958 O ATOM 2639 CB ARG A 329 30.965 23.772 57.192 1.00 51.62 C ANISOU 2639 CB ARG A 329 5868 7701 6043 367 39 910 C ATOM 2640 CG ARG A 329 30.623 25.011 56.378 1.00 57.02 C ANISOU 2640 CG ARG A 329 6471 8456 6738 373 79 860 C ATOM 2641 CD ARG A 329 30.470 26.240 57.248 1.00 64.04 C ANISOU 2641 CD ARG A 329 7282 9435 7615 350 73 856 C ATOM 2642 NE ARG A 329 29.389 26.081 58.230 1.00 73.79 N ANISOU 2642 NE ARG A 329 8522 10719 8793 260 61 858 N ATOM 2643 CZ ARG A 329 28.134 26.456 58.047 1.00 76.54 C ANISOU 2643 CZ ARG A 329 8845 11131 9102 203 74 812 C ATOM 2644 NH1 ARG A 329 27.240 26.290 59.012 1.00 88.97 N ANISOU 2644 NH1 ARG A 329 10409 12782 10612 118 63 811 N ATOM 2645 NH2 ARG A 329 27.778 26.999 56.896 1.00 68.08 N ANISOU 2645 NH2 ARG A 329 7754 10061 8050 228 94 766 N ATOM 2646 N ARG A 330 31.202 20.585 57.854 1.00 77.37 N ANISOU 2646 N ARG A 330 9396 10717 9283 345 -78 997 N ATOM 2647 CA ARG A 330 31.758 19.472 58.663 1.00 76.22 C ANISOU 2647 CA ARG A 330 9356 10468 9135 356 -158 1055 C ATOM 2648 C ARG A 330 32.230 18.376 57.705 1.00 67.88 C ANISOU 2648 C ARG A 330 8399 9277 8114 450 -198 1025 C ATOM 2649 O ARG A 330 33.166 17.645 58.050 1.00 88.44 O ANISOU 2649 O ARG A 330 11066 11792 10743 537 -267 1045 O ATOM 2650 CB ARG A 330 30.706 18.960 59.652 1.00 83.55 C ANISOU 2650 CB ARG A 330 10354 11399 9990 193 -196 1116 C ATOM 2651 CG ARG A 330 30.510 19.840 60.878 1.00 81.99 C ANISOU 2651 CG ARG A 330 10065 11333 9753 123 -180 1145 C ATOM 2652 CD ARG A 330 29.214 19.493 61.582 1.00 96.26 C ANISOU 2652 CD ARG A 330 11907 13196 11468 -56 -195 1181 C ATOM 2653 NE ARG A 330 29.199 19.905 62.978 1.00103.89 N ANISOU 2653 NE ARG A 330 12822 14266 12385 -127 -210 1224 N ATOM 2654 CZ ARG A 330 28.219 19.626 63.833 1.00118.36 C ANISOU 2654 CZ ARG A 330 14668 16181 14120 -292 -229 1263 C ATOM 2655 NH1 ARG A 330 28.293 20.041 65.087 1.00150.29 N ANISOU 2655 NH1 ARG A 330 18652 20331 18117 -346 -240 1295 N ATOM 2656 NH2 ARG A 330 27.165 18.935 63.436 1.00129.96 N ANISOU 2656 NH2 ARG A 330 16205 17642 15529 -411 -238 1269 N ATOM 2657 N LEU A 331 31.604 18.286 56.534 1.00 66.24 N ANISOU 2657 N LEU A 331 8201 9058 7906 440 -161 973 N ATOM 2658 CA LEU A 331 31.953 17.278 55.507 1.00 69.25 C ANISOU 2658 CA LEU A 331 8673 9321 8316 530 -195 927 C ATOM 2659 C LEU A 331 33.309 17.661 54.936 1.00 72.41 C ANISOU 2659 C LEU A 331 8984 9758 8767 699 -175 873 C ATOM 2660 O LEU A 331 34.172 16.790 54.854 1.00 74.12 O ANISOU 2660 O LEU A 331 9266 9885 9011 815 -240 853 O ATOM 2661 CB LEU A 331 30.892 17.281 54.409 1.00 69.37 C ANISOU 2661 CB LEU A 331 8697 9346 8311 465 -147 882 C ATOM 2662 CG LEU A 331 30.969 16.116 53.423 1.00 74.40 C ANISOU 2662 CG LEU A 331 9450 9852 8964 526 -192 836 C ATOM 2663 CD1 LEU A 331 30.121 14.942 53.894 1.00 76.71 C ANISOU 2663 CD1 LEU A 331 9911 10019 9214 406 -274 889 C ATOM 2664 CD2 LEU A 331 30.531 16.569 52.043 1.00 75.76 C ANISOU 2664 CD2 LEU A 331 9559 10085 9139 535 -115 764 C ATOM 2665 N SER A 332 33.477 18.941 54.605 1.00 82.61 N ANISOU 2665 N SER A 332 10135 11186 10066 707 -96 850 N ATOM 2666 CA SER A 332 34.743 19.444 54.020 1.00 88.33 C ANISOU 2666 CA SER A 332 10756 11983 10820 838 -70 803 C ATOM 2667 C SER A 332 35.878 19.155 54.994 1.00 78.91 C ANISOU 2667 C SER A 332 9564 10773 9644 923 -127 833 C ATOM 2668 O SER A 332 36.915 18.674 54.549 1.00 87.68 O ANISOU 2668 O SER A 332 10665 11873 10775 1059 -153 785 O ATOM 2669 CB SER A 332 34.659 20.912 53.738 1.00 92.24 C ANISOU 2669 CB SER A 332 11120 12615 11310 796 3 797 C ATOM 2670 OG SER A 332 34.798 21.652 54.942 1.00100.30 O ANISOU 2670 OG SER A 332 12094 13689 12326 752 -2 852 O ATOM 2671 N GLU A 333 35.665 19.454 56.273 1.00 82.24 N ANISOU 2671 N GLU A 333 9989 