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*** 7avq ***elNémo ID: 230125035839121270Job options:ID = 230125035839121270 JOBID = 7avq 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 7avq
HEADER TRANSFERASE 05-NOV-20 7AVQ
TITLE CRYSTAL STRUCTURE OF HASPIN IN COMPLEX WITH DISUBSTITUTED IMIDAZO[1,2-
TITLE 2 B]PYRIDAZINE INHIBITOR (COMPOUND 12)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERINE/THREONINE-PROTEIN KINASE HASPIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: GERM CELL-SPECIFIC GENE 2 PROTEIN,H-HASPIN,HAPLOID GERM
COMPND 5 CELL-SPECIFIC NUCLEAR PROTEIN KINASE;
COMPND 6 EC: 2.7.11.1;
COMPND 7 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: HASPIN, GSG2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: -R3-PRARE2;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PNIC28-BSA4
KEYWDS KINASE, HASPIN, GSG2, INHIBITOR, STRUCTURAL GENOMICS, STRUCTURAL
KEYWDS 2 GENOMICS CONSORTIUM, SGC, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.CHAIKUAD,P.BONNET,S.ROUTIER,S.KNAPP,STRUCTURAL GENOMICS CONSORTIUM
AUTHOR 2 (SGC)
REVDAT 2 08-DEC-21 7AVQ 1 AUTHOR
REVDAT 1 18-NOV-20 7AVQ 0
JRNL AUTH J.ELIE,O.FEIZBAKHSH,N.DESBAN,B.JOSSELIN,B.BARATTE,A.BESCOND,
JRNL AUTH 2 J.DUEZ,X.FANT,S.BACH,D.MARIE,M.PLACE,S.BEN SALAH,A.CHARTIER,
JRNL AUTH 3 S.BERTEINA-RABOIN,A.CHAIKUAD,S.KNAPP,F.CARLES,P.BONNET,
JRNL AUTH 4 F.BURON,S.ROUTIER,S.RUCHAUD
JRNL TITL DESIGN OF NEW DISUBSTITUTED IMIDAZO[1,2- B ]PYRIDAZINE
JRNL TITL 2 DERIVATIVES AS SELECTIVE HASPIN INHIBITORS. SYNTHESIS,
JRNL TITL 3 BINDING MODE AND ANTICANCER BIOLOGICAL EVALUATION.
JRNL REF J ENZYME INHIB MED CHEM V. 35 1840 2020
JRNL REFN ESSN 1475-6374
JRNL PMID 33040634
JRNL DOI 10.1080/14756366.2020.1825408
REMARK 2
REMARK 2 RESOLUTION. 1.65 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0131
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.65
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 57.83
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 3 NUMBER OF REFLECTIONS : 53758
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.160
REMARK 3 R VALUE (WORKING SET) : 0.159
REMARK 3 FREE R VALUE : 0.179
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2837
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.65
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.69
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3847
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.03
REMARK 3 BIN R VALUE (WORKING SET) : 0.2660
REMARK 3 BIN FREE R VALUE SET COUNT : 215
REMARK 3 BIN FREE R VALUE : 0.2820
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2627
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 45
REMARK 3 SOLVENT ATOMS : 294
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.10
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.49000
REMARK 3 B22 (A**2) : 0.21000
REMARK 3 B33 (A**2) : -1.69000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.073
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.072
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.056
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.336
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.975
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.969
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2803 ; 0.016 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2698 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3804 ; 1.610 ; 1.962
REMARK 3 BOND ANGLES OTHERS (DEGREES): 6240 ; 0.917 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 351 ; 6.292 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 126 ;34.781 ;24.444
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 511 ;11.830 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 13 ;13.822 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 425 ; 0.101 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3256 ; 0.010 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 647 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 471 A 798
REMARK 3 ORIGIN FOR THE GROUP (A): 80.5891 72.0721 35.1926
REMARK 3 T TENSOR
REMARK 3 T11: 0.0145 T22: 0.0371
REMARK 3 T33: 0.0140 T12: -0.0028
REMARK 3 T13: -0.0020 T23: 0.0204
REMARK 3 L TENSOR
REMARK 3 L11: 1.0084 L22: 2.1837
REMARK 3 L33: 1.7709 L12: 0.4668
REMARK 3 L13: 0.1761 L23: 0.9572
REMARK 3 S TENSOR
REMARK 3 S11: -0.0108 S12: -0.1154 S13: -0.0432
REMARK 3 S21: 0.1253 S22: -0.0229 S23: -0.0343
REMARK 3 S31: 0.1301 S32: -0.0031 S33: 0.0336
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: U VALUES : WITH TLS ADDED HYDROGENS
REMARK 3 HAVE BEEN ADDED IN THE RIDING POSITIONS
REMARK 4
REMARK 4 7AVQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 06-NOV-20.
REMARK 100 THE DEPOSITION ID IS D_1292112172.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-DEC-15
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I03
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97626
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : IMOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.22
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 56638
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.650
REMARK 200 RESOLUTION RANGE LOW (A) : 57.830
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 200 DATA REDUNDANCY : 5.300
REMARK 200 R MERGE (I) : 0.06700
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.74
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.1
REMARK 200 DATA REDUNDANCY IN SHELL : 5.10
REMARK 200 R MERGE FOR SHELL (I) : 0.77600
REMARK 200 R SYM FOR SHELL (I) : 0.45700
REMARK 200 FOR SHELL : 2.200
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: 4OUC
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.63
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.90
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 63% MPD AND 0.1 M SPG, PH 6.5, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 277.15K
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 35.17450
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 43.07500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 39.00450
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 43.07500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 35.17450
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 39.00450
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 442
REMARK 465 HIS A 443
REMARK 465 HIS A 444
REMARK 465 HIS A 445
REMARK 465 HIS A 446
REMARK 465 HIS A 447
REMARK 465 HIS A 448
REMARK 465 SER A 449
REMARK 465 SER A 450
REMARK 465 GLY A 451
REMARK 465 VAL A 452
REMARK 465 ASP A 453
REMARK 465 LEU A 454
REMARK 465 GLY A 455
REMARK 465 THR A 456
REMARK 465 GLU A 457
REMARK 465 ASN A 458
REMARK 465 LEU A 459
REMARK 465 TYR A 460
REMARK 465 PHE A 461
REMARK 465 GLN A 462
REMARK 465 SER A 463
REMARK 465 MET A 464
REMARK 465 GLY A 465
REMARK 465 GLU A 466
REMARK 465 CYS A 467
REMARK 465 SER A 468
REMARK 465 GLN A 469
REMARK 465 LYS A 470
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASP A 716 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 GLU A 516 -4.92 72.69
REMARK 500 PHE A 556 -139.91 -97.23
REMARK 500 ASP A 649 45.57 -155.24
REMARK 500 ASP A 687 91.95 69.03
REMARK 500 CYS A 762 56.43 -90.23
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 802 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 554 O
REMARK 620 2 PHE A 556 O 93.9
REMARK 620 3 SER A 684 OG 145.0 85.2
REMARK 620 4 HOH A 942 O 88.2 92.5 126.8
REMARK 620 5 HOH A1142 O 90.6 174.9 89.8 89.8
REMARK 620 N 1 2 3 4
DBREF 7AVQ A 465 798 UNP Q8TF76 HASP_HUMAN 465 798
SEQADV 7AVQ MET A 442 UNP Q8TF76 INITIATING METHIONINE
SEQADV 7AVQ HIS A 443 UNP Q8TF76 EXPRESSION TAG
SEQADV 7AVQ HIS A 444 UNP Q8TF76 EXPRESSION TAG
SEQADV 7AVQ HIS A 445 UNP Q8TF76 EXPRESSION TAG
SEQADV 7AVQ HIS A 446 UNP Q8TF76 EXPRESSION TAG
SEQADV 7AVQ HIS A 447 UNP Q8TF76 EXPRESSION TAG
SEQADV 7AVQ HIS A 448 UNP Q8TF76 EXPRESSION TAG
SEQADV 7AVQ SER A 449 UNP Q8TF76 EXPRESSION TAG
SEQADV 7AVQ SER A 450 UNP Q8TF76 EXPRESSION TAG
SEQADV 7AVQ GLY A 451 UNP Q8TF76 EXPRESSION TAG
SEQADV 7AVQ VAL A 452 UNP Q8TF76 EXPRESSION TAG
SEQADV 7AVQ ASP A 453 UNP Q8TF76 EXPRESSION TAG
SEQADV 7AVQ LEU A 454 UNP Q8TF76 EXPRESSION TAG
SEQADV 7AVQ GLY A 455 UNP Q8TF76 EXPRESSION TAG
SEQADV 7AVQ THR A 456 UNP Q8TF76 EXPRESSION TAG
SEQADV 7AVQ GLU A 457 UNP Q8TF76 EXPRESSION TAG
SEQADV 7AVQ ASN A 458 UNP Q8TF76 EXPRESSION TAG
SEQADV 7AVQ LEU A 459 UNP Q8TF76 EXPRESSION TAG
SEQADV 7AVQ TYR A 460 UNP Q8TF76 EXPRESSION TAG
SEQADV 7AVQ PHE A 461 UNP Q8TF76 EXPRESSION TAG
SEQADV 7AVQ GLN A 462 UNP Q8TF76 EXPRESSION TAG
SEQADV 7AVQ SER A 463 UNP Q8TF76 EXPRESSION TAG
SEQADV 7AVQ MET A 464 UNP Q8TF76 EXPRESSION TAG
SEQRES 1 A 357 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 A 357 GLY THR GLU ASN LEU TYR PHE GLN SER MET GLY GLU CYS
SEQRES 3 A 357 SER GLN LYS GLY PRO VAL PRO PHE SER HIS CYS LEU PRO
SEQRES 4 A 357 THR GLU LYS LEU GLN ARG CYS GLU LYS ILE GLY GLU GLY
SEQRES 5 A 357 VAL PHE GLY GLU VAL PHE GLN THR ILE ALA ASP HIS THR
SEQRES 6 A 357 PRO VAL ALA ILE LYS ILE ILE ALA ILE GLU GLY PRO ASP
SEQRES 7 A 357 LEU VAL ASN GLY SER HIS GLN LYS THR PHE GLU GLU ILE
SEQRES 8 A 357 LEU PRO GLU ILE ILE ILE SER LYS GLU LEU SER LEU LEU
SEQRES 9 A 357 SER GLY GLU VAL CYS ASN ARG THR GLU GLY PHE ILE GLY
SEQRES 10 A 357 LEU ASN SER VAL HIS CYS VAL GLN GLY SER TYR PRO PRO
SEQRES 11 A 357 LEU LEU LEU LYS ALA TRP ASP HIS TYR ASN SER THR LYS
SEQRES 12 A 357 GLY SER ALA ASN ASP ARG PRO ASP PHE PHE LYS ASP ASP
SEQRES 13 A 357 GLN LEU PHE ILE VAL LEU GLU PHE GLU PHE GLY GLY ILE
SEQRES 14 A 357 ASP LEU GLU GLN MET ARG THR LYS LEU SER SER LEU ALA
SEQRES 15 A 357 THR ALA LYS SER ILE LEU HIS GLN LEU THR ALA SER LEU
SEQRES 16 A 357 ALA VAL ALA GLU ALA SER LEU ARG PHE GLU HIS ARG ASP
SEQRES 17 A 357 LEU HIS TRP GLY ASN VAL LEU LEU LYS LYS THR SER LEU
SEQRES 18 A 357 LYS LYS LEU HIS TYR THR LEU ASN GLY LYS SER SER THR
SEQRES 19 A 357 ILE PRO SER CYS GLY LEU GLN VAL SER ILE ILE ASP TYR
SEQRES 20 A 357 THR LEU SER ARG LEU GLU ARG ASP GLY ILE VAL VAL PHE
SEQRES 21 A 357 CYS ASP VAL SER MET ASP GLU ASP LEU PHE THR GLY ASP
SEQRES 22 A 357 GLY ASP TYR GLN PHE ASP ILE TYR ARG LEU MET LYS LYS
SEQRES 23 A 357 GLU ASN ASN ASN ARG TRP GLY GLU TYR HIS PRO TYR SER
SEQRES 24 A 357 ASN VAL LEU TRP LEU HIS TYR LEU THR ASP LYS MET LEU
SEQRES 25 A 357 LYS GLN MET THR PHE LYS THR LYS CYS ASN THR PRO ALA
SEQRES 26 A 357 MET LYS GLN ILE LYS ARG LYS ILE GLN GLU PHE HIS ARG
SEQRES 27 A 357 THR MET LEU ASN PHE SER SER ALA THR ASP LEU LEU CYS
SEQRES 28 A 357 GLN HIS SER LEU PHE LYS
HET S1Z A 801 24
HET NA A 802 1
HET GOL A 803 6
HET GOL A 804 6
HET MPD A 805 8
HETNAM S1Z (2~{R})-2-[[3-(2~{H}-INDAZOL-5-YL)IMIDAZO[1,2-
HETNAM 2 S1Z B]PYRIDAZIN-6-YL]AMINO]BUTAN-1-OL
HETNAM NA SODIUM ION
HETNAM GOL GLYCEROL
HETNAM MPD (4S)-2-METHYL-2,4-PENTANEDIOL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 S1Z C17 H18 N6 O
FORMUL 3 NA NA 1+
FORMUL 4 GOL 2(C3 H8 O3)
FORMUL 6 MPD C6 H14 O2
FORMUL 7 HOH *294(H2 O)
HELIX 1 AA1 PHE A 475 LEU A 479 1 5
HELIX 2 AA2 PRO A 480 ARG A 486 1 7
HELIX 3 AA3 THR A 528 LEU A 545 1 18
HELIX 4 AA4 SER A 546 GLU A 548 5 3
HELIX 5 AA5 PRO A 570 LYS A 584 1 15
HELIX 6 AA6 SER A 621 ARG A 644 1 24
HELIX 7 AA7 GLU A 708 THR A 712 5 5
HELIX 8 AA8 ASP A 716 ASN A 730 1 15
HELIX 9 AA9 PRO A 738 GLN A 755 1 18
HELIX 10 AB1 THR A 764 MET A 781 1 18
HELIX 11 AB2 LEU A 782 PHE A 784 5 3
HELIX 12 AB3 SER A 786 HIS A 794 1 9
HELIX 13 AB4 SER A 795 LYS A 798 5 4
SHEET 1 AA1 6 VAL A 473 PRO A 474 0
SHEET 2 AA1 6 LEU A 559 GLN A 566 1 O CYS A 564 N VAL A 473
SHEET 3 AA1 6 LEU A 599 GLU A 606 -1 O VAL A 602 N HIS A 563
SHEET 4 AA1 6 THR A 506 ILE A 515 -1 N ALA A 509 O PHE A 605
SHEET 5 AA1 6 GLY A 496 ALA A 503 -1 N PHE A 499 O ILE A 510
SHEET 6 AA1 6 GLU A 488 GLY A 493 -1 N GLU A 488 O GLN A 500
SHEET 1 AA2 3 ILE A 610 ASP A 611 0
SHEET 2 AA2 3 VAL A 655 LYS A 659 -1 O LEU A 657 N ILE A 610
SHEET 3 AA2 3 LEU A 681 ILE A 685 -1 O SER A 684 N LEU A 656
SHEET 1 AA3 2 LYS A 664 LEU A 669 0
SHEET 2 AA3 2 LYS A 672 PRO A 677 -1 O ILE A 676 N LEU A 665
SHEET 1 AA4 2 ARG A 692 ARG A 695 0
SHEET 2 AA4 2 ILE A 698 PHE A 701 -1 O VAL A 700 N LEU A 693
LINK O GLU A 554 NA NA A 802 1555 1555 2.31
LINK O PHE A 556 NA NA A 802 1555 1555 2.31
LINK OG SER A 684 NA NA A 802 1555 1555 2.40
LINK NA NA A 802 O HOH A 942 1555 1555 2.38
LINK NA NA A 802 O HOH A1142 1555 1555 2.29
CRYST1 70.349 78.009 86.150 90.00 90.00 90.00 P 21 21 21 4
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 0.014215 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012819 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011608 0.00000
ATOM 1 N GLY A 471 60.387 69.896 12.111 1.00 58.05 N
ANISOU 1 N GLY A 471 7248 7538 7272 -47 -2328 -783 N
ATOM 2 CA GLY A 471 60.445 69.592 13.568 1.00 53.64 C
ANISOU 2 CA GLY A 471 6492 7029 6861 -77 -2110 -809 C
ATOM 3 C GLY A 471 61.710 68.827 13.953 1.00 50.23 C
ANISOU 3 C GLY A 471 6172 6567 6345 -179 -1851 -725 C
ATOM 4 O GLY A 471 62.825 69.240 13.607 1.00 47.71 O
ANISOU 4 O GLY A 471 6055 6182 5890 -170 -1802 -613 O
ATOM 5 N PRO A 472 61.563 67.703 14.667 1.00 46.01 N
ANISOU 5 N PRO A 472 5513 6077 5893 -280 -1685 -781 N
ATOM 6 CA PRO A 472 62.805 66.976 15.011 1.00 41.30 C
ANISOU 6 CA PRO A 472 5034 5440 5220 -358 -1462 -700 C
ATOM 7 C PRO A 472 63.499 66.343 13.800 1.00 38.59 C
ANISOU 7 C PRO A 472 4903 5044 4714 -421 -1464 -666 C
ATOM 8 O PRO A 472 62.855 66.044 12.809 1.00 38.74 O
ANISOU 8 O PRO A 472 4955 5072 4692 -446 -1608 -728 O
ATOM 9 CB PRO A 472 62.308 65.887 15.944 1.00 41.77 C
ANISOU 9 CB PRO A 472 4927 5545 5400 -453 -1319 -776 C
ATOM 10 CG PRO A 472 60.965 65.569 15.424 1.00 46.76 C
ANISOU 10 CG PRO A 472 5428 6232 6106 -479 -1470 -905 C
ATOM 11 CD PRO A 472 60.374 66.912 14.983 1.00 48.37 C
ANISOU 11 CD PRO A 472 5598 6450 6329 -343 -1696 -919 C
ATOM 12 N VAL A 473 64.795 66.095 13.914 1.00 35.33 N
ANISOU 12 N VAL A 473 4625 4583 4218 -450 -1300 -581 N
ATOM 13 CA VAL A 473 65.549 65.357 12.876 1.00 36.46 C
ANISOU 13 CA VAL A 473 4956 4679 4217 -520 -1255 -566 C
ATOM 14 C VAL A 473 65.939 63.969 13.366 1.00 34.72 C
ANISOU 14 C VAL A 473 4710 4445 4038 -610 -1071 -593 C
ATOM 15 O VAL A 473 65.997 63.746 14.561 1.00 33.41 O
ANISOU 15 O VAL A 473 4427 4292 3977 -611 -954 -583 O
ATOM 16 CB VAL A 473 66.800 66.179 12.474 1.00 36.44 C
ANISOU 16 CB VAL A 473 5138 4625 4083 -483 -1212 -461 C
ATOM 17 CG1 VAL A 473 66.376 67.566 11.980 1.00 39.31 C
ANISOU 17 CG1 VAL A 473 5557 4981 4400 -398 -1405 -427 C
ATOM 18 CG2 VAL A 473 67.790 66.307 13.592 1.00 35.22 C
ANISOU 18 CG2 VAL A 473 4943 4459 3980 -465 -1031 -396 C
ATOM 19 N PRO A 474 66.239 63.032 12.465 1.00 36.41 N
ANISOU 19 N PRO A 474 5047 4625 4163 -684 -1043 -625 N
ATOM 20 CA PRO A 474 66.676 61.711 12.924 1.00 35.34 C
ANISOU 20 CA PRO A 474 4904 4455 4068 -758 -872 -648 C
ATOM 21 C PRO A 474 68.037 61.784 13.531 1.00 33.28 C
ANISOU 21 C PRO A 474 4699 4154 3793 -724 -708 -564 C
ATOM 22 O PRO A 474 68.782 62.701 13.283 1.00 33.55 O
ANISOU 22 O PRO A 474 4813 4181 3753 -670 -711 -499 O
ATOM 23 CB PRO A 474 66.732 60.872 11.648 1.00 37.86 C
ANISOU 23 CB PRO A 474 5365 4740 4278 -832 -899 -707 C
ATOM 24 CG PRO A 474 66.808 61.865 10.533 1.00 40.05 C
ANISOU 24 CG PRO A 474 5775 5026 4418 -792 -1040 -680 C
ATOM 25 CD PRO A 474 66.181 63.133 10.995 1.00 39.75 C
ANISOU 25 CD PRO A 474 5634 5033 4439 -704 -1170 -645 C
ATOM 26 N PHE A 475 68.336 60.839 14.420 1.00 31.84 N
ANISOU 26 N PHE A 475 4469 3942 3689 -757 -568 -566 N
ATOM 27 CA PHE A 475 69.624 60.785 15.078 1.00 31.11 C
ANISOU 27 CA PHE A 475 4414 3809 3599 -719 -424 -496 C
ATOM 28 C PHE A 475 70.797 60.855 14.090 1.00 32.00 C
ANISOU 28 C PHE A 475 4681 3884 3593 -708 -378 -480 C
ATOM 29 O PHE A 475 71.842 61.457 14.409 1.00 31.24 O
ANISOU 29 O PHE A 475 4607 3782 3480 -655 -307 -418 O
ATOM 30 CB PHE A 475 69.774 59.470 15.856 1.00 31.28 C
ANISOU 30 CB PHE A 475 4412 3777 3697 -766 -302 -514 C
ATOM 31 CG PHE A 475 69.602 59.596 17.342 1.00 28.53 C
ANISOU 31 CG PHE A 475 3951 3443 3447 -748 -248 -471 C
ATOM 32 CD1 PHE A 475 70.619 60.051 18.147 1.00 28.70 C
ANISOU 32 CD1 PHE A 475 3974 3453 3478 -679 -174 -394 C
ATOM 33 CD2 PHE A 475 68.434 59.156 17.936 1.00 29.52 C
ANISOU 33 CD2 PHE A 475 3973 3591 3653 -814 -261 -519 C
ATOM 34 CE1 PHE A 475 70.472 60.099 19.535 1.00 27.36 C
ANISOU 34 CE1 PHE A 475 3721 3293 3383 -671 -123 -357 C
ATOM 35 CE2 PHE A 475 68.275 59.189 19.272 1.00 28.14 C
ANISOU 35 CE2 PHE A 475 3715 3425 3550 -816 -194 -486 C
ATOM 36 CZ PHE A 475 69.294 59.665 20.092 1.00 27.47 C
ANISOU 36 CZ PHE A 475 3650 3327 3462 -742 -129 -401 C
ATOM 37 N SER A 476 70.649 60.182 12.951 1.00 33.67 N
ANISOU 37 N SER A 476 4994 4072 3727 -768 -403 -545 N
ATOM 38 CA SER A 476 71.704 60.196 11.926 1.00 37.78 C
ANISOU 38 CA SER A 476 5670 4563 4123 -775 -345 -548 C
ATOM 39 C SER A 476 72.019 61.577 11.373 1.00 39.81 C
ANISOU 39 C SER A 476 6000 4850 4276 -741 -408 -492 C
ATOM 40 O SER A 476 73.124 61.776 10.822 1.00 40.85 O
ANISOU 40 O SER A 476 6241 4962 4319 -746 -317 -479 O
ATOM 41 CB SER A 476 71.379 59.283 10.766 1.00 41.52 C
ANISOU 41 CB SER A 476 6250 5009 4517 -853 -370 -637 C
ATOM 42 OG SER A 476 70.170 59.686 10.181 1.00 42.13 O
ANISOU 42 OG SER A 476 6323 5130 4556 -878 -545 -666 O
ATOM 43 N HIS A 477 71.103 62.540 11.495 1.00 39.92 N
ANISOU 43 N HIS A 477 5961 4907 4301 -708 -556 -464 N
ATOM 44 CA HIS A 477 71.479 63.947 11.218 1.00 40.94 C
ANISOU 44 CA HIS A 477 6160 5045 4349 -664 -610 -393 C
ATOM 45 C HIS A 477 72.632 64.436 12.049 1.00 39.69 C
ANISOU 45 C HIS A 477 5970 4880 4231 -622 -476 -328 C
ATOM 46 O HIS A 477 73.554 65.069 11.543 1.00 41.67 O
ANISOU 46 O HIS A 477 6331 5116 4384 -629 -424 -293 O
ATOM 47 CB HIS A 477 70.309 64.885 11.466 1.00 44.49 C
ANISOU 47 CB HIS A 477 6529 5531 4844 -612 -790 -377 C
ATOM 48 CG HIS A 477 70.500 66.257 10.881 1.00 47.74 C
ANISOU 48 CG HIS A 477 7062 5931 5147 -575 -886 -312 C
ATOM 49 ND1 HIS A 477 70.973 67.340 11.611 1.00 50.70 N
ANISOU 49 ND1 HIS A 477 7404 6302 5557 -514 -861 -239 N
ATOM 50 CD2 HIS A 477 70.257 66.721 9.636 1.00 49.78 C
ANISOU 50 CD2 HIS A 477 7490 6169 5255 -595 -1016 -309 C
ATOM 51 CE1 HIS A 477 71.020 68.404 10.830 1.00 50.01 C
ANISOU 51 CE1 HIS A 477 7465 6186 5350 -501 -965 -191 C
ATOM 52 NE2 HIS A 477 70.591 68.053 9.630 1.00 51.62 N
ANISOU 52 NE2 HIS A 477 7799 6379 5436 -549 -1063 -228 N
ATOM 53 N CYS A 478 72.567 64.211 13.346 1.00 36.17 N
ANISOU 53 N CYS A 478 5374 4446 3922 -584 -424 -314 N
ATOM 54 CA CYS A 478 73.611 64.638 14.281 1.00 35.26 C
ANISOU 54 CA CYS A 478 5211 4328 3857 -539 -313 -257 C
ATOM 55 C CYS A 478 74.781 63.705 14.382 1.00 34.81 C
ANISOU 55 C CYS A 478 5174 4237 3814 -553 -156 -277 C
ATOM 56 O CYS A 478 75.896 64.129 14.785 1.00 34.00 O
ANISOU 56 O CYS A 478 5063 4133 3722 -523 -65 -242 O
ATOM 57 CB CYS A 478 73.042 64.701 15.728 1.00 37.03 C
ANISOU 57 CB CYS A 478 5274 4578 4217 -496 -321 -237 C
ATOM 58 SG CYS A 478 71.916 66.043 15.826 1.00 40.53 S
ANISOU 58 SG CYS A 478 5665 5061 4674 -450 -486 -217 S
ATOM 59 N LEU A 479 74.465 62.412 14.276 1.00 31.72 N
ANISOU 59 N LEU A 479 4779 3819 3455 -587 -128 -336 N
ATOM 60 CA LEU A 479 75.414 61.377 14.517 1.00 32.49 C
ANISOU 60 CA LEU A 479 4880 3869 3594 -583 3 -363 C
ATOM 61 C LEU A 479 75.417 60.448 13.341 1.00 30.96 C
ANISOU 61 C LEU A 479 4794 3640 3329 -643 26 -443 C
ATOM 62 O LEU A 479 74.895 59.344 13.415 1.00 31.72 O
ANISOU 62 O LEU A 479 4883 3699 3471 -673 27 -491 O
ATOM 63 CB LEU A 479 75.079 60.654 15.801 1.00 33.35 C
ANISOU 63 CB LEU A 479 4886 3958 3827 -562 23 -350 C
ATOM 64 CG LEU A 479 75.329 61.516 17.030 1.00 36.08 C
ANISOU 64 CG LEU A 479 5139 4336 4236 -502 25 -276 C
ATOM 65 CD1 LEU A 479 74.699 60.891 18.249 1.00 35.70 C
ANISOU 65 CD1 LEU A 479 5008 4274 4283 -503 27 -263 C
ATOM 66 CD2 LEU A 479 76.835 61.718 17.287 1.00 37.37 C
ANISOU 66 CD2 LEU A 479 5306 4486 4408 -451 122 -254 C
ATOM 67 N PRO A 480 76.044 60.897 12.227 1.00 30.49 N
ANISOU 67 N PRO A 480 4850 3587 3147 -671 55 -462 N
ATOM 68 CA PRO A 480 76.294 59.968 11.132 1.00 31.49 C
ANISOU 68 CA PRO A 480 5089 3677 3200 -727 111 -550 C
ATOM 69 C PRO A 480 77.193 58.806 11.570 1.00 30.82 C
ANISOU 69 C PRO A 480 4968 3534 3209 -697 247 -598 C
ATOM 70 O PRO A 480 77.794 58.868 12.637 1.00 29.91 O
ANISOU 70 O PRO A 480 4755 3412 3197 -630 297 -556 O
ATOM 71 CB PRO A 480 77.000 60.826 10.062 1.00 33.07 C
ANISOU 71 CB PRO A 480 5416 3900 3250 -764 148 -550 C
ATOM 72 CG PRO A 480 77.408 62.044 10.748 1.00 32.89 C
ANISOU 72 CG PRO A 480 5333 3911 3253 -718 144 -465 C
ATOM 73 CD PRO A 480 76.571 62.236 11.962 1.00 29.68 C
ANISOU 73 CD PRO A 480 4790 3520 2968 -661 51 -408 C
ATOM 74 N THR A 481 77.202 57.745 10.766 1.00 30.89 N
ANISOU 74 N THR A 481 5060 3494 3182 -742 290 -690 N
ATOM 75 CA THR A 481 77.870 56.506 11.136 1.00 32.20 C
ANISOU 75 CA THR A 481 5204 3584 3447 -707 395 -747 C
ATOM 76 C THR A 481 79.298 56.742 11.671 1.00 31.79 C
ANISOU 76 C THR A 481 5087 3530 3462 -627 510 -736 C
ATOM 77 O THR A 481 79.637 56.198 12.674 1.00 30.01 O
ANISOU 77 O THR A 481 4783 3259 3359 -559 533 -718 O
