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*** pdz de 3nfk ***elNémo ID: 2502031613461658301Job options:ID = 2502031613461658301 JOBID = pdz de 3nfk USERID = unknown PRIVAT = 0 NMODES = 5 DQMIN = -100 DQMAX = 100 DQSTEP = 20 DOGRAPHS = on DOPROJMODS = 0 DORMSD = 0 NRBL = 0 CUTOFF = 0 CAONLY = 0 Input data for this run:
HEADER pdz de 3nfk
HEADER PROTEIN BINDING 10-JUN-10 3NFK
TITLE CRYSTAL STRUCTURE OF THE PTPN4 PDZ DOMAIN COMPLEXED WITH THE C-
TITLE 2 TERMINUS OF A RABIES VIRUS G PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TYROSINE-PROTEIN PHOSPHATASE NON-RECEPTOR TYPE 4;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: PDZ DOMAIN (UNP RESIDUES 499-604);
COMPND 5 SYNONYM: PROTEIN-TYROSINE PHOSPHATASE MEG1, PTPASE-MEG1, MEG;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: GLYCOPROTEIN G;
COMPND 9 CHAIN: C, D;
COMPND 10 FRAGMENT: UNP RESIDUES 512-524;
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: PTPN4;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3) STAR;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PDEST15;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 ORGANISM_SCIENTIFIC: RABIES VIRUS;
SOURCE 14 ORGANISM_TAXID: 11292;
SOURCE 15 OTHER_DETAILS: CYTO13-ATT PEPTIDE HAS BEEN CHEMICALLY SYNTHETIZED.
SOURCE 16 THE SEQUENCE OCCURS NATURALLY IN RABIES VIRUS G PROTEIN
KEYWDS PDZ-PDZ-BINDING SITE COMPLEX, PROTEIN BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR N.BABAULT,F.CORDIER,M.LAFAGE,J.COCKBURN,A.HAOUZ,F.A.REY,M.DELEPIERRE,
AUTHOR 2 H.BUC,M.LAFON,N.WOLFF
REVDAT 4 30-OCT-24 3NFK 1 REMARK
REVDAT 3 06-SEP-23 3NFK 1 REMARK SEQADV
REVDAT 2 30-NOV-11 3NFK 1 JRNL
REVDAT 1 24-AUG-11 3NFK 0
JRNL AUTH N.BABAULT,F.CORDIER,M.LAFAGE,J.COCKBURN,A.HAOUZ,C.PREHAUD,
JRNL AUTH 2 F.A.REY,M.DELEPIERRE,H.BUC,M.LAFON,N.WOLFF
JRNL TITL PEPTIDES TARGETING THE PDZ DOMAIN OF PTPN4 ARE EFFICIENT
JRNL TITL 2 INDUCERS OF GLIOBLASTOMA CELL DEATH.
JRNL REF STRUCTURE V. 19 1518 2011
JRNL REFN ISSN 0969-2126
JRNL PMID 22000519
JRNL DOI 10.1016/J.STR.2011.07.007
REMARK 2
REMARK 2 RESOLUTION. 1.43 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.9.3
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.43
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 14.41
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.7
REMARK 3 NUMBER OF REFLECTIONS : 42710
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) : 0.193
REMARK 3 R VALUE (WORKING SET) : 0.192
REMARK 3 FREE R VALUE : 0.204
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.050
REMARK 3 FREE R VALUE TEST SET COUNT : 2155
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 1.43
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 1.47
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.70
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 3160
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.1876
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3001
REMARK 3 BIN R VALUE (WORKING SET) : 0.1853
REMARK 3 BIN FREE R VALUE : 0.2333
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.03
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 159
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1548
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 12
REMARK 3 SOLVENT ATOMS : 181
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 16.28
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.78
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.22030
REMARK 3 B22 (A**2) : 0.75720
REMARK 3 B33 (A**2) : 0.46310
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.175
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.062
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.950
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.945
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 1600 ; 2.000 ; NULL
REMARK 3 BOND ANGLES : 2160 ; 2.000 ; NULL
REMARK 3 TORSION ANGLES : 579 ; 2.000 ; NULL
REMARK 3 TRIGONAL CARBON PLANES : 47 ; 2.000 ; NULL
REMARK 3 GENERAL PLANES : 232 ; 5.000 ; NULL
REMARK 3 ISOTROPIC THERMAL FACTORS : 1600 ; 20.000 ; NULL
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 201 ; 5.000 ; NULL
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 1976 ; 4.000 ; NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.14
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 4.10
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 13.85
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|513 - A|604 }
REMARK 3 ORIGIN FOR THE GROUP (A): 33.1435 -18.5056 15.3124
REMARK 3 T TENSOR
REMARK 3 T11: -0.0748 T22: -0.0464
REMARK 3 T33: -0.0379 T12: 0.0017
REMARK 3 T13: -0.0011 T23: 0.0080
REMARK 3 L TENSOR
REMARK 3 L11: 1.0555 L22: 1.2897
REMARK 3 L33: 0.6118 L12: 0.0333
REMARK 3 L13: -0.0672 L23: -0.0627
REMARK 3 S TENSOR
REMARK 3 S11: -0.0058 S12: 0.0209 S13: 0.0121
REMARK 3 S21: -0.0172 S22: 0.0061 S23: -0.1331
REMARK 3 S31: 0.0005 S32: 0.0419 S33: -0.0003
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: { C|1 - C|13 }
REMARK 3 ORIGIN FOR THE GROUP (A): 24.4260 -9.4236 18.0277
REMARK 3 T TENSOR
REMARK 3 T11: -0.0200 T22: -0.0039
REMARK 3 T33: 0.0056 T12: -0.0048
REMARK 3 T13: -0.0143 T23: -0.0058
REMARK 3 L TENSOR
REMARK 3 L11: 2.1534 L22: 3.4346
REMARK 3 L33: 1.7466 L12: -0.8889
REMARK 3 L13: -1.1209 L23: -0.2264
REMARK 3 S TENSOR
REMARK 3 S11: 0.0393 S12: 0.1537 S13: 0.0018
REMARK 3 S21: -0.1086 S22: -0.0241 S23: 0.2286
REMARK 3 S31: 0.0717 S32: -0.1022 S33: -0.0152
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: { B|512 - B|591 B|594 - B|604 }
REMARK 3 ORIGIN FOR THE GROUP (A): 27.3935 -1.7889 -5.2299
REMARK 3 T TENSOR
REMARK 3 T11: -0.0365 T22: 0.0188
REMARK 3 T33: -0.0154 T12: -0.0055
REMARK 3 T13: -0.0006 T23: 0.0221
REMARK 3 L TENSOR
REMARK 3 L11: 1.4659 L22: 3.2971
REMARK 3 L33: 1.8874 L12: -1.3715
REMARK 3 L13: 0.2031 L23: -1.0075
REMARK 3 S TENSOR
REMARK 3 S11: -0.0566 S12: -0.0667 S13: 0.0731
REMARK 3 S21: 0.0211 S22: 0.1581 S23: 0.0588
REMARK 3 S31: -0.1304 S32: -0.1310 S33: -0.1014
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: { D|9 - D|13 }
REMARK 3 ORIGIN FOR THE GROUP (A): 34.6610 1.0037 2.3660
REMARK 3 T TENSOR
REMARK 3 T11: 0.0233 T22: 0.0082
REMARK 3 T33: -0.0320 T12: 0.0300
REMARK 3 T13: -0.0207 T23: -0.0216
REMARK 3 L TENSOR
REMARK 3 L11: 0.0207 L22: 0.0000
REMARK 3 L33: 0.3054 L12: 0.3334
REMARK 3 L13: -0.8913 L23: -0.1162
REMARK 3 S TENSOR
REMARK 3 S11: -0.0160 S12: -0.0145 S13: 0.0308
REMARK 3 S21: 0.0268 S22: -0.0158 S23: -0.0154
REMARK 3 S31: -0.0331 S32: 0.0132 S33: 0.0318
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3NFK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-JUN-10.
REMARK 100 THE DEPOSITION ID IS D_1000059766.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-MAY-09
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 : SOLEIL
REMARK 200 BEAMLINE : PROXIMA 1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.918
REMARK 200 MONOCHROMATOR : CRYOGENICALLY COOLED
REMARK 200 MONOCHROMATOR CRYSTAL
REMARK 200 OPTICS : BI-MORPH MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 42795
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.430
REMARK 200 RESOLUTION RANGE LOW (A) : 34.370
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.9
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : 0.06800
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.43
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.51
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.5
REMARK 200 DATA REDUNDANCY IN SHELL : 3.60
REMARK 200 R MERGE FOR SHELL (I) : 0.30100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 4.300
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: PDB ENTRY 2VPH
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.78
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.23
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 24% PEG 1500, 20% GLYCEROL, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 26.71500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 40.90000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 26.85000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 40.90000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 26.71500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 26.85000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1220 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 6040 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -2.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 870 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 5880 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -3.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2280 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11730 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350 BIOMT1 1 -1.000000 0.000000 0.000000 53.43000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 -26.85000
REMARK 350 BIOMT3 1 0.000000 0.000000 -1.000000 40.90000
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, D
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A 498
REMARK 465 SER A 499
REMARK 465 SER A 500
REMARK 465 PRO A 501
REMARK 465 GLU A 502
REMARK 465 LYS A 503
REMARK 465 PRO A 504
REMARK 465 THR A 505
REMARK 465 PRO A 506
REMARK 465 ASN A 507
REMARK 465 GLY A 508
REMARK 465 GLY A 509
REMARK 465 ILE A 510
REMARK 465 PRO A 511
REMARK 465 HIS A 512
REMARK 465 GLY B 498
REMARK 465 SER B 499
REMARK 465 SER B 500
REMARK 465 PRO B 501
REMARK 465 GLU B 502
REMARK 465 LYS B 503
REMARK 465 PRO B 504
REMARK 465 THR B 505
REMARK 465 PRO B 506
REMARK 465 ASN B 507
REMARK 465 GLY B 508
REMARK 465 GLY B 509
REMARK 465 ILE B 510
REMARK 465 PRO B 511
REMARK 465 ARG B 592
REMARK 465 HIS B 593
REMARK 465 SER D 1
REMARK 465 TRP D 2
REMARK 465 GLU D 3
REMARK 465 SER D 4
REMARK 465 HIS D 5
REMARK 465 LYS D 6
REMARK 465 SER D 7
REMARK 465 GLY D 8
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 HIS A 593 CG ND1 CD2 CE1 NE2
REMARK 470 TYR B 536 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 MET B 598 CG SD CE
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 605
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2VPH RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF PTPN4-PDZ
REMARK 900 RELATED ID: 2CS5 RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF PTPN4-PDZ
REMARK 900 RELATED ID: 3NFL RELATED DB: PDB
DBREF 3NFK A 499 604 UNP P29074 PTN4_HUMAN 499 604
DBREF 3NFK B 499 604 UNP P29074 PTN4_HUMAN 499 604
DBREF 3NFK C 1 13 UNP P03524 VGLG_RABVE 512 524
DBREF 3NFK D 1 13 UNP P03524 VGLG_RABVE 512 524
SEQADV 3NFK GLY A 498 UNP P29074 EXPRESSION TAG
SEQADV 3NFK GLY B 498 UNP P29074 EXPRESSION TAG
SEQRES 1 A 107 GLY SER SER PRO GLU LYS PRO THR PRO ASN GLY GLY ILE
SEQRES 2 A 107 PRO HIS ASP ASN LEU VAL LEU ILE ARG MET LYS PRO ASP
SEQRES 3 A 107 GLU ASN GLY ARG PHE GLY PHE ASN VAL LYS GLY GLY TYR
SEQRES 4 A 107 ASP GLN LYS MET PRO VAL ILE VAL SER ARG VAL ALA PRO
SEQRES 5 A 107 GLY THR PRO ALA ASP LEU CYS VAL PRO ARG LEU ASN GLU
SEQRES 6 A 107 GLY ASP GLN VAL VAL LEU ILE ASN GLY ARG ASP ILE ALA
SEQRES 7 A 107 GLU HIS THR HIS ASP GLN VAL VAL LEU PHE ILE LYS ALA
SEQRES 8 A 107 SER CYS GLU ARG HIS SER GLY GLU LEU MET LEU LEU VAL
SEQRES 9 A 107 ARG PRO ASN
SEQRES 1 B 107 GLY SER SER PRO GLU LYS PRO THR PRO ASN GLY GLY ILE
SEQRES 2 B 107 PRO HIS ASP ASN LEU VAL LEU ILE ARG MET LYS PRO ASP
SEQRES 3 B 107 GLU ASN GLY ARG PHE GLY PHE ASN VAL LYS GLY GLY TYR
SEQRES 4 B 107 ASP GLN LYS MET PRO VAL ILE VAL SER ARG VAL ALA PRO
SEQRES 5 B 107 GLY THR PRO ALA ASP LEU CYS VAL PRO ARG LEU ASN GLU
SEQRES 6 B 107 GLY ASP GLN VAL VAL LEU ILE ASN GLY ARG ASP ILE ALA
SEQRES 7 B 107 GLU HIS THR HIS ASP GLN VAL VAL LEU PHE ILE LYS ALA
SEQRES 8 B 107 SER CYS GLU ARG HIS SER GLY GLU LEU MET LEU LEU VAL
SEQRES 9 B 107 ARG PRO ASN
SEQRES 1 C 13 SER TRP GLU SER HIS LYS SER GLY GLY GLU THR ARG LEU
SEQRES 1 D 13 SER TRP GLU SER HIS LYS SER GLY GLY GLU THR ARG LEU
HET GOL A 1 6
HET GOL A 605 6
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 5 GOL 2(C3 H8 O3)
FORMUL 7 HOH *181(H2 O)
HELIX 1 1 TYR A 536 LYS A 539 5 4
HELIX 2 2 THR A 551 CYS A 556 1 6
HELIX 3 3 THR A 578 ALA A 588 1 11
HELIX 4 4 SER A 589 ARG A 592 5 4
HELIX 5 5 TYR B 536 LYS B 539 5 4
HELIX 6 6 THR B 551 CYS B 556 1 6
HELIX 7 7 THR B 578 ALA B 588 1 11
SHEET 1 A 4 VAL A 516 MET A 520 0
SHEET 2 A 4 LEU A 597 ARG A 602 -1 O LEU A 599 N ILE A 518
SHEET 3 A 4 GLN A 565 ILE A 569 -1 N VAL A 567 O LEU A 600
SHEET 4 A 4 ARG A 572 ASP A 573 -1 O ARG A 572 N ILE A 569
SHEET 1 B 4 MET A 540 VAL A 547 0
SHEET 2 B 4 PHE A 530 GLY A 535 -1 N GLY A 535 O MET A 540
SHEET 3 B 4 GLU C 10 ARG C 12 -1 O THR C 11 N VAL A 532
SHEET 4 B 4 LYS C 6 SER C 7 -1 N SER C 7 O GLU C 10
SHEET 1 C 4 VAL B 516 MET B 520 0
SHEET 2 C 4 LEU B 597 ARG B 602 -1 O LEU B 599 N ILE B 518
SHEET 3 C 4 GLN B 565 ILE B 569 -1 N VAL B 567 O LEU B 600
SHEET 4 C 4 ARG B 572 ASP B 573 -1 O ARG B 572 N ILE B 569
SHEET 1 D 3 MET B 540 VAL B 547 0
SHEET 2 D 3 PHE B 530 GLY B 535 -1 N GLY B 535 O MET B 540
SHEET 3 D 3 GLU D 10 ARG D 12 -1 O THR D 11 N VAL B 532
SSBOND 1 CYS A 590 CYS B 590 1555 1555 2.08
CISPEP 1 VAL A 557 PRO A 558 0 -11.94
CISPEP 2 VAL B 557 PRO B 558 0 1.24
SITE 1 AC1 6 HOH A 61 HOH A 315 ASP A 537 PRO A 549
SITE 2 AC1 6 GLY A 550 ASP B 554
SITE 1 AC2 9 HOH A 23 HOH A 28 VAL A 547 ARG A 559
SITE 2 AC2 9 GLU A 562 ASP A 580 ASP B 580 TRP C 2
SITE 3 AC2 9 HOH C 53
CRYST1 53.430 53.700 81.800 90.00 90.00 90.00 P 21 21 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.018716 0.000000 0.000000 0.00000
SCALE2 0.000000 0.018622 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012225 0.00000
ATOM 1 N ASP A 513 48.264 -24.342 19.914 1.00 23.96 N
ANISOU 1 N ASP A 513 2085 2970 4049 226 -319 188 N
ATOM 2 CA ASP A 513 48.245 -25.792 19.826 1.00 22.81 C
ANISOU 2 CA ASP A 513 1943 2793 3932 278 -303 206 C
ATOM 3 C ASP A 513 46.897 -26.289 20.311 1.00 25.07 C
ANISOU 3 C ASP A 513 2338 3081 4107 278 -320 216 C
ATOM 4 O ASP A 513 46.123 -25.481 20.816 1.00 22.27 O
ANISOU 4 O ASP A 513 2044 2756 3661 241 -351 210 O
ATOM 5 CB ASP A 513 49.418 -26.416 20.629 1.00 26.45 C
ANISOU 5 CB ASP A 513 2315 3238 4495 317 -385 243 C
ATOM 6 CG ASP A 513 49.324 -26.279 22.144 1.00 39.91 C
ANISOU 6 CG ASP A 513 4048 4967 6150 310 -517 277 C
ATOM 7 OD1 ASP A 513 48.640 -25.349 22.618 1.00 39.57 O
ANISOU 7 OD1 ASP A 513 4069 4957 6010 265 -548 262 O
ATOM 8 OD2 ASP A 513 49.942 -27.103 22.854 1.00 46.71 O
ANISOU 8 OD2 ASP A 513 4868 5812 7066 350 -589 319 O
ATOM 9 N ASN A 514 46.611 -27.595 20.121 1.00 22.55 N
ANISOU 9 N ASN A 514 2041 2725 3800 318 -292 229 N
ATOM 10 CA ASN A 514 45.363 -28.292 20.470 1.00 20.93 C
ANISOU 10 CA ASN A 514 1930 2511 3510 320 -295 242 C
ATOM 11 C ASN A 514 44.167 -27.708 19.738 1.00 21.34 C
ANISOU 11 C ASN A 514 2054 2583 3473 281 -231 205 C
ATOM 12 O ASN A 514 43.030 -27.795 20.188 1.00 23.82 O
ANISOU 12 O ASN A 514 2442 2905 3703 265 -245 213 O
ATOM 13 CB ASN A 514 45.126 -28.337 22.004 1.00 29.15 C
ANISOU 13 CB ASN A 514 3008 3571 4499 318 -400 288 C
ATOM 14 CG ASN A 514 43.997 -29.271 22.400 1.00 53.59 C
ANISOU 14 CG ASN A 514 6186 6646 7530 326 -397 314 C
ATOM 15 OD1 ASN A 514 43.821 -30.360 21.833 1.00 56.28 O
ANISOU 15 OD1 ASN A 514 6532 6941 7911 353 -347 315 O
ATOM 16 ND2 ASN A 514 43.149 -28.829 23.314 1.00 39.57 N
ANISOU 16 ND2 ASN A 514 4478 4904 5654 298 -438 329 N
ATOM 17 N LEU A 515 44.422 -27.172 18.576 1.00 15.29 N
ANISOU 17 N LEU A 515 1261 1820 2727 269 -158 168 N
ATOM 18 CA LEU A 515 43.379 -26.493 17.833 1.00 12.33 C
ANISOU 18 CA LEU A 515 948 1468 2271 233 -106 139 C
ATOM 19 C LEU A 515 42.508 -27.425 17.031 1.00 13.14 C
ANISOU 19 C LEU A 515 1103 1546 2343 243 -47 118 C
ATOM 20 O LEU A 515 42.953 -28.496 16.612 1.00 13.87 O
ANISOU 20 O LEU A 515 1175 1602 2495 277 -14 112 O
ATOM 21 CB LEU A 515 44.027 -25.440 16.936 1.00 12.13 C
ANISOU 21 CB LEU A 515 878 1459 2273 212 -56 116 C
ATOM 22 CG LEU A 515 44.932 -24.435 17.664 1.00 15.03 C
ANISOU 22 CG LEU A 515 1185 1844 2682 194 -114 129 C
ATOM 23 CD1 LEU A 515 45.595 -23.485 16.650 1.00 17.90 C
ANISOU 23 CD1 LEU A 515 1501 2216 3086 171 -49 111 C
ATOM 24 CD2 LEU A 515 44.160 -23.621 18.671 1.00 14.40 C
ANISOU 24 CD2 LEU A 515 1158 1790 2523 163 -182 136 C
ATOM 25 N VAL A 516 41.260 -27.020 16.840 1.00 11.18 N
ANISOU 25 N VAL A 516 923 1319 2008 213 -36 107 N
ATOM 26 CA VAL A 516 40.251 -27.798 16.148 1.00 10.91 C
ANISOU 26 CA VAL A 516 942 1266 1935 211 6 85 C
ATOM 27 C VAL A 516 39.722 -26.922 15.008 1.00 12.26 C
ANISOU 27 C VAL A 516 1140 1466 2052 182 57 54 C
ATOM 28 O VAL A 516 39.327 -25.762 15.232 1.00 11.18 O
ANISOU 28 O VAL A 516 1016 1362 1871 155 38 62 O
ATOM 29 CB VAL A 516 39.117 -28.178 17.148 1.00 14.78 C
ANISOU 29 CB VAL A 516 1487 1756 2375 202 -41 111 C
ATOM 30 CG1 VAL A 516 37.974 -28.919 16.450 1.00 15.91 C
ANISOU 30 CG1 VAL A 516 1680 1879 2484 192 -4 88 C
ATOM 31 CG2 VAL A 516 39.652 -29.007 18.306 1.00 15.96 C
ANISOU 31 CG2 VAL A 516 1617 1878 2567 230 -95 154 C
ATOM 32 N LEU A 517 39.683 -27.488 13.795 1.00 11.31 N
ANISOU 32 N LEU A 517 1033 1331 1933 189 121 19 N
ATOM 33 CA LEU A 517 39.178 -26.782 12.626 1.00 11.71 C
ANISOU 33 CA LEU A 517 1116 1410 1922 164 167 -7 C
ATOM 34 C LEU A 517 37.784 -27.249 12.317 1.00 15.39 C
ANISOU 34 C LEU A 517 1646 1876 2326 148 162 -24 C
ATOM 35 O LEU A 517 37.574 -28.435 12.024 1.00 17.22 O
ANISOU 35 O LEU A 517 1896 2074 2572 161 177 -48 O
ATOM 36 CB LEU A 517 40.089 -27.069 11.424 1.00 13.63 C
ANISOU 36 CB LEU A 517 1336 1644 2196 180 244 -39 C
ATOM 37 CG LEU A 517 39.808 -26.266 10.127 1.00 16.58 C
ANISOU 37 CG LEU A 517 1743 2052 2503 156 299 -58 C
ATOM 38 CD1 LEU A 517 40.085 -24.809 10.323 1.00 18.92 C
ANISOU 38 CD1 LEU A 517 2016 2379 2793 133 288 -26 C
ATOM 39 CD2 LEU A 517 40.730 -26.733 8.985 1.00 20.66 C
ANISOU 39 CD2 LEU A 517 2244 2559 3046 176 386 -93 C
ATOM 40 N ILE A 518 36.841 -26.321 12.378 1.00 12.93 N
ANISOU 40 N ILE A 518 1364 1597 1953 119 139 -12 N
ATOM 41 CA ILE A 518 35.445 -26.648 12.122 1.00 14.64 C
ANISOU 41 CA ILE A 518 1630 1816 2116 101 127 -25 C
ATOM 42 C ILE A 518 34.931 -25.910 10.913 1.00 15.08 C
ANISOU 42 C ILE A 518 1716 1905 2111 80 152 -42 C
ATOM 43 O ILE A 518 35.265 -24.747 10.715 1.00 13.88 O
ANISOU 43 O ILE A 518 1552 1778 1945 72 160 -25 O
ATOM 44 CB ILE A 518 34.629 -26.265 13.357 1.00 18.27 C
ANISOU 44 CB ILE A 518 2096 2286 2561 89 74 8 C
ATOM 45 CG1 ILE A 518 35.063 -27.127 14.578 1.00 21.07 C
ANISOU 45 CG1 ILE A 518 2433 2610 2963 109 45 32 C
ATOM 46 CG2 ILE A 518 33.085 -26.429 13.079 1.00 21.73 C
ANISOU 46 CG2 ILE A 518 2574 2732 2951 66 62 -1 C
ATOM 47 CD1 ILE A 518 34.514 -26.688 15.910 1.00 22.78 C
ANISOU 47 CD1 ILE A 518 2657 2840 3159 100 -1 66 C
ATOM 48 N ARG A 519 34.131 -26.595 10.103 1.00 15.67 N
ANISOU 48 N ARG A 519 1829 1975 2149 70 160 -73 N
ATOM 49 CA ARG A 519 33.458 -26.000 8.974 1.00 15.92 C
ANISOU 49 CA ARG A 519 1896 2040 2111 50 169 -86 C
ATOM 50 C ARG A 519 31.968 -26.209 9.202 1.00 17.94 C
ANISOU 50 C ARG A 519 2176 2299 2339 29 122 -86 C
ATOM 51 O ARG A 519 31.532 -27.237 9.735 1.00 17.79 O
ANISOU 51 O ARG A 519 2159 2251 2351 29 105 -96 O
ATOM 52 CB ARG A 519 33.894 -26.640 7.665 1.00 19.70 C
ANISOU 52 CB ARG A 519 2403 2516 2565 55 220 -133 C
ATOM 53 CG ARG A 519 35.333 -26.329 7.312 1.00 28.35 C
ANISOU 53 CG ARG A 519 3470 3613 3689 74 280 -132 C
ATOM 54 CD ARG A 519 35.762 -27.066 6.062 1.00 48.48 C
ANISOU 54 CD ARG A 519 6050 6158 6213 83 342 -185 C
ATOM 55 NE ARG A 519 37.206 -26.955 5.852 1.00 60.62 N
ANISOU 55 NE ARG A 519 7547 7689 7798 106 409 -186 N
ATOM 56 CZ ARG A 519 38.093 -27.834 6.303 1.00 77.61 C
ANISOU 56 CZ ARG A 519 9656 9798 10033 136 433 -201 C
ATOM 57 NH1 ARG A 519 37.695 -28.900 6.985 1.00 62.28 N
ANISOU 57 NH1 ARG A 519 7716 7815 8133 147 395 -214 N
ATOM 58 NH2 ARG A 519 39.385 -27.656 6.073 1.00 72.80 N
ANISOU 58 NH2 ARG A 519 9000 9185 9474 157 494 -199 N
ATOM 59 N MET A 520 31.177 -25.205 8.864 1.00 13.33 N
ANISOU 59 N MET A 520 1606 1751 1709 13 101 -68 N
ATOM 60 CA MET A 520 29.722 -25.312 8.997 1.00 11.83 C
ANISOU 60 CA MET A 520 1426 1567 1500 -7 56 -66 C
ATOM 61 C MET A 520 29.034 -24.399 8.018 1.00 12.06 C
ANISOU 61 C MET A 520 1477 1634 1469 -20 41 -58 C
ATOM 62 O MET A 520 29.479 -23.274 7.778 1.00 11.37 O
ANISOU 62 O MET A 520 1388 1567 1364 -15 54 -31 O
ATOM 63 CB MET A 520 29.228 -24.979 10.416 1.00 12.39 C
ANISOU 63 CB MET A 520 1470 1631 1605 -6 29 -31 C
ATOM 64 CG MET A 520 29.516 -23.575 10.878 1.00 13.09 C
ANISOU 64 CG MET A 520 1542 1739 1691 1 27 3 C
ATOM 65 SD MET A 520 28.933 -23.202 12.587 1.00 17.09 S
ANISOU 65 SD MET A 520 2028 2239 2226 3 1 33 S
ATOM 66 CE MET A 520 30.260 -23.840 13.506 1.00 15.32 C
ANISOU 66 CE MET A 520 1788 1990 2041 21 11 36 C
ATOM 67 N LYS A 521 27.986 -24.897 7.426 1.00 12.62 N
ANISOU 67 N LYS A 521 1569 1713 1513 -39 10 -80 N
ATOM 68 CA LYS A 521 27.149 -24.065 6.566 1.00 12.26 C
ANISOU 68 CA LYS A 521 1541 1706 1412 -51 -22 -66 C
ATOM 69 C LYS A 521 26.056 -23.456 7.452 1.00 12.86 C
ANISOU 69 C LYS A 521 1583 1784 1520 -54 -62 -30 C
ATOM 70 O LYS A 521 25.580 -24.104 8.382 1.00 11.60 O
ANISOU 70 O LYS A 521 1400 1602 1407 -58 -71 -34 O
ATOM 71 CB LYS A 521 26.514 -24.904 5.458 1.00 15.53 C
ANISOU 71 CB LYS A 521 1992 2130 1780 -71 -46 -111 C
ATOM 72 CG LYS A 521 27.555 -25.389 4.467 1.00 18.79 C
ANISOU 72 CG LYS A 521 2446 2544 2149 -66 3 -151 C
ATOM 73 CD LYS A 521 26.899 -25.956 3.225 1.00 24.84 C
ANISOU 73 CD LYS A 521 3261 3330 2846 -88 -27 -198 C
ATOM 74 CE LYS A 521 27.939 -26.230 2.163 1.00 34.10 C
ANISOU 74 CE LYS A 521 4484 4513 3960 -80 32 -237 C
ATOM 75 NZ LYS A 521 27.834 -27.621 1.657 1.00 38.19 N
ANISOU 75 NZ LYS A 521 5036 5005 4470 -93 35 -316 N
ATOM 76 N PRO A 522 25.573 -22.252 7.144 1.00 10.02 N
ANISOU 76 N PRO A 522 1220 1450 1137 -51 -83 5 N
ATOM 77 CA PRO A 522 24.458 -21.688 7.915 1.00 9.71 C
ANISOU 77 CA PRO A 522 1145 1411 1134 -50 -115 34 C
ATOM 78 C PRO A 522 23.148 -22.397 7.562 1.00 12.34 C
ANISOU 78 C PRO A 522 1469 1752 1469 -71 -163 16 C
ATOM 79 O PRO A 522 23.088 -23.152 6.559 1.00 12.55 O
ANISOU 79 O PRO A 522 1525 1787 1455 -88 -180 -19 O
ATOM 80 CB PRO A 522 24.396 -20.237 7.425 1.00 11.63 C
ANISOU 80 CB PRO A 522 1392 1673 1352 -38 -124 75 C
ATOM 81 CG PRO A 522 24.904 -20.307 5.991 1.00 14.26 C
ANISOU 81 CG PRO A 522 1772 2031 1615 -44 -120 66 C
ATOM 82 CD PRO A 522 25.997 -21.359 6.043 1.00 11.73 C
ANISOU 82 CD PRO A 522 1467 1694 1297 -46 -74 25 C
ATOM 83 N ASP A 523 22.102 -22.130 8.381 1.00 10.77 N
ANISOU 83 N ASP A 523 1228 1549 1317 -71 -183 36 N
ATOM 84 CA ASP A 523 20.791 -22.611 8.043 1.00 10.63 C
ANISOU 84 CA ASP A 523 1187 1540 1314 -92 -231 26 C
ATOM 85 C ASP A 523 20.269 -21.797 6.849 1.00 16.06 C
ANISOU 85 C ASP A 523 1885 2262 1956 -90 -281 45 C
ATOM 86 O ASP A 523 20.958 -20.897 6.352 1.00 15.17 O
ANISOU 86 O ASP A 523 1800 2162 1801 -73 -268 69 O
ATOM 87 CB ASP A 523 19.868 -22.599 9.272 1.00 12.06 C
ANISOU 87 CB ASP A 523 1314 1705 1564 -92 -226 44 C
ATOM 88 CG ASP A 523 19.498 -21.245 9.824 1.00 12.65 C
ANISOU 88 CG ASP A 523 1359 1787 1660 -65 -220 84 C
ATOM 89 OD1 ASP A 523 19.695 -20.247 9.122 1.00 13.05 O
ANISOU 89 OD1 ASP A 523 1424 1853 1679 -50 -236 106 O
ATOM 90 OD2 ASP A 523 18.979 -21.197 10.954 1.00 15.47 O
ANISOU 90 OD2 ASP A 523 1681 2131 2066 -60 -197 95 O
ATOM 91 N GLU A 524 19.064 -22.126 6.374 1.00 15.71 N
ANISOU 91 N GLU A 524 1815 2231 1921 -110 -340 38 N
ATOM 92 CA GLU A 524 18.481 -21.458 5.211 1.00 16.97 C
ANISOU 92 CA GLU A 524 1985 2428 2035 -109 -403 59 C
ATOM 93 C GLU A 524 18.291 -19.971 5.396 1.00 21.92 C
ANISOU 93 C GLU A 524 2590 3061 2677 -76 -405 119 C
ATOM 94 O GLU A 524 18.268 -19.222 4.401 1.00 23.33 O
ANISOU 94 O GLU A 524 2796 3266 2803 -66 -440 149 O
ATOM 95 CB GLU A 524 17.188 -22.157 4.819 1.00 18.63 C
ANISOU 95 CB GLU A 524 2161 2649 2269 -139 -474 38 C
ATOM 96 CG GLU A 524 17.430 -23.546 4.240 1.00 22.01 C
ANISOU 96 CG GLU A 524 2627 3070 2664 -175 -484 -28 C
ATOM 97 CD GLU A 524 16.182 -24.304 3.812 1.00 30.00 C
ANISOU 97 CD GLU A 524 3606 4090 3704 -213 -561 -57 C
ATOM 98 OE1 GLU A 524 15.079 -23.718 3.862 1.00 27.47 O
ANISOU 98 OE1 GLU A 524 3226 3785 3426 -211 -613 -22 O
ATOM 99 OE2 GLU A 524 16.298 -25.515 3.526 1.00 33.79 O
ANISOU 99 OE2 GLU A 524 4111 4550 4176 -246 -565 -117 O
ATOM 100 N ASN A 525 18.250 -19.520 6.656 1.00 15.92 N
ANISOU 100 N ASN A 525 1791 2275 1984 -57 -362 136 N
ATOM 101 CA ASN A 525 18.149 -18.119 7.004 1.00 15.67 C
ANISOU 101 CA ASN A 525 1739 2236 1978 -23 -352 183 C
ATOM 102 C ASN A 525 19.440 -17.435 7.432 1.00 16.78 C
ANISOU 102 C ASN A 525 1913 2358 2105 -6 -292 193 C
ATOM 103 O ASN A 525 19.401 -16.346 8.003 1.00 17.49 O