11205 10051 845 -146 904 N ATOM 2672 CA GLU A 333 36.675 19.221 57.331 1.00 86.27 C ANISOU 2672 CA GLU A 333 10501 11703 10573 911 -203 944 C ATOM 2673 C GLU A 333 36.958 17.721 57.448 1.00 84.09 C ANISOU 2673 C GLU A 333 10370 11271 10308 983 -304 945 C ATOM 2674 O GLU A 333 38.137 17.369 57.601 1.00 94.82 O ANISOU 2674 O GLU A 333 11716 12618 11690 1119 -351 926 O ATOM 2675 CB GLU A 333 36.213 19.819 58.654 1.00 99.60 C ANISOU 2675 CB GLU A 333 12170 13437 12233 794 -203 1017 C ATOM 2676 CG GLU A 333 36.431 21.318 58.719 1.00109.84 C ANISOU 2676 CG GLU A 333 13323 14880 13531 775 -134 1009 C ATOM 2677 CD GLU A 333 36.242 21.913 60.101 1.00115.18 C ANISOU 2677 CD GLU A 333 13969 15610 14183 693 -143 1067 C ATOM 2678 OE1 GLU A 333 35.340 21.432 60.814 1.00146.20 O ANISOU 2678 OE1 GLU A 333 17970 19500 18076 592 -171 1108 O ATOM 2679 OE2 GLU A 333 37.023 22.832 60.477 1.00 87.04 O ANISOU 2679 OE2 GLU A 333 10307 12134 10628 725 -126 1072 O ATOM 2680 N THR A 334 35.928 16.877 57.380 1.00 70.28 N ANISOU 2680 N THR A 334 8755 9408 8540 895 -343 965 N ATOM 2681 CA THR A 334 36.140 15.407 57.485 1.00 73.26 C ANISOU 2681 CA THR A 334 9299 9608 8927 954 -461 971 C ATOM 2682 C THR A 334 37.116 14.947 56.391 1.00 79.12 C ANISOU 2682 C THR A 334 10027 10324 9709 1148 -479 869 C ATOM 2683 O THR A 334 38.057 14.198 56.722 1.00 68.85 O ANISOU 2683 O THR A 334 8782 8944 8431 1281 -573 856 O ATOM 2684 CB THR A 334 34.802 14.665 57.431 1.00 70.41 C ANISOU 2684 CB THR A 334 9080 9141 8529 804 -495 1007 C ATOM 2685 OG1 THR A 334 33.948 15.333 58.349 1.00 82.57 O ANISOU 2685 OG1 THR A 334 10581 10770 10021 633 -456 1080 O ATOM 2686 CG2 THR A 334 34.903 13.205 57.809 1.00 66.30 C ANISOU 2686 CG2 THR A 334 8759 8423 8009 822 -640 1041 C ATOM 2687 N MET A 335 36.899 15.408 55.155 1.00 81.89 N ANISOU 2687 N MET A 335 10299 10752 10062 1164 -394 795 N ATOM 2688 CA MET A 335 37.736 15.103 53.965 1.00 85.51 C ANISOU 2688 CA MET A 335 10714 11232 10542 1335 -391 683 C ATOM 2689 C MET A 335 39.134 15.718 54.117 1.00 97.89 C ANISOU 2689 C MET A 335 12135 12938 12121 1464 -371 653 C ATOM 2690 O MET A 335 40.107 15.098 53.678 1.00112.61 O ANISOU 2690 O MET A 335 13992 14795 13999 1637 -421 571 O ATOM 2691 CB MET A 335 37.088 15.708 52.725 1.00 85.14 C ANISOU 2691 CB MET A 335 10594 11271 10481 1280 -291 632 C ATOM 2692 CG MET A 335 35.758 15.097 52.382 1.00 91.62 C ANISOU 2692 CG MET A 335 11545 11978 11286 1163 -304 645 C ATOM 2693 SD MET A 335 34.793 16.138 51.254 1.00110.98 S ANISOU 2693 SD MET A 335 13894 14557 13715 1055 -178 617 S ATOM 2694 CE MET A 335 36.104 16.984 50.383 1.00 99.69 C ANISOU 2694 CE MET A 335 12283 13300 12294 1192 -113 540 C ATOM 2695 N CYS A 336 39.203 16.909 54.712 1.00 97.05 N ANISOU 2695 N CYS A 336 11912 12958 12002 1382 -304 710 N ATOM 2696 CA CYS A 336 40.456 17.681 54.917 1.00 87.39 C ANISOU 2696 CA CYS A 336 10537 11887 10777 1466 -276 696 C ATOM 2697 C CYS A 336 41.357 16.993 55.956 1.00122.89 C ANISOU 2697 C CYS A 336 15080 16322 15289 1570 -374 719 C ATOM 2698 O CYS A 336 42.540 16.748 55.643 1.00172.74 O ANISOU 2698 O CYS A 336 21326 22700 21606 1733 -400 649 O ATOM 2699 CB CYS A 336 40.127 19.089 55.380 1.00 75.25 C ANISOU 2699 CB CYS A 336 8898 10468 9223 1331 -197 760 C ATOM 2700 SG CYS A 336 41.573 20.041 55.895 1.00 78.42 S ANISOU 2700 SG CYS A 336 9138 11041 9616 1394 -177 768 S ATOM 2701 N THR A 337 40.827 16.708 57.150 1.00118.11 N ANISOU 2701 N THR A 337 14578 15613 14683 1478 -429 813 N ATOM 2702 CA THR A 337 41.626 16.091 58.247 1.00100.90 C ANISOU 2702 CA THR A 337 12452 13368 12515 1560 -531 851 C ATOM 2703 C THR A 337 42.031 14.670 57.816 1.00104.66 C ANISOU 2703 C THR A 337 13057 13694 13015 1718 -648 785 C ATOM 2704 O