ATOM 78 CB THR A 481 78.000 55.564 9.962 1.00 34.29 C
ANISOU 78 CB THR A 481 5589 3801 3640 -764 452 -862 C
ATOM 79 OG1 THR A 481 76.748 55.454 9.298 1.00 36.52 O
ANISOU 79 OG1 THR A 481 5940 4097 3841 -846 336 -884 O
ATOM 80 CG2 THR A 481 78.424 54.182 10.409 1.00 35.61 C
ANISOU 80 CG2 THR A 481 5737 3866 3925 -723 529 -922 C
ATOM 81 N GLU A 482 80.134 57.512 10.979 1.00 33.04 N
ANISOU 81 N GLU A 482 5283 3735 3536 -643 581 -754 N
ATOM 82 CA GLU A 482 81.518 57.623 11.440 1.00 34.52 C
ANISOU 82 CA GLU A 482 5390 3924 3804 -575 698 -770 C
ATOM 83 C GLU A 482 81.601 58.321 12.771 1.00 31.30 C
ANISOU 83 C GLU A 482 4859 3545 3491 -506 646 -668 C
ATOM 84 O GLU A 482 82.378 57.884 13.620 1.00 31.77 O
ANISOU 84 O GLU A 482 4827 3573 3672 -423 690 -673 O
ATOM 85 CB GLU A 482 82.450 58.316 10.441 1.00 39.72 C
ANISOU 85 CB GLU A 482 6106 4630 4355 -626 808 -822 C
ATOM 86 CG GLU A 482 83.939 58.144 10.861 1.00 46.33 C
ANISOU 86 CG GLU A 482 6833 5465 5304 -554 944 -881 C
ATOM 87 CD GLU A 482 84.879 59.244 10.320 1.00 54.24 C
ANISOU 87 CD GLU A 482 7842 6538 6229 -608 1049 -898 C
ATOM 88 OE1 GLU A 482 85.645 59.866 11.140 1.00 61.56 O
ANISOU 88 OE1 GLU A 482 8645 7500 7246 -556 1075 -864 O
ATOM 89 OE2 GLU A 482 84.827 59.507 9.097 1.00 56.07 O
ANISOU 89 OE2 GLU A 482 8211 6790 6303 -711 1103 -943 O
ATOM 90 N LYS A 483 80.793 59.360 12.980 1.00 29.24 N
ANISOU 90 N LYS A 483 4597 3336 3177 -533 544 -581 N
ATOM 91 CA LYS A 483 80.718 60.060 14.251 1.00 28.96 C
ANISOU 91 CA LYS A 483 4454 3328 3221 -476 489 -488 C
ATOM 92 C LYS A 483 80.245 59.120 15.380 1.00 28.00 C
ANISOU 92 C LYS A 483 4269 3155 3217 -426 449 -464 C
ATOM 93 O LYS A 483 80.786 59.105 16.481 1.00 27.28 O
ANISOU 93 O LYS A 483 4094 3054 3219 -356 460 -426 O
ATOM 94 CB LYS A 483 79.793 61.275 14.137 1.00 31.08 C
ANISOU 94 CB LYS A 483 4747 3651 3411 -513 381 -417 C
ATOM 95 CG LYS A 483 79.949 62.298 15.226 1.00 31.74 C
ANISOU 95 CG LYS A 483 4736 3772 3550 -464 349 -335 C
ATOM 96 CD LYS A 483 79.340 63.602 14.757 1.00 33.65 C
ANISOU 96 CD LYS A 483 5034 4055 3696 -501 264 -286 C
ATOM 97 CE LYS A 483 79.154 64.545 15.929 1.00 35.54 C
ANISOU 97 CE LYS A 483 5180 4325 4000 -452 208 -210 C
ATOM 98 NZ LYS A 483 78.448 65.786 15.516 1.00 37.29 N
ANISOU 98 NZ LYS A 483 5457 4569 4143 -472 107 -165 N
ATOM 99 N LEU A 484 79.250 58.285 15.081 1.00 26.84 N
ANISOU 99 N LEU A 484 4173 2968 3057 -471 404 -492 N
ATOM 100 CA LEU A 484 78.759 57.306 16.091 1.00 26.59 C
ANISOU 100 CA LEU A 484 4107 2873 3124 -449 379 -473 C
ATOM 101 C LEU A 484 79.804 56.270 16.421 1.00 26.85 C
ANISOU 101 C LEU A 484 4139 2822 3241 -381 458 -512 C
ATOM 102 O LEU A 484 79.967 55.892 17.552 1.00 27.15 O
ANISOU 102 O LEU A 484 4135 2816 3363 -325 446 -466 O
ATOM 103 CB LEU A 484 77.560 56.502 15.555 1.00 29.08 C
ANISOU 103 CB LEU A 484 4484 3155 3411 -529 331 -516 C
ATOM 104 CG LEU A 484 76.200 57.061 15.724 1.00 30.77 C
ANISOU 104 CG LEU A 484 4664 3424 3603 -583 227 -481 C
ATOM 105 CD1 LEU A 484 75.204 56.137 15.047 1.00 32.01 C
ANISOU 105 CD1 LEU A 484 4879 3546 3739 -668 191 -550 C
ATOM 106 CD2 LEU A 484 75.871 57.259 17.179 1.00 31.28 C
ANISOU 106 CD2 LEU A 484 4636 3497 3751 -553 206 -406 C
ATOM 107 N GLN A 485 80.526 55.803 15.417 1.00 27.04 N
ANISOU 107 N GLN A 485 4216 2819 3239 -382 536 -604 N
ATOM 108 CA GLN A 485 81.563 54.804 15.602 1.00 29.95 C
ANISOU 108 CA GLN A 485 4578 3102 3699 -303 609 -664 C
ATOM 109 C GLN A 485 82.705 55.295 16.467 1.00 30.93 C
ANISOU 109 C GLN A 485 4598 3249 3905 -204 632 -632 C
ATOM 110 O GLN A 485 83.365 54.486 17.130 1.00 33.33 O
ANISOU 110 O GLN A 485 4876 3474 4314 -113 641 -646 O
ATOM 111 CB GLN A 485 82.150 54.317 14.266 1.00 32.23 C
ANISOU 111 CB GLN A 485 4934 3370 3941 -327 704 -791 C
ATOM 112 CG GLN A 485 81.186 53.513 13.464 1.00 34.06 C
ANISOU 112 CG GLN A 485 5277 3554 4111 -412 683 -844 C
ATOM 113 CD GLN A 485 81.769 53.115 12.110 1.00 37.39 C
ANISOU 113 CD GLN A 485 5777 3963 4466 -444 785 -976 C
ATOM 114 OE1 GLN A 485 82.269 53.940 11.373 1.00 42.60 O
ANISOU 114 OE1 GLN A 485 6446 4701 5039 -477 842 -1002 O
ATOM 115 NE2 GLN A 485 81.761 51.876 11.837 1.00 39.45 N
ANISOU 115 NE2 GLN A 485 6099 4121 4768 -438 816 -1058 N
ATOM 116 N ARG A 486 82.926 56.590 16.502 1.00 28.13 N
ANISOU 116 N ARG A 486 4189 2994 3506 -218 629 -588 N
ATOM 117 CA ARG A 486 83.974 57.143 17.339 1.00 28.13 C
ANISOU 117 CA ARG A 486 4081 3025 3581 -135 643 -562 C
ATOM 118 C ARG A 486 83.493 57.578 18.738 1.00 26.70 C
ANISOU 118 C ARG A 486 3850 2856 3437 -105 549 -447 C
ATOM 119 O ARG A 486 84.279 58.103 19.545 1.00 26.88 O
ANISOU 119 O ARG A 486 3786 2909 3516 -40 541 -417 O
ATOM 120 CB ARG A 486 84.626 58.315 16.604 1.00 29.66 C
ANISOU 120 CB ARG A 486 4250 3312 3708 -178 709 -589 C
ATOM 121 CG ARG A 486 85.413 57.843 15.368 1.00 34.71 C
ANISOU 121 CG ARG A 486 4924 3941 4323 -200 832 -718 C
ATOM 122 CD ARG A 486 85.803 59.011 14.463 1.00 39.22 C
ANISOU 122 CD ARG A 486 5518 4600 4785 -287 905 -739 C
ATOM 123 NE ARG A 486 86.614 58.479 13.390 1.00 46.41 N
ANISOU 123 NE ARG A 486 6457 5501 5677 -311 1041 -874 N
ATOM 124 CZ ARG A 486 87.900 58.130 13.513 1.00 52.89 C
ANISOU 124 CZ ARG A 486 7169 6319 6607 -242 1141 -971 C
ATOM 125 NH1 ARG A 486 88.520 57.593 12.474 1.00 58.78 N
ANISOU 125 NH1 ARG A 486 7945 7056 7333 -271 1274 -1109 N
ATOM 126 NH2 ARG A 486 88.589 58.347 14.646 1.00 55.30 N
ANISOU 126 NH2 ARG A 486 7332 6636 7042 -146 1108 -941 N
ATOM 127 N CYS A 487 82.217 57.403 19.038 1.00 24.85 N
ANISOU 127 N CYS A 487 3664 2607 3171 -157 482 -392 N
ATOM 128 CA CYS A 487 81.706 57.833 20.319 1.00 24.34 C
ANISOU 128 CA CYS A 487 3557 2561 3130 -143 411 -297 C
ATOM 129 C CYS A 487 82.226 56.950 21.456 1.00 24.82 C
ANISOU 129 C CYS A 487 3612 2538 3282 -59 394 -270 C
ATOM 130 O CYS A 487 82.217 55.715 21.325 1.00 25.91 O
ANISOU 130 O CYS A 487 3815 2574 3455 -45 406 -306 O
ATOM 131 CB CYS A 487 80.160 57.770 20.365 1.00 25.44 C
ANISOU 131 CB CYS A 487 3737 2706 3225 -228 356 -264 C
ATOM 132 SG CYS A 487 79.408 59.210 19.548 1.00 27.48 S
ANISOU 132 SG CYS A 487 3983 3073 3385 -297 318 -254 S
ATOM 133 N GLU A 488 82.673 57.599 22.522 1.00 23.78 N
ANISOU 133 N GLU A 488 3414 2441 3179 -6 359 -209 N
ATOM 134 CA GLU A 488 83.022 56.931 23.780 1.00 25.07 C
ANISOU 134 CA GLU A 488 3590 2531 3406 68 312 -160 C
ATOM 135 C GLU A 488 82.297 57.652 24.873 1.00 22.50 C
ANISOU 135 C GLU A 488 3250 2254 3045 35 262 -70 C
ATOM 136 O GLU A 488 82.269 58.903 24.893 1.00 21.60 O
ANISOU 136 O GLU A 488 3068 2239 2898 16 257 -53 O
ATOM 137 CB GLU A 488 84.522 57.020 24.050 1.00 29.75 C
ANISOU 137 CB GLU A 488 4105 3124 4075 182 313 -192 C
ATOM 138 CG GLU A 488 85.305 56.265 23.016 1.00 36.89 C
ANISOU 138 CG GLU A 488 5008 3979 5029 223 377 -301 C
ATOM 139 CD GLU A 488 86.824 56.387 23.226 1.00 44.00 C
ANISOU 139 CD GLU A 488 5800 4893 6024 337 383 -357 C
ATOM 140 OE1 GLU A 488 87.537 55.627 22.561 1.00 50.29 O
ANISOU 140 OE1 GLU A 488 6585 5636 6885 393 432 -456 O
ATOM 141 OE2 GLU A 488 87.292 57.239 24.030 1.00 50.03 O
ANISOU 141 OE2 GLU A 488 6483 5722 6804 370 340 -315 O
ATOM 142 N LYS A 489 81.712 56.913 25.831 1.00 21.37 N
ANISOU 142 N LYS A 489 3178 2039 2904 22 228 -14 N
ATOM 143 CA LYS A 489 80.967 57.601 26.882 1.00 19.94 C
ANISOU 143 CA LYS A 489 2984 1910 2680 -23 197 59 C
ATOM 144 C LYS A 489 81.949 58.166 27.916 1.00 20.87 C
ANISOU 144 C LYS A 489 3057 2053 2819 63 152 102 C
ATOM 145 O LYS A 489 82.878 57.464 28.296 1.00 23.01 O
ANISOU 145 O LYS A 489 3354 2249 3140 151 121 104 O
ATOM 146 CB LYS A 489 79.991 56.660 27.579 1.00 20.44 C
ANISOU 146 CB LYS A 489 3149 1894 2725 -90 194 101 C
ATOM 147 CG LYS A 489 79.260 57.276 28.745 1.00 20.18 C
ANISOU 147 CG LYS A 489 3108 1913 2647 -142 181 165 C
ATOM 148 CD LYS A 489 78.200 56.393 29.344 1.00 21.83 C
ANISOU 148 CD LYS A 489 3414 2052 2828 -239 204 194 C
ATOM 149 CE LYS A 489 77.792 56.969 30.695 1.00 21.86 C
ANISOU 149 CE LYS A 489 3420 2101 2784 -274 199 256 C
ATOM 150 NZ LYS A 489 76.689 56.218 31.312 1.00 23.69 N
ANISOU 150 NZ LYS A 489 3742 2280 2979 -395 244 277 N
ATOM 151 N ILE A 490 81.735 59.411 28.285 1.00 20.06 N
ANISOU 151 N ILE A 490 2887 2051 2684 40 143 127 N
ATOM 152 CA ILE A 490 82.576 60.093 29.274 1.00 20.88 C
ANISOU 152 CA ILE A 490 2944 2192 2799 105 97 161 C
ATOM 153 C ILE A 490 81.896 60.533 30.543 1.00 20.89 C
ANISOU 153 C ILE A 490 2970 2220 2748 67 70 228 C
ATOM 154 O ILE A 490 82.588 60.804 31.545 1.00 21.40 O
ANISOU 154 O ILE A 490 3028 2289 2812 122 19 263 O
ATOM 155 CB ILE A 490 83.356 61.290 28.636 1.00 20.77 C
ANISOU 155 CB ILE A 490 2821 2269 2801 128 114 118 C
ATOM 156 CG1 ILE A 490 82.382 62.349 28.067 1.00 20.88 C
ANISOU 156 CG1 ILE A 490 2811 2361 2762 44 141 114 C
ATOM 157 CG2 ILE A 490 84.349 60.761 27.593 1.00 22.44 C
ANISOU 157 CG2 ILE A 490 3006 2451 3070 177 151 43 C
ATOM 158 CD1 ILE A 490 83.078 63.613 27.560 1.00 21.30 C
ANISOU 158 CD1 ILE A 490 2788 2490 2814 50 155 87 C
ATOM 159 N GLY A 491 80.581 60.584 30.576 1.00 19.50 N
ANISOU 159 N GLY A 491 2819 2060 2528 -27 101 238 N
ATOM 160 CA GLY A 491 79.874 61.028 31.770 1.00 20.06 C
ANISOU 160 CA GLY A 491 2907 2165 2548 -75 97 284 C
ATOM 161 C GLY A 491 78.394 60.801 31.669 1.00 20.40 C
ANISOU 161 C GLY A 491 2969 2217 2566 -184 145 271 C
ATOM 162 O GLY A 491 77.897 60.317 30.643 1.00 20.23 O
ANISOU 162 O GLY A 491 2947 2176 2564 -222 170 229 O
ATOM 163 N GLU A 492 77.714 61.115 32.776 1.00 21.52 N
ANISOU 163 N GLU A 492 3126 2389 2662 -238 161 299 N
ATOM 164 CA GLU A 492 76.326 60.814 32.928 1.00 22.58 C
ANISOU 164 CA GLU A 492 3271 2532 2777 -350 218 280 C
ATOM 165 C GLU A 492 75.737 61.626 34.065 1.00 24.12 C
ANISOU 165 C GLU A 492 3439 2796 2928 -394 243 288 C
ATOM 166 O GLU A 492 76.453 62.203 34.910 1.00 25.68 O
ANISOU 166 O GLU A 492 3649 3014 3095 -342 212 325 O
ATOM 167 CB GLU A 492 76.134 59.351 33.177 1.00 24.10 C
ANISOU 167 CB GLU A 492 3592 2612 2954 -403 243 308 C
ATOM 168 CG GLU A 492 76.761 58.840 34.486 1.00 25.59 C
ANISOU 168 CG GLU A 492 3910 2726 3086 -382 220 387 C
ATOM 169 CD GLU A 492 76.386 57.421 34.838 1.00 27.62 C
ANISOU 169 CD GLU A 492 4325 2857 3314 -456 249 423 C
ATOM 170 OE1 GLU A 492 76.342 56.527 33.952 1.00 28.04 O
ANISOU 170 OE1 GLU A 492 4409 2833 3410 -463 256 397 O
ATOM 171 OE2 GLU A 492 76.177 57.148 36.077 1.00 29.62 O
ANISOU 171 OE2 GLU A 492 4695 3072 3488 -513 267 481 O
ATOM 172 N GLY A 493 74.415 61.614 34.122 1.00 26.35 N
ANISOU 172 N GLY A 493 3685 3116 3210 -496 304 244 N
ATOM 173 CA GLY A 493 73.665 62.144 35.268 1.00 25.70 C
ANISOU 173 CA GLY A 493 3587 3093 3085 -563 358 235 C
ATOM 174 C GLY A 493 72.252 61.709 35.113 1.00 26.81 C
ANISOU 174 C GLY A 493 3688 3252 3244 -686 434 172 C
ATOM 175 O GLY A 493 71.925 60.932 34.204 1.00 25.22 O
ANISOU 175 O GLY A 493 3490 3010 3081 -720 435 147 O
ATOM 176 N VAL A 494 71.381 62.179 36.016 1.00 26.88 N
ANISOU 176 N VAL A 494 3656 3327 3230 -763 505 135 N
ATOM 177 CA VAL A 494 69.990 61.771 35.915 1.00 27.42 C
ANISOU 177 CA VAL A 494 3662 3426 3330 -892 589 55 C
ATOM 178 C VAL A 494 69.473 62.217 34.553 1.00 27.10 C
ANISOU 178 C VAL A 494 3475 3438 3385 -852 532 -23 C
ATOM 179 O VAL A 494 68.666 61.546 33.942 1.00 26.31 O
ANISOU 179 O VAL A 494 3340 3330 3325 -930 556 -77 O
ATOM 180 CB VAL A 494 69.156 62.404 37.057 1.00 30.49 C
ANISOU 180 CB VAL A 494 3997 3896 3690 -970 682 3 C
ATOM 181 CG1 VAL A 494 67.653 62.269 36.790 1.00 31.78 C
ANISOU 181 CG1 VAL A 494 4029 4124 3923 -1087 763 -115 C
ATOM 182 CG2 VAL A 494 69.529 61.688 38.353 1.00 33.28 C
ANISOU 182 CG2 VAL A 494 4538 4182 3926 -1045 746 84 C
ATOM 183 N PHE A 495 69.951 63.368 34.068 1.00 25.91 N
ANISOU 183 N PHE A 495 3247 3335 3262 -733 450 -27 N
ATOM 184 CA PHE A 495 69.518 63.900 32.773 1.00 26.18 C
ANISOU 184 CA PHE A 495 3169 3411 3369 -686 378 -90 C
ATOM 185 C PHE A 495 69.726 62.933 31.563 1.00 27.01 C
ANISOU 185 C PHE A 495 3326 3451 3487 -693 340 -83 C
ATOM 186 O PHE A 495 69.077 63.102 30.495 1.00 27.62 O
ANISOU 186 O PHE A 495 3323 3560 3613 -692 287 -148 O
ATOM 187 CB PHE A 495 70.297 65.199 32.400 1.00 27.12 C
ANISOU 187 CB PHE A 495 3254 3558 3493 -558 292 -69 C
ATOM 188 CG PHE A 495 71.779 64.954 32.251 1.00 26.27 C
ANISOU 188 CG PHE A 495 3255 3386 3342 -489 258 18 C
ATOM 189 CD1 PHE A 495 72.307 64.410 31.087 1.00 26.54 C
ANISOU 189 CD1 PHE A 495 3330 3371 3384 -462 217 31 C
ATOM 190 CD2 PHE A 495 72.635 65.214 33.309 1.00 27.73 C
ANISOU 190 CD2 PHE A 495 3497 3560 3479 -457 271 76 C
ATOM 191 CE1 PHE A 495 73.630 64.109 30.989 1.00 25.70 C
ANISOU 191 CE1 PHE A 495 3304 3210 3253 -402 200 91 C
ATOM 192 CE2 PHE A 495 73.991 64.905 33.216 1.00 27.32 C
ANISOU 192 CE2 PHE A 495 3525 3452 3403 -393 235 142 C
ATOM 193 CZ PHE A 495 74.482 64.341 32.069 1.00 26.12 C
ANISOU 193 CZ PHE A 495 3397 3254 3272 -364 205 145 C
ATOM 194 N GLY A 496 70.675 62.009 31.653 1.00 23.89 N
ANISOU 194 N GLY A 496 3064 2965 3049 -686 350 -10 N
ATOM 195 CA GLY A 496 71.064 61.206 30.479 1.00 24.56 C
ANISOU 195 CA GLY A 496 3202 2984 3145 -672 313 -9 C
ATOM 196 C GLY A 496 72.581 61.020 30.396 1.00 23.58 C
ANISOU 196 C GLY A 496 3173 2795 2994 -575 282 64 C
ATOM 197 O GLY A 496 73.209 60.718 31.396 1.00 22.16 O
ANISOU 197 O GLY A 496 3071 2571 2779 -561 302 125 O
ATOM 198 N GLU A 497 73.173 61.217 29.202 1.00 21.35 N
ANISOU 198 N GLU A 497 2881 2507 2724 -510 231 51 N
ATOM 199 CA GLU A 497 74.471 60.643 28.880 1.00 20.65 C
ANISOU 199 CA GLU A 497 2875 2344 2628 -442 220 88 C
ATOM 200 C GLU A 497 75.342 61.644 28.151 1.00 20.39 C
ANISOU 200 C GLU A 497 2799 2354 2596 -356 178 85 C
ATOM 201 O GLU A 497 74.812 62.500 27.418 1.00 20.97 O
ANISOU 201 O GLU A 497 2809 2489 2669 -361 146 49 O
ATOM 202 CB GLU A 497 74.242 59.431 27.968 1.00 21.73 C
ANISOU 202 CB GLU A 497 3072 2408 2778 -488 233 52 C
ATOM 203 CG GLU A 497 73.227 58.415 28.506 1.00 23.95 C
ANISOU 203 CG GLU A 497 3398 2641 3060 -602 282 41 C
ATOM 204 CD GLU A 497 73.731 57.689 29.732 1.00 25.23 C
ANISOU 204 CD GLU A 497 3670 2718 3197 -603 313 113 C
ATOM 205 OE1 GLU A 497 74.979 57.678 29.913 1.00 25.60 O
ANISOU 205 OE1 GLU A 497 3763 2723 3241 -500 281 159 O
ATOM 206 OE2 GLU A 497 72.889 57.081 30.499 1.00 26.22 O
ANISOU 206 OE2 GLU A 497 3844 2814 3305 -712 368 119 O
ATOM 207 N VAL A 498 76.656 61.571 28.362 1.00 19.33 N
ANISOU 207 N VAL A 498 2697 2185 2463 -281 173 120 N
ATOM 208 CA VAL A 498 77.611 62.440 27.674 1.00 18.58 C
ANISOU 208 CA VAL A 498 2564 2126 2369 -216 153 111 C
ATOM 209 C VAL A 498 78.656 61.595 27.007 1.00 19.42 C
ANISOU 209 C VAL A 498 2715 2167 2494 -173 169 93 C
ATOM 210 O VAL A 498 79.258 60.714 27.635 1.00 19.39 O
ANISOU 210 O VAL A 498 2758 2095 2513 -136 172 116 O
ATOM 211 CB VAL A 498 78.338 63.453 28.614 1.00 18.86 C
ANISOU 211 CB VAL A 498 2558 2205 2401 -162 134 148 C
ATOM 212 CG1 VAL A 498 79.177 64.437 27.792 1.00 20.74 C
ANISOU 212 CG1 VAL A 498 2758 2483 2640 -124 125 129 C
ATOM 213 CG2 VAL A 498 77.305 64.212 29.425 1.00 19.02 C
ANISOU 213 CG2 VAL A 498 2538 2281 2406 -202 128 157 C
ATOM 214 N PHE A 499 78.855 61.820 25.695 1.00 17.78 N
ANISOU 214 N PHE A 499 2504 1976 2276 -177 179 47 N
ATOM 215 CA PHE A 499 79.816 61.102 24.897 1.00 18.19 C
ANISOU 215 CA PHE A 499 2588 1977 2345 -142 211 7 C
ATOM 216 C PHE A 499 80.838 62.034 24.352 1.00 19.76 C
ANISOU 216 C PHE A 499 2744 2225 2538 -108 229 -13 C
ATOM 217 O PHE A 499 80.525 63.223 24.159 1.00 21.46 O
ANISOU 217 O PHE A 499 2932 2505 2717 -133 210 0 O
ATOM 218 CB PHE A 499 79.125 60.395 23.723 1.00 18.71 C
ANISOU 218 CB PHE A 499 2708 2013 2388 -202 227 -46 C
ATOM 219 CG PHE A 499 78.089 59.387 24.131 1.00 18.99 C
ANISOU 219 CG PHE A 499 2788 1995 2434 -257 221 -41 C
ATOM 220 CD1 PHE A 499 76.778 59.782 24.374 1.00 19.06 C
ANISOU 220 CD1 PHE A 499 2765 2050 2424 -326 194 -35 C
ATOM 221 CD2 PHE A 499 78.431 58.053 24.358 1.00 19.66 C
ANISOU 221 CD2 PHE A 499 2941 1976 2552 -242 244 -47 C
ATOM 222 CE1 PHE A 499 75.814 58.893 24.802 1.00 20.04 C
ANISOU 222 CE1 PHE A 499 2920 2133 2562 -396 204 -39 C
ATOM 223 CE2 PHE A 499 77.462 57.141 24.803 1.00 20.24 C
ANISOU 223 CE2 PHE A 499 3070 1991 2631 -313 247 -38 C
ATOM 224 CZ PHE A 499 76.154 57.571 25.036 1.00 20.14 C
ANISOU 224 CZ PHE A 499 3018 2038 2597 -398 235 -35 C
ATOM 225 N GLN A 500 82.043 61.542 24.133 1.00 19.78 N
ANISOU 225 N GLN A 500 2739 2195 2581 -53 264 -48 N
ATOM 226 CA GLN A 500 83.068 62.233 23.376 1.00 20.39 C
ANISOU 226 CA GLN A 500 2777 2315 2655 -42 310 -92 C
ATOM 227 C GLN A 500 83.147 61.590 22.002 1.00 20.40 C
ANISOU 227 C GLN A 500 2833 2288 2631 -75 368 -165 C
ATOM 228 O GLN A 500 83.097 60.383 21.850 1.00 19.79 O
ANISOU 228 O GLN A 500 2796 2140 2583 -58 381 -197 O
ATOM 229 CB GLN A 500 84.396 62.110 24.107 1.00 22.55 C
ANISOU 229 CB GLN A 500 2982 2582 3006 42 314 -103 C
ATOM 230 CG GLN A 500 85.515 62.887 23.460 1.00 26.60 C
ANISOU 230 CG GLN A 500 3431 3148 3526 41 374 -159 C
ATOM 231 CD GLN A 500 86.836 62.649 24.186 1.00 30.63 C
ANISOU 231 CD GLN A 500 3849 3655 4134 132 368 -189 C
ATOM 232 OE1 GLN A 500 86.832 62.130 25.347 1.00 28.50 O
ANISOU 232 OE1 GLN A 500 3576 3344 3907 199 294 -143 O
ATOM 233 NE2 GLN A 500 87.976 63.031 23.539 1.00 32.38 N
ANISOU 233 NE2 GLN A 500 3997 3918 4390 132 442 -270 N
ATOM 234 N THR A 501 83.328 62.417 20.939 1.00 19.30 N
ANISOU 234 N THR A 501 2709 2197 2427 -127 409 -196 N
ATOM 235 CA THR A 501 83.503 61.926 19.645 1.00 20.95 C
ANISOU 235 CA THR A 501 2979 2388 2595 -166 472 -270 C
ATOM 236 C THR A 501 84.299 62.943 18.824 1.00 21.49 C
ANISOU 236 C THR A 501 3046 2512 2607 -209 541 -303 C
ATOM 237 O THR A 501 84.935 63.833 19.426 1.00 20.33 O
ANISOU 237 O THR A 501 2828 2407 2489 -191 543 -277 O
ATOM 238 CB THR A 501 82.195 61.553 18.915 1.00 21.25 C
ANISOU 238 CB THR A 501 3108 2406 2559 -233 433 -271 C
ATOM 239 OG1 THR A 501 82.511 60.833 17.733 1.00 21.93 O
ANISOU 239 OG1 THR A 501 3260 2461 2610 -263 501 -355 O
ATOM 240 CG2 THR A 501 81.280 62.727 18.675 1.00 21.42 C
ANISOU 240 CG2 THR A 501 3155 2480 2502 -286 366 -221 C
ATOM 241 N ILE A 502 84.363 62.718 17.515 1.00 23.70 N
ANISOU 241 N ILE A 502 3406 2786 2813 -270 605 -367 N
ATOM 242 CA AILE A 502 85.133 63.601 16.611 0.50 25.45 C
ANISOU 242 CA AILE A 502 3655 3052 2961 -335 692 -405 C
ATOM 243 CA BILE A 502 85.121 63.624 16.633 0.50 25.56 C
ANISOU 243 CA BILE A 502 3669 3067 2976 -335 690 -403 C
ATOM 244 C ILE A 502 84.151 64.116 15.577 1.00 27.39 C
ANISOU 244 C ILE A 502 4041 3304 3063 -424 651 -379 C
ATOM 245 O ILE A 502 83.453 63.290 14.963 1.00 28.17 O
ANISOU 245 O ILE A 502 4213 3369 3122 -445 630 -409 O
ATOM 246 CB AILE A 502 86.224 62.818 15.892 0.50 27.38 C
ANISOU 246 CB AILE A 502 3884 3284 3234 -334 823 -523 C
ATOM 247 CB BILE A 502 86.289 62.896 15.993 0.50 27.71 C
ANISOU 247 CB BILE A 502 3915 3330 3284 -330 822 -519 C
ATOM 248 CG1AILE A 502 87.271 62.265 16.882 0.50 27.68 C
ANISOU 248 CG1AILE A 502 3775 3312 3430 -227 846 -562 C
ATOM 249 CG1BILE A 502 87.355 62.555 17.049 0.50 28.09 C
ANISOU 249 CG1BILE A 502 3810 3377 3485 -227 840 -547 C
ATOM 250 CG2AILE A 502 86.951 63.705 14.867 0.50 28.08 C
ANISOU 250 CG2AILE A 502 4019 3421 3227 -431 937 -571 C
ATOM 251 CG2BILE A 502 86.959 63.758 14.913 0.50 28.43 C
ANISOU 251 CG2BILE A 502 4061 3468 3274 -430 934 -567 C
ATOM 252 CD1AILE A 502 88.058 63.327 17.603 0.50 27.57 C
ANISOU 252 CD1AILE A 502 3657 3357 3463 -214 851 -536 C
ATOM 253 CD1BILE A 502 88.458 61.679 16.519 0.50 30.09 C
ANISOU 253 CD1BILE A 502 4011 3614 3808 -195 957 -679 C
ATOM 254 N ALA A 503 84.105 65.453 15.404 1.00 27.60 N
ANISOU 254 N ALA A 503 4107 3364 3014 -474 631 -327 N
ATOM 255 CA ALA A 503 83.301 66.084 14.344 1.00 29.67 C
ANISOU 255 CA ALA A 503 4522 3623 3128 -554 579 -300 C
ATOM 256 C ALA A 503 84.271 66.947 13.539 1.00 28.27 C
ANISOU 256 C ALA A 503 4416 3466 2858 -639 688 -324 C
ATOM 257 O ALA A 503 84.846 67.824 14.117 1.00 27.79 O
ANISOU 257 O ALA A 503 4298 3428 2834 -637 708 -293 O
ATOM 258 CB ALA A 503 82.250 66.989 14.939 1.00 30.85 C
ANISOU 258 CB ALA A 503 4672 3779 3273 -531 436 -207 C
ATOM 259 N ASP A 504 84.361 66.676 12.246 1.00 30.52 N
ANISOU 259 N ASP A 504 4836 3741 3020 -722 754 -379 N
ATOM 260 CA ASP A 504 85.273 67.467 11.320 1.00 31.25 C
ANISOU 260 CA ASP A 504 5030 3849 2994 -835 882 -409 C
ATOM 261 C ASP A 504 86.679 67.619 11.946 1.00 30.51 C
ANISOU 261 C ASP A 504 4782 3793 3018 -822 1020 -464 C
ATOM 262 O ASP A 504 87.162 68.693 12.141 1.00 28.73 O
ANISOU 262 O ASP A 504 4554 3585 2777 -868 1048 -430 O
ATOM 263 CB ASP A 504 84.639 68.841 11.019 1.00 31.49 C
ANISOU 263 CB ASP A 504 5205 3864 2898 -891 780 -307 C
ATOM 264 CG ASP A 504 83.453 68.720 10.012 1.00 31.63 C
ANISOU 264 CG ASP A 504 5406 3847 2765 -926 660 -281 C
ATOM 265 OD1 ASP A 504 83.579 68.032 8.996 1.00 32.46 O
ANISOU 265 OD1 ASP A 504 5612 3947 2774 -989 730 -352 O
ATOM 266 OD2 ASP A 504 82.393 69.316 10.310 1.00 35.15 O
ANISOU 266 OD2 ASP A 504 5881 4274 3202 -884 488 -197 O
ATOM 267 N HIS A 505 87.253 66.461 12.269 1.00 29.96 N
ANISOU 267 N HIS A 505 4582 3728 3072 -753 1088 -552 N
ATOM 268 CA HIS A 505 88.598 66.307 12.817 1.00 30.40 C