ANISOU 103 O ASN A 525 1985 2430 2232 19 -274 222 O
ATOM 104 CB ASN A 525 16.989 -17.844 7.932 1.00 16.65 C
ANISOU 104 CB ASN A 525 1792 2347 2186 -12 -356 196 C
ATOM 105 CG ASN A 525 15.683 -17.969 7.186 1.00 25.18 C
ANISOU 105 CG ASN A 525 2832 3451 3286 -21 -431 208 C
ATOM 106 OD1 ASN A 525 15.242 -17.040 6.491 1.00 23.32 O
ANISOU 106 OD1 ASN A 525 2587 3228 3045 0 -478 249 O
ATOM 107 ND2 ASN A 525 15.136 -19.168 7.160 1.00 16.16 N
ANISOU 107 ND2 ASN A 525 1668 2313 2158 -55 -453 172 N
ATOM 108 N GLY A 526 20.584 -18.079 7.162 1.00 13.18 N
ANISOU 108 N GLY A 526 1503 1903 1603 -19 -261 166 N
ATOM 109 CA GLY A 526 21.895 -17.473 7.343 1.00 12.98 C
ANISOU 109 CA GLY A 526 1505 1863 1563 -8 -211 176 C
ATOM 110 C GLY A 526 22.465 -17.531 8.749 1.00 13.62 C
ANISOU 110 C GLY A 526 1568 1915 1691 -1 -165 161 C
ATOM 111 O GLY A 526 23.474 -16.874 9.046 1.00 15.53 O
ANISOU 111 O GLY A 526 1822 2143 1936 7 -132 170 O
ATOM 112 N ARG A 527 21.817 -18.287 9.638 1.00 11.67 N
ANISOU 112 N ARG A 527 1293 1661 1481 -8 -166 141 N
ATOM 113 CA ARG A 527 22.214 -18.348 11.043 1.00 10.88 C
ANISOU 113 CA ARG A 527 1180 1538 1415 -1 -128 132 C
ATOM 114 C ARG A 527 22.953 -19.624 11.377 1.00 10.60 C
ANISOU 114 C ARG A 527 1159 1494 1372 -15 -108 103 C
ATOM 115 O ARG A 527 22.660 -20.696 10.828 1.00 10.51 O
ANISOU 115 O ARG A 527 1154 1488 1351 -33 -123 83 O
ATOM 116 CB ARG A 527 21.016 -18.197 11.956 1.00 13.01 C
ANISOU 116 CB ARG A 527 1409 1803 1731 5 -129 138 C
ATOM 117 CG ARG A 527 20.313 -16.852 11.684 1.00 15.73 C
ANISOU 117 CG ARG A 527 1732 2147 2097 27 -146 168 C
ATOM 118 CD ARG A 527 19.251 -16.528 12.727 1.00 25.28 C
ANISOU 118 CD ARG A 527 2898 3347 3360 41 -130 171 C
ATOM 119 NE ARG A 527 18.508 -15.311 12.381 1.00 34.04 N
ANISOU 119 NE ARG A 527 3981 4451 4502 67 -148 200 N
ATOM 120 CZ ARG A 527 17.343 -15.290 11.734 1.00 47.67 C
ANISOU 120 CZ ARG A 527 5668 6190 6255 70 -190 218 C
ATOM 121 NH1 ARG A 527 16.752 -16.425 11.373 1.00 26.81 N
ANISOU 121 NH1 ARG A 527 3007 3568 3611 44 -218 206 N
ATOM 122 NH2 ARG A 527 16.750 -14.135 11.462 1.00 41.28 N
ANISOU 122 NH2 ARG A 527 4834 5371 5482 99 -207 249 N
ATOM 123 N PHE A 528 23.904 -19.503 12.281 1.00 8.72 N
ANISOU 123 N PHE A 528 929 1242 1144 -6 -79 101 N
ATOM 124 CA PHE A 528 24.753 -20.634 12.676 1.00 8.16 C
ANISOU 124 CA PHE A 528 869 1158 1073 -13 -62 82 C
ATOM 125 C PHE A 528 24.363 -21.220 14.031 1.00 8.88 C
ANISOU 125 C PHE A 528 948 1237 1190 -14 -52 83 C
ATOM 126 O PHE A 528 24.656 -22.395 14.247 1.00 9.87 O
ANISOU 126 O PHE A 528 1080 1348 1323 -21 -46 73 O
ATOM 127 CB PHE A 528 26.200 -20.189 12.727 1.00 8.83 C
ANISOU 127 CB PHE A 528 965 1236 1152 -3 -42 82 C
ATOM 128 CG PHE A 528 26.744 -19.815 11.375 1.00 8.31 C
ANISOU 128 CG PHE A 528 917 1183 1058 -5 -37 83 C
ATOM 129 CD1 PHE A 528 27.113 -20.796 10.455 1.00 9.52 C
ANISOU 129 CD1 PHE A 528 1089 1340 1190 -12 -30 60 C
ATOM 130 CD2 PHE A 528 26.878 -18.487 11.015 1.00 9.42 C
ANISOU 130 CD2 PHE A 528 1058 1327 1193 1 -36 107 C
ATOM 131 CE1 PHE A 528 27.642 -20.455 9.217 1.00 11.27 C
ANISOU 131 CE1 PHE A 528 1333 1576 1373 -14 -16 61 C
ATOM 132 CE2 PHE A 528 27.373 -18.138 9.752 1.00 10.39 C
ANISOU 132 CE2 PHE A 528 1202 1463 1283 -2 -25 116 C
ATOM 133 CZ PHE A 528 27.749 -19.123 8.859 1.00 10.12 C
ANISOU 133 CZ PHE A 528 1189 1439 1216 -10 -14 93 C
ATOM 134 N GLY A 529 23.777 -20.435 14.933 1.00 7.35 N
ANISOU 134 N GLY A 529 739 1044 1008 -5 -45 96 N
ATOM 135 CA GLY A 529 23.320 -20.988 16.206 1.00 8.47 C
ANISOU 135 CA GLY A 529 876 1180 1164 -7 -28 100 C
ATOM 136 C GLY A 529 24.267 -20.849 17.366 1.00 10.52 C
ANISOU 136 C GLY A 529 1153 1432 1410 3 -15 102 C
ATOM 137 O GLY A 529 24.019 -21.453 18.410 1.00 11.88 O
ANISOU 137 O GLY A 529 1330 1601 1581 1 -1 110 O
ATOM 138 N PHE A 530 25.345 -20.082 17.223 1.00 7.72 N
ANISOU 138 N PHE A 530 808 1077 1047 12 -21 97 N
ATOM 139 CA PHE A 530 26.260 -19.845 18.314 1.00 7.61 C
ANISOU 139 CA PHE A 530 809 1060 1024 20 -21 95 C
ATOM 140 C PHE A 530 26.316 -18.374 18.627 1.00 9.47 C
ANISOU 140 C PHE A 530 1045 1295 1258 28 -20 87 C
ATOM 141 O PHE A 530 26.033 -17.519 17.778 1.00 9.03 O
ANISOU 141 O PHE A 530 979 1236 1214 30 -20 88 O
ATOM 142 CB PHE A 530 27.647 -20.444 18.053 1.00 8.58 C
ANISOU 142 CB PHE A 530 935 1174 1151 20 -32 93 C
ATOM 143 CG PHE A 530 28.458 -19.756 16.986 1.00 7.63 C
ANISOU 143 CG PHE A 530 806 1053 1040 20 -33 86 C
ATOM 144 CD1 PHE A 530 29.424 -18.808 17.326 1.00 9.83 C
ANISOU 144 CD1 PHE A 530 1081 1328 1327 23 -40 83 C
ATOM 145 CD2 PHE A 530 28.276 -20.071 15.642 1.00 9.11 C
ANISOU 145 CD2 PHE A 530 992 1243 1225 15 -27 84 C
ATOM 146 CE1 PHE A 530 30.181 -18.183 16.343 1.00 10.84 C
ANISOU 146 CE1 PHE A 530 1198 1452 1468 19 -32 83 C
ATOM 147 CE2 PHE A 530 29.050 -19.455 14.658 1.00 9.42 C
ANISOU 147 CE2 PHE A 530 1029 1285 1265 15 -18 84 C
ATOM 148 CZ PHE A 530 29.988 -18.497 15.015 1.00 10.18 C
ANISOU 148 CZ PHE A 530 1117 1374 1377 16 -17 87 C
ATOM 149 N ASN A 531 26.674 -18.108 19.885 1.00 8.65 N
ANISOU 149 N ASN A 531 957 1191 1138 31 -20 79 N
ATOM 150 CA ASN A 531 26.886 -16.730 20.323 1.00 8.62 C
ANISOU 150 CA ASN A 531 960 1179 1135 37 -21 61 C
ATOM 151 C ASN A 531 28.337 -16.580 20.663 1.00 9.33 C
ANISOU 151 C ASN A 531 1056 1265 1225 31 -47 52 C
ATOM 152 O ASN A 531 29.015 -17.537 21.022 1.00 9.67 O
ANISOU 152 O ASN A 531 1102 1314 1258 29 -63 60 O
ATOM 153 CB ASN A 531 26.102 -16.440 21.619 1.00 9.80 C
ANISOU 153 CB ASN A 531 1129 1335 1261 44 -1 49 C
ATOM 154 CG ASN A 531 24.624 -16.522 21.504 1.00 10.53 C
ANISOU 154 CG ASN A 531 1206 1432 1364 50 30 57 C
ATOM 155 OD1 ASN A 531 24.058 -16.913 20.491 1.00 10.98 O
ANISOU 155 OD1 ASN A 531 1237 1490 1445 47 29 73 O
ATOM 156 ND2 ASN A 531 23.949 -16.264 22.620 1.00 14.23 N
ANISOU 156 ND2 ASN A 531 1689 1906 1812 58 60 44 N
ATOM 157 N VAL A 532 28.822 -15.331 20.572 1.00 9.18 N
ANISOU 157 N VAL A 532 1034 1230 1223 29 -54 36 N
ATOM 158 CA VAL A 532 30.190 -15.037 20.996 1.00 9.64 C
ANISOU 158 CA VAL A 532 1091 1281 1291 19 -83 23 C
ATOM 159 C VAL A 532 30.219 -13.855 21.962 1.00 10.12 C
ANISOU 159 C VAL A 532 1171 1330 1346 15 -92 -10 C
ATOM 160 O VAL A 532 29.350 -12.983 21.894 1.00 9.25 O
ANISOU 160 O VAL A 532 1068 1204 1243 22 -69 -22 O
ATOM 161 CB VAL A 532 31.145 -14.716 19.822 1.00 12.93 C
ANISOU 161 CB VAL A 532 1478 1684 1749 9 -84 33 C
ATOM 162 CG1 VAL A 532 31.375 -15.949 18.941 1.00 13.58 C
ANISOU 162 CG1 VAL A 532 1547 1779 1834 13 -75 55 C
ATOM 163 CG2 VAL A 532 30.661 -13.521 18.985 1.00 14.07 C
ANISOU 163 CG2 VAL A 532 1619 1808 1918 8 -64 37 C
ATOM 164 N LYS A 533 31.215 -13.855 22.865 1.00 9.68 N
ANISOU 164 N LYS A 533 1124 1278 1278 6 -130 -28 N
ATOM 165 CA LYS A 533 31.566 -12.727 23.719 1.00 10.03 C
ANISOU 165 CA LYS A 533 1186 1305 1319 -5 -151 -70 C
ATOM 166 C LYS A 533 33.040 -12.429 23.409 1.00 11.09 C
ANISOU 166 C LYS A 533 1287 1426 1501 -25 -189 -73 C
ATOM 167 O LYS A 533 33.724 -13.262 22.775 1.00 10.57 O
ANISOU 167 O LYS A 533 1189 1370 1458 -25 -196 -43 O
ATOM 168 CB LYS A 533 31.433 -13.055 25.225 1.00 12.09 C
ANISOU 168 CB LYS A 533 1491 1591 1511 -2 -172 -92 C
ATOM 169 CG LYS A 533 29.992 -13.208 25.701 1.00 15.65 C
ANISOU 169 CG LYS A 533 1974 2055 1918 15 -124 -94 C
ATOM 170 CD LYS A 533 29.907 -13.623 27.149 1.00 17.24 C
ANISOU 170 CD LYS A 533 2225 2285 2041 17 -136 -108 C
ATOM 171 CE LYS A 533 28.485 -13.814 27.592 1.00 20.69 C
ANISOU 171 CE LYS A 533 2687 2735 2440 33 -76 -106 C
ATOM 172 NZ LYS A 533 28.428 -14.060 29.078 1.00 26.22 N
ANISOU 172 NZ LYS A 533 3447 3465 3051 33 -80 -122 N
ATOM 173 N GLY A 534 33.529 -11.276 23.861 1.00 9.59 N
ANISOU 173 N GLY A 534 1102 1211 1333 -43 -212 -111 N
ATOM 174 CA GLY A 534 34.942 -10.966 23.689 1.00 10.22 C
ANISOU 174 CA GLY A 534 1142 1275 1466 -68 -251 -116 C
ATOM 175 C GLY A 534 35.289 -10.148 22.456 1.00 12.26 C
ANISOU 175 C GLY A 534 1363 1497 1798 -82 -222 -100 C
ATOM 176 O GLY A 534 34.419 -9.726 21.689 1.00 10.37 O
ANISOU 176 O GLY A 534 1133 1242 1567 -71 -177 -84 O
ATOM 177 N GLY A 535 36.578 -9.941 22.271 1.00 11.19 N
ANISOU 177 N GLY A 535 1184 1349 1719 -107 -249 -100 N
ATOM 178 CA GLY A 535 37.094 -9.099 21.203 1.00 11.25 C
ANISOU 178 CA GLY A 535 1155 1319 1801 -127 -220 -83 C
ATOM 179 C GLY A 535 38.021 -8.055 21.803 1.00 11.10 C
ANISOU 179 C GLY A 535 1116 1263 1837 -164 -262 -122 C
ATOM 180 O GLY A 535 38.057 -7.826 23.022 1.00 11.72 O
ANISOU 180 O GLY A 535 1222 1344 1886 -172 -313 -170 O
ATOM 181 N TYR A 536 38.793 -7.409 20.950 1.00 10.66 N
ANISOU 181 N TYR A 536 1016 1174 1861 -190 -241 -102 N
ATOM 182 CA TYR A 536 39.812 -6.460 21.394 1.00 10.53 C
ANISOU 182 CA TYR A 536 966 1117 1916 -234 -282 -136 C
ATOM 183 C TYR A 536 39.233 -5.346 22.261 1.00 12.79 C
ANISOU 183 C TYR A 536 1302 1364 2194 -245 -304 -192 C
ATOM 184 O TYR A 536 39.847 -4.932 23.237 1.00 14.22 O
ANISOU 184 O TYR A 536 1481 1533 2390 -273 -366 -245 O
ATOM 185 CB TYR A 536 40.515 -5.862 20.181 1.00 13.69 C
ANISOU 185 CB TYR A 536 1315 1481 2406 -260 -234 -95 C
ATOM 186 CG TYR A 536 41.569 -4.851 20.536 1.00 17.24 C
ANISOU 186 CG TYR A 536 1722 1882 2948 -311 -270 -125 C
ATOM 187 CD1 TYR A 536 42.850 -5.251 20.903 1.00 19.19 C
ANISOU 187 CD1 TYR A 536 1902 2143 3245 -335 -319 -135 C
ATOM 188 CD2 TYR A 536 41.298 -3.485 20.488 1.00 19.41 C
ANISOU 188 CD2 TYR A 536 2017 2089 3270 -336 -256 -143 C
ATOM 189 CE1 TYR A 536 43.826 -4.316 21.236 1.00 20.52 C
ANISOU 189 CE1 TYR A 536 2023 2265 3508 -388 -358 -166 C
ATOM 190 CE2 TYR A 536 42.248 -2.548 20.866 1.00 22.15 C
ANISOU 190 CE2 TYR A 536 2326 2384 3708 -389 -293 -177 C
ATOM 191 CZ TYR A 536 43.514 -2.966 21.214 1.00 23.49 C
ANISOU 191 CZ TYR A 536 2427 2574 3927 -417 -345 -188 C
ATOM 192 OH TYR A 536 44.442 -2.006 21.511 1.00 24.55 O
ANISOU 192 OH TYR A 536 2515 2652 4161 -475 -382 -221 O
ATOM 193 N ASP A 537 38.036 -4.854 21.891 1.00 12.05 N
ANISOU 193 N ASP A 537 1252 1248 2077 -222 -254 -184 N
ATOM 194 CA ASP A 537 37.372 -3.792 22.648 1.00 11.15 C
ANISOU 194 CA ASP A 537 1188 1090 1960 -224 -262 -240 C
ATOM 195 C ASP A 537 36.865 -4.255 24.006 1.00 13.62 C
ANISOU 195 C ASP A 537 1551 1441 2182 -206 -299 -294 C
ATOM 196 O ASP A 537 36.618 -3.407 24.872 1.00 13.94 O
ANISOU 196 O ASP A 537 1632 1448 2217 -216 -317 -358 O
ATOM 197 CB ASP A 537 36.209 -3.260 21.818 1.00 10.82 C
ANISOU 197 CB ASP A 537 1170 1018 1925 -196 -197 -206 C
ATOM 198 CG ASP A 537 35.219 -4.293 21.353 1.00 10.31 C
ANISOU 198 CG ASP A 537 1119 1007 1792 -152 -164 -163 C
ATOM 199 OD1 ASP A 537 35.641 -5.429 21.030 1.00 10.25 O
ANISOU 199 OD1 ASP A 537 1088 1050 1757 -148 -169 -131 O
ATOM 200 OD2 ASP A 537 34.017 -3.952 21.236 1.00 11.35 O
ANISOU 200 OD2 ASP A 537 1281 1124 1907 -122 -131 -159 O
ATOM 201 N GLN A 538 36.718 -5.556 24.207 1.00 12.36 N
ANISOU 201 N GLN A 538 1395 1347 1954 -182 -307 -270 N
ATOM 202 CA GLN A 538 36.286 -6.123 25.479 1.00 12.35 C
ANISOU 202 CA GLN A 538 1444 1388 1860 -167 -339 -307 C
ATOM 203 C GLN A 538 37.501 -6.588 26.307 1.00 16.63 C
ANISOU 203 C GLN A 538 1969 1960 2391 -191 -421 -328 C
ATOM 204 O GLN A 538 37.314 -7.059 27.428 1.00 18.67 O
ANISOU 204 O GLN A 538 2272 2256 2565 -183 -458 -356 O
ATOM 205 CB GLN A 538 35.304 -7.265 25.264 1.00 11.20 C
ANISOU 205 CB GLN A 538 1316 1290 1648 -126 -299 -264 C
ATOM 206 CG GLN A 538 33.992 -6.768 24.645 1.00 11.32 C
ANISOU 206 CG GLN A 538 1351 1281 1671 -100 -230 -251 C
ATOM 207 CD GLN A 538 32.953 -7.853 24.611 1.00 11.22 C
ANISOU 207 CD GLN A 538 1354 1314 1594 -66 -197 -219 C
ATOM 208 OE1 GLN A 538 33.069 -8.905 25.285 1.00 12.51 O
ANISOU 208 OE1 GLN A 538 1531 1524 1697 -60 -221 -214 O
ATOM 209 NE2 GLN A 538 31.937 -7.637 23.806 1.00 10.79 N
ANISOU 209 NE2 GLN A 538 1297 1246 1558 -44 -146 -192 N
ATOM 210 N LYS A 539 38.717 -6.503 25.728 1.00 14.79 N
ANISOU 210 N LYS A 539 1668 1710 2241 -220 -447 -308 N
ATOM 211 CA LYS A 539 39.969 -6.899 26.396 1.00 15.08 C
ANISOU 211 CA LYS A 539 1669 1771 2291 -245 -531 -322 C
ATOM 212 C LYS A 539 39.939 -8.347 26.807 1.00 19.18 C
ANISOU 212 C LYS A 539 2196 2353 2738 -213 -555 -287 C
ATOM 213 O LYS A 539 40.492 -8.741 27.845 1.00 19.51 O
ANISOU 213 O LYS A 539 2247 2427 2740 -219 -633 -307 O
ATOM 214 CB LYS A 539 40.301 -6.001 27.612 1.00 18.14 C
ANISOU 214 CB LYS A 539 2091 2140 2664 -278 -603 -402 C
ATOM 215 CG LYS A 539 40.329 -4.517 27.322 1.00 23.58 C
ANISOU 215 CG LYS A 539 2776 2752 3429 -312 -583 -444 C
ATOM 216 CD LYS A 539 40.585 -3.776 28.637 1.00 35.83 C
ANISOU 216 CD LYS A 539 4374 4290 4950 -343 -659 -535 C
ATOM 217 CE LYS A 539 39.664 -2.603 28.878 1.00 46.60 C
ANISOU 217 CE LYS A 539 5801 5597 6307 -343 -616 -596 C
ATOM 218 NZ LYS A 539 39.858 -1.528 27.868 1.00 45.37 N
ANISOU 218 NZ LYS A 539 5602 5359 6276 -368 -571 -584 N
ATOM 219 N MET A 540 39.247 -9.157 25.995 1.00 16.74 N
ANISOU 219 N MET A 540 1887 2062 2412 -179 -489 -234 N
ATOM 220 CA AMET A 540 39.241 -10.578 26.254 0.50 17.09 C
ANISOU 220 CA AMET A 540 1933 2155 2404 -150 -504 -196 C
ATOM 221 CA BMET A 540 39.046 -10.579 26.253 0.50 16.03 C
ANISOU 221 CA BMET A 540 1808 2022 2261 -147 -496 -196 C
ATOM 222 C MET A 540 39.165 -11.350 24.965 1.00 17.92 C
ANISOU 222 C MET A 540 1998 2262 2547 -129 -443 -139 C
ATOM 223 O MET A 540 38.767 -10.804 23.923 1.00 15.46 O
ANISOU 223 O MET A 540 1677 1924 2273 -131 -381 -127 O
ATOM 224 CB AMET A 540 38.204 -10.996 27.303 0.50 20.22 C
ANISOU 224 CB AMET A 540 2409 2584 2689 -127 -507 -210 C
ATOM 225 CB BMET A 540 37.617 -10.803 26.806 0.50 18.00 C
ANISOU 225 CB BMET A 540 2135 2291 2415 -120 -460 -204 C
ATOM 226 CG AMET A 540 36.804 -10.729 26.908 0.50 24.00 C
ANISOU 226 CG AMET A 540 2929 3052 3138 -108 -428 -209 C
ATOM 227 CG BMET A 540 37.418 -10.331 28.252 0.50 22.77 C
ANISOU 227 CG BMET A 540 2802 2907 2941 -129 -506 -260 C
ATOM 228 SD AMET A 540 35.733 -11.350 28.207 0.50 29.80 S
ANISOU 228 SD AMET A 540 3746 3830 3748 -84 -425 -220 S
ATOM 229 SD BMET A 540 38.580 -11.021 29.467 0.50 29.11 S
ANISOU 229 SD BMET A 540 3606 3753 3703 -140 -619 -264 S
ATOM 230 CE AMET A 540 34.171 -10.875 27.534 0.50 24.78 C
ANISOU 230 CE AMET A 540 3130 3172 3114 -64 -329 -219 C
ATOM 231 CE BMET A 540 38.097 -12.739 29.476 0.50 25.43 C
ANISOU 231 CE BMET A 540 3153 3331 3179 -98 -597 -191 C
ATOM 232 N PRO A 541 39.603 -12.629 24.967 1.00 16.60 N
ANISOU 232 N PRO A 541 1807 2125 2376 -108 -461 -102 N
ATOM 233 CA PRO A 541 39.577 -13.369 23.705 1.00 14.45 C
ANISOU 233 CA PRO A 541 1499 1852 2140 -90 -400 -58 C
ATOM 234 C PRO A 541 38.122 -13.608 23.254 1.00 14.26 C
ANISOU 234 C PRO A 541 1527 1833 2060 -69 -337 -46 C
ATOM 235 O PRO A 541 37.166 -13.543 24.067 1.00 13.48 O
ANISOU 235 O PRO A 541 1484 1745 1891 -61 -340 -62 O
ATOM 236 CB PRO A 541 40.227 -14.712 24.055 1.00 17.90 C
ANISOU 236 CB PRO A 541 1911 2314 2578 -68 -439 -29 C
ATOM 237 CG PRO A 541 40.040 -14.849 25.540 1.00 24.64 C
ANISOU 237 CG PRO A 541 2814 3191 3356 -66 -507 -45 C
ATOM 238 CD PRO A 541 40.148 -13.462 26.073 1.00 19.04 C
ANISOU 238 CD PRO A 541 2120 2466 2647 -99 -537 -97 C
ATOM 239 N VAL A 542 37.949 -13.834 21.944 1.00 11.88 N
ANISOU 239 N VAL A 542 1203 1522 1788 -61 -277 -19 N
ATOM 240 CA VAL A 542 36.635 -14.170 21.410 1.00 11.44 C
ANISOU 240 CA VAL A 542 1185 1473 1687 -43 -226 -4 C
ATOM 241 C VAL A 542 36.307 -15.595 21.841 1.00 12.52 C
ANISOU 241 C VAL A 542 1339 1635 1782 -19 -235 15 C
ATOM 242 O VAL A 542 37.087 -16.514 21.577 1.00 12.08 O
ANISOU 242 O VAL A 542 1250 1584 1756 -10 -243 34 O
ATOM 243 CB VAL A 542 36.559 -13.993 19.885 1.00 13.91 C
ANISOU 243 CB VAL A 542 1478 1775 2034 -44 -169 18 C
ATOM 244 CG1 VAL A 542 35.222 -14.479 19.357 1.00 12.81 C
ANISOU 244 CG1 VAL A 542 1372 1646 1848 -26 -132 32 C
ATOM 245 CG2 VAL A 542 36.765 -12.524 19.521 1.00 15.09 C
ANISOU 245 CG2 VAL A 542 1618 1893 2224 -67 -158 8 C
ATOM 246 N ILE A 543 35.234 -15.768 22.588 1.00 11.78 N
ANISOU 246 N ILE A 543 1294 1555 1628 -10 -234 10 N
ATOM 247 CA ILE A 543 34.833 -17.081 23.152 1.00 10.92 C
ANISOU 247 CA ILE A 543 1207 1466 1477 8 -240 33 C
ATOM 248 C ILE A 543 33.403 -17.378 22.731 1.00 12.74 C
ANISOU 248 C ILE A 543 1464 1699 1678 17 -190 42 C
ATOM 249 O ILE A 543 32.535 -16.481 22.745 1.00 13.31 O
ANISOU 249 O ILE A 543 1555 1768 1735 13 -167 24 O
ATOM 250 CB ILE A 543 34.933 -17.071 24.722 1.00 16.14 C
ANISOU 250 CB ILE A 543 1905 2145 2083 7 -291 22 C
ATOM 251 CG1 ILE A 543 36.326 -16.620 25.234 1.00 18.89 C
ANISOU 251 CG1 ILE A 543 2225 2491 2460 -6 -356 6 C
ATOM 252 CG2 ILE A 543 34.524 -18.427 25.385 1.00 20.22 C
ANISOU 252 CG2 ILE A 543 2450 2678 2553 25 -296 57 C
ATOM 253 CD1 ILE A 543 37.442 -17.621 25.120 1.00 28.20 C
ANISOU 253 CD1 ILE A 543 3359 3672 3683 5 -392 37 C
ATOM 254 N VAL A 544 33.136 -18.663 22.438 1.00 10.46 N
ANISOU 254 N VAL A 544 1174 1413 1387 29 -176 68 N
ATOM 255 CA VAL A 544 31.772 -19.105 22.151 1.00 10.13 C
ANISOU 255 CA VAL A 544 1152 1375 1322 32 -137 78 C
ATOM 256 C VAL A 544 31.061 -19.153 23.485 1.00 12.45 C
ANISOU 256 C VAL A 544 1485 1683 1562 34 -140 79 C
ATOM 257 O VAL A 544 31.490 -19.862 24.414 1.00 12.11 O
ANISOU 257 O VAL A 544 1459 1649 1493 39 -168 96 O
ATOM 258 CB VAL A 544 31.793 -20.487 21.481 1.00 11.57 C
ANISOU 258 CB VAL A 544 1323 1549 1525 40 -125 100 C
ATOM 259 CG1 VAL A 544 30.364 -20.991 21.259 1.00 11.18 C
ANISOU 259 CG1 VAL A 544 1289 1501 1458 38 -92 108 C
ATOM 260 CG2 VAL A 544 32.539 -20.393 20.153 1.00 11.73 C
ANISOU 260 CG2 VAL A 544 1310 1558 1590 39 -112 93 C
ATOM 261 N SER A 545 29.965 -18.398 23.612 1.00 10.11 N
ANISOU 261 N SER A 545 1205 1391 1247 32 -110 63 N
ATOM 262 CA SER A 545 29.248 -18.311 24.864 1.00 9.54 C
ANISOU 262 CA SER A 545 1172 1334 1120 35 -98 59 C
ATOM 263 C SER A 545 27.966 -19.130 24.925 1.00 12.03 C
ANISOU 263 C SER A 545 1494 1655 1423 37 -55 82 C
ATOM 264 O SER A 545 27.409 -19.327 26.017 1.00 13.28 O
ANISOU 264 O SER A 545 1686 1829 1532 39 -37 89 O
ATOM 265 CB SER A 545 28.959 -16.846 25.166 1.00 11.99 C
ANISOU 265 CB SER A 545 1494 1640 1422 33 -89 18 C
ATOM 266 OG SER A 545 28.298 -16.254 24.057 1.00 11.80 O
ANISOU 266 OG SER A 545 1442 1599 1442 35 -59 15 O
ATOM 267 N ARG A 546 27.452 -19.581 23.762 1.00 8.37 N
ANISOU 267 N ARG A 546 999 1180 1001 35 -36 94 N
ATOM 268 CA ARG A 546 26.242 -20.386 23.716 1.00 8.80 C
ANISOU 268 CA ARG A 546 1050 1236 1059 31 -1 115 C
ATOM 269 C ARG A 546 26.237 -21.112 22.388 1.00 9.81 C
ANISOU 269 C ARG A 546 1148 1349 1231 25 -6 123 C
ATOM 270 O ARG A 546 26.712 -20.577 21.370 1.00 9.44 O
ANISOU 270 O ARG A 546 1083 1297 1208 26 -19 109 O
ATOM 271 CB ARG A 546 24.979 -19.487 23.785 1.00 11.29 C
ANISOU 271 CB ARG A 546 1357 1557 1377 34 38 99 C
ATOM 272 CG ARG A 546 23.713 -20.313 24.012 1.00 18.08 C
ANISOU 272 CG ARG A 546 2208 2421 2243 28 78 122 C
ATOM 273 CD ARG A 546 22.458 -19.497 24.259 1.00 30.78 C
ANISOU 273 CD ARG A 546 3800 4035 3860 35 123 108 C
ATOM 274 NE ARG A 546 21.305 -20.401 24.271 1.00 43.48 N
ANISOU 274 NE ARG A 546 5384 5643 5491 23 158 134 N
ATOM 275 CZ ARG A 546 20.528 -20.641 23.219 1.00 57.42 C
ANISOU 275 CZ ARG A 546 7103 7401 7312 14 155 139 C
ATOM 276 NH1 ARG A 546 20.717 -19.983 22.080 1.00 34.55 N
ANISOU 276 NH1 ARG A 546 4186 4500 4442 21 122 124 N
ATOM 277 NH2 ARG A 546 19.532 -21.514 23.309 1.00 46.25 N
ANISOU 277 NH2 ARG A 546 5663 5984 5924 -2 184 161 N
ATOM 278 N VAL A 547 25.707 -22.334 22.391 1.00 9.25 N
ANISOU 278 N VAL A 547 1075 1270 1170 17 7 146 N
ATOM 279 CA VAL A 547 25.478 -23.114 21.185 1.00 9.01 C
ANISOU 279 CA VAL A 547 1023 1224 1178 8 6 146 C
ATOM 280 C VAL A 547 24.053 -23.628 21.328 1.00 11.60 C
ANISOU 280 C VAL A 547 1338 1549 1519 -7 35 159 C
ATOM 281 O VAL A 547 23.748 -24.339 22.307 1.00 12.19 O
ANISOU 281 O VAL A 547 1428 1620 1583 -12 54 185 O
ATOM 282 CB VAL A 547 26.474 -24.254 21.009 1.00 10.80 C
ANISOU 282 CB VAL A 547 1255 1429 1421 10 -13 157 C
ATOM 283 CG1 VAL A 547 26.087 -25.117 19.798 1.00 12.28 C
ANISOU 283 CG1 VAL A 547 1427 1596 1644 -2 -9 147 C
ATOM 284 CG2 VAL A 547 27.908 -23.712 20.867 1.00 10.78 C
ANISOU 284 CG2 VAL A 547 1251 1428 1416 24 -39 145 C
ATOM 285 N ALA A 548 23.180 -23.273 20.380 1.00 9.53 N
ANISOU 285 N ALA A 548 1047 1291 1283 -14 37 145 N
ATOM 286 CA ALA A 548 21.772 -23.639 20.449 1.00 10.08 C
ANISOU 286 CA ALA A 548 1091 1361 1379 -30 61 155 C
ATOM 287 C ALA A 548 21.487 -25.049 19.883 1.00 10.15 C
ANISOU 287 C ALA A 548 1090 1345 1423 -54 55 161 C
ATOM 288 O ALA A 548 22.062 -25.456 18.861 1.00 10.00 O
ANISOU 288 O ALA A 548 1074 1314 1412 -57 27 143 O
ATOM 289 CB ALA A 548 20.929 -22.607 19.724 1.00 11.43 C
ANISOU 289 CB ALA A 548 1229 1546 1569 -26 57 141 C
ATOM 290 N PRO A 549 20.572 -25.783 20.512 1.00 9.56 N
ANISOU 290 N PRO A 549 1003 1260 1370 -73 84 184 N
ATOM 291 CA PRO A 549 20.291 -27.144 20.040 1.00 9.27 C
ANISOU 291 CA PRO A 549 958 1190 1376 -100 77 187 C
ATOM 292 C PRO A 549 19.773 -27.213 18.601 1.00 9.85 C
ANISOU 292 C PRO A 549 1001 1260 1480 -117 44 155 C
ATOM 293 O PRO A 549 18.931 -26.413 18.217 1.00 10.63 O
ANISOU 293 O PRO A 549 1066 1383 1589 -118 38 147 O
ATOM 294 CB PRO A 549 19.182 -27.642 20.992 1.00 11.87 C
ANISOU 294 CB PRO A 549 1269 1512 1730 -120 123 221 C
ATOM 295 CG PRO A 549 19.321 -26.791 22.243 1.00 15.73 C
ANISOU 295 CG PRO A 549 1780 2029 2167 -97 157 239 C
ATOM 296 CD PRO A 549 19.795 -25.441 21.725 1.00 10.33 C
ANISOU 296 CD PRO A 549 1097 1371 1456 -71 130 206 C
ATOM 297 N GLY A 550 20.328 -28.138 17.815 1.00 9.60 N
ANISOU 297 N GLY A 550 985 1201 1462 -128 21 135 N
ATOM 298 CA GLY A 550 19.834 -28.422 16.469 1.00 9.98 C
ANISOU 298 CA GLY A 550 1016 1246 1532 -150 -14 99 C
ATOM 299 C GLY A 550 20.229 -27.424 15.416 1.00 11.17 C
ANISOU 299 C GLY A 550 1172 1428 1643 -132 -44 73 C
ATOM 300 O GLY A 550 19.704 -27.485 14.301 1.00 12.22 O
ANISOU 300 O GLY A 550 1294 1568 1780 -150 -78 47 O
ATOM 301 N THR A 551 21.132 -26.529 15.741 1.00 8.90 N
ANISOU 301 N THR A 551 904 1158 1318 -102 -35 82 N
ATOM 302 CA THR A 551 21.626 -25.541 14.809 1.00 9.16 C
ANISOU 302 CA THR A 551 946 1217 1316 -86 -55 67 C
ATOM 303 C THR A 551 22.926 -26.015 14.180 1.00 8.33 C
ANISOU 303 C THR A 551 874 1099 1192 -78 -56 45 C
ATOM 304 O THR A 551 23.522 -27.003 14.644 1.00 9.58 O
ANISOU 304 O THR A 551 1045 1226 1367 -77 -42 45 O
ATOM 305 CB THR A 551 21.859 -24.226 15.526 1.00 8.42 C
ANISOU 305 CB THR A 551 851 1145 1205 -61 -41 87 C
ATOM 306 OG1 THR A 551 22.892 -24.371 16.506 1.00 8.05 O
ANISOU 306 OG1 THR A 551 827 1087 1146 -46 -21 97 O
ATOM 307 CG2 THR A 551 20.551 -23.656 16.124 1.00 10.23 C
ANISOU 307 CG2 THR A 551 1045 1386 1456 -62 -30 103 C
ATOM 308 N PRO A 552 23.433 -25.362 13.125 1.00 8.43 N
ANISOU 308 N PRO A 552 900 1131 1171 -69 -68 29 N
ATOM 309 CA PRO A 552 24.678 -25.835 12.502 1.00 9.11 C
ANISOU 309 CA PRO A 552 1013 1205 1243 -61 -56 6 C
ATOM 310 C PRO A 552 25.833 -25.976 13.484 1.00 9.03 C
ANISOU 310 C PRO A 552 1005 1177 1248 -40 -33 22 C
ATOM 311 O PRO A 552 26.625 -26.936 13.388 1.00 9.57 O
ANISOU 311 O PRO A 552 1084 1217 1333 -34 -21 7 O
ATOM 312 CB PRO A 552 24.964 -24.771 11.425 1.00 9.92 C
ANISOU 312 CB PRO A 552 1128 1340 1303 -54 -63 2 C
ATOM 313 CG PRO A 552 23.542 -24.360 11.012 1.00 10.78 C
ANISOU 313 CG PRO A 552 1220 1470 1407 -69 -98 8 C
ATOM 314 CD PRO A 552 22.796 -24.288 12.324 1.00 9.51 C
ANISOU 314 CD PRO A 552 1028 1300 1285 -69 -91 33 C
ATOM 315 N ALA A 553 25.932 -25.049 14.440 1.00 7.79 N
ANISOU 315 N ALA A 553 838 1034 1087 -27 -30 49 N
ATOM 316 CA ALA A 553 27.017 -25.090 15.416 1.00 7.40 C
ANISOU 316 CA ALA A 553 791 974 1046 -10 -22 64 C
ATOM 317 C ALA A 553 26.913 -26.300 16.357 1.00 8.50 C
ANISOU 317 C ALA A 553 934 1084 1210 -12 -19 80 C
ATOM 318 O ALA A 553 27.915 -26.729 16.947 1.00 8.14 O
ANISOU 318 O ALA A 553 894 1022 1179 5 -19 92 O
ATOM 319 CB ALA A 553 27.069 -23.786 16.206 1.00 8.76 C
ANISOU 319 CB ALA A 553 959 1168 1203 0 -25 81 C
ATOM 320 N ASP A 554 25.670 -26.795 16.553 1.00 7.97 N
ANISOU 320 N ASP A 554 863 1010 1154 -32 -17 86 N
ATOM 321 CA ASP A 554 25.456 -27.954 17.404 1.00 7.52 C
ANISOU 321 CA ASP A 554 812 921 1124 -38 -8 108 C
ATOM 322 C ASP A 554 25.674 -29.251 16.630 1.00 8.86 C
ANISOU 322 C ASP A 554 989 1049 1330 -47 -8 86 C
ATOM 323 O ASP A 554 25.886 -30.290 17.245 1.00 8.88 O
ANISOU 323 O ASP A 554 999 1012 1363 -45 -1 106 O
ATOM 324 CB ASP A 554 24.009 -27.903 17.907 1.00 7.51 C
ANISOU 324 CB ASP A 554 797 929 1129 -60 3 125 C
ATOM 325 CG ASP A 554 23.619 -29.033 18.804 1.00 9.10 C
ANISOU 325 CG ASP A 554 1003 1096 1357 -73 20 157 C
ATOM 326 OD1 ASP A 554 24.342 -29.278 19.806 1.00 9.63 O
ANISOU 326 OD1 ASP A 554 1091 1155 1412 -56 25 189 O
ATOM 327 OD2 ASP A 554 22.614 -29.702 18.504 1.00 10.29 O
ANISOU 327 OD2 ASP A 554 1138 1227 1543 -102 26 153 O
ATOM 328 N LEU A 555 25.501 -29.198 15.290 1.00 8.28 N