THR A 337 43.138 14.239 58.187 1.00138.74 O ANISOU 2704 O THR A 337 17363 18007 17345 1873 -724 757 O ATOM 2705 CB THR A 337 40.883 16.173 59.595 1.00 81.30 C ANISOU 2705 CB THR A 337 10046 10827 10014 1399 -559 971 C ATOM 2706 OG1 THR A 337 39.577 15.605 59.454 1.00 78.81 O ANISOU 2706 OG1 THR A 337 9867 10393 9685 1271 -578 1001 O ATOM 2707 CG2 THR A 337 40.760 17.587 60.126 1.00 63.97 C ANISOU 2707 CG2 THR A 337 7713 8792 7801 1289 -464 1016 C ATOM 2708 N SER A 338 41.186 13.980 57.040 1.00102.24 N ANISOU 2708 N SER A 338 12865 13270 12712 1689 -666 752 N ATOM 2709 CA SER A 338 41.481 12.635 56.473 1.00106.72 C ANISOU 2709 CA SER A 338 13565 13680 13301 1843 -783 672 C ATOM 2710 C SER A 338 42.532 12.764 55.363 1.00124.88 C ANISOU 2710 C SER A 338 15725 16115 15607 2039 -746 531 C ATOM 2711 O SER A 338 43.295 11.793 55.142 1.00131.95 O ANISOU 2711 O SER A 338 16680 16932 16521 2233 -855 445 O ATOM 2712 CB SER A 338 40.226 11.963 55.975 1.00 97.96 C ANISOU 2712 CB SER A 338 12613 12420 12186 1733 -806 682 C ATOM 2713 OG SER A 338 40.497 10.648 55.509 1.00100.89 O ANISOU 2713 OG SER A 338 13134 12619 12580 1878 -937 607 O ATOM 2714 N CYS A 339 42.548 13.916 54.683 1.00147.18 N ANISOU 2714 N CYS A 339 18373 19137 18409 1986 -606 506 N ATOM 2715 CA CYS A 339 43.508 14.250 53.595 1.00139.45 C ANISOU 2715 CA CYS A 339 17229 18341 17413 2129 -549 382 C ATOM 2716 C CYS A 339 44.857 14.588 54.227 1.00135.41 C ANISOU 2716 C CYS A 339 16591 17964 16894 2245 -567 372 C ATOM 2717 O CYS A 339 45.890 14.216 53.656 1.00133.57 O ANISOU 2717 O CYS A 339 16279 17821 16649 2434 -597 255 O ATOM 2718 CB CYS A 339 43.010 15.424 52.759 1.00133.96 C ANISOU 2718 CB CYS A 339 16404 17805 16690 1997 -406 384 C ATOM 2719 SG CYS A 339 44.231 16.096 51.597 1.00117.10 S ANISOU 2719 SG CYS A 339 14038 15943 14508 2114 -327 265 S ATOM 2720 N MET A 340 44.832 15.249 55.384 1.00129.65 N ANISOU 2720 N MET A 340 15841 17254 16163 2137 -552 486 N ATOM 2721 CA MET A 340 46.061 15.547 56.149 1.00113.68 C ANISOU 2721 CA MET A 340 13713 15348 14133 2230 -577 492 C ATOM 2722 C MET A 340 46.584 14.221 56.697 1.00144.62 C ANISOU 2722 C MET A 340 17764 19105 18080 2400 -734 464 C ATOM 2723 O MET A 340 47.809 14.013 56.696 1.00162.69 O ANISOU 2723 O MET A 340 19961 21492 20359 2582 -778 386 O ATOM 2724 CB MET A 340 45.749 16.484 57.307 1.00118.63 C ANISOU 2724 CB MET A 340 14313 16004 14753 2063 -535 623 C ATOM 2725 CG MET A 340 45.622 17.934 56.892 1.00123.43 C ANISOU 2725 CG MET A 340 14766 16798 15332 1935 -403 642 C ATOM 2726 SD MET A 340 45.046 18.967 58.263 1.00126.64 S ANISOU 2726 SD MET A 340 15171 17209 15735 1740 -369 782 S ATOM 2727 CE MET A 340 46.373 20.165 58.408 1.00101.26 C ANISOU 2727 CE MET A 340 11748 14238 12486 1765 -314 775 C ATOM 2728 N GLU A 601 45.654 13.353 57.107 1.00135.40 N ANISOU 2728 N GLU A 601 16804 17700 16938 2336 -820 522 N ATOM 2729 CA GLU A 601 45.955 12.028 57.716 1.00122.21 C ANISOU 2729 CA GLU A 601 15311 15824 15297 2465 -997 519 C ATOM 2730 C GLU A 601 46.504 11.049 56.667 1.00137.63 C ANISOU 2730 C GLU A 601 17296 17730 17263 2693 -1077 360 C ATOM 2731 O GLU A 601 47.517 10.384 56.954 1.00130.50 O ANISOU 2731 O GLU A 601 16406 16802 16373 2898 -1195 296 O ATOM 2732 CB GLU A 601 44.691 11.453 58.360 1.00 94.75 C ANISOU 2732 CB GLU A 601 12050 12121 11828 2289 -1062 636 C ATOM 2733 N PHE A 602 45.833 10.912 55.520 1.00143.90 N ANISOU 2733 N PHE A 602 18113 18508 18055 2665 -1027 294 N ATOM 2734 CA PHE A 602 46.244 9.955 54.456 1.00127.05 C ANISOU 2734 CA PHE A 602 16016 16325 15930 2878 -1103 130 C ATOM 2735 C PHE A 602 47.589 10.387 53.873 1.00125.13 C ANISOU 2735 C PHE A 602 15541 16345 15655 3068 -1053 -3 C ATOM 2736 O PHE A 602 48.223 9.588 