ANISOU 268 CA HIS A 505 4467 3818 3264 -718 1207 -632 C
ATOM 269 C HIS A 505 88.825 67.011 14.105 1.00 27.94 C
ANISOU 269 C HIS A 505 4025 3530 3062 -656 1137 -567 C
ATOM 270 O HIS A 505 89.979 67.348 14.440 1.00 28.74 O
ANISOU 270 O HIS A 505 4005 3672 3244 -662 1230 -624 O
ATOM 271 CB HIS A 505 89.689 66.720 11.789 1.00 32.52 C
ANISOU 271 CB HIS A 505 4779 4123 3454 -845 1400 -730 C
ATOM 272 CG HIS A 505 89.713 65.934 10.512 1.00 35.02 C
ANISOU 272 CG HIS A 505 5212 4425 3667 -911 1506 -827 C
ATOM 273 ND1 HIS A 505 88.928 64.837 10.250 1.00 37.37 N
ANISOU 273 ND1 HIS A 505 5564 4680 3957 -859 1439 -841 N
ATOM 274 CD2 HIS A 505 90.478 66.100 9.408 1.00 36.63 C
ANISOU 274 CD2 HIS A 505 5495 4655 3766 -1040 1688 -925 C
ATOM 275 CE1 HIS A 505 89.193 64.367 9.049 1.00 38.21 C
ANISOU 275 CE1 HIS A 505 5778 4783 3957 -944 1566 -943 C
ATOM 276 NE2 HIS A 505 90.148 65.098 8.528 1.00 38.34 N
ANISOU 276 NE2 HIS A 505 5810 4843 3913 -1053 1724 -998 N
ATOM 277 N THR A 506 87.737 67.299 14.856 1.00 25.59 N
ANISOU 277 N THR A 506 3745 3210 2769 -601 976 -455 N
ATOM 278 CA THR A 506 87.777 68.081 16.011 1.00 26.14 C
ANISOU 278 CA THR A 506 3725 3298 2911 -556 902 -387 C
ATOM 279 C THR A 506 87.077 67.307 17.163 1.00 24.50 C
ANISOU 279 C THR A 506 3435 3067 2806 -436 781 -342 C
ATOM 280 O THR A 506 85.947 66.888 16.987 1.00 23.20 O
ANISOU 280 O THR A 506 3345 2871 2597 -426 700 -303 O
ATOM 281 CB THR A 506 87.062 69.450 15.771 1.00 27.18 C
ANISOU 281 CB THR A 506 3983 3420 2924 -625 831 -292 C
ATOM 282 OG1 THR A 506 87.680 70.086 14.608 1.00 28.68 O
ANISOU 282 OG1 THR A 506 4288 3616 2993 -755 949 -329 O
ATOM 283 CG2 THR A 506 87.168 70.358 16.939 1.00 28.19 C
ANISOU 283 CG2 THR A 506 4024 3564 3123 -587 768 -233 C
ATOM 284 N PRO A 507 87.717 67.234 18.335 1.00 24.03 N
ANISOU 284 N PRO A 507 3234 3026 2872 -358 765 -343 N
ATOM 285 CA PRO A 507 86.993 66.547 19.443 1.00 23.43 C
ANISOU 285 CA PRO A 507 3114 2921 2867 -262 652 -290 C
ATOM 286 C PRO A 507 85.837 67.335 19.924 1.00 21.50 C
ANISOU 286 C PRO A 507 2918 2677 2573 -271 545 -194 C
ATOM 287 O PRO A 507 85.917 68.563 20.023 1.00 22.43 O
ANISOU 287 O PRO A 507 3047 2820 2655 -310 534 -158 O
ATOM 288 CB PRO A 507 88.068 66.407 20.549 1.00 24.30 C
ANISOU 288 CB PRO A 507 3078 3051 3106 -182 654 -315 C
ATOM 289 CG PRO A 507 89.069 67.443 20.239 1.00 26.27 C
ANISOU 289 CG PRO A 507 3282 3351 3348 -245 736 -356 C
ATOM 290 CD PRO A 507 89.066 67.677 18.741 1.00 26.69 C
ANISOU 290 CD PRO A 507 3446 3406 3289 -355 839 -398 C
ATOM 291 N VAL A 508 84.726 66.668 20.230 1.00 19.36 N
ANISOU 291 N VAL A 508 2677 2376 2304 -240 467 -157 N
ATOM 292 CA VAL A 508 83.559 67.296 20.791 1.00 18.97 C
ANISOU 292 CA VAL A 508 2647 2332 2230 -239 367 -85 C
ATOM 293 C VAL A 508 82.945 66.405 21.861 1.00 19.16 C
ANISOU 293 C VAL A 508 2626 2333 2319 -181 312 -59 C
ATOM 294 O VAL A 508 83.241 65.214 21.902 1.00 18.94 O
ANISOU 294 O VAL A 508 2591 2270 2337 -150 341 -92 O
ATOM 295 CB VAL A 508 82.450 67.592 19.752 1.00 20.60 C
ANISOU 295 CB VAL A 508 2963 2527 2337 -296 321 -72 C
ATOM 296 CG1 VAL A 508 82.977 68.644 18.779 1.00 22.90 C
ANISOU 296 CG1 VAL A 508 3332 2829 2539 -364 363 -77 C
ATOM 297 CG2 VAL A 508 82.039 66.344 19.040 1.00 21.25 C
ANISOU 297 CG2 VAL A 508 3093 2578 2403 -309 335 -116 C
ATOM 298 N ALA A 509 82.120 67.022 22.697 1.00 18.19 N
ANISOU 298 N ALA A 509 2485 2228 2200 -172 241 -5 N
ATOM 299 CA ALA A 509 81.314 66.314 23.667 1.00 18.02 C
ANISOU 299 CA ALA A 509 2441 2189 2216 -145 198 21 C
ATOM 300 C ALA A 509 79.856 66.478 23.331 1.00 19.22 C
ANISOU 300 C ALA A 509 2626 2347 2331 -184 142 29 C
ATOM 301 O ALA A 509 79.440 67.578 22.903 1.00 20.44 O
ANISOU 301 O ALA A 509 2797 2527 2444 -202 102 40 O
ATOM 302 CB ALA A 509 81.552 66.840 25.075 1.00 19.53 C
ANISOU 302 CB ALA A 509 2571 2404 2446 -106 171 61 C
ATOM 303 N ILE A 510 79.104 65.379 23.398 1.00 18.06 N
ANISOU 303 N ILE A 510 2493 2171 2200 -198 136 17 N
ATOM 304 CA AILE A 510 77.701 65.323 23.054 0.50 18.53 C
ANISOU 304 CA AILE A 510 2562 2239 2241 -240 84 4 C
ATOM 305 CA BILE A 510 77.704 65.455 23.139 0.50 18.27 C
ANISOU 305 CA BILE A 510 2524 2211 2209 -237 81 8 C
ATOM 306 C ILE A 510 76.881 64.980 24.309 1.00 18.80 C
ANISOU 306 C ILE A 510 2546 2277 2319 -244 72 23 C
ATOM 307 O ILE A 510 77.094 63.890 24.865 1.00 19.86 O
ANISOU 307 O ILE A 510 2697 2368 2481 -245 109 28 O
ATOM 308 CB AILE A 510 77.449 64.234 21.969 0.50 20.45 C
ANISOU 308 CB AILE A 510 2868 2443 2460 -280 99 -44 C
ATOM 309 CB BILE A 510 77.311 64.772 21.838 0.50 19.90 C
ANISOU 309 CB BILE A 510 2794 2391 2374 -281 77 -38 C
ATOM 310 CG1AILE A 510 78.188 64.561 20.675 0.50 22.48 C
ANISOU 310 CG1AILE A 510 3190 2698 2653 -293 123 -70 C
ATOM 311 CG1BILE A 510 77.567 63.277 21.880 0.50 20.70 C
ANISOU 311 CG1BILE A 510 2922 2435 2506 -289 129 -64 C
ATOM 312 CG2AILE A 510 75.974 64.142 21.621 0.50 20.81 C
ANISOU 312 CG2AILE A 510 2909 2503 2496 -327 33 -68 C
ATOM 313 CG2BILE A 510 78.100 65.390 20.692 0.50 20.68 C
ANISOU 313 CG2BILE A 510 2954 2496 2408 -289 95 -51 C
ATOM 314 CD1AILE A 510 77.698 65.903 20.155 0.50 23.85 C
ANISOU 314 CD1AILE A 510 3384 2910 2768 -306 55 -52 C
ATOM 315 CD1BILE A 510 76.829 62.536 20.824 0.50 22.31 C
ANISOU 315 CD1BILE A 510 3183 2617 2678 -344 113 -115 C
ATOM 316 N LYS A 511 75.953 65.830 24.693 1.00 17.63 N
ANISOU 316 N LYS A 511 2348 2173 2176 -250 25 26 N
ATOM 317 CA LYS A 511 75.055 65.551 25.842 1.00 18.52 C
ANISOU 317 CA LYS A 511 2410 2301 2326 -273 32 27 C
ATOM 318 C LYS A 511 73.698 65.253 25.298 1.00 19.09 C
ANISOU 318 C LYS A 511 2456 2389 2410 -325 -3 -25 C
ATOM 319 O LYS A 511 73.159 66.049 24.518 1.00 19.02 O
ANISOU 319 O LYS A 511 2428 2409 2390 -315 -72 -50 O
ATOM 320 CB LYS A 511 74.997 66.748 26.780 1.00 18.13 C
ANISOU 320 CB LYS A 511 2305 2298 2288 -240 16 47 C
ATOM 321 CG LYS A 511 74.143 66.558 28.022 1.00 19.49 C
ANISOU 321 CG LYS A 511 2428 2492 2485 -271 43 40 C
ATOM 322 CD LYS A 511 74.361 67.702 28.998 1.00 20.92 C
ANISOU 322 CD LYS A 511 2570 2711 2668 -233 38 57 C
ATOM 323 CE LYS A 511 73.675 67.481 30.335 1.00 23.38 C
ANISOU 323 CE LYS A 511 2850 3046 2987 -272 85 49 C
ATOM 324 NZ LYS A 511 73.959 68.596 31.292 1.00 24.36 N
ANISOU 324 NZ LYS A 511 2946 3204 3104 -235 83 59 N
ATOM 325 N ILE A 512 73.126 64.101 25.684 1.00 18.40 N
ANISOU 325 N ILE A 512 2370 2275 2344 -384 37 -43 N
ATOM 326 CA ILE A 512 71.907 63.620 25.113 1.00 18.86 C
ANISOU 326 CA ILE A 512 2399 2346 2422 -448 10 -105 C
ATOM 327 C ILE A 512 70.885 63.483 26.246 1.00 20.46 C
ANISOU 327 C ILE A 512 2525 2580 2668 -503 48 -129 C
ATOM 328 O ILE A 512 71.093 62.740 27.202 1.00 20.90 O
ANISOU 328 O ILE A 512 2619 2601 2723 -539 121 -98 O
ATOM 329 CB ILE A 512 72.133 62.280 24.350 1.00 19.58 C
ANISOU 329 CB ILE A 512 2573 2369 2498 -492 37 -124 C
ATOM 330 CG1 ILE A 512 73.256 62.407 23.288 1.00 20.10 C
ANISOU 330 CG1 ILE A 512 2715 2407 2517 -442 26 -111 C
ATOM 331 CG2 ILE A 512 70.813 61.765 23.784 1.00 21.23 C
ANISOU 331 CG2 ILE A 512 2743 2593 2730 -572 4 -198 C
ATOM 332 CD1 ILE A 512 73.582 61.157 22.518 1.00 21.18 C
ANISOU 332 CD1 ILE A 512 2934 2474 2639 -474 59 -142 C
ATOM 333 N ILE A 513 69.770 64.165 26.082 1.00 20.03 N
ANISOU 333 N ILE A 513 2370 2591 2652 -512 -5 -189 N
ATOM 334 CA ILE A 513 68.739 64.264 27.103 1.00 21.47 C
ANISOU 334 CA ILE A 513 2452 2824 2884 -563 37 -234 C
ATOM 335 C ILE A 513 67.402 63.863 26.515 1.00 21.27 C
ANISOU 335 C ILE A 513 2338 2833 2912 -633 4 -331 C
ATOM 336 O ILE A 513 66.920 64.533 25.605 1.00 20.88 O
ANISOU 336 O ILE A 513 2233 2817 2882 -588 -104 -376 O
ATOM 337 CB ILE A 513 68.625 65.720 27.672 1.00 21.83 C
ANISOU 337 CB ILE A 513 2417 2928 2950 -490 5 -238 C
ATOM 338 CG1 ILE A 513 69.946 66.215 28.209 1.00 23.03 C
ANISOU 338 CG1 ILE A 513 2646 3052 3052 -425 27 -152 C
ATOM 339 CG2 ILE A 513 67.552 65.727 28.780 1.00 24.12 C
ANISOU 339 CG2 ILE A 513 2600 3274 3292 -553 74 -302 C
ATOM 340 CD1 ILE A 513 69.963 67.695 28.593 1.00 23.89 C
ANISOU 340 CD1 ILE A 513 2699 3203 3175 -351 -14 -156 C
ATOM 341 N ALA A 514 66.743 62.823 27.055 1.00 21.99 N
ANISOU 341 N ALA A 514 2412 2915 3028 -746 88 -369 N
ATOM 342 CA ALA A 514 65.390 62.443 26.623 1.00 24.26 C
ANISOU 342 CA ALA A 514 2588 3247 3382 -830 66 -480 C
ATOM 343 C ALA A 514 64.384 63.471 27.063 1.00 25.44 C
ANISOU 343 C ALA A 514 2565 3494 3608 -808 39 -562 C
ATOM 344 O ALA A 514 64.466 63.939 28.200 1.00 25.60 O
ANISOU 344 O ALA A 514 2559 3538 3629 -801 115 -546 O
ATOM 345 CB ALA A 514 64.978 61.087 27.175 1.00 25.14 C
ANISOU 345 CB ALA A 514 2734 3318 3499 -976 182 -500 C
ATOM 346 N ILE A 515 63.468 63.853 26.178 1.00 26.46 N
ANISOU 346 N ILE A 515 2580 3675 3799 -787 -75 -655 N
ATOM 347 CA ILE A 515 62.419 64.807 26.557 1.00 28.99 C
ANISOU 347 CA ILE A 515 2713 4086 4216 -753 -113 -755 C
ATOM 348 C ILE A 515 61.048 64.333 26.137 1.00 31.06 C
ANISOU 348 C ILE A 515 2818 4407 4575 -836 -147 -897 C
ATOM 349 O ILE A 515 60.908 63.519 25.234 1.00 30.11 O
ANISOU 349 O ILE A 515 2740 4260 4441 -890 -195 -915 O
ATOM 350 CB ILE A 515 62.672 66.229 25.961 1.00 28.92 C
ANISOU 350 CB ILE A 515 2695 4086 4208 -593 -264 -735 C
ATOM 351 CG1 ILE A 515 62.777 66.179 24.432 1.00 30.02 C
ANISOU 351 CG1 ILE A 515 2904 4193 4309 -551 -418 -725 C
ATOM 352 CG2 ILE A 515 63.913 66.880 26.565 1.00 28.61 C
ANISOU 352 CG2 ILE A 515 2771 4005 4094 -521 -219 -618 C
ATOM 353 CD1 ILE A 515 62.649 67.498 23.732 1.00 30.12 C
ANISOU 353 CD1 ILE A 515 2898 4214 4332 -415 -589 -730 C
ATOM 354 N GLU A 516 60.025 64.857 26.815 1.00 33.04 N
ANISOU 354 N GLU A 516 2879 4745 4931 -847 -120 -1011 N
ATOM 355 CA GLU A 516 58.602 64.752 26.386 1.00 35.92 C
ANISOU 355 CA GLU A 516 3034 5191 5423 -892 -186 -1178 C
ATOM 356 C GLU A 516 57.912 63.399 26.522 1.00 38.23 C
ANISOU 356 C GLU A 516 3283 5496 5748 -1084 -73 -1256 C
ATOM 357 O GLU A 516 56.695 63.305 26.309 1.00 41.79 O
ANISOU 357 O GLU A 516 3534 6028 6318 -1138 -108 -1412 O
ATOM 358 CB GLU A 516 58.399 65.300 24.941 1.00 37.44 C
ANISOU 358 CB GLU A 516 3212 5383 5631 -773 -422 -1201 C
ATOM 359 CG GLU A 516 58.766 66.785 24.811 1.00 37.16 C
ANISOU 359 CG GLU A 516 3187 5341 5592 -590 -547 -1156 C
ATOM 360 CD GLU A 516 57.724 67.744 25.401 1.00 41.44 C
ANISOU 360 CD GLU A 516 3498 5969 6278 -523 -578 -1291 C
ATOM 361 OE1 GLU A 516 56.620 67.289 25.697 1.00 45.90 O
ANISOU 361 OE1 GLU A 516 3870 6612 6956 -613 -529 -1437 O
ATOM 362 OE2 GLU A 516 57.967 68.967 25.543 1.00 42.91 O
ANISOU 362 OE2 GLU A 516 3685 6144 6475 -382 -653 -1265 O
ATOM 363 N GLY A 517 58.627 62.357 26.919 1.00 37.10 N
ANISOU 363 N GLY A 517 3314 5273 5509 -1190 62 -1160 N
ATOM 364 CA GLY A 517 58.088 61.006 27.009 1.00 39.44 C
ANISOU 364 CA GLY A 517 3615 5552 5820 -1381 171 -1216 C
ATOM 365 C GLY A 517 57.554 60.729 28.410 1.00 41.91 C
ANISOU 365 C GLY A 517 3860 5903 6162 -1521 375 -1267 C
ATOM 366 O GLY A 517 57.857 61.458 29.324 1.00 41.69 O
ANISOU 366 O GLY A 517 3832 5897 6113 -1466 439 -1230 O
ATOM 367 N PRO A 518 56.757 59.661 28.575 1.00 47.16 N
ANISOU 367 N PRO A 518 4477 6574 6866 -1716 484 -1356 N
ATOM 368 CA PRO A 518 56.198 59.378 29.898 1.00 49.29 C
ANISOU 368 CA PRO A 518 4695 6882 7152 -1875 696 -1412 C
ATOM 369 C PRO A 518 56.985 58.321 30.724 1.00 49.61 C
ANISOU 369 C PRO A 518 4996 6798 7056 -2001 860 -1275 C
ATOM 370 O PRO A 518 56.671 58.153 31.896 1.00 51.58 O
ANISOU 370 O PRO A 518 5249 7065 7284 -2128 1038 -1295 O
ATOM 371 CB PRO A 518 54.800 58.840 29.542 1.00 51.57 C
ANISOU 371 CB PRO A 518 4770 7251 7572 -2030 718 -1605 C
ATOM 372 CG PRO A 518 55.007 58.126 28.236 1.00 51.08 C
ANISOU 372 CG PRO A 518 4794 7121 7495 -2024 579 -1582 C
ATOM 373 CD PRO A 518 56.192 58.759 27.549 1.00 48.83 C
ANISOU 373 CD PRO A 518 4660 6773 7122 -1810 419 -1435 C
ATOM 374 N ASP A 519 57.967 57.618 30.134 1.00 48.76 N
ANISOU 374 N ASP A 519 5106 6563 6858 -1966 801 -1145 N
ATOM 375 CA ASP A 519 58.785 56.624 30.879 1.00 47.72 C
ANISOU 375 CA ASP A 519 5234 6296 6603 -2056 926 -1009 C
ATOM 376 C ASP A 519 59.684 57.311 31.894 1.00 46.10 C
ANISOU 376 C ASP A 519 5132 6075 6308 -1957 965 -890 C
ATOM 377 O ASP A 519 60.181 58.418 31.654 1.00 41.45 O
ANISOU 377 O ASP A 519 4491 5532 5726 -1776 854 -860 O
ATOM 378 CB ASP A 519 59.706 55.786 29.975 1.00 48.89 C
ANISOU 378 CB ASP A 519 5579 6309 6690 -2010 840 -908 C
ATOM 379 CG ASP A 519 58.950 55.080 28.854 1.00 52.22 C
ANISOU 379 CG ASP A 519 5927 6732 7184 -2098 781 -1019 C
ATOM 380 OD1 ASP A 519 57.846 54.565 29.116 1.00 53.25 O
ANISOU 380 OD1 ASP A 519 5950 6903 7379 -2281 878 -1138 O
ATOM 381 OD2 ASP A 519 59.485 55.088 27.710 1.00 55.85 O
ANISOU 381 OD2 ASP A 519 6435 7156 7631 -1985 639 -991 O
ATOM 382 N LEU A 520 59.886 56.630 33.027 1.00 44.08 N
ANISOU 382 N LEU A 520 5038 5748 5963 -2084 1119 -823 N
ATOM 383 CA LEU A 520 60.884 57.071 34.016 1.00 41.89 C
ANISOU 383 CA LEU A 520 4908 5432 5577 -2001 1146 -692 C
ATOM 384 C LEU A 520 62.233 56.854 33.423 1.00 37.94 C
ANISOU 384 C LEU A 520 4580 4820 5016 -1851 1022 -553 C
ATOM 385 O LEU A 520 62.484 55.775 32.807 1.00 39.86 O
ANISOU 385 O LEU A 520 4945 4954 5247 -1896 1002 -520 O
ATOM 386 CB LEU A 520 60.778 56.222 35.285 1.00 43.30 C
ANISOU 386 CB LEU A 520 5257 5540 5656 -2187 1326 -645 C
ATOM 387 CG LEU A 520 59.539 56.547 36.096 1.00 45.03 C
ANISOU 387 CG LEU A 520 5313 5879 5916 -2343 1485 -785 C
ATOM 388 CD1 LEU A 520 59.281 55.442 37.116 1.00 47.71 C
ANISOU 388 CD1 LEU A 520 5843 6132 6154 -2578 1675 -750 C
ATOM 389 CD2 LEU A 520 59.673 57.950 36.729 1.00 44.04 C
ANISOU 389 CD2 LEU A 520 5078 5864 5792 -2216 1475 -802 C
ATOM 390 N VAL A 521 63.123 57.807 33.665 1.00 36.10 N
ANISOU 390 N VAL A 521 4365 4606 4745 -1687 952 -477 N
ATOM 391 CA VAL A 521 64.471 57.745 33.140 1.00 32.61 C
ANISOU 391 CA VAL A 521 4060 4075 4255 -1537 841 -359 C
ATOM 392 C VAL A 521 65.395 58.098 34.278 1.00 30.94 C
ANISOU 392 C VAL A 521 3973 3833 3950 -1478 866 -250 C
ATOM 393 O VAL A 521 65.345 59.204 34.732 1.00 30.76 O
ANISOU 393 O VAL A 521 3854 3900 3933 -1415 861 -271 O
ATOM 394 CB VAL A 521 64.689 58.719 31.931 1.00 31.37 C
ANISOU 394 CB VAL A 521 3773 3984 4163 -1375 691 -392 C
ATOM 395 CG1 VAL A 521 66.127 58.667 31.472 1.00 30.30 C
ANISOU 395 CG1 VAL A 521 3776 3764 3975 -1238 604 -279 C
ATOM 396 CG2 VAL A 521 63.780 58.314 30.757 1.00 32.43 C
ANISOU 396 CG2 VAL A 521 3800 4143 4377 -1433 644 -499 C
ATOM 397 N ASN A 522 66.198 57.137 34.722 1.00 32.23 N
ANISOU 397 N ASN A 522 4352 3864 4031 -1498 885 -141 N
ATOM 398 CA ASN A 522 67.158 57.360 35.824 1.00 32.61 C
ANISOU 398 CA ASN A 522 4541 3870 3980 -1438 887 -31 C
ATOM 399 C ASN A 522 66.460 57.905 37.067 1.00 35.80 C
ANISOU 399 C ASN A 522 4909 4355 4337 -1537 1002 -67 C
ATOM 400 O ASN A 522 66.974 58.775 37.751 1.00 35.59 O
ANISOU 400 O ASN A 522 4883 4373 4266 -1455 982 -32 O
ATOM 401 CB ASN A 522 68.265 58.281 35.349 1.00 29.99 C
ANISOU 401 CB ASN A 522 4169 3564 3664 -1239 759 14 C
ATOM 402 CG ASN A 522 68.929 57.761 34.082 1.00 28.05 C
ANISOU 402 CG ASN A 522 3951 3247 3460 -1154 666 32 C
ATOM 403 OD1 ASN A 522 69.057 56.572 33.921 1.00 29.49 O
ANISOU 403 OD1 ASN A 522 4262 3316 3627 -1209 683 61 O
ATOM 404 ND2 ASN A 522 69.357 58.659 33.192 1.00 26.83 N
ANISOU 404 ND2 ASN A 522 3688 3152 3352 -1025 573 11 N
ATOM 405 N GLY A 523 65.227 57.460 37.250 1.00 39.55 N
ANISOU 405 N GLY A 523 5326 4863 4836 -1714 1124 -158 N
ATOM 406 CA GLY A 523 64.488 57.749 38.441 1.00 42.42 C
ANISOU 406 CA GLY A 523 5674 5294 5150 -1845 1268 -205 C
ATOM 407 C GLY A 523 63.689 59.008 38.446 1.00 43.76 C
ANISOU 407 C GLY A 523 5593 5627 5405 -1815 1289 -337 C
ATOM 408 O GLY A 523 62.995 59.271 39.432 1.00 48.57 O
ANISOU 408 O GLY A 523 6169 6303 5982 -1930 1426 -401 O
ATOM 409 N SER A 524 63.762 59.798 37.380 1.00 42.39 N
ANISOU 409 N SER A 524 5254 5514 5338 -1664 1158 -383 N
ATOM 410 CA SER A 524 62.919 60.955 37.236 1.00 42.91 C
ANISOU 410 CA SER A 524 5078 5720 5506 -1623 1155 -518 C
ATOM 411 C SER A 524 62.110 60.835 35.989 1.00 45.83 C
ANISOU 411 C SER A 524 5277 6132 6006 -1624 1089 -624 C
ATOM 412 O SER A 524 62.485 60.090 35.034 1.00 43.24 O
ANISOU 412 O SER A 524 5021 5725 5684 -1606 1009 -575 O
ATOM 413 CB SER A 524 63.710 62.255 37.195 1.00 42.32 C
ANISOU 413 CB SER A 524 4966 5681 5432 -1429 1042 -479 C
ATOM 414 OG SER A 524 64.271 62.517 38.458 1.00 45.16 O
ANISOU 414 OG SER A 524 5450 6030 5680 -1439 1107 -413 O
ATOM 415 N HIS A 525 60.988 61.566 36.007 1.00 45.56 N
ANISOU 415 N HIS A 525 5012 6221 6077 -1643 1120 -778 N
ATOM 416 CA HIS A 525 60.283 61.882 34.775 1.00 46.64 C
ANISOU 416 CA HIS A 525 4952 6418 6350 -1583 1003 -886 C
ATOM 417 C HIS A 525 61.179 62.756 33.864 1.00 40.47 C
ANISOU 417 C HIS A 525 4185 5616 5574 -1367 811 -813 C
ATOM 418 O HIS A 525 62.048 63.482 34.324 1.00 37.47 O
ANISOU 418 O HIS A 525 3882 5221 5134 -1261 785 -729 O
ATOM 419 CB HIS A 525 58.932 62.535 35.056 1.00 50.77 C
ANISOU 419 CB HIS A 525 5216 7076 6997 -1629 1064 -1075 C
ATOM 420 CG HIS A 525 57.930 61.574 35.575 1.00 54.84 C
ANISOU 420 CG HIS A 525 5685 7618 7532 -1860 1241 -1175 C
ATOM 421 ND1 HIS A 525 57.473 60.503 34.829 1.00 57.76 N
ANISOU 421 ND1 HIS A 525 6052 7954 7942 -1974 1235 -1209 N
ATOM 422 CD2 HIS A 525 57.294 61.504 36.766 1.00 58.22 C
ANISOU 422 CD2 HIS A 525 6078 8102 7941 -2013 1440 -1252 C
ATOM 423 CE1 HIS A 525 56.608 59.810 35.543 1.00 60.02 C
ANISOU 423 CE1 HIS A 525 6301 8270 8236 -2193 1424 -1301 C
ATOM 424 NE2 HIS A 525 56.484 60.396 36.721 1.00 61.48 N
ANISOU 424 NE2 HIS A 525 6468 8511 8382 -2223 1556 -1328 N
ATOM 425 N GLN A 526 60.941 62.622 32.557 1.00 36.98 N
ANISOU 425 N GLN A 526 3680 5173 5200 -1321 683 -848 N
ATOM 426 CA GLN A 526 61.637 63.393 31.534 1.00 35.55 C
ANISOU 426 CA GLN A 526 3514 4973 5021 -1142 507 -794 C
ATOM 427 C GLN A 526 61.143 64.794 31.535 1.00 35.78 C
ANISOU 427 C GLN A 526 3375 5089 5132 -1027 432 -876 C
ATOM 428 O GLN A 526 59.936 65.043 31.758 1.00 37.26 O
ANISOU 428 O GLN A 526 3368 5366 5425 -1074 466 -1023 O
ATOM 429 CB GLN A 526 61.341 62.805 30.145 1.00 33.79 C
ANISOU 429 CB GLN A 526 3272 4728 4837 -1149 397 -827 C
ATOM 430 CG GLN A 526 61.826 61.393 29.999 1.00 33.63 C
ANISOU 430 CG GLN A 526 3422 4608 4747 -1254 458 -756 C
ATOM 431 CD GLN A 526 61.285 60.764 28.728 1.00 33.19 C
ANISOU 431 CD GLN A 526 3326 4545 4739 -1293 370 -824 C
ATOM 432 OE1 GLN A 526 61.156 61.456 27.695 1.00 32.65 O
ANISOU 432 OE1 GLN A 526 3185 4512 4707 -1184 217 -858 O
ATOM 433 NE2 GLN A 526 60.912 59.501 28.810 1.00 34.92 N
ANISOU 433 NE2 GLN A 526 3596 4718 4955 -1451 461 -849 N
ATOM 434 N LYS A 527 62.035 65.710 31.214 1.00 35.19 N
ANISOU 434 N LYS A 527 3364 4985 5021 -875 326 -794 N
ATOM 435 CA LYS A 527 61.687 67.102 31.108 1.00 36.24 C
ANISOU 435 CA LYS A 527 3369 5174 5225 -746 232 -857 C
ATOM 436 C LYS A 527 60.953 67.352 29.813 1.00 36.74 C
ANISOU 436 C LYS A 527 3319 5262 5377 -685 70 -937 C
ATOM 437 O LYS A 527 61.130 66.597 28.849 1.00 34.18 O
ANISOU 437 O LYS A 527 3069 4896 5023 -713 9 -904 O
ATOM 438 CB LYS A 527 62.945 67.946 31.159 1.00 37.55 C
ANISOU 438 CB LYS A 527 3666 5288 5314 -622 175 -736 C
ATOM 439 CG LYS A 527 63.618 67.818 32.530 1.00 41.81 C
ANISOU 439 CG LYS A 527 4304 5813 5771 -672 316 -669 C
ATOM 440 CD LYS A 527 64.734 68.826 32.716 1.00 44.92 C
ANISOU 440 CD LYS A 527 4787 6173 6109 -552 261 -580 C
ATOM 441 CE LYS A 527 65.310 68.822 34.143 1.00 48.15 C
ANISOU 441 CE LYS A 527 5279 6578 6438 -595 383 -531 C
ATOM 442 NZ LYS A 527 64.240 68.812 35.191 1.00 51.64 N
ANISOU 442 NZ LYS A 527 5613 7093 6915 -688 512 -642 N
ATOM 443 N THR A 528 60.105 68.384 29.801 1.00 36.52 N
ANISOU 443 N THR A 528 3118 5300 5459 -600 -5 -1051 N
ATOM 444 CA THR A 528 59.547 68.926 28.571 1.00 36.58 C
ANISOU 444 CA THR A 528 3040 5319 5541 -496 -205 -1111 C
ATOM 445 C THR A 528 60.585 69.782 27.864 1.00 36.66 C
ANISOU 445 C THR A 528 3205 5253 5472 -355 -342 -988 C
ATOM 446 O THR A 528 61.599 70.204 28.465 1.00 33.63 O
ANISOU 446 O THR A 528 2942 4828 5009 -322 -280 -886 O
ATOM 447 CB THR A 528 58.328 69.835 28.822 1.00 39.10 C
ANISOU 447 CB THR A 528 3119 5721 6014 -426 -258 -1279 C
ATOM 448 OG1 THR A 528 58.714 70.927 29.684 1.00 38.39 O
ANISOU 448 OG1 THR A 528 3037 5627 5920 -337 -220 -1260 O
ATOM 449 CG2 THR A 528 57.221 69.056 29.431 1.00 39.91 C
ANISOU 449 CG2 THR A 528 3043 5912 6210 -574 -121 -1425 C
ATOM 450 N PHE A 529 60.315 70.097 26.601 1.00 39.49 N
ANISOU 450 N PHE A 529 3561 5593 5848 -275 -530 -1002 N
ATOM 451 CA PHE A 529 61.209 70.972 25.849 1.00 41.92 C
ANISOU 451 CA PHE A 529 4025 5826 6077 -155 -660 -893 C
ATOM 452 C PHE A 529 61.372 72.297 26.614 1.00 41.87 C
ANISOU 452 C PHE A 529 3989 5816 6104 -48 -662 -893 C
ATOM 453 O PHE A 529 62.497 72.810 26.801 1.00 39.08 O
ANISOU 453 O PHE A 529 3784 5404 5662 -9 -638 -779 O
ATOM 454 CB PHE A 529 60.684 71.243 24.449 1.00 46.53 C
ANISOU 454 CB PHE A 529 4606 6395 6678 -83 -876 -926 C
ATOM 455 CG PHE A 529 61.522 72.229 23.696 1.00 49.30 C
ANISOU 455 CG PHE A 529 5129 6664 6940 30 -1005 -818 C
ATOM 456 CD1 PHE A 529 62.850 71.931 23.384 1.00 50.56 C
ANISOU 456 CD1 PHE A 529 5495 6758 6958 -6 -944 -681 C