ANISOU 328 N LEU A 555 915 982 1250 -57 -16 44 N
ATOM 329 CA LEU A 555 25.509 -30.427 14.472 1.00 9.16 C
ANISOU 329 CA LEU A 555 1038 1051 1391 -71 -15 8 C
ATOM 330 C LEU A 555 26.750 -30.625 13.632 1.00 10.34 C
ANISOU 330 C LEU A 555 1202 1190 1536 -49 -4 -26 C
ATOM 331 O LEU A 555 26.846 -31.622 12.910 1.00 10.41 O
ANISOU 331 O LEU A 555 1225 1162 1567 -56 2 -64 O
ATOM 332 CB LEU A 555 24.267 -30.421 13.554 1.00 9.14 C
ANISOU 332 CB LEU A 555 1029 1062 1383 -104 -36 -22 C
ATOM 333 CG LEU A 555 22.926 -30.280 14.247 1.00 9.94 C
ANISOU 333 CG LEU A 555 1102 1171 1503 -128 -42 7 C
ATOM 334 CD1 LEU A 555 21.815 -30.202 13.220 1.00 10.40 C
ANISOU 334 CD1 LEU A 555 1146 1246 1561 -159 -73 -24 C
ATOM 335 CD2 LEU A 555 22.681 -31.488 15.169 1.00 11.73 C
ANISOU 335 CD2 LEU A 555 1328 1347 1783 -143 -24 32 C
ATOM 336 N CYS A 556 27.725 -29.723 13.777 1.00 9.26 N
ANISOU 336 N CYS A 556 1060 1080 1377 -23 2 -13 N
ATOM 337 CA CYS A 556 28.920 -29.789 12.967 1.00 8.71 C
ANISOU 337 CA CYS A 556 997 1006 1307 -2 22 -41 C
ATOM 338 C CYS A 556 29.900 -30.843 13.417 1.00 10.74 C
ANISOU 338 C CYS A 556 1250 1214 1619 23 37 -38 C
ATOM 339 O CYS A 556 29.700 -31.496 14.450 1.00 9.99 O
ANISOU 339 O CYS A 556 1151 1087 1556 24 27 -4 O
ATOM 340 CB CYS A 556 29.543 -28.406 12.828 1.00 9.43 C
ANISOU 340 CB CYS A 556 1078 1142 1364 11 26 -29 C
ATOM 341 SG CYS A 556 29.826 -27.559 14.380 1.00 10.71 S
ANISOU 341 SG CYS A 556 1219 1320 1531 23 9 22 S
ATOM 342 N VAL A 557 30.972 -31.016 12.631 1.00 11.46 N
ANISOU 342 N VAL A 557 1340 1295 1721 44 64 -69 N
ATOM 343 CA VAL A 557 31.971 -32.057 12.850 1.00 13.26 C
ANISOU 343 CA VAL A 557 1557 1469 2012 74 82 -73 C
ATOM 344 C VAL A 557 33.318 -31.461 13.251 1.00 15.42 C
ANISOU 344 C VAL A 557 1796 1757 2305 106 89 -48 C
ATOM 345 O VAL A 557 34.032 -30.983 12.349 1.00 17.68 O
ANISOU 345 O VAL A 557 2074 2063 2580 115 121 -77 O
ATOM 346 CB VAL A 557 32.120 -32.930 11.583 1.00 17.10 C
ANISOU 346 CB VAL A 557 2065 1922 2509 75 117 -139 C
ATOM 347 CG1 VAL A 557 33.241 -33.967 11.754 1.00 17.95 C
ANISOU 347 CG1 VAL A 557 2157 1969 2695 114 143 -145 C
ATOM 348 CG2 VAL A 557 30.796 -33.573 11.189 1.00 16.64 C
ANISOU 348 CG2 VAL A 557 2039 1846 2439 37 100 -168 C
ATOM 349 N PRO A 558 33.744 -31.530 14.531 1.00 12.45 N
ANISOU 349 N PRO A 558 1400 1371 1961 124 61 3 N
ATOM 350 CA PRO A 558 32.955 -31.917 15.708 1.00 11.67 C
ANISOU 350 CA PRO A 558 1314 1259 1863 113 28 47 C
ATOM 351 C PRO A 558 32.106 -30.717 16.121 1.00 11.51 C
ANISOU 351 C PRO A 558 1301 1294 1778 87 9 65 C
ATOM 352 O PRO A 558 32.172 -29.659 15.472 1.00 11.61 O
ANISOU 352 O PRO A 558 1309 1347 1755 80 17 44 O
ATOM 353 CB PRO A 558 34.039 -32.267 16.730 1.00 12.83 C
ANISOU 353 CB PRO A 558 1436 1384 2056 148 6 92 C
ATOM 354 CG PRO A 558 35.091 -31.196 16.446 1.00 16.38 C
ANISOU 354 CG PRO A 558 1851 1872 2500 161 8 82 C
ATOM 355 CD PRO A 558 35.075 -31.025 14.947 1.00 14.28 C
ANISOU 355 CD PRO A 558 1591 1614 2222 153 55 24 C
ATOM 356 N ARG A 559 31.359 -30.859 17.197 1.00 10.43 N
ANISOU 356 N ARG A 559 1177 1157 1630 76 -10 104 N
ATOM 357 CA ARG A 559 30.495 -29.784 17.665 1.00 8.26 C
ANISOU 357 CA ARG A 559 909 929 1302 55 -21 117 C
ATOM 358 C ARG A 559 31.305 -28.569 18.073 1.00 8.68 C
ANISOU 358 C ARG A 559 947 1020 1331 68 -37 126 C
ATOM 359 O ARG A 559 32.385 -28.729 18.626 1.00 10.77 O
ANISOU 359 O ARG A 559 1197 1275 1619 91 -54 144 O
ATOM 360 CB ARG A 559 29.719 -30.290 18.884 1.00 9.26 C
ANISOU 360 CB ARG A 559 1052 1044 1423 45 -28 162 C
ATOM 361 CG ARG A 559 28.550 -29.372 19.185 1.00 11.18 C
ANISOU 361 CG ARG A 559 1300 1328 1622 22 -24 165 C
ATOM 362 CD ARG A 559 28.183 -29.507 20.631 1.00 14.23 C
ANISOU 362 CD ARG A 559 1703 1718 1986 21 -27 214 C
ATOM 363 NE ARG A 559 26.902 -28.881 20.942 1.00 9.81 N
ANISOU 363 NE ARG A 559 1145 1186 1396 -1 -9 216 N
ATOM 364 CZ ARG A 559 26.742 -28.046 21.948 1.00 10.48 C
ANISOU 364 CZ ARG A 559 1242 1305 1435 3 -8 233 C
ATOM 365 NH1 ARG A 559 27.796 -27.663 22.688 1.00 12.30 N
ANISOU 365 NH1 ARG A 559 1486 1549 1639 24 -34 246 N
ATOM 366 NH2 ARG A 559 25.539 -27.574 22.232 1.00 12.19 N
ANISOU 366 NH2 ARG A 559 1456 1541 1634 -13 18 235 N
ATOM 367 N LEU A 560 30.748 -27.369 17.858 1.00 9.03 N
ANISOU 367 N LEU A 560 993 1103 1335 53 -35 114 N
ATOM 368 CA LEU A 560 31.339 -26.155 18.420 1.00 8.49 C
ANISOU 368 CA LEU A 560 915 1065 1246 59 -52 122 C
ATOM 369 C LEU A 560 30.850 -26.133 19.874 1.00 12.37 C
ANISOU 369 C LEU A 560 1426 1565 1710 57 -70 154 C
ATOM 370 O LEU A 560 29.684 -26.464 20.144 1.00 14.91 O
ANISOU 370 O LEU A 560 1764 1886 2017 43 -57 164 O
ATOM 371 CB LEU A 560 30.834 -24.928 17.661 1.00 9.02 C
ANISOU 371 CB LEU A 560 980 1160 1287 45 -41 101 C
ATOM 372 CG LEU A 560 31.487 -23.618 18.062 1.00 10.22 C
ANISOU 372 CG LEU A 560 1122 1332 1429 48 -55 101 C
ATOM 373 CD1 LEU A 560 32.969 -23.582 17.694 1.00 11.75 C
ANISOU 373 CD1 LEU A 560 1287 1518 1658 60 -57 96 C
ATOM 374 CD2 LEU A 560 30.752 -22.472 17.391 1.00 11.49 C
ANISOU 374 CD2 LEU A 560 1286 1511 1568 35 -43 89 C
ATOM 375 N ASN A 561 31.720 -25.804 20.821 1.00 10.20 N
ANISOU 375 N ASN A 561 1149 1299 1428 70 -101 170 N
ATOM 376 CA ASN A 561 31.330 -25.847 22.228 1.00 9.80 C
ANISOU 376 CA ASN A 561 1127 1260 1336 69 -117 201 C
ATOM 377 C ASN A 561 31.477 -24.526 22.934 1.00 10.40 C
ANISOU 377 C ASN A 561 1212 1369 1370 65 -137 189 C
ATOM 378 O ASN A 561 32.393 -23.742 22.658 1.00 10.33 O
ANISOU 378 O ASN A 561 1180 1367 1377 67 -156 169 O
ATOM 379 CB ASN A 561 32.146 -26.909 22.982 1.00 10.07 C
ANISOU 379 CB ASN A 561 1165 1273 1389 88 -148 240 C
ATOM 380 CG ASN A 561 31.820 -28.293 22.570 1.00 12.82 C
ANISOU 380 CG ASN A 561 1514 1578 1777 91 -127 256 C
ATOM 381 OD1 ASN A 561 30.660 -28.707 22.697 1.00 15.38 O
ANISOU 381 OD1 ASN A 561 1859 1896 2088 74 -99 267 O
ATOM 382 ND2 ASN A 561 32.814 -29.016 22.073 1.00 13.13 N
ANISOU 382 ND2 ASN A 561 1529 1585 1874 112 -135 256 N
ATOM 383 N GLU A 562 30.630 -24.319 23.922 1.00 9.69 N
ANISOU 383 N GLU A 562 1155 1297 1230 57 -129 201 N
ATOM 384 CA GLU A 562 30.791 -23.171 24.812 1.00 9.42 C
ANISOU 384 CA GLU A 562 1140 1290 1148 55 -149 185 C
ATOM 385 C GLU A 562 32.166 -23.214 25.447 1.00 12.74 C
ANISOU 385 C GLU A 562 1557 1714 1569 66 -207 195 C
ATOM 386 O GLU A 562 32.654 -24.305 25.810 1.00 13.03 O
ANISOU 386 O GLU A 562 1595 1738 1616 79 -231 232 O
ATOM 387 CB GLU A 562 29.716 -23.201 25.902 1.00 10.83 C
ANISOU 387 CB GLU A 562 1361 1486 1266 49 -124 200 C
ATOM 388 CG GLU A 562 28.350 -22.970 25.340 1.00 13.15 C
ANISOU 388 CG GLU A 562 1648 1780 1570 39 -70 187 C
ATOM 389 CD GLU A 562 27.574 -24.207 24.951 1.00 25.28 C
ANISOU 389 CD GLU A 562 3176 3295 3135 32 -40 216 C
ATOM 390 OE1 GLU A 562 28.179 -25.298 24.756 1.00 19.52 O
ANISOU 390 OE1 GLU A 562 2441 2541 2433 37 -58 241 O
ATOM 391 OE2 GLU A 562 26.329 -24.066 24.861 1.00 24.90 O
ANISOU 391 OE2 GLU A 562 3123 3252 3088 21 1 213 O
ATOM 392 N GLY A 563 32.818 -22.062 25.479 1.00 10.84 N
ANISOU 392 N GLY A 563 1304 1485 1329 60 -233 162 N
ATOM 393 CA GLY A 563 34.160 -21.971 26.039 1.00 11.14 C
ANISOU 393 CA GLY A 563 1328 1529 1377 66 -297 165 C
ATOM 394 C GLY A 563 35.256 -22.083 24.999 1.00 11.83 C
ANISOU 394 C GLY A 563 1354 1595 1545 72 -306 160 C
ATOM 395 O GLY A 563 36.416 -21.731 25.281 1.00 13.63 O
ANISOU 395 O GLY A 563 1552 1826 1800 72 -357 155 O
ATOM 396 N ASP A 564 34.888 -22.498 23.761 1.00 9.69 N
ANISOU 396 N ASP A 564 1062 1304 1314 74 -255 158 N
ATOM 397 CA ASP A 564 35.895 -22.573 22.721 1.00 9.25 C
ANISOU 397 CA ASP A 564 954 1233 1329 81 -249 149 C
ATOM 398 C ASP A 564 36.351 -21.170 22.383 1.00 10.69 C
ANISOU 398 C ASP A 564 1114 1423 1526 62 -251 119 C
ATOM 399 O ASP A 564 35.521 -20.260 22.236 1.00 10.66 O
ANISOU 399 O ASP A 564 1133 1425 1491 47 -228 99 O
ATOM 400 CB ASP A 564 35.318 -23.202 21.454 1.00 10.11 C
ANISOU 400 CB ASP A 564 1059 1324 1459 83 -192 145 C
ATOM 401 CG ASP A 564 35.141 -24.724 21.454 1.00 13.08 C
ANISOU 401 CG ASP A 564 1442 1675 1851 101 -184 170 C
ATOM 402 OD1 ASP A 564 35.553 -25.377 22.442 1.00 12.21 O
ANISOU 402 OD1 ASP A 564 1338 1560 1742 115 -222 201 O
ATOM 403 OD2 ASP A 564 34.556 -25.236 20.470 1.00 12.25 O
ANISOU 403 OD2 ASP A 564 1341 1555 1757 98 -141 158 O
ATOM 404 N GLN A 565 37.671 -20.971 22.262 1.00 10.10 N
ANISOU 404 N GLN A 565 988 1341 1507 64 -279 116 N
ATOM 405 CA GLN A 565 38.221 -19.659 21.936 1.00 10.98 C
ANISOU 405 CA GLN A 565 1072 1453 1647 42 -280 91 C
ATOM 406 C GLN A 565 38.441 -19.601 20.430 1.00 12.04 C
ANISOU 406 C GLN A 565 1174 1574 1828 41 -219 87 C
ATOM 407 O GLN A 565 39.087 -20.503 19.869 1.00 12.71 O
ANISOU 407 O GLN A 565 1224 1648 1957 59 -201 98 O
ATOM 408 CB GLN A 565 39.560 -19.457 22.653 1.00 12.32 C
ANISOU 408 CB GLN A 565 1197 1624 1860 39 -346 90 C
ATOM 409 CG GLN A 565 40.182 -18.111 22.299 1.00 21.20 C
ANISOU 409 CG GLN A 565 2286 2741 3028 10 -346 64 C
ATOM 410 CD GLN A 565 41.544 -17.877 22.912 1.00 41.34 C
ANISOU 410 CD GLN A 565 4779 5291 5636 1 -414 61 C
ATOM 411 OE1 GLN A 565 41.890 -18.432 23.962 1.00 40.28 O
ANISOU 411 OE1 GLN A 565 4650 5171 5485 12 -483 73 O
ATOM 412 NE2 GLN A 565 42.328 -16.996 22.293 1.00 25.13 N
ANISOU 412 NE2 GLN A 565 2672 3223 3654 -23 -400 47 N
ATOM 413 N VAL A 566 37.906 -18.557 19.773 1.00 10.52 N
ANISOU 413 N VAL A 566 994 1380 1623 22 -184 73 N
ATOM 414 CA VAL A 566 38.039 -18.459 18.317 1.00 10.38 C
ANISOU 414 CA VAL A 566 957 1354 1631 20 -124 74 C
ATOM 415 C VAL A 566 39.392 -17.856 17.958 1.00 12.17 C
ANISOU 415 C VAL A 566 1125 1571 1929 7 -120 73 C
ATOM 416 O VAL A 566 39.698 -16.741 18.386 1.00 14.16 O
ANISOU 416 O VAL A 566 1366 1817 2198 -16 -145 63 O
ATOM 417 CB VAL A 566 36.862 -17.667 17.719 1.00 13.34 C
ANISOU 417 CB VAL A 566 1372 1731 1964 8 -92 71 C
ATOM 418 CG1 VAL A 566 36.953 -17.614 16.191 1.00 13.09 C
ANISOU 418 CG1 VAL A 566 1332 1697 1942 6 -34 77 C
ATOM 419 CG2 VAL A 566 35.534 -18.317 18.125 1.00 13.08 C
ANISOU 419 CG2 VAL A 566 1385 1709 1875 19 -96 72 C
ATOM 420 N VAL A 567 40.217 -18.591 17.195 1.00 10.70 N
ANISOU 420 N VAL A 567 897 1378 1789 21 -86 80 N
ATOM 421 CA VAL A 567 41.555 -18.142 16.791 1.00 11.41 C
ANISOU 421 CA VAL A 567 918 1459 1958 10 -70 81 C
ATOM 422 C VAL A 567 41.511 -17.569 15.378 1.00 13.88 C
ANISOU 422 C VAL A 567 1233 1769 2271 -3 8 86 C
ATOM 423 O VAL A 567 42.017 -16.467 15.153 1.00 13.86 O
ANISOU 423 O VAL A 567 1204 1758 2306 -30 20 90 O
ATOM 424 CB VAL A 567 42.565 -19.327 16.883 1.00 15.75 C
ANISOU 424 CB VAL A 567 1413 2002 2569 39 -75 88 C
ATOM 425 CG1 VAL A 567 43.955 -18.919 16.370 1.00 18.11 C
ANISOU 425 CG1 VAL A 567 1628 2291 2961 30 -47 90 C
ATOM 426 CG2 VAL A 567 42.642 -19.844 18.324 1.00 15.48 C
ANISOU 426 CG2 VAL A 567 1380 1971 2529 53 -161 94 C
ATOM 427 N LEU A 568 40.886 -18.308 14.435 1.00 11.05 N
ANISOU 427 N LEU A 568 911 1418 1868 13 59 85 N
ATOM 428 CA LEU A 568 40.759 -17.852 13.037 1.00 11.50 C
ANISOU 428 CA LEU A 568 984 1480 1904 2 131 92 C
ATOM 429 C LEU A 568 39.331 -17.951 12.596 1.00 11.43 C
ANISOU 429 C LEU A 568 1047 1484 1812 5 135 91 C
ATOM 430 O LEU A 568 38.597 -18.847 13.023 1.00 10.71 O
ANISOU 430 O LEU A 568 983 1396 1688 21 108 80 O
ATOM 431 CB LEU A 568 41.530 -18.734 12.063 1.00 12.84 C
ANISOU 431 CB LEU A 568 1127 1650 2101 21 197 86 C
ATOM 432 CG LEU A 568 43.038 -18.952 12.246 1.00 16.98 C
ANISOU 432 CG LEU A 568 1567 2162 2724 28 211 86 C
ATOM 433 CD1 LEU A 568 43.592 -19.832 11.104 1.00 16.63 C
ANISOU 433 CD1 LEU A 568 1508 2118 2695 51 296 74 C
ATOM 434 CD2 LEU A 568 43.813 -17.634 12.274 1.00 15.17 C
ANISOU 434 CD2 LEU A 568 1288 1925 2551 -6 216 103 C
ATOM 435 N ILE A 569 38.924 -17.008 11.713 1.00 10.23 N
ANISOU 435 N ILE A 569 921 1337 1628 -13 169 107 N
ATOM 436 CA ILE A 569 37.632 -17.033 11.074 1.00 9.02 C
ANISOU 436 CA ILE A 569 828 1199 1400 -11 173 110 C
ATOM 437 C ILE A 569 37.913 -16.979 9.595 1.00 11.76 C
ANISOU 437 C ILE A 569 1190 1559 1720 -15 240 121 C
ATOM 438 O ILE A 569 38.464 -15.974 9.120 1.00 12.40 O
ANISOU 438 O ILE A 569 1257 1634 1821 -33 273 146 O
ATOM 439 CB ILE A 569 36.714 -15.875 11.509 1.00 10.47 C
ANISOU 439 CB ILE A 569 1036 1377 1565 -24 137 125 C
ATOM 440 CG1 ILE A 569 36.476 -15.976 13.022 1.00 12.10 C
ANISOU 440 CG1 ILE A 569 1235 1575 1789 -19 79 109 C
ATOM 441 CG2 ILE A 569 35.385 -15.904 10.697 1.00 11.21 C
ANISOU 441 CG2 ILE A 569 1182 1488 1588 -20 140 134 C
ATOM 442 CD1 ILE A 569 35.697 -14.851 13.611 1.00 15.69 C
ANISOU 442 CD1 ILE A 569 1708 2018 2235 -28 50 113 C
ATOM 443 N ASN A 570 37.523 -18.020 8.856 1.00 11.01 N
ANISOU 443 N ASN A 570 1127 1479 1576 -1 262 101 N
ATOM 444 CA ASN A 570 37.829 -18.088 7.422 1.00 11.42 C
ANISOU 444 CA ASN A 570 1203 1549 1588 -4 331 104 C
ATOM 445 C ASN A 570 39.304 -17.765 7.161 1.00 14.84 C
ANISOU 445 C ASN A 570 1583 1973 2084 -9 392 114 C
ATOM 446 O ASN A 570 39.636 -17.018 6.239 1.00 16.10 O
ANISOU 446 O ASN A 570 1753 2141 2225 -24 446 141 O
ATOM 447 CB ASN A 570 36.904 -17.183 6.616 1.00 12.46 C
ANISOU 447 CB ASN A 570 1386 1697 1649 -18 328 135 C
ATOM 448 CG ASN A 570 35.480 -17.645 6.725 1.00 12.74 C
ANISOU 448 CG ASN A 570 1464 1745 1630 -12 273 121 C
ATOM 449 OD1 ASN A 570 35.201 -18.854 6.707 1.00 13.87 O
ANISOU 449 OD1 ASN A 570 1620 1892 1758 -1 265 84 O
ATOM 450 ND2 ASN A 570 34.574 -16.696 6.788 1.00 11.82 N
ANISOU 450 ND2 ASN A 570 1368 1631 1493 -20 236 151 N
ATOM 451 N GLY A 571 40.163 -18.320 8.002 1.00 13.92 N
ANISOU 451 N GLY A 571 1407 1837 2044 4 381 97 N
ATOM 452 CA GLY A 571 41.617 -18.165 7.856 1.00 15.02 C
ANISOU 452 CA GLY A 571 1478 1965 2263 2 435 103 C
ATOM 453 C GLY A 571 42.251 -16.907 8.396 1.00 19.08 C
ANISOU 453 C GLY A 571 1943 2464 2844 -26 420 133 C
ATOM 454 O GLY A 571 43.491 -16.795 8.422 1.00 22.03 O
ANISOU 454 O GLY A 571 2244 2825 3300 -30 455 137 O
ATOM 455 N ARG A 572 41.417 -15.959 8.849 1.00 15.19 N
ANISOU 455 N ARG A 572 1482 1966 2324 -44 367 150 N
ATOM 456 CA ARG A 572 41.880 -14.665 9.315 1.00 15.56 C
ANISOU 456 CA ARG A 572 1493 1990 2430 -74 351 174 C
ATOM 457 C ARG A 572 42.108 -14.644 10.792 1.00 16.13 C
ANISOU 457 C ARG A 572 1525 2045 2557 -75 271 154 C
ATOM 458 O ARG A 572 41.236 -15.057 11.545 1.00 13.72 O
ANISOU 458 O ARG A 572 1256 1747 2212 -60 213 137 O
ATOM 459 CB ARG A 572 40.844 -13.626 8.954 1.00 16.61 C
ANISOU 459 CB ARG A 572 1685 2120 2507 -89 342 201 C
ATOM 460 CG ARG A 572 41.272 -12.200 9.236 1.00 21.71 C
ANISOU 460 CG ARG A 572 2302 2732 3214 -123 337 227 C
ATOM 461 CD ARG A 572 40.077 -11.289 9.287 1.00 20.67 C
ANISOU 461 CD ARG A 572 2228 2589 3038 -127 304 246 C
ATOM 462 NE ARG A 572 39.256 -11.369 8.077 1.00 25.01 N
ANISOU 462 NE ARG A 572 2839 3162 3502 -117 339 274 N
ATOM 463 CZ ARG A 572 39.364 -10.557 7.031 1.00 40.51 C
ANISOU 463 CZ ARG A 572 4823 5119 5450 -133 392 323 C
ATOM 464 NH1 ARG A 572 40.262 -9.576 7.030 1.00 30.90 N
ANISOU 464 NH1 ARG A 572 3566 3868 4309 -164 422 351 N
ATOM 465 NH2 ARG A 572 38.549 -10.691 5.997 1.00 28.17 N
ANISOU 465 NH2 ARG A 572 3322 3585 3797 -122 409 348 N
ATOM 466 N ASP A 573 43.276 -14.147 11.215 1.00 16.65 N
ANISOU 466 N ASP A 573 1520 2092 2716 -95 267 157 N
ATOM 467 CA ASP A 573 43.627 -13.973 12.601 1.00 15.93 C
ANISOU 467 CA ASP A 573 1389 1986 2676 -102 185 139 C
ATOM 468 C ASP A 573 42.825 -12.781 13.130 1.00 18.63 C
ANISOU 468 C ASP A 573 1774 2310 2993 -125 141 139 C
ATOM 469 O ASP A 573 42.991 -11.650 12.653 1.00 20.86 O
ANISOU 469 O ASP A 573 2052 2569 3304 -155 171 160 O
ATOM 470 CB ASP A 573 45.147 -13.701 12.680 1.00 18.31 C
ANISOU 470 CB ASP A 573 1595 2271 3091 -122 198 143 C
ATOM 471 CG ASP A 573 45.695 -13.441 14.060 1.00 25.64 C
ANISOU 471 CG ASP A 573 2475 3187 4080 -135 105 123 C
ATOM 472 OD1 ASP A 573 44.899 -13.402 15.022 1.00 22.14 O
ANISOU 472 OD1 ASP A 573 2082 2747 3585 -130 33 105 O
ATOM 473 OD2 ASP A 573 46.917 -13.214 14.174 1.00 33.63 O
ANISOU 473 OD2 ASP A 573 3400 4185 5192 -154 104 126 O
ATOM 474 N ILE A 574 41.992 -13.018 14.128 1.00 14.44 N
ANISOU 474 N ILE A 574 1283 1786 2416 -112 75 118 N
ATOM 475 CA ILE A 574 41.126 -11.958 14.668 1.00 14.49 C
ANISOU 475 CA ILE A 574 1334 1775 2397 -127 40 111 C
ATOM 476 C ILE A 574 41.587 -11.303 15.973 1.00 18.07 C
ANISOU 476 C ILE A 574 1763 2208 2896 -149 -30 82 C
ATOM 477 O ILE A 574 40.819 -10.560 16.581 1.00 17.45 O
ANISOU 477 O ILE A 574 1726 2114 2789 -155 -61 65 O
ATOM 478 CB ILE A 574 39.675 -12.497 14.786 1.00 16.17 C
ANISOU 478 CB ILE A 574 1615 2008 2520 -99 28 106 C
ATOM 479 CG1 ILE A 574 39.618 -13.739 15.727 1.00 17.06 C
ANISOU 479 CG1 ILE A 574 1728 2143 2610 -74 -17 85 C
ATOM 480 CG2 ILE A 574 39.093 -12.768 13.389 1.00 19.78 C
ANISOU 480 CG2 ILE A 574 2105 2481 2931 -88 90 133 C
ATOM 481 CD1 ILE A 574 38.226 -14.068 16.244 1.00 20.69 C
ANISOU 481 CD1 ILE A 574 2247 2616 2997 -56 -40 76 C
ATOM 482 N ALA A 575 42.821 -11.567 16.419 1.00 17.99 N
ANISOU 482 N ALA A 575 1685 2196 2953 -159 -59 73 N
ATOM 483 CA ALA A 575 43.298 -11.049 17.711 1.00 19.03 C
ANISOU 483 CA ALA A 575 1795 2314 3120 -181 -140 40 C
ATOM 484 C ALA A 575 43.153 -9.561 17.970 1.00 23.11 C
ANISOU 484 C ALA A 575 2327 2791 3664 -219 -154 23 C
ATOM 485 O ALA A 575 42.893 -9.161 19.105 1.00 26.10 O
ANISOU 485 O ALA A 575 2732 3162 4022 -228 -220 -15 O
ATOM 486 CB ALA A 575 44.744 -11.485 17.942 1.00 20.98 C
ANISOU 486 CB ALA A 575 1954 2565 3454 -189 -167 40 C
ATOM 487 N GLU A 576 43.355 -8.739 16.962 1.00 18.70 N
ANISOU 487 N GLU A 576 1753 2202 3152 -242 -92 50 N
ATOM 488 CA GLU A 576 43.323 -7.294 17.219 1.00 18.74 C
ANISOU 488 CA GLU A 576 1766 2155 3201 -281 -106 35 C
ATOM 489 C GLU A 576 42.003 -6.654 16.828 1.00 16.75 C
ANISOU 489 C GLU A 576 1588 1884 2892 -267 -73 47 C
ATOM 490 O GLU A 576 41.875 -5.430 16.878 1.00 18.33 O
ANISOU 490 O GLU A 576 1800 2032 3132 -294 -72 42 O
ATOM 491 CB GLU A 576 44.491 -6.599 16.492 1.00 22.32 C
ANISOU 491 CB GLU A 576 2147 2573 3763 -324 -64 62 C
ATOM 492 CG GLU A 576 45.876 -7.189 16.771 1.00 36.39 C
ANISOU 492 CG GLU A 576 3835 4369 5622 -337 -90 54 C
ATOM 493 CD GLU A 576 46.355 -7.260 18.213 1.00 69.33 C
ANISOU 493 CD GLU A 576 7982 8545 9814 -349 -199 2 C
ATOM 494 OE1 GLU A 576 46.005 -6.363 19.015 1.00 68.29 O
ANISOU 494 OE1 GLU A 576 7887 8383 9676 -373 -252 -38 O
ATOM 495 OE2 GLU A 576 47.123 -8.198 18.529 1.00 70.46 O
ANISOU 495 OE2 GLU A 576 8070 8721 9983 -335 -233 1 O
ATOM 496 N HIS A 577 41.007 -7.495 16.476 1.00 13.65 N
ANISOU 496 N HIS A 577 1243 1531 2413 -226 -51 63 N
ATOM 497 CA HIS A 577 39.733 -7.025 15.992 1.00 12.91 C
ANISOU 497 CA HIS A 577 1210 1426 2269 -208 -22 81 C
ATOM 498 C HIS A 577 38.696 -6.880 17.078 1.00 13.23 C
ANISOU 498 C HIS A 577 1301 1466 2261 -190 -68 40 C
ATOM 499 O HIS A 577 38.682 -7.635 18.057 1.00 13.34 O
ANISOU 499 O HIS A 577 1321 1511 2239 -178 -113 7 O
ATOM 500 CB HIS A 577 39.204 -7.953 14.878 1.00 13.20 C
ANISOU 500 CB HIS A 577 1266 1503 2245 -178 28 121 C
ATOM 501 CG HIS A 577 39.982 -7.854 13.602 1.00 16.41 C
ANISOU 501 CG HIS A 577 1643 1908 2685 -194 92 166 C
ATOM 502 ND1 HIS A 577 40.869 -8.847 13.219 1.00 20.54 N
ANISOU 502 ND1 HIS A 577 2124 2461 3219 -189 118 171 N
ATOM 503 CD2 HIS A 577 39.949 -6.901 12.645 1.00 19.13 C
ANISOU 503 CD2 HIS A 577 1997 2221 3050 -211 141 211 C
ATOM 504 CE1 HIS A 577 41.396 -8.434 12.071 1.00 20.30 C
ANISOU 504 CE1 HIS A 577 2077 2420 3214 -206 186 213 C
ATOM 505 NE2 HIS A 577 40.850 -7.294 11.667 1.00 20.23 N
ANISOU 505 NE2 HIS A 577 2102 2377 3207 -220 201 242 N
ATOM 506 N THR A 578 37.833 -5.874 16.902 1.00 11.17 N
ANISOU 506 N THR A 578 1075 1166 2001 -187 -52 46 N
ATOM 507 CA THR A 578 36.792 -5.683 17.893 1.00 10.94 C
ANISOU 507 CA THR A 578 1093 1134 1930 -167 -81 5 C
ATOM 508 C THR A 578 35.752 -6.791 17.748 1.00 11.55 C
ANISOU 508 C THR A 578 1198 1264 1927 -128 -71 19 C
ATOM 509 O THR A 578 35.656 -7.484 16.715 1.00 10.99 O
ANISOU 509 O THR A 578 1120 1221 1834 -116 -39 61 O
ATOM 510 CB THR A 578 36.081 -4.349 17.678 1.00 11.54 C
ANISOU 510 CB THR A 578 1195 1150 2039 -167 -62 10 C
ATOM 511 OG1 THR A 578 35.315 -4.402 16.462 1.00 12.62 O
ANISOU 511 OG1 THR A 578 1346 1295 2155 -144 -18 70 O
ATOM 512 CG2 THR A 578 37.011 -3.155 17.723 1.00 11.62 C
ANISOU 512 CG2 THR A 578 1181 1096 2141 -210 -66 -1 C
ATOM 513 N HIS A 579 34.879 -6.877 18.760 1.00 9.91 N
ANISOU 513 N HIS A 579 1025 1065 1676 -108 -93 -18 N
ATOM 514 CA HIS A 579 33.764 -7.798 18.734 1.00 9.13 C
ANISOU 514 CA HIS A 579 950 1007 1512 -75 -81 -8 C
ATOM 515 C HIS A 579 32.940 -7.633 17.451 1.00 10.33 C
ANISOU 515 C HIS A 579 1108 1156 1662 -59 -43 41 C
ATOM 516 O HIS A 579 32.620 -8.638 16.803 1.00 9.53 O
ANISOU 516 O HIS A 579 1005 1093 1523 -45 -31 67 O
ATOM 517 CB HIS A 579 32.856 -7.502 19.951 1.00 9.33 C
ANISOU 517 CB HIS A 579 1012 1028 1506 -60 -95 -53 C
ATOM 518 CG HIS A 579 31.687 -8.424 20.119 1.00 9.54 C
ANISOU 518 CG HIS A 579 1058 1093 1473 -30 -81 -45 C
ATOM 519 ND1 HIS A 579 31.751 -9.541 20.934 1.00 9.89 N
ANISOU 519 ND1 HIS A 579 1113 1180 1466 -25 -100 -57 N
ATOM 520 CD2 HIS A 579 30.452 -8.364 19.566 1.00 10.44 C
ANISOU 520 CD2 HIS A 579 1179 1208 1580 -6 -52 -22 C
ATOM 521 CE1 HIS A 579 30.547 -10.114 20.865 1.00 8.86 C
ANISOU 521 CE1 HIS A 579 995 1071 1302 -2 -76 -43 C
ATOM 522 NE2 HIS A 579 29.730 -9.432 20.069 1.00 9.08 N
ANISOU 522 NE2 HIS A 579 1018 1076 1355 10 -50 -25 N
ATOM 523 N ASP A 580 32.498 -6.397 17.140 1.00 10.04 N
ANISOU 523 N ASP A 580 1080 1071 1664 -58 -29 52 N
ATOM 524 CA ASP A 580 31.639 -6.218 15.976 1.00 8.97 C
ANISOU 524 CA ASP A 580 952 935 1522 -38 -4 103 C
ATOM 525 C ASP A 580 32.392 -6.467 14.668 1.00 11.39 C
ANISOU 525 C ASP A 580 1245 1255 1830 -54 19 153 C
ATOM 526 O ASP A 580 31.754 -6.886 13.693 1.00 10.25 O
ANISOU 526 O ASP A 580 1111 1137 1648 -38 31 192 O
ATOM 527 CB ASP A 580 30.960 -4.859 16.015 1.00 10.04 C
ANISOU 527 CB ASP A 580 1100 1011 1704 -27 4 107 C
ATOM 528 CG ASP A 580 29.845 -4.731 17.049 1.00 9.76 C
ANISOU 528 CG ASP A 580 1081 971 1656 1 -2 64 C
ATOM 529 OD1 ASP A 580 29.471 -5.771 17.684 1.00 9.56 O
ANISOU 529 OD1 ASP A 580 1060 994 1578 11 -10 40 O
ATOM 530 OD2 ASP A 580 29.344 -3.601 17.227 1.00 12.52 O
ANISOU 530 OD2 ASP A 580 1440 1265 2053 13 6 57 O
ATOM 531 N GLN A 581 33.705 -6.248 14.634 1.00 10.25 N
ANISOU 531 N GLN A 581 1076 1094 1726 -85 25 151 N
ATOM 532 CA GLN A 581 34.468 -6.595 13.429 1.00 10.53 C
ANISOU 532 CA GLN A 581 1096 1148 1758 -98 59 195 C
ATOM 533 C GLN A 581 34.443 -8.099 13.220 1.00 12.97 C
ANISOU 533 C GLN A 581 1403 1516 2008 -84 59 188 C
ATOM 534 O GLN A 581 34.241 -8.562 12.081 1.00 12.63 O
ANISOU 534 O GLN A 581 1373 1501 1926 -76 87 223 O
ATOM 535 CB GLN A 581 35.891 -6.100 13.545 1.00 12.17 C
ANISOU 535 CB GLN A 581 1266 1326 2034 -135 68 191 C
ATOM 536 CG GLN A 581 35.994 -4.611 13.224 1.00 12.27 C
ANISOU 536 CG GLN A 581 1281 1273 2110 -155 85 218 C
ATOM 537 CD GLN A 581 37.303 -4.003 13.636 1.00 16.95 C
ANISOU 537 CD GLN A 581 1830 1825 2785 -198 83 200 C
ATOM 538 OE1 GLN A 581 38.142 -4.607 14.290 1.00 14.66 O
ANISOU 538 OE1 GLN A 581 1505 1555 2509 -212 59 163 O
ATOM 539 NE2 GLN A 581 37.426 -2.701 13.406 1.00 24.40 N
ANISOU 539 NE2 GLN A 581 2774 2701 3795 -221 98 223 N
ATOM 540 N VAL A 582 34.533 -8.861 14.328 1.00 9.71 N
ANISOU 540 N VAL A 582 983 1123 1584 -78 28 144 N
ATOM 541 CA VAL A 582 34.458 -10.334 14.303 1.00 9.93 C
ANISOU 541 CA VAL A 582 1010 1197 1565 -63 24 135 C
ATOM 542 C VAL A 582 33.082 -10.774 13.852 1.00 10.72 C
ANISOU 542 C VAL A 582 1143 1321 1612 -39 26 148 C
ATOM 543 O VAL A 582 32.963 -11.725 13.057 1.00 10.82 O
ANISOU 543 O VAL A 582 1160 1363 1586 -32 41 159 O
ATOM 544 CB VAL A 582 34.846 -10.879 15.701 1.00 11.44 C
ANISOU 544 CB VAL A 582 1190 1397 1761 -62 -15 94 C
ATOM 545 CG1 VAL A 582 34.421 -12.340 15.884 1.00 12.12 C
ANISOU 545 CG1 VAL A 582 1286 1520 1799 -42 -23 88 C
ATOM 546 CG2 VAL A 582 36.354 -10.739 15.912 1.00 12.60 C
ANISOU 546 CG2 VAL A 582 1293 1530 1963 -86 -22 86 C
ATOM 547 N VAL A 583 31.999 -10.130 14.337 1.00 9.08 N
ANISOU 547 N VAL A 583 952 1097 1401 -27 11 143 N
ATOM 548 CA VAL A 583 30.662 -10.460 13.889 1.00 8.48 C
ANISOU 548 CA VAL A 583 894 1040 1287 -6 9 158 C
ATOM 549 C VAL A 583 30.542 -10.271 12.369 1.00 11.30 C
ANISOU 549 C VAL A 583 1261 1405 1627 -7 27 204 C
ATOM 550 O VAL A 583 30.017 -11.186 11.693 1.00 10.05 O
ANISOU 550 O VAL A 583 1114 1282 1423 1 25 211 O
ATOM 551 CB VAL A 583 29.608 -9.631 14.669 1.00 9.89 C
ANISOU 551 CB VAL A 583 1080 1194 1483 10 -3 145 C
ATOM 552 CG1 VAL A 583 28.208 -9.718 14.046 1.00 10.25 C
ANISOU 552 CG1 VAL A 583 1132 1254 1510 32 -7 170 C
ATOM 553 CG2 VAL A 583 29.589 -10.052 16.123 1.00 9.80 C
ANISOU 553 CG2 VAL A 583 1071 1189 1464 12 -16 100 C
ATOM 554 N LEU A 584 31.063 -9.154 11.834 1.00 10.75 N
ANISOU 554 N LEU A 584 1192 1304 1589 -18 44 234 N