53.174 1.00117.09 O ANISOU 2736 O PHE A 602 14524 15324 14638 3291 -1134 -157 O ATOM 2737 CB PHE A 602 45.217 9.888 53.324 1.00105.31 C ANISOU 2737 CB PHE A 602 13307 13533 13170 2784 -1036 93 C ATOM 2738 N LEU A 603 47.965 11.636 54.149 1.00129.48 N ANISOU 2738 N LEU A 603 15900 17121 16173 2972 -927 53 N ATOM 2739 CA LEU A 603 49.185 12.277 53.611 1.00117.40 C ANISOU 2739 CA LEU A 603 14123 15888 14593 3093 -855 -50 C ATOM 2740 C LEU A 603 50.318 12.162 54.626 1.00120.99 C ANISOU 2740 C LEU A 603 14528 16394 15048 3225 -937 -44 C ATOM 2741 O LEU A 603 51.417 12.666 54.327 1.00142.37 O ANISOU 2741 O LEU A 603 17025 19363 17705 3326 -888 -125 O ATOM 2742 CB LEU A 603 48.862 13.745 53.323 1.00 91.70 C ANISOU 2742 CB LEU A 603 10709 12833 11298 2881 -681 22 C ATOM 2743 CG LEU A 603 49.581 14.353 52.122 1.00 98.05 C ANISOU 2743 CG LEU A 603 11293 13925 12036 2935 -582 -94 C ATOM 2744 CD1 LEU A 603 49.619 13.379 50.938 1.00 95.95 C ANISOU 2744 CD1 LEU A 603 11057 13634 11763 3102 -628 -258 C ATOM 2745 CD2 LEU A 603 48.919 15.674 51.731 1.00 95.52 C ANISOU 2745 CD2 LEU A 603 10883 13723 11685 2697 -435 -7 C ATOM 2746 N GLU A 604 50.082 11.518 55.771 1.00116.10 N ANISOU 2746 N GLU A 604 14088 15548 14474 3221 -1060 48 N ATOM 2747 CA GLU A 604 51.124 11.444 56.832 1.00125.22 C ANISOU 2747 CA GLU A 604 15201 16746 15629 3334 -1141 69 C ATOM 2748 C GLU A 604 52.327 10.638 56.315 1.00138.97 C ANISOU 2748 C GLU A 604 16878 18564 17359 3645 -1245 -115 C ATOM 2749 O GLU A 604 53.456 10.984 56.719 1.00151.32 O ANISOU 2749 O GLU A 604 18283 20320 18892 3751 -1246 -147 O ATOM 2750 CB GLU A 604 50.566 10.890 58.146 1.00112.13 C ANISOU 2750 CB GLU A 604 13761 14827 14016 3250 -1259 213 C ATOM 2751 CG GLU A 604 51.117 11.587 59.382 1.00 98.98 C ANISOU 2751 CG GLU A 604 12011 13260 12337 3187 -1243 320 C ATOM 2752 CD GLU A 604 52.561 11.243 59.742 1.00114.77 C ANISOU 2752 CD GLU A 604 13918 15361 14326 3429 -1338 236 C ATOM 2753 OE1 GLU A 604 53.105 11.840 60.699 1.00102.57 O ANISOU 2753 OE1 GLU A 604 12286 13920 12764 3386 -1321 314 O ATOM 2754 OE2 GLU A 604 53.156 10.368 59.080 1.00120.12 O ANISOU 2754 OE2 GLU A 604 14608 16021 15009 3668 -1435 85 O ATOM 2755 N VAL A 605 52.086 9.624 55.471 1.00133.03 N ANISOU 2755 N VAL A 605 16240 17676 16627 3784 -1330 -236 N ATOM 2756 CA VAL A 605 53.111 8.758 54.802 1.00113.01 C ANISOU 2756 CA VAL A 605 13653 15204 14080 4102 -1439 -446 C ATOM 2757 C VAL A 605 54.378 9.567 54.497 1.00 87.65 C ANISOU 2757 C VAL A 605 10135 12374 10793 4201 -1342 -542 C ATOM 2758 O VAL A 605 55.389 9.318 55.115 1.00 82.91 O ANISOU 2758 O VAL A 605 9478 11838 10185 4372 -1432 -585 O ATOM 2759 CB VAL A 605 52.543 8.139 53.511 1.00108.19 C ANISOU 2759 CB VAL A 605 13112 14519 13474 4161 -1445 -572 C ATOM 2760 CG1 VAL A 605 53.657 7.560 52.648 1.00109.96 C ANISOU 2760 CG1 VAL A 605 13208 14908 13662 4475 -1510 -812 C ATOM 2761 CG2 VAL A 605 51.482 7.084 53.798 1.00103.43 C ANISOU 2761 CG2 VAL A 605 12828 13531 12939 4113 -1586 -507 C TER 2762 VAL A 605 HETATM 2763 ZN ZN A1201 29.122 27.497 68.814 1.00 56.13 ZN2+ HETATM 2764 C24 OLC A1202 12.404 36.262 46.648 1.00 99.97 C HETATM 2765 C7 OLC A1202 12.913 34.448 34.936 1.00 58.24 C HETATM 2766 C6 OLC A1202 14.055 34.731 35.909 1.00 71.70 C HETATM 2767 C5 OLC A1202 13.773 34.182 37.299 1.00 82.78 C HETATM 2768 C4 OLC A1202 14.048 35.259 38.344 1.00 76.70 C HETATM 2769 C3 OLC A1202 13.301 34.985 39.622 1.00 60.48 C HETATM 2770 C2 OLC A1202 13.057 36.279 40.392 1.00 81.09 C HETATM 2771 C21 OLC A1202 12.562 36.053 44.195 1.00105.71 C HETATM 2772 C1 OLC A1202 13.283 35.987 41.861 1.00100.92 C HETATM 2773 C22 OLC A1202 12.524 37.033 45.346 1.00 82.62 C HETATM 2774 O19 OLC A1202 14.025 35.081 42.191 