ATOM 457 CD2 PHE A 529 61.021 73.472 23.336 1.00 52.43 C
ANISOU 457 CD2 PHE A 529 5484 7042 7394 169 -1180 -857 C
ATOM 458 CE1 PHE A 529 63.650 72.845 22.700 1.00 51.99 C
ANISOU 458 CE1 PHE A 529 5839 6864 7051 75 -1041 -586 C
ATOM 459 CE2 PHE A 529 61.817 74.395 22.648 1.00 53.90 C
ANISOU 459 CE2 PHE A 529 5857 7138 7485 256 -1290 -749 C
ATOM 460 CZ PHE A 529 63.126 74.080 22.325 1.00 53.56 C
ANISOU 460 CZ PHE A 529 6018 7038 7295 199 -1213 -615 C
ATOM 461 N GLU A 530 60.261 72.816 27.122 1.00 42.34 N
ANISOU 461 N GLU A 530 3849 5941 6299 -8 -677 -1034 N
ATOM 462 CA GLU A 530 60.284 74.072 27.899 1.00 44.15 C
ANISOU 462 CA GLU A 530 4033 6165 6575 95 -674 -1060 C
ATOM 463 C GLU A 530 61.176 73.981 29.128 1.00 39.91 C
ANISOU 463 C GLU A 530 3581 5624 5959 30 -484 -987 C
ATOM 464 O GLU A 530 61.865 74.947 29.468 1.00 39.44 O
ANISOU 464 O GLU A 530 3603 5518 5863 108 -496 -930 O
ATOM 465 CB GLU A 530 58.850 74.507 28.308 1.00 49.50 C
ANISOU 465 CB GLU A 530 4453 6926 7430 140 -699 -1253 C
ATOM 466 CG GLU A 530 57.989 74.946 27.128 1.00 56.39 C
ANISOU 466 CG GLU A 530 5236 7792 8396 254 -939 -1331 C
ATOM 467 CD GLU A 530 57.378 73.784 26.296 1.00 62.00 C
ANISOU 467 CD GLU A 530 5890 8546 9122 160 -985 -1378 C
ATOM 468 OE1 GLU A 530 57.489 72.559 26.655 1.00 61.40 O
ANISOU 468 OE1 GLU A 530 5822 8505 9001 -4 -818 -1367 O
ATOM 469 OE2 GLU A 530 56.771 74.108 25.242 1.00 68.57 O
ANISOU 469 OE2 GLU A 530 6677 9366 10009 254 -1204 -1428 O
ATOM 470 N GLU A 531 61.192 72.829 29.791 1.00 37.74 N
ANISOU 470 N GLU A 531 3302 5388 5649 -116 -315 -987 N
ATOM 471 CA GLU A 531 62.020 72.645 30.993 1.00 35.30 C
ANISOU 471 CA GLU A 531 3088 5072 5253 -182 -147 -915 C
ATOM 472 C GLU A 531 63.536 72.468 30.686 1.00 32.94 C
ANISOU 472 C GLU A 531 3010 4690 4817 -175 -157 -743 C
ATOM 473 O GLU A 531 64.361 72.667 31.558 1.00 30.79 O
ANISOU 473 O GLU A 531 2821 4400 4477 -184 -72 -678 O
ATOM 474 CB GLU A 531 61.543 71.479 31.824 1.00 37.98 C
ANISOU 474 CB GLU A 531 3377 5465 5589 -343 30 -964 C
ATOM 475 CG GLU A 531 60.209 71.741 32.552 1.00 41.09 C
ANISOU 475 CG GLU A 531 3550 5955 6109 -374 107 -1144 C
ATOM 476 CD GLU A 531 59.540 70.470 33.067 1.00 44.76 C
ANISOU 476 CD GLU A 531 3956 6471 6578 -558 270 -1208 C
ATOM 477 OE1 GLU A 531 59.762 69.369 32.523 1.00 41.00 O
ANISOU 477 OE1 GLU A 531 3567 5960 6051 -645 273 -1145 O
ATOM 478 OE2 GLU A 531 58.713 70.590 34.001 1.00 47.66 O
ANISOU 478 OE2 GLU A 531 4182 6916 7009 -623 399 -1337 O
ATOM 479 N ILE A 532 63.886 72.130 29.457 1.00 31.21 N
ANISOU 479 N ILE A 532 2875 4424 4560 -158 -261 -682 N
ATOM 480 CA AILE A 532 65.307 72.042 29.040 0.50 29.50 C
ANISOU 480 CA AILE A 532 2847 4134 4229 -144 -273 -540 C
ATOM 481 CA BILE A 532 65.297 72.032 29.071 0.50 30.08 C
ANISOU 481 CA BILE A 532 2918 4208 4303 -146 -269 -541 C
ATOM 482 C ILE A 532 65.824 73.376 28.536 1.00 28.08 C
ANISOU 482 C ILE A 532 2729 3905 4034 -26 -391 -498 C
ATOM 483 O ILE A 532 67.036 73.584 28.465 1.00 26.22 O
ANISOU 483 O ILE A 532 2628 3620 3716 -14 -377 -396 O
ATOM 484 CB AILE A 532 65.503 70.989 27.928 0.50 29.53 C
ANISOU 484 CB AILE A 532 2927 4106 4186 -195 -309 -501 C
ATOM 485 CB BILE A 532 65.466 70.872 28.063 0.50 30.80 C
ANISOU 485 CB BILE A 532 3081 4272 4349 -208 -290 -505 C
ATOM 486 CG1AILE A 532 65.203 69.609 28.460 0.50 30.08 C
ANISOU 486 CG1AILE A 532 2976 4198 4255 -322 -182 -522 C
ATOM 487 CG1BILE A 532 66.931 70.474 27.928 0.50 30.95 C
ANISOU 487 CG1BILE A 532 3271 4229 4261 -221 -247 -380 C
ATOM 488 CG2AILE A 532 66.953 70.982 27.421 0.50 28.17 C
ANISOU 488 CG2AILE A 532 2930 3864 3908 -174 -317 -377 C
ATOM 489 CG2BILE A 532 64.899 71.226 26.703 0.50 31.35 C
ANISOU 489 CG2BILE A 532 3134 4333 4447 -149 -457 -541 C
ATOM 490 CD1AILE A 532 66.016 69.304 29.667 0.50 29.96 C
ANISOU 490 CD1AILE A 532 3035 4168 4180 -367 -47 -456 C
ATOM 491 CD1BILE A 532 67.549 70.052 29.221 0.50 31.87 C
ANISOU 491 CD1BILE A 532 3422 4345 4341 -272 -110 -337 C
ATOM 492 N LEU A 533 64.915 74.289 28.165 1.00 28.73 N
ANISOU 492 N LEU A 533 2717 3998 4201 62 -511 -579 N
ATOM 493 CA LEU A 533 65.368 75.549 27.616 1.00 29.53 C
ANISOU 493 CA LEU A 533 2905 4033 4282 170 -634 -532 C
ATOM 494 C LEU A 533 66.332 76.322 28.543 1.00 26.45 C
ANISOU 494 C LEU A 533 2583 3615 3851 190 -559 -476 C
ATOM 495 O LEU A 533 67.289 76.906 28.046 1.00 25.52 O
ANISOU 495 O LEU A 533 2604 3431 3663 221 -605 -387 O
ATOM 496 CB LEU A 533 64.207 76.467 27.226 1.00 32.74 C
ANISOU 496 CB LEU A 533 3199 4442 4798 279 -786 -634 C
ATOM 497 CG LEU A 533 63.743 76.275 25.791 1.00 36.94 C
ANISOU 497 CG LEU A 533 3762 4949 5324 308 -954 -637 C
ATOM 498 CD1 LEU A 533 62.403 76.953 25.618 1.00 40.78 C
ANISOU 498 CD1 LEU A 533 4090 5458 5948 413 -1099 -767 C
ATOM 499 CD2 LEU A 533 64.772 76.912 24.861 1.00 38.23 C
ANISOU 499 CD2 LEU A 533 4141 5014 5371 348 -1044 -512 C
ATOM 500 N PRO A 534 66.074 76.347 29.888 1.00 26.85 N
ANISOU 500 N PRO A 534 2542 3718 3941 163 -439 -534 N
ATOM 501 CA PRO A 534 67.024 77.051 30.742 1.00 25.98 C
ANISOU 501 CA PRO A 534 2506 3582 3782 176 -379 -482 C
ATOM 502 C PRO A 534 68.464 76.614 30.583 1.00 24.12 C
ANISOU 502 C PRO A 534 2422 3307 3434 127 -336 -356 C
ATOM 503 O PRO A 534 69.335 77.449 30.441 1.00 23.70 O
ANISOU 503 O PRO A 534 2462 3201 3341 166 -371 -298 O
ATOM 504 CB PRO A 534 66.472 76.805 32.172 1.00 26.94 C
ANISOU 504 CB PRO A 534 2519 3778 3940 125 -241 -566 C
ATOM 505 CG PRO A 534 64.990 76.753 31.943 1.00 29.62 C
ANISOU 505 CG PRO A 534 2688 4168 4397 146 -279 -698 C
ATOM 506 CD PRO A 534 64.836 76.004 30.637 1.00 28.56 C
ANISOU 506 CD PRO A 534 2581 4017 4254 130 -370 -665 C
ATOM 507 N GLU A 535 68.720 75.322 30.569 1.00 22.99 N
ANISOU 507 N GLU A 535 2302 3185 3248 44 -263 -321 N
ATOM 508 CA GLU A 535 70.064 74.848 30.375 1.00 22.54 C
ANISOU 508 CA GLU A 535 2370 3090 3103 10 -228 -218 C
ATOM 509 C GLU A 535 70.617 75.236 29.015 1.00 21.60 C
ANISOU 509 C GLU A 535 2345 2913 2947 45 -324 -164 C
ATOM 510 O GLU A 535 71.808 75.553 28.912 1.00 21.64 O
ANISOU 510 O GLU A 535 2445 2883 2897 46 -311 -96 O
ATOM 511 CB GLU A 535 70.180 73.341 30.560 1.00 23.99 C
ANISOU 511 CB GLU A 535 2568 3292 3257 -76 -143 -196 C
ATOM 512 CG GLU A 535 71.610 72.871 30.322 1.00 23.68 C
ANISOU 512 CG GLU A 535 2644 3210 3144 -91 -118 -102 C
ATOM 513 CD GLU A 535 71.829 71.393 30.582 1.00 25.18 C
ANISOU 513 CD GLU A 535 2866 3397 3306 -160 -43 -76 C
ATOM 514 OE1 GLU A 535 70.824 70.719 30.999 1.00 27.57 O
ANISOU 514 OE1 GLU A 535 3108 3729 3637 -215 2 -127 O
ATOM 515 OE2 GLU A 535 72.998 70.908 30.397 1.00 25.18 O
ANISOU 515 OE2 GLU A 535 2948 3360 3261 -162 -25 -12 O
ATOM 516 N ILE A 536 69.798 75.165 27.976 1.00 21.07 N
ANISOU 516 N ILE A 536 2260 2839 2906 65 -417 -197 N
ATOM 517 CA ILE A 536 70.236 75.610 26.649 1.00 21.57 C
ANISOU 517 CA ILE A 536 2437 2843 2916 92 -515 -147 C
ATOM 518 C ILE A 536 70.636 77.062 26.665 1.00 21.23 C
ANISOU 518 C ILE A 536 2455 2748 2865 156 -573 -123 C
ATOM 519 O ILE A 536 71.705 77.441 26.197 1.00 21.20 O
ANISOU 519 O ILE A 536 2570 2694 2789 142 -568 -53 O
ATOM 520 CB ILE A 536 69.175 75.326 25.564 1.00 22.91 C
ANISOU 520 CB ILE A 536 2582 3014 3108 107 -628 -194 C
ATOM 521 CG1 ILE A 536 68.941 73.818 25.415 1.00 24.52 C
ANISOU 521 CG1 ILE A 536 2753 3256 3307 26 -563 -212 C
ATOM 522 CG2 ILE A 536 69.557 76.026 24.270 1.00 24.49 C
ANISOU 522 CG2 ILE A 536 2925 3144 3238 141 -743 -141 C
ATOM 523 CD1 ILE A 536 67.667 73.479 24.662 1.00 25.83 C
ANISOU 523 CD1 ILE A 536 2845 3446 3522 31 -666 -289 C
ATOM 524 N ILE A 537 69.775 77.906 27.215 1.00 22.21 N
ANISOU 524 N ILE A 537 2493 2879 3068 223 -623 -189 N
ATOM 525 CA ILE A 537 70.038 79.362 27.292 1.00 22.45 C
ANISOU 525 CA ILE A 537 2583 2844 3103 291 -688 -177 C
ATOM 526 C ILE A 537 71.308 79.646 28.045 1.00 21.52 C
ANISOU 526 C ILE A 537 2525 2716 2936 251 -587 -122 C
ATOM 527 O ILE A 537 72.169 80.442 27.628 1.00 21.55 O
ANISOU 527 O ILE A 537 2649 2652 2887 252 -612 -64 O
ATOM 528 CB ILE A 537 68.828 80.064 27.922 1.00 24.61 C
ANISOU 528 CB ILE A 537 2727 3135 3490 375 -741 -281 C
ATOM 529 CG1 ILE A 537 67.642 80.013 26.948 1.00 26.48 C
ANISOU 529 CG1 ILE A 537 2913 3367 3782 434 -886 -337 C
ATOM 530 CG2 ILE A 537 69.175 81.474 28.384 1.00 24.96 C
ANISOU 530 CG2 ILE A 537 2822 3114 3548 438 -771 -280 C
ATOM 531 CD1 ILE A 537 66.318 80.401 27.579 1.00 28.90 C
ANISOU 531 CD1 ILE A 537 3039 3716 4225 510 -924 -470 C
ATOM 532 N ILE A 538 71.456 78.989 29.183 1.00 19.61 N
ANISOU 532 N ILE A 538 2206 2538 2705 208 -472 -142 N
ATOM 533 CA ILE A 538 72.627 79.240 30.027 1.00 19.56 C
ANISOU 533 CA ILE A 538 2244 2531 2658 176 -391 -101 C
ATOM 534 C ILE A 538 73.906 78.786 29.311 1.00 19.56 C
ANISOU 534 C ILE A 538 2346 2506 2581 123 -363 -19 C
ATOM 535 O ILE A 538 74.941 79.479 29.363 1.00 19.54 O
ANISOU 535 O ILE A 538 2412 2468 2545 110 -351 19 O
ATOM 536 CB ILE A 538 72.468 78.669 31.467 1.00 19.73 C
ANISOU 536 CB ILE A 538 2179 2622 2694 143 -287 -140 C
ATOM 537 CG1 ILE A 538 71.329 79.364 32.172 1.00 20.77 C
ANISOU 537 CG1 ILE A 538 2215 2777 2902 193 -299 -236 C
ATOM 538 CG2 ILE A 538 73.751 78.795 32.260 1.00 19.09 C
ANISOU 538 CG2 ILE A 538 2151 2541 2561 110 -225 -93 C
ATOM 539 CD1 ILE A 538 71.047 78.829 33.564 1.00 22.29 C
ANISOU 539 CD1 ILE A 538 2335 3039 3094 146 -185 -283 C
ATOM 540 N SER A 539 73.874 77.588 28.698 1.00 18.40 N
ANISOU 540 N SER A 539 2201 2379 2412 84 -342 -2 N
ATOM 541 CA SER A 539 75.023 77.099 27.968 1.00 18.24 C
ANISOU 541 CA SER A 539 2264 2338 2329 38 -308 57 C
ATOM 542 C SER A 539 75.430 78.109 26.867 1.00 19.68 C
ANISOU 542 C SER A 539 2559 2453 2466 43 -372 90 C
ATOM 543 O SER A 539 76.621 78.437 26.710 1.00 20.38 O
ANISOU 543 O SER A 539 2712 2519 2513 6 -328 127 O
ATOM 544 CB SER A 539 74.736 75.760 27.356 1.00 18.66 C
ANISOU 544 CB SER A 539 2309 2410 2369 5 -290 55 C
ATOM 545 OG SER A 539 74.324 74.780 28.298 1.00 19.18 O
ANISOU 545 OG SER A 539 2296 2523 2467 -14 -230 31 O
ATOM 546 N LYS A 540 74.444 78.665 26.167 1.00 20.63 N
ANISOU 546 N LYS A 540 2703 2538 2596 88 -478 72 N
ATOM 547 CA LYS A 540 74.760 79.617 25.151 1.00 22.03 C
ANISOU 547 CA LYS A 540 3017 2637 2717 89 -547 112 C
ATOM 548 C LYS A 540 75.379 80.891 25.728 1.00 22.22 C
ANISOU 548 C LYS A 540 3083 2615 2745 98 -540 126 C
ATOM 549 O LYS A 540 76.344 81.389 25.214 1.00 21.85 O
ANISOU 549 O LYS A 540 3147 2520 2636 47 -516 171 O
ATOM 550 CB LYS A 540 73.487 80.020 24.366 1.00 25.95 C
ANISOU 550 CB LYS A 540 3536 3095 3228 154 -694 89 C
ATOM 551 CG LYS A 540 73.849 81.057 23.287 1.00 32.57 C
ANISOU 551 CG LYS A 540 4557 3832 3985 151 -777 145 C
ATOM 552 CD LYS A 540 74.986 80.506 22.381 1.00 37.96 C
ANISOU 552 CD LYS A 540 5358 4508 4558 49 -693 199 C
ATOM 553 CE LYS A 540 75.382 81.410 21.221 1.00 44.38 C
ANISOU 553 CE LYS A 540 6379 5221 5263 15 -753 258 C
ATOM 554 NZ LYS A 540 74.217 81.860 20.443 1.00 49.55 N
ANISOU 554 NZ LYS A 540 7107 5816 5904 87 -932 258 N
ATOM 555 N GLU A 541 74.795 81.437 26.793 1.00 21.00 N
ANISOU 555 N GLU A 541 2842 2473 2665 155 -556 79 N
ATOM 556 CA GLU A 541 75.316 82.676 27.397 1.00 21.69 C
ANISOU 556 CA GLU A 541 2970 2510 2761 165 -555 81 C
ATOM 557 C GLU A 541 76.766 82.539 27.901 1.00 20.16 C
ANISOU 557 C GLU A 541 2787 2340 2531 87 -443 111 C
ATOM 558 O GLU A 541 77.546 83.447 27.742 1.00 20.35 O
ANISOU 558 O GLU A 541 2901 2307 2526 53 -439 136 O
ATOM 559 CB GLU A 541 74.418 83.160 28.554 1.00 23.94 C
ANISOU 559 CB GLU A 541 3146 2816 3133 238 -574 6 C
ATOM 560 CG GLU A 541 73.050 83.682 28.149 1.00 25.65 C
ANISOU 560 CG GLU A 541 3340 2994 3412 335 -700 -43 C
ATOM 561 CD GLU A 541 73.124 84.896 27.221 1.00 30.97 C
ANISOU 561 CD GLU A 541 4171 3541 4056 371 -817 -3 C
ATOM 562 OE1 GLU A 541 74.006 85.770 27.349 1.00 33.67 O
ANISOU 562 OE1 GLU A 541 4615 3816 4362 338 -795 33 O
ATOM 563 OE2 GLU A 541 72.294 84.975 26.279 1.00 39.38 O
ANISOU 563 OE2 GLU A 541 5273 4563 5126 428 -942 -4 O
ATOM 564 N LEU A 542 77.048 81.409 28.518 1.00 18.17 N
ANISOU 564 N LEU A 542 2445 2171 2288 61 -364 101 N
ATOM 565 CA LEU A 542 78.390 81.179 29.077 1.00 18.24 C
ANISOU 565 CA LEU A 542 2442 2210 2277 4 -277 118 C
ATOM 566 C LEU A 542 79.423 80.901 28.014 1.00 19.11 C
ANISOU 566 C LEU A 542 2625 2302 2333 -62 -238 158 C
ATOM 567 O LEU A 542 80.567 81.401 28.072 1.00 19.33 O
ANISOU 567 O LEU A 542 2682 2318 2345 -115 -192 166 O
ATOM 568 CB LEU A 542 78.328 80.031 30.075 1.00 18.01 C
ANISOU 568 CB LEU A 542 2312 2261 2271 7 -223 100 C
ATOM 569 CG LEU A 542 77.505 80.325 31.336 1.00 18.30 C
ANISOU 569 CG LEU A 542 2277 2327 2347 48 -229 52 C
ATOM 570 CD1 LEU A 542 77.430 79.043 32.168 1.00 18.91 C
ANISOU 570 CD1 LEU A 542 2290 2472 2423 33 -171 47 C
ATOM 571 CD2 LEU A 542 78.065 81.444 32.219 1.00 18.61 C
ANISOU 571 CD2 LEU A 542 2329 2352 2392 48 -225 33 C
ATOM 572 N SER A 543 78.971 80.218 26.982 1.00 19.50 N
ANISOU 572 N SER A 543 2710 2346 2354 -65 -256 172 N
ATOM 573 CA SER A 543 79.816 80.051 25.745 1.00 20.27 C
ANISOU 573 CA SER A 543 2902 2416 2383 -134 -216 201 C
ATOM 574 C SER A 543 80.196 81.379 25.136 1.00 21.42 C
ANISOU 574 C SER A 543 3176 2481 2480 -173 -240 228 C
ATOM 575 O SER A 543 81.362 81.595 24.748 1.00 20.39 O
ANISOU 575 O SER A 543 3095 2341 2311 -255 -163 237 O
ATOM 576 CB SER A 543 79.113 79.161 24.727 1.00 20.52 C
ANISOU 576 CB SER A 543 2965 2450 2381 -130 -246 206 C
ATOM 577 OG SER A 543 79.892 79.052 23.572 1.00 21.22 O
ANISOU 577 OG SER A 543 3155 2514 2394 -201 -199 226 O
ATOM 578 N LEU A 544 79.235 82.312 25.068 1.00 19.76 N
ANISOU 578 N LEU A 544 3023 2209 2277 -118 -344 233 N
ATOM 579 CA LEU A 544 79.529 83.623 24.478 1.00 21.52 C
ANISOU 579 CA LEU A 544 3400 2330 2448 -154 -381 267 C
ATOM 580 C LEU A 544 80.538 84.463 25.206 1.00 20.09 C
ANISOU 580 C LEU A 544 3217 2133 2284 -205 -319 259 C
ATOM 581 O LEU A 544 81.118 85.373 24.627 1.00 21.12 O
ANISOU 581 O LEU A 544 3482 2182 2358 -275 -308 288 O
ATOM 582 CB LEU A 544 78.219 84.404 24.338 1.00 23.39 C
ANISOU 582 CB LEU A 544 3687 2493 2706 -59 -527 266 C
ATOM 583 CG LEU A 544 77.298 83.900 23.244 1.00 27.29 C
ANISOU 583 CG LEU A 544 4238 2972 3159 -25 -619 281 C
ATOM 584 CD1 LEU A 544 75.935 84.590 23.447 1.00 28.24 C
ANISOU 584 CD1 LEU A 544 4342 3043 3345 97 -772 252 C
ATOM 585 CD2 LEU A 544 77.862 84.164 21.831 1.00 28.34 C
ANISOU 585 CD2 LEU A 544 4575 3030 3162 -112 -621 342 C
ATOM 586 N LEU A 545 80.720 84.199 26.489 1.00 19.26 N
ANISOU 586 N LEU A 545 2970 2098 2250 -176 -281 219 N
ATOM 587 CA LEU A 545 81.649 84.954 27.289 1.00 20.58 C
ANISOU 587 CA LEU A 545 3121 2261 2439 -222 -234 200 C
ATOM 588 C LEU A 545 83.067 84.883 26.740 1.00 20.16 C
ANISOU 588 C LEU A 545 3099 2217 2345 -339 -133 209 C
ATOM 589 O LEU A 545 83.832 85.788 27.006 1.00 20.85 O
ANISOU 589 O LEU A 545 3220 2269 2434 -403 -102 198 O
ATOM 590 CB LEU A 545 81.651 84.512 28.772 1.00 19.95 C
ANISOU 590 CB LEU A 545 2889 2266 2425 -176 -214 155 C
ATOM 591 CG LEU A 545 80.384 84.856 29.575 1.00 20.97 C
ANISOU 591 CG LEU A 545 2977 2389 2603 -80 -286 123 C
ATOM 592 CD1 LEU A 545 80.532 84.326 30.997 1.00 21.55 C
ANISOU 592 CD1 LEU A 545 2926 2550 2711 -62 -246 83 C
ATOM 593 CD2 LEU A 545 80.046 86.341 29.579 1.00 23.26 C
ANISOU 593 CD2 LEU A 545 3361 2575 2902 -58 -351 114 C
ATOM 594 N SER A 546 83.411 83.843 26.010 1.00 19.82 N
ANISOU 594 N SER A 546 3040 2220 2273 -371 -77 215 N
ATOM 595 CA SER A 546 84.774 83.772 25.433 1.00 21.43 C
ANISOU 595 CA SER A 546 3259 2438 2445 -486 35 204 C
ATOM 596 C SER A 546 85.049 84.847 24.393 1.00 23.29 C
ANISOU 596 C SER A 546 3679 2574 2598 -585 51 237 C
ATOM 597 O SER A 546 86.229 85.166 24.119 1.00 25.02 O
ANISOU 597 O SER A 546 3913 2795 2799 -702 154 216 O
ATOM 598 CB SER A 546 85.059 82.364 24.888 1.00 22.84 C
ANISOU 598 CB SER A 546 3375 2686 2618 -490 97 190 C
ATOM 599 OG SER A 546 84.256 82.141 23.713 1.00 25.69 O
ANISOU 599 OG SER A 546 3858 3002 2903 -486 59 227 O
ATOM 600 N GLY A 547 83.984 85.408 23.767 1.00 22.35 N
ANISOU 600 N GLY A 547 3706 2362 2424 -544 -51 286 N
ATOM 601 CA GLY A 547 84.093 86.371 22.708 1.00 23.63 C
ANISOU 601 CA GLY A 547 4083 2409 2487 -630 -59 334 C
ATOM 602 C GLY A 547 83.714 87.811 23.092 1.00 24.68 C
ANISOU 602 C GLY A 547 4324 2426 2628 -609 -147 356 C
ATOM 603 O GLY A 547 83.746 88.717 22.259 1.00 25.34 O
ANISOU 603 O GLY A 547 4616 2388 2625 -676 -171 405 O
ATOM 604 N GLU A 548 83.349 88.006 24.345 1.00 24.04 N
ANISOU 604 N GLU A 548 4115 2373 2646 -518 -193 318 N
ATOM 605 CA GLU A 548 82.985 89.320 24.851 1.00 24.93 C
ANISOU 605 CA GLU A 548 4308 2380 2785 -485 -272 320 C
ATOM 606 C GLU A 548 84.212 90.150 25.176 1.00 25.80 C
ANISOU 606 C GLU A 548 4451 2460 2894 -614 -180 302 C
ATOM 607 O GLU A 548 85.325 89.750 24.857 1.00 26.21 O
ANISOU 607 O GLU A 548 4470 2569 2919 -733 -56 288 O
ATOM 608 CB GLU A 548 82.066 89.174 26.042 1.00 25.25 C
ANISOU 608 CB GLU A 548 4200 2469 2926 -345 -346 274 C
ATOM 609 CG GLU A 548 80.697 88.661 25.678 1.00 26.85 C
ANISOU 609 CG GLU A 548 4389 2673 3138 -223 -454 284 C
ATOM 610 CD GLU A 548 79.866 89.704 24.883 1.00 32.66 C
ANISOU 610 CD GLU A 548 5315 3255 3838 -171 -591 325 C
ATOM 611 OE1 GLU A 548 80.292 90.814 24.644 1.00 36.48 O
ANISOU 611 OE1 GLU A 548 5955 3620 4284 -227 -602 353 O
ATOM 612 OE2 GLU A 548 78.767 89.344 24.428 1.00 43.82 O
ANISOU 612 OE2 GLU A 548 6726 4664 5258 -75 -696 329 O
ATOM 613 N VAL A 549 84.001 91.402 25.562 1.00 25.85 N
ANISOU 613 N VAL A 549 4554 2352 2917 -603 -241 302 N
ATOM 614 CA VAL A 549 85.081 92.366 25.709 1.00 27.27 C
ANISOU 614 CA VAL A 549 4807 2471 3083 -742 -164 289 C
ATOM 615 C VAL A 549 85.167 92.861 27.144 1.00 27.91 C
ANISOU 615 C VAL A 549 4769 2576 3260 -699 -180 221 C
ATOM 616 O VAL A 549 86.221 92.733 27.785 1.00 29.16 O
ANISOU 616 O VAL A 549 4809 2817 3453 -783 -89 168 O
ATOM 617 CB VAL A 549 84.917 93.580 24.720 1.00 28.76 C
ANISOU 617 CB VAL A 549 5282 2464 3181 -807 -214 357 C
ATOM 618 CG1 VAL A 549 85.959 94.628 24.957 1.00 30.18 C
ANISOU 618 CG1 VAL A 549 5542 2570 3355 -959 -133 337 C
ATOM 619 CG2 VAL A 549 84.936 93.098 23.289 1.00 29.40 C
ANISOU 619 CG2 VAL A 549 5502 2525 3144 -872 -189 423 C
ATOM 620 N CYS A 550 84.090 93.422 27.703 1.00 26.69 N
ANISOU 620 N CYS A 550 4635 2355 3152 -566 -297 210 N
ATOM 621 CA CYS A 550 84.165 94.001 29.055 1.00 26.74 C
ANISOU 621 CA CYS A 550 4553 2371 3234 -535 -306 138 C
ATOM 622 C CYS A 550 84.195 92.917 30.144 1.00 24.18 C
ANISOU 622 C CYS A 550 3996 2223 2967 -475 -273 81 C
ATOM 623 O CYS A 550 84.802 93.089 31.164 1.00 24.10 O
ANISOU 623 O CYS A 550 3896 2265 2994 -508 -237 24 O
ATOM 624 CB CYS A 550 83.013 94.967 29.364 1.00 28.76 C
ANISOU 624 CB CYS A 550 4897 2500 3530 -409 -431 125 C
ATOM 625 SG CYS A 550 82.920 96.291 28.165 1.00 35.55 S
ANISOU 625 SG CYS A 550 6063 3124 4320 -461 -500 200 S
ATOM 626 N ASN A 551 83.428 91.862 29.934 1.00 21.96 N
ANISOU 626 N ASN A 551 3637 2018 2690 -383 -299 99 N
ATOM 627 CA ASN A 551 83.427 90.708 30.787 1.00 21.25 C
ANISOU 627 CA ASN A 551 3359 2079 2635 -338 -266 63 C
ATOM 628 C ASN A 551 83.651 89.476 29.943 1.00 21.25 C
ANISOU 628 C ASN A 551 3320 2154 2601 -361 -220 103 C
ATOM 629 O ASN A 551 82.745 88.938 29.264 1.00 20.74 O
ANISOU 629 O ASN A 551 3277 2083 2519 -294 -266 136 O
ATOM 630 CB ASN A 551 82.139 90.623 31.610 1.00 21.90 C
ANISOU 630 CB ASN A 551 3373 2181 2767 -200 -335 23 C
ATOM 631 CG ASN A 551 82.167 91.558 32.758 1.00 22.79 C
ANISOU 631 CG ASN A 551 3476 2265 2919 -187 -347 -42 C
ATOM 632 OD1 ASN A 551 83.068 91.481 33.611 1.00 23.48 O
ANISOU 632 OD1 ASN A 551 3493 2420 3009 -249 -295 -78 O
ATOM 633 ND2 ASN A 551 81.253 92.510 32.775 1.00 23.57 N
ANISOU 633 ND2 ASN A 551 3652 2256 3048 -109 -423 -64 N
ATOM 634 N ARG A 552 84.924 89.035 29.954 1.00 21.67 N
ANISOU 634 N ARG A 552 3310 2276 2647 -459 -130 91 N
ATOM 635 CA AARG A 552 85.396 88.011 29.016 0.50 21.21 C
ANISOU 635 CA AARG A 552 3231 2273 2555 -504 -67 118 C
ATOM 636 CA BARG A 552 85.430 88.037 28.997 0.50 21.18 C
ANISOU 636 CA BARG A 552 3231 2267 2551 -508 -65 118 C
ATOM 637 C ARG A 552 86.102 86.924 29.777 1.00 20.92 C
ANISOU 637 C ARG A 552 3020 2366 2562 -497 -19 78 C
ATOM 638 O ARG A 552 86.923 87.204 30.588 1.00 20.67 O
ANISOU 638 O ARG A 552 2919 2371 2565 -536 3 34 O
ATOM 639 CB AARG A 552 86.346 88.553 27.954 0.50 23.40 C
ANISOU 639 CB AARG A 552 3622 2490 2778 -645 8 136 C
ATOM 640 CB BARG A 552 86.434 88.663 28.020 0.50 23.34 C
ANISOU 640 CB BARG A 552 3615 2479 2773 -654 11 132 C
ATOM 641 CG AARG A 552 86.541 87.568 26.807 0.50 24.54 C
ANISOU 641 CG AARG A 552 3780 2672 2873 -680 67 162 C
ATOM 642 CG BARG A 552 86.987 87.734 26.939 0.50 24.53 C
ANISOU 642 CG BARG A 552 3762 2678 2881 -718 96 146 C
ATOM 643 CD AARG A 552 87.691 87.939 25.892 0.50 26.82 C
ANISOU 643 CD AARG A 552 4147 2933 3110 -841 180 157 C
ATOM 644 CD BARG A 552 88.055 88.454 26.105 0.50 26.71 C
ANISOU 644 CD BARG A 552 4145 2900 3106 -885 196 143 C
ATOM 645 NE AARG A 552 88.912 87.497 26.502 0.50 29.06 N
ANISOU 645 NE AARG A 552 4259 3322 3460 -895 268 86 N
ATOM 646 NE BARG A 552 88.593 87.643 24.998 0.50 29.30 N
ANISOU 646 NE BARG A 552 4482 3269 3382 -959 296 144 N