ATOM 555 CA LEU A 584 30.946 -8.980 10.379 1.00 10.39 C
ANISOU 555 CA LEU A 584 1165 1270 1514 -19 63 285 C
ATOM 556 C LEU A 584 31.757 -10.059 9.649 1.00 12.32 C
ANISOU 556 C LEU A 584 1411 1553 1718 -29 89 282 C
ATOM 557 O LEU A 584 31.275 -10.575 8.631 1.00 12.28 O
ANISOU 557 O LEU A 584 1431 1581 1655 -23 92 301 O
ATOM 558 CB LEU A 584 31.406 -7.581 9.964 1.00 11.32 C
ANISOU 558 CB LEU A 584 1284 1341 1676 -31 83 327 C
ATOM 559 CG LEU A 584 31.162 -7.242 8.450 1.00 14.96 C
ANISOU 559 CG LEU A 584 1775 1814 2097 -29 101 393 C
ATOM 560 CD1 LEU A 584 29.714 -7.476 8.057 1.00 16.09 C
ANISOU 560 CD1 LEU A 584 1938 1982 2195 -2 63 409 C
ATOM 561 CD2 LEU A 584 31.579 -5.823 8.140 1.00 17.78 C
ANISOU 561 CD2 LEU A 584 2134 2114 2508 -42 122 441 C
ATOM 562 N PHE A 585 32.958 -10.431 10.143 1.00 10.28 N
ANISOU 562 N PHE A 585 1125 1291 1490 -44 106 255 N
ATOM 563 CA PHE A 585 33.700 -11.504 9.460 1.00 10.04 C
ANISOU 563 CA PHE A 585 1092 1292 1431 -48 138 248 C
ATOM 564 C PHE A 585 32.866 -12.793 9.444 1.00 11.16 C
ANISOU 564 C PHE A 585 1252 1469 1521 -31 116 222 C
ATOM 565 O PHE A 585 32.843 -13.504 8.419 1.00 10.97 O
ANISOU 565 O PHE A 585 1249 1472 1446 -29 137 225 O
ATOM 566 CB PHE A 585 35.000 -11.812 10.189 1.00 11.22 C
ANISOU 566 CB PHE A 585 1198 1430 1634 -59 148 221 C
ATOM 567 CG PHE A 585 36.010 -10.702 10.089 1.00 12.78 C
ANISOU 567 CG PHE A 585 1368 1595 1893 -84 174 243 C
ATOM 568 CD1 PHE A 585 36.102 -9.916 8.935 1.00 16.72 C
ANISOU 568 CD1 PHE A 585 1885 2085 2382 -95 217 292 C
ATOM 569 CD2 PHE A 585 36.867 -10.433 11.141 1.00 16.38 C
ANISOU 569 CD2 PHE A 585 1781 2025 2415 -98 154 217 C
ATOM 570 CE1 PHE A 585 37.053 -8.889 8.834 1.00 19.79 C
ANISOU 570 CE1 PHE A 585 2245 2437 2837 -123 247 318 C
ATOM 571 CE2 PHE A 585 37.797 -9.395 11.050 1.00 19.54 C
ANISOU 571 CE2 PHE A 585 2151 2390 2884 -127 176 236 C
ATOM 572 CZ PHE A 585 37.870 -8.622 9.902 1.00 18.30 C
ANISOU 572 CZ PHE A 585 2009 2220 2725 -140 225 286 C
ATOM 573 N ILE A 586 32.152 -13.098 10.536 1.00 9.75 N
ANISOU 573 N ILE A 586 1067 1287 1351 -20 78 196 N
ATOM 574 CA ILE A 586 31.315 -14.299 10.503 1.00 8.98 C
ANISOU 574 CA ILE A 586 984 1216 1214 -9 60 176 C
ATOM 575 C ILE A 586 30.207 -14.184 9.457 1.00 11.02 C
ANISOU 575 C ILE A 586 1270 1493 1424 -5 48 199 C
ATOM 576 O ILE A 586 29.849 -15.179 8.831 1.00 12.39 O
ANISOU 576 O ILE A 586 1460 1692 1555 -4 45 186 O
ATOM 577 CB ILE A 586 30.749 -14.559 11.927 1.00 10.26 C
ANISOU 577 CB ILE A 586 1134 1370 1395 -1 28 151 C
ATOM 578 CG1 ILE A 586 31.929 -14.983 12.866 1.00 10.96 C
ANISOU 578 CG1 ILE A 586 1199 1449 1517 -5 30 129 C
ATOM 579 CG2 ILE A 586 29.659 -15.675 11.927 1.00 11.73 C
ANISOU 579 CG2 ILE A 586 1331 1577 1550 6 11 138 C
ATOM 580 CD1 ILE A 586 31.630 -14.901 14.382 1.00 10.35 C
ANISOU 580 CD1 ILE A 586 1117 1362 1452 0 0 110 C
ATOM 581 N LYS A 587 29.655 -12.990 9.303 1.00 9.45 N
ANISOU 581 N LYS A 587 1076 1280 1236 -1 37 232 N
ATOM 582 CA LYS A 587 28.556 -12.760 8.357 1.00 10.76 C
ANISOU 582 CA LYS A 587 1263 1462 1362 7 14 262 C
ATOM 583 C LYS A 587 29.060 -12.501 6.938 1.00 13.70 C
ANISOU 583 C LYS A 587 1668 1851 1687 -2 38 298 C
ATOM 584 O LYS A 587 28.231 -12.358 6.023 1.00 14.15 O
ANISOU 584 O LYS A 587 1749 1928 1697 3 13 327 O
ATOM 585 CB LYS A 587 27.669 -11.621 8.880 1.00 13.99 C
ANISOU 585 CB LYS A 587 1661 1844 1812 22 -11 284 C
ATOM 586 CG LYS A 587 27.058 -12.015 10.225 1.00 15.81 C
ANISOU 586 CG LYS A 587 1867 2067 2073 31 -26 246 C
ATOM 587 CD LYS A 587 25.979 -11.056 10.725 1.00 20.59 C
ANISOU 587 CD LYS A 587 2458 2648 2718 51 -44 259 C
ATOM 588 CE LYS A 587 24.658 -11.241 9.993 1.00 20.24 C
ANISOU 588 CE LYS A 587 2409 2626 2654 64 -79 283 C
ATOM 589 NZ LYS A 587 23.549 -10.566 10.742 1.00 25.16 N
ANISOU 589 NZ LYS A 587 3004 3227 3330 88 -90 284 N
ATOM 590 N ALA A 588 30.385 -12.442 6.720 1.00 12.54 N
ANISOU 590 N ALA A 588 1519 1698 1549 -15 87 298 N
ATOM 591 CA ALA A 588 30.931 -12.159 5.378 1.00 12.81 C
ANISOU 591 CA ALA A 588 1585 1748 1534 -25 125 336 C
ATOM 592 C ALA A 588 30.868 -13.441 4.550 1.00 12.90 C
ANISOU 592 C ALA A 588 1626 1802 1471 -26 133 305 C
ATOM 593 O ALA A 588 31.809 -14.229 4.494 1.00 13.85 O
ANISOU 593 O ALA A 588 1740 1929 1593 -31 176 272 O
ATOM 594 CB ALA A 588 32.368 -11.660 5.491 1.00 14.38 C
ANISOU 594 CB ALA A 588 1761 1922 1780 -41 182 345 C
ATOM 595 N SER A 589 29.702 -13.663 3.932 1.00 12.10 N
ANISOU 595 N SER A 589 1556 1729 1313 -20 87 313 N
ATOM 596 CA SER A 589 29.457 -14.897 3.188 1.00 10.34 C
ANISOU 596 CA SER A 589 1366 1543 1020 -24 81 274 C
ATOM 597 C SER A 589 30.433 -15.215 2.050 1.00 14.76 C
ANISOU 597 C SER A 589 1966 2128 1516 -34 144 271 C
ATOM 598 O SER A 589 30.655 -16.383 1.736 1.00 14.66 O
ANISOU 598 O SER A 589 1969 2131 1469 -36 161 218 O
ATOM 599 CB SER A 589 28.022 -14.930 2.662 1.00 11.97 C
ANISOU 599 CB SER A 589 1595 1775 1179 -21 11 287 C
ATOM 600 OG SER A 589 27.885 -13.959 1.631 1.00 15.04 O
ANISOU 600 OG SER A 589 2021 2179 1514 -20 7 349 O
ATOM 601 N CYS A 590 31.007 -14.189 1.415 1.00 13.51 N
ANISOU 601 N CYS A 590 1825 1968 1340 -39 184 326 N
ATOM 602 CA CYS A 590 31.928 -14.436 0.306 1.00 14.19 C
ANISOU 602 CA CYS A 590 1951 2080 1360 -48 257 328 C
ATOM 603 C CYS A 590 33.328 -14.855 0.710 1.00 17.31 C
ANISOU 603 C CYS A 590 2307 2456 1815 -51 333 295 C
ATOM 604 O CYS A 590 34.141 -15.203 -0.142 1.00 18.04 O
ANISOU 604 O CYS A 590 2424 2568 1862 -56 405 286 O
ATOM 605 CB CYS A 590 31.937 -13.272 -0.675 1.00 15.31 C
ANISOU 605 CB CYS A 590 2136 2234 1449 -55 274 407 C
ATOM 606 SG CYS A 590 30.323 -13.005 -1.460 1.00 19.36 S
ANISOU 606 SG CYS A 590 2704 2782 1871 -48 179 445 S
ATOM 607 N GLU A 591 33.628 -14.804 2.026 1.00 14.12 N
ANISOU 607 N GLU A 591 1839 2013 1513 -47 318 278 N
ATOM 608 CA GLU A 591 34.919 -15.232 2.569 1.00 13.81 C
ANISOU 608 CA GLU A 591 1750 1954 1544 -47 373 248 C
ATOM 609 C GLU A 591 34.868 -16.683 2.987 1.00 15.21 C
ANISOU 609 C GLU A 591 1917 2133 1728 -34 360 181 C
ATOM 610 O GLU A 591 35.865 -17.233 3.441 1.00 15.01 O
ANISOU 610 O GLU A 591 1849 2092 1762 -28 397 153 O
ATOM 611 CB GLU A 591 35.321 -14.339 3.734 1.00 15.28 C
ANISOU 611 CB GLU A 591 1878 2099 1830 -53 357 269 C
ATOM 612 CG GLU A 591 35.489 -12.909 3.276 1.00 17.17 C
ANISOU 612 CG GLU A 591 2125 2323 2074 -68 378 336 C
ATOM 613 CD GLU A 591 35.823 -11.878 4.334 1.00 21.32 C
ANISOU 613 CD GLU A 591 2602 2802 2698 -79 359 353 C
ATOM 614 OE1 GLU A 591 36.252 -12.266 5.447 1.00 21.61 O
ANISOU 614 OE1 GLU A 591 2589 2820 2800 -76 340 313 O
ATOM 615 OE2 GLU A 591 35.676 -10.676 4.030 1.00 19.93 O
ANISOU 615 OE2 GLU A 591 2438 2604 2530 -89 363 408 O
ATOM 616 N ARG A 592 33.703 -17.334 2.789 1.00 14.93 N
ANISOU 616 N ARG A 592 1919 2117 1637 -30 307 157 N
ATOM 617 CA ARG A 592 33.543 -18.734 3.094 1.00 14.99 C
ANISOU 617 CA ARG A 592 1924 2120 1651 -21 294 95 C
ATOM 618 C ARG A 592 34.063 -19.533 1.920 1.00 25.06 C
ANISOU 618 C ARG A 592 3241 3417 2863 -20 354 59 C
ATOM 619 O ARG A 592 34.051 -19.051 0.791 1.00 29.19 O
ANISOU 619 O ARG A 592 3813 3971 3307 -28 382 81 O
ATOM 620 CB ARG A 592 32.054 -19.036 3.333 1.00 13.06 C
ANISOU 620 CB ARG A 592 1698 1884 1381 -23 214 86 C
ATOM 621 CG ARG A 592 31.527 -18.293 4.554 1.00 13.20 C
ANISOU 621 CG ARG A 592 1674 1879 1462 -21 165 115 C
ATOM 622 CD ARG A 592 30.051 -18.492 4.792 1.00 12.87 C
ANISOU 622 CD ARG A 592 1640 1844 1405 -22 96 112 C
ATOM 623 NE ARG A 592 29.580 -17.549 5.801 1.00 11.22 N
ANISOU 623 NE ARG A 592 1397 1616 1248 -17 65 144 N
ATOM 624 CZ ARG A 592 28.311 -17.156 5.947 1.00 11.58 C
ANISOU 624 CZ ARG A 592 1441 1668 1292 -15 13 161 C
ATOM 625 NH1 ARG A 592 27.351 -17.654 5.157 1.00 11.91 N
ANISOU 625 NH1 ARG A 592 1507 1735 1283 -21 -24 153 N
ATOM 626 NH2 ARG A 592 28.003 -16.206 6.820 1.00 10.70 N
ANISOU 626 NH2 ARG A 592 1301 1534 1228 -7 -2 187 N
ATOM 627 N HIS A 593 34.538 -20.726 2.179 1.00 22.60 N
ANISOU 627 N HIS A 593 2914 3087 2586 -8 377 4 N
ATOM 628 CA HIS A 593 34.988 -21.595 1.100 1.00 23.03 C
ANISOU 628 CA HIS A 593 3010 3156 2584 -3 438 -45 C
ATOM 629 C HIS A 593 33.923 -22.658 0.913 1.00 25.40 C
ANISOU 629 C HIS A 593 3351 3458 2841 -7 384 -98 C
ATOM 630 O HIS A 593 33.550 -23.369 1.852 1.00 23.04 O
ANISOU 630 O HIS A 593 3022 3128 2605 -2 341 -120 O
ATOM 631 CB HIS A 593 36.374 -22.182 1.376 1.00 24.56 C
ANISOU 631 CB HIS A 593 3156 3322 2855 16 513 -72 C
ATOM 632 N SER A 594 33.378 -22.727 -0.310 1.00 24.19 N
ANISOU 632 N SER A 594 3270 3343 2579 -20 382 -114 N
ATOM 633 CA SER A 594 32.309 -23.665 -0.673 1.00 24.13 C
ANISOU 633 CA SER A 594 3307 3341 2521 -32 323 -168 C
ATOM 634 C SER A 594 31.074 -23.499 0.240 1.00 24.15 C
ANISOU 634 C SER A 594 3278 3334 2566 -41 226 -144 C
ATOM 635 O SER A 594 30.391 -24.476 0.553 1.00 23.45 O
ANISOU 635 O SER A 594 3187 3224 2499 -48 183 -188 O
ATOM 636 CB SER A 594 32.825 -25.103 -0.692 1.00 30.35 C
ANISOU 636 CB SER A 594 4098 4095 3340 -20 365 -249 C
ATOM 637 OG SER A 594 34.010 -25.174 -1.468 1.00 42.72 O
ANISOU 637 OG SER A 594 5683 5669 4878 -7 467 -270 O
ATOM 638 N GLY A 595 30.832 -22.253 0.673 1.00 19.57 N
ANISOU 638 N GLY A 595 2670 2762 2004 -41 200 -74 N
ATOM 639 CA GLY A 595 29.688 -21.881 1.500 1.00 18.46 C
ANISOU 639 CA GLY A 595 2498 2615 1902 -47 120 -44 C
ATOM 640 C GLY A 595 29.865 -22.185 2.978 1.00 18.94 C
ANISOU 640 C GLY A 595 2496 2633 2066 -37 115 -46 C
ATOM 641 O GLY A 595 28.949 -21.933 3.755 1.00 17.18 O
ANISOU 641 O GLY A 595 2246 2403 1879 -40 61 -25 O
ATOM 642 N GLU A 596 31.026 -22.711 3.378 1.00 16.28 N
ANISOU 642 N GLU A 596 2137 2270 1780 -23 172 -67 N
ATOM 643 CA GLU A 596 31.238 -23.078 4.776 1.00 14.64 C
ANISOU 643 CA GLU A 596 1877 2024 1661 -12 161 -66 C
ATOM 644 C GLU A 596 32.015 -22.028 5.524 1.00 14.32 C
ANISOU 644 C GLU A 596 1795 1977 1669 -4 178 -21 C
ATOM 645 O GLU A 596 33.083 -21.563 5.065 1.00 14.77 O
ANISOU 645 O GLU A 596 1846 2038 1727 1 232 -10 O
ATOM 646 CB GLU A 596 32.042 -24.383 4.880 1.00 16.09 C
ANISOU 646 CB GLU A 596 2054 2176 1884 1 201 -115 C
ATOM 647 CG GLU A 596 31.267 -25.608 4.444 1.00 22.47 C
ANISOU 647 CG GLU A 596 2896 2972 2668 -10 178 -169 C
ATOM 648 CD GLU A 596 32.114 -26.850 4.291 1.00 32.90 C
ANISOU 648 CD GLU A 596 4220 4257 4023 6 227 -222 C
ATOM 649 OE1 GLU A 596 33.279 -26.729 3.850 1.00 31.21 O
ANISOU 649 OE1 GLU A 596 4002 4045 3813 23 293 -229 O
ATOM 650 OE2 GLU A 596 31.610 -27.945 4.622 1.00 40.64 O
ANISOU 650 OE2 GLU A 596 5204 5203 5036 2 203 -255 O
ATOM 651 N LEU A 597 31.455 -21.613 6.652 1.00 10.01 N
ANISOU 651 N LEU A 597 1221 1420 1164 -4 134 4 N
ATOM 652 CA LEU A 597 32.188 -20.811 7.607 1.00 9.67 C
ANISOU 652 CA LEU A 597 1136 1362 1175 3 141 33 C
ATOM 653 C LEU A 597 33.258 -21.738 8.237 1.00 11.76 C
ANISOU 653 C LEU A 597 1370 1600 1497 17 165 10 C
ATOM 654 O LEU A 597 32.940 -22.851 8.665 1.00 12.01 O
ANISOU 654 O LEU A 597 1402 1614 1545 23 148 -14 O
ATOM 655 CB LEU A 597 31.242 -20.341 8.716 1.00 9.45 C
ANISOU 655 CB LEU A 597 1093 1328 1170 1 90 52 C
ATOM 656 CG LEU A 597 31.895 -19.665 9.944 1.00 11.17 C
ANISOU 656 CG LEU A 597 1274 1527 1441 6 85 69 C
ATOM 657 CD1 LEU A 597 32.424 -18.288 9.575 1.00 11.13 C
ANISOU 657 CD1 LEU A 597 1264 1525 1440 0 104 99 C
ATOM 658 CD2 LEU A 597 30.905 -19.556 11.065 1.00 10.65 C
ANISOU 658 CD2 LEU A 597 1203 1457 1387 7 45 75 C
ATOM 659 N MET A 598 34.510 -21.287 8.245 1.00 11.12 N
ANISOU 659 N MET A 598 1259 1513 1452 23 202 21 N
ATOM 660 CA MET A 598 35.601 -22.035 8.848 1.00 11.88 C
ANISOU 660 CA MET A 598 1314 1585 1613 40 219 6 C
ATOM 661 C MET A 598 36.000 -21.335 10.145 1.00 14.51 C
ANISOU 661 C MET A 598 1606 1908 1999 40 183 32 C
ATOM 662 O MET A 598 36.263 -20.115 10.153 1.00 16.02 O
ANISOU 662 O MET A 598 1784 2105 2196 27 185 56 O
ATOM 663 CB MET A 598 36.809 -22.022 7.873 1.00 16.17 C
ANISOU 663 CB MET A 598 1844 2132 2168 46 291 -3 C
ATOM 664 CG MET A 598 38.033 -22.747 8.391 1.00 23.82 C
ANISOU 664 CG MET A 598 2759 3075 3218 69 312 -15 C
ATOM 665 SD MET A 598 39.633 -21.870 8.146 1.00 34.28 S
ANISOU 665 SD MET A 598 4019 4399 4606 67 370 6 S
ATOM 666 CE MET A 598 39.550 -20.786 9.669 1.00 28.10 C
ANISOU 666 CE MET A 598 3201 3610 3865 51 288 42 C
ATOM 667 N LEU A 599 35.993 -22.074 11.252 1.00 11.24 N
ANISOU 667 N LEU A 599 1176 1476 1619 52 147 29 N
ATOM 668 CA LEU A 599 36.487 -21.543 12.516 1.00 10.35 C
ANISOU 668 CA LEU A 599 1028 1356 1548 52 108 47 C
ATOM 669 C LEU A 599 37.627 -22.410 12.961 1.00 11.40 C
ANISOU 669 C LEU A 599 1119 1469 1744 74 110 43 C
ATOM 670 O LEU A 599 37.523 -23.656 12.927 1.00 13.66 O
ANISOU 670 O LEU A 599 1414 1738 2039 92 114 29 O
ATOM 671 CB LEU A 599 35.433 -21.584 13.642 1.00 10.55 C
ANISOU 671 CB LEU A 599 1076 1382 1551 49 56 56 C
ATOM 672 CG LEU A 599 34.139 -20.832 13.321 1.00 11.70 C
ANISOU 672 CG LEU A 599 1256 1544 1644 34 50 60 C
ATOM 673 CD1 LEU A 599 33.141 -20.971 14.481 1.00 12.81 C
ANISOU 673 CD1 LEU A 599 1411 1684 1770 33 12 66 C
ATOM 674 CD2 LEU A 599 34.417 -19.330 13.110 1.00 13.61 C
ANISOU 674 CD2 LEU A 599 1490 1792 1890 21 56 75 C
ATOM 675 N LEU A 600 38.727 -21.784 13.405 1.00 9.43 N
ANISOU 675 N LEU A 600 820 1216 1547 73 101 55 N
ATOM 676 CA LEU A 600 39.821 -22.525 14.039 1.00 9.72 C
ANISOU 676 CA LEU A 600 805 1234 1654 95 85 58 C
ATOM 677 C LEU A 600 39.680 -22.150 15.506 1.00 11.37 C
ANISOU 677 C LEU A 600 1011 1446 1861 89 10 75 C
ATOM 678 O LEU A 600 39.726 -20.962 15.811 1.00 10.61 O
ANISOU 678 O LEU A 600 911 1362 1760 67 -9 79 O
ATOM 679 CB LEU A 600 41.199 -22.149 13.472 1.00 10.77 C
ANISOU 679 CB LEU A 600 874 1364 1855 97 127 57 C
ATOM 680 CG LEU A 600 42.323 -22.945 14.109 1.00 12.18 C
ANISOU 680 CG LEU A 600 989 1522 2117 125 104 63 C
ATOM 681 CD1 LEU A 600 42.214 -24.429 13.795 1.00 12.42 C
ANISOU 681 CD1 LEU A 600 1033 1528 2158 159 130 48 C
ATOM 682 CD2 LEU A 600 43.665 -22.423 13.659 1.00 13.55 C
ANISOU 682 CD2 LEU A 600 1087 1693 2369 122 143 65 C
ATOM 683 N VAL A 601 39.410 -23.144 16.381 1.00 9.99 N
ANISOU 683 N VAL A 601 850 1261 1684 108 -29 84 N
ATOM 684 CA VAL A 601 39.162 -22.839 17.792 1.00 9.76 C
ANISOU 684 CA VAL A 601 834 1241 1632 102 -97 101 C
ATOM 685 C VAL A 601 40.062 -23.619 18.721 1.00 11.40 C
ANISOU 685 C VAL A 601 1007 1436 1888 127 -147 122 C
ATOM 686 O VAL A 601 40.628 -24.661 18.353 1.00 11.40 O
ANISOU 686 O VAL A 601 979 1412 1940 154 -128 126 O
ATOM 687 CB VAL A 601 37.665 -23.123 18.153 1.00 11.20 C
ANISOU 687 CB VAL A 601 1081 1430 1744 96 -102 104 C
ATOM 688 CG1 VAL A 601 36.713 -22.374 17.227 1.00 11.00 C
ANISOU 688 CG1 VAL A 601 1085 1417 1677 76 -63 88 C
ATOM 689 CG2 VAL A 601 37.356 -24.623 18.129 1.00 10.98 C
ANISOU 689 CG2 VAL A 601 1069 1379 1725 117 -94 113 C
ATOM 690 N ARG A 602 40.217 -23.095 19.959 1.00 10.84 N
ANISOU 690 N ARG A 602 938 1380 1800 118 -214 134 N
ATOM 691 CA ARG A 602 40.937 -23.789 21.000 1.00 11.15 C
ANISOU 691 CA ARG A 602 955 1413 1867 140 -278 161 C
ATOM 692 C ARG A 602 39.906 -24.210 22.049 1.00 14.34 C
ANISOU 692 C ARG A 602 1427 1826 2194 140 -311 183 C
ATOM 693 O ARG A 602 39.321 -23.333 22.728 1.00 13.35 O
ANISOU 693 O ARG A 602 1341 1726 2006 117 -333 173 O
ATOM 694 CB ARG A 602 42.008 -22.872 21.602 1.00 13.46 C
ANISOU 694 CB ARG A 602 1199 1720 2197 127 -337 158 C
ATOM 695 CG ARG A 602 42.900 -23.611 22.602 1.00 22.78 C
ANISOU 695 CG ARG A 602 2344 2896 3414 152 -415 191 C
ATOM 696 CD ARG A 602 43.952 -22.680 23.178 1.00 32.84 C
ANISOU 696 CD ARG A 602 3565 4186 4728 134 -482 182 C
ATOM 697 NE ARG A 602 45.042 -22.450 22.229 1.00 42.06 N
ANISOU 697 NE ARG A 602 4643 5337 5999 134 -446 171 N
ATOM 698 CZ ARG A 602 45.233 -21.326 21.545 1.00 49.96 C
ANISOU 698 CZ ARG A 602 5620 6340 7023 101 -407 142 C
ATOM 699 NH1 ARG A 602 44.410 -20.294 21.703 1.00 42.02 N
ANISOU 699 NH1 ARG A 602 4671 5348 5946 67 -404 120 N
ATOM 700 NH2 ARG A 602 46.249 -21.224 20.698 1.00 27.36 N
ANISOU 700 NH2 ARG A 602 2675 3464 4258 103 -365 139 N
ATOM 701 N PRO A 603 39.674 -25.522 22.230 1.00 13.78 N
ANISOU 701 N PRO A 603 1373 1733 2131 166 -309 211 N
ATOM 702 CA PRO A 603 38.748 -25.953 23.306 1.00 14.78 C
ANISOU 702 CA PRO A 603 1563 1868 2187 164 -335 241 C
ATOM 703 C PRO A 603 39.234 -25.464 24.687 1.00 18.70 C
ANISOU 703 C PRO A 603 2068 2392 2645 161 -417 260 C
ATOM 704 O PRO A 603 40.436 -25.290 24.894 1.00 19.79 O
ANISOU 704 O PRO A 603 2153 2532 2835 171 -467 264 O
ATOM 705 CB PRO A 603 38.839 -27.485 23.241 1.00 17.96 C
ANISOU 705 CB PRO A 603 1963 2230 2633 195 -328 275 C
ATOM 706 CG PRO A 603 39.217 -27.777 21.815 1.00 21.38 C
ANISOU 706 CG PRO A 603 2355 2636 3134 205 -268 242 C
ATOM 707 CD PRO A 603 40.228 -26.681 21.504 1.00 15.93 C
ANISOU 707 CD PRO A 603 1609 1967 2478 197 -278 218 C
ATOM 708 N ASN A 604 38.285 -25.228 25.634 1.00 20.16 N
ANISOU 708 N ASN A 604 2319 2601 2740 146 -429 269 N
ATOM 709 CA ASN A 604 38.602 -24.751 26.993 1.00 34.42 C
ANISOU 709 CA ASN A 604 4152 4440 4487 141 -503 280 C
ATOM 710 C ASN A 604 39.311 -25.807 27.824 1.00 58.61 C
ANISOU 710 C ASN A 604 7212 7495 7562 170 -569 338 C
ATOM 711 O ASN A 604 39.149 -26.989 27.546 1.00 37.43 O
ANISOU 711 O ASN A 604 4528 4779 4914 193 -544 375 O
ATOM 712 CB ASN A 604 37.347 -24.226 27.722 1.00 35.76 C
ANISOU 712 CB ASN A 604 4397 4637 4553 119 -482 270 C
ATOM 713 CG ASN A 604 36.227 -25.216 27.992 1.00 57.59 C
ANISOU 713 CG ASN A 604 7213 7392 7276 126 -439 309 C
ATOM 714 OD1 ASN A 604 36.245 -26.381 27.573 1.00 57.34 O
ANISOU 714 OD1 ASN A 604 7167 7327 7293 144 -421 343 O
ATOM 715 ND2 ASN A 604 35.181 -24.742 28.657 1.00 43.75 N
ANISOU 715 ND2 ASN A 604 5519 5666 5440 109 -414 301 N
TER 716 ASN A 604
ATOM 717 N HIS B 512 14.759 6.234 -11.681 1.00 32.35 N
ANISOU 717 N HIS B 512 3390 4584 4320 648 -294 1100 N
ATOM 718 CA HIS B 512 14.574 4.793 -11.858 1.00 31.28 C
ANISOU 718 CA HIS B 512 3143 4491 4251 519 -414 1102 C
ATOM 719 C HIS B 512 14.513 4.372 -13.347 1.00 31.55 C
ANISOU 719 C HIS B 512 3233 4511 4245 454 -615 1083 C
ATOM 720 O HIS B 512 13.931 3.349 -13.705 1.00 28.40 O
ANISOU 720 O HIS B 512 2724 4140 3926 372 -771 1111 O
ATOM 721 CB HIS B 512 13.385 4.271 -11.025 1.00 32.92 C
ANISOU 721 CB HIS B 512 3109 4779 4621 543 -397 1226 C
ATOM 722 CG HIS B 512 13.629 4.278 -9.545 1.00 35.98 C
ANISOU 722 CG HIS B 512 3479 5177 5014 595 -206 1227 C
ATOM 723 ND1 HIS B 512 12.585 4.439 -8.644 1.00 39.38 N
ANISOU 723 ND1 HIS B 512 3740 5672 5550 707 -97 1362 N
ATOM 724 CD2 HIS B 512 14.786 4.143 -8.852 1.00 36.16 C
ANISOU 724 CD2 HIS B 512 3640 5155 4944 563 -111 1116 C
ATOM 725 CE1 HIS B 512 13.138 4.392 -7.441 1.00 37.98 C
ANISOU 725 CE1 HIS B 512 3630 5485 5317 750 60 1321 C
ATOM 726 NE2 HIS B 512 14.457 4.211 -7.513 1.00 36.60 N
ANISOU 726 NE2 HIS B 512 3636 5244 5027 660 42 1170 N
ATOM 727 N ASP B 513 15.147 5.167 -14.210 1.00 27.71 N
ANISOU 727 N ASP B 513 2933 3968 3628 496 -611 1036 N
ATOM 728 CA ASP B 513 15.305 4.849 -15.634 1.00 27.43 C
ANISOU 728 CA ASP B 513 3018 3907 3498 467 -772 1006 C
ATOM 729 C ASP B 513 16.800 4.986 -15.970 1.00 27.52 C
ANISOU 729 C ASP B 513 3243 3844 3371 439 -671 909 C
ATOM 730 O ASP B 513 17.573 5.427 -15.108 1.00 25.53 O
ANISOU 730 O ASP B 513 3016 3561 3124 436 -506 873 O
ATOM 731 CB ASP B 513 14.407 5.696 -16.550 1.00 31.01 C
ANISOU 731 CB ASP B 513 3477 4373 3931 578 -875 1088 C
ATOM 732 CG ASP B 513 14.569 7.202 -16.453 1.00 37.79 C
ANISOU 732 CG ASP B 513 4424 5195 4740 707 -724 1123 C
ATOM 733 OD1 ASP B 513 13.810 7.918 -17.130 1.00 39.65 O
ANISOU 733 OD1 ASP B 513 4662 5442 4962 812 -797 1200 O
ATOM 734 OD2 ASP B 513 15.458 7.664 -15.692 1.00 36.78 O
ANISOU 734 OD2 ASP B 513 4368 5016 4592 702 -545 1072 O
ATOM 735 N ASN B 514 17.219 4.543 -17.180 1.00 23.56 N
ANISOU 735 N ASN B 514 2889 3311 2750 420 -774 868 N
ATOM 736 CA ASN B 514 18.622 4.559 -17.627 1.00 22.50 C
ANISOU 736 CA ASN B 514 2943 3112 2493 405 -669 801 C
ATOM 737 C ASN B 514 19.517 3.758 -16.665 1.00 23.09 C
ANISOU 737 C ASN B 514 2976 3182 2616 304 -575 730 C
ATOM 738 O ASN B 514 20.689 4.048 -16.484 1.00 22.49 O
ANISOU 738 O ASN B 514 2979 3060 2506 291 -435 692 O
ATOM 739 CB ASN B 514 19.121 5.997 -17.848 1.00 29.02 C
ANISOU 739 CB ASN B 514 3875 3881 3268 492 -522 839 C
ATOM 740 CG ASN B 514 20.391 6.096 -18.654 1.00 62.98 C
ANISOU 740 CG ASN B 514 8363 8116 7450 497 -427 814 C
ATOM 741 OD1 ASN B 514 20.400 5.912 -19.878 1.00 61.68 O
ANISOU 741 OD1 ASN B 514 8342 7939 7153 553 -499 828 O
ATOM 742 ND2 ASN B 514 21.495 6.393 -17.977 1.00 54.69 N
ANISOU 742 ND2 ASN B 514 7315 7019 6446 449 -264 784 N
ATOM 743 N LEU B 515 18.952 2.737 -16.046 1.00 16.73 N
ANISOU 743 N LEU B 515 2033 2420 1902 233 -658 721 N
ATOM 744 CA LEU B 515 19.711 1.978 -15.087 1.00 14.87 C
ANISOU 744 CA LEU B 515 1758 2184 1709 153 -575 664 C
ATOM 745 C LEU B 515 20.549 0.889 -15.748 1.00 16.84 C
ANISOU 745 C LEU B 515 2127 2398 1872 97 -621 592 C
ATOM 746 O LEU B 515 20.237 0.478 -16.866 1.00 16.45 O
ANISOU 746 O LEU B 515 2173 2333 1745 110 -761 584 O
ATOM 747 CB LEU B 515 18.738 1.393 -14.064 1.00 15.31 C
ANISOU 747 CB LEU B 515 1617 2296 1905 116 -612 708 C
ATOM 748 CG LEU B 515 17.828 2.404 -13.392 1.00 19.47 C
ANISOU 748 CG LEU B 515 2025 2861 2510 201 -550 792 C
ATOM 749 CD1 LEU B 515 16.841 1.696 -12.475 1.00 22.63 C
ANISOU 749 CD1 LEU B 515 2222 3321 3056 174 -571 863 C
ATOM 750 CD2 LEU B 515 18.645 3.416 -12.548 1.00 20.83 C
ANISOU 750 CD2 LEU B 515 2262 3002 2652 254 -369 759 C
ATOM 751 N VAL B 516 21.620 0.449 -15.062 1.00 14.58 N
ANISOU 751 N VAL B 516 1851 2098 1592 49 -509 537 N
ATOM 752 CA VAL B 516 22.544 -0.560 -15.554 1.00 15.55 C
ANISOU 752 CA VAL B 516 2084 2186 1638 14 -517 474 C
ATOM 753 C VAL B 516 22.686 -1.649 -14.511 1.00 17.34 C
ANISOU 753 C VAL B 516 2214 2428 1947 -64 -514 442 C
ATOM 754 O VAL B 516 22.863 -1.364 -13.314 1.00 14.50 O
ANISOU 754 O VAL B 516 1753 2093 1663 -76 -416 449 O
ATOM 755 CB VAL B 516 23.915 0.087 -15.893 1.00 19.14 C
ANISOU 755 CB VAL B 516 2653 2601 2019 53 -359 460 C
ATOM 756 CG1 VAL B 516 24.912 -0.954 -16.394 1.00 19.80 C
ANISOU 756 CG1 VAL B 516 2846 2656 2023 44 -338 410 C
ATOM 757 CG2 VAL B 516 23.757 1.201 -16.937 1.00 19.85 C
ANISOU 757 CG2 VAL B 516 2847 2666 2028 140 -343 513 C
ATOM 758 N LEU B 517 22.575 -2.903 -14.969 1.00 16.47 N
ANISOU 758 N LEU B 517 2152 2294 1813 -108 -631 407 N
ATOM 759 CA LEU B 517 22.684 -4.084 -14.133 1.00 16.83 C
ANISOU 759 CA LEU B 517 2127 2336 1931 -181 -641 383 C
ATOM 760 C LEU B 517 24.113 -4.599 -14.198 1.00 18.03 C
ANISOU 760 C LEU B 517 2391 2456 2004 -173 -542 320 C
ATOM 761 O LEU B 517 24.633 -4.894 -15.282 1.00 18.32 O
ANISOU 761 O LEU B 517 2590 2449 1923 -133 -564 284 O
ATOM 762 CB LEU B 517 21.641 -5.132 -14.584 1.00 18.53 C
ANISOU 762 CB LEU B 517 2323 2522 2196 -242 -844 389 C
ATOM 763 CG LEU B 517 21.353 -6.261 -13.629 1.00 23.25 C
ANISOU 763 CG LEU B 517 2804 3111 2918 -328 -866 403 C
ATOM 764 CD1 LEU B 517 20.923 -5.759 -12.255 1.00 23.83 C
ANISOU 764 CD1 LEU B 517 2689 3254 3112 -326 -747 480 C
ATOM 765 CD2 LEU B 517 20.279 -7.165 -14.209 1.00 26.95 C
ANISOU 765 CD2 LEU B 517 3248 3528 3463 -402 -1092 417 C
ATOM 766 N ILE B 518 24.781 -4.595 -13.044 1.00 16.10 N
ANISOU 766 N ILE B 518 2066 2235 1816 -189 -422 314 N
ATOM 767 CA ILE B 518 26.177 -5.015 -12.920 1.00 16.00 C
ANISOU 767 CA ILE B 518 2115 2203 1760 -178 -321 269 C
ATOM 768 C ILE B 518 26.223 -6.332 -12.145 1.00 17.64 C
ANISOU 768 C ILE B 518 2282 2405 2017 -228 -350 249 C
ATOM 769 O ILE B 518 25.511 -6.505 -11.144 1.00 18.15 O
ANISOU 769 O ILE B 518 2226 2498 2172 -264 -366 282 O
ATOM 770 CB ILE B 518 26.974 -3.894 -12.212 1.00 20.00 C
ANISOU 770 CB ILE B 518 2565 2732 2302 -157 -189 277 C
ATOM 771 CG1 ILE B 518 26.940 -2.602 -13.055 1.00 22.67 C
ANISOU 771 CG1 ILE B 518 2957 3055 2601 -110 -154 309 C
ATOM 772 CG2 ILE B 518 28.441 -4.308 -11.921 1.00 22.16 C
ANISOU 772 CG2 ILE B 518 2855 2993 2572 -153 -94 244 C
ATOM 773 CD1 ILE B 518 27.235 -1.489 -12.376 1.00 32.08 C
ANISOU 773 CD1 ILE B 518 4089 4248 3850 -104 -78 321 C
ATOM 774 N ARG B 519 27.037 -7.264 -12.624 1.00 16.18 N
ANISOU 774 N ARG B 519 2204 2176 1767 -215 -343 205 N
ATOM 775 CA ARG B 519 27.204 -8.558 -11.978 1.00 16.88 C
ANISOU 775 CA ARG B 519 2278 2242 1893 -251 -363 186 C
ATOM 776 C ARG B 519 28.678 -8.836 -11.824 1.00 17.17 C
ANISOU 776 C ARG B 519 2360 2276 1889 -204 -245 157 C
ATOM 777 O ARG B 519 29.449 -8.646 -12.768 1.00 17.30 O
ANISOU 777 O ARG B 519 2482 2272 1819 -143 -190 142 O
ATOM 778 CB ARG B 519 26.548 -9.666 -12.815 1.00 21.72 C
ANISOU 778 CB ARG B 519 2996 2778 2477 -281 -515 161 C
ATOM 779 CG ARG B 519 25.068 -9.850 -12.479 1.00 38.95 C
ANISOU 779 CG ARG B 519 5063 4959 4778 -362 -646 210 C
ATOM 780 CD ARG B 519 24.366 -10.812 -13.420 1.00 54.48 C
ANISOU 780 CD ARG B 519 7133 6832 6736 -407 -841 179 C