1.00106.32 O HETATM 2775 O25 OLC A1202 12.494 37.144 47.772 1.00 81.21 O HETATM 2776 O23 OLC A1202 13.751 37.743 45.361 1.00 77.66 O HETATM 2777 O20 OLC A1202 12.635 36.719 42.934 1.00 96.07 O HETATM 2778 C8 OLC A1203 18.642 30.259 36.173 1.00 58.80 C HETATM 2779 C24 OLC A1203 19.457 29.783 48.178 1.00 81.89 C HETATM 2780 C7 OLC A1203 18.175 31.583 36.783 1.00 74.78 C HETATM 2781 C6 OLC A1203 17.822 31.434 38.260 1.00 69.35 C HETATM 2782 C5 OLC A1203 18.051 32.709 39.084 1.00 61.25 C HETATM 2783 C4 OLC A1203 17.429 32.656 40.492 1.00 59.72 C HETATM 2784 C3 OLC A1203 17.601 31.281 41.132 1.00 62.79 C HETATM 2785 C2 OLC A1203 17.450 31.323 42.642 1.00 76.96 C HETATM 2786 C21 OLC A1203 18.697 30.202 45.857 1.00 88.18 C HETATM 2787 C1 OLC A1203 18.528 30.507 43.372 1.00101.67 C HETATM 2788 C22 OLC A1203 19.884 30.265 46.793 1.00 80.62 C HETATM 2789 O19 OLC A1203 19.043 29.464 42.930 1.00 64.88 O HETATM 2790 O25 OLC A1203 20.298 30.337 49.193 1.00 70.72 O HETATM 2791 O23 OLC A1203 20.909 29.429 46.241 1.00 67.02 O HETATM 2792 O20 OLC A1203 18.965 30.973 44.689 1.00101.69 O HETATM 2793 C8 OLC A1204 28.305 18.372 29.643 1.00 61.86 C HETATM 2794 C24 OLC A1204 25.204 14.985 17.752 1.00111.13 C HETATM 2795 C7 OLC A1204 27.153 17.885 28.765 1.00 76.63 C HETATM 2796 C6 OLC A1204 27.469 16.534 28.134 1.00 85.14 C HETATM 2797 C5 OLC A1204 26.746 16.346 26.802 1.00 93.45 C HETATM 2798 C4 OLC A1204 27.583 16.815 25.611 1.00 98.72 C HETATM 2799 C3 OLC A1204 26.926 16.400 24.296 1.00105.99 C HETATM 2800 C2 OLC A1204 27.939 15.930 23.253 1.00 96.14 C HETATM 2801 C21 OLC A1204 25.642 15.293 20.189 1.00102.04 C HETATM 2802 C1 OLC A1204 27.205 15.232 22.132 1.00111.19 C HETATM 2803 C22 OLC A1204 26.193 15.494 18.791 1.00109.76 C HETATM 2804 O19 OLC A1204 27.170 14.013 22.112 1.00125.94 O HETATM 2805 O25 OLC A1204 25.864 14.789 16.495 1.00100.61 O HETATM 2806 O23 OLC A1204 26.382 16.889 18.587 1.00107.43 O HETATM 2807 O20 OLC A1204 26.527 15.969 21.078 1.00108.93 O HETATM 2808 C10 OLC A1205 28.567 24.901 47.574 1.00 81.28 C HETATM 2809 C9 OLC A1205 28.531 25.127 48.876 1.00 89.07 C HETATM 2810 C11 OLC A1205 28.315 25.978 46.553 1.00 74.49 C HETATM 2811 C8 OLC A1205 28.252 26.479 49.466 1.00 82.97 C HETATM 2812 C24 OLC A1205 31.407 22.971 49.887 1.00 80.21 C HETATM 2813 C12 OLC A1205 28.691 25.403 45.196 1.00 73.66 C HETATM 2814 C7 OLC A1205 27.538 26.323 50.798 1.00 67.56 C HETATM 2815 C13 OLC A1205 27.798 25.940 44.079 1.00 69.69 C HETATM 2816 C6 OLC A1205 28.387 25.578 51.819 1.00 81.39 C HETATM 2817 C14 OLC A1205 28.177 25.338 42.725 1.00 52.15 C HETATM 2818 C5 OLC A1205 28.037 25.990 53.247 1.00 68.04 C HETATM 2819 C4 OLC A1205 28.612 27.371 53.565 1.00 82.45 C HETATM 2820 C3 OLC A1205 30.119 27.344 53.846 1.00 98.49 C HETATM 2821 C2 OLC A1205 30.959 27.842 52.672 1.00 88.61 C HETATM 2822 C21 OLC A1205 32.432 24.536 51.562 1.00 83.96 C HETATM 2823 C1 OLC A1205 32.094 26.889 52.373 1.00 82.12 C HETATM 2824 C22 OLC A1205 31.464 23.374 51.355 1.00 75.73 C HETATM 2825 O19 OLC A1205 33.138 27.347 51.944 1.00 62.86 O HETATM 2826 O25 OLC A1205 30.461 21.908 49.712 1.00 67.80 O HETATM 2827 O23 OLC A1205 31.921 22.253 52.095 1.00 63.70 O HETATM 2828 O20 OLC A1205 31.950 25.442 52.551 1.00 87.92 O HETATM 2829 C24 OLC A1206 20.930 17.344 57.530 1.00 63.19 C HETATM 2830 C5 OLC A1206 25.105 16.083 50.537 1.00 61.61 C HETATM 2831 C4 OLC A1206 24.577 16.147 51.965 1.00 73.72 C HETATM 2832 C3 OLC A1206 25.604 16.804 52.869 1.00 80.67 C HETATM 2833 C2 OLC A1206 24.928 17.795 53.804 1.00 87.20 C HETATM 2834 C21 OLC A1206 23.276 16.721 57.081 1.00 74.70 C HETATM 2835 C1 OLC A1206 24.728 17.154 55.133 1.00 81.69 C HETATM 2836 C22 OLC A1206 22.378 17.639 57.876 1.00 72.32 C HETATM 2837 