ATOM 647 CZ AARG A 552 89.433 86.297 26.347 0.50 29.23 C
ANISOU 647 CZ AARG A 552 4152 3445 3509 -886 329 53 C
ATOM 648 CZ BARG A 552 88.185 87.718 23.720 0.50 31.91 C
ANISOU 648 CZ BARG A 552 4991 3525 3608 -1002 301 200 C
ATOM 649 NH1AARG A 552 90.539 86.027 26.993 0.50 30.46 N
ANISOU 649 NH1AARG A 552 4147 3687 3740 -921 384 -19 N
ATOM 650 NH1BARG A 552 87.185 88.533 23.354 0.50 33.47 N
ANISOU 650 NH1BARG A 552 5373 3598 3746 -962 193 267 N
ATOM 651 NH2AARG A 552 88.890 85.394 25.535 0.50 28.49 N
ANISOU 651 NH2AARG A 552 4090 3362 3372 -844 331 84 N
ATOM 652 NH2BARG A 552 88.769 86.969 22.792 0.50 33.27 N
ANISOU 652 NH2BARG A 552 5163 3744 3733 -1079 408 185 N
ATOM 653 N THR A 553 85.707 85.676 29.515 1.00 20.42 N
ANISOU 653 N THR A 553 2898 2364 2496 -440 -16 95 N
ATOM 654 CA THR A 553 86.408 84.517 30.102 1.00 20.22 C
ANISOU 654 CA THR A 553 2727 2446 2509 -426 22 65 C
ATOM 655 C THR A 553 86.249 83.314 29.157 1.00 21.38 C
ANISOU 655 C THR A 553 2867 2620 2636 -412 54 88 C
ATOM 656 O THR A 553 85.166 83.103 28.569 1.00 19.66 O
ANISOU 656 O THR A 553 2717 2368 2386 -366 14 124 O
ATOM 657 CB THR A 553 85.927 84.157 31.512 1.00 21.36 C
ANISOU 657 CB THR A 553 2784 2645 2688 -341 -31 46 C
ATOM 658 OG1 THR A 553 86.666 83.000 31.951 1.00 20.50 O
ANISOU 658 OG1 THR A 553 2562 2621 2606 -327 -8 28 O
ATOM 659 CG2 THR A 553 84.440 83.848 31.584 1.00 20.81 C
ANISOU 659 CG2 THR A 553 2739 2560 2608 -253 -84 69 C
ATOM 660 N GLU A 554 87.316 82.538 29.028 1.00 19.68 N
ANISOU 660 N GLU A 554 2565 2466 2445 -446 119 58 N
ATOM 661 CA GLU A 554 87.218 81.233 28.386 1.00 20.91 C
ANISOU 661 CA GLU A 554 2694 2655 2597 -417 148 65 C
ATOM 662 C GLU A 554 86.965 80.086 29.369 1.00 20.53 C
ANISOU 662 C GLU A 554 2544 2666 2591 -324 109 61 C
ATOM 663 O GLU A 554 87.067 78.923 28.979 1.00 19.95 O
ANISOU 663 O GLU A 554 2435 2617 2526 -299 134 58 O
ATOM 664 CB GLU A 554 88.496 80.984 27.609 1.00 23.57 C
ANISOU 664 CB GLU A 554 2996 3018 2942 -501 249 23 C
ATOM 665 CG GLU A 554 88.679 82.006 26.501 1.00 27.94 C
ANISOU 665 CG GLU A 554 3684 3505 3429 -613 304 36 C
ATOM 666 CD GLU A 554 89.964 81.869 25.725 1.00 33.61 C
ANISOU 666 CD GLU A 554 4368 4251 4150 -721 431 -21 C
ATOM 667 OE1 GLU A 554 90.615 80.786 25.788 1.00 36.61 O
ANISOU 667 OE1 GLU A 554 4620 4702 4588 -692 474 -72 O
ATOM 668 OE2 GLU A 554 90.277 82.832 24.994 1.00 34.75 O
ANISOU 668 OE2 GLU A 554 4626 4340 4236 -838 489 -15 O
ATOM 669 N GLY A 555 86.614 80.396 30.614 1.00 18.58 N
ANISOU 669 N GLY A 555 2265 2433 2361 -278 50 60 N
ATOM 670 CA GLY A 555 86.565 79.409 31.669 1.00 19.43 C
ANISOU 670 CA GLY A 555 2297 2591 2494 -210 16 57 C
ATOM 671 C GLY A 555 85.346 78.571 31.747 1.00 19.27 C
ANISOU 671 C GLY A 555 2300 2566 2455 -153 -9 90 C
ATOM 672 O GLY A 555 85.286 77.711 32.625 1.00 18.50 O
ANISOU 672 O GLY A 555 2162 2501 2366 -108 -31 95 O
ATOM 673 N PHE A 556 84.365 78.778 30.854 1.00 18.17 N
ANISOU 673 N PHE A 556 2230 2386 2287 -156 -11 112 N
ATOM 674 CA PHE A 556 83.266 77.873 30.715 1.00 18.01 C
ANISOU 674 CA PHE A 556 2218 2367 2257 -116 -27 130 C
ATOM 675 C PHE A 556 83.548 76.926 29.562 1.00 18.82 C
ANISOU 675 C PHE A 556 2335 2463 2351 -132 13 135 C
ATOM 676 O PHE A 556 84.718 76.536 29.397 1.00 18.55 O
ANISOU 676 O PHE A 556 2264 2447 2338 -150 55 117 O
ATOM 677 CB PHE A 556 81.973 78.662 30.649 1.00 18.08 C
ANISOU 677 CB PHE A 556 2270 2344 2254 -96 -72 133 C
ATOM 678 CG PHE A 556 81.736 79.391 31.931 1.00 17.86 C
ANISOU 678 CG PHE A 556 2217 2330 2241 -75 -96 112 C
ATOM 679 CD1 PHE A 556 81.178 78.742 33.002 1.00 18.18 C
ANISOU 679 CD1 PHE A 556 2213 2410 2284 -46 -96 103 C
ATOM 680 CD2 PHE A 556 82.152 80.699 32.083 1.00 18.67 C
ANISOU 680 CD2 PHE A 556 2348 2401 2344 -96 -109 98 C
ATOM 681 CE1 PHE A 556 81.004 79.384 34.232 1.00 19.09 C
ANISOU 681 CE1 PHE A 556 2313 2542 2398 -35 -107 76 C
ATOM 682 CE2 PHE A 556 82.007 81.341 33.323 1.00 18.15 C
ANISOU 682 CE2 PHE A 556 2260 2349 2287 -80 -126 68 C
ATOM 683 CZ PHE A 556 81.435 80.691 34.380 1.00 17.88 C
ANISOU 683 CZ PHE A 556 2182 2362 2250 -48 -124 55 C
ATOM 684 N ILE A 557 82.565 76.591 28.738 1.00 18.69 N
ANISOU 684 N ILE A 557 2367 2423 2311 -127 -1 149 N
ATOM 685 CA ILE A 557 82.832 75.672 27.636 1.00 18.48 C
ANISOU 685 CA ILE A 557 2364 2390 2268 -148 39 146 C
ATOM 686 C ILE A 557 82.043 76.161 26.435 1.00 19.10 C
ANISOU 686 C ILE A 557 2536 2428 2295 -172 11 159 C
ATOM 687 O ILE A 557 80.936 76.683 26.569 1.00 18.96 O
ANISOU 687 O ILE A 557 2538 2393 2274 -144 -55 168 O
ATOM 688 CB ILE A 557 82.474 74.221 28.054 1.00 18.78 C
ANISOU 688 CB ILE A 557 2362 2445 2330 -111 42 145 C
ATOM 689 CG1 ILE A 557 83.079 73.162 27.084 1.00 19.82 C
ANISOU 689 CG1 ILE A 557 2505 2567 2459 -126 95 127 C
ATOM 690 CG2 ILE A 557 80.976 74.014 28.194 1.00 18.89 C
ANISOU 690 CG2 ILE A 557 2387 2454 2337 -92 -3 154 C
ATOM 691 CD1 ILE A 557 84.591 73.122 27.016 1.00 21.02 C
ANISOU 691 CD1 ILE A 557 2611 2735 2641 -137 150 96 C
ATOM 692 N GLY A 558 82.622 75.969 25.257 1.00 19.21 N
ANISOU 692 N GLY A 558 2607 2425 2266 -222 59 153 N
ATOM 693 CA GLY A 558 81.910 76.361 24.033 1.00 20.22 C
ANISOU 693 CA GLY A 558 2850 2509 2324 -248 21 171 C
ATOM 694 C GLY A 558 80.742 75.446 23.688 1.00 19.66 C
ANISOU 694 C GLY A 558 2781 2440 2249 -215 -29 168 C
ATOM 695 O GLY A 558 80.834 74.236 23.839 1.00 21.05 O
ANISOU 695 O GLY A 558 2905 2642 2453 -205 8 149 O
ATOM 696 N LEU A 559 79.669 76.034 23.215 1.00 19.53 N
ANISOU 696 N LEU A 559 2826 2392 2203 -199 -119 182 N
ATOM 697 CA LEU A 559 78.494 75.332 22.759 1.00 19.97 C
ANISOU 697 CA LEU A 559 2883 2451 2255 -176 -182 169 C
ATOM 698 C LEU A 559 78.458 75.459 21.246 1.00 20.25 C
ANISOU 698 C LEU A 559 3057 2446 2194 -221 -208 180 C
ATOM 699 O LEU A 559 78.428 76.609 20.671 1.00 22.25 O
ANISOU 699 O LEU A 559 3421 2647 2387 -235 -263 210 O
ATOM 700 CB LEU A 559 77.225 75.937 23.330 1.00 21.10 C
ANISOU 700 CB LEU A 559 2980 2593 2445 -115 -282 161 C
ATOM 701 CG LEU A 559 75.915 75.338 22.804 1.00 21.99 C
ANISOU 701 CG LEU A 559 3078 2713 2565 -95 -362 133 C
ATOM 702 CD1 LEU A 559 75.771 73.899 23.220 1.00 22.73 C
ANISOU 702 CD1 LEU A 559 3089 2850 2696 -111 -299 106 C
ATOM 703 CD2 LEU A 559 74.712 76.122 23.324 1.00 23.13 C
ANISOU 703 CD2 LEU A 559 3162 2857 2770 -29 -462 108 C
ATOM 704 N ASN A 560 78.524 74.344 20.553 1.00 19.40 N
ANISOU 704 N ASN A 560 2967 2350 2056 -252 -170 158 N
ATOM 705 CA ASN A 560 78.574 74.384 19.090 1.00 20.95 C
ANISOU 705 CA ASN A 560 3309 2510 2140 -307 -183 162 C
ATOM 706 C ASN A 560 77.204 74.302 18.455 1.00 21.17 C
ANISOU 706 C ASN A 560 3380 2523 2139 -281 -318 157 C
ATOM 707 O ASN A 560 76.949 74.986 17.456 1.00 21.54 O
ANISOU 707 O ASN A 560 3570 2522 2090 -301 -395 182 O
ATOM 708 CB ASN A 560 79.409 73.260 18.542 1.00 22.61 C
ANISOU 708 CB ASN A 560 3529 2738 2324 -359 -67 127 C
ATOM 709 CG ASN A 560 80.875 73.360 18.930 1.00 24.96 C
ANISOU 709 CG ASN A 560 3785 3053 2648 -389 62 116 C
ATOM 710 OD1 ASN A 560 81.387 74.414 19.285 1.00 26.92 O
ANISOU 710 OD1 ASN A 560 4040 3291 2897 -402 74 140 O
ATOM 711 ND2 ASN A 560 81.538 72.245 18.856 1.00 26.72 N
ANISOU 711 ND2 ASN A 560 3958 3296 2898 -399 155 71 N
ATOM 712 N SER A 561 76.324 73.455 18.984 1.00 20.83 N
ANISOU 712 N SER A 561 3224 2516 2174 -242 -350 123 N
ATOM 713 CA SER A 561 75.018 73.274 18.398 1.00 21.13 C
ANISOU 713 CA SER A 561 3275 2551 2203 -221 -478 99 C
ATOM 714 C SER A 561 74.056 72.638 19.363 1.00 20.89 C
ANISOU 714 C SER A 561 3084 2566 2285 -182 -498 57 C
ATOM 715 O SER A 561 74.476 72.002 20.316 1.00 20.07 O
ANISOU 715 O SER A 561 2891 2490 2243 -187 -399 50 O
ATOM 716 CB SER A 561 75.104 72.428 17.133 1.00 22.97 C
ANISOU 716 CB SER A 561 3612 2773 2341 -282 -469 78 C
ATOM 717 OG SER A 561 75.474 71.098 17.385 1.00 22.55 O
ANISOU 717 OG SER A 561 3495 2747 2327 -310 -361 42 O
ATOM 718 N VAL A 562 72.780 72.778 19.031 1.00 22.21 N
ANISOU 718 N VAL A 562 3227 2738 2472 -151 -630 25 N
ATOM 719 CA VAL A 562 71.713 72.147 19.740 1.00 22.83 C
ANISOU 719 CA VAL A 562 3156 2864 2653 -134 -650 -33 C
ATOM 720 C VAL A 562 70.711 71.616 18.744 1.00 23.72 C
ANISOU 720 C VAL A 562 3284 2983 2746 -149 -759 -82 C
ATOM 721 O VAL A 562 70.277 72.329 17.785 1.00 23.93 O
ANISOU 721 O VAL A 562 3400 2979 2714 -121 -900 -77 O
ATOM 722 CB VAL A 562 70.998 73.129 20.680 1.00 24.62 C
ANISOU 722 CB VAL A 562 3277 3108 2971 -62 -709 -50 C
ATOM 723 CG1 VAL A 562 69.921 72.405 21.445 1.00 27.30 C
ANISOU 723 CG1 VAL A 562 3453 3505 3414 -65 -700 -123 C
ATOM 724 CG2 VAL A 562 71.992 73.721 21.647 1.00 25.67 C
ANISOU 724 CG2 VAL A 562 3405 3234 3115 -51 -613 -5 C
ATOM 725 N HIS A 563 70.364 70.332 18.880 1.00 23.12 N
ANISOU 725 N HIS A 563 3140 2936 2707 -199 -704 -130 N
ATOM 726 CA HIS A 563 69.361 69.729 18.031 1.00 24.99 C
ANISOU 726 CA HIS A 563 3371 3186 2938 -225 -804 -192 C
ATOM 727 C HIS A 563 68.310 68.991 18.835 1.00 25.13 C
ANISOU 727 C HIS A 563 3218 3256 3075 -246 -789 -267 C
ATOM 728 O HIS A 563 68.580 68.491 19.937 1.00 23.37 O
ANISOU 728 O HIS A 563 2921 3048 2909 -270 -661 -262 O
ATOM 729 CB HIS A 563 69.954 68.734 17.038 1.00 27.32 C
ANISOU 729 CB HIS A 563 3789 3454 3136 -298 -754 -193 C
ATOM 730 CG HIS A 563 70.866 69.355 16.025 1.00 30.28 C
ANISOU 730 CG HIS A 563 4346 3784 3377 -303 -764 -138 C
ATOM 731 ND1 HIS A 563 72.217 69.543 16.240 1.00 32.07 N
ANISOU 731 ND1 HIS A 563 4635 3988 3563 -316 -633 -85 N
ATOM 732 CD2 HIS A 563 70.616 69.785 14.763 1.00 34.93 C
ANISOU 732 CD2 HIS A 563 5073 4344 3853 -310 -887 -134 C
ATOM 733 CE1 HIS A 563 72.751 70.116 15.179 1.00 33.88 C
ANISOU 733 CE1 HIS A 563 5028 4180 3666 -339 -659 -53 C
ATOM 734 NE2 HIS A 563 71.806 70.262 14.265 1.00 35.72 N
ANISOU 734 NE2 HIS A 563 5325 4405 3843 -336 -813 -75 N
ATOM 735 N CYS A 564 67.132 68.919 18.247 1.00 25.38 N
ANISOU 735 N CYS A 564 3194 3312 3136 -243 -922 -338 N
ATOM 736 CA CYS A 564 66.103 67.996 18.734 1.00 27.14 C
ANISOU 736 CA CYS A 564 3265 3586 3461 -297 -900 -428 C
ATOM 737 C CYS A 564 66.066 66.828 17.754 1.00 27.22 C
ANISOU 737 C CYS A 564 3353 3579 3411 -380 -905 -460 C
ATOM 738 O CYS A 564 65.811 66.994 16.532 1.00 27.26 O
ANISOU 738 O CYS A 564 3446 3571 3342 -372 -1040 -476 O
ATOM 739 CB CYS A 564 64.753 68.667 18.816 1.00 30.32 C
ANISOU 739 CB CYS A 564 3517 4040 3965 -241 -1044 -512 C
ATOM 740 SG CYS A 564 63.434 67.549 19.431 1.00 33.78 S
ANISOU 740 SG CYS A 564 3744 4551 4538 -332 -997 -644 S
ATOM 741 N VAL A 565 66.322 65.610 18.262 1.00 26.20 N
ANISOU 741 N VAL A 565 3210 3441 3304 -462 -761 -471 N
ATOM 742 CA VAL A 565 66.378 64.450 17.414 1.00 26.89 C
ANISOU 742 CA VAL A 565 3380 3500 3339 -542 -747 -504 C
ATOM 743 C VAL A 565 65.281 63.479 17.831 1.00 26.57 C
ANISOU 743 C VAL A 565 3208 3492 3396 -627 -727 -598 C
ATOM 744 O VAL A 565 64.831 63.524 18.983 1.00 25.69 O
ANISOU 744 O VAL A 565 2966 3415 3381 -637 -661 -616 O
ATOM 745 CB VAL A 565 67.735 63.728 17.474 1.00 28.90 C
ANISOU 745 CB VAL A 565 3760 3691 3529 -569 -598 -443 C
ATOM 746 CG1 VAL A 565 68.850 64.666 17.074 1.00 29.26 C
ANISOU 746 CG1 VAL A 565 3922 3713 3485 -504 -597 -364 C
ATOM 747 CG2 VAL A 565 68.004 63.218 18.843 1.00 29.55 C
ANISOU 747 CG2 VAL A 565 3775 3767 3687 -588 -458 -419 C
ATOM 748 N GLN A 566 64.897 62.615 16.915 1.00 26.35 N
ANISOU 748 N GLN A 566 3223 3450 3337 -697 -772 -660 N
ATOM 749 CA GLN A 566 63.877 61.633 17.174 1.00 27.48 C
ANISOU 749 CA GLN A 566 3256 3619 3568 -799 -751 -757 C
ATOM 750 C GLN A 566 64.393 60.258 16.794 1.00 27.52 C
ANISOU 750 C GLN A 566 3383 3552 3523 -891 -654 -763 C
ATOM 751 O GLN A 566 64.939 60.083 15.695 1.00 28.64 O
ANISOU 751 O GLN A 566 3667 3654 3560 -886 -696 -754 O
ATOM 752 CB GLN A 566 62.608 61.954 16.387 1.00 30.35 C
ANISOU 752 CB GLN A 566 3520 4043 3968 -798 -939 -860 C
ATOM 753 CG GLN A 566 61.442 61.001 16.656 1.00 32.71 C
ANISOU 753 CG GLN A 566 3672 4382 4375 -917 -921 -983 C
ATOM 754 CD GLN A 566 60.151 61.534 16.056 1.00 37.61 C
ANISOU 754 CD GLN A 566 4146 5081 5062 -891 -1123 -1095 C
ATOM 755 OE1 GLN A 566 60.110 61.760 14.909 1.00 40.74 O
ANISOU 755 OE1 GLN A 566 4630 5470 5379 -857 -1278 -1105 O
ATOM 756 NE2 GLN A 566 59.094 61.674 16.847 1.00 41.24 N
ANISOU 756 NE2 GLN A 566 4383 5617 5668 -915 -1118 -1189 N
ATOM 757 N GLY A 567 64.120 59.266 17.633 1.00 26.41 N
ANISOU 757 N GLY A 567 3191 3390 3453 -984 -532 -790 N
ATOM 758 CA GLY A 567 64.482 57.893 17.348 1.00 26.48 C
ANISOU 758 CA GLY A 567 3312 3316 3432 -1075 -445 -806 C
ATOM 759 C GLY A 567 64.765 57.048 18.558 1.00 26.12 C
ANISOU 759 C GLY A 567 3276 3212 3436 -1135 -281 -771 C
ATOM 760 O GLY A 567 64.815 57.550 19.693 1.00 26.82 O
ANISOU 760 O GLY A 567 3295 3327 3567 -1105 -221 -722 O
ATOM 761 N SER A 568 64.941 55.757 18.343 1.00 26.97 N
ANISOU 761 N SER A 568 3483 3232 3531 -1221 -212 -795 N
ATOM 762 CA SER A 568 65.372 54.915 19.463 1.00 27.30 C
ANISOU 762 CA SER A 568 3581 3191 3603 -1267 -65 -743 C
ATOM 763 C SER A 568 66.862 55.135 19.635 1.00 25.52 C
ANISOU 763 C SER A 568 3471 2906 3321 -1150 -17 -638 C
ATOM 764 O SER A 568 67.519 55.732 18.759 1.00 25.32 O
ANISOU 764 O SER A 568 3492 2897 3232 -1065 -77 -623 O
ATOM 765 CB SER A 568 65.090 53.451 19.166 1.00 29.09 C
ANISOU 765 CB SER A 568 3890 3322 3839 -1394 -13 -804 C
ATOM 766 OG SER A 568 65.565 53.125 17.881 1.00 29.54 O
ANISOU 766 OG SER A 568 4055 3339 3830 -1370 -67 -836 O
ATOM 767 N TYR A 569 67.431 54.711 20.762 1.00 25.36 N
ANISOU 767 N TYR A 569 3498 2819 3317 -1146 86 -567 N
ATOM 768 CA TYR A 569 68.825 55.042 21.009 1.00 24.14 C
ANISOU 768 CA TYR A 569 3421 2627 3126 -1025 116 -477 C
ATOM 769 C TYR A 569 69.679 54.249 20.021 1.00 24.86 C
ANISOU 769 C TYR A 569 3642 2626 3176 -1002 128 -497 C
ATOM 770 O TYR A 569 69.483 53.033 19.885 1.00 25.27 O
ANISOU 770 O TYR A 569 3772 2587 3244 -1080 168 -537 O
ATOM 771 CB TYR A 569 69.231 54.661 22.458 1.00 24.30 C
ANISOU 771 CB TYR A 569 3477 2586 3170 -1025 207 -399 C
ATOM 772 CG TYR A 569 70.045 55.640 23.172 1.00 23.02 C
ANISOU 772 CG TYR A 569 3288 2462 2994 -916 208 -317 C
ATOM 773 CD1 TYR A 569 69.495 56.830 23.625 1.00 22.74 C
ANISOU 773 CD1 TYR A 569 3130 2538 2972 -897 175 -313 C
ATOM 774 CD2 TYR A 569 71.382 55.418 23.404 1.00 22.44 C
ANISOU 774 CD2 TYR A 569 3305 2318 2905 -824 236 -254 C
ATOM 775 CE1 TYR A 569 70.219 57.723 24.328 1.00 22.13 C
ANISOU 775 CE1 TYR A 569 3034 2493 2883 -807 179 -244 C
ATOM 776 CE2 TYR A 569 72.132 56.316 24.118 1.00 22.50 C
ANISOU 776 CE2 TYR A 569 3282 2364 2904 -732 234 -185 C
ATOM 777 CZ TYR A 569 71.575 57.479 24.557 1.00 21.45 C
ANISOU 777 CZ TYR A 569 3040 2336 2774 -726 206 -178 C
ATOM 778 OH TYR A 569 72.288 58.380 25.251 1.00 23.36 O
ANISOU 778 OH TYR A 569 3255 2614 3006 -643 203 -118 O
ATOM 779 N PRO A 570 70.671 54.909 19.382 1.00 24.68 N
ANISOU 779 N PRO A 570 3650 2623 3103 -900 106 -473 N
ATOM 780 CA PRO A 570 71.506 54.126 18.472 1.00 25.12 C
ANISOU 780 CA PRO A 570 3824 2596 3124 -882 137 -509 C
ATOM 781 C PRO A 570 72.254 52.960 19.144 1.00 25.61 C
ANISOU 781 C PRO A 570 3975 2525 3229 -865 221 -483 C
ATOM 782 O PRO A 570 72.883 53.160 20.189 1.00 25.00 O
ANISOU 782 O PRO A 570 3888 2431 3180 -798 252 -406 O
ATOM 783 CB PRO A 570 72.491 55.170 17.936 1.00 24.57 C
ANISOU 783 CB PRO A 570 3756 2580 2999 -782 122 -481 C
ATOM 784 CG PRO A 570 71.718 56.465 18.014 1.00 24.42 C
ANISOU 784 CG PRO A 570 3636 2676 2967 -780 38 -461 C
ATOM 785 CD PRO A 570 70.935 56.352 19.285 1.00 23.80 C
ANISOU 785 CD PRO A 570 3474 2609 2962 -819 52 -435 C
ATOM 786 N PRO A 571 72.228 51.806 18.548 1.00 27.71 N
ANISOU 786 N PRO A 571 4336 2696 3498 -915 247 -547 N
ATOM 787 CA PRO A 571 72.986 50.657 19.097 1.00 28.09 C
ANISOU 787 CA PRO A 571 4488 2594 3589 -883 313 -527 C
ATOM 788 C PRO A 571 74.475 50.929 19.306 1.00 27.28 C
ANISOU 788 C PRO A 571 4400 2468 3498 -738 341 -484 C
ATOM 789 O PRO A 571 75.071 50.441 20.280 1.00 27.23 O
ANISOU 789 O PRO A 571 4435 2373 3538 -681 366 -426 O
ATOM 790 CB PRO A 571 72.778 49.589 18.040 1.00 30.32 C
ANISOU 790 CB PRO A 571 4867 2794 3861 -949 326 -627 C
ATOM 791 CG PRO A 571 71.388 49.895 17.501 1.00 30.88 C
ANISOU 791 CG PRO A 571 4871 2957 3903 -1072 265 -685 C
ATOM 792 CD PRO A 571 71.255 51.386 17.517 1.00 28.27 C
ANISOU 792 CD PRO A 571 4422 2779 3542 -1022 206 -644 C
ATOM 793 N LEU A 572 75.073 51.772 18.478 1.00 26.53 N
ANISOU 793 N LEU A 572 4267 2456 3359 -679 333 -507 N
ATOM 794 CA LEU A 572 76.468 52.110 18.732 1.00 26.72 C
ANISOU 794 CA LEU A 572 4276 2472 3403 -553 365 -477 C
ATOM 795 C LEU A 572 76.673 52.945 19.984 1.00 26.63 C
ANISOU 795 C LEU A 572 4187 2515 3417 -498 345 -377 C
ATOM 796 O LEU A 572 77.728 52.859 20.659 1.00 26.78 O
ANISOU 796 O LEU A 572 4203 2490 3481 -399 361 -340 O
ATOM 797 CB LEU A 572 77.101 52.798 17.519 1.00 28.67 C
ANISOU 797 CB LEU A 572 4512 2791 3589 -525 383 -534 C
ATOM 798 CG LEU A 572 77.444 51.864 16.353 1.00 30.53 C
ANISOU 798 CG LEU A 572 4841 2954 3805 -541 432 -642 C
ATOM 799 CD1 LEU A 572 77.617 52.671 15.086 1.00 30.72 C
ANISOU 799 CD1 LEU A 572 4873 3071 3729 -566 439 -694 C
ATOM 800 CD2 LEU A 572 78.688 51.018 16.637 1.00 32.79 C
ANISOU 800 CD2 LEU A 572 5158 3130 4171 -436 496 -670 C
ATOM 801 N LEU A 573 75.695 53.782 20.330 1.00 23.73 N
ANISOU 801 N LEU A 573 3749 2242 3025 -557 302 -341 N
ATOM 802 CA LEU A 573 75.797 54.476 21.591 1.00 23.27 C
ANISOU 802 CA LEU A 573 3629 2225 2986 -517 289 -256 C
ATOM 803 C LEU A 573 75.596 53.499 22.768 1.00 23.74 C
ANISOU 803 C LEU A 573 3751 2182 3086 -540 308 -208 C
ATOM 804 O LEU A 573 76.224 53.675 23.821 1.00 23.56 O
ANISOU 804 O LEU A 573 3727 2143 3081 -473 306 -139 O
ATOM 805 CB LEU A 573 74.787 55.608 21.693 1.00 23.04 C
ANISOU 805 CB LEU A 573 3507 2317 2930 -567 243 -242 C
ATOM 806 CG LEU A 573 75.067 56.802 20.775 1.00 23.25 C
ANISOU 806 CG LEU A 573 3488 2438 2907 -531 210 -258 C
ATOM 807 CD1 LEU A 573 74.140 57.915 21.136 1.00 22.84 C
ANISOU 807 CD1 LEU A 573 3347 2485 2848 -555 154 -235 C
ATOM 808 CD2 LEU A 573 76.514 57.293 20.866 1.00 24.05 C
ANISOU 808 CD2 LEU A 573 3584 2542 3010 -431 241 -230 C
ATOM 809 N LEU A 574 74.672 52.574 22.616 1.00 24.31 N
ANISOU 809 N LEU A 574 3881 2193 3163 -645 322 -244 N
ATOM 810 CA LEU A 574 74.469 51.504 23.649 1.00 26.69 C
ANISOU 810 CA LEU A 574 4281 2371 3490 -689 350 -200 C
ATOM 811 C LEU A 574 75.781 50.731 23.854 1.00 28.25 C
ANISOU 811 C LEU A 574 4576 2437 3722 -572 355 -177 C
ATOM 812 O LEU A 574 76.141 50.399 24.976 1.00 26.81 O
ANISOU 812 O LEU A 574 4456 2179 3550 -536 348 -102 O
ATOM 813 CB LEU A 574 73.317 50.559 23.335 1.00 28.74 C
ANISOU 813 CB LEU A 574 4594 2573 3753 -835 374 -255 C
ATOM 814 CG LEU A 574 71.944 51.267 23.366 1.00 29.71 C
ANISOU 814 CG LEU A 574 4600 2824 3863 -950 363 -283 C
ATOM 815 CD1 LEU A 574 70.851 50.390 22.848 1.00 31.46 C
ANISOU 815 CD1 LEU A 574 4851 3007 4097 -1096 379 -363 C
ATOM 816 CD2 LEU A 574 71.611 51.777 24.765 1.00 30.62 C
ANISOU 816 CD2 LEU A 574 4676 2984 3976 -972 385 -209 C
ATOM 817 N LYS A 575 76.498 50.457 22.765 1.00 28.55 N
ANISOU 817 N LYS A 575 4626 2447 3774 -511 362 -249 N
ATOM 818 CA LYS A 575 77.789 49.775 22.888 1.00 31.54 C
ANISOU 818 CA LYS A 575 5069 2710 4205 -382 364 -250 C
ATOM 819 C LYS A 575 78.779 50.602 23.727 1.00 28.87 C
ANISOU 819 C LYS A 575 4659 2425 3884 -261 333 -183 C
ATOM 820 O LYS A 575 79.456 50.059 24.636 1.00 29.12 O
ANISOU 820 O LYS A 575 4754 2354 3955 -177 302 -131 O
ATOM 821 CB LYS A 575 78.361 49.497 21.484 1.00 35.61 C
ANISOU 821 CB LYS A 575 5586 3213 4730 -345 396 -361 C
ATOM 822 CG LYS A 575 79.833 49.101 21.422 1.00 42.11 C
ANISOU 822 CG LYS A 575 6418 3961 5622 -192 405 -394 C
ATOM 823 CD LYS A 575 80.241 48.799 19.963 1.00 46.54 C
ANISOU 823 CD LYS A 575 6985 4517 6180 -184 461 -523 C
ATOM 824 CE LYS A 575 81.305 47.720 19.886 1.00 51.62 C
ANISOU 824 CE LYS A 575 7688 5011 6913 -64 479 -585 C
ATOM 825 NZ LYS A 575 82.587 48.268 20.418 1.00 54.48 N
ANISOU 825 NZ LYS A 575 7950 5410 7338 84 463 -568 N
ATOM 826 N ALA A 576 78.859 51.899 23.463 1.00 25.82 N
ANISOU 826 N ALA A 576 4152 2191 3467 -251 329 -183 N
ATOM 827 CA ALA A 576 79.683 52.765 24.262 1.00 25.21 C
ANISOU 827 CA ALA A 576 4001 2175 3403 -158 300 -126 C
ATOM 828 C ALA A 576 79.196 52.828 25.729 1.00 24.52 C
ANISOU 828 C ALA A 576 3946 2073 3298 -186 267 -25 C
ATOM 829 O ALA A 576 79.993 52.932 26.640 1.00 23.55 O
ANISOU 829 O ALA A 576 3826 1926 3195 -97 228 29 O
ATOM 830 CB ALA A 576 79.733 54.132 23.688 1.00 25.21 C
ANISOU 830 CB ALA A 576 3886 2325 3366 -164 307 -144 C
ATOM 831 N TRP A 577 77.886 52.866 25.918 1.00 23.75 N
ANISOU 831 N TRP A 577 3862 2005 3159 -314 283 -11 N
ATOM 832 CA TRP A 577 77.296 52.926 27.257 1.00 23.27 C
ANISOU 832 CA TRP A 577 3837 1938 3067 -368 277 70 C
ATOM 833 C TRP A 577 77.737 51.658 28.039 1.00 24.76 C
ANISOU 833 C TRP A 577 4184 1953 3271 -338 262 121 C
ATOM 834 O TRP A 577 78.170 51.747 29.202 1.00 24.99 O
ANISOU 834 O TRP A 577 4259 1954 3281 -290 225 200 O
ATOM 835 CB TRP A 577 75.800 52.971 27.129 1.00 23.44 C
ANISOU 835 CB TRP A 577 3838 2009 3059 -521 314 45 C
ATOM 836 CG TRP A 577 75.091 53.328 28.402 1.00 23.20 C
ANISOU 836 CG TRP A 577 3807 2016 2992 -593 331 105 C