ATOM 781 NE ARG B 519 24.037 -10.185 -14.701 1.00 66.20 N
ANISOU 781 NE ARG B 519 8732 8302 8119 -362 -938 156 N
ATOM 782 CZ ARG B 519 22.800 -9.984 -15.151 1.00 80.75 C
ANISOU 782 CZ ARG B 519 10526 10135 10021 -405 -1109 186 C
ATOM 783 NH1 ARG B 519 21.752 -10.367 -14.430 1.00 64.74 N
ANISOU 783 NH1 ARG B 519 8314 8108 8176 -503 -1192 252 N
ATOM 784 NH2 ARG B 519 22.602 -9.408 -16.329 1.00 68.63 N
ANISOU 784 NH2 ARG B 519 9120 8588 8368 -343 -1197 162 N
ATOM 785 N MET B 520 29.086 -9.259 -10.635 1.00 14.12 N
ANISOU 785 N MET B 520 1888 1914 1564 -219 -198 159 N
ATOM 786 CA MET B 520 30.491 -9.566 -10.387 1.00 13.54 C
ANISOU 786 CA MET B 520 1827 1843 1473 -174 -101 139 C
ATOM 787 C MET B 520 30.646 -10.661 -9.377 1.00 16.05 C
ANISOU 787 C MET B 520 2112 2157 1830 -186 -108 137 C
ATOM 788 O MET B 520 29.852 -10.788 -8.438 1.00 15.82 O
ANISOU 788 O MET B 520 2004 2148 1860 -225 -142 164 O
ATOM 789 CB MET B 520 31.280 -8.327 -9.956 1.00 13.78 C
ANISOU 789 CB MET B 520 1774 1921 1541 -156 -13 151 C
ATOM 790 CG MET B 520 30.829 -7.759 -8.621 1.00 13.49 C
ANISOU 790 CG MET B 520 1625 1928 1571 -183 -26 160 C
ATOM 791 SD MET B 520 31.711 -6.253 -8.208 1.00 13.85 S
ANISOU 791 SD MET B 520 1603 1992 1666 -172 33 155 S
ATOM 792 CE MET B 520 30.834 -5.088 -9.115 1.00 12.48 C
ANISOU 792 CE MET B 520 1461 1805 1476 -177 25 181 C
ATOM 793 N LYS B 521 31.708 -11.438 -9.554 1.00 14.52 N
ANISOU 793 N LYS B 521 1978 1939 1601 -136 -58 116 N
ATOM 794 CA LYS B 521 32.024 -12.492 -8.606 1.00 14.00 C
ANISOU 794 CA LYS B 521 1890 1864 1563 -129 -54 118 C
ATOM 795 C LYS B 521 33.131 -11.977 -7.671 1.00 14.37 C
ANISOU 795 C LYS B 521 1836 1976 1648 -91 20 123 C
ATOM 796 O LYS B 521 34.018 -11.243 -8.147 1.00 14.33 O
ANISOU 796 O LYS B 521 1811 1991 1644 -60 82 122 O
ATOM 797 CB LYS B 521 32.531 -13.737 -9.371 1.00 18.57 C
ANISOU 797 CB LYS B 521 2611 2365 2079 -80 -54 91 C
ATOM 798 CG LYS B 521 31.401 -14.462 -10.095 1.00 26.95 C
ANISOU 798 CG LYS B 521 3785 3337 3117 -130 -175 73 C
ATOM 799 CD LYS B 521 31.785 -15.877 -10.480 1.00 41.35 C
ANISOU 799 CD LYS B 521 5759 5060 4892 -87 -196 40 C
ATOM 800 CE LYS B 521 30.558 -16.677 -10.851 1.00 57.43 C
ANISOU 800 CE LYS B 521 7877 6989 6954 -169 -355 25 C
ATOM 801 NZ LYS B 521 30.680 -18.106 -10.447 1.00 68.03 N
ANISOU 801 NZ LYS B 521 9293 8233 8324 -171 -383 20 N
ATOM 802 N PRO B 522 33.111 -12.321 -6.374 1.00 12.77 N
ANISOU 802 N PRO B 522 1571 1801 1480 -90 11 136 N
ATOM 803 CA PRO B 522 34.180 -11.881 -5.478 1.00 12.72 C
ANISOU 803 CA PRO B 522 1483 1847 1502 -49 41 129 C
ATOM 804 C PRO B 522 35.496 -12.568 -5.836 1.00 14.09 C
ANISOU 804 C PRO B 522 1672 2009 1674 14 92 126 C
ATOM 805 O PRO B 522 35.505 -13.638 -6.467 1.00 16.62 O
ANISOU 805 O PRO B 522 2088 2275 1951 41 107 126 O
ATOM 806 CB PRO B 522 33.679 -12.345 -4.105 1.00 14.65 C
ANISOU 806 CB PRO B 522 1705 2113 1750 -40 13 149 C
ATOM 807 CG PRO B 522 32.862 -13.560 -4.408 1.00 19.18 C
ANISOU 807 CG PRO B 522 2348 2625 2314 -65 -2 176 C
ATOM 808 CD PRO B 522 32.124 -13.160 -5.657 1.00 15.42 C
ANISOU 808 CD PRO B 522 1911 2115 1833 -120 -31 167 C
ATOM 809 N ASP B 523 36.618 -11.966 -5.402 1.00 11.92 N
ANISOU 809 N ASP B 523 1300 1777 1453 41 112 126 N
ATOM 810 CA ASP B 523 37.896 -12.580 -5.640 1.00 12.35 C
ANISOU 810 CA ASP B 523 1332 1831 1529 112 168 143 C
ATOM 811 C ASP B 523 38.121 -13.713 -4.613 1.00 16.29 C
ANISOU 811 C ASP B 523 1842 2336 2013 163 137 146 C
ATOM 812 O ASP B 523 37.224 -13.977 -3.805 1.00 16.67 O
ANISOU 812 O ASP B 523 1922 2383 2030 139 85 141 O
ATOM 813 CB ASP B 523 39.011 -11.530 -5.663 1.00 13.43 C
ANISOU 813 CB ASP B 523 1335 2003 1766 111 192 160 C
ATOM 814 CG ASP B 523 39.286 -10.827 -4.352 1.00 15.21 C
ANISOU 814 CG ASP B 523 1456 2266 2056 84 96 136 C
ATOM 815 OD1 ASP B 523 38.880 -11.361 -3.278 1.00 12.95 O
ANISOU 815 OD1 ASP B 523 1204 1996 1721 105 31 114 O
ATOM 816 OD2 ASP B 523 39.996 -9.798 -4.368 1.00 17.36 O
ANISOU 816 OD2 ASP B 523 1620 2544 2431 53 84 143 O
ATOM 817 N GLU B 524 39.315 -14.338 -4.608 1.00 16.49 N
ANISOU 817 N GLU B 524 1832 2369 2064 244 179 167 N
ATOM 818 CA GLU B 524 39.598 -15.469 -3.713 1.00 18.10 C
ANISOU 818 CA GLU B 524 2058 2572 2246 311 155 177 C
ATOM 819 C GLU B 524 39.633 -15.076 -2.229 1.00 23.21 C
ANISOU 819 C GLU B 524 2634 3275 2911 310 64 167 C
ATOM 820 O GLU B 524 39.697 -15.963 -1.384 1.00 26.22 O
ANISOU 820 O GLU B 524 3051 3657 3256 370 41 182 O
ATOM 821 CB GLU B 524 40.890 -16.197 -4.135 1.00 20.67 C
ANISOU 821 CB GLU B 524 2361 2896 2598 417 229 211 C
ATOM 822 CG GLU B 524 42.155 -15.358 -4.046 1.00 29.15 C
ANISOU 822 CG GLU B 524 3255 4033 3789 437 238 239 C
ATOM 823 CD GLU B 524 43.459 -16.118 -4.234 1.00 51.53 C
ANISOU 823 CD GLU B 524 6027 6880 6671 558 312 294 C
ATOM 824 OE1 GLU B 524 43.423 -17.293 -4.667 1.00 47.32 O
ANISOU 824 OE1 GLU B 524 5625 6296 6059 643 380 305 O
ATOM 825 OE2 GLU B 524 44.525 -15.527 -3.950 1.00 47.13 O
ANISOU 825 OE2 GLU B 524 5287 6377 6242 570 296 331 O
ATOM 826 N ASN B 525 39.563 -13.772 -1.917 1.00 17.52 N
ANISOU 826 N ASN B 525 1836 2590 2231 254 9 140 N
ATOM 827 CA ASN B 525 39.550 -13.246 -0.543 1.00 17.64 C
ANISOU 827 CA ASN B 525 1820 2645 2238 266 -94 113 C
ATOM 828 C ASN B 525 38.156 -12.672 -0.195 1.00 19.19 C
ANISOU 828 C ASN B 525 2086 2835 2371 219 -108 97 C
ATOM 829 O ASN B 525 38.010 -11.977 0.820 1.00 20.20 O
ANISOU 829 O ASN B 525 2214 2988 2473 236 -182 68 O
ATOM 830 CB ASN B 525 40.643 -12.194 -0.355 1.00 19.61 C
ANISOU 830 CB ASN B 525 1936 2920 2593 250 -166 90 C
ATOM 831 CG ASN B 525 42.036 -12.736 -0.623 1.00 31.50 C
ANISOU 831 CG ASN B 525 3337 4444 4189 306 -147 129 C
ATOM 832 OD1 ASN B 525 42.452 -13.764 -0.081 1.00 29.75 O
ANISOU 832 OD1 ASN B 525 3132 4237 3934 392 -158 149 O
ATOM 833 ND2 ASN B 525 42.775 -12.059 -1.473 1.00 28.91 N
ANISOU 833 ND2 ASN B 525 2893 4111 3982 267 -104 155 N
ATOM 834 N GLY B 526 37.172 -12.907 -1.077 1.00 15.40 N
ANISOU 834 N GLY B 526 1664 2318 1869 167 -44 117 N
ATOM 835 CA GLY B 526 35.809 -12.418 -0.868 1.00 15.32 C
ANISOU 835 CA GLY B 526 1693 2305 1824 126 -45 124 C
ATOM 836 C GLY B 526 35.635 -10.916 -1.035 1.00 18.90 C
ANISOU 836 C GLY B 526 2106 2770 2304 82 -72 89 C
ATOM 837 O GLY B 526 34.679 -10.318 -0.525 1.00 18.71 O
ANISOU 837 O GLY B 526 2105 2755 2247 80 -82 91 O
ATOM 838 N ARG B 527 36.552 -10.284 -1.789 1.00 15.53 N
ANISOU 838 N ARG B 527 1619 2336 1947 53 -71 69 N
ATOM 839 CA ARG B 527 36.520 -8.836 -2.010 1.00 15.11 C
ANISOU 839 CA ARG B 527 1528 2274 1939 5 -95 43 C
ATOM 840 C ARG B 527 36.019 -8.529 -3.408 1.00 13.66 C
ANISOU 840 C ARG B 527 1363 2062 1764 -45 -28 67 C
ATOM 841 O ARG B 527 36.241 -9.300 -4.343 1.00 13.03 O
ANISOU 841 O ARG B 527 1310 1967 1675 -38 30 93 O
ATOM 842 CB ARG B 527 37.929 -8.246 -1.888 1.00 18.04 C
ANISOU 842 CB ARG B 527 1799 2643 2412 -1 -141 24 C
ATOM 843 CG ARG B 527 38.583 -8.423 -0.519 1.00 28.48 C
ANISOU 843 CG ARG B 527 3101 3989 3730 53 -249 -11 C
ATOM 844 CD ARG B 527 40.091 -8.237 -0.571 1.00 46.27 C
ANISOU 844 CD ARG B 527 5223 6241 6117 44 -298 -7 C
ATOM 845 NE ARG B 527 40.499 -6.834 -0.694 1.00 61.94 N
ANISOU 845 NE ARG B 527 7134 8183 8218 -30 -361 -31 N
ATOM 846 CZ ARG B 527 41.707 -6.432 -1.083 1.00 76.69 C
ANISOU 846 CZ ARG B 527 8853 10032 10253 -72 -377 0 C
ATOM 847 NH1 ARG B 527 42.629 -7.320 -1.436 1.00 61.62 N
ANISOU 847 NH1 ARG B 527 6852 8156 8405 -32 -319 60 N
ATOM 848 NH2 ARG B 527 41.987 -5.138 -1.164 1.00 66.43 N
ANISOU 848 NH2 ARG B 527 7492 8673 9075 -152 -440 -16 N
ATOM 849 N PHE B 528 35.404 -7.354 -3.550 1.00 11.50 N
ANISOU 849 N PHE B 528 1093 1776 1500 -81 -40 57 N
ATOM 850 CA PHE B 528 34.900 -6.897 -4.840 1.00 10.61 C
ANISOU 850 CA PHE B 528 1007 1637 1386 -118 11 82 C
ATOM 851 C PHE B 528 35.726 -5.762 -5.440 1.00 13.26 C
ANISOU 851 C PHE B 528 1289 1943 1805 -147 36 89 C
ATOM 852 O PHE B 528 35.747 -5.637 -6.664 1.00 13.78 O
ANISOU 852 O PHE B 528 1380 1989 1866 -154 105 126 O
ATOM 853 CB PHE B 528 33.454 -6.462 -4.688 1.00 11.34 C
ANISOU 853 CB PHE B 528 1140 1733 1433 -127 -8 87 C
ATOM 854 CG PHE B 528 32.521 -7.590 -4.388 1.00 11.58 C
ANISOU 854 CG PHE B 528 1204 1779 1415 -116 -14 112 C
ATOM 855 CD1 PHE B 528 32.215 -8.537 -5.362 1.00 12.97 C
ANISOU 855 CD1 PHE B 528 1426 1931 1571 -135 -3 133 C
ATOM 856 CD2 PHE B 528 31.985 -7.750 -3.110 1.00 11.59 C
ANISOU 856 CD2 PHE B 528 1202 1808 1392 -78 -30 119 C
ATOM 857 CE1 PHE B 528 31.338 -9.597 -5.073 1.00 12.96 C
ANISOU 857 CE1 PHE B 528 1445 1921 1558 -143 -24 163 C
ATOM 858 CE2 PHE B 528 31.126 -8.814 -2.819 1.00 12.75 C
ANISOU 858 CE2 PHE B 528 1362 1959 1522 -74 -19 168 C
ATOM 859 CZ PHE B 528 30.808 -9.727 -3.796 1.00 12.28 C
ANISOU 859 CZ PHE B 528 1326 1865 1475 -118 -23 190 C
ATOM 860 N GLY B 529 36.385 -4.962 -4.608 1.00 12.17 N
ANISOU 860 N GLY B 529 1088 1794 1742 -162 -24 59 N
ATOM 861 CA GLY B 529 37.251 -3.905 -5.093 1.00 14.20 C
ANISOU 861 CA GLY B 529 1272 2005 2119 -207 -8 79 C
ATOM 862 C GLY B 529 36.667 -2.523 -5.224 1.00 15.79 C
ANISOU 862 C GLY B 529 1501 2155 2343 -244 -26 69 C
ATOM 863 O GLY B 529 37.268 -1.682 -5.882 1.00 18.17 O
ANISOU 863 O GLY B 529 1751 2404 2747 -287 14 108 O
ATOM 864 N PHE B 530 35.532 -2.241 -4.588 1.00 13.11 N
ANISOU 864 N PHE B 530 1239 1823 1919 -220 -73 30 N
ATOM 865 CA PHE B 530 34.998 -0.898 -4.674 1.00 12.54 C
ANISOU 865 CA PHE B 530 1203 1695 1866 -238 -87 21 C
ATOM 866 C PHE B 530 34.653 -0.420 -3.291 1.00 15.94 C
ANISOU 866 C PHE B 530 1684 2111 2260 -200 -186 -51 C
ATOM 867 O PHE B 530 34.519 -1.224 -2.367 1.00 16.04 O
ANISOU 867 O PHE B 530 1718 2174 2201 -148 -222 -79 O
ATOM 868 CB PHE B 530 33.737 -0.846 -5.560 1.00 12.26 C
ANISOU 868 CB PHE B 530 1232 1677 1750 -218 -22 64 C
ATOM 869 CG PHE B 530 32.533 -1.617 -5.042 1.00 11.12 C
ANISOU 869 CG PHE B 530 1130 1593 1503 -169 -34 61 C
ATOM 870 CD1 PHE B 530 31.496 -0.961 -4.370 1.00 11.74 C
ANISOU 870 CD1 PHE B 530 1250 1672 1539 -124 -55 51 C
ATOM 871 CD2 PHE B 530 32.392 -2.977 -5.305 1.00 11.37 C
ANISOU 871 CD2 PHE B 530 1158 1671 1490 -164 -13 84 C
ATOM 872 CE1 PHE B 530 30.360 -1.659 -3.956 1.00 11.66 C
ANISOU 872 CE1 PHE B 530 1250 1718 1463 -79 -42 80 C
ATOM 873 CE2 PHE B 530 31.243 -3.663 -4.909 1.00 12.03 C
ANISOU 873 CE2 PHE B 530 1261 1795 1515 -136 -21 103 C
ATOM 874 CZ PHE B 530 30.242 -3.009 -4.222 1.00 12.00 C
ANISOU 874 CZ PHE B 530 1270 1801 1488 -96 -29 110 C
ATOM 875 N ASN B 531 34.490 0.887 -3.159 1.00 13.96 N
ANISOU 875 N ASN B 531 1473 1785 2048 -211 -223 -78 N
ATOM 876 CA ASN B 531 34.087 1.508 -1.904 1.00 13.86 C
ANISOU 876 CA ASN B 531 1551 1740 1977 -150 -314 -154 C
ATOM 877 C ASN B 531 32.727 2.157 -2.091 1.00 14.93 C
ANISOU 877 C ASN B 531 1769 1871 2035 -93 -256 -131 C
ATOM 878 O ASN B 531 32.389 2.611 -3.203 1.00 14.79 O
ANISOU 878 O ASN B 531 1734 1832 2053 -127 -187 -74 O
ATOM 879 CB ASN B 531 35.063 2.612 -1.460 1.00 15.29 C
ANISOU 879 CB ASN B 531 1732 1804 2274 -201 -436 -219 C
ATOM 880 CG ASN B 531 36.507 2.215 -1.290 1.00 22.88 C
ANISOU 880 CG ASN B 531 2579 2754 3360 -269 -516 -231 C
ATOM 881 OD1 ASN B 531 36.902 1.068 -1.494 1.00 21.92 O
ANISOU 881 OD1 ASN B 531 2382 2715 3232 -267 -470 -192 O
ATOM 882 ND2 ASN B 531 37.310 3.175 -0.853 1.00 25.28 N
ANISOU 882 ND2 ASN B 531 2871 2944 3789 -326 -652 -288 N
ATOM 883 N VAL B 532 31.947 2.230 -1.003 1.00 14.12 N
ANISOU 883 N VAL B 532 1758 1785 1820 12 -278 -167 N
ATOM 884 CA VAL B 532 30.683 2.961 -1.034 1.00 14.38 C
ANISOU 884 CA VAL B 532 1862 1810 1790 89 -222 -141 C
ATOM 885 C VAL B 532 30.644 4.005 0.041 1.00 18.51 C
ANISOU 885 C VAL B 532 2520 2249 2264 175 -297 -225 C
ATOM 886 O VAL B 532 31.200 3.806 1.129 1.00 17.34 O
ANISOU 886 O VAL B 532 2434 2089 2067 218 -387 -300 O
ATOM 887 CB VAL B 532 29.410 2.102 -0.956 1.00 18.42 C
ANISOU 887 CB VAL B 532 2355 2428 2217 163 -128 -63 C
ATOM 888 CG1 VAL B 532 29.210 1.286 -2.224 1.00 19.19 C
ANISOU 888 CG1 VAL B 532 2350 2579 2361 81 -74 14 C
ATOM 889 CG2 VAL B 532 29.375 1.235 0.295 1.00 17.98 C
ANISOU 889 CG2 VAL B 532 2332 2428 2070 246 -137 -79 C
ATOM 890 N LYS B 533 29.950 5.111 -0.247 1.00 16.46 N
ANISOU 890 N LYS B 533 2327 1927 2002 216 -265 -214 N
ATOM 891 CA LYS B 533 29.637 6.160 0.714 1.00 16.40 C
ANISOU 891 CA LYS B 533 2484 1829 1919 331 -316 -289 C
ATOM 892 C LYS B 533 28.104 6.312 0.686 1.00 17.96 C
ANISOU 892 C LYS B 533 2712 2088 2026 465 -185 -207 C
ATOM 893 O LYS B 533 27.438 5.917 -0.286 1.00 16.39 O
ANISOU 893 O LYS B 533 2398 1965 1865 428 -94 -105 O
ATOM 894 CB LYS B 533 30.281 7.501 0.338 1.00 19.24 C
ANISOU 894 CB LYS B 533 2897 2025 2390 258 -400 -345 C
ATOM 895 CG LYS B 533 31.740 7.618 0.714 1.00 32.62 C
ANISOU 895 CG LYS B 533 4579 3627 4188 152 -561 -436 C
ATOM 896 CD LYS B 533 32.299 8.991 0.353 1.00 40.77 C
ANISOU 896 CD LYS B 533 5656 4475 5360 68 -643 -475 C
ATOM 897 CE LYS B 533 33.781 9.062 0.640 1.00 48.88 C
ANISOU 897 CE LYS B 533 6621 5409 6541 -63 -813 -543 C
ATOM 898 NZ LYS B 533 34.457 10.109 -0.172 1.00 57.37 N
ANISOU 898 NZ LYS B 533 7643 6328 7829 -203 -843 -515 N
ATOM 899 N GLY B 534 27.549 6.858 1.753 1.00 17.26 N
ANISOU 899 N GLY B 534 2776 1966 1815 630 -181 -249 N
ATOM 900 CA GLY B 534 26.118 7.161 1.784 1.00 17.51 C
ANISOU 900 CA GLY B 534 2830 2046 1775 779 -46 -160 C
ATOM 901 C GLY B 534 25.241 6.148 2.483 1.00 19.88 C
ANISOU 901 C GLY B 534 3092 2482 1981 900 68 -73 C
ATOM 902 O GLY B 534 25.715 5.135 3.009 1.00 19.32 O
ANISOU 902 O GLY B 534 2994 2469 1878 878 46 -84 O
ATOM 903 N GLY B 535 23.953 6.444 2.496 1.00 18.55 N
ANISOU 903 N GLY B 535 2913 2359 1778 1034 197 28 N
ATOM 904 CA GLY B 535 22.972 5.602 3.163 1.00 19.35 C
ANISOU 904 CA GLY B 535 2957 2580 1814 1163 334 146 C
ATOM 905 C GLY B 535 21.983 6.467 3.902 1.00 25.39 C
ANISOU 905 C GLY B 535 3849 3328 2471 1402 449 185 C
ATOM 906 O GLY B 535 22.251 7.652 4.126 1.00 26.43 O
ANISOU 906 O GLY B 535 4161 3337 2544 1475 391 82 O
ATOM 907 N TYR B 536 20.831 5.885 4.250 1.00 24.54 N
ANISOU 907 N TYR B 536 3640 3333 2350 1525 615 344 N
ATOM 908 CA TYR B 536 19.731 6.600 4.907 1.00 28.28 C
ANISOU 908 CA TYR B 536 4199 3815 2732 1781 771 426 C
ATOM 909 C TYR B 536 20.165 7.404 6.150 1.00 33.37 C
ANISOU 909 C TYR B 536 5157 4355 3167 1986 750 292 C
ATOM 910 O TYR B 536 19.754 8.552 6.304 1.00 34.42 O
ANISOU 910 O TYR B 536 5437 4408 3234 2141 784 265 O
ATOM 911 CB TYR B 536 18.582 5.641 5.223 1.00 31.97 C
ANISOU 911 CB TYR B 536 4484 4425 3238 1871 959 636 C
ATOM 912 N ASP B 537 21.035 6.825 6.991 1.00 30.24 N
ANISOU 912 N ASP B 537 4878 3947 2664 1987 673 198 N
ATOM 913 CA ASP B 537 21.601 7.450 8.187 1.00 30.91 C
ANISOU 913 CA ASP B 537 5281 3925 2538 2166 600 46 C
ATOM 914 C ASP B 537 22.494 8.680 7.910 1.00 36.88 C
ANISOU 914 C ASP B 537 6209 4498 3307 2087 390 -150 C
ATOM 915 O ASP B 537 22.567 9.581 8.752 1.00 38.71 O
ANISOU 915 O ASP B 537 6724 4610 3373 2276 346 -262 O
ATOM 916 CB ASP B 537 22.360 6.404 9.020 1.00 30.81 C
ANISOU 916 CB ASP B 537 5319 3955 2432 2159 541 2 C
ATOM 917 CG ASP B 537 23.566 5.774 8.333 1.00 26.34 C
ANISOU 917 CG ASP B 537 4618 3381 2010 1871 353 -81 C
ATOM 918 OD1 ASP B 537 23.471 5.471 7.114 1.00 26.82 O
ANISOU 918 OD1 ASP B 537 4441 3484 2265 1667 359 -12 O
ATOM 919 OD2 ASP B 537 24.558 5.481 9.036 1.00 33.93 O
ANISOU 919 OD2 ASP B 537 5704 4304 2883 1867 211 -199 O
ATOM 920 N GLN B 538 23.156 8.717 6.733 1.00 31.57 N
ANISOU 920 N GLN B 538 5373 3793 2830 1817 267 -184 N
ATOM 921 CA GLN B 538 24.037 9.802 6.286 1.00 30.56 C
ANISOU 921 CA GLN B 538 5347 3490 2775 1697 82 -333 C
ATOM 922 C GLN B 538 23.248 10.854 5.494 1.00 34.33 C
ANISOU 922 C GLN B 538 5812 3911 3319 1732 160 -275 C
ATOM 923 O GLN B 538 23.844 11.845 5.062 1.00 33.79 O
ANISOU 923 O GLN B 538 5829 3685 3323 1642 33 -374 O
ATOM 924 CB GLN B 538 25.175 9.253 5.390 1.00 29.93 C
ANISOU 924 CB GLN B 538 5083 3412 2877 1402 -56 -368 C
ATOM 925 CG GLN B 538 26.161 8.307 6.095 1.00 27.71 C
ANISOU 925 CG GLN B 538 4811 3164 2553 1349 -168 -440 C
ATOM 926 CD GLN B 538 27.367 7.915 5.275 1.00 34.97 C
ANISOU 926 CD GLN B 538 5569 4067 3653 1087 -303 -479 C
ATOM 927 OE1 GLN B 538 27.729 8.534 4.256 1.00 29.40 O
ANISOU 927 OE1 GLN B 538 4785 3285 3101 935 -347 -483 O
ATOM 928 NE2 GLN B 538 28.051 6.882 5.729 1.00 31.99 N
ANISOU 928 NE2 GLN B 538 5145 3756 3255 1044 -361 -499 N
ATOM 929 N LYS B 539 21.925 10.614 5.265 1.00 30.07 N
ANISOU 929 N LYS B 539 5149 3499 2777 1853 364 -101 N
ATOM 930 CA LYS B 539 21.004 11.448 4.473 1.00 30.14 C
ANISOU 930 CA LYS B 539 5105 3493 2855 1906 458 -9 C
ATOM 931 C LYS B 539 21.580 11.755 3.072 1.00 31.74 C
ANISOU 931 C LYS B 539 5179 3638 3241 1656 350 -25 C
ATOM 932 O LYS B 539 21.448 12.864 2.540 1.00 31.21 O
ANISOU 932 O LYS B 539 5186 3458 3215 1671 333 -40 O
ATOM 933 CB LYS B 539 20.556 12.707 5.240 1.00 35.56 C
ANISOU 933 CB LYS B 539 6070 4049 3394 2165 499 -68 C
ATOM 934 CG LYS B 539 19.585 12.434 6.393 1.00 51.25 C
ANISOU 934 CG LYS B 539 8146 6125 5200 2467 690 20 C
ATOM 935 CD LYS B 539 18.217 11.913 5.916 1.00 62.24 C
ANISOU 935 CD LYS B 539 9269 7697 6681 2535 909 261 C
ATOM 936 CE LYS B 539 17.052 12.691 6.483 1.00 75.91 C
ANISOU 936 CE LYS B 539 11117 9424 8300 2860 1103 356 C
ATOM 937 NZ LYS B 539 16.813 12.378 7.917 1.00 87.36 N
ANISOU 937 NZ LYS B 539 12751 10906 9534 3128 1234 368 N
ATOM 938 N MET B 540 22.266 10.755 2.501 1.00 26.52 N
ANISOU 938 N MET B 540 4344 3051 2682 1439 283 -18 N
ATOM 939 CA MET B 540 22.927 10.889 1.213 1.00 26.78 C
ANISOU 939 CA MET B 540 4264 3041 2869 1215 198 -25 C
ATOM 940 C MET B 540 22.688 9.613 0.408 1.00 24.39 C
ANISOU 940 C MET B 540 3718 2898 2650 1086 241 88 C
ATOM 941 O MET B 540 22.618 8.531 1.000 1.00 21.05 O
ANISOU 941 O MET B 540 3233 2578 2186 1099 272 114 O
ATOM 942 CB MET B 540 24.453 11.079 1.415 1.00 30.83 C
ANISOU 942 CB MET B 540 4867 3426 3423 1070 26 -177 C
ATOM 943 CG MET B 540 24.861 12.445 1.991 1.00 38.63 C
ANISOU 943 CG MET B 540 6099 4208 4372 1143 -72 -307 C
ATOM 944 SD MET B 540 24.798 13.813 0.799 1.00 46.13 S
ANISOU 944 SD MET B 540 7070 5005 5452 1077 -75 -279 S
ATOM 945 CE MET B 540 26.317 13.517 -0.112 1.00 42.34 C
ANISOU 945 CE MET B 540 6448 4474 5166 780 -196 -307 C
ATOM 946 N PRO B 541 22.615 9.681 -0.940 1.00 19.97 N
ANISOU 946 N PRO B 541 3037 2350 2200 962 233 151 N
ATOM 947 CA PRO B 541 22.450 8.439 -1.704 1.00 17.62 C
ANISOU 947 CA PRO B 541 2544 2183 1968 842 243 236 C
ATOM 948 C PRO B 541 23.673 7.548 -1.560 1.00 18.52 C
ANISOU 948 C PRO B 541 2635 2302 2100 699 165 159 C
ATOM 949 O PRO B 541 24.773 8.035 -1.258 1.00 18.81 O
ANISOU 949 O PRO B 541 2772 2231 2143 648 82 49 O
ATOM 950 CB PRO B 541 22.320 8.923 -3.155 1.00 21.00 C
ANISOU 950 CB PRO B 541 2916 2587 2479 759 227 290 C
ATOM 951 CG PRO B 541 22.906 10.272 -3.182 1.00 27.04 C
ANISOU 951 CG PRO B 541 3834 3191 3250 771 191 214 C
ATOM 952 CD PRO B 541 22.689 10.866 -1.821 1.00 23.56 C
ANISOU 952 CD PRO B 541 3547 2690 2714 936 210 149 C
ATOM 953 N VAL B 542 23.480 6.252 -1.801 1.00 15.77 N
ANISOU 953 N VAL B 542 2149 2067 1775 634 183 221 N
ATOM 954 CA VAL B 542 24.577 5.275 -1.807 1.00 13.85 C
ANISOU 954 CA VAL B 542 1869 1840 1554 506 121 167 C
ATOM 955 C VAL B 542 25.326 5.423 -3.144 1.00 17.47 C
ANISOU 955 C VAL B 542 2287 2254 2097 361 74 159 C
ATOM 956 O VAL B 542 24.720 5.273 -4.213 1.00 16.08 O
ANISOU 956 O VAL B 542 2040 2118 1953 331 94 237 O
ATOM 957 CB VAL B 542 24.023 3.850 -1.627 1.00 17.89 C
ANISOU 957 CB VAL B 542 2263 2471 2063 499 163 245 C
ATOM 958 CG1 VAL B 542 25.148 2.831 -1.679 1.00 16.60 C
ANISOU 958 CG1 VAL B 542 2071 2318 1919 381 105 193 C
ATOM 959 CG2 VAL B 542 23.254 3.738 -0.307 1.00 19.34 C
ANISOU 959 CG2 VAL B 542 2484 2699 2165 662 245 283 C
ATOM 960 N ILE B 543 26.584 5.866 -3.066 1.00 14.40 N
ANISOU 960 N ILE B 543 1955 1772 1744 290 10 73 N
ATOM 961 CA ILE B 543 27.422 6.153 -4.234 1.00 14.77 C
ANISOU 961 CA ILE B 543 1972 1761 1879 171 -7 79 C
ATOM 962 C ILE B 543 28.693 5.349 -4.170 1.00 17.41 C
ANISOU 962 C ILE B 543 2253 2101 2259 70 -49 37 C
ATOM 963 O ILE B 543 29.325 5.262 -3.112 1.00 18.20 O
ANISOU 963 O ILE B 543 2386 2177 2351 78 -112 -39 O
ATOM 964 CB ILE B 543 27.719 7.697 -4.302 1.00 19.02 C
ANISOU 964 CB ILE B 543 2608 2153 2465 179 -28 46 C
ATOM 965 CG1 ILE B 543 26.430 8.557 -4.323 1.00 20.09 C
ANISOU 965 CG1 ILE B 543 2808 2277 2548 306 22 91 C
ATOM 966 CG2 ILE B 543 28.718 8.107 -5.417 1.00 20.64 C
ANISOU 966 CG2 ILE B 543 2781 2279 2781 58 -26 71 C
ATOM 967 CD1 ILE B 543 25.545 8.485 -5.553 1.00 28.61 C
ANISOU 967 CD1 ILE B 543 3822 3419 3628 315 79 200 C
ATOM 968 N VAL B 544 29.111 4.831 -5.325 1.00 15.42 N
ANISOU 968 N VAL B 544 1934 1875 2050 -12 -19 87 N
ATOM 969 CA VAL B 544 30.385 4.129 -5.433 1.00 14.55 C
ANISOU 969 CA VAL B 544 1764 1766 1997 -96 -37 66 C
ATOM 970 C VAL B 544 31.459 5.240 -5.382 1.00 17.67 C
ANISOU 970 C VAL B 544 2172 2035 2508 -156 -75 33 C
ATOM 971 O VAL B 544 31.486 6.115 -6.256 1.00 18.28 O
ANISOU 971 O VAL B 544 2265 2041 2639 -180 -31 82 O
ATOM 972 CB VAL B 544 30.431 3.322 -6.743 1.00 15.36 C
ANISOU 972 CB VAL B 544 1822 1922 2093 -135 22 135 C
ATOM 973 CG1 VAL B 544 31.827 2.754 -6.975 1.00 14.98 C
ANISOU 973 CG1 VAL B 544 1714 1865 2113 -202 32 130 C
ATOM 974 CG2 VAL B 544 29.391 2.231 -6.757 1.00 14.89 C
ANISOU 974 CG2 VAL B 544 1747 1960 1949 -97 24 161 C
ATOM 975 N SER B 545 32.271 5.256 -4.312 1.00 15.54 N
ANISOU 975 N SER B 545 1900 1725 2278 -175 -167 -47 N
ATOM 976 CA SER B 545 33.266 6.312 -4.102 1.00 17.43 C
ANISOU 976 CA SER B 545 2143 1826 2654 -245 -244 -87 C
ATOM 977 C SER B 545 34.658 5.960 -4.643 1.00 22.20 C
ANISOU 977 C SER B 545 2613 2413 3407 -354 -238 -47 C
ATOM 978 O SER B 545 35.536 6.838 -4.690 1.00 22.81 O
ANISOU 978 O SER B 545 2653 2368 3647 -437 -288 -47 O
ATOM 979 CB SER B 545 33.354 6.648 -2.621 1.00 19.30 C
ANISOU 979 CB SER B 545 2469 2010 2852 -195 -382 -203 C
ATOM 980 OG SER B 545 33.616 5.464 -1.878 1.00 21.46 O
ANISOU 980 OG SER B 545 2710 2384 3060 -167 -420 -237 O
ATOM 981 N ARG B 546 34.869 4.692 -5.047 1.00 17.71 N
ANISOU 981 N ARG B 546 1969 1959 2800 -352 -174 -5 N
ATOM 982 CA ARG B 546 36.158 4.251 -5.572 1.00 17.51 C
ANISOU 982 CA ARG B 546 1814 1933 2905 -426 -141 48 C
ATOM 983 C ARG B 546 35.992 2.884 -6.183 1.00 18.52 C
ANISOU 983 C ARG B 546 1919 2183 2936 -385 -47 95 C
ATOM 984 O ARG B 546 35.224 2.062 -5.668 1.00 15.68 O
ANISOU 984 O ARG B 546 1611 1904 2444 -325 -69 56 O
ATOM 985 CB ARG B 546 37.201 4.125 -4.433 1.00 22.33 C
ANISOU 985 CB ARG B 546 2357 2515 3613 -465 -285 -25 C
ATOM 986 CG ARG B 546 38.650 4.081 -4.939 1.00 32.57 C
ANISOU 986 CG ARG B 546 3485 3776 5114 -555 -262 48 C
ATOM 987 CD ARG B 546 39.648 3.827 -3.834 1.00 40.97 C
ANISOU 987 CD ARG B 546 4465 4826 6277 -589 -428 -20 C
ATOM 988 NE ARG B 546 40.977 3.520 -4.370 1.00 52.79 N
ANISOU 988 NE ARG B 546 5766 6322 7970 -656 -381 75 N
ATOM 989 CZ ARG B 546 41.590 2.347 -4.244 1.00 66.29 C
ANISOU 989 CZ ARG B 546 7385 8129 9672 -621 -364 96 C
ATOM 990 NH1 ARG B 546 41.008 1.352 -3.584 1.00 49.82 N
ANISOU 990 NH1 ARG B 546 5392 6140 7396 -532 -398 26 N
ATOM 991 NH2 ARG B 546 42.793 2.161 -4.770 1.00 55.21 N
ANISOU 991 NH2 ARG B 546 5793 6722 8463 -668 -302 199 N
ATOM 992 N VAL B 547 36.705 2.647 -7.291 1.00 16.68 N
ANISOU 992 N VAL B 547 1618 1952 2769 -410 66 187 N
ATOM 993 CA VAL B 547 36.791 1.335 -7.943 1.00 14.86 C
ANISOU 993 CA VAL B 547 1380 1812 2454 -365 152 227 C
ATOM 994 C VAL B 547 38.303 1.094 -8.121 1.00 17.29 C
ANISOU 994 C VAL B 547 1550 2107 2915 -400 197 284 C
ATOM 995 O VAL B 547 38.985 1.862 -8.810 1.00 18.11 O
ANISOU 995 O VAL B 547 1587 2143 3151 -440 277 370 O
ATOM 996 CB VAL B 547 36.007 1.202 -9.268 1.00 18.45 C
ANISOU 996 CB VAL B 547 1929 2289 2792 -315 260 291 C
ATOM 997 CG1 VAL B 547 36.143 -0.223 -9.822 1.00 18.44 C
ANISOU 997 CG1 VAL B 547 1950 2361 2696 -263 317 309 C
ATOM 998 CG2 VAL B 547 34.527 1.528 -9.061 1.00 18.04 C
ANISOU 998 CG2 VAL B 547 1976 2250 2628 -284 203 250 C
ATOM 999 N ALA B 548 38.832 0.077 -7.441 1.00 16.09 N
ANISOU 999 N ALA B 548 1341 2012 2760 -383 148 248 N
ATOM 1000 CA ALA B 548 40.274 -0.177 -7.514 1.00 18.07 C
ANISOU 1000 CA ALA B 548 1435 2258 3173 -407 182 310 C
ATOM 1001 C ALA B 548 40.633 -0.906 -8.811 1.00 17.24 C
ANISOU 1001 C ALA B 548 1332 2192 3028 -341 369 414 C
ATOM 1002 O ALA B 548 39.891 -1.797 -9.224 1.00 16.12 O
ANISOU 1002 O ALA B 548 1316 2104 2707 -269 409 394 O
ATOM 1003 CB ALA B 548 40.746 -0.955 -6.296 1.00 19.62 C
ANISOU 1003 CB ALA B 548 1574 2500 3379 -396 53 238 C
ATOM 1004 N PRO B 549 41.727 -0.547 -9.488 1.00 16.47 N
ANISOU 1004 N PRO B 549 1107 2059 3091 -355 487 532 N
ATOM 1005 CA PRO B 549 42.024 -1.207 -10.758 1.00 16.88 C
ANISOU 1005 CA PRO B 549 1197 2145 3071 -257 688 637 C
ATOM 1006 C PRO B 549 42.338 -2.691 -10.574 1.00 18.26 C