O19 OLC A1206 25.631 16.520 55.640 1.00 94.80 O HETATM 2838 O25 OLC A1206 20.112 18.422 57.977 1.00 53.02 O HETATM 2839 O23 OLC A1206 22.613 17.360 59.247 1.00 89.79 O HETATM 2840 O20 OLC A1206 23.461 17.291 55.805 1.00 81.16 O HETATM 2841 C8 OLC A1207 23.216 12.248 46.006 1.00 65.46 C HETATM 2842 C24 OLC A1207 21.348 12.315 57.150 1.00 80.65 C HETATM 2843 C7 OLC A1207 22.667 11.917 47.394 1.00 73.89 C HETATM 2844 C6 OLC A1207 23.698 12.215 48.481 1.00 83.81 C HETATM 2845 C5 OLC A1207 23.053 12.295 49.858 1.00 86.77 C HETATM 2846 C4 OLC A1207 24.035 11.885 50.948 1.00 86.89 C HETATM 2847 C3 OLC A1207 23.408 11.951 52.340 1.00 81.96 C HETATM 2848 C2 OLC A1207 24.049 10.916 53.257 1.00 91.92 C HETATM 2849 C21 OLC A1207 23.806 11.954 56.927 1.00 98.15 C HETATM 2850 C1 OLC A1207 24.415 11.547 54.578 1.00 92.06 C HETATM 2851 C22 OLC A1207 22.726 12.724 57.663 1.00 99.74 C HETATM 2852 O19 OLC A1207 25.560 11.846 54.844 1.00103.89 O HETATM 2853 O25 OLC A1207 20.566 13.494 57.035 1.00 70.69 O HETATM 2854 O23 OLC A1207 22.833 12.457 59.069 1.00 72.17 O HETATM 2855 O20 OLC A1207 23.407 11.812 55.569 1.00 97.64 O HETATM 2856 C24 OLC A1208 30.316 9.685 54.155 1.00117.28 C HETATM 2857 C5 OLC A1208 28.583 13.036 45.548 1.00 69.58 C HETATM 2858 C4 OLC A1208 28.073 12.132 46.667 1.00 87.23 C HETATM 2859 C3 OLC A1208 28.534 12.569 48.057 1.00 90.23 C HETATM 2860 C2 OLC A1208 28.061 11.560 49.106 1.00101.80 C HETATM 2861 C21 OLC A1208 28.870 11.186 52.829 1.00122.88 C HETATM 2862 C1 OLC A1208 28.389 12.006 50.519 1.00119.62 C HETATM 2863 C22 OLC A1208 28.992 9.784 53.397 1.00120.60 C HETATM 2864 O19 OLC A1208 28.957 13.062 50.723 1.00124.09 O HETATM 2865 O25 OLC A1208 30.391 8.454 54.875 1.00124.30 O HETATM 2866 O23 OLC A1208 27.870 9.549 54.255 1.00118.89 O HETATM 2867 O20 OLC A1208 28.030 11.192 51.674 1.00121.75 O HETATM 2868 C8 OLC A1209 -15.225 24.635 32.328 1.00 78.51 C HETATM 2869 C24 OLC A1209 -19.331 20.885 20.143 1.00 96.72 C HETATM 2870 C7 OLC A1209 -15.057 23.807 31.055 1.00 82.47 C HETATM 2871 C6 OLC A1209 -15.682 24.418 29.805 1.00 69.67 C HETATM 2872 C5 OLC A1209 -15.949 23.308 28.789 1.00 77.59 C HETATM 2873 C4 OLC A1209 -16.079 23.825 27.357 1.00 80.92 C HETATM 2874 C3 OLC A1209 -16.489 22.682 26.440 1.00 84.95 C HETATM 2875 C2 OLC A1209 -16.499 23.083 24.969 1.00 84.37 C HETATM 2876 C21 OLC A1209 -18.197 21.661 22.202 1.00 99.09 C HETATM 2877 C1 OLC A1209 -16.636 21.840 24.124 1.00 94.85 C HETATM 2878 C22 OLC A1209 -18.183 20.606 21.090 1.00101.25 C HETATM 2879 O19 OLC A1209 -16.563 20.739 24.640 1.00112.23 O HETATM 2880 O25 OLC A1209 -18.996 22.078 19.439 1.00106.16 O HETATM 2881 O23 OLC A1209 -16.948 20.627 20.362 1.00101.26 O HETATM 2882 O20 OLC A1209 -16.881 21.914 22.689 1.00 91.10 O HETATM 2883 C24 OLC A1210 -12.500 20.450 26.514 1.00 80.72 C HETATM 2884 C6 OLC A1210 -11.792 28.356 30.565 1.00 89.90 C HETATM 2885 C5 OLC A1210 -12.409 27.568 29.438 1.00 78.42 C HETATM 2886 C4 OLC A1210 -11.941 28.120 28.095 1.00 71.66 C HETATM 2887 C3 OLC A1210 -12.460 27.252 26.969 1.00 83.91 C HETATM 2888 C2 OLC A1210 -12.516 25.802 27.432 1.00 93.23 C HETATM 2889 C21 OLC A1210 -11.626 22.626 25.701 1.00107.05 C HETATM 2890 C1 OLC A1210 -12.498 24.879 26.256 1.00111.58 C HETATM 2891 C22 OLC A1210 -11.331 21.424 26.578 1.00 99.98 C HETATM 2892 O19 OLC A1210 -12.473 25.294 25.120 1.00132.50 O HETATM 2893 O25 OLC A1210 -12.046 19.188 26.998 1.00 66.83 O HETATM 2894 O23 OLC A1210 -10.145 20.786 26.120 1.00 94.88 O HETATM 2895 O20 OLC A1210 -12.501 23.451 26.449 1.00111.87 O HETATM 2896 C24 OLC A1211 29.245 26.603 16.850 1.00 75.73 C HETATM 2897 C5 OLC A1211 32.194 31.587 21.571 1.00 62.93 C HETATM 2898 C4 OLC A1211 30.797 31.323 22.132 1.00 60.74 C HETATM 