ATOM 837 CD1 TRP A 577 74.665 54.546 28.754 1.00 23.00 C
ANISOU 837 CD1 TRP A 577 3667 2126 2948 -606 329 111 C
ATOM 838 CD2 TRP A 577 74.696 52.438 29.436 1.00 24.33 C
ANISOU 838 CD2 TRP A 577 4082 2055 3108 -672 361 160 C
ATOM 839 NE1 TRP A 577 74.046 54.491 29.970 1.00 23.83 N
ANISOU 839 NE1 TRP A 577 3810 2228 3016 -685 363 158 N
ATOM 840 CE2 TRP A 577 74.064 53.208 30.425 1.00 24.00 C
ANISOU 840 CE2 TRP A 577 3991 2104 3024 -734 386 193 C
ATOM 841 CE3 TRP A 577 74.859 51.091 29.653 1.00 25.95 C
ANISOU 841 CE3 TRP A 577 4455 2090 3315 -695 370 185 C
ATOM 842 CZ2 TRP A 577 73.575 52.647 31.593 1.00 25.12 C
ANISOU 842 CZ2 TRP A 577 4250 2178 3115 -832 432 250 C
ATOM 843 CZ3 TRP A 577 74.347 50.546 30.818 1.00 26.97 C
ANISOU 843 CZ3 TRP A 577 4711 2143 3392 -794 405 251 C
ATOM 844 CH2 TRP A 577 73.739 51.357 31.767 1.00 26.22 C
ANISOU 844 CH2 TRP A 577 4564 2153 3246 -863 439 283 C
ATOM 845 N ASP A 578 77.631 50.530 27.382 1.00 25.93 N
ANISOU 845 N ASP A 578 4423 1983 3445 -363 281 74 N
ATOM 846 CA ASP A 578 77.989 49.209 27.986 1.00 29.19 C
ANISOU 846 CA ASP A 578 5014 2201 3877 -336 260 117 C
ATOM 847 C ASP A 578 79.470 49.225 28.399 1.00 31.34 C
ANISOU 847 C ASP A 578 5288 2424 4195 -150 187 146 C
ATOM 848 O ASP A 578 79.811 48.772 29.516 1.00 32.05 O
ANISOU 848 O ASP A 578 5496 2410 4272 -106 132 231 O
ATOM 849 CB ASP A 578 77.728 48.102 27.021 1.00 29.76 C
ANISOU 849 CB ASP A 578 5167 2159 3981 -380 292 41 C
ATOM 850 CG ASP A 578 76.280 47.794 26.896 1.00 31.29 C
ANISOU 850 CG ASP A 578 5393 2360 4136 -571 350 22 C
ATOM 851 OD1 ASP A 578 75.471 48.198 27.775 1.00 32.25 O
ANISOU 851 OD1 ASP A 578 5505 2540 4209 -673 371 78 O
ATOM 852 OD2 ASP A 578 75.921 47.120 25.935 1.00 32.06 O
ANISOU 852 OD2 ASP A 578 5522 2405 4254 -628 378 -58 O
ATOM 853 N HIS A 579 80.342 49.771 27.541 1.00 30.19 N
ANISOU 853 N HIS A 579 5015 2356 4101 -45 183 74 N
ATOM 854 CA HIS A 579 81.760 49.814 27.859 1.00 31.54 C
ANISOU 854 CA HIS A 579 5154 2497 4335 129 118 77 C
ATOM 855 C HIS A 579 82.045 50.632 29.096 1.00 31.20 C
ANISOU 855 C HIS A 579 5077 2520 4256 166 58 167 C
ATOM 856 O HIS A 579 82.825 50.220 29.957 1.00 32.21 O
ANISOU 856 O HIS A 579 5274 2556 4410 274 -26 218 O
ATOM 857 CB HIS A 579 82.581 50.327 26.674 1.00 33.67 C
ANISOU 857 CB HIS A 579 5279 2854 4660 204 152 -31 C
ATOM 858 CG HIS A 579 84.049 50.348 26.936 1.00 36.18 C
ANISOU 858 CG HIS A 579 5534 3150 5062 378 95 -53 C
ATOM 859 ND1 HIS A 579 84.822 49.207 26.903 1.00 40.43 N
ANISOU 859 ND1 HIS A 579 6144 3529 5687 497 55 -93 N
ATOM 860 CD2 HIS A 579 84.873 51.346 27.327 1.00 38.50 C
ANISOU 860 CD2 HIS A 579 5699 3554 5377 455 61 -45 C
ATOM 861 CE1 HIS A 579 86.066 49.507 27.227 1.00 40.60 C
ANISOU 861 CE1 HIS A 579 6068 3573 5787 647 -5 -116 C
ATOM 862 NE2 HIS A 579 86.125 50.800 27.477 1.00 40.62 N
ANISOU 862 NE2 HIS A 579 5945 3740 5747 617 1 -89 N
ATOM 863 N TYR A 580 81.437 51.799 29.191 1.00 27.64 N
ANISOU 863 N TYR A 580 4527 2225 3749 85 91 183 N
ATOM 864 CA TYR A 580 81.544 52.609 30.384 1.00 27.03 C
ANISOU 864 CA TYR A 580 4428 2215 3625 98 45 262 C
ATOM 865 C TYR A 580 81.011 51.843 31.629 1.00 28.06 C
ANISOU 865 C TYR A 580 4740 2229 3693 40 17 360 C
ATOM 866 O TYR A 580 81.633 51.888 32.699 1.00 29.52 O
ANISOU 866 O TYR A 580 4980 2379 3858 114 -63 429 O
ATOM 867 CB TYR A 580 80.769 53.856 30.245 1.00 25.49 C
ANISOU 867 CB TYR A 580 4120 2184 3382 5 93 255 C
ATOM 868 CG TYR A 580 80.822 54.855 31.347 1.00 25.47 C
ANISOU 868 CG TYR A 580 4076 2269 3331 10 61 317 C
ATOM 869 CD1 TYR A 580 79.968 54.753 32.471 1.00 26.82 C
ANISOU 869 CD1 TYR A 580 4343 2423 3425 -84 70 388 C
ATOM 870 CD2 TYR A 580 81.645 55.991 31.258 1.00 24.87 C
ANISOU 870 CD2 TYR A 580 3866 2303 3279 87 34 296 C
ATOM 871 CE1 TYR A 580 79.967 55.722 33.464 1.00 26.44 C
ANISOU 871 CE1 TYR A 580 4260 2463 3324 -88 50 433 C
ATOM 872 CE2 TYR A 580 81.670 56.956 32.250 1.00 25.10 C
ANISOU 872 CE2 TYR A 580 3860 2414 3263 85 5 344 C
ATOM 873 CZ TYR A 580 80.832 56.811 33.382 1.00 26.75 C
ANISOU 873 CZ TYR A 580 4170 2602 3393 2 10 412 C
ATOM 874 OH TYR A 580 80.790 57.791 34.382 1.00 28.46 O
ANISOU 874 OH TYR A 580 4357 2903 3555 -9 -9 450 O
ATOM 875 N ASN A 581 79.859 51.191 31.496 1.00 28.39 N
ANISOU 875 N ASN A 581 4875 2215 3696 -100 82 363 N
ATOM 876 CA ASN A 581 79.295 50.478 32.663 1.00 29.39 C
ANISOU 876 CA ASN A 581 5188 2230 3748 -185 78 454 C
ATOM 877 C ASN A 581 80.248 49.377 33.131 1.00 33.01 C
ANISOU 877 C ASN A 581 5813 2495 4233 -64 -16 503 C
ATOM 878 O ASN A 581 80.429 49.167 34.346 1.00 32.92 O
ANISOU 878 O ASN A 581 5941 2410 4156 -52 -78 600 O
ATOM 879 CB ASN A 581 77.935 49.925 32.327 1.00 29.47 C
ANISOU 879 CB ASN A 581 5256 2213 3728 -367 175 429 C
ATOM 880 CG ASN A 581 77.263 49.251 33.531 1.00 30.47 C
ANISOU 880 CG ASN A 581 5578 2233 3765 -489 199 518 C
ATOM 881 OD1 ASN A 581 77.130 49.842 34.579 1.00 30.85 O
ANISOU 881 OD1 ASN A 581 5643 2340 3739 -519 196 580 O
ATOM 882 ND2 ASN A 581 76.868 48.076 33.352 1.00 32.04 N
ANISOU 882 ND2 ASN A 581 5928 2281 3967 -564 227 518 N
ATOM 883 N SER A 582 80.886 48.714 32.186 1.00 34.47 N
ANISOU 883 N SER A 582 5987 2598 4511 32 -35 434 N
ATOM 884 CA SER A 582 81.823 47.620 32.506 1.00 39.42 C
ANISOU 884 CA SER A 582 6761 3029 5189 171 -135 461 C
ATOM 885 C SER A 582 83.104 48.078 33.176 1.00 40.86 C
ANISOU 885 C SER A 582 6888 3231 5406 351 -259 490 C
ATOM 886 O SER A 582 83.708 47.318 33.870 1.00 43.79 O
ANISOU 886 O SER A 582 7406 3445 5786 452 -368 547 O
ATOM 887 CB SER A 582 82.214 46.893 31.252 1.00 41.00 C
ANISOU 887 CB SER A 582 6933 3152 5493 237 -113 354 C
ATOM 888 OG SER A 582 81.164 46.062 30.870 1.00 44.80 O
ANISOU 888 OG SER A 582 7538 3541 5945 87 -35 343 O
ATOM 889 N THR A 583 83.542 49.285 32.920 1.00 40.42 N
ANISOU 889 N THR A 583 6626 3358 5375 395 -251 445 N
ATOM 890 CA THR A 583 84.846 49.740 33.348 1.00 42.89 C
ANISOU 890 CA THR A 583 6847 3704 5746 568 -363 440 C
ATOM 891 C THR A 583 84.727 50.703 34.525 1.00 44.06 C
ANISOU 891 C THR A 583 6988 3955 5798 532 -405 525 C
ATOM 892 O THR A 583 85.485 50.597 35.484 1.00 46.21 O
ANISOU 892 O THR A 583 7323 4171 6063 639 -535 582 O
ATOM 893 CB THR A 583 85.599 50.394 32.156 1.00 42.08 C
ANISOU 893 CB THR A 583 6512 3726 5749 644 -317 312 C
ATOM 894 OG1 THR A 583 84.768 51.390 31.556 1.00 40.98 O
ANISOU 894 OG1 THR A 583 6262 3751 5558 507 -203 284 O
ATOM 895 CG2 THR A 583 85.943 49.343 31.109 1.00 43.80 C
ANISOU 895 CG2 THR A 583 6751 3826 6066 709 -291 219 C
ATOM 896 N LYS A 584 83.783 51.631 34.467 1.00 41.76 N
ANISOU 896 N LYS A 584 6623 3808 5434 388 -305 528 N
ATOM 897 CA LYS A 584 83.568 52.602 35.511 1.00 42.50 C
ANISOU 897 CA LYS A 584 6704 4007 5437 341 -324 591 C
ATOM 898 C LYS A 584 82.314 52.354 36.337 1.00 42.62 C
ANISOU 898 C LYS A 584 6883 3988 5324 173 -265 672 C
ATOM 899 O LYS A 584 82.275 52.757 37.494 1.00 44.49 O
ANISOU 899 O LYS A 584 7189 4248 5468 151 -305 743 O
ATOM 900 CB LYS A 584 83.507 53.985 34.932 1.00 44.47 C
ANISOU 900 CB LYS A 584 6739 4451 5706 314 -260 526 C
ATOM 901 CG LYS A 584 84.758 54.346 34.167 1.00 47.67 C
ANISOU 901 CG LYS A 584 6979 4905 6227 454 -297 442 C
ATOM 902 CD LYS A 584 84.869 55.823 33.957 1.00 50.50 C
ANISOU 902 CD LYS A 584 7163 5442 6584 431 -261 404 C
ATOM 903 CE LYS A 584 86.167 56.161 33.207 1.00 56.06 C
ANISOU 903 CE LYS A 584 7705 6194 7401 552 -283 313 C
ATOM 904 NZ LYS A 584 86.117 57.527 32.588 1.00 57.36 N
ANISOU 904 NZ LYS A 584 7713 6518 7564 498 -211 263 N
ATOM 905 N GLY A 585 81.329 51.626 35.812 1.00 40.24 N
ANISOU 905 N GLY A 585 6655 3622 5011 52 -171 658 N
ATOM 906 CA GLY A 585 80.054 51.464 36.519 1.00 37.92 C
ANISOU 906 CA GLY A 585 6486 3318 4605 -133 -86 712 C
ATOM 907 C GLY A 585 79.152 52.671 36.285 1.00 35.20 C
ANISOU 907 C GLY A 585 5969 3166 4239 -241 15 661 C
ATOM 908 O GLY A 585 79.578 53.798 36.341 1.00 34.93 O
ANISOU 908 O GLY A 585 5792 3264 4218 -179 -11 640 O
ATOM 909 N SER A 586 77.878 52.407 36.045 1.00 33.87 N
ANISOU 909 N SER A 586 5819 3007 4044 -406 126 635 N
ATOM 910 CA SER A 586 76.876 53.448 35.814 1.00 30.72 C
ANISOU 910 CA SER A 586 5259 2778 3637 -510 216 576 C
ATOM 911 C SER A 586 75.825 53.497 36.907 1.00 30.55 C
ANISOU 911 C SER A 586 5320 2775 3512 -672 300 612 C
ATOM 912 O SER A 586 75.427 52.479 37.362 1.00 33.48 O
ANISOU 912 O SER A 586 5868 3023 3831 -768 335 655 O
ATOM 913 CB SER A 586 76.150 53.146 34.503 1.00 29.19 C
ANISOU 913 CB SER A 586 4980 2599 3511 -576 279 488 C
ATOM 914 OG SER A 586 75.299 54.240 34.276 1.00 28.48 O
ANISOU 914 OG SER A 586 4725 2673 3425 -643 335 430 O
ATOM 915 N ALA A 587 75.359 54.666 37.272 1.00 31.26 N
ANISOU 915 N ALA A 587 5284 3016 3577 -709 341 583 N
ATOM 916 CA ALA A 587 74.153 54.798 38.140 1.00 31.70 C
ANISOU 916 CA ALA A 587 5375 3119 3551 -884 455 579 C
ATOM 917 C ALA A 587 72.862 54.951 37.311 1.00 32.66 C
ANISOU 917 C ALA A 587 5347 3327 3736 -1004 555 474 C
ATOM 918 O ALA A 587 71.762 55.139 37.882 1.00 33.58 O
ANISOU 918 O ALA A 587 5440 3505 3812 -1153 663 437 O
ATOM 919 CB ALA A 587 74.325 56.002 39.032 1.00 32.69 C
ANISOU 919 CB ALA A 587 5439 3361 3621 -854 446 590 C
ATOM 920 N ASN A 588 72.968 54.862 35.980 1.00 29.07 N
ANISOU 920 N ASN A 588 4789 2879 3378 -945 519 415 N
ATOM 921 CA ASN A 588 71.811 55.039 35.115 1.00 28.01 C
ANISOU 921 CA ASN A 588 4508 2828 3306 -1040 582 312 C
ATOM 922 C ASN A 588 71.210 53.765 34.601 1.00 27.85 C
ANISOU 922 C ASN A 588 4573 2703 3306 -1154 630 286 C
ATOM 923 O ASN A 588 71.824 52.751 34.580 1.00 28.84 O
ANISOU 923 O ASN A 588 4859 2682 3419 -1128 600 340 O
ATOM 924 CB ASN A 588 72.188 55.912 33.918 1.00 25.43 C
ANISOU 924 CB ASN A 588 4012 2593 3058 -917 510 256 C
ATOM 925 CG ASN A 588 72.237 57.382 34.253 1.00 24.66 C
ANISOU 925 CG ASN A 588 3779 2632 2958 -856 492 242 C
ATOM 926 OD1 ASN A 588 71.992 57.798 35.394 1.00 26.53 O
ANISOU 926 OD1 ASN A 588 4036 2907 3138 -900 533 265 O
ATOM 927 ND2 ASN A 588 72.558 58.186 33.263 1.00 22.60 N
ANISOU 927 ND2 ASN A 588 3395 2439 2752 -761 432 201 N
ATOM 928 N ASP A 589 69.952 53.826 34.199 1.00 29.21 N
ANISOU 928 N ASP A 589 4632 2949 3516 -1285 703 193 N
ATOM 929 CA ASP A 589 69.345 52.749 33.425 1.00 30.11 C
ANISOU 929 CA ASP A 589 4785 2986 3670 -1390 736 140 C
ATOM 930 C ASP A 589 69.947 52.688 31.999 1.00 28.38 C
ANISOU 930 C ASP A 589 4511 2752 3518 -1268 644 104 C
ATOM 931 O ASP A 589 70.162 53.729 31.369 1.00 28.03 O
ANISOU 931 O ASP A 589 4319 2822 3509 -1165 585 69 O
ATOM 932 CB ASP A 589 67.869 52.950 33.249 1.00 31.90 C
ANISOU 932 CB ASP A 589 4864 3319 3938 -1549 819 29 C
ATOM 933 CG ASP A 589 67.127 52.992 34.546 1.00 34.12 C
ANISOU 933 CG ASP A 589 5177 3628 4159 -1697 939 34 C
ATOM 934 OD1 ASP A 589 67.199 51.987 35.280 1.00 37.21 O
ANISOU 934 OD1 ASP A 589 5775 3885 4477 -1798 1001 102 O
ATOM 935 OD2 ASP A 589 66.500 54.030 34.800 1.00 35.05 O
ANISOU 935 OD2 ASP A 589 5122 3895 4300 -1708 970 -31 O
ATOM 936 N ARG A 590 70.168 51.468 31.505 1.00 28.61 N
ANISOU 936 N ARG A 590 4674 2638 3559 -1293 640 108 N
ATOM 937 CA ARG A 590 70.628 51.311 30.113 1.00 28.76 C
ANISOU 937 CA ARG A 590 4652 2642 3635 -1203 574 55 C
ATOM 938 C ARG A 590 69.562 51.897 29.204 1.00 28.09 C
ANISOU 938 C ARG A 590 4386 2694 3595 -1270 576 -56 C
ATOM 939 O ARG A 590 68.408 51.461 29.293 1.00 28.43 O
ANISOU 939 O ARG A 590 4405 2745 3651 -1432 640 -115 O
ATOM 940 CB ARG A 590 70.885 49.862 29.780 1.00 29.74 C
ANISOU 940 CB ARG A 590 4950 2583 3766 -1236 582 61 C
ATOM 941 CG ARG A 590 71.551 49.605 28.432 1.00 30.30 C
ANISOU 941 CG ARG A 590 5008 2621 3884 -1132 523 7 C
ATOM 942 CD ARG A 590 71.905 48.142 28.325 1.00 32.90 C
ANISOU 942 CD ARG A 590 5531 2747 4222 -1150 532 20 C
ATOM 943 NE ARG A 590 72.705 47.836 27.152 1.00 33.47 N
ANISOU 943 NE ARG A 590 5608 2773 4337 -1036 486 -33 N
ATOM 944 CZ ARG A 590 72.242 47.438 25.979 1.00 34.77 C
ANISOU 944 CZ ARG A 590 5748 2935 4526 -1095 494 -132 C
ATOM 945 NH1 ARG A 590 70.941 47.275 25.755 1.00 35.50 N
ANISOU 945 NH1 ARG A 590 5797 3073 4620 -1267 534 -195 N
ATOM 946 NH2 ARG A 590 73.104 47.201 25.000 1.00 35.58 N
ANISOU 946 NH2 ARG A 590 5866 2995 4656 -983 461 -179 N
ATOM 947 N PRO A 591 69.948 52.830 28.315 1.00 27.00 N
ANISOU 947 N PRO A 591 4128 2652 3480 -1153 503 -88 N
ATOM 948 CA PRO A 591 68.931 53.578 27.550 1.00 27.90 C
ANISOU 948 CA PRO A 591 4069 2901 3630 -1197 477 -184 C
ATOM 949 C PRO A 591 68.402 52.815 26.344 1.00 29.58 C
ANISOU 949 C PRO A 591 4287 3080 3871 -1268 459 -272 C
ATOM 950 O PRO A 591 68.399 53.341 25.249 1.00 31.39 O
ANISOU 950 O PRO A 591 4441 3375 4110 -1213 387 -324 O
ATOM 951 CB PRO A 591 69.660 54.865 27.148 1.00 27.12 C
ANISOU 951 CB PRO A 591 3883 2896 3526 -1044 402 -165 C
ATOM 952 CG PRO A 591 71.117 54.521 27.169 1.00 25.72 C
ANISOU 952 CG PRO A 591 3824 2623 3326 -927 385 -93 C
ATOM 953 CD PRO A 591 71.296 53.419 28.173 1.00 26.44 C
ANISOU 953 CD PRO A 591 4064 2583 3398 -979 441 -33 C
ATOM 954 N ASP A 592 67.987 51.580 26.535 1.00 29.78 N
ANISOU 954 N ASP A 592 4417 2997 3901 -1393 520 -287 N
ATOM 955 CA ASP A 592 67.612 50.715 25.457 1.00 30.84 C
ANISOU 955 CA ASP A 592 4585 3074 4057 -1464 506 -369 C
ATOM 956 C ASP A 592 66.103 50.568 25.306 1.00 31.27 C
ANISOU 956 C ASP A 592 4527 3200 4154 -1635 532 -474 C
ATOM 957 O ASP A 592 65.630 49.761 24.498 1.00 33.25 O
ANISOU 957 O ASP A 592 4804 3403 4425 -1726 525 -554 O
ATOM 958 CB ASP A 592 68.276 49.334 25.626 1.00 33.24 C
ANISOU 958 CB ASP A 592 5100 3183 4347 -1480 547 -324 C
ATOM 959 CG ASP A 592 67.962 48.657 26.954 1.00 35.20 C
ANISOU 959 CG ASP A 592 5461 3339 4575 -1595 637 -262 C
ATOM 960 OD1 ASP A 592 66.960 48.998 27.637 1.00 35.97 O
ANISOU 960 OD1 ASP A 592 5471 3522 4675 -1718 696 -285 O
ATOM 961 OD2 ASP A 592 68.701 47.716 27.309 1.00 37.95 O
ANISOU 961 OD2 ASP A 592 5999 3518 4903 -1568 652 -195 O
ATOM 962 N PHE A 593 65.338 51.297 26.085 1.00 30.08 N
ANISOU 962 N PHE A 593 4246 3161 4022 -1687 566 -489 N
ATOM 963 CA PHE A 593 63.904 51.133 26.171 1.00 31.54 C
ANISOU 963 CA PHE A 593 4306 3416 4261 -1859 612 -597 C
ATOM 964 C PHE A 593 63.137 52.247 25.408 1.00 30.63 C
ANISOU 964 C PHE A 593 3966 3472 4202 -1815 512 -698 C
ATOM 965 O PHE A 593 61.933 52.216 25.351 1.00 32.70 O
ANISOU 965 O PHE A 593 4087 3812 4528 -1937 526 -810 O
ATOM 966 CB PHE A 593 63.455 51.144 27.651 1.00 32.42 C
ANISOU 966 CB PHE A 593 4419 3538 4362 -1966 737 -565 C
ATOM 967 CG PHE A 593 63.940 52.336 28.417 1.00 32.06 C
ANISOU 967 CG PHE A 593 4316 3575 4288 -1840 726 -496 C
ATOM 968 CD1 PHE A 593 63.201 53.518 28.461 1.00 32.78 C
ANISOU 968 CD1 PHE A 593 4191 3831 4431 -1815 699 -570 C
ATOM 969 CD2 PHE A 593 65.192 52.315 29.059 1.00 31.00 C
ANISOU 969 CD2 PHE A 593 4342 3352 4083 -1729 728 -362 C
ATOM 970 CE1 PHE A 593 63.662 54.639 29.147 1.00 32.30 C
ANISOU 970 CE1 PHE A 593 4086 3839 4346 -1698 688 -513 C
ATOM 971 CE2 PHE A 593 65.664 53.397 29.733 1.00 30.60 C
ANISOU 971 CE2 PHE A 593 4243 3377 4007 -1619 712 -306 C
ATOM 972 CZ PHE A 593 64.929 54.601 29.785 1.00 31.89 C
ANISOU 972 CZ PHE A 593 4201 3701 4216 -1601 695 -377 C
ATOM 973 N PHE A 594 63.856 53.191 24.842 1.00 28.32 N
ANISOU 973 N PHE A 594 3648 3228 3886 -1643 410 -660 N
ATOM 974 CA PHE A 594 63.260 54.271 24.094 1.00 28.30 C
ANISOU 974 CA PHE A 594 3471 3361 3921 -1580 294 -736 C
ATOM 975 C PHE A 594 62.765 53.764 22.731 1.00 29.09 C
ANISOU 975 C PHE A 594 3559 3458 4035 -1627 205 -833 C
ATOM 976 O PHE A 594 63.410 52.956 22.101 1.00 29.44 O
ANISOU 976 O PHE A 594 3753 3400 4035 -1626 204 -812 O
ATOM 977 CB PHE A 594 64.282 55.327 23.868 1.00 26.14 C
ANISOU 977 CB PHE A 594 3219 3112 3600 -1399 221 -654 C
ATOM 978 CG PHE A 594 64.696 56.050 25.117 1.00 26.30 C
ANISOU 978 CG PHE A 594 3225 3159 3610 -1341 281 -574 C
ATOM 979 CD1 PHE A 594 63.769 56.741 25.875 1.00 26.62 C
ANISOU 979 CD1 PHE A 594 3109 3302 3703 -1379 309 -626 C
ATOM 980 CD2 PHE A 594 66.003 56.043 25.490 1.00 25.14 C
ANISOU 980 CD2 PHE A 594 3210 2938 3403 -1246 305 -462 C
ATOM 981 CE1 PHE A 594 64.181 57.442 27.000 1.00 27.16 C
ANISOU 981 CE1 PHE A 594 3174 3394 3751 -1325 363 -558 C
ATOM 982 CE2 PHE A 594 66.413 56.691 26.630 1.00 25.37 C
ANISOU 982 CE2 PHE A 594 3234 2990 3415 -1196 349 -392 C
ATOM 983 CZ PHE A 594 65.509 57.411 27.380 1.00 25.57 C
ANISOU 983 CZ PHE A 594 3121 3115 3479 -1236 379 -437 C
ATOM 984 N LYS A 595 61.560 54.187 22.345 1.00 29.57 N
ANISOU 984 N LYS A 595 3438 3631 4164 -1677 133 -952 N
ATOM 985 CA LYS A 595 61.006 53.836 21.076 1.00 30.00 C
ANISOU 985 CA LYS A 595 3467 3701 4231 -1718 24 -1053 C
ATOM 986 C LYS A 595 61.417 54.766 19.962 1.00 28.50 C
ANISOU 986 C LYS A 595 3283 3557 3990 -1567 -136 -1040 C
ATOM 987 O LYS A 595 61.970 55.835 20.198 1.00 27.46 O
ANISOU 987 O LYS A 595 3139 3463 3833 -1434 -168 -965 O
ATOM 988 CB LYS A 595 59.483 53.874 21.192 1.00 32.31 C
ANISOU 988 CB LYS A 595 3546 4100 4632 -1840 5 -1198 C
ATOM 989 CG LYS A 595 58.911 53.091 22.299 1.00 34.30 C
ANISOU 989 CG LYS A 595 3771 4327 4935 -2013 174 -1229 C
ATOM 990 CD LYS A 595 59.370 51.685 22.312 1.00 36.17 C
ANISOU 990 CD LYS A 595 4210 4409 5123 -2125 273 -1191 C
ATOM 991 CE LYS A 595 58.571 51.009 23.404 1.00 39.19 C
ANISOU 991 CE LYS A 595 4552 4780 5559 -2324 436 -1236 C
ATOM 992 NZ LYS A 595 58.487 49.595 23.177 1.00 41.28 N
ANISOU 992 NZ LYS A 595 4960 4913 5812 -2483 504 -1262 N
ATOM 993 N ASP A 596 61.062 54.357 18.743 1.00 29.68 N
ANISOU 993 N ASP A 596 3453 3703 4120 -1604 -239 -1120 N
ATOM 994 CA ASP A 596 61.439 55.137 17.546 1.00 29.41 C
ANISOU 994 CA ASP A 596 3464 3700 4011 -1481 -396 -1110 C
ATOM 995 C ASP A 596 60.755 56.542 17.426 1.00 30.51 C
ANISOU 995 C ASP A 596 3438 3963 4191 -1384 -543 -1141 C
ATOM 996 O ASP A 596 61.202 57.366 16.627 1.00 30.78 O
ANISOU 996 O ASP A 596 3535 4011 4150 -1269 -662 -1101 O
ATOM 997 CB ASP A 596 61.299 54.336 16.271 1.00 30.35 C
ANISOU 997 CB ASP A 596 3677 3778 4077 -1546 -469 -1185 C
ATOM 998 CG ASP A 596 59.879 53.908 15.972 1.00 31.64 C
ANISOU 998 CG ASP A 596 3693 4003 4325 -1674 -543 -1335 C
ATOM 999 OD1 ASP A 596 58.947 54.160 16.777 1.00 32.09 O
ANISOU 999 OD1 ASP A 596 3561 4138 4495 -1725 -522 -1392 O
ATOM 1000 OD2 ASP A 596 59.674 53.229 14.953 1.00 32.22 O
ANISOU 1000 OD2 ASP A 596 3836 4047 4358 -1740 -610 -1409 O
ATOM 1001 N ASP A 597 59.784 56.855 18.303 1.00 30.94 N
ANISOU 1001 N ASP A 597 3295 4098 4361 -1424 -519 -1204 N
ATOM 1002 CA ASP A 597 59.222 58.219 18.365 1.00 31.04 C
ANISOU 1002 CA ASP A 597 3149 4215 4429 -1311 -645 -1232 C
ATOM 1003 C ASP A 597 59.766 59.063 19.465 1.00 29.38 C
ANISOU 1003 C ASP A 597 2920 4015 4228 -1223 -558 -1140 C
ATOM 1004 O ASP A 597 59.385 60.224 19.583 1.00 29.79 O
ANISOU 1004 O ASP A 597 2854 4138 4326 -1120 -653 -1158 O
ATOM 1005 CB ASP A 597 57.680 58.158 18.455 1.00 33.56 C
ANISOU 1005 CB ASP A 597 3228 4636 4889 -1395 -705 -1397 C
ATOM 1006 CG ASP A 597 57.194 57.668 19.800 1.00 35.16 C
ANISOU 1006 CG ASP A 597 3317 4859 5185 -1520 -514 -1437 C
ATOM 1007 OD1 ASP A 597 57.922 56.932 20.468 1.00 34.43 O
ANISOU 1007 OD1 ASP A 597 3364 4679 5040 -1587 -344 -1350 O
ATOM 1008 OD2 ASP A 597 56.036 57.934 20.186 1.00 38.29 O
ANISOU 1008 OD2 ASP A 597 3484 5355 5710 -1566 -528 -1566 O
ATOM 1009 N GLN A 598 60.714 58.547 20.245 1.00 27.18 N
ANISOU 1009 N GLN A 598 2769 3658 3900 -1248 -394 -1038 N
ATOM 1010 CA GLN A 598 61.267 59.298 21.336 1.00 26.01 C
ANISOU 1010 CA GLN A 598 2612 3518 3752 -1173 -313 -953 C
ATOM 1011 C GLN A 598 62.008 60.559 20.866 1.00 25.85 C
ANISOU 1011 C GLN A 598 2644 3506 3671 -1007 -422 -875 C
ATOM 1012 O GLN A 598 62.845 60.493 19.974 1.00 24.66 O
ANISOU 1012 O GLN A 598 2644 3299 3426 -961 -470 -818 O
ATOM 1013 CB GLN A 598 62.263 58.426 22.139 1.00 25.13 C
ANISOU 1013 CB GLN A 598 2657 3308 3585 -1222 -144 -852 C
ATOM 1014 CG GLN A 598 62.888 59.084 23.378 1.00 24.32 C
ANISOU 1014 CG GLN A 598 2561 3208 3472 -1159 -55 -762 C
ATOM 1015 CD GLN A 598 61.883 59.444 24.494 1.00 25.39 C
ANISOU 1015 CD GLN A 598 2527 3427 3695 -1218 15 -831 C
ATOM 1016 OE1 GLN A 598 61.064 58.631 24.908 1.00 27.94 O
ANISOU 1016 OE1 GLN A 598 2791 3757 4067 -1363 102 -905 O
ATOM 1017 NE2 GLN A 598 61.953 60.649 24.937 1.00 25.72 N
ANISOU 1017 NE2 GLN A 598 2493 3527 3753 -1113 -17 -814 N
ATOM 1018 N LEU A 599 61.772 61.682 21.553 1.00 25.72 N
ANISOU 1018 N LEU A 599 2517 3551 3706 -927 -440 -873 N
ATOM 1019 CA LEU A 599 62.544 62.885 21.341 1.00 25.13 C
ANISOU 1019 CA LEU A 599 2505 3469 3575 -783 -515 -789 C
ATOM 1020 C LEU A 599 63.691 63.035 22.343 1.00 23.92 C
ANISOU 1020 C LEU A 599 2441 3272 3376 -753 -381 -676 C
ATOM 1021 O LEU A 599 63.571 62.654 23.489 1.00 23.74 O
ANISOU 1021 O LEU A 599 2376 3255 3389 -814 -253 -676 O
ATOM 1022 CB LEU A 599 61.641 64.104 21.463 1.00 26.55 C
ANISOU 1022 CB LEU A 599 2519 3729 3841 -699 -631 -858 C
ATOM 1023 CG LEU A 599 60.455 64.184 20.538 1.00 29.22 C
ANISOU 1023 CG LEU A 599 2741 4121 4242 -698 -799 -978 C
ATOM 1024 CD1 LEU A 599 59.647 65.468 20.768 1.00 31.04 C
ANISOU 1024 CD1 LEU A 599 2803 4419 4572 -587 -919 -1046 C
ATOM 1025 CD2 LEU A 599 60.863 64.055 19.092 1.00 29.39 C
ANISOU 1025 CD2 LEU A 599 2918 4093 4155 -673 -933 -945 C