ANISOU 1006 C PRO B 549 1382 2397 3157 -172 700 612 C
ATOM 1007 O PRO B 549 42.966 -3.089 -9.588 1.00 18.04 O
ANISOU 1007 O PRO B 549 1236 2394 3224 -195 601 577 O
ATOM 1008 CB PRO B 549 43.244 -0.456 -11.281 1.00 20.16 C
ANISOU 1008 CB PRO B 549 1436 2505 3719 -292 815 786 C
ATOM 1009 CG PRO B 549 43.821 0.260 -10.109 1.00 23.39 C
ANISOU 1009 CG PRO B 549 1674 2860 4351 -420 641 744 C
ATOM 1010 CD PRO B 549 42.703 0.505 -9.149 1.00 17.00 C
ANISOU 1010 CD PRO B 549 996 2043 3418 -457 445 583 C
ATOM 1011 N GLY B 550 41.882 -3.484 -11.537 1.00 15.58 N
ANISOU 1011 N GLY B 550 1203 2086 2632 -66 810 628 N
ATOM 1012 CA GLY B 550 42.184 -4.904 -11.636 1.00 15.51 C
ANISOU 1012 CA GLY B 550 1243 2127 2524 36 854 619 C
ATOM 1013 C GLY B 550 41.332 -5.792 -10.761 1.00 16.25 C
ANISOU 1013 C GLY B 550 1428 2251 2495 27 698 492 C
ATOM 1014 O GLY B 550 41.562 -7.004 -10.698 1.00 17.10 O
ANISOU 1014 O GLY B 550 1579 2386 2532 103 714 477 O
ATOM 1015 N THR B 551 40.396 -5.194 -10.010 1.00 14.35 N
ANISOU 1015 N THR B 551 1210 2002 2241 -58 556 411 N
ATOM 1016 CA THR B 551 39.530 -5.930 -9.100 1.00 13.44 C
ANISOU 1016 CA THR B 551 1165 1915 2027 -66 426 315 C
ATOM 1017 C THR B 551 38.294 -6.404 -9.829 1.00 13.90 C
ANISOU 1017 C THR B 551 1400 1966 1916 -37 427 288 C
ATOM 1018 O THR B 551 38.010 -5.942 -10.932 1.00 14.12 O
ANISOU 1018 O THR B 551 1505 1968 1893 -16 498 327 O
ATOM 1019 CB THR B 551 39.141 -5.021 -7.929 1.00 13.62 C
ANISOU 1019 CB THR B 551 1131 1930 2114 -146 290 255 C
ATOM 1020 OG1 THR B 551 38.359 -3.934 -8.422 1.00 14.50 O
ANISOU 1020 OG1 THR B 551 1296 2003 2209 -184 297 260 O
ATOM 1021 CG2 THR B 551 40.361 -4.517 -7.130 1.00 16.74 C
ANISOU 1021 CG2 THR B 551 1359 2315 2688 -187 236 264 C
ATOM 1022 N PRO B 552 37.463 -7.252 -9.185 1.00 12.56 N
ANISOU 1022 N PRO B 552 1294 1813 1667 -41 334 226 N
ATOM 1023 CA PRO B 552 36.234 -7.689 -9.853 1.00 11.50 C
ANISOU 1023 CA PRO B 552 1303 1659 1407 -33 303 205 C
ATOM 1024 C PRO B 552 35.369 -6.529 -10.326 1.00 12.19 C
ANISOU 1024 C PRO B 552 1417 1733 1481 -71 285 214 C
ATOM 1025 O PRO B 552 34.807 -6.587 -11.410 1.00 12.79 O
ANISOU 1025 O PRO B 552 1607 1786 1467 -42 297 226 O
ATOM 1026 CB PRO B 552 35.545 -8.518 -8.769 1.00 12.54 C
ANISOU 1026 CB PRO B 552 1437 1808 1520 -56 206 160 C
ATOM 1027 CG PRO B 552 36.711 -9.157 -8.049 1.00 15.50 C
ANISOU 1027 CG PRO B 552 1738 2203 1947 -20 228 162 C
ATOM 1028 CD PRO B 552 37.705 -8.012 -7.944 1.00 13.28 C
ANISOU 1028 CD PRO B 552 1332 1932 1781 -38 263 189 C
ATOM 1029 N ALA B 553 35.250 -5.458 -9.529 1.00 11.65 N
ANISOU 1029 N ALA B 553 1260 1672 1494 -123 246 205 N
ATOM 1030 CA ALA B 553 34.399 -4.309 -9.887 1.00 12.44 C
ANISOU 1030 CA ALA B 553 1387 1753 1586 -148 230 216 C
ATOM 1031 C ALA B 553 34.951 -3.517 -11.069 1.00 14.91 C
ANISOU 1031 C ALA B 553 1723 2029 1912 -127 332 280 C
ATOM 1032 O ALA B 553 34.186 -2.875 -11.792 1.00 14.44 O
ANISOU 1032 O ALA B 553 1735 1952 1801 -117 333 301 O
ATOM 1033 CB ALA B 553 34.228 -3.391 -8.689 1.00 13.70 C
ANISOU 1033 CB ALA B 553 1473 1913 1821 -188 167 185 C
ATOM 1034 N ASP B 554 36.264 -3.599 -11.316 1.00 13.28 N
ANISOU 1034 N ASP B 554 1454 1813 1777 -107 428 326 N
ATOM 1035 CA ASP B 554 36.891 -2.906 -12.406 1.00 14.34 C
ANISOU 1035 CA ASP B 554 1598 1913 1939 -76 560 415 C
ATOM 1036 C ASP B 554 36.831 -3.748 -13.672 1.00 17.03 C
ANISOU 1036 C ASP B 554 2089 2255 2126 27 643 445 C
ATOM 1037 O ASP B 554 36.826 -3.184 -14.774 1.00 18.15 O
ANISOU 1037 O ASP B 554 2313 2368 2213 81 738 513 O
ATOM 1038 CB ASP B 554 38.352 -2.653 -12.036 1.00 14.92 C
ANISOU 1038 CB ASP B 554 1508 1975 2186 -99 630 470 C
ATOM 1039 CG ASP B 554 39.119 -1.847 -13.051 1.00 19.57 C
ANISOU 1039 CG ASP B 554 2065 2519 2852 -76 792 593 C
ATOM 1040 OD1 ASP B 554 38.609 -0.794 -13.465 1.00 20.97 O
ANISOU 1040 OD1 ASP B 554 2285 2652 3031 -99 803 622 O
ATOM 1041 OD2 ASP B 554 40.214 -2.280 -13.440 1.00 21.11 O
ANISOU 1041 OD2 ASP B 554 2192 2723 3106 -23 919 673 O
ATOM 1042 N LEU B 555 36.839 -5.082 -13.518 1.00 14.96 N
ANISOU 1042 N LEU B 555 1880 2016 1789 67 610 397 N
ATOM 1043 CA LEU B 555 36.907 -5.974 -14.664 1.00 16.12 C
ANISOU 1043 CA LEU B 555 2196 2146 1783 179 678 411 C
ATOM 1044 C LEU B 555 35.591 -6.546 -15.145 1.00 19.56 C
ANISOU 1044 C LEU B 555 2807 2563 2061 191 550 343 C
ATOM 1045 O LEU B 555 35.577 -7.188 -16.197 1.00 22.30 O
ANISOU 1045 O LEU B 555 3335 2879 2261 292 581 342 O
ATOM 1046 CB LEU B 555 37.940 -7.084 -14.404 1.00 17.45 C
ANISOU 1046 CB LEU B 555 2331 2327 1970 239 743 416 C
ATOM 1047 CG LEU B 555 39.367 -6.611 -14.030 1.00 22.75 C
ANISOU 1047 CG LEU B 555 2804 3018 2820 237 866 502 C
ATOM 1048 CD1 LEU B 555 40.285 -7.796 -13.794 1.00 24.03 C
ANISOU 1048 CD1 LEU B 555 2939 3199 2992 315 921 510 C
ATOM 1049 CD2 LEU B 555 39.969 -5.670 -15.112 1.00 26.17 C
ANISOU 1049 CD2 LEU B 555 3234 3428 3283 293 1045 626 C
ATOM 1050 N CYS B 556 34.479 -6.316 -14.420 1.00 16.96 N
ANISOU 1050 N CYS B 556 2433 2247 1763 98 404 291 N
ATOM 1051 CA CYS B 556 33.203 -6.850 -14.894 1.00 17.20 C
ANISOU 1051 CA CYS B 556 2596 2255 1683 96 268 242 C
ATOM 1052 C CYS B 556 32.691 -6.027 -16.050 1.00 20.97 C
ANISOU 1052 C CYS B 556 3187 2712 2067 144 273 276 C
ATOM 1053 O CYS B 556 33.154 -4.896 -16.269 1.00 18.46 O
ANISOU 1053 O CYS B 556 2821 2400 1794 157 380 341 O
ATOM 1054 CB CYS B 556 32.185 -6.946 -13.757 1.00 16.95 C
ANISOU 1054 CB CYS B 556 2461 2248 1730 -4 135 202 C
ATOM 1055 SG CYS B 556 31.929 -5.399 -12.863 1.00 18.34 S
ANISOU 1055 SG CYS B 556 2481 2461 2026 -66 146 230 S
ATOM 1056 N VAL B 557 31.791 -6.615 -16.854 1.00 20.73 N
ANISOU 1056 N VAL B 557 3319 2648 1908 177 151 236 N
ATOM 1057 CA VAL B 557 31.231 -5.938 -18.023 1.00 21.18 C
ANISOU 1057 CA VAL B 557 3514 2685 1847 242 126 262 C
ATOM 1058 C VAL B 557 29.688 -6.072 -18.001 1.00 25.63 C
ANISOU 1058 C VAL B 557 4089 3244 2406 178 -94 218 C
ATOM 1059 O VAL B 557 29.185 -7.192 -18.118 1.00 27.53 O
ANISOU 1059 O VAL B 557 4410 3447 2605 161 -234 157 O
ATOM 1060 CB VAL B 557 31.847 -6.430 -19.364 1.00 26.07 C
ANISOU 1060 CB VAL B 557 4371 3257 2277 395 205 272 C
ATOM 1061 CG1 VAL B 557 31.281 -5.634 -20.544 1.00 27.14 C
ANISOU 1061 CG1 VAL B 557 4662 3375 2274 479 181 308 C
ATOM 1062 CG2 VAL B 557 33.371 -6.362 -19.351 1.00 25.55 C
ANISOU 1062 CG2 VAL B 557 4258 3202 2246 464 441 341 C
ATOM 1063 N PRO B 558 28.918 -4.986 -17.806 1.00 22.21 N
ANISOU 1063 N PRO B 558 3563 2841 2034 138 -132 254 N
ATOM 1064 CA PRO B 558 29.353 -3.591 -17.621 1.00 21.57 C
ANISOU 1064 CA PRO B 558 3394 2782 2018 144 5 323 C
ATOM 1065 C PRO B 558 30.137 -3.404 -16.330 1.00 23.91 C
ANISOU 1065 C PRO B 558 3512 3105 2469 74 101 325 C
ATOM 1066 O PRO B 558 29.901 -4.103 -15.345 1.00 20.79 O
ANISOU 1066 O PRO B 558 3026 2731 2143 9 35 281 O
ATOM 1067 CB PRO B 558 28.034 -2.789 -17.582 1.00 23.53 C
ANISOU 1067 CB PRO B 558 3597 3049 2295 117 -113 340 C
ATOM 1068 CG PRO B 558 26.971 -3.718 -18.132 1.00 29.66 C
ANISOU 1068 CG PRO B 558 4464 3810 2996 116 -315 295 C
ATOM 1069 CD PRO B 558 27.444 -5.105 -17.781 1.00 24.43 C
ANISOU 1069 CD PRO B 558 3821 3126 2336 84 -334 234 C
ATOM 1070 N ARG B 559 31.079 -2.459 -16.384 1.00 19.77 N
ANISOU 1070 N ARG B 559 2946 2570 1997 92 250 383 N
ATOM 1071 CA AARG B 559 31.971 -2.068 -15.302 0.50 19.64 C
ANISOU 1071 CA AARG B 559 2771 2560 2131 31 327 389 C
ATOM 1072 CA BARG B 559 31.941 -2.122 -15.277 0.50 19.81 C
ANISOU 1072 CA BARG B 559 2793 2584 2152 30 321 386 C
ATOM 1073 C ARG B 559 31.219 -1.266 -14.248 1.00 20.43 C
ANISOU 1073 C ARG B 559 2763 2674 2327 -37 252 368 C
ATOM 1074 O ARG B 559 30.313 -0.516 -14.587 1.00 19.19 O
ANISOU 1074 O ARG B 559 2639 2510 2142 -23 209 389 O
ATOM 1075 CB AARG B 559 33.108 -1.186 -15.879 0.50 21.01 C
ANISOU 1075 CB AARG B 559 2935 2697 2351 66 496 477 C
ATOM 1076 CB BARG B 559 33.137 -1.359 -15.836 0.50 22.16 C
ANISOU 1076 CB BARG B 559 3081 2847 2493 66 491 469 C
ATOM 1077 CG AARG B 559 34.254 -0.897 -14.910 0.50 24.99 C
ANISOU 1077 CG AARG B 559 3271 3194 3029 1 560 488 C
ATOM 1078 CG BARG B 559 34.256 -1.124 -14.856 0.50 29.13 C
ANISOU 1078 CG BARG B 559 3798 3726 3545 3 551 477 C
ATOM 1079 CD AARG B 559 35.248 0.145 -15.401 0.50 18.21 C
ANISOU 1079 CD AARG B 559 2364 2283 2273 7 712 593 C
ATOM 1080 CD BARG B 559 35.379 -0.414 -15.551 0.50 26.06 C
ANISOU 1080 CD BARG B 559 3383 3294 3225 34 722 585 C
ATOM 1081 NE AARG B 559 36.295 0.346 -14.393 0.50 22.16 N
ANISOU 1081 NE AARG B 559 2686 2771 2965 -73 724 593 N
ATOM 1082 NE BARG B 559 35.122 1.010 -15.732 0.50 17.72 N
ANISOU 1082 NE BARG B 559 2316 2185 2233 6 747 640 N
ATOM 1083 CZ AARG B 559 36.335 1.360 -13.529 0.50 34.74 C
ANISOU 1083 CZ AARG B 559 4180 4319 4700 -161 663 575 C
ATOM 1084 CZ BARG B 559 36.063 1.866 -16.120 0.50 28.95 C
ANISOU 1084 CZ BARG B 559 3678 3549 3773 1 888 747 C
ATOM 1085 NH1AARG B 559 35.428 2.324 -13.583 0.50 20.95 N
ANISOU 1085 NH1AARG B 559 2492 2536 2931 -171 617 568 N
ATOM 1086 NH1BARG B 559 37.296 1.441 -16.361 0.50 24.37 N
ANISOU 1086 NH1BARG B 559 3025 2970 3264 26 1022 819 N
ATOM 1087 NH2AARG B 559 37.318 1.447 -12.645 0.50 22.68 N
ANISOU 1087 NH2AARG B 559 2503 2775 3340 -229 641 565 N
ATOM 1088 NH2BARG B 559 35.778 3.152 -16.269 0.50 24.12 N
ANISOU 1088 NH2BARG B 559 3070 2872 3223 -26 904 796 N
ATOM 1089 N LEU B 560 31.650 -1.354 -12.972 1.00 16.22 N
ANISOU 1089 N LEU B 560 2109 2155 1897 -94 242 332 N
ATOM 1090 CA LEU B 560 31.108 -0.494 -11.954 1.00 15.08 C
ANISOU 1090 CA LEU B 560 1892 2011 1826 -130 193 312 C
ATOM 1091 C LEU B 560 31.977 0.766 -12.007 1.00 18.95 C
ANISOU 1091 C LEU B 560 2349 2440 2410 -146 272 349 C
ATOM 1092 O LEU B 560 33.200 0.669 -12.085 1.00 19.91 O
ANISOU 1092 O LEU B 560 2425 2541 2600 -162 344 371 O
ATOM 1093 CB LEU B 560 31.242 -1.140 -10.568 1.00 13.78 C
ANISOU 1093 CB LEU B 560 1646 1879 1709 -163 143 256 C
ATOM 1094 CG LEU B 560 30.586 -0.363 -9.427 1.00 15.03 C
ANISOU 1094 CG LEU B 560 1763 2040 1909 -168 95 230 C
ATOM 1095 CD1 LEU B 560 29.057 -0.269 -9.602 1.00 16.54 C
ANISOU 1095 CD1 LEU B 560 1976 2260 2050 -139 47 254 C
ATOM 1096 CD2 LEU B 560 30.895 -1.040 -8.127 1.00 13.79 C
ANISOU 1096 CD2 LEU B 560 1554 1913 1773 -177 60 182 C
ATOM 1097 N ASN B 561 31.356 1.946 -12.008 1.00 16.11 N
ANISOU 1097 N ASN B 561 2007 2043 2069 -141 261 367 N
ATOM 1098 CA ASN B 561 32.106 3.196 -12.090 1.00 16.63 C
ANISOU 1098 CA ASN B 561 2051 2025 2241 -166 326 408 C
ATOM 1099 C ASN B 561 31.981 4.096 -10.878 1.00 19.73 C
ANISOU 1099 C ASN B 561 2405 2370 2722 -200 260 355 C
ATOM 1100 O ASN B 561 30.908 4.173 -10.277 1.00 16.70 O
ANISOU 1100 O ASN B 561 2045 2017 2284 -166 194 316 O
ATOM 1101 CB ASN B 561 31.656 4.000 -13.330 1.00 18.53 C
ANISOU 1101 CB ASN B 561 2386 2228 2428 -114 387 489 C
ATOM 1102 CG ASN B 561 31.977 3.305 -14.631 1.00 31.01 C
ANISOU 1102 CG ASN B 561 4044 3831 3907 -58 466 547 C
ATOM 1103 OD1 ASN B 561 33.123 2.955 -14.897 1.00 29.53 O
ANISOU 1103 OD1 ASN B 561 3824 3633 3764 -64 562 584 O
ATOM 1104 ND2 ASN B 561 30.970 3.042 -15.447 1.00 27.31 N
ANISOU 1104 ND2 ASN B 561 3683 3395 3297 9 420 556 N
ATOM 1105 N GLU B 562 33.051 4.855 -10.573 1.00 19.31 N
ANISOU 1105 N GLU B 562 2298 2231 2810 -259 280 362 N
ATOM 1106 CA GLU B 562 33.020 5.837 -9.499 1.00 20.03 C
ANISOU 1106 CA GLU B 562 2387 2243 2980 -286 199 301 C
ATOM 1107 C GLU B 562 31.900 6.837 -9.835 1.00 21.23 C
ANISOU 1107 C GLU B 562 2634 2355 3077 -229 207 326 C
ATOM 1108 O GLU B 562 31.773 7.298 -10.991 1.00 21.34 O
ANISOU 1108 O GLU B 562 2690 2340 3078 -208 289 413 O
ATOM 1109 CB GLU B 562 34.363 6.592 -9.387 1.00 22.56 C
ANISOU 1109 CB GLU B 562 2634 2449 3491 -374 205 323 C
ATOM 1110 CG GLU B 562 34.482 7.444 -8.126 1.00 33.13 C
ANISOU 1110 CG GLU B 562 3987 3691 4911 -409 75 229 C
ATOM 1111 CD GLU B 562 35.700 8.344 -8.021 1.00 63.05 C
ANISOU 1111 CD GLU B 562 7702 7334 8920 -515 43 250 C
ATOM 1112 OE1 GLU B 562 36.461 8.453 -9.010 1.00 66.28 O
ANISOU 1112 OE1 GLU B 562 8032 7712 9440 -562 158 365 O
ATOM 1113 OE2 GLU B 562 35.874 8.971 -6.952 1.00 57.84 O
ANISOU 1113 OE2 GLU B 562 7070 6581 8324 -546 -98 155 O
ATOM 1114 N GLY B 563 31.106 7.159 -8.824 1.00 17.97 N
ANISOU 1114 N GLY B 563 2262 1941 2625 -186 131 257 N
ATOM 1115 CA GLY B 563 29.985 8.067 -9.007 1.00 17.78 C
ANISOU 1115 CA GLY B 563 2320 1887 2550 -111 138 281 C
ATOM 1116 C GLY B 563 28.667 7.363 -9.271 1.00 18.77 C
ANISOU 1116 C GLY B 563 2449 2132 2549 -32 138 307 C
ATOM 1117 O GLY B 563 27.610 7.996 -9.224 1.00 18.80 O
ANISOU 1117 O GLY B 563 2498 2133 2513 47 135 328 O
ATOM 1118 N ASP B 564 28.696 6.055 -9.599 1.00 14.60 N
ANISOU 1118 N ASP B 564 1870 1704 1972 -52 137 315 N
ATOM 1119 CA ASP B 564 27.451 5.328 -9.835 1.00 14.21 C
ANISOU 1119 CA ASP B 564 1809 1753 1836 0 109 342 C
ATOM 1120 C ASP B 564 26.615 5.334 -8.569 1.00 15.53 C
ANISOU 1120 C ASP B 564 1954 1957 1991 56 77 310 C
ATOM 1121 O ASP B 564 27.166 5.175 -7.481 1.00 15.08 O
ANISOU 1121 O ASP B 564 1889 1888 1952 44 62 246 O
ATOM 1122 CB ASP B 564 27.715 3.866 -10.233 1.00 14.43 C
ANISOU 1122 CB ASP B 564 1801 1855 1826 -39 95 339 C
ATOM 1123 CG ASP B 564 28.222 3.635 -11.641 1.00 18.73 C
ANISOU 1123 CG ASP B 564 2394 2386 2335 -50 134 385 C
ATOM 1124 OD1 ASP B 564 28.270 4.616 -12.434 1.00 20.86 O
ANISOU 1124 OD1 ASP B 564 2722 2599 2604 -24 181 437 O
ATOM 1125 OD2 ASP B 564 28.642 2.499 -11.927 1.00 18.94 O
ANISOU 1125 OD2 ASP B 564 2417 2450 2328 -72 131 371 O
ATOM 1126 N GLN B 565 25.306 5.540 -8.706 1.00 14.24 N
ANISOU 1126 N GLN B 565 1780 1835 1794 130 71 362 N
ATOM 1127 CA GLN B 565 24.420 5.527 -7.563 1.00 14.09 C
ANISOU 1127 CA GLN B 565 1731 1859 1763 208 74 361 C
ATOM 1128 C GLN B 565 23.779 4.174 -7.482 1.00 17.04 C
ANISOU 1128 C GLN B 565 2009 2335 2129 191 50 397 C
ATOM 1129 O GLN B 565 23.198 3.725 -8.464 1.00 16.78 O
ANISOU 1129 O GLN B 565 1938 2341 2097 169 10 451 O
ATOM 1130 CB GLN B 565 23.353 6.606 -7.715 1.00 16.04 C
ANISOU 1130 CB GLN B 565 2003 2089 2003 313 96 418 C
ATOM 1131 CG GLN B 565 22.390 6.575 -6.546 1.00 25.07 C
ANISOU 1131 CG GLN B 565 3112 3283 3130 421 130 440 C
ATOM 1132 CD GLN B 565 21.366 7.650 -6.597 1.00 29.81 C
ANISOU 1132 CD GLN B 565 3734 3867 3726 548 167 501 C
ATOM 1133 OE1 GLN B 565 21.441 8.584 -7.410 1.00 32.23 O
ANISOU 1133 OE1 GLN B 565 4103 4103 4038 557 162 515 O
ATOM 1134 NE2 GLN B 565 20.398 7.536 -5.700 1.00 24.85 N
ANISOU 1134 NE2 GLN B 565 3055 3299 3086 663 220 551 N
ATOM 1135 N VAL B 566 23.892 3.521 -6.322 1.00 14.13 N
ANISOU 1135 N VAL B 566 1615 2001 1755 201 63 368 N
ATOM 1136 CA VAL B 566 23.320 2.189 -6.127 1.00 13.07 C
ANISOU 1136 CA VAL B 566 1387 1948 1633 178 49 412 C
ATOM 1137 C VAL B 566 21.826 2.244 -5.848 1.00 16.88 C
ANISOU 1137 C VAL B 566 1781 2488 2144 259 75 512 C
ATOM 1138 O VAL B 566 21.420 2.896 -4.898 1.00 19.01 O
ANISOU 1138 O VAL B 566 2070 2759 2393 369 142 526 O
ATOM 1139 CB VAL B 566 24.070 1.470 -5.004 1.00 14.76 C
ANISOU 1139 CB VAL B 566 1612 2171 1826 169 65 358 C
ATOM 1140 CG1 VAL B 566 23.464 0.083 -4.739 1.00 14.70 C
ANISOU 1140 CG1 VAL B 566 1511 2230 1843 145 64 418 C
ATOM 1141 CG2 VAL B 566 25.586 1.392 -5.311 1.00 13.49 C
ANISOU 1141 CG2 VAL B 566 1505 1957 1663 88 36 274 C
ATOM 1142 N VAL B 567 21.002 1.530 -6.662 1.00 14.75 N
ANISOU 1142 N VAL B 567 1414 2263 1927 212 15 585 N
ATOM 1143 CA VAL B 567 19.550 1.465 -6.522 1.00 15.37 C
ANISOU 1143 CA VAL B 567 1361 2401 2078 269 23 704 C
ATOM 1144 C VAL B 567 19.149 0.142 -5.877 1.00 16.28 C
ANISOU 1144 C VAL B 567 1364 2564 2259 228 31 762 C
ATOM 1145 O VAL B 567 18.359 0.142 -4.928 1.00 17.89 O
ANISOU 1145 O VAL B 567 1482 2812 2503 315 122 852 O
ATOM 1146 CB VAL B 567 18.875 1.680 -7.907 1.00 19.31 C
ANISOU 1146 CB VAL B 567 1824 2903 2612 242 -82 751 C
ATOM 1147 CG1 VAL B 567 17.356 1.532 -7.823 1.00 21.02 C
ANISOU 1147 CG1 VAL B 567 1865 3183 2939 286 -99 888 C
ATOM 1148 CG2 VAL B 567 19.252 3.052 -8.468 1.00 19.13 C
ANISOU 1148 CG2 VAL B 567 1920 2825 2523 299 -64 714 C
ATOM 1149 N LEU B 568 19.653 -0.979 -6.415 1.00 14.51 N
ANISOU 1149 N LEU B 568 1144 2323 2047 108 -52 723 N
ATOM 1150 CA LEU B 568 19.370 -2.325 -5.881 1.00 14.60 C
ANISOU 1150 CA LEU B 568 1063 2355 2130 52 -54 776 C
ATOM 1151 C LEU B 568 20.660 -3.041 -5.562 1.00 14.91 C
ANISOU 1151 C LEU B 568 1204 2362 2101 2 -45 678 C
ATOM 1152 O LEU B 568 21.637 -2.894 -6.291 1.00 13.79 O
ANISOU 1152 O LEU B 568 1167 2179 1892 -39 -91 583 O
ATOM 1153 CB LEU B 568 18.629 -3.261 -6.840 1.00 15.96 C
ANISOU 1153 CB LEU B 568 1139 2517 2407 -55 -194 830 C
ATOM 1154 CG LEU B 568 17.332 -2.822 -7.498 1.00 20.27 C
ANISOU 1154 CG LEU B 568 1561 3089 3051 -42 -272 929 C
ATOM 1155 CD1 LEU B 568 16.797 -3.935 -8.387 1.00 21.14 C
ANISOU 1155 CD1 LEU B 568 1601 3167 3266 -169 -453 955 C
ATOM 1156 CD2 LEU B 568 16.279 -2.415 -6.491 1.00 23.75 C
ANISOU 1156 CD2 LEU B 568 1846 3592 3584 60 -148 1069 C
ATOM 1157 N ILE B 569 20.631 -3.890 -4.522 1.00 13.85 N
ANISOU 1157 N ILE B 569 1027 2246 1990 11 18 719 N
ATOM 1158 CA ILE B 569 21.739 -4.782 -4.182 1.00 13.05 C
ANISOU 1158 CA ILE B 569 1001 2119 1840 -32 18 646 C
ATOM 1159 C ILE B 569 21.122 -6.161 -4.131 1.00 16.05 C
ANISOU 1159 C ILE B 569 1286 2490 2322 -106 -12 730 C
ATOM 1160 O ILE B 569 20.245 -6.410 -3.285 1.00 16.60 O
ANISOU 1160 O ILE B 569 1250 2593 2465 -62 67 849 O
ATOM 1161 CB ILE B 569 22.409 -4.416 -2.845 1.00 14.39 C
ANISOU 1161 CB ILE B 569 1241 2305 1921 68 118 609 C
ATOM 1162 CG1 ILE B 569 23.006 -3.009 -2.947 1.00 15.00 C
ANISOU 1162 CG1 ILE B 569 1414 2362 1923 122 119 522 C
ATOM 1163 CG2 ILE B 569 23.505 -5.458 -2.514 1.00 14.62 C
ANISOU 1163 CG2 ILE B 569 1328 2312 1913 26 103 549 C
ATOM 1164 CD1 ILE B 569 23.657 -2.460 -1.666 1.00 17.57 C
ANISOU 1164 CD1 ILE B 569 1834 2683 2157 226 175 463 C
ATOM 1165 N ASN B 570 21.591 -7.066 -5.030 1.00 15.89 N
ANISOU 1165 N ASN B 570 1312 2415 2310 -209 -119 675 N
ATOM 1166 CA ASN B 570 21.048 -8.433 -5.094 1.00 16.08 C
ANISOU 1166 CA ASN B 570 1266 2398 2444 -298 -177 741 C
ATOM 1167 C ASN B 570 19.521 -8.435 -5.157 1.00 21.14 C
ANISOU 1167 C ASN B 570 1733 3056 3244 -325 -208 881 C
ATOM 1168 O ASN B 570 18.871 -9.205 -4.449 1.00 22.08 O
ANISOU 1168 O ASN B 570 1737 3172 3482 -346 -161 999 O
ATOM 1169 CB ASN B 570 21.588 -9.271 -3.934 1.00 16.03 C
ANISOU 1169 CB ASN B 570 1278 2390 2421 -271 -81 760 C
ATOM 1170 CG ASN B 570 23.083 -9.392 -4.028 1.00 20.22 C
ANISOU 1170 CG ASN B 570 1956 2900 2827 -258 -83 629 C
ATOM 1171 OD1 ASN B 570 23.636 -9.514 -5.127 1.00 18.32 O
ANISOU 1171 OD1 ASN B 570 1796 2617 2550 -309 -170 546 O
ATOM 1172 ND2 ASN B 570 23.786 -9.244 -2.913 1.00 17.06 N
ANISOU 1172 ND2 ASN B 570 1598 2534 2351 -174 12 611 N
ATOM 1173 N GLY B 571 18.987 -7.522 -5.968 1.00 20.41 N
ANISOU 1173 N GLY B 571 1615 2982 3157 -314 -275 880 N
ATOM 1174 CA GLY B 571 17.554 -7.367 -6.219 1.00 22.00 C
ANISOU 1174 CA GLY B 571 1637 3205 3517 -334 -332 1010 C
ATOM 1175 C GLY B 571 16.784 -6.603 -5.165 1.00 25.48 C
ANISOU 1175 C GLY B 571 1951 3726 4005 -213 -167 1138 C
ATOM 1176 O GLY B 571 15.575 -6.411 -5.309 1.00 27.74 O
ANISOU 1176 O GLY B 571 2062 4041 4438 -212 -191 1268 O
ATOM 1177 N ARG B 572 17.474 -6.125 -4.112 1.00 21.91 N
ANISOU 1177 N ARG B 572 1592 3308 3426 -98 -4 1103 N
ATOM 1178 CA ARG B 572 16.819 -5.440 -3.005 1.00 21.91 C
ANISOU 1178 CA ARG B 572 1518 3374 3431 51 171 1216 C
ATOM 1179 C ARG B 572 16.873 -3.932 -3.116 1.00 23.62 C
ANISOU 1179 C ARG B 572 1813 3619 3544 169 208 1162 C
ATOM 1180 O ARG B 572 17.950 -3.370 -3.310 1.00 19.75 O
ANISOU 1180 O ARG B 572 1493 3099 2914 179 184 1015 O
ATOM 1181 CB ARG B 572 17.472 -5.872 -1.696 1.00 23.09 C
ANISOU 1181 CB ARG B 572 1750 3532 3490 128 313 1211 C
ATOM 1182 CG ARG B 572 16.596 -5.662 -0.484 1.00 33.63 C
ANISOU 1182 CG ARG B 572 2994 4927 4857 279 506 1374 C
ATOM 1183 CD ARG B 572 17.085 -6.468 0.704 1.00 46.39 C
ANISOU 1183 CD ARG B 572 4676 6542 6407 335 625 1402 C
ATOM 1184 NE ARG B 572 17.350 -7.879 0.394 1.00 48.07 N
ANISOU 1184 NE ARG B 572 4850 6699 6717 177 541 1411 N
ATOM 1185 CZ ARG B 572 16.467 -8.863 0.545 1.00 60.86 C
ANISOU 1185 CZ ARG B 572 6296 8304 8526 111 575 1585 C
ATOM 1186 NH1 ARG B 572 16.802 -10.113 0.253 1.00 41.82 N
ANISOU 1186 NH1 ARG B 572 3883 5817 6190 -31 485 1573 N
ATOM 1187 NH2 ARG B 572 15.244 -8.605 0.998 1.00 49.06 N
ANISOU 1187 NH2 ARG B 572 4622 6860 7159 191 704 1781 N
ATOM 1188 N ASP B 573 15.730 -3.263 -2.913 1.00 23.36 N
ANISOU 1188 N ASP B 573 1651 3636 3588 268 281 1293 N
ATOM 1189 CA ASP B 573 15.707 -1.807 -2.929 1.00 22.71 C
ANISOU 1189 CA ASP B 573 1653 3567 3408 400 330 1253 C
ATOM 1190 C ASP B 573 16.279 -1.312 -1.612 1.00 26.17 C
ANISOU 1190 C ASP B 573 2238 4010 3695 554 489 1209 C
ATOM 1191 O ASP B 573 15.731 -1.598 -0.547 1.00 28.42 O
ANISOU 1191 O ASP B 573 2463 4337 3997 663 638 1328 O
ATOM 1192 CB ASP B 573 14.272 -1.300 -3.193 1.00 25.07 C
ANISOU 1192 CB ASP B 573 1762 3918 3845 468 351 1415 C
ATOM 1193 CG ASP B 573 14.067 0.201 -3.249 1.00 31.56 C
ANISOU 1193 CG ASP B 573 2660 4748 4584 620 407 1398 C
ATOM 1194 OD1 ASP B 573 14.998 0.937 -2.935 1.00 28.25 O
ANISOU 1194 OD1 ASP B 573 2447 4287 4001 683 443 1263 O
ATOM 1195 OD2 ASP B 573 12.922 0.634 -3.499 1.00 42.36 O
ANISOU 1195 OD2 ASP B 573 3870 6161 6064 688 423 1533 O
ATOM 1196 N ILE B 574 17.410 -0.592 -1.692 1.00 22.01 N
ANISOU 1196 N ILE B 574 1908 3432 3021 564 450 1041 N
ATOM 1197 CA ILE B 574 18.118 -0.106 -0.509 1.00 21.24 C
ANISOU 1197 CA ILE B 574 1982 3317 2772 693 543 963 C
ATOM 1198 C ILE B 574 17.866 1.349 -0.124 1.00 25.12 C
ANISOU 1198 C ILE B 574 2580 3789 3175 865 614 943 C
ATOM 1199 O ILE B 574 18.534 1.852 0.782 1.00 23.31 O
ANISOU 1199 O ILE B 574 2528 3521 2808 968 651 849 O
ATOM 1200 CB ILE B 574 19.644 -0.415 -0.625 1.00 22.00 C
ANISOU 1200 CB ILE B 574 2217 3356 2785 588 444 796 C
ATOM 1201 CG1 ILE B 574 20.261 0.100 -1.954 1.00 22.09 C
ANISOU 1201 CG1 ILE B 574 2267 3316 2811 471 317 698 C
ATOM 1202 CG2 ILE B 574 19.895 -1.907 -0.450 1.00 22.00 C
ANISOU 1202 CG2 ILE B 574 2154 3374 2832 492 430 826 C
ATOM 1203 CD1 ILE B 574 20.671 1.514 -1.959 1.00 32.70 C
ANISOU 1203 CD1 ILE B 574 3742 4602 4081 542 315 614 C
ATOM 1204 N ALA B 575 16.907 2.026 -0.781 1.00 24.66 N
ANISOU 1204 N ALA B 575 2428 3749 3193 904 620 1027 N
ATOM 1205 CA ALA B 575 16.650 3.450 -0.536 1.00 26.21 C
ANISOU 1205 CA ALA B 575 2737 3912 3311 1071 682 1007 C
ATOM 1206 C ALA B 575 16.522 3.852 0.939 1.00 29.87 C
ANISOU 1206 C ALA B 575 3330 4375 3644 1291 838 1019 C
ATOM 1207 O ALA B 575 17.016 4.911 1.322 1.00 30.40 O
ANISOU 1207 O ALA B 575 3601 4365 3586 1394 837 905 O
ATOM 1208 CB ALA B 575 15.436 3.920 -1.325 1.00 28.36 C
ANISOU 1208 CB ALA B 575 2852 4224 3699 1107 688 1138 C
ATOM 1209 N GLU B 576 15.875 3.022 1.756 1.00 26.50 N
ANISOU 1209 N GLU B 576 2801 4024 3244 1369 969 1157 N
ATOM 1210 CA GLU B 576 15.687 3.334 3.174 1.00 27.76 C
ANISOU 1210 CA GLU B 576 3101 4190 3256 1611 1140 1187 C
ATOM 1211 C GLU B 576 16.682 2.664 4.138 1.00 29.57 C
ANISOU 1211 C GLU B 576 3486 4400 3350 1616 1132 1091 C
ATOM 1212 O GLU B 576 16.557 2.817 5.355 1.00 30.63 O
ANISOU 1212 O GLU B 576 3761 4540 3336 1830 1267 1114 O
ATOM 1213 CB GLU B 576 14.238 3.030 3.592 1.00 31.75 C
ANISOU 1213 CB GLU B 576 3406 4793 3863 1757 1339 1435 C
ATOM 1214 CG GLU B 576 13.228 4.004 3.007 1.00 45.21 C
ANISOU 1214 CG GLU B 576 5012 6515 5651 1851 1380 1530 C
ATOM 1215 CD GLU B 576 11.762 3.727 3.288 1.00 71.87 C
ANISOU 1215 CD GLU B 576 8138 9993 9175 1982 1569 1799 C
ATOM 1216 OE1 GLU B 576 11.454 2.965 4.234 1.00 73.04 O
ANISOU 1216 OE1 GLU B 576 8235 10193 9323 2072 1733 1929 O
ATOM 1217 OE2 GLU B 576 10.914 4.297 2.564 1.00 68.64 O
ANISOU 1217 OE2 GLU B 576 7580 9611 8891 2005 1559 1893 O
ATOM 1218 N HIS B 577 17.659 1.922 3.612 1.00 24.63 N
ANISOU 1218 N HIS B 577 2845 3750 2762 1401 979 987 N
ATOM 1219 CA HIS B 577 18.645 1.237 4.439 1.00 23.69 C
ANISOU 1219 CA HIS B 577 2855 3616 2531 1396 952 900 C
ATOM 1220 C HIS B 577 19.824 2.112 4.828 1.00 24.04 C
ANISOU 1220 C HIS B 577 3152 3565 2418 1433 838 691 C
ATOM 1221 O HIS B 577 20.224 3.004 4.079 1.00 22.64 O
ANISOU 1221 O HIS B 577 3017 3317 2266 1358 729 587 O
ATOM 1222 CB HIS B 577 19.106 -0.057 3.768 1.00 24.33 C
ANISOU 1222 CB HIS B 577 2795 3714 2733 1169 857 905 C
ATOM 1223 CG HIS B 577 18.014 -1.074 3.652 1.00 28.26 C
ANISOU 1223 CG HIS B 577 3067 4285 3387 1135 956 1110 C
ATOM 1224 ND1 HIS B 577 17.315 -1.241 2.478 1.00 30.65 N
ANISOU 1224 ND1 HIS B 577 3170 4603 3871 996 894 1187 N
ATOM 1225 CD2 HIS B 577 17.545 -1.953 4.563 1.00 31.86 C
ANISOU 1225 CD2 HIS B 577 3470 4788 3848 1218 1100 1253 C
ATOM 1226 CE1 HIS B 577 16.442 -2.205 2.709 1.00 31.30 C
ANISOU 1226 CE1 HIS B 577 3071 4735 4086 984 985 1369 C