2899 C3 OLC A1211 29.719 31.698 21.104 1.00 78.04 C HETATM 2900 C2 OLC A1211 29.343 30.565 20.149 1.00 71.72 C HETATM 2901 C21 OLC A1211 29.633 29.079 16.984 1.00 91.22 C HETATM 2902 C1 OLC A1211 29.735 30.875 18.718 1.00106.26 C HETATM 2903 C22 OLC A1211 28.634 27.986 16.601 1.00 77.73 C HETATM 2904 O19 OLC A1211 30.650 31.661 18.478 1.00115.58 O HETATM 2905 O25 OLC A1211 28.197 25.643 16.856 1.00 61.46 O HETATM 2906 O23 OLC A1211 27.416 28.113 17.347 1.00 76.11 O HETATM 2907 O20 OLC A1211 29.032 30.222 17.608 1.00109.78 O HETATM 2908 C18 OLC A1212 14.782 32.954 27.861 1.00 69.09 C HETATM 2909 C10 OLC A1212 18.262 35.810 30.477 1.00 65.66 C HETATM 2910 C9 OLC A1212 18.531 36.080 29.213 1.00 68.66 C HETATM 2911 C17 OLC A1212 13.715 33.921 27.407 1.00 75.23 C HETATM 2912 C11 OLC A1212 17.134 36.509 31.185 1.00 82.22 C HETATM 2913 C8 OLC A1212 17.695 37.078 28.442 1.00 57.94 C HETATM 2914 C24 OLC A1212 15.930 34.181 17.022 1.00 75.72 C HETATM 2915 C16 OLC A1212 13.874 35.253 28.122 1.00 82.34 C HETATM 2916 C12 OLC A1212 16.178 35.510 31.811 1.00 92.32 C HETATM 2917 C7 OLC A1212 18.409 37.344 27.136 1.00 53.04 C HETATM 2918 C15 OLC A1212 14.387 35.041 29.537 1.00 67.24 C HETATM 2919 C13 OLC A1212 14.744 36.049 31.776 1.00 87.46 C HETATM 2920 C6 OLC A1212 18.375 36.096 26.269 1.00 60.59 C HETATM 2921 C14 OLC A1212 14.275 36.309 30.341 1.00 66.35 C HETATM 2922 C5 OLC A1212 17.128 36.086 25.406 1.00 65.71 C HETATM 2923 C4 OLC A1212 17.293 35.066 24.283 1.00 72.55 C HETATM 2924 C3 OLC A1212 16.041 35.019 23.417 1.00 72.39 C HETATM 2925 C2 OLC A1212 16.293 34.301 22.098 1.00 62.76 C HETATM 2926 C21 OLC A1212 16.573 35.815 18.802 1.00 78.33 C HETATM 2927 C1 OLC A1212 15.711 35.135 20.980 1.00 81.77 C HETATM 2928 C22 OLC A1212 16.238 35.635 17.332 1.00 69.18 C HETATM 2929 O19 OLC A1212 15.013 36.115 21.219 1.00 74.07 O HETATM 2930 O25 OLC A1212 15.446 34.117 15.687 1.00 68.84 O HETATM 2931 O23 OLC A1212 15.092 36.413 17.001 1.00 61.14 O HETATM 2932 O20 OLC A1212 15.979 34.796 19.595 1.00 57.69 O HETATM 2933 C1 PEG A1213 9.257 9.930 10.160 1.00 39.77 C HETATM 2934 O1 PEG A1213 10.432 10.485 10.692 1.00 36.34 O HETATM 2935 C2 PEG A1213 8.524 10.948 9.359 1.00 57.20 C HETATM 2936 O2 PEG A1213 8.107 12.008 10.218 1.00 55.55 O HETATM 2937 C3 PEG A1213 7.272 12.945 9.542 1.00 71.76 C HETATM 2938 C4 PEG A1213 7.056 14.147 10.400 1.00 60.09 C HETATM 2939 O4 PEG A1213 6.661 15.272 9.645 1.00 53.92 O HETATM 2940 O HOH A1301 20.674 28.164 41.681 1.00 52.94 O HETATM 2941 O HOH A1302 20.031 29.360 83.124 1.00 48.19 O HETATM 2942 O HOH A1303 32.714 40.169 67.936 1.00 72.92 O HETATM 2943 O HOH A1304 -2.838 24.139 23.033 1.00 33.82 O HETATM 2944 O HOH A1305 -3.718 36.263 23.919 1.00 51.74 O HETATM 2945 O HOH A1306 28.325 46.556 69.617 1.00 61.34 O HETATM 2946 O HOH A1307 13.672 8.179 23.332 1.00 59.23 O HETATM 2947 O HOH A1308 -4.866 33.965 24.577 1.00 45.56 O HETATM 2948 O HOH A1309 18.155 29.503 58.539 1.00 37.38 O HETATM 2949 O HOH A1310 28.614 13.005 13.266 1.00 45.33 O HETATM 2950 O HOH A1311 12.918 7.033 33.027 1.00 68.42 O HETATM 2951 O HOH A1312 33.307 33.511 18.587 1.00 44.04 O HETATM 2952 O HOH A1313 2.186 12.835 11.322 1.00 40.59 O HETATM 2953 O HOH A1314 10.649 29.023 61.453 1.00 51.60 O HETATM 2954 O HOH A1315 36.553 40.819 66.636 1.00 65.66 O HETATM 2955 O HOH A1316 -4.841 31.456 24.311 1.00 43.18 O HETATM 2956 O HOH A1317 -4.383 22.559 52.879 1.00 43.30 O HETATM 2957 O HOH A1318 15.171 5.999 24.792 1.00 66.33 O CONECT 42 137 CONECT 137 42 CONECT 692 1333 CONECT 1333 692 CONECT 1724 2763 CONECT 1744 2763 CONECT 1975 2763 CONECT 1996 2763 CONECT 2763 1724 1744 1975 1996 CONECT 2764 2773 2775 CONECT 2765 2766 CONECT 2766 2765 2767 CONECT 2767 2766 2768 CONECT 