ATOM 1026 N PHE A 600 64.785 63.621 21.881 1.00 22.94 N
ANISOU 1026 N PHE A 600 2443 3106 3167 -662 -418 -585 N
ATOM 1027 CA PHE A 600 65.935 63.961 22.663 1.00 22.66 C
ANISOU 1027 CA PHE A 600 2483 3037 3090 -613 -327 -485 C
ATOM 1028 C PHE A 600 66.414 65.359 22.270 1.00 22.93 C
ANISOU 1028 C PHE A 600 2545 3079 3088 -496 -423 -439 C
ATOM 1029 O PHE A 600 66.271 65.761 21.125 1.00 24.28 O
ANISOU 1029 O PHE A 600 2759 3246 3222 -461 -545 -452 O
ATOM 1030 CB PHE A 600 67.122 63.042 22.434 1.00 22.20 C
ANISOU 1030 CB PHE A 600 2579 2897 2957 -636 -247 -416 C
ATOM 1031 CG PHE A 600 66.825 61.586 22.696 1.00 21.86 C
ANISOU 1031 CG PHE A 600 2557 2814 2936 -749 -159 -448 C
ATOM 1032 CD1 PHE A 600 66.186 60.777 21.763 1.00 22.37 C
ANISOU 1032 CD1 PHE A 600 2629 2866 3002 -821 -202 -520 C
ATOM 1033 CD2 PHE A 600 67.229 61.008 23.909 1.00 22.25 C
ANISOU 1033 CD2 PHE A 600 2635 2825 2992 -785 -34 -400 C
ATOM 1034 CE1 PHE A 600 65.941 59.455 22.030 1.00 23.02 C
ANISOU 1034 CE1 PHE A 600 2744 2899 3105 -932 -116 -548 C
ATOM 1035 CE2 PHE A 600 66.943 59.668 24.175 1.00 22.47 C
ANISOU 1035 CE2 PHE A 600 2707 2798 3034 -895 46 -422 C
ATOM 1036 CZ PHE A 600 66.308 58.905 23.236 1.00 23.04 C
ANISOU 1036 CZ PHE A 600 2783 2855 3117 -969 9 -496 C
ATOM 1037 N ILE A 601 67.021 66.027 23.229 1.00 22.12 N
ANISOU 1037 N ILE A 601 2439 2977 2987 -448 -362 -382 N
ATOM 1038 CA ILE A 601 67.874 67.193 22.941 1.00 21.95 C
ANISOU 1038 CA ILE A 601 2489 2937 2913 -355 -414 -316 C
ATOM 1039 C ILE A 601 69.297 66.732 22.924 1.00 21.58 C
ANISOU 1039 C ILE A 601 2569 2836 2795 -362 -326 -236 C
ATOM 1040 O ILE A 601 69.750 66.003 23.836 1.00 20.85 O
ANISOU 1040 O ILE A 601 2482 2727 2713 -396 -217 -210 O
ATOM 1041 CB ILE A 601 67.662 68.277 23.999 1.00 23.40 C
ANISOU 1041 CB ILE A 601 2584 3157 3151 -298 -408 -317 C
ATOM 1042 CG1 ILE A 601 66.218 68.746 23.916 1.00 25.15 C
ANISOU 1042 CG1 ILE A 601 2660 3434 3461 -278 -504 -417 C
ATOM 1043 CG2 ILE A 601 68.642 69.416 23.787 1.00 24.45 C
ANISOU 1043 CG2 ILE A 601 2804 3258 3228 -219 -444 -245 C
ATOM 1044 CD1 ILE A 601 65.900 69.450 22.626 1.00 27.00 C
ANISOU 1044 CD1 ILE A 601 2933 3654 3673 -213 -676 -430 C
ATOM 1045 N VAL A 602 70.029 67.136 21.918 1.00 20.72 N
ANISOU 1045 N VAL A 602 2566 2696 2612 -330 -372 -200 N
ATOM 1046 CA VAL A 602 71.440 66.792 21.798 1.00 20.54 C
ANISOU 1046 CA VAL A 602 2645 2628 2530 -331 -288 -142 C
ATOM 1047 C VAL A 602 72.233 68.088 21.766 1.00 20.43 C
ANISOU 1047 C VAL A 602 2672 2610 2479 -272 -308 -90 C
ATOM 1048 O VAL A 602 72.036 68.905 20.843 1.00 21.11 O
ANISOU 1048 O VAL A 602 2812 2690 2518 -250 -401 -89 O
ATOM 1049 CB VAL A 602 71.709 66.007 20.488 1.00 21.42 C
ANISOU 1049 CB VAL A 602 2860 2703 2575 -371 -295 -162 C
ATOM 1050 CG1 VAL A 602 73.207 65.786 20.261 1.00 21.97 C
ANISOU 1050 CG1 VAL A 602 3021 2733 2593 -363 -206 -120 C
ATOM 1051 CG2 VAL A 602 70.936 64.710 20.475 1.00 22.64 C
ANISOU 1051 CG2 VAL A 602 2984 2851 2766 -439 -277 -218 C
ATOM 1052 N LEU A 603 73.049 68.322 22.788 1.00 19.33 N
ANISOU 1052 N LEU A 603 2513 2471 2360 -249 -233 -49 N
ATOM 1053 CA LEU A 603 73.881 69.530 22.888 1.00 20.82 C
ANISOU 1053 CA LEU A 603 2735 2655 2522 -206 -238 -4 C
ATOM 1054 C LEU A 603 75.286 69.106 22.492 1.00 20.58 C
ANISOU 1054 C LEU A 603 2779 2594 2445 -221 -158 22 C
ATOM 1055 O LEU A 603 75.814 68.134 23.066 1.00 20.35 O
ANISOU 1055 O LEU A 603 2732 2556 2444 -229 -83 24 O
ATOM 1056 CB LEU A 603 73.839 70.106 24.266 1.00 21.33 C
ANISOU 1056 CB LEU A 603 2720 2745 2639 -174 -215 8 C
ATOM 1057 CG LEU A 603 72.487 70.544 24.854 1.00 26.07 C
ANISOU 1057 CG LEU A 603 3221 3383 3302 -157 -269 -37 C
ATOM 1058 CD1 LEU A 603 71.852 69.407 25.587 1.00 29.84 C
ANISOU 1058 CD1 LEU A 603 3633 3883 3823 -206 -209 -70 C
ATOM 1059 CD2 LEU A 603 72.619 71.688 25.854 1.00 29.93 C
ANISOU 1059 CD2 LEU A 603 3666 3887 3817 -111 -268 -26 C
ATOM 1060 N GLU A 604 75.906 69.788 21.525 1.00 18.65 N
ANISOU 1060 N GLU A 604 2622 2331 2132 -227 -171 38 N
ATOM 1061 CA GLU A 604 77.269 69.484 21.117 1.00 20.00 C
ANISOU 1061 CA GLU A 604 2848 2485 2268 -247 -81 44 C
ATOM 1062 C GLU A 604 78.173 70.591 21.634 1.00 19.16 C
ANISOU 1062 C GLU A 604 2732 2383 2164 -229 -55 78 C
ATOM 1063 O GLU A 604 77.981 71.751 21.264 1.00 17.97 O
ANISOU 1063 O GLU A 604 2632 2223 1973 -230 -110 98 O
ATOM 1064 CB GLU A 604 77.397 69.357 19.604 1.00 22.36 C
ANISOU 1064 CB GLU A 604 3262 2760 2474 -294 -85 25 C
ATOM 1065 CG GLU A 604 78.863 69.083 19.216 1.00 25.90 C
ANISOU 1065 CG GLU A 604 3747 3198 2895 -320 31 13 C
ATOM 1066 CD GLU A 604 79.125 68.990 17.709 1.00 33.57 C
ANISOU 1066 CD GLU A 604 4848 4149 3757 -381 55 -13 C
ATOM 1067 OE1 GLU A 604 79.862 69.926 17.146 1.00 39.15 O
ANISOU 1067 OE1 GLU A 604 5634 4849 4392 -420 90 3 O
ATOM 1068 OE2 GLU A 604 78.594 68.012 17.160 1.00 38.38 O
ANISOU 1068 OE2 GLU A 604 5484 4747 4350 -399 43 -51 O
ATOM 1069 N PHE A 605 79.139 70.251 22.455 1.00 17.88 N
ANISOU 1069 N PHE A 605 2515 2231 2049 -214 18 81 N
ATOM 1070 CA PHE A 605 80.058 71.199 23.066 1.00 17.72 C
ANISOU 1070 CA PHE A 605 2468 2223 2043 -202 44 101 C
ATOM 1071 C PHE A 605 81.465 70.997 22.569 1.00 18.61 C
ANISOU 1071 C PHE A 605 2594 2333 2144 -229 134 79 C
ATOM 1072 O PHE A 605 81.875 69.887 22.147 1.00 18.54 O
ANISOU 1072 O PHE A 605 2587 2315 2143 -233 188 45 O
ATOM 1073 CB PHE A 605 80.081 70.958 24.576 1.00 17.55 C
ANISOU 1073 CB PHE A 605 2355 2222 2091 -159 45 112 C
ATOM 1074 CG PHE A 605 78.811 71.241 25.298 1.00 17.44 C
ANISOU 1074 CG PHE A 605 2306 2222 2099 -139 -17 120 C
ATOM 1075 CD1 PHE A 605 78.498 72.529 25.751 1.00 17.62 C
ANISOU 1075 CD1 PHE A 605 2315 2254 2125 -122 -62 131 C
ATOM 1076 CD2 PHE A 605 77.927 70.237 25.585 1.00 18.85 C
ANISOU 1076 CD2 PHE A 605 2459 2403 2301 -143 -23 106 C
ATOM 1077 CE1 PHE A 605 77.371 72.769 26.501 1.00 18.31 C
ANISOU 1077 CE1 PHE A 605 2352 2361 2246 -99 -104 120 C
ATOM 1078 CE2 PHE A 605 76.797 70.465 26.344 1.00 18.76 C
ANISOU 1078 CE2 PHE A 605 2395 2413 2318 -135 -58 98 C
ATOM 1079 CZ PHE A 605 76.489 71.732 26.780 1.00 18.63 C
ANISOU 1079 CZ PHE A 605 2353 2414 2310 -110 -99 99 C
ATOM 1080 N GLU A 606 82.261 72.046 22.637 1.00 18.27 N
ANISOU 1080 N GLU A 606 2555 2296 2090 -249 159 87 N
ATOM 1081 CA GLU A 606 83.690 71.930 22.608 1.00 19.89 C
ANISOU 1081 CA GLU A 606 2720 2517 2320 -267 249 53 C
ATOM 1082 C GLU A 606 84.153 70.910 23.654 1.00 19.06 C
ANISOU 1082 C GLU A 606 2511 2428 2304 -203 260 37 C
ATOM 1083 O GLU A 606 83.594 70.845 24.742 1.00 18.98 O
ANISOU 1083 O GLU A 606 2462 2423 2328 -158 202 67 O
ATOM 1084 CB GLU A 606 84.249 73.303 23.032 1.00 22.81 C
ANISOU 1084 CB GLU A 606 3081 2896 2691 -291 250 70 C
ATOM 1085 CG GLU A 606 85.732 73.461 23.087 1.00 27.07 C
ANISOU 1085 CG GLU A 606 3559 3461 3265 -322 339 25 C
ATOM 1086 CD GLU A 606 86.193 74.797 23.738 1.00 31.53 C
ANISOU 1086 CD GLU A 606 4103 4033 3842 -348 328 39 C
ATOM 1087 OE1 GLU A 606 85.415 75.517 24.455 1.00 29.11 O
ANISOU 1087 OE1 GLU A 606 3810 3713 3535 -318 246 82 O
ATOM 1088 OE2 GLU A 606 87.419 75.108 23.542 1.00 33.27 O
ANISOU 1088 OE2 GLU A 606 4284 4276 4083 -403 411 -7 O
ATOM 1089 N PHE A 607 85.158 70.134 23.292 1.00 19.64 N
ANISOU 1089 N PHE A 607 2550 2503 2409 -200 333 -15 N
ATOM 1090 CA PHE A 607 85.734 69.164 24.237 1.00 19.76 C
ANISOU 1090 CA PHE A 607 2478 2517 2511 -127 328 -33 C
ATOM 1091 C PHE A 607 86.624 69.962 25.235 1.00 20.17 C
ANISOU 1091 C PHE A 607 2443 2606 2613 -107 314 -32 C
ATOM 1092 O PHE A 607 87.509 70.705 24.800 1.00 21.50 O
ANISOU 1092 O PHE A 607 2587 2801 2783 -154 371 -69 O
ATOM 1093 CB PHE A 607 86.549 68.082 23.526 1.00 21.48 C
ANISOU 1093 CB PHE A 607 2676 2719 2765 -113 401 -103 C
ATOM 1094 CG PHE A 607 87.181 67.105 24.462 1.00 22.16 C
ANISOU 1094 CG PHE A 607 2684 2791 2947 -23 376 -120 C
ATOM 1095 CD1 PHE A 607 86.387 66.309 25.278 1.00 23.02 C
ANISOU 1095 CD1 PHE A 607 2822 2860 3066 25 306 -71 C
ATOM 1096 CD2 PHE A 607 88.560 67.054 24.595 1.00 23.57 C
ANISOU 1096 CD2 PHE A 607 2761 2992 3203 11 415 -186 C
ATOM 1097 CE1 PHE A 607 86.983 65.416 26.191 1.00 24.01 C
ANISOU 1097 CE1 PHE A 607 2902 2953 3266 111 266 -75 C
ATOM 1098 CE2 PHE A 607 89.136 66.151 25.486 1.00 24.59 C
ANISOU 1098 CE2 PHE A 607 2823 3096 3422 111 364 -200 C
ATOM 1099 CZ PHE A 607 88.344 65.327 26.254 1.00 24.71 C
ANISOU 1099 CZ PHE A 607 2897 3058 3435 162 286 -138 C
ATOM 1100 N GLY A 608 86.431 69.693 26.517 1.00 20.16 N
ANISOU 1100 N GLY A 608 2405 2605 2650 -47 246 2 N
ATOM 1101 CA GLY A 608 87.105 70.493 27.569 1.00 21.28 C
ANISOU 1101 CA GLY A 608 2478 2782 2826 -30 212 6 C
ATOM 1102 C GLY A 608 88.173 69.791 28.357 1.00 22.74 C
ANISOU 1102 C GLY A 608 2575 2974 3090 41 187 -25 C
ATOM 1103 O GLY A 608 88.832 70.423 29.165 1.00 21.88 O
ANISOU 1103 O GLY A 608 2403 2899 3011 53 152 -34 O
ATOM 1104 N GLY A 609 88.387 68.505 28.095 1.00 23.33 N
ANISOU 1104 N GLY A 609 2646 3013 3204 93 196 -49 N
ATOM 1105 CA GLY A 609 89.419 67.754 28.841 1.00 24.72 C
ANISOU 1105 CA GLY A 609 2743 3181 3466 183 149 -82 C
ATOM 1106 C GLY A 609 88.815 66.801 29.835 1.00 24.76 C
ANISOU 1106 C GLY A 609 2812 3133 3463 247 65 -19 C
ATOM 1107 O GLY A 609 87.719 66.320 29.656 1.00 23.25 O
ANISOU 1107 O GLY A 609 2711 2902 3219 222 72 24 O
ATOM 1108 N ILE A 610 89.583 66.522 30.893 1.00 24.54 N
ANISOU 1108 N ILE A 610 2737 3101 3485 325 -19 -19 N
ATOM 1109 CA ILE A 610 89.289 65.465 31.861 1.00 26.60 C
ANISOU 1109 CA ILE A 610 3074 3295 3739 395 -106 37 C
ATOM 1110 C ILE A 610 88.896 66.128 33.188 1.00 24.17 C
ANISOU 1110 C ILE A 610 2804 3013 3366 380 -179 103 C
ATOM 1111 O ILE A 610 89.504 67.137 33.562 1.00 23.87 O
ANISOU 1111 O ILE A 610 2691 3039 3341 371 -200 78 O
ATOM 1112 CB ILE A 610 90.568 64.643 32.156 1.00 30.20 C
ANISOU 1112 CB ILE A 610 3460 3718 4297 512 -175 -13 C
ATOM 1113 CG1 ILE A 610 91.192 64.067 30.881 1.00 35.11 C
ANISOU 1113 CG1 ILE A 610 4015 4326 5001 534 -93 -107 C
ATOM 1114 CG2 ILE A 610 90.268 63.512 33.154 1.00 32.08 C
ANISOU 1114 CG2 ILE A 610 3812 3864 4515 584 -278 57 C
ATOM 1115 CD1 ILE A 610 90.274 63.127 30.180 1.00 36.29 C
ANISOU 1115 CD1 ILE A 610 4275 4400 5113 512 -41 -85 C
ATOM 1116 N ASP A 611 87.931 65.545 33.885 1.00 23.61 N
ANISOU 1116 N ASP A 611 2852 2893 3228 371 -209 175 N
ATOM 1117 CA ASP A 611 87.413 66.120 35.096 1.00 23.89 C
ANISOU 1117 CA ASP A 611 2939 2952 3186 341 -255 230 C
ATOM 1118 C ASP A 611 88.426 66.040 36.251 1.00 23.54 C
ANISOU 1118 C ASP A 611 2882 2907 3155 419 -373 238 C
ATOM 1119 O ASP A 611 89.296 65.168 36.307 1.00 24.15 O
ANISOU 1119 O ASP A 611 2944 2935 3297 510 -440 221 O
ATOM 1120 CB ASP A 611 86.052 65.608 35.491 1.00 25.94 C
ANISOU 1120 CB ASP A 611 3322 3170 3363 286 -230 293 C
ATOM 1121 CG ASP A 611 86.016 64.180 35.754 1.00 30.53 C
ANISOU 1121 CG ASP A 611 4002 3655 3944 327 -266 330 C
ATOM 1122 OD1 ASP A 611 86.246 63.787 36.930 1.00 33.80 O
ANISOU 1122 OD1 ASP A 611 4496 4031 4314 362 -349 379 O
ATOM 1123 OD2 ASP A 611 85.778 63.393 34.757 1.00 35.31 O
ANISOU 1123 OD2 ASP A 611 4620 4211 4586 324 -215 309 O
ATOM 1124 N LEU A 612 88.323 67.043 37.124 1.00 22.63 N
ANISOU 1124 N LEU A 612 2765 2848 2984 384 -402 252 N
ATOM 1125 CA LEU A 612 89.204 67.191 38.288 1.00 24.29 C
ANISOU 1125 CA LEU A 612 2967 3072 3188 441 -523 256 C
ATOM 1126 C LEU A 612 89.209 65.911 39.155 1.00 25.10 C
ANISOU 1126 C LEU A 612 3201 3085 3250 507 -622 321 C
ATOM 1127 O LEU A 612 90.242 65.474 39.629 1.00 25.60 O
ANISOU 1127 O LEU A 612 3243 3125 3358 603 -742 310 O
ATOM 1128 CB LEU A 612 88.761 68.420 39.095 1.00 24.76 C
ANISOU 1128 CB LEU A 612 3043 3197 3168 372 -520 266 C
ATOM 1129 CG LEU A 612 89.615 68.722 40.344 1.00 26.65 C
ANISOU 1129 CG LEU A 612 3282 3461 3383 416 -650 265 C
ATOM 1130 CD1 LEU A 612 91.084 68.933 40.023 1.00 28.39 C
ANISOU 1130 CD1 LEU A 612 3348 3718 3722 483 -714 187 C
ATOM 1131 CD2 LEU A 612 89.055 69.903 41.074 1.00 26.09 C
ANISOU 1131 CD2 LEU A 612 3239 3447 3226 339 -629 267 C
ATOM 1132 N GLU A 613 88.049 65.314 39.366 1.00 25.60 N
ANISOU 1132 N GLU A 613 3404 3094 3228 452 -574 387 N
ATOM 1133 CA GLU A 613 87.986 64.068 40.138 1.00 28.61 C
ANISOU 1133 CA GLU A 613 3942 3372 3557 495 -656 458 C
ATOM 1134 C GLU A 613 88.866 62.979 39.521 1.00 28.99 C
ANISOU 1134 C GLU A 613 3961 3339 3714 609 -715 433 C
ATOM 1135 O GLU A 613 89.651 62.318 40.249 1.00 31.30 O
ANISOU 1135 O GLU A 613 4310 3568 4016 709 -857 458 O
ATOM 1136 CB GLU A 613 86.530 63.589 40.255 1.00 29.79 C
ANISOU 1136 CB GLU A 613 4232 3476 3609 392 -561 516 C
ATOM 1137 CG GLU A 613 86.457 62.210 40.919 1.00 33.14 C
ANISOU 1137 CG GLU A 613 4842 3773 3978 421 -631 593 C
ATOM 1138 CD GLU A 613 85.056 61.779 41.269 1.00 35.79 C
ANISOU 1138 CD GLU A 613 5326 4069 4204 296 -535 649 C
ATOM 1139 OE1 GLU A 613 84.161 62.191 40.528 1.00 38.18 O
ANISOU 1139 OE1 GLU A 613 5558 4425 4524 214 -410 611 O
ATOM 1140 OE2 GLU A 613 84.903 61.024 42.285 1.00 41.65 O
ANISOU 1140 OE2 GLU A 613 6257 4724 4843 282 -591 727 O
ATOM 1141 N GLN A 614 88.775 62.810 38.183 1.00 28.29 N
ANISOU 1141 N GLN A 614 3787 3252 3709 599 -614 378 N
ATOM 1142 CA AGLN A 614 89.571 61.796 37.467 0.50 30.78 C
ANISOU 1142 CA AGLN A 614 4063 3494 4138 703 -645 333 C
ATOM 1143 CA BGLN A 614 89.567 61.781 37.474 0.50 30.96 C
ANISOU 1143 CA BGLN A 614 4088 3515 4160 704 -646 334 C
ATOM 1144 C GLN A 614 91.051 62.154 37.425 1.00 31.48 C
ANISOU 1144 C GLN A 614 3987 3632 4342 808 -727 250 C
ATOM 1145 O GLN A 614 91.901 61.282 37.292 1.00 33.65 O
ANISOU 1145 O GLN A 614 4234 3840 4712 928 -805 213 O
ATOM 1146 CB AGLN A 614 89.036 61.563 36.056 0.50 31.67 C
ANISOU 1146 CB AGLN A 614 4139 3602 4292 650 -508 288 C
ATOM 1147 CB BGLN A 614 89.017 61.483 36.066 0.50 32.35 C
ANISOU 1147 CB BGLN A 614 4233 3680 4377 653 -510 291 C
ATOM 1148 CG AGLN A 614 87.656 60.931 36.052 0.50 32.90 C
ANISOU 1148 CG AGLN A 614 4448 3693 4360 561 -443 355 C
ATOM 1149 CG BGLN A 614 87.846 60.495 36.036 0.50 34.31 C
ANISOU 1149 CG BGLN A 614 4647 3832 4557 594 -465 355 C
ATOM 1150 CD AGLN A 614 87.611 59.618 36.800 0.50 35.59 C
ANISOU 1150 CD AGLN A 614 4957 3896 4671 612 -528 423 C
ATOM 1151 CD BGLN A 614 87.058 60.575 34.730 0.50 35.46 C
ANISOU 1151 CD BGLN A 614 4757 4002 4714 509 -330 313 C
ATOM 1152 OE1AGLN A 614 86.685 59.367 37.571 0.50 37.54 O
ANISOU 1152 OE1AGLN A 614 5352 4104 4809 534 -521 501 O
ATOM 1153 OE1BGLN A 614 85.855 60.873 34.713 0.50 34.58 O
ANISOU 1153 OE1BGLN A 614 4696 3916 4526 400 -260 345 O
ATOM 1154 NE2AGLN A 614 88.615 58.777 36.588 0.50 37.16 N
ANISOU 1154 NE2AGLN A 614 5139 4015 4966 740 -608 389 N
ATOM 1155 NE2BGLN A 614 87.758 60.395 33.624 0.50 37.32 N
ANISOU 1155 NE2BGLN A 614 4896 4241 5044 557 -293 231 N
ATOM 1156 N MET A 615 91.354 63.427 37.631 1.00 29.88 N
ANISOU 1156 N MET A 615 3678 3541 4133 765 -719 217 N
ATOM 1157 CA MET A 615 92.715 63.943 37.642 1.00 31.97 C
ANISOU 1157 CA MET A 615 3769 3872 4505 837 -786 128 C
ATOM 1158 C MET A 615 93.297 64.081 39.068 1.00 32.28 C
ANISOU 1158 C MET A 615 3840 3916 4510 901 -961 159 C
ATOM 1159 O MET A 615 94.338 64.694 39.268 1.00 33.28 O
ANISOU 1159 O MET A 615 3820 4113 4711 942 -1028 85 O
ATOM 1160 CB MET A 615 92.775 65.324 36.991 1.00 32.77 C
ANISOU 1160 CB MET A 615 3740 4090 4622 738 -672 65 C
ATOM 1161 CG MET A 615 92.489 65.387 35.473 1.00 34.79 C
ANISOU 1161 CG MET A 615 3942 4358 4917 676 -511 13 C
ATOM 1162 SD MET A 615 93.816 64.634 34.496 1.00 41.62 S
ANISOU 1162 SD MET A 615 4651 5211 5952 776 -495 -113 S
ATOM 1163 CE MET A 615 95.074 65.934 34.567 1.00 43.30 C
ANISOU 1163 CE MET A 615 4657 5550 6247 754 -499 -218 C
ATOM 1164 N ARG A 616 92.606 63.558 40.059 1.00 32.31 N
ANISOU 1164 N ARG A 616 4039 3847 4390 897 -1031 265 N
ATOM 1165 CA ARG A 616 92.999 63.771 41.432 1.00 33.97 C
ANISOU 1165 CA ARG A 616 4314 4062 4529 934 -1190 305 C
ATOM 1166 C ARG A 616 94.364 63.225 41.844 1.00 36.66 C
ANISOU 1166 C ARG A 616 4584 4371 4974 1096 -1383 261 C
ATOM 1167 O ARG A 616 94.896 63.678 42.835 1.00 37.51 O
ANISOU 1167 O ARG A 616 4691 4517 5045 1125 -1520 263 O
ATOM 1168 CB ARG A 616 91.914 63.288 42.372 1.00 35.03 C
ANISOU 1168 CB ARG A 616 4696 4122 4493 876 -1205 429 C
ATOM 1169 CG ARG A 616 91.785 61.790 42.508 1.00 37.22 C
ANISOU 1169 CG ARG A 616 5138 4247 4756 949 -1273 497 C
ATOM 1170 CD ARG A 616 90.539 61.486 43.336 1.00 38.55 C
ANISOU 1170 CD ARG A 616 5550 4358 4740 839 -1233 612 C
ATOM 1171 NE ARG A 616 90.410 60.051 43.476 1.00 40.89 N
ANISOU 1171 NE ARG A 616 6026 4494 5016 894 -1296 682 N
ATOM 1172 CZ ARG A 616 89.885 59.250 42.552 1.00 43.38 C
ANISOU 1172 CZ ARG A 616 6365 4735 5382 875 -1193 681 C
ATOM 1173 NH1 ARG A 616 89.870 57.925 42.770 1.00 47.46 N
ANISOU 1173 NH1 ARG A 616 7062 5088 5882 933 -1269 745 N
ATOM 1174 NH2 ARG A 616 89.365 59.736 41.403 1.00 42.26 N
ANISOU 1174 NH2 ARG A 616 6084 4670 5302 798 -1022 616 N
ATOM 1175 N THR A 617 94.932 62.294 41.080 1.00 37.73 N
ANISOU 1175 N THR A 617 4652 4441 5243 1203 -1397 209 N
ATOM 1176 CA THR A 617 96.280 61.825 41.313 1.00 41.57 C
ANISOU 1176 CA THR A 617 5024 4906 5865 1370 -1573 136 C
ATOM 1177 C THR A 617 97.273 62.315 40.279 1.00 41.43 C
ANISOU 1177 C THR A 617 4724 4986 6032 1397 -1500 -22 C
ATOM 1178 O THR A 617 98.401 61.859 40.261 1.00 43.58 O
ANISOU 1178 O THR A 617 4861 5245 6451 1540 -1621 -112 O
ATOM 1179 CB THR A 617 96.356 60.261 41.306 1.00 45.11 C
ANISOU 1179 CB THR A 617 5603 5185 6351 1504 -1672 178 C
ATOM 1180 OG1 THR A 617 96.105 59.790 39.973 1.00 46.14 O
ANISOU 1180 OG1 THR A 617 5672 5289 6570 1488 -1506 122 O
ATOM 1181 CG2 THR A 617 95.329 59.627 42.279 1.00 45.35 C
ANISOU 1181 CG2 THR A 617 5946 5097 6189 1460 -1726 341 C
ATOM 1182 N LYS A 618 96.862 63.210 39.406 1.00 40.48 N
ANISOU 1182 N LYS A 618 4517 4958 5907 1260 -1304 -63 N
ATOM 1183 CA LYS A 618 97.633 63.512 38.218 1.00 42.60 C
ANISOU 1183 CA LYS A 618 4557 5298 6330 1258 -1189 -205 C
ATOM 1184 C LYS A 618 98.211 64.919 38.214 1.00 40.86 C
ANISOU 1184 C LYS A 618 4165 5220 6141 1173 -1148 -286 C
ATOM 1185 O LYS A 618 99.005 65.203 37.364 1.00 44.28 O
ANISOU 1185 O LYS A 618 4403 5717 6703 1166 -1064 -414 O
ATOM 1186 CB LYS A 618 96.723 63.374 36.973 1.00 43.70 C
ANISOU 1186 CB LYS A 618 4748 5419 6438 1158 -979 -194 C
ATOM 1187 CG LYS A 618 96.020 62.028 36.843 1.00 46.78 C
ANISOU 1187 CG LYS A 618 5314 5668 6793 1211 -988 -119 C
ATOM 1188 CD LYS A 618 96.992 60.904 36.656 1.00 51.78 C
ANISOU 1188 CD LYS A 618 5876 6222 7576 1382 -1085 -197 C
ATOM 1189 CE LYS A 618 96.296 59.679 36.094 1.00 55.40 C
ANISOU 1189 CE LYS A 618 6484 6547 8019 1404 -1033 -154 C
ATOM 1190 NZ LYS A 618 97.339 58.688 35.713 1.00 59.41 N
ANISOU 1190 NZ LYS A 618 6888 6983 8701 1575 -1103 -262 N
ATOM 1191 N LEU A 619 97.823 65.795 39.134 1.00 38.25 N
ANISOU 1191 N LEU A 619 3908 4934 5691 1098 -1195 -221 N
ATOM 1192 CA LEU A 619 98.295 67.180 39.117 1.00 35.72 C
ANISOU 1192 CA LEU A 619 3444 4736 5393 1001 -1148 -296 C
ATOM 1193 C LEU A 619 99.736 67.271 39.644 1.00 36.93 C
ANISOU 1193 C LEU A 619 3407 4945 5681 1100 -1306 -408 C
ATOM 1194 O LEU A 619 100.154 66.502 40.523 1.00 37.58 O
ANISOU 1194 O LEU A 619 3529 4973 5778 1238 -1507 -386 O
ATOM 1195 CB LEU A 619 97.381 68.040 39.968 1.00 34.94 C
ANISOU 1195 CB LEU A 619 3494 4655 5125 897 -1151 -199 C
ATOM 1196 CG LEU A 619 95.870 68.084 39.727 1.00 35.17 C
ANISOU 1196 CG LEU A 619 3708 4642 5015 799 -1023 -90 C
ATOM 1197 CD1 LEU A 619 95.169 69.101 40.617 1.00 34.30 C
ANISOU 1197 CD1 LEU A 619 3698 4569 4767 704 -1028 -33 C
ATOM 1198 CD2 LEU A 619 95.633 68.442 38.293 1.00 34.33 C
ANISOU 1198 CD2 LEU A 619 3526 4560 4956 716 -832 -139 C
ATOM 1199 N SER A 620 100.498 68.221 39.115 1.00 34.85 N
ANISOU 1199 N SER A 620 2940 4788 5515 1025 -1221 -532 N
ATOM 1200 CA SER A 620 101.894 68.334 39.432 1.00 36.53 C
ANISOU 1200 CA SER A 620 2929 5067 5882 1104 -1345 -668 C
ATOM 1201 C SER A 620 102.160 68.768 40.898 1.00 36.77 C
ANISOU 1201 C SER A 620 2998 5124 5848 1135 -1559 -636 C
ATOM 1202 O SER A 620 102.987 68.163 41.573 1.00 36.63 O
ANISOU 1202 O SER A 620 2913 5094 5913 1283 -1767 -678 O
ATOM 1203 CB SER A 620 102.540 69.317 38.457 1.00 37.08 C
ANISOU 1203 CB SER A 620 2788 5245 6056 977 -1168 -807 C
ATOM 1204 OG SER A 620 103.869 69.486 38.776 1.00 41.85 O
ANISOU 1204 OG SER A 620 3157 5926 6817 1036 -1278 -953 O
ATOM 1205 N SER A 621 101.496 69.822 41.363 1.00 35.06 N
ANISOU 1205 N SER A 621 2889 4943 5491 1001 -1514 -572 N
ATOM 1206 CA SER A 621 101.779 70.356 42.698 1.00 36.38 C
ANISOU 1206 CA SER A 621 3088 5146 5590 1009 -1699 -559 C
ATOM 1207 C SER A 621 100.633 71.208 43.177 1.00 35.02 C
ANISOU 1207 C SER A 621 3110 4971 5226 876 -1625 -453 C
ATOM 1208 O SER A 621 99.690 71.491 42.440 1.00 33.02 O
ANISOU 1208 O SER A 621 2939 4698 4912 777 -1436 -401 O
ATOM 1209 CB SER A 621 103.062 71.191 42.671 1.00 37.51 C
ANISOU 1209 CB SER A 621 2967 5404 5881 980 -1735 -724 C
ATOM 1210 OG SER A 621 102.800 72.427 42.006 1.00 37.71 O
ANISOU 1210 OG SER A 621 2950 5491 5888 796 -1530 -759 O
ATOM 1211 N LEU A 622 100.753 71.692 44.401 1.00 35.78 N
ANISOU 1211 N LEU A 622 3269 5094 5233 870 -1776 -435 N