ATOM 1227 NE2 HIS B 577 16.542 -2.663 3.949 1.00 32.32 N
ANISOU 1227 NE2 HIS B 577 3274 4885 4122 1114 1126 1425 N
ATOM 1228 N THR B 578 20.400 1.842 6.007 1.00 21.47 N
ANISOU 1228 N THR B 578 2993 3228 1936 1548 852 633 N
ATOM 1229 CA THR B 578 21.552 2.600 6.494 1.00 21.02 C
ANISOU 1229 CA THR B 578 3176 3071 1740 1581 710 430 C
ATOM 1230 C THR B 578 22.820 2.158 5.740 1.00 20.64 C
ANISOU 1230 C THR B 578 3073 2986 1783 1337 523 312 C
ATOM 1231 O THR B 578 22.834 1.116 5.046 1.00 18.79 O
ANISOU 1231 O THR B 578 2659 2808 1673 1179 520 381 O
ATOM 1232 CB THR B 578 21.806 2.307 7.973 1.00 24.43 C
ANISOU 1232 CB THR B 578 3805 3508 1970 1780 757 406 C
ATOM 1233 OG1 THR B 578 22.177 0.926 8.089 1.00 23.50 O
ANISOU 1233 OG1 THR B 578 3585 3454 1892 1683 757 459 O
ATOM 1234 CG2 THR B 578 20.618 2.647 8.873 1.00 21.88 C
ANISOU 1234 CG2 THR B 578 3564 3225 1524 2065 977 538 C
ATOM 1235 N HIS B 579 23.897 2.929 5.908 1.00 18.72 N
ANISOU 1235 N HIS B 579 2990 2641 1483 1315 367 138 N
ATOM 1236 CA HIS B 579 25.203 2.608 5.322 1.00 16.74 C
ANISOU 1236 CA HIS B 579 2690 2350 1321 1110 201 33 C
ATOM 1237 C HIS B 579 25.633 1.197 5.726 1.00 17.34 C
ANISOU 1237 C HIS B 579 2707 2499 1383 1075 204 67 C
ATOM 1238 O HIS B 579 26.024 0.397 4.865 1.00 15.92 O
ANISOU 1238 O HIS B 579 2376 2349 1325 903 173 92 O
ATOM 1239 CB HIS B 579 26.269 3.620 5.774 1.00 17.59 C
ANISOU 1239 CB HIS B 579 2983 2330 1371 1122 30 -145 C
ATOM 1240 CG HIS B 579 27.627 3.340 5.207 1.00 18.45 C
ANISOU 1240 CG HIS B 579 3015 2400 1596 922 -128 -231 C
ATOM 1241 ND1 HIS B 579 28.013 3.843 3.974 1.00 18.36 N
ANISOU 1241 ND1 HIS B 579 2900 2336 1741 753 -174 -242 N
ATOM 1242 CD2 HIS B 579 28.648 2.612 5.720 1.00 20.07 C
ANISOU 1242 CD2 HIS B 579 3228 2614 1782 884 -232 -291 C
ATOM 1243 CE1 HIS B 579 29.241 3.382 3.760 1.00 17.64 C
ANISOU 1243 CE1 HIS B 579 2744 2229 1730 618 -287 -298 C
ATOM 1244 NE2 HIS B 579 29.663 2.635 4.783 1.00 18.34 N
ANISOU 1244 NE2 HIS B 579 2890 2355 1724 688 -333 -332 N
ATOM 1245 N ASP B 580 25.569 0.884 7.040 1.00 17.95 N
ANISOU 1245 N ASP B 580 2923 2598 1298 1253 246 70 N
ATOM 1246 CA ASP B 580 26.008 -0.440 7.473 1.00 17.03 C
ANISOU 1246 CA ASP B 580 2767 2542 1162 1233 250 108 C
ATOM 1247 C ASP B 580 25.088 -1.572 7.007 1.00 19.57 C
ANISOU 1247 C ASP B 580 2895 2952 1588 1177 404 289 C
ATOM 1248 O ASP B 580 25.587 -2.673 6.766 1.00 17.37 O
ANISOU 1248 O ASP B 580 2529 2699 1371 1067 374 309 O
ATOM 1249 CB ASP B 580 26.233 -0.447 8.994 1.00 19.97 C
ANISOU 1249 CB ASP B 580 3364 2907 1316 1451 245 64 C
ATOM 1250 CG ASP B 580 27.465 0.321 9.463 1.00 25.47 C
ANISOU 1250 CG ASP B 580 4238 3504 1934 1459 18 -137 C
ATOM 1251 OD1 ASP B 580 28.268 0.759 8.602 1.00 25.58 O
ANISOU 1251 OD1 ASP B 580 4170 3456 2091 1272 -127 -229 O
ATOM 1252 OD2 ASP B 580 27.677 0.411 10.697 1.00 29.12 O
ANISOU 1252 OD2 ASP B 580 4918 3948 2199 1649 -23 -195 O
ATOM 1253 N GLN B 581 23.769 -1.308 6.816 1.00 19.70 N
ANISOU 1253 N GLN B 581 2835 3006 1646 1243 554 422 N
ATOM 1254 CA GLN B 581 22.892 -2.357 6.257 1.00 18.61 C
ANISOU 1254 CA GLN B 581 2484 2935 1654 1156 663 594 C
ATOM 1255 C GLN B 581 23.303 -2.608 4.808 1.00 19.92 C
ANISOU 1255 C GLN B 581 2510 3079 1981 918 542 549 C
ATOM 1256 O GLN B 581 23.331 -3.753 4.372 1.00 19.24 O
ANISOU 1256 O GLN B 581 2308 3012 1989 799 536 608 O
ATOM 1257 CB GLN B 581 21.418 -1.951 6.316 1.00 21.32 C
ANISOU 1257 CB GLN B 581 2745 3321 2036 1272 831 753 C
ATOM 1258 CG GLN B 581 20.892 -2.008 7.744 1.00 20.76 C
ANISOU 1258 CG GLN B 581 2793 3285 1809 1526 1004 848 C
ATOM 1259 CD GLN B 581 19.478 -1.501 7.840 1.00 30.43 C
ANISOU 1259 CD GLN B 581 3933 4555 3076 1668 1190 1016 C
ATOM 1260 OE1 GLN B 581 19.092 -0.510 7.212 1.00 25.12 O
ANISOU 1260 OE1 GLN B 581 3234 3861 2448 1664 1165 989 O
ATOM 1261 NE2 GLN B 581 18.673 -2.171 8.644 1.00 34.67 N
ANISOU 1261 NE2 GLN B 581 4417 5152 3603 1807 1393 1208 N
ATOM 1262 N VAL B 582 23.602 -1.530 4.052 1.00 16.25 N
ANISOU 1262 N VAL B 582 2070 2562 1541 860 452 451 N
ATOM 1263 CA VAL B 582 24.074 -1.661 2.670 1.00 14.62 C
ANISOU 1263 CA VAL B 582 1766 2332 1458 663 349 408 C
ATOM 1264 C VAL B 582 25.358 -2.506 2.616 1.00 14.70 C
ANISOU 1264 C VAL B 582 1790 2326 1469 563 256 327 C
ATOM 1265 O VAL B 582 25.495 -3.390 1.768 1.00 14.58 O
ANISOU 1265 O VAL B 582 1677 2320 1543 434 230 355 O
ATOM 1266 CB VAL B 582 24.278 -0.255 2.059 1.00 17.75 C
ANISOU 1266 CB VAL B 582 2218 2665 1861 650 287 323 C
ATOM 1267 CG1 VAL B 582 25.182 -0.274 0.812 1.00 17.31 C
ANISOU 1267 CG1 VAL B 582 2115 2568 1892 474 181 254 C
ATOM 1268 CG2 VAL B 582 22.915 0.415 1.759 1.00 18.73 C
ANISOU 1268 CG2 VAL B 582 2284 2812 2019 725 377 427 C
ATOM 1269 N VAL B 583 26.312 -2.213 3.504 1.00 13.61 N
ANISOU 1269 N VAL B 583 1782 2158 1232 630 193 223 N
ATOM 1270 CA VAL B 583 27.577 -2.959 3.557 1.00 12.61 C
ANISOU 1270 CA VAL B 583 1660 2020 1110 555 101 153 C
ATOM 1271 C VAL B 583 27.264 -4.440 3.814 1.00 15.15 C
ANISOU 1271 C VAL B 583 1920 2396 1440 554 173 255 C
ATOM 1272 O VAL B 583 27.786 -5.303 3.097 1.00 14.10 O
ANISOU 1272 O VAL B 583 1714 2260 1383 437 137 255 O
ATOM 1273 CB VAL B 583 28.512 -2.379 4.638 1.00 15.29 C
ANISOU 1273 CB VAL B 583 2149 2319 1341 649 2 35 C
ATOM 1274 CG1 VAL B 583 29.640 -3.347 5.001 1.00 15.08 C
ANISOU 1274 CG1 VAL B 583 2119 2304 1305 618 -76 -5 C
ATOM 1275 CG2 VAL B 583 29.068 -1.039 4.186 1.00 15.01 C
ANISOU 1275 CG2 VAL B 583 2153 2200 1349 596 -101 -72 C
ATOM 1276 N LEU B 584 26.371 -4.722 4.781 1.00 14.66 N
ANISOU 1276 N LEU B 584 1891 2374 1306 691 289 353 N
ATOM 1277 CA LEU B 584 25.997 -6.114 5.061 1.00 15.08 C
ANISOU 1277 CA LEU B 584 1881 2462 1387 687 371 472 C
ATOM 1278 C LEU B 584 25.313 -6.805 3.845 1.00 18.03 C
ANISOU 1278 C LEU B 584 2090 2834 1928 531 388 560 C
ATOM 1279 O LEU B 584 25.672 -7.939 3.525 1.00 16.79 O
ANISOU 1279 O LEU B 584 1891 2663 1826 443 363 578 O
ATOM 1280 CB LEU B 584 25.196 -6.273 6.361 1.00 17.35 C
ANISOU 1280 CB LEU B 584 2234 2789 1569 877 516 584 C
ATOM 1281 CG LEU B 584 24.860 -7.714 6.715 1.00 20.70 C
ANISOU 1281 CG LEU B 584 2596 3235 2035 873 612 724 C
ATOM 1282 CD1 LEU B 584 26.145 -8.567 6.951 1.00 20.47 C
ANISOU 1282 CD1 LEU B 584 2632 3188 1959 841 514 643 C
ATOM 1283 CD2 LEU B 584 23.905 -7.771 7.851 1.00 25.19 C
ANISOU 1283 CD2 LEU B 584 3205 3845 2523 1064 793 872 C
ATOM 1284 N PHE B 585 24.415 -6.117 3.135 1.00 16.61 N
ANISOU 1284 N PHE B 585 1832 2658 1822 499 408 601 N
ATOM 1285 CA PHE B 585 23.795 -6.712 1.943 1.00 16.62 C
ANISOU 1285 CA PHE B 585 1694 2647 1972 353 380 666 C
ATOM 1286 C PHE B 585 24.867 -7.086 0.927 1.00 15.75 C
ANISOU 1286 C PHE B 585 1603 2494 1886 221 259 557 C
ATOM 1287 O PHE B 585 24.778 -8.154 0.338 1.00 15.36 O
ANISOU 1287 O PHE B 585 1501 2421 1914 124 229 593 O
ATOM 1288 CB PHE B 585 22.807 -5.745 1.296 1.00 18.35 C
ANISOU 1288 CB PHE B 585 1842 2878 2252 353 390 708 C
ATOM 1289 CG PHE B 585 21.507 -5.550 2.037 1.00 22.79 C
ANISOU 1289 CG PHE B 585 2334 3487 2839 473 528 860 C
ATOM 1290 CD1 PHE B 585 20.790 -6.642 2.517 1.00 28.76 C
ANISOU 1290 CD1 PHE B 585 2988 4262 3678 475 618 1013 C
ATOM 1291 CD2 PHE B 585 20.956 -4.282 2.177 1.00 26.30 C
ANISOU 1291 CD2 PHE B 585 2801 3949 3244 584 577 866 C
ATOM 1292 CE1 PHE B 585 19.587 -6.459 3.204 1.00 32.52 C
ANISOU 1292 CE1 PHE B 585 3377 4785 4196 597 773 1182 C
ATOM 1293 CE2 PHE B 585 19.745 -4.100 2.850 1.00 32.76 C
ANISOU 1293 CE2 PHE B 585 3546 4815 4088 718 728 1023 C
ATOM 1294 CZ PHE B 585 19.074 -5.187 3.363 1.00 32.59 C
ANISOU 1294 CZ PHE B 585 3410 4822 4150 726 833 1187 C
ATOM 1295 N ILE B 586 25.916 -6.259 0.762 1.00 12.11 N
ANISOU 1295 N ILE B 586 1222 2014 1364 223 194 431 N
ATOM 1296 CA ILE B 586 26.989 -6.612 -0.150 1.00 10.71 C
ANISOU 1296 CA ILE B 586 1054 1802 1212 122 113 350 C
ATOM 1297 C ILE B 586 27.740 -7.836 0.353 1.00 15.38 C
ANISOU 1297 C ILE B 586 1669 2391 1783 123 108 346 C
ATOM 1298 O ILE B 586 28.008 -8.766 -0.427 1.00 14.26 O
ANISOU 1298 O ILE B 586 1507 2221 1689 42 80 349 O
ATOM 1299 CB ILE B 586 27.891 -5.406 -0.460 1.00 12.32 C
ANISOU 1299 CB ILE B 586 1308 1981 1394 117 59 247 C
ATOM 1300 CG1 ILE B 586 27.068 -4.321 -1.217 1.00 12.85 C
ANISOU 1300 CG1 ILE B 586 1353 2038 1492 105 66 266 C
ATOM 1301 CG2 ILE B 586 29.114 -5.830 -1.307 1.00 12.26 C
ANISOU 1301 CG2 ILE B 586 1297 1944 1418 34 6 188 C
ATOM 1302 CD1 ILE B 586 27.688 -2.944 -1.142 1.00 13.10 C
ANISOU 1302 CD1 ILE B 586 1446 2030 1501 130 34 185 C
ATOM 1303 N LYS B 587 28.052 -7.859 1.661 1.00 14.57 N
ANISOU 1303 N LYS B 587 1627 2313 1598 231 134 341 N
ATOM 1304 CA LYS B 587 28.772 -9.007 2.245 1.00 15.09 C
ANISOU 1304 CA LYS B 587 1722 2378 1633 254 130 345 C
ATOM 1305 C LYS B 587 27.967 -10.315 2.261 1.00 16.39 C
ANISOU 1305 C LYS B 587 1841 2533 1853 227 196 464 C
ATOM 1306 O LYS B 587 28.579 -11.405 2.314 1.00 17.38 O
ANISOU 1306 O LYS B 587 1985 2635 1983 211 183 467 O
ATOM 1307 CB LYS B 587 29.352 -8.626 3.638 1.00 19.73 C
ANISOU 1307 CB LYS B 587 2408 2989 2099 391 116 301 C
ATOM 1308 CG LYS B 587 30.677 -7.905 3.391 1.00 27.50 C
ANISOU 1308 CG LYS B 587 3412 3951 3084 360 -3 171 C
ATOM 1309 CD LYS B 587 31.304 -7.186 4.551 1.00 37.63 C
ANISOU 1309 CD LYS B 587 4796 5235 4266 470 -79 92 C
ATOM 1310 CE LYS B 587 32.415 -6.284 4.057 1.00 28.15 C
ANISOU 1310 CE LYS B 587 3571 3993 3129 397 -201 -17 C
ATOM 1311 NZ LYS B 587 33.549 -7.025 3.420 1.00 26.86 N
ANISOU 1311 NZ LYS B 587 3325 3828 3054 315 -244 -31 N
ATOM 1312 N ALA B 588 26.626 -10.233 2.166 1.00 16.20 N
ANISOU 1312 N ALA B 588 1748 2517 1892 216 261 568 N
ATOM 1313 CA ALA B 588 25.729 -11.387 2.110 1.00 15.87 C
ANISOU 1313 CA ALA B 588 1633 2449 1950 165 312 699 C
ATOM 1314 C ALA B 588 25.530 -11.927 0.703 1.00 19.02 C
ANISOU 1314 C ALA B 588 1977 2787 2462 13 224 685 C
ATOM 1315 O ALA B 588 24.734 -12.851 0.502 1.00 20.21 O
ANISOU 1315 O ALA B 588 2062 2893 2726 -57 228 784 O
ATOM 1316 CB ALA B 588 24.369 -11.006 2.695 1.00 17.95 C
ANISOU 1316 CB ALA B 588 1820 2749 2253 230 423 836 C
ATOM 1317 N SER B 589 26.259 -11.381 -0.283 1.00 15.95 N
ANISOU 1317 N SER B 589 1626 2386 2047 -36 139 567 N
ATOM 1318 CA SER B 589 26.056 -11.787 -1.691 1.00 15.09 C
ANISOU 1318 CA SER B 589 1504 2219 2010 -153 50 545 C
ATOM 1319 C SER B 589 26.204 -13.255 -1.994 1.00 19.73 C
ANISOU 1319 C SER B 589 2121 2729 2644 -215 13 562 C
ATOM 1320 O SER B 589 25.572 -13.734 -2.935 1.00 19.86 O
ANISOU 1320 O SER B 589 2123 2682 2741 -308 -67 577 O
ATOM 1321 CB SER B 589 27.005 -11.030 -2.612 1.00 15.94 C
ANISOU 1321 CB SER B 589 1672 2327 2058 -164 -2 428 C
ATOM 1322 OG SER B 589 26.709 -9.650 -2.551 1.00 15.68 O
ANISOU 1322 OG SER B 589 1614 2338 2004 -127 14 416 O
ATOM 1323 N CYS B 590 27.075 -13.960 -1.282 1.00 15.86 N
ANISOU 1323 N CYS B 590 1690 2233 2104 -162 51 549 N
ATOM 1324 CA CYS B 590 27.326 -15.373 -1.514 1.00 17.26 C
ANISOU 1324 CA CYS B 590 1918 2324 2317 -203 23 562 C
ATOM 1325 C CYS B 590 26.450 -16.315 -0.702 1.00 22.90 C
ANISOU 1325 C CYS B 590 2583 2999 3121 -217 76 698 C
ATOM 1326 O CYS B 590 26.670 -17.526 -0.750 1.00 25.94 O
ANISOU 1326 O CYS B 590 3019 3297 3540 -246 59 717 O
ATOM 1327 CB CYS B 590 28.802 -15.677 -1.331 1.00 16.10 C
ANISOU 1327 CB CYS B 590 1857 2183 2077 -133 32 482 C
ATOM 1328 SG CYS B 590 29.863 -14.758 -2.472 1.00 18.35 S
ANISOU 1328 SG CYS B 590 2180 2491 2301 -132 -13 355 S
ATOM 1329 N GLU B 591 25.430 -15.785 -0.002 1.00 18.97 N
ANISOU 1329 N GLU B 591 1985 2553 2669 -192 149 805 N
ATOM 1330 CA GLU B 591 24.481 -16.639 0.737 1.00 21.53 C
ANISOU 1330 CA GLU B 591 2234 2839 3108 -206 226 971 C
ATOM 1331 C GLU B 591 23.617 -17.416 -0.256 1.00 52.76 C
ANISOU 1331 C GLU B 591 6125 6681 7241 -367 118 1017 C
ATOM 1332 O GLU B 591 23.384 -16.921 -1.356 1.00 27.72 O
ANISOU 1332 O GLU B 591 2942 3499 4092 -440 3 943 O
ATOM 1333 CB GLU B 591 23.561 -15.786 1.623 1.00 22.99 C
ANISOU 1333 CB GLU B 591 2321 3113 3302 -122 348 1087 C
ATOM 1334 CG GLU B 591 24.213 -15.080 2.802 1.00 25.15 C
ANISOU 1334 CG GLU B 591 2678 3479 3397 53 448 1058 C
ATOM 1335 CD GLU B 591 24.689 -15.883 4.000 1.00 41.23 C
ANISOU 1335 CD GLU B 591 4795 5515 5356 163 543 1121 C
ATOM 1336 OE1 GLU B 591 25.330 -15.269 4.879 1.00 32.14 O
ANISOU 1336 OE1 GLU B 591 3738 4433 4039 309 582 1069 O
ATOM 1337 OE2 GLU B 591 24.474 -17.114 4.051 1.00 31.20 O
ANISOU 1337 OE2 GLU B 591 3508 4165 4183 106 564 1215 O
ATOM 1338 N SER B 594 24.265 -18.256 -3.943 1.00 27.66 N
ANISOU 1338 N SER B 594 3177 3266 4066 -603 -307 712 N
ATOM 1339 CA SER B 594 24.708 -17.325 -4.966 1.00 26.42 C
ANISOU 1339 CA SER B 594 3087 3154 3798 -579 -368 590 C
ATOM 1340 C SER B 594 26.222 -17.166 -4.923 1.00 29.37 C
ANISOU 1340 C SER B 594 3581 3570 4010 -474 -297 487 C
ATOM 1341 O SER B 594 26.827 -17.266 -3.864 1.00 28.84 O
ANISOU 1341 O SER B 594 3502 3552 3904 -398 -190 514 O
ATOM 1342 CB SER B 594 24.037 -15.970 -4.755 1.00 28.22 C
ANISOU 1342 CB SER B 594 3187 3497 4038 -557 -326 633 C
ATOM 1343 OG SER B 594 24.734 -14.920 -5.412 1.00 31.53 O
ANISOU 1343 OG SER B 594 3673 3976 4329 -503 -329 527 O
ATOM 1344 N GLY B 595 26.826 -16.959 -6.079 1.00 24.90 N
ANISOU 1344 N GLY B 595 3128 2979 3354 -461 -358 381 N
ATOM 1345 CA GLY B 595 28.268 -16.763 -6.140 1.00 23.54 C
ANISOU 1345 CA GLY B 595 3040 2848 3058 -362 -283 304 C
ATOM 1346 C GLY B 595 28.595 -15.391 -6.670 1.00 23.89 C
ANISOU 1346 C GLY B 595 3066 2975 3034 -328 -260 258 C
ATOM 1347 O GLY B 595 29.719 -15.151 -7.110 1.00 23.19 O
ANISOU 1347 O GLY B 595 3043 2904 2863 -262 -214 199 O
ATOM 1348 N GLU B 596 27.590 -14.518 -6.734 1.00 19.38 N
ANISOU 1348 N GLU B 596 2407 2445 2511 -371 -291 294 N
ATOM 1349 CA GLU B 596 27.801 -13.198 -7.304 1.00 18.95 C
ANISOU 1349 CA GLU B 596 2347 2452 2401 -341 -274 257 C
ATOM 1350 C GLU B 596 27.032 -12.101 -6.636 1.00 20.47 C
ANISOU 1350 C GLU B 596 2416 2722 2639 -341 -242 311 C
ATOM 1351 O GLU B 596 25.994 -12.313 -5.996 1.00 21.63 O
ANISOU 1351 O GLU B 596 2472 2876 2873 -373 -249 392 O
ATOM 1352 CB GLU B 596 27.595 -13.182 -8.844 1.00 22.62 C
ANISOU 1352 CB GLU B 596 2923 2857 2815 -360 -371 209 C
ATOM 1353 CG GLU B 596 26.163 -13.169 -9.328 1.00 33.26 C
ANISOU 1353 CG GLU B 596 4230 4170 4235 -438 -501 246 C
ATOM 1354 CD GLU B 596 25.991 -13.498 -10.804 1.00 52.35 C
ANISOU 1354 CD GLU B 596 6803 6503 6586 -448 -636 184 C
ATOM 1355 OE1 GLU B 596 24.981 -14.154 -11.142 1.00 53.81 O
ANISOU 1355 OE1 GLU B 596 6986 6610 6848 -529 -789 200 O
ATOM 1356 OE2 GLU B 596 26.874 -13.134 -11.617 1.00 38.49 O
ANISOU 1356 OE2 GLU B 596 5173 4750 4701 -371 -592 125 O
ATOM 1357 N LEU B 597 27.565 -10.907 -6.804 1.00 16.01 N
ANISOU 1357 N LEU B 597 1853 2209 2022 -298 -198 276 N
ATOM 1358 CA LEU B 597 26.936 -9.669 -6.392 1.00 13.85 C
ANISOU 1358 CA LEU B 597 1499 1993 1768 -280 -171 308 C
ATOM 1359 C LEU B 597 26.279 -9.074 -7.612 1.00 15.34 C
ANISOU 1359 C LEU B 597 1708 2166 1954 -306 -240 307 C
ATOM 1360 O LEU B 597 26.909 -8.978 -8.673 1.00 14.50 O
ANISOU 1360 O LEU B 597 1697 2029 1782 -298 -258 256 O
ATOM 1361 CB LEU B 597 27.981 -8.695 -5.836 1.00 12.16 C
ANISOU 1361 CB LEU B 597 1289 1820 1510 -221 -99 264 C
ATOM 1362 CG LEU B 597 27.532 -7.218 -5.663 1.00 13.08 C
ANISOU 1362 CG LEU B 597 1369 1972 1629 -192 -78 273 C
ATOM 1363 CD1 LEU B 597 26.470 -7.057 -4.558 1.00 13.85 C
ANISOU 1363 CD1 LEU B 597 1397 2108 1758 -156 -48 340 C
ATOM 1364 CD2 LEU B 597 28.730 -6.336 -5.390 1.00 12.74 C
ANISOU 1364 CD2 LEU B 597 1349 1932 1561 -160 -43 215 C
ATOM 1365 N MET B 598 25.016 -8.667 -7.462 1.00 13.41 N
ANISOU 1365 N MET B 598 1374 1946 1777 -322 -271 374 N
ATOM 1366 CA MET B 598 24.300 -7.980 -8.522 1.00 14.68 C
ANISOU 1366 CA MET B 598 1541 2101 1937 -333 -346 383 C
ATOM 1367 C MET B 598 23.992 -6.564 -8.011 1.00 17.47 C
ANISOU 1367 C MET B 598 1832 2513 2293 -273 -274 413 C
ATOM 1368 O MET B 598 23.513 -6.398 -6.889 1.00 20.90 O
ANISOU 1368 O MET B 598 2179 2987 2773 -241 -209 468 O
ATOM 1369 CB MET B 598 23.005 -8.732 -8.910 1.00 18.63 C
ANISOU 1369 CB MET B 598 1975 2567 2535 -404 -474 444 C
ATOM 1370 N LEU B 599 24.385 -5.543 -8.763 1.00 13.45 N
ANISOU 1370 N LEU B 599 1388 2000 1722 -242 -266 377 N
ATOM 1371 CA LEU B 599 24.037 -4.181 -8.403 1.00 13.01 C
ANISOU 1371 CA LEU B 599 1296 1976 1672 -185 -211 403 C
ATOM 1372 C LEU B 599 23.249 -3.592 -9.530 1.00 16.12 C
ANISOU 1372 C LEU B 599 1700 2363 2061 -179 -285 433 C
ATOM 1373 O LEU B 599 23.595 -3.802 -10.700 1.00 17.94 O
ANISOU 1373 O LEU B 599 2027 2558 2232 -196 -344 399 O
ATOM 1374 CB LEU B 599 25.295 -3.282 -8.241 1.00 12.11 C
ANISOU 1374 CB LEU B 599 1250 1846 1506 -151 -134 341 C
ATOM 1375 CG LEU B 599 26.240 -3.662 -7.123 1.00 13.90 C
ANISOU 1375 CG LEU B 599 1474 2078 1729 -145 -81 300 C
ATOM 1376 CD1 LEU B 599 27.538 -2.860 -7.252 1.00 14.27 C
ANISOU 1376 CD1 LEU B 599 1571 2092 1758 -139 -42 244 C
ATOM 1377 CD2 LEU B 599 25.611 -3.388 -5.766 1.00 15.81 C
ANISOU 1377 CD2 LEU B 599 1661 2355 1989 -89 -41 331 C
ATOM 1378 N LEU B 600 22.195 -2.844 -9.197 1.00 13.16 N
ANISOU 1378 N LEU B 600 1238 2023 1738 -136 -278 501 N
ATOM 1379 CA LEU B 600 21.495 -2.063 -10.219 1.00 13.45 C
ANISOU 1379 CA LEU B 600 1287 2058 1765 -109 -344 534 C
ATOM 1380 C LEU B 600 21.889 -0.613 -9.913 1.00 15.66 C
ANISOU 1380 C LEU B 600 1611 2333 2008 -32 -241 522 C
ATOM 1381 O LEU B 600 21.678 -0.156 -8.788 1.00 14.75 O
ANISOU 1381 O LEU B 600 1444 2239 1921 19 -161 542 O
ATOM 1382 CB LEU B 600 19.982 -2.250 -10.158 1.00 15.07 C
ANISOU 1382 CB LEU B 600 1347 2301 2078 -111 -420 633 C
ATOM 1383 CG LEU B 600 19.188 -1.490 -11.234 1.00 17.68 C
ANISOU 1383 CG LEU B 600 1680 2634 2402 -74 -515 673 C
ATOM 1384 CD1 LEU B 600 19.479 -2.047 -12.649 1.00 16.56 C
ANISOU 1384 CD1 LEU B 600 1667 2443 2181 -120 -659 617 C
ATOM 1385 CD2 LEU B 600 17.703 -1.526 -10.935 1.00 19.48 C
ANISOU 1385 CD2 LEU B 600 1720 2912 2771 -62 -568 792 C
ATOM 1386 N VAL B 601 22.478 0.068 -10.891 1.00 13.90 N
ANISOU 1386 N VAL B 601 1496 2069 1716 -19 -241 494 N
ATOM 1387 CA VAL B 601 22.972 1.424 -10.661 1.00 13.75 C
ANISOU 1387 CA VAL B 601 1528 2017 1681 36 -151 482 C
ATOM 1388 C VAL B 601 22.462 2.416 -11.645 1.00 17.10 C
ANISOU 1388 C VAL B 601 2000 2420 2076 90 -173 528 C
ATOM 1389 O VAL B 601 22.097 2.072 -12.782 1.00 16.89 O
ANISOU 1389 O VAL B 601 2012 2398 2008 86 -260 549 O
ATOM 1390 CB VAL B 601 24.529 1.462 -10.635 1.00 15.91 C
ANISOU 1390 CB VAL B 601 1878 2240 1928 -1 -85 415 C
ATOM 1391 CG1 VAL B 601 25.098 0.471 -9.613 1.00 14.68 C
ANISOU 1391 CG1 VAL B 601 1679 2106 1795 -43 -72 370 C
ATOM 1392 CG2 VAL B 601 25.125 1.224 -12.021 1.00 16.27 C
ANISOU 1392 CG2 VAL B 601 2017 2255 1909 -17 -97 414 C
ATOM 1393 N ARG B 602 22.520 3.687 -11.224 1.00 16.82 N
ANISOU 1393 N ARG B 602 1989 2349 2052 150 -99 535 N
ATOM 1394 CA ARG B 602 22.252 4.848 -12.053 1.00 17.19 C
ANISOU 1394 CA ARG B 602 2104 2355 2072 213 -91 579 C
ATOM 1395 C ARG B 602 23.630 5.415 -12.373 1.00 19.63 C
ANISOU 1395 C ARG B 602 2515 2579 2364 182 -13 543 C
ATOM 1396 O ARG B 602 24.317 5.872 -11.458 1.00 18.11 O
ANISOU 1396 O ARG B 602 2324 2340 2217 166 44 498 O
ATOM 1397 CB ARG B 602 21.389 5.864 -11.300 1.00 17.82 C
ANISOU 1397 CB ARG B 602 2147 2434 2191 306 -53 619 C
ATOM 1398 CG ARG B 602 21.232 7.216 -12.006 1.00 33.13 C
ANISOU 1398 CG ARG B 602 4173 4309 4107 382 -27 662 C
ATOM 1399 CD ARG B 602 20.030 7.293 -12.922 1.00 47.04 C
ANISOU 1399 CD ARG B 602 5901 6121 5852 446 -109 747 C
ATOM 1400 NE ARG B 602 19.913 8.629 -13.514 1.00 61.06 N
ANISOU 1400 NE ARG B 602 7771 7828 7601 534 -72 794 N
ATOM 1401 CZ ARG B 602 18.933 9.012 -14.324 1.00 79.08 C
ANISOU 1401 CZ ARG B 602 10048 10138 9861 617 -138 875 C
ATOM 1402 NH1 ARG B 602 17.963 8.166 -14.651 1.00 64.22 N
ANISOU 1402 NH1 ARG B 602 8056 8349 7996 614 -264 915 N
ATOM 1403 NH2 ARG B 602 18.912 10.245 -14.810 1.00 72.80 N
ANISOU 1403 NH2 ARG B 602 9354 9270 9038 703 -90 920 N
ATOM 1404 N PRO B 603 24.107 5.345 -13.635 1.00 22.02 N
ANISOU 1404 N PRO B 603 2904 2857 2607 176 -11 565 N
ATOM 1405 CA PRO B 603 25.452 5.884 -13.939 1.00 24.64 C
ANISOU 1405 CA PRO B 603 3304 3107 2951 147 91 561 C
ATOM 1406 C PRO B 603 25.547 7.386 -13.682 1.00 33.14 C
ANISOU 1406 C PRO B 603 4415 4093 4085 180 153 587 C
ATOM 1407 O PRO B 603 24.544 8.084 -13.795 1.00 33.22 O
ANISOU 1407 O PRO B 603 4440 4103 4078 255 128 628 O
ATOM 1408 CB PRO B 603 25.640 5.572 -15.432 1.00 27.44 C
ANISOU 1408 CB PRO B 603 3761 3461 3205 178 94 607 C
ATOM 1409 CG PRO B 603 24.615 4.560 -15.758 1.00 31.81 C
ANISOU 1409 CG PRO B 603 4300 4091 3694 192 -39 597 C
ATOM 1410 CD PRO B 603 23.451 4.830 -14.850 1.00 25.82 C
ANISOU 1410 CD PRO B 603 3431 3375 3004 206 -100 603 C
ATOM 1411 N ASN B 604 26.742 7.881 -13.293 1.00 34.22 N
ANISOU 1411 N ASN B 604 4555 4144 4303 122 224 565 N
ATOM 1412 CA ASN B 604 26.953 9.305 -13.000 1.00 65.02 C
ANISOU 1412 CA ASN B 604 8499 7925 8280 134 267 579 C
ATOM 1413 C ASN B 604 26.979 10.178 -14.245 1.00 92.63 C
ANISOU 1413 C ASN B 604 12087 11352 11756 180 337 679 C
ATOM 1414 O ASN B 604 26.535 11.322 -14.187 1.00 58.08 O
ANISOU 1414 O ASN B 604 7765 6897 7405 232 350 709 O
ATOM 1415 CB ASN B 604 28.207 9.528 -12.146 1.00 65.26 C
ANISOU 1415 CB ASN B 604 8493 7871 8431 41 285 522 C
ATOM 1416 CG ASN B 604 29.442 8.808 -12.631 1.00 78.97 C
ANISOU 1416 CG ASN B 604 10184 9616 10206 -35 337 539 C
ATOM 1417 OD1 ASN B 604 29.458 7.578 -12.791 1.00 68.46 O
ANISOU 1417 OD1 ASN B 604 8818 8385 8807 -40 321 522 O
ATOM 1418 ND2 ASN B 604 30.521 9.555 -12.819 1.00 68.61 N
ANISOU 1418 ND2 ASN B 604 8863 8189 9018 -95 403 580 N
TER 1419 ASN B 604
ATOM 1420 N SER C 1 24.947 -6.077 16.597 1.00 11.11 N
ANISOU 1420 N SER C 1 1260 1445 1518 47 -101 61 N
ATOM 1421 CA SER C 1 25.278 -5.205 15.460 1.00 10.97 C
ANISOU 1421 CA SER C 1 1271 1431 1464 103 -79 123 C
ATOM 1422 C SER C 1 25.254 -6.046 14.207 1.00 12.11 C
ANISOU 1422 C SER C 1 1469 1629 1503 136 -143 119 C
ATOM 1423 O SER C 1 25.083 -7.273 14.299 1.00 12.43 O
ANISOU 1423 O SER C 1 1518 1686 1519 99 -197 57 O
ATOM 1424 CB SER C 1 26.643 -4.546 15.647 1.00 12.76 C
ANISOU 1424 CB SER C 1 1513 1613 1723 94 11 134 C
ATOM 1425 OG SER C 1 26.659 -3.914 16.921 1.00 13.43 O
ANISOU 1425 OG SER C 1 1561 1651 1891 51 45 102 O
ATOM 1426 N TRP C 2 25.340 -5.376 13.025 1.00 12.70 N
ANISOU 1426 N TRP C 2 1596 1722 1509 211 -131 187 N
ATOM 1427 CA TRP C 2 25.342 -6.098 11.757 1.00 13.61 C
ANISOU 1427 CA TRP C 2 1797 1890 1484 257 -192 177 C
ATOM 1428 C TRP C 2 24.118 -7.007 11.639 1.00 15.31 C
ANISOU 1428 C TRP C 2 1980 2159 1679 228 -339 107 C
ATOM 1429 O TRP C 2 24.220 -8.139 11.184 1.00 16.59 O
ANISOU 1429 O TRP C 2 2199 2338 1768 205 -393 33 O
ATOM 1430 CB TRP C 2 26.671 -6.884 11.580 1.00 13.31 C
ANISOU 1430 CB TRP C 2 1827 1827 1404 245 -120 147 C
ATOM 1431 CG TRP C 2 27.889 -5.997 11.582 1.00 12.07 C
ANISOU 1431 CG TRP C 2 1674 1616 1297 268 23 215 C
ATOM 1432 CD1 TRP C 2 28.900 -5.986 12.500 1.00 12.56 C
ANISOU 1432 CD1 TRP C 2 1675 1632 1466 213 94 196 C
ATOM 1433 CD2 TRP C 2 28.185 -4.958 10.642 1.00 12.59 C
ANISOU 1433 CD2 TRP C 2 1796 1664 1325 350 112 314 C
ATOM 1434 NE1 TRP C 2 29.805 -4.996 12.192 1.00 13.76 N
ANISOU 1434 NE1 TRP C 2 1821 1732 1676 238 217 264 N
ATOM 1435 CE2 TRP C 2 29.409 -4.370 11.032 1.00 15.01 C
ANISOU 1435 CE2 TRP C 2 2059 1896 1747 325 250 345 C
ATOM 1436 CE3 TRP C 2 27.569 -4.511 9.466 1.00 14.44 C
ANISOU 1436 CE3 TRP C 2 2118 1938 1432 452 89 384 C
ATOM 1437 CZ2 TRP C 2 29.989 -3.310 10.333 1.00 15.92 C
ANISOU 1437 CZ2 TRP C 2 2209 1954 1886 385 393 447 C
ATOM 1438 CZ3 TRP C 2 28.162 -3.487 8.745 1.00 17.20 C
ANISOU 1438 CZ3 TRP C 2 2527 2240 1769 535 231 500 C
ATOM 1439 CH2 TRP C 2 29.360 -2.893 9.177 1.00 17.37 C
ANISOU 1439 CH2 TRP C 2 2499 2166 1935 496 396 532 C
ATOM 1440 N GLU C 3 22.950 -6.500 12.058 1.00 15.36 N
ANISOU 1440 N GLU C 3 1887 2180 1771 225 -394 127 N
ATOM 1441 CA GLU C 3 21.674 -7.226 11.990 1.00 17.28 C
ANISOU 1441 CA GLU C 3 2053 2467 2046 188 -532 67 C
ATOM 1442 C GLU C 3 21.601 -8.485 12.844 1.00 18.76 C
ANISOU 1442 C GLU C 3 2206 2613 2310 84 -530 -28 C
ATOM 1443 O GLU C 3 20.785 -9.369 12.600 1.00 21.97 O
ANISOU 1443 O GLU C 3 2569 3039 2741 36 -634 -102 O
ATOM 1444 CB GLU C 3 21.181 -7.456 10.545 1.00 20.61 C
ANISOU 1444 CB GLU C 3 2529 2977 2326 248 -681 52 C
ATOM 1445 CG GLU C 3 21.028 -6.171 9.738 1.00 25.89 C
ANISOU 1445 CG GLU C 3 3229 3690 2917 377 -685 173 C
ATOM 1446 CD GLU C 3 19.791 -5.344 10.019 1.00 53.14 C
ANISOU 1446 CD GLU C 3 6539 7169 6483 415 -742 240 C
ATOM 1447 OE1 GLU C 3 18.832 -5.435 9.219 1.00 54.44 O
ANISOU 1447 OE1 GLU C 3 6663 7427 6597 465 -913 238 O
ATOM 1448 OE2 GLU C 3 19.800 -4.561 10.996 1.00 47.22 O
ANISOU 1448 OE2 GLU C 3 5724 6348 5868 406 -616 296 O
ATOM 1449 N SER C 4 22.446 -8.543 13.877 1.00 14.03 N
ANISOU 1449 N SER C 4 1622 1952 1758 51 -410 -26 N