2768 2767 2769 CONECT 2769 2768 2770 CONECT 2770 2769 2772 CONECT 2771 2773 2777 CONECT 2772 2770 2774 2777 CONECT 2773 2764 2771 2776 CONECT 2774 2772 CONECT 2775 2764 CONECT 2776 2773 CONECT 2777 2771 2772 CONECT 2778 2780 CONECT 2779 2788 2790 CONECT 2780 2778 2781 CONECT 2781 2780 2782 CONECT 2782 2781 2783 CONECT 2783 2782 2784 CONECT 2784 2783 2785 CONECT 2785 2784 2787 CONECT 2786 2788 2792 CONECT 2787 2785 2789 2792 CONECT 2788 2779 2786 2791 CONECT 2789 2787 CONECT 2790 2779 CONECT 2791 2788 CONECT 2792 2786 2787 CONECT 2793 2795 CONECT 2794 2803 2805 CONECT 2795 2793 2796 CONECT 2796 2795 2797 CONECT 2797 2796 2798 CONECT 2798 2797 2799 CONECT 2799 2798 2800 CONECT 2800 2799 2802 CONECT 2801 2803 2807 CONECT 2802 2800 2804 2807 CONECT 2803 2794 2801 2806 CONECT 2804 2802 CONECT 2805 2794 CONECT 2806 2803 CONECT 2807 2801 2802 CONECT 2808 2809 2810 CONECT 2809 2808 2811 CONECT 2810 2808 2813 CONECT 2811 2809 2814 CONECT 2812 2824 2826 CONECT 2813 2810 2815 CONECT 2814 2811 2816 CONECT 2815 2813 2817 CONECT 2816 2814 2818 CONECT 2817 2815 CONECT 2818 2816 2819 CONECT 2819 2818 2820 CONECT 2820 2819 2821 CONECT 2821 2820 2823 CONECT 2822 2824 2828 CONECT 2823 2821 2825 2828 CONECT 2824 2812 2822 2827 CONECT 2825 2823 CONECT 2826 2812 CONECT 2827 2824 CONECT 2828 2822 2823 CONECT 2829 2836 2838 CONECT 2830 2831 CONECT 2831 2830 2832 CONECT 2832 2831 2833 CONECT 2833 2832 2835 CONECT 2834 2836 2840 CONECT 2835 2833 2837 2840 CONECT 2836 2829 2834 2839 CONECT 2837 2835 CONECT 2838 2829 CONECT 2839 2836 CONECT 2840 2834 2835 CONECT 2841 2843 CONECT 2842 2851 2853 CONECT 2843 2841 2844 CONECT 2844 2843 2845 CONECT 2845 2844 2846 CONECT 2846 2845 2847 CONECT 2847 2846 2848 CONECT 2848 2847 2850 CONECT 2849 2851 2855 CONECT 2850 2848 2852 2855 CONECT 2851 2842 2849 2854 CONECT 2852 2850 CONECT 2853 2842 CONECT 2854 2851 CONECT 2855 2849 2850 CONECT 2856 2863 2865 CONECT 2857 2858 CONECT 2858 2857 2859 CONECT 2859 2858 2860 CONECT 2860 2859 2862 CONECT 2861 2863 2867 CONECT 2862 2860 2864 2867 CONECT 2863 2856 2861 2866 CONECT 2864 2862 CONECT 2865 2856 CONECT 2866 2863 CONECT 2867 2861 2862 CONECT 2868 2870 CONECT 2869 2878 2880 CONECT 2870 2868 2871 CONECT 2871 2870 2872 CONECT 2872 2871 2873 CONECT 2873 2872 2874 CONECT 2874 2873 2875 CONECT 2875 2874 2877 CONECT 2876 2878 2882 CONECT 2877 2875 2879 2882 CONECT 2878 2869 2876 2881 CONECT 2879 2877 CONECT 2880 2869 CONECT 2881 2878 CONECT 2882 2876 2877 CONECT 2883 2891 2893 CONECT 2884 2885 CONECT 2885 2884 2886 CONECT 2886 2885 2887 CONECT 2887 2886 2888 CONECT 2888 2887 2890 CONECT 2889 2891 2895 CONECT 2890 2888 2892 2895 CONECT 2891 2883 2889 2894 CONECT 2892 2890 CONECT 2893 2883 CONECT 2894 2891 CONECT 2895 2889 2890 CONECT 2896 2903 2905 CONECT 2897 2898 CONECT 2898 2897 2899 CONECT 2899 2898 2900 CONECT 2900 2899 2902 CONECT 2901 2903 2907 CONECT 2902 2900 2904 2907 CONECT 2903 2896 2901 2906 CONECT 2904 2902 CONECT 2905 2896 CONECT 2906 2903 CONECT 2907 2901 2902 CONECT 2908 2911 CONECT 2909 2910 2912 CONECT 2910 2909 2913 CONECT 2911 2908 2915 CONECT 2912 2909 2916 CONECT 2913 2910 2917 CONECT 2914 2928 2930 CONECT 2915 2911 2918 CONECT 2916 2912 2919 CONECT 2917 2913 2920 CONECT 2918 2915 2921 CONECT 2919 2916 2921 CONECT 2920 2917 2922 CONECT 2921 2918 2919 CONECT 2922 2920 2923 CONECT 2923 2922 2924 CONECT 2924 2923 2925 CONECT 2925 2924 2927 CONECT 2926 2928 2932 CONECT 2927 2925 2929 2932 CONECT 2928 2914 2926 2931 CONECT 2929 2927 CONECT 2930 2914 CONECT 2931 2928 CONECT 2932 2926 2927 CONECT 2933 2934 2935 CONECT 2934 2933 CONECT 2935 2933 2936 CONECT 2936 2935 2937 CONECT 2937 2936 2938 CONECT 2938 2937 2939 CONECT 2939 2938 MASTER 461 0 13 18 3 0 15 6 2956 1 185 29 END