ATOM 1450 CA ASER C 4 22.433 -9.631 14.843 0.50 13.27 C
ANISOU 1450 CA ASER C 4 1505 1807 1731 -23 -378 -86 C
ATOM 1451 CA BSER C 4 22.497 -9.631 14.846 0.50 13.14 C
ANISOU 1451 CA BSER C 4 1492 1789 1711 -22 -375 -85 C
ATOM 1452 C SER C 4 22.243 -9.005 16.220 1.00 13.94 C
ANISOU 1452 C SER C 4 1531 1849 1916 -34 -291 -49 C
ATOM 1453 O SER C 4 22.721 -7.891 16.488 1.00 14.66 O
ANISOU 1453 O SER C 4 1633 1933 2004 1 -234 1 O
ATOM 1454 CB ASER C 4 23.699 -10.473 14.762 0.50 14.97 C
ANISOU 1454 CB ASER C 4 1816 1996 1874 -28 -328 -117 C
ATOM 1455 CB BSER C 4 23.859 -10.309 14.806 0.50 15.02 C
ANISOU 1455 CB BSER C 4 1826 2002 1877 -21 -315 -107 C
ATOM 1456 OG ASER C 4 23.547 -11.520 13.808 0.50 14.46 O
ANISOU 1456 OG ASER C 4 1809 1940 1746 -44 -397 -188 O
ATOM 1457 OG BSER C 4 24.191 -10.701 13.480 0.50 19.20 O
ANISOU 1457 OG BSER C 4 2442 2562 2291 10 -363 -133 O
ATOM 1458 N HIS C 5 21.507 -9.684 17.083 1.00 12.07 N
ANISOU 1458 N HIS C 5 1240 1574 1770 -83 -268 -75 N
ATOM 1459 CA HIS C 5 21.204 -9.194 18.421 1.00 11.39 C
ANISOU 1459 CA HIS C 5 1123 1445 1760 -84 -173 -44 C
ATOM 1460 C HIS C 5 22.427 -9.209 19.294 1.00 11.53 C
ANISOU 1460 C HIS C 5 1225 1441 1717 -76 -102 -46 C
ATOM 1461 O HIS C 5 23.092 -10.246 19.411 1.00 10.52 O
ANISOU 1461 O HIS C 5 1147 1301 1548 -90 -97 -72 O
ATOM 1462 CB HIS C 5 20.108 -10.060 19.072 1.00 13.18 C
ANISOU 1462 CB HIS C 5 1279 1625 2102 -131 -141 -62 C
ATOM 1463 CG HIS C 5 19.512 -9.421 20.287 1.00 17.73 C
ANISOU 1463 CG HIS C 5 1823 2157 2756 -113 -30 -19 C
ATOM 1464 ND1 HIS C 5 19.868 -9.822 21.563 1.00 20.36 N
ANISOU 1464 ND1 HIS C 5 2227 2439 3069 -111 79 -16 N
ATOM 1465 CD2 HIS C 5 18.633 -8.391 20.378 1.00 21.36 C
ANISOU 1465 CD2 HIS C 5 2204 2616 3297 -80 -6 25 C
ATOM 1466 CE1 HIS C 5 19.135 -9.078 22.388 1.00 20.78 C
ANISOU 1466 CE1 HIS C 5 2252 2457 3186 -85 173 20 C
ATOM 1467 NE2 HIS C 5 18.406 -8.179 21.724 1.00 22.29 N
ANISOU 1467 NE2 HIS C 5 2349 2672 3449 -66 133 46 N
ATOM 1468 N LYS C 6 22.717 -8.076 19.931 1.00 9.03 N
ANISOU 1468 N LYS C 6 920 1112 1398 -51 -52 -23 N
ATOM 1469 CA LYS C 6 23.840 -7.924 20.843 1.00 8.88 C
ANISOU 1469 CA LYS C 6 965 1082 1325 -47 -14 -39 C
ATOM 1470 C LYS C 6 23.286 -7.452 22.188 1.00 10.34 C
ANISOU 1470 C LYS C 6 1166 1227 1535 -39 62 -40 C
ATOM 1471 O LYS C 6 22.502 -6.488 22.244 1.00 9.79 O
ANISOU 1471 O LYS C 6 1063 1132 1523 -25 101 -21 O
ATOM 1472 CB LYS C 6 24.869 -6.945 20.285 1.00 9.72 C
ANISOU 1472 CB LYS C 6 1083 1203 1407 -35 -27 -34 C
ATOM 1473 CG LYS C 6 26.126 -6.828 21.146 1.00 8.79 C
ANISOU 1473 CG LYS C 6 1000 1084 1255 -44 -19 -67 C
ATOM 1474 CD LYS C 6 27.225 -6.002 20.454 1.00 8.75 C
ANISOU 1474 CD LYS C 6 979 1079 1266 -47 -21 -62 C
ATOM 1475 CE LYS C 6 28.489 -5.901 21.257 1.00 10.17 C
ANISOU 1475 CE LYS C 6 1156 1265 1442 -66 -39 -106 C
ATOM 1476 NZ LYS C 6 29.505 -5.105 20.464 1.00 9.48 N
ANISOU 1476 NZ LYS C 6 1027 1162 1416 -80 -18 -94 N
ATOM 1477 N SER C 7 23.699 -8.123 23.263 1.00 10.36 N
ANISOU 1477 N SER C 7 1232 1221 1483 -33 92 -56 N
ATOM 1478 CA SER C 7 23.213 -7.780 24.590 1.00 8.73 C
ANISOU 1478 CA SER C 7 1077 976 1263 -11 176 -59 C
ATOM 1479 C SER C 7 24.296 -8.242 25.574 1.00 9.98 C
ANISOU 1479 C SER C 7 1329 1158 1305 13 158 -84 C
ATOM 1480 O SER C 7 24.798 -9.381 25.423 1.00 9.76 O
ANISOU 1480 O SER C 7 1312 1150 1248 20 130 -68 O
ATOM 1481 CB SER C 7 21.900 -8.501 24.853 1.00 10.87 C
ANISOU 1481 CB SER C 7 1314 1202 1613 -10 258 -21 C
ATOM 1482 OG SER C 7 21.400 -8.185 26.144 1.00 11.94 O
ANISOU 1482 OG SER C 7 1518 1292 1728 27 373 -12 O
ATOM 1483 N GLY C 8 24.675 -7.399 26.533 1.00 8.82 N
ANISOU 1483 N GLY C 8 1253 1009 1091 30 165 -126 N
ATOM 1484 CA GLY C 8 25.714 -7.783 27.486 1.00 8.83 C
ANISOU 1484 CA GLY C 8 1337 1052 965 62 113 -155 C
ATOM 1485 C GLY C 8 27.041 -8.085 26.807 1.00 11.93 C
ANISOU 1485 C GLY C 8 1673 1504 1358 45 1 -167 C
ATOM 1486 O GLY C 8 27.843 -8.862 27.331 1.00 13.03 O
ANISOU 1486 O GLY C 8 1847 1686 1417 86 -49 -159 O
ATOM 1487 N GLY C 9 27.280 -7.479 25.645 1.00 9.32 N
ANISOU 1487 N GLY C 9 1256 1169 1115 0 -25 -173 N
ATOM 1488 CA GLY C 9 28.520 -7.707 24.911 1.00 9.68 C
ANISOU 1488 CA GLY C 9 1241 1256 1180 -11 -96 -174 C
ATOM 1489 C GLY C 9 28.580 -9.057 24.229 1.00 10.62 C
ANISOU 1489 C GLY C 9 1348 1387 1300 12 -90 -121 C
ATOM 1490 O GLY C 9 29.650 -9.500 23.826 1.00 11.39 O
ANISOU 1490 O GLY C 9 1412 1515 1401 26 -129 -112 O
ATOM 1491 N GLU C 10 27.421 -9.720 24.068 1.00 9.83 N
ANISOU 1491 N GLU C 10 1268 1251 1216 14 -32 -91 N
ATOM 1492 CA GLU C 10 27.325 -11.049 23.445 1.00 9.28 C
ANISOU 1492 CA GLU C 10 1200 1168 1159 23 -16 -61 C
ATOM 1493 C GLU C 10 26.442 -10.938 22.215 1.00 10.38 C
ANISOU 1493 C GLU C 10 1294 1288 1363 -17 -13 -65 C
ATOM 1494 O GLU C 10 25.350 -10.355 22.324 1.00 9.57 O
ANISOU 1494 O GLU C 10 1166 1164 1305 -35 10 -64 O
ATOM 1495 CB GLU C 10 26.637 -11.976 24.482 1.00 10.72 C
ANISOU 1495 CB GLU C 10 1444 1310 1318 52 53 -33 C
ATOM 1496 CG GLU C 10 26.346 -13.377 23.969 1.00 11.95 C
ANISOU 1496 CG GLU C 10 1608 1417 1514 48 96 -11 C
ATOM 1497 CD GLU C 10 25.654 -14.286 24.971 1.00 15.70 C
ANISOU 1497 CD GLU C 10 2143 1829 1994 75 198 31 C
ATOM 1498 OE1 GLU C 10 24.901 -13.783 25.838 1.00 22.50 O
ANISOU 1498 OE1 GLU C 10 3026 2672 2851 84 256 44 O
ATOM 1499 OE2 GLU C 10 25.849 -15.513 24.884 1.00 12.51 O
ANISOU 1499 OE2 GLU C 10 1772 1377 1604 94 243 57 O
ATOM 1500 N THR C 11 26.869 -11.509 21.084 1.00 7.61 N
ANISOU 1500 N THR C 11 937 943 1012 -20 -37 -68 N
ATOM 1501 CA THR C 11 26.091 -11.446 19.858 1.00 7.45 C
ANISOU 1501 CA THR C 11 892 920 1018 -46 -63 -81 C
ATOM 1502 C THR C 11 25.655 -12.831 19.473 1.00 10.11 C
ANISOU 1502 C THR C 11 1252 1219 1370 -66 -57 -105 C
ATOM 1503 O THR C 11 26.442 -13.770 19.601 1.00 9.25 O
ANISOU 1503 O THR C 11 1191 1089 1236 -43 -28 -103 O
ATOM 1504 CB THR C 11 26.910 -10.800 18.733 1.00 9.90 C
ANISOU 1504 CB THR C 11 1202 1263 1295 -28 -88 -73 C
ATOM 1505 OG1 THR C 11 27.257 -9.469 19.154 1.00 9.19 O
ANISOU 1505 OG1 THR C 11 1083 1185 1225 -24 -78 -57 O
ATOM 1506 CG2 THR C 11 26.119 -10.683 17.430 1.00 9.63 C
ANISOU 1506 CG2 THR C 11 1167 1244 1248 -32 -131 -82 C
ATOM 1507 N ARG C 12 24.404 -12.965 18.985 1.00 10.51 N
ANISOU 1507 N ARG C 12 1262 1255 1476 -109 -87 -131 N
ATOM 1508 CA ARG C 12 23.850 -14.204 18.479 1.00 10.55 C
ANISOU 1508 CA ARG C 12 1277 1213 1521 -152 -97 -181 C
ATOM 1509 C ARG C 12 24.091 -14.285 16.976 1.00 13.06 C
ANISOU 1509 C ARG C 12 1630 1564 1769 -151 -176 -228 C
ATOM 1510 O ARG C 12 23.651 -13.394 16.231 1.00 13.74 O
ANISOU 1510 O ARG C 12 1683 1708 1830 -142 -249 -226 O
ATOM 1511 CB ARG C 12 22.337 -14.246 18.727 1.00 14.60 C
ANISOU 1511 CB ARG C 12 1699 1696 2153 -208 -104 -196 C
ATOM 1512 CG ARG C 12 21.896 -14.219 20.159 1.00 20.29 C
ANISOU 1512 CG ARG C 12 2399 2369 2943 -203 3 -146 C
ATOM 1513 CD ARG C 12 20.382 -14.340 20.172 1.00 35.90 C
ANISOU 1513 CD ARG C 12 4262 4307 5071 -262 7 -161 C
ATOM 1514 NE ARG C 12 19.790 -13.907 21.435 1.00 44.98 N
ANISOU 1514 NE ARG C 12 5384 5420 6286 -240 123 -99 N
ATOM 1515 CZ ARG C 12 18.654 -13.221 21.526 1.00 56.04 C
ANISOU 1515 CZ ARG C 12 6672 6822 7799 -251 132 -80 C
ATOM 1516 NH1 ARG C 12 18.002 -12.852 20.429 1.00 32.27 N
ANISOU 1516 NH1 ARG C 12 3555 3863 4843 -279 7 -111 N
ATOM 1517 NH2 ARG C 12 18.174 -12.878 22.713 1.00 47.00 N
ANISOU 1517 NH2 ARG C 12 5525 5631 6702 -220 269 -23 N
ATOM 1518 N LEU C 13 24.722 -15.366 16.526 1.00 10.82 N
ANISOU 1518 N LEU C 13 1425 1240 1447 -149 -152 -268 N
ATOM 1519 CA LEU C 13 25.082 -15.606 15.115 1.00 11.91 C
ANISOU 1519 CA LEU C 13 1639 1397 1490 -134 -201 -320 C
ATOM 1520 C LEU C 13 24.369 -16.785 14.532 1.00 11.92 C
ANISOU 1520 C LEU C 13 1673 1337 1518 -199 -241 -425 C
ATOM 1521 O LEU C 13 23.742 -17.577 15.294 1.00 12.41 O
ANISOU 1521 O LEU C 13 1694 1320 1700 -259 -199 -447 O
ATOM 1522 CB LEU C 13 26.619 -15.883 14.943 1.00 12.75 C
ANISOU 1522 CB LEU C 13 1829 1492 1525 -64 -117 -287 C
ATOM 1523 CG LEU C 13 27.592 -14.714 15.072 1.00 18.89 C
ANISOU 1523 CG LEU C 13 2579 2327 2270 -4 -89 -207 C
ATOM 1524 CD1 LEU C 13 27.246 -13.548 14.138 1.00 19.86 C
ANISOU 1524 CD1 LEU C 13 2697 2512 2336 12 -147 -193 C
ATOM 1525 CD2 LEU C 13 27.933 -14.398 16.511 1.00 23.18 C
ANISOU 1525 CD2 LEU C 13 3058 2872 2879 1 -53 -152 C
ATOM 1526 OXT LEU C 13 24.497 -16.988 13.313 1.00 12.66 O
ANISOU 1526 OXT LEU C 13 1848 1450 1512 -189 -299 -490 O
TER 1527 LEU C 13
ATOM 1528 N GLY D 9 32.660 7.702 6.780 1.00 29.20 N
ANISOU 1528 N GLY D 9 4033 3670 3390 212 -108 -246 N
ATOM 1529 CA GLY D 9 31.411 7.410 6.080 1.00 28.17 C
ANISOU 1529 CA GLY D 9 3897 3531 3276 250 -112 -232 C
ATOM 1530 C GLY D 9 31.575 6.519 4.863 1.00 30.50 C
ANISOU 1530 C GLY D 9 4166 3855 3567 280 -142 -228 C
ATOM 1531 O GLY D 9 30.602 6.255 4.147 1.00 29.84 O
ANISOU 1531 O GLY D 9 4072 3778 3489 306 -144 -216 O
ATOM 1532 N GLU D 10 32.798 6.039 4.643 1.00 26.35 N
ANISOU 1532 N GLU D 10 3630 3351 3031 273 -162 -234 N
ATOM 1533 CA GLU D 10 33.176 5.199 3.510 1.00 24.68 C
ANISOU 1533 CA GLU D 10 3399 3161 2819 291 -183 -229 C
ATOM 1534 C GLU D 10 33.597 3.794 3.946 1.00 24.62 C
ANISOU 1534 C GLU D 10 3383 3170 2803 289 -203 -233 C
ATOM 1535 O GLU D 10 34.334 3.647 4.920 1.00 23.89 O
ANISOU 1535 O GLU D 10 3292 3083 2703 272 -208 -238 O
ATOM 1536 CB GLU D 10 34.336 5.884 2.769 1.00 26.38 C
ANISOU 1536 CB GLU D 10 3613 3378 3032 287 -180 -229 C
ATOM 1537 CG GLU D 10 34.678 5.273 1.424 1.00 32.13 C
ANISOU 1537 CG GLU D 10 4326 4116 3766 300 -194 -221 C
ATOM 1538 CD GLU D 10 35.880 5.864 0.714 1.00 44.28 C
ANISOU 1538 CD GLU D 10 5868 5648 5307 296 -195 -226 C
ATOM 1539 OE1 GLU D 10 36.763 6.456 1.378 1.00 43.79 O
ANISOU 1539 OE1 GLU D 10 5817 5586 5235 279 -188 -238 O
ATOM 1540 OE2 GLU D 10 35.946 5.708 -0.523 1.00 30.19 O
ANISOU 1540 OE2 GLU D 10 4077 3861 3532 306 -200 -220 O
ATOM 1541 N THR D 11 33.194 2.770 3.172 1.00 19.39 N
ANISOU 1541 N THR D 11 2708 2518 2140 303 -206 -230 N
ATOM 1542 CA THR D 11 33.588 1.384 3.443 1.00 18.14 C
ANISOU 1542 CA THR D 11 2544 2373 1975 304 -207 -231 C
ATOM 1543 C THR D 11 34.129 0.754 2.160 1.00 18.55 C
ANISOU 1543 C THR D 11 2583 2434 2029 304 -201 -218 C
ATOM 1544 O THR D 11 33.533 0.911 1.090 1.00 18.02 O
ANISOU 1544 O THR D 11 2512 2371 1964 305 -197 -216 O
ATOM 1545 CB THR D 11 32.411 0.545 4.009 1.00 19.92 C
ANISOU 1545 CB THR D 11 2776 2598 2194 314 -197 -247 C
ATOM 1546 OG1 THR D 11 31.900 1.157 5.194 1.00 18.56 O
ANISOU 1546 OG1 THR D 11 2620 2407 2026 310 -202 -258 O
ATOM 1547 CG2 THR D 11 32.809 -0.914 4.333 1.00 18.13 C
ANISOU 1547 CG2 THR D 11 2546 2383 1958 320 -182 -249 C
ATOM 1548 N ARG D 12 35.244 0.018 2.284 1.00 18.77 N
ANISOU 1548 N ARG D 12 2606 2468 2058 300 -198 -206 N
ATOM 1549 CA ARG D 12 35.869 -0.730 1.202 1.00 18.70 C
ANISOU 1549 CA ARG D 12 2590 2459 2056 293 -184 -190 C
ATOM 1550 C ARG D 12 35.222 -2.128 1.186 1.00 21.86 C
ANISOU 1550 C ARG D 12 2991 2869 2447 295 -149 -193 C
ATOM 1551 O ARG D 12 35.095 -2.766 2.244 1.00 22.92 O
ANISOU 1551 O ARG D 12 3128 3010 2573 307 -137 -197 O
ATOM 1552 CB ARG D 12 37.381 -0.861 1.479 1.00 21.73 C
ANISOU 1552 CB ARG D 12 2968 2844 2446 289 -189 -170 C
ATOM 1553 CG ARG D 12 38.119 0.486 1.573 1.00 32.78 C
ANISOU 1553 CG ARG D 12 4370 4240 3846 283 -215 -175 C
ATOM 1554 CD ARG D 12 39.359 0.421 2.454 1.00 50.92 C
ANISOU 1554 CD ARG D 12 6657 6556 6134 277 -222 -160 C
ATOM 1555 NE ARG D 12 39.143 -0.411 3.643 1.00 62.40 N
ANISOU 1555 NE ARG D 12 8103 8032 7576 285 -213 -151 N
ATOM 1556 CZ ARG D 12 40.028 -0.585 4.617 1.00 78.74 C
ANISOU 1556 CZ ARG D 12 10156 10131 9630 281 -218 -133 C
ATOM 1557 NH1 ARG D 12 41.199 0.039 4.581 1.00 69.89 N
ANISOU 1557 NH1 ARG D 12 9027 9027 8502 267 -233 -124 N
ATOM 1558 NH2 ARG D 12 39.742 -1.372 5.646 1.00 63.99 N
ANISOU 1558 NH2 ARG D 12 8281 8282 7752 292 -208 -126 N
ATOM 1559 N LEU D 13 34.801 -2.590 0.006 1.00 17.74 N
ANISOU 1559 N LEU D 13 2468 2349 1924 280 -127 -192 N
ATOM 1560 CA LEU D 13 34.167 -3.902 -0.218 1.00 16.59 C
ANISOU 1560 CA LEU D 13 2325 2216 1763 271 -79 -199 C
ATOM 1561 C LEU D 13 34.990 -4.780 -1.123 1.00 15.64 C
ANISOU 1561 C LEU D 13 2204 2086 1651 247 -39 -177 C
ATOM 1562 O LEU D 13 34.691 -5.988 -1.182 1.00 16.70 O
ANISOU 1562 O LEU D 13 2345 2228 1772 236 19 -180 O
ATOM 1563 CB LEU D 13 32.764 -3.757 -0.891 1.00 17.18 C
ANISOU 1563 CB LEU D 13 2397 2312 1819 259 -75 -220 C
ATOM 1564 CG LEU D 13 31.541 -3.249 -0.078 1.00 22.98 C
ANISOU 1564 CG LEU D 13 3134 3055 2541 279 -95 -243 C
ATOM 1565 CD1 LEU D 13 31.359 -3.960 1.235 1.00 23.63 C
ANISOU 1565 CD1 LEU D 13 3231 3130 2616 298 -80 -262 C
ATOM 1566 CD2 LEU D 13 31.518 -1.751 0.055 1.00 23.47 C
ANISOU 1566 CD2 LEU D 13 3193 3107 2619 292 -139 -235 C
ATOM 1567 OXT LEU D 13 35.855 -4.243 -1.848 1.00 16.77 O
ANISOU 1567 OXT LEU D 13 2345 2212 1815 235 -58 -159 O
TER 1568 LEU D 13
HETATM 1569 C1 GOL A 1 15.466 -25.894 15.333 1.00 37.25 C
HETATM 1570 O1 GOL A 1 16.758 -25.259 15.128 1.00 38.59 O
HETATM 1571 C2 GOL A 1 15.509 -26.958 16.437 1.00 36.37 C
HETATM 1572 O2 GOL A 1 16.653 -26.735 17.210 1.00 37.74 O
HETATM 1573 C3 GOL A 1 14.443 -26.614 17.426 1.00 35.33 C
HETATM 1574 O3 GOL A 1 14.293 -27.667 18.332 1.00 30.41 O
HETATM 1575 C1 GOL A 605 25.638 -26.999 25.963 1.00 27.91 C
HETATM 1576 O1 GOL A 605 25.279 -26.222 24.826 1.00 22.00 O
HETATM 1577 C2 GOL A 605 24.487 -27.773 26.552 1.00 28.81 C
HETATM 1578 O2 GOL A 605 23.815 -28.524 25.560 1.00 29.42 O
HETATM 1579 C3 GOL A 605 24.941 -28.817 27.551 1.00 28.51 C
HETATM 1580 O3 GOL A 605 25.982 -28.304 28.344 1.00 28.03 O
HETATM 1581 O HOH A 2 27.754 -32.187 16.461 1.00 9.19 O
HETATM 1582 O HOH A 4 33.522 -30.971 19.805 1.00 13.87 O
HETATM 1583 O HOH A 5 21.583 -32.125 18.753 1.00 10.50 O
HETATM 1584 O HOH A 6 31.777 -15.886 6.769 1.00 12.59 O
HETATM 1585 O HOH A 8 32.481 -4.111 18.995 1.00 12.47 O
HETATM 1586 O HOH A 9 34.919 -27.633 19.247 1.00 14.84 O
HETATM 1587 O HOH A 10 30.178 -31.356 22.719 1.00 12.10 O
HETATM 1588 O HOH A 11 17.362 -19.150 11.479 1.00 15.96 O
HETATM 1589 O HOH A 13 27.318 -19.696 3.228 1.00 16.34 O
HETATM 1590 O HOH A 14 26.477 -28.419 11.034 1.00 15.21 O
HETATM 1591 O HOH A 15 31.372 -11.566 2.136 1.00 17.06 O
HETATM 1592 O HOH A 17 21.042 -21.617 13.315 1.00 14.57 O
HETATM 1593 O HOH A 18 33.654 -2.307 15.798 1.00 16.27 O
HETATM 1594 O HOH A 19 35.240 -13.940 7.181 1.00 12.57 O
HETATM 1595 O HOH A 20 30.925 -29.827 10.021 1.00 15.47 O
HETATM 1596 O HOH A 22 35.499 -28.064 22.621 1.00 16.56 O
HETATM 1597 O HOH A 23 22.591 -26.102 23.824 1.00 17.81 O
HETATM 1598 O HOH A 24 17.642 -24.174 19.186 1.00 17.39 O
HETATM 1599 O HOH A 25 23.110 -19.608 20.657 1.00 19.20 O
HETATM 1600 O HOH A 26 33.745 -10.099 2.100 1.00 21.88 O
HETATM 1601 O HOH A 27 18.979 -23.454 12.522 1.00 18.27 O
HETATM 1602 O AHOH A 28 31.351 -1.893 17.589 0.50 9.96 O
HETATM 1603 O BHOH A 28 30.807 -1.778 18.659 0.50 13.37 O
HETATM 1604 O HOH A 29 34.985 -6.602 10.042 1.00 17.15 O
HETATM 1605 O HOH A 31 19.788 -26.075 11.964 1.00 16.61 O
HETATM 1606 O HOH A 32 36.119 -29.766 20.172 1.00 16.89 O
HETATM 1607 O HOH A 34 35.703 -2.508 27.267 1.00 19.84 O
HETATM 1608 O HOH A 36 19.941 -19.793 15.079 1.00 17.40 O
HETATM 1609 O HOH A 37 34.447 -8.765 5.419 1.00 25.48 O
HETATM 1610 O HOH A 40 13.464 -21.494 3.424 1.00 22.90 O
HETATM 1611 O HOH A 42 37.523 -13.521 8.480 1.00 20.75 O
HETATM 1612 O HOH A 49 42.640 -26.706 24.888 1.00 36.68 O
HETATM 1613 O HOH A 50 34.051 -29.536 10.224 1.00 19.99 O
HETATM 1614 O HOH A 55 37.561 -4.681 30.747 1.00 36.07 O
HETATM 1615 O HOH A 59 23.731 -28.294 10.111 1.00 18.71 O
HETATM 1616 O HOH A 61 38.305 -0.803 20.087 1.00 24.99 O
HETATM 1617 O HOH A 66 33.616 -3.040 31.018 1.00 25.56 O
HETATM 1618 O HOH A 72 23.990 -26.508 8.077 1.00 22.62 O
HETATM 1619 O AHOH A 73 35.345 -28.260 25.335 0.50 21.58 O
HETATM 1620 O BHOH A 73 33.428 -28.898 25.399 0.50 23.70 O
HETATM 1621 O HOH A 74 34.994 -6.846 7.223 1.00 25.94 O
HETATM 1622 O HOH A 75 17.418 -19.470 14.174 1.00 21.40 O
HETATM 1623 O HOH A 79 36.815 -31.044 12.268 1.00 24.50 O
HETATM 1624 O HOH A 88 23.613 -23.184 3.807 1.00 33.79 O
HETATM 1625 O HOH A 91 21.040 -16.014 23.295 1.00 27.56 O
HETATM 1626 O HOH A 94 42.575 -8.918 8.828 1.00 32.65 O
HETATM 1627 O HOH A 96 19.933 -26.203 7.612 1.00 28.79 O
HETATM 1628 O HOH A 98 43.619 -15.043 16.776 1.00 21.87 O
HETATM 1629 O HOH A 99 35.321 -3.996 29.338 1.00 26.73 O
HETATM 1630 O HOH A 101 28.294 -29.572 9.329 1.00 25.43 O
HETATM 1631 O HOH A 103 31.873 -26.781 26.607 1.00 21.85 O
HETATM 1632 O HOH A 104 20.970 -27.604 10.015 1.00 27.47 O
HETATM 1633 O HOH A 105 37.568 1.808 19.738 1.00 27.63 O
HETATM 1634 O HOH A 106 34.245 -4.320 6.228 1.00 33.43 O
HETATM 1635 O HOH A 108 32.828 -31.052 8.088 1.00 34.58 O
HETATM 1636 O HOH A 109 44.136 -9.402 14.345 1.00 37.27 O
HETATM 1637 O HOH A 111 33.706 -4.086 10.496 1.00 25.51 O
HETATM 1638 O HOH A 113 45.165 -13.275 9.213 1.00 25.43 O
HETATM 1639 O HOH A 117 23.929 -30.862 9.309 1.00 28.90 O
HETATM 1640 O HOH A 125 38.838 -14.549 5.093 1.00 28.56 O
HETATM 1641 O HOH A 127 40.441 -3.135 16.155 1.00 35.21 O
HETATM 1642 O HOH A 130 37.368 -5.175 10.058 1.00 34.69 O
HETATM 1643 O HOH A 131 37.022 -20.792 27.827 1.00 29.49 O
HETATM 1644 O HOH A 133 36.689 -32.588 10.115 1.00 41.68 O
HETATM 1645 O HOH A 134 25.937 -32.901 10.831 1.00 30.85 O
HETATM 1646 O HOH A 137 23.277 -33.067 10.546 1.00 39.65 O
HETATM 1647 O HOH A 138 22.066 -9.064 4.991 1.00 33.46 O
HETATM 1648 O HOH A 139 16.791 -21.936 14.890 1.00 34.47 O
HETATM 1649 O HOH A 142 17.340 -21.953 17.697 1.00 36.30 O
HETATM 1650 O HOH A 150 40.168 -1.105 18.091 1.00 30.61 O
HETATM 1651 O HOH A 151 20.488 -25.196 25.462 1.00 34.18 O
HETATM 1652 O HOH A 161 40.017 2.835 20.035 1.00 40.04 O
HETATM 1653 O HOH A 163 34.961 -22.139 29.625 1.00 34.80 O
HETATM 1654 O HOH A 164 44.150 -10.299 10.456 1.00 35.87 O
HETATM 1655 O HOH A 170 16.838 -21.223 8.256 1.00 20.47 O
HETATM 1656 O HOH A 173 41.377 -20.807 25.089 1.00 39.67 O
HETATM 1657 O HOH A 179 42.436 -30.505 19.489 1.00 26.69 O
HETATM 1658 O HOH A 180 22.285 -25.708 6.337 1.00 42.53 O
HETATM 1659 O HOH A 182 35.346 -25.402 25.063 1.00 17.46 O
HETATM 1660 O HOH A 187 37.736 -28.982 26.516 1.00 37.41 O
HETATM 1661 O HOH A 188 25.158 -20.681 2.161 1.00 34.91 O
HETATM 1662 O HOH A 196 44.875 -7.541 12.452 1.00 50.84 O
HETATM 1663 O HOH A 199 23.238 -11.366 6.310 1.00 30.49 O
HETATM 1664 O HOH A 203 36.267 -17.264 -0.287 1.00 34.29 O
HETATM 1665 O HOH A 205 21.675 -10.480 8.562 1.00 38.23 O
HETATM 1666 O HOH A 212 33.223 -26.568 28.883 1.00 33.01 O
HETATM 1667 O HOH A 216 36.632 -20.179 4.573 1.00 30.57 O
HETATM 1668 O HOH A 221 40.627 -12.894 20.512 1.00 37.28 O
HETATM 1669 O HOH A 249 34.632 -6.429 28.536 1.00 32.19 O
HETATM 1670 O HOH A 250 29.576 -16.690 29.221 1.00 31.51 O
HETATM 1671 O HOH A 256 39.558 -10.427 19.123 1.00 32.56 O
HETATM 1672 O HOH A 258 27.598 -32.073 8.517 1.00 45.94 O
HETATM 1673 O HOH A 262 40.669 -10.020 21.586 1.00 36.75 O
HETATM 1674 O HOH A 266 13.162 -25.012 2.745 1.00 40.35 O
HETATM 1675 O HOH A 280 24.937 -22.858 27.009 1.00 32.53 O
HETATM 1676 O HOH A 303 19.458 -20.242 17.569 1.00 28.97 O
HETATM 1677 O HOH A 307 46.843 -18.475 21.441 1.00 30.45 O
HETATM 1678 O AHOH A 311 27.686 -27.881 7.190 0.50 16.91 O
HETATM 1679 O BHOH A 311 27.184 -27.477 8.534 0.50 15.08 O
HETATM 1680 O HOH A 315 40.543 -2.556 24.285 1.00 28.66 O
HETATM 1681 O HOH A 318 35.309 -13.710 26.381 1.00 31.86 O
HETATM 1682 O HOH A 323 28.824 -19.102 28.420 1.00 38.54 O
HETATM 1683 O HOH B 12 44.294 -2.370 -7.414 1.00 19.11 O
HETATM 1684 O HOH B 16 39.747 -7.204 -5.211 1.00 19.04 O
HETATM 1685 O HOH B 30 35.477 -3.858 -17.225 1.00 21.98 O
HETATM 1686 O HOH B 33 34.788 -9.104 -12.603 1.00 20.90 O
HETATM 1687 O HOH B 35 33.251 -11.129 -11.904 1.00 23.56 O
HETATM 1688 O HOH B 38 28.725 -18.491 1.034 1.00 22.37 O
HETATM 1689 O HOH B 39 22.371 -9.188 -0.303 1.00 18.33 O
HETATM 1690 O HOH B 43 28.359 1.296 -14.313 1.00 24.81 O
HETATM 1691 O HOH B 44 16.900 2.260 -4.242 1.00 26.43 O
HETATM 1692 O HOH B 47 24.123 -4.181 8.942 1.00 22.01 O
HETATM 1693 O HOH B 48 28.594 -6.495 -14.997 1.00 23.35 O
HETATM 1694 O HOH B 52 25.370 -15.505 7.551 1.00 24.73 O
HETATM 1695 O HOH B 57 31.655 -16.962 -6.706 1.00 26.32 O
HETATM 1696 O HOH B 60 25.269 1.632 12.064 1.00 30.36 O
HETATM 1697 O HOH B 63 26.656 10.133 -1.152 1.00 33.41 O
HETATM 1698 O HOH B 64 38.363 -1.489 -16.591 1.00 28.01 O
HETATM 1699 O HOH B 71 30.114 0.764 -17.231 1.00 32.51 O
HETATM 1700 O HOH B 77 25.324 2.858 9.140 1.00 23.17 O
HETATM 1701 O HOH B 78 34.636 -2.256 -19.316 1.00 26.75 O
HETATM 1702 O HOH B 80 20.289 -7.458 -0.691 1.00 29.89 O
HETATM 1703 O HOH B 82 36.106 -12.123 -9.912 1.00 30.72 O
HETATM 1704 O HOH B 83 23.361 -2.469 10.857 1.00 24.24 O
HETATM 1705 O HOH B 84 38.324 0.523 -3.820 1.00 29.10 O
HETATM 1706 O HOH B 85 34.293 -16.085 -7.041 1.00 32.92 O
HETATM 1707 O HOH B 89 39.962 -9.271 -10.200 1.00 28.63 O
HETATM 1708 O HOH B 90 43.104 -9.446 -15.610 1.00 29.50 O
HETATM 1709 O HOH B 93 24.948 -7.615 -15.876 1.00 29.57 O
HETATM 1710 O HOH B 95 31.601 -9.565 -16.468 1.00 27.91 O
HETATM 1711 O HOH B 110 28.395 3.747 9.328 1.00 35.35 O
HETATM 1712 O HOH B 112 37.551 -10.396 -11.651 1.00 29.75 O
HETATM 1713 O HOH B 115 13.159 -4.640 -2.906 1.00 28.18 O
HETATM 1714 O HOH B 116 41.595 -8.585 -17.724 1.00 31.57 O
HETATM 1715 O HOH B 122 39.087 -4.015 -18.379 1.00 39.29 O
HETATM 1716 O HOH B 123 27.234 10.584 -8.427 1.00 29.77 O
HETATM 1717 O HOH B 129 32.055 -1.555 -19.111 1.00 28.87 O
HETATM 1718 O HOH B 136 25.061 8.393 -10.430 1.00 33.83 O
HETATM 1719 O HOH B 147 41.658 -5.960 -18.111 1.00 34.27 O
HETATM 1720 O HOH B 149 25.689 -12.699 5.330 1.00 26.99 O
HETATM 1721 O HOH B 152 20.331 5.555 -1.834 1.00 44.00 O
HETATM 1722 O HOH B 158 29.539 11.406 -7.205 1.00 41.96 O
HETATM 1723 O HOH B 159 24.133 5.279 11.749 1.00 40.38 O
HETATM 1724 O HOH B 167 22.750 9.440 -9.544 1.00 41.16 O
HETATM 1725 O HOH B 178 22.318 0.021 10.458 1.00 27.45 O
HETATM 1726 O HOH B 181 37.558 -7.754 -18.161 1.00 36.40 O
HETATM 1727 O HOH B 185 41.522 -11.090 -14.114 1.00 46.79 O
HETATM 1728 O HOH B 192 35.631 4.656 -11.746 1.00 29.71 O
HETATM 1729 O HOH B 198 35.964 6.850 -13.170 1.00 35.65 O
HETATM 1730 O HOH B 217 20.323 3.867 1.275 1.00 40.76 O
HETATM 1731 O HOH B 224 41.177 -13.962 -6.808 1.00 31.03 O
HETATM 1732 O HOH B 226 27.862 2.050 -16.891 1.00 35.52 O
HETATM 1733 O HOH B 298 36.814 -0.585 -19.588 1.00 36.35 O
HETATM 1734 O HOH B 302 21.436 -5.836 5.625 1.00 32.20 O
HETATM 1735 O HOH B 310 30.346 1.240 11.401 1.00 34.01 O
HETATM 1736 O HOH B 312 21.622 2.946 -19.028 1.00 31.56 O
HETATM 1737 O HOH B 313 42.039 -9.692 -2.678 1.00 41.43 O
HETATM 1738 O HOH B 314 37.769 5.588 -16.633 1.00 28.63 O
HETATM 1739 O HOH B 316 19.915 5.066 -4.534 1.00 45.74 O
HETATM 1740 O HOH B 317 37.677 5.236 -8.462 1.00 26.70 O
HETATM 1741 O HOH B 322 11.592 5.879 -13.954 1.00 35.93 O
HETATM 1742 O HOH C 14 27.274 -7.476 17.257 1.00 10.63 O
HETATM 1743 O HOH C 15 21.027 -5.739 19.246 1.00 12.24 O
HETATM 1744 O HOH C 21 32.386 -3.132 13.105 1.00 15.66 O
HETATM 1745 O HOH C 41 20.318 -12.156 16.189 1.00 27.71 O
HETATM 1746 O HOH C 45 24.627 -15.236 11.303 1.00 19.39 O
HETATM 1747 O HOH C 53 25.247 -2.510 12.864 1.00 22.90 O
HETATM 1748 O HOH C 54 22.950 -17.811 18.014 1.00 19.70 O
HETATM 1749 O HOH C 58 22.303 -10.183 27.899 1.00 21.55 O
HETATM 1750 O HOH C 65 24.778 -11.742 27.589 1.00 27.27 O
HETATM 1751 O HOH C 67 18.982 -5.964 17.500 1.00 26.27 O
HETATM 1752 O HOH C 69 18.636 -8.829 25.800 1.00 28.24 O
HETATM 1753 O HOH C 81 27.176 -10.720 29.165 1.00 34.30 O
HETATM 1754 O HOH C 87 30.792 -9.767 27.289 1.00 29.34 O
HETATM 1755 O HOH C 92 25.341 -16.952 27.141 1.00 32.47 O
HETATM 1756 O HOH C 107 22.051 -5.497 14.871 1.00 29.75 O
HETATM 1757 O HOH C 118 24.258 -0.278 14.362 1.00 25.49 O
HETATM 1758 O AHOH C 191 23.045 -11.839 24.357 0.50 19.63 O
HETATM 1759 O BHOH C 191 22.568 -11.529 22.170 0.50 13.86 O
HETATM 1760 O HOH D 51 32.901 -2.642 7.833 1.00 26.82 O
HETATM 1761 O HOH D 56 33.278 -7.539 0.542 1.00 24.13 O
HETATM 1762 O HOH D 68 31.005 -0.209 7.379 1.00 25.28 O
HETATM 1763 O HOH D 76 38.615 -4.325 -1.482 1.00 31.54 O
HETATM 1764 O HOH D 296 36.582 0.038 4.975 1.00 25.13 O
HETATM 1765 O HOH D 309 32.249 0.364 9.650 1.00 33.81 O
CONECT 606 1328
CONECT 1328 606
CONECT 1569 1570 1571
CONECT 1570 1569
CONECT 1571 1569 1572 1573
CONECT 1572 1571
CONECT 1573 1571 1574
CONECT 1574 1573
CONECT 1575 1576 1577
CONECT 1576 1575
CONECT 1577 1575 1578 1579
CONECT 1578 1577
CONECT 1579 1577 1580
CONECT 1580 1579
MASTER 379 0 2 7 15 0 5 6 1741 4 14 20
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