ATOM 1212 CA LEU A 622 99.826 72.720 44.910 1.00 35.66 C
ANISOU 1212 CA LEU A 622 3401 5094 5055 736 -1702 -372 C
ATOM 1213 C LEU A 622 99.829 74.050 44.110 1.00 33.30 C
ANISOU 1213 C LEU A 622 2988 4863 4803 582 -1517 -448 C
ATOM 1214 O LEU A 622 98.835 74.788 44.154 1.00 32.68 O
ANISOU 1214 O LEU A 622 3038 4772 4606 477 -1406 -390 O
ATOM 1215 CB LEU A 622 100.092 72.995 46.403 1.00 38.32 C
ANISOU 1215 CB LEU A 622 3820 5452 5288 759 -1908 -358 C
ATOM 1216 CG LEU A 622 99.541 71.919 47.332 1.00 40.66 C
ANISOU 1216 CG LEU A 622 4349 5658 5442 853 -2047 -231 C
ATOM 1217 CD1 LEU A 622 100.146 72.112 48.725 1.00 43.52 C
ANISOU 1217 CD1 LEU A 622 4762 6048 5727 895 -2286 -242 C
ATOM 1218 CD2 LEU A 622 98.027 71.932 47.393 1.00 40.92 C
ANISOU 1218 CD2 LEU A 622 4608 5636 5304 763 -1898 -109 C
ATOM 1219 N ALA A 623 100.916 74.343 43.381 1.00 32.97 N
ANISOU 1219 N ALA A 623 2713 4883 4930 568 -1480 -580 N
ATOM 1220 CA ALA A 623 100.914 75.521 42.485 1.00 32.57 C
ANISOU 1220 CA ALA A 623 2580 4877 4918 412 -1287 -643 C
ATOM 1221 C ALA A 623 99.859 75.308 41.389 1.00 29.89 C
ANISOU 1221 C ALA A 623 2349 4477 4531 366 -1093 -566 C
ATOM 1222 O ALA A 623 99.160 76.249 40.985 1.00 28.91 O
ANISOU 1222 O ALA A 623 2299 4346 4340 244 -957 -539 O
ATOM 1223 CB ALA A 623 102.290 75.762 41.865 1.00 33.59 C
ANISOU 1223 CB ALA A 623 2442 5085 5238 393 -1265 -806 C
ATOM 1224 N THR A 624 99.745 74.073 40.896 1.00 29.75 N
ANISOU 1224 N THR A 624 2343 4410 4552 468 -1089 -534 N
ATOM 1225 CA THR A 624 98.717 73.729 39.934 1.00 28.78 C
ANISOU 1225 CA THR A 624 2331 4227 4376 435 -932 -459 C
ATOM 1226 C THR A 624 97.312 73.886 40.538 1.00 26.91 C
ANISOU 1226 C THR A 624 2318 3939 3968 403 -926 -329 C
ATOM 1227 O THR A 624 96.399 74.458 39.931 1.00 24.70 O
ANISOU 1227 O THR A 624 2117 3641 3625 311 -788 -289 O
ATOM 1228 CB THR A 624 98.885 72.279 39.439 1.00 30.42 C
ANISOU 1228 CB THR A 624 2520 4383 4655 560 -952 -454 C
ATOM 1229 OG1 THR A 624 100.257 72.021 39.117 1.00 31.99 O
ANISOU 1229 OG1 THR A 624 2496 4632 5026 619 -990 -590 O
ATOM 1230 CG2 THR A 624 97.974 72.002 38.244 1.00 29.26 C
ANISOU 1230 CG2 THR A 624 2456 4188 4474 508 -775 -406 C
ATOM 1231 N ALA A 625 97.166 73.458 41.796 1.00 27.39 N
ANISOU 1231 N ALA A 625 2480 3980 3948 473 -1082 -272 N
ATOM 1232 CA ALA A 625 95.918 73.662 42.515 1.00 26.98 C
ANISOU 1232 CA ALA A 625 2627 3893 3733 431 -1072 -170 C
ATOM 1233 C ALA A 625 95.560 75.159 42.646 1.00 25.79 C
ANISOU 1233 C ALA A 625 2486 3783 3530 307 -996 -195 C
ATOM 1234 O ALA A 625 94.366 75.521 42.430 1.00 24.48 O
ANISOU 1234 O ALA A 625 2434 3587 3279 245 -887 -138 O
ATOM 1235 CB ALA A 625 95.989 73.001 43.878 1.00 27.80 C
ANISOU 1235 CB ALA A 625 2842 3972 3750 514 -1253 -116 C
ATOM 1236 N LYS A 626 96.551 75.999 42.942 1.00 26.25 N
ANISOU 1236 N LYS A 626 2422 3903 3647 274 -1051 -286 N
ATOM 1237 CA LYS A 626 96.302 77.437 43.055 1.00 27.40 C
ANISOU 1237 CA LYS A 626 2581 4075 3753 155 -984 -318 C
ATOM 1238 C LYS A 626 95.793 78.010 41.720 1.00 25.72 C
ANISOU 1238 C LYS A 626 2360 3841 3573 69 -798 -320 C
ATOM 1239 O LYS A 626 94.807 78.768 41.678 1.00 24.03 O
ANISOU 1239 O LYS A 626 2252 3597 3280 4 -720 -282 O
ATOM 1240 CB LYS A 626 97.565 78.170 43.444 1.00 29.97 C
ANISOU 1240 CB LYS A 626 2760 4469 4159 124 -1066 -429 C
ATOM 1241 CG LYS A 626 97.354 79.650 43.695 1.00 31.25 C
ANISOU 1241 CG LYS A 626 2952 4645 4276 1 -1013 -466 C
ATOM 1242 CD LYS A 626 98.615 80.277 44.221 1.00 35.72 C
ANISOU 1242 CD LYS A 626 3376 5279 4915 -33 -1114 -580 C
ATOM 1243 CE LYS A 626 98.498 81.790 44.087 1.00 38.47 C
ANISOU 1243 CE LYS A 626 3739 5627 5251 -175 -1020 -629 C
ATOM 1244 NZ LYS A 626 99.867 82.352 44.199 1.00 44.39 N
ANISOU 1244 NZ LYS A 626 4307 6446 6114 -232 -1077 -760 N
ATOM 1245 N SER A 627 96.477 77.626 40.657 1.00 26.03 N
ANISOU 1245 N SER A 627 2275 3890 3725 75 -737 -368 N
ATOM 1246 CA SER A 627 96.030 78.005 39.304 1.00 25.04 C
ANISOU 1246 CA SER A 627 2162 3737 3616 -3 -568 -363 C
ATOM 1247 C SER A 627 94.606 77.642 39.014 1.00 23.83 C
ANISOU 1247 C SER A 627 2164 3521 3368 11 -508 -261 C
ATOM 1248 O SER A 627 93.838 78.454 38.515 1.00 22.27 O
ANISOU 1248 O SER A 627 2041 3295 3125 -63 -417 -238 O
ATOM 1249 CB SER A 627 96.947 77.437 38.239 1.00 26.45 C
ANISOU 1249 CB SER A 627 2198 3936 3915 7 -505 -432 C
ATOM 1250 OG SER A 627 96.478 77.867 36.974 1.00 26.52 O
ANISOU 1250 OG SER A 627 2250 3915 3912 -81 -346 -421 O
ATOM 1251 N ILE A 628 94.218 76.415 39.339 1.00 22.48 N
ANISOU 1251 N ILE A 628 2048 3325 3170 106 -564 -203 N
ATOM 1252 CA ILE A 628 92.904 75.968 39.065 1.00 21.99 C
ANISOU 1252 CA ILE A 628 2114 3210 3031 113 -507 -119 C
ATOM 1253 C ILE A 628 91.906 76.797 39.897 1.00 21.28 C
ANISOU 1253 C ILE A 628 2137 3113 2836 69 -511 -81 C
ATOM 1254 O ILE A 628 90.888 77.244 39.384 1.00 19.77 O
ANISOU 1254 O ILE A 628 2013 2893 2606 25 -426 -53 O
ATOM 1255 CB ILE A 628 92.753 74.459 39.322 1.00 22.29 C
ANISOU 1255 CB ILE A 628 2196 3213 3061 212 -568 -68 C
ATOM 1256 CG1 ILE A 628 93.539 73.675 38.279 1.00 22.84 C
ANISOU 1256 CG1 ILE A 628 2160 3277 3240 254 -534 -114 C
ATOM 1257 CG2 ILE A 628 91.337 74.021 39.364 1.00 21.04 C
ANISOU 1257 CG2 ILE A 628 2178 3006 2810 206 -523 15 C
ATOM 1258 CD1 ILE A 628 93.773 72.199 38.657 1.00 24.31 C
ANISOU 1258 CD1 ILE A 628 2368 3422 3447 371 -628 -85 C
ATOM 1259 N LEU A 629 92.229 77.032 41.165 1.00 21.76 N
ANISOU 1259 N LEU A 629 2215 3201 2854 83 -614 -92 N
ATOM 1260 CA LEU A 629 91.305 77.819 42.014 1.00 21.94 C
ANISOU 1260 CA LEU A 629 2342 3219 2773 40 -608 -73 C
ATOM 1261 C LEU A 629 91.169 79.264 41.495 1.00 21.41 C
ANISOU 1261 C LEU A 629 2256 3151 2729 -45 -530 -119 C
ATOM 1262 O LEU A 629 90.064 79.840 41.503 1.00 21.27 O
ANISOU 1262 O LEU A 629 2321 3105 2657 -75 -471 -99 O
ATOM 1263 CB LEU A 629 91.758 77.819 43.469 1.00 23.51 C
ANISOU 1263 CB LEU A 629 2576 3450 2909 63 -736 -83 C
ATOM 1264 CG LEU A 629 91.575 76.475 44.183 1.00 23.99 C
ANISOU 1264 CG LEU A 629 2723 3488 2903 138 -818 -16 C
ATOM 1265 CD1 LEU A 629 92.317 76.540 45.525 1.00 26.64 C
ANISOU 1265 CD1 LEU A 629 3084 3856 3182 163 -971 -35 C
ATOM 1266 CD2 LEU A 629 90.105 76.116 44.370 1.00 24.60 C
ANISOU 1266 CD2 LEU A 629 2939 3528 2880 118 -739 52 C
ATOM 1267 N HIS A 630 92.272 79.799 41.031 1.00 21.19 N
ANISOU 1267 N HIS A 630 2121 3147 2784 -83 -529 -184 N
ATOM 1268 CA HIS A 630 92.286 81.177 40.495 1.00 21.19 C
ANISOU 1268 CA HIS A 630 2116 3130 2804 -176 -456 -226 C
ATOM 1269 C HIS A 630 91.455 81.237 39.211 1.00 20.46 C
ANISOU 1269 C HIS A 630 2074 2985 2716 -198 -345 -185 C
ATOM 1270 O HIS A 630 90.597 82.095 39.048 1.00 20.11 O
ANISOU 1270 O HIS A 630 2110 2896 2635 -233 -303 -172 O
ATOM 1271 CB HIS A 630 93.724 81.584 40.265 1.00 22.53 C
ANISOU 1271 CB HIS A 630 2154 3341 3066 -226 -470 -309 C
ATOM 1272 CG HIS A 630 93.919 83.054 40.094 1.00 23.96 C
ANISOU 1272 CG HIS A 630 2344 3503 3257 -334 -422 -361 C
ATOM 1273 ND1 HIS A 630 95.174 83.626 40.150 1.00 25.43 N
ANISOU 1273 ND1 HIS A 630 2417 3731 3516 -404 -438 -450 N
ATOM 1274 CD2 HIS A 630 93.041 84.073 39.904 1.00 23.28 C
ANISOU 1274 CD2 HIS A 630 2367 3355 3123 -385 -365 -342 C
ATOM 1275 CE1 HIS A 630 95.063 84.935 40.004 1.00 25.95 C
ANISOU 1275 CE1 HIS A 630 2535 3754 3570 -504 -386 -478 C
ATOM 1276 NE2 HIS A 630 93.784 85.230 39.839 1.00 25.30 N
ANISOU 1276 NE2 HIS A 630 2592 3604 3416 -487 -346 -411 N
ATOM 1277 N GLN A 631 91.654 80.263 38.325 1.00 20.21 N
ANISOU 1277 N GLN A 631 2001 2952 2725 -167 -310 -166 N
ATOM 1278 CA GLN A 631 90.857 80.214 37.115 1.00 19.07 C
ANISOU 1278 CA GLN A 631 1914 2760 2572 -185 -220 -127 C
ATOM 1279 C GLN A 631 89.387 80.111 37.384 1.00 19.40 C
ANISOU 1279 C GLN A 631 2060 2767 2542 -151 -219 -69 C
ATOM 1280 O GLN A 631 88.565 80.780 36.761 1.00 18.53 O
ANISOU 1280 O GLN A 631 2014 2613 2413 -180 -173 -53 O
ATOM 1281 CB GLN A 631 91.361 79.064 36.210 1.00 19.88 C
ANISOU 1281 CB GLN A 631 1955 2872 2726 -154 -185 -127 C
ATOM 1282 CG GLN A 631 92.740 79.276 35.640 1.00 20.99 C
ANISOU 1282 CG GLN A 631 1979 3047 2949 -204 -148 -204 C
ATOM 1283 CD GLN A 631 93.140 78.171 34.647 1.00 21.50 C
ANISOU 1283 CD GLN A 631 1989 3116 3065 -174 -94 -217 C
ATOM 1284 OE1 GLN A 631 92.377 77.867 33.698 1.00 20.70 O
ANISOU 1284 OE1 GLN A 631 1964 2974 2928 -182 -28 -175 O
ATOM 1285 NE2 GLN A 631 94.276 77.521 34.899 1.00 22.43 N
ANISOU 1285 NE2 GLN A 631 1975 3280 3267 -129 -134 -280 N
ATOM 1286 N LEU A 632 89.017 79.187 38.283 1.00 18.88 N
ANISOU 1286 N LEU A 632 2015 2720 2440 -89 -272 -38 N
ATOM 1287 CA LEU A 632 87.621 79.012 38.617 1.00 19.03 C
ANISOU 1287 CA LEU A 632 2118 2717 2397 -69 -258 3 C
ATOM 1288 C LEU A 632 87.006 80.305 39.198 1.00 18.62 C
ANISOU 1288 C LEU A 632 2111 2654 2309 -101 -254 -25 C
ATOM 1289 O LEU A 632 85.898 80.720 38.830 1.00 18.61 O
ANISOU 1289 O LEU A 632 2156 2620 2296 -104 -215 -17 O
ATOM 1290 CB LEU A 632 87.474 77.901 39.672 1.00 19.71 C
ANISOU 1290 CB LEU A 632 2234 2822 2434 -19 -312 35 C
ATOM 1291 CG LEU A 632 87.706 76.473 39.147 1.00 20.32 C
ANISOU 1291 CG LEU A 632 2297 2886 2538 28 -315 71 C
ATOM 1292 CD1 LEU A 632 87.871 75.495 40.269 1.00 20.91 C
ANISOU 1292 CD1 LEU A 632 2416 2964 2564 74 -391 103 C
ATOM 1293 CD2 LEU A 632 86.594 76.024 38.203 1.00 20.76 C
ANISOU 1293 CD2 LEU A 632 2390 2906 2590 22 -242 103 C
ATOM 1294 N THR A 633 87.728 80.912 40.137 1.00 19.26 N
ANISOU 1294 N THR A 633 2176 2762 2379 -120 -305 -65 N
ATOM 1295 CA THR A 633 87.248 82.119 40.785 1.00 19.34 C
ANISOU 1295 CA THR A 633 2233 2759 2357 -150 -304 -104 C
ATOM 1296 C THR A 633 87.060 83.230 39.766 1.00 19.06 C
ANISOU 1296 C THR A 633 2211 2666 2364 -190 -256 -120 C
ATOM 1297 O THR A 633 86.044 83.908 39.773 1.00 19.91 O
ANISOU 1297 O THR A 633 2373 2734 2457 -184 -234 -129 O
ATOM 1298 CB THR A 633 88.176 82.570 41.926 1.00 20.71 C
ANISOU 1298 CB THR A 633 2388 2971 2509 -172 -374 -151 C
ATOM 1299 OG1 THR A 633 88.316 81.478 42.859 1.00 21.18 O
ANISOU 1299 OG1 THR A 633 2461 3071 2513 -128 -435 -124 O
ATOM 1300 CG2 THR A 633 87.612 83.716 42.647 1.00 20.36 C
ANISOU 1300 CG2 THR A 633 2401 2909 2425 -199 -368 -197 C
ATOM 1301 N ALA A 634 88.014 83.400 38.906 1.00 18.28 N
ANISOU 1301 N ALA A 634 2069 2560 2317 -232 -240 -129 N
ATOM 1302 CA ALA A 634 87.935 84.447 37.880 1.00 18.93 C
ANISOU 1302 CA ALA A 634 2193 2576 2425 -285 -194 -135 C
ATOM 1303 C ALA A 634 86.769 84.202 36.942 1.00 18.67 C
ANISOU 1303 C ALA A 634 2218 2495 2381 -251 -162 -87 C
ATOM 1304 O ALA A 634 86.021 85.135 36.592 1.00 18.49 O
ANISOU 1304 O ALA A 634 2266 2405 2353 -254 -158 -88 O
ATOM 1305 CB ALA A 634 89.233 84.602 37.104 1.00 18.88 C
ANISOU 1305 CB ALA A 634 2131 2575 2466 -357 -162 -159 C
ATOM 1306 N SER A 635 86.572 82.943 36.501 1.00 18.45 N
ANISOU 1306 N SER A 635 2163 2496 2352 -212 -148 -48 N
ATOM 1307 CA SER A 635 85.523 82.696 35.549 1.00 18.36 C
ANISOU 1307 CA SER A 635 2200 2444 2332 -187 -126 -11 C
ATOM 1308 C SER A 635 84.176 82.955 36.182 1.00 17.98 C
ANISOU 1308 C SER A 635 2184 2383 2265 -139 -147 -17 C
ATOM 1309 O SER A 635 83.261 83.558 35.559 1.00 17.68 O
ANISOU 1309 O SER A 635 2196 2289 2232 -123 -151 -14 O
ATOM 1310 CB SER A 635 85.591 81.237 35.089 1.00 18.88 C
ANISOU 1310 CB SER A 635 2228 2542 2401 -159 -109 22 C
ATOM 1311 OG SER A 635 86.801 80.993 34.398 1.00 20.96 O
ANISOU 1311 OG SER A 635 2451 2819 2694 -198 -79 12 O
ATOM 1312 N LEU A 636 84.006 82.491 37.399 1.00 18.03 N
ANISOU 1312 N LEU A 636 2165 2438 2246 -114 -161 -30 N
ATOM 1313 CA LEU A 636 82.778 82.754 38.151 1.00 18.07 C
ANISOU 1313 CA LEU A 636 2190 2445 2232 -82 -160 -57 C
ATOM 1314 C LEU A 636 82.540 84.242 38.376 1.00 18.50 C
ANISOU 1314 C LEU A 636 2279 2449 2300 -87 -172 -106 C
ATOM 1315 O LEU A 636 81.390 84.725 38.293 1.00 18.71 O
ANISOU 1315 O LEU A 636 2322 2443 2344 -50 -171 -133 O
ATOM 1316 CB LEU A 636 82.730 81.970 39.462 1.00 18.70 C
ANISOU 1316 CB LEU A 636 2259 2585 2261 -74 -161 -61 C
ATOM 1317 CG LEU A 636 82.649 80.441 39.253 1.00 18.83 C
ANISOU 1317 CG LEU A 636 2263 2628 2264 -59 -149 -9 C
ATOM 1318 CD1 LEU A 636 82.867 79.745 40.560 1.00 20.94 C
ANISOU 1318 CD1 LEU A 636 2551 2939 2468 -61 -165 -2 C
ATOM 1319 CD2 LEU A 636 81.284 80.038 38.685 1.00 19.00 C
ANISOU 1319 CD2 LEU A 636 2284 2636 2298 -40 -112 -4 C
ATOM 1320 N ALA A 637 83.602 84.968 38.681 1.00 18.06 N
ANISOU 1320 N ALA A 637 2231 2387 2246 -132 -189 -129 N
ATOM 1321 CA ALA A 637 83.478 86.425 38.855 1.00 19.46 C
ANISOU 1321 CA ALA A 637 2456 2499 2437 -146 -202 -177 C
ATOM 1322 C ALA A 637 83.000 87.126 37.586 1.00 19.22 C
ANISOU 1322 C ALA A 637 2485 2376 2442 -138 -207 -157 C
ATOM 1323 O ALA A 637 82.073 87.992 37.625 1.00 20.43 O
ANISOU 1323 O ALA A 637 2681 2466 2616 -95 -226 -191 O
ATOM 1324 CB ALA A 637 84.783 87.012 39.306 1.00 19.86 C
ANISOU 1324 CB ALA A 637 2502 2558 2487 -212 -217 -206 C
ATOM 1325 N VAL A 638 83.561 86.749 36.470 1.00 18.48 N
ANISOU 1325 N VAL A 638 2400 2270 2353 -172 -193 -107 N
ATOM 1326 CA VAL A 638 83.184 87.362 35.217 1.00 19.51 C
ANISOU 1326 CA VAL A 638 2613 2308 2493 -175 -205 -78 C
ATOM 1327 C VAL A 638 81.698 87.065 34.889 1.00 20.10 C
ANISOU 1327 C VAL A 638 2692 2366 2580 -87 -235 -70 C
ATOM 1328 O VAL A 638 80.971 87.934 34.389 1.00 19.21 O
ANISOU 1328 O VAL A 638 2649 2165 2486 -50 -280 -76 O
ATOM 1329 CB VAL A 638 84.113 86.886 34.090 1.00 20.15 C
ANISOU 1329 CB VAL A 638 2705 2391 2561 -241 -168 -31 C
ATOM 1330 CG1 VAL A 638 83.594 87.242 32.724 1.00 21.28 C
ANISOU 1330 CG1 VAL A 638 2951 2446 2687 -243 -183 12 C
ATOM 1331 CG2 VAL A 638 85.549 87.404 34.277 1.00 20.81 C
ANISOU 1331 CG2 VAL A 638 2777 2481 2650 -337 -136 -57 C
ATOM 1332 N ALA A 639 81.259 85.838 35.159 1.00 18.70 N
ANISOU 1332 N ALA A 639 2441 2269 2397 -55 -216 -62 N
ATOM 1333 CA ALA A 639 79.851 85.483 34.978 1.00 19.37 C
ANISOU 1333 CA ALA A 639 2502 2354 2502 15 -237 -73 C
ATOM 1334 C ALA A 639 78.922 86.175 35.962 1.00 19.71 C
ANISOU 1334 C ALA A 639 2522 2393 2574 68 -249 -147 C
ATOM 1335 O ALA A 639 77.800 86.490 35.628 1.00 21.19 O
ANISOU 1335 O ALA A 639 2704 2544 2803 132 -285 -176 O
ATOM 1336 CB ALA A 639 79.671 83.952 35.049 1.00 19.53 C
ANISOU 1336 CB ALA A 639 2457 2457 2506 16 -202 -48 C
ATOM 1337 N GLU A 640 79.361 86.354 37.194 1.00 19.17 N
ANISOU 1337 N GLU A 640 2434 2366 2486 45 -219 -186 N
ATOM 1338 CA GLU A 640 78.604 87.160 38.170 1.00 20.18 C
ANISOU 1338 CA GLU A 640 2550 2483 2635 85 -218 -271 C
ATOM 1339 C GLU A 640 78.422 88.557 37.630 1.00 21.03 C
ANISOU 1339 C GLU A 640 2728 2475 2787 117 -273 -295 C
ATOM 1340 O GLU A 640 77.328 89.107 37.675 1.00 20.91 O
ANISOU 1340 O GLU A 640 2700 2420 2825 192 -299 -355 O
ATOM 1341 CB GLU A 640 79.296 87.205 39.542 1.00 21.18 C
ANISOU 1341 CB GLU A 640 2671 2666 2712 39 -184 -306 C
ATOM 1342 CG GLU A 640 79.191 85.932 40.368 1.00 22.00 C
ANISOU 1342 CG GLU A 640 2727 2870 2761 21 -137 -297 C
ATOM 1343 CD GLU A 640 80.078 85.971 41.605 1.00 22.21 C
ANISOU 1343 CD GLU A 640 2772 2943 2722 -28 -131 -316 C
ATOM 1344 OE1 GLU A 640 80.799 86.991 41.778 1.00 23.85 O
ANISOU 1344 OE1 GLU A 640 3015 3111 2936 -51 -159 -343 O
ATOM 1345 OE2 GLU A 640 80.012 85.042 42.453 1.00 22.54 O
ANISOU 1345 OE2 GLU A 640 2806 3056 2702 -46 -102 -308 O
ATOM 1346 N ALA A 641 79.512 89.125 37.131 1.00 20.28 N
ANISOU 1346 N ALA A 641 2708 2322 2675 58 -289 -253 N
ATOM 1347 CA ALA A 641 79.500 90.505 36.637 1.00 21.93 C
ANISOU 1347 CA ALA A 641 3018 2400 2913 69 -340 -265 C
ATOM 1348 C ALA A 641 78.609 90.684 35.458 1.00 22.95 C
ANISOU 1348 C ALA A 641 3196 2450 3075 136 -405 -235 C
ATOM 1349 O ALA A 641 77.915 91.701 35.363 1.00 24.84 O
ANISOU 1349 O ALA A 641 3488 2588 3361 205 -467 -276 O
ATOM 1350 CB ALA A 641 80.923 90.979 36.270 1.00 22.53 C
ANISOU 1350 CB ALA A 641 3168 2435 2957 -36 -327 -224 C
ATOM 1351 N SER A 642 78.636 89.769 34.515 1.00 21.40 N
ANISOU 1351 N SER A 642 2993 2285 2854 122 -405 -168 N
ATOM 1352 CA ASER A 642 77.922 89.927 33.246 0.50 22.38 C
ANISOU 1352 CA ASER A 642 3185 2328 2989 173 -482 -129 C
ATOM 1353 CA BSER A 642 77.906 89.985 33.278 0.50 22.18 C
ANISOU 1353 CA BSER A 642 3161 2299 2966 175 -484 -132 C
ATOM 1354 C SER A 642 76.482 89.435 33.348 1.00 22.38 C
ANISOU 1354 C SER A 642 3087 2370 3046 277 -519 -178 C
ATOM 1355 O SER A 642 75.591 89.936 32.644 1.00 23.06 O
ANISOU 1355 O SER A 642 3213 2375 3172 359 -615 -187 O
ATOM 1356 CB ASER A 642 78.632 89.110 32.139 0.50 22.17 C
ANISOU 1356 CB ASER A 642 3199 2323 2902 99 -458 -42 C
ATOM 1357 CB BSER A 642 78.667 89.318 32.145 0.50 21.95 C
ANISOU 1357 CB BSER A 642 3187 2278 2875 99 -463 -44 C
ATOM 1358 OG ASER A 642 77.953 89.263 30.877 0.50 23.85 O
ANISOU 1358 OG ASER A 642 3500 2456 3105 142 -542 -1 O
ATOM 1359 OG BSER A 642 78.945 87.985 32.473 0.50 20.97 O
ANISOU 1359 OG BSER A 642 2954 2279 2734 69 -394 -36 O
ATOM 1360 N LEU A 643 76.279 88.368 34.137 1.00 21.16 N
ANISOU 1360 N LEU A 643 2808 2341 2890 267 -448 -207 N
ATOM 1361 CA LEU A 643 75.047 87.559 34.029 1.00 21.24 C
ANISOU 1361 CA LEU A 643 2716 2411 2943 327 -459 -242 C
ATOM 1362 C LEU A 643 74.364 87.267 35.381 1.00 21.26 C
ANISOU 1362 C LEU A 643 2598 2502 2978 347 -391 -336 C
ATOM 1363 O LEU A 643 73.324 86.606 35.413 1.00 21.40 O
ANISOU 1363 O LEU A 643 2518 2577 3036 381 -381 -381 O
ATOM 1364 CB LEU A 643 75.354 86.251 33.303 1.00 21.26 C
ANISOU 1364 CB LEU A 643 2707 2473 2898 275 -432 -171 C
ATOM 1365 CG LEU A 643 75.864 86.389 31.881 1.00 22.09 C
ANISOU 1365 CG LEU A 643 2928 2503 2961 249 -487 -89 C
ATOM 1366 CD1 LEU A 643 76.588 85.116 31.461 1.00 22.28 C
ANISOU 1366 CD1 LEU A 643 2941 2595 2930 175 -423 -30 C
ATOM 1367 CD2 LEU A 643 74.693 86.707 30.982 1.00 24.25 C
ANISOU 1367 CD2 LEU A 643 3221 2716 3276 335 -599 -104 C
ATOM 1368 N ARG A 644 74.929 87.780 36.470 1.00 20.93 N
ANISOU 1368 N ARG A 644 2568 2470 2915 316 -341 -372 N
ATOM 1369 CA ARG A 644 74.424 87.447 37.825 1.00 22.00 C
ANISOU 1369 CA ARG A 644 2614 2694 3050 311 -258 -456 C
ATOM 1370 C ARG A 644 74.275 85.928 37.923 1.00 21.09 C
ANISOU 1370 C ARG A 644 2436 2681 2896 262 -195 -421 C
ATOM 1371 O ARG A 644 73.220 85.417 38.324 1.00 21.01 O
ANISOU 1371 O ARG A 644 2336 2731 2917 277 -150 -486 O
ATOM 1372 CB ARG A 644 73.158 88.233 38.147 1.00 25.07 C
ANISOU 1372 CB ARG A 644 2939 3056 3529 403 -277 -576 C
ATOM 1373 CG ARG A 644 73.480 89.711 38.331 1.00 28.23 C
ANISOU 1373 CG ARG A 644 3420 3350 3955 441 -325 -614 C
ATOM 1374 CD ARG A 644 72.288 90.621 38.277 1.00 34.40 C
ANISOU 1374 CD ARG A 644 4157 4066 4847 560 -383 -724 C
ATOM 1375 NE ARG A 644 71.298 90.411 39.332 1.00 38.39 N
ANISOU 1375 NE ARG A 644 4531 4660 5397 586 -297 -857 N
ATOM 1376 CZ ARG A 644 71.251 91.027 40.524 1.00 40.79 C
ANISOU 1376 CZ ARG A 644 4824 4976 5699 582 -229 -960 C
ATOM 1377 NH1 ARG A 644 72.210 91.866 40.937 1.00 42.52 N
ANISOU 1377 NH1 ARG A 644 5154 5130 5870 549 -236 -945 N
ATOM 1378 NH2 ARG A 644 70.241 90.747 41.340 1.00 40.63 N
ANISOU 1378 NH2 ARG A 644 4679 5042 5718 599 -139 -1087 N
ATOM 1379 N PHE A 645 75.336 85.262 37.525 1.00 20.19 N
ANISOU 1379 N PHE A 645 2372 2578 2722 202 -191 -325 N
ATOM 1380 CA PHE A 645 75.366 83.803 37.390 1.00 18.98 C
ANISOU 1380 CA PHE A 645 2185 2492 2532 159 -149 -275 C
ATOM 1381 C PHE A 645 75.669 83.100 38.729 1.00 19.62 C
ANISOU 1381 C PHE A 645 2255 2651 2548 104 -71 -284 C
ATOM 1382 O PHE A 645 76.610 83.483 39.466 1.00 19.69 O
ANISOU 1382 O PHE A 645 2309 2663 2510 74 -67 -277 O
ATOM 1383 CB PHE A 645 76.443 83.427 36.401 1.00 18.83 C
ANISOU 1383 CB PHE A 645 2226 2446 2482 126 -178 -181 C
ATOM 1384 CG PHE A 645 76.674 81.977 36.244 1.00 18.08 C
ANISOU 1384 CG PHE A 645 2113 2404 2353 87 -141 -130 C
ATOM 1385 CD1 PHE A 645 75.747 81.177 35.593 1.00 17.76 C
ANISOU 1385 CD1 PHE A 645 2033 2378 2337 100 -142 -130 C
ATOM 1386 CD2 PHE A 645 77.807 81.390 36.762 1.00 18.23 C
ANISOU 1386 CD2 PHE A 645 2152 2453 2320 42 -113 -87 C
ATOM 1387 CE1 PHE A 645 75.987 79.827 35.409 1.00 18.61 C
ANISOU 1387 CE1 PHE A 645 2137 2520 2415 62 -108 -83 C
ATOM 1388 CE2 PHE A 645 78.057 80.031 36.588 1.00 18.36 C
ANISOU 1388 CE2 PHE A 645 2162 2502 2312 17 -88 -39 C
ATOM 1389 CZ PHE A 645 77.142 79.255 35.913 1.00 18.38 C
ANISOU 1389 CZ PHE A 645 2138 2509 2335 24 -81 -37 C
ATOM 1390 N GLU A 646 74.981 81.999 38.945 1.00 19.71 N
ANISOU 1390 N GLU A 646 2222 2719 2549 81 -19 -289 N
ATOM 1391 CA GLU A 646 75.368 80.985 39.955 1.00 20.36 C
ANISOU 1391 CA GLU A 646 2328 2860 2549 17 44 -261 C
ATOM 1392 C GLU A 646 75.390 79.634 39.311 1.00 19.64 C
ANISOU 1392 C GLU A 646 2236 2778 2446 -8 52 -195 C
ATOM 1393 O GLU A 646 74.421 79.220 38.652 1.00 19.60 O
ANISOU 1393 O GLU A 646 2179 2778 2490 0 60 -216 O
ATOM 1394 CB GLU A 646 74.407 80.931 41.104 1.00 20.57 C
ANISOU 1394 CB GLU A 646 2322 2939 2554 -9 127 -344 C
ATOM 1395 CG GLU A 646 74.240 82.176 41.942 1.00 21.59 C
ANISOU 1395 CG GLU A 646 2450 3066 2688 12 140 -434 C
ATOM 1396 CD GLU A 646 73.033 82.008 42.844 1.00 23.78 C
ANISOU 1396 CD GLU A 646 2672 3402 2961 -16 243 -535 C
ATOM 1397 OE1 GLU A 646 72.944 80.996 43.590 1.00 24.84 O
ANISOU 1397 OE1 GLU A 646 2838 3588 3011 -94 320 -516 O
ATOM 1398 OE2 GLU A 646 72.125 82.843 42.792 1.00 24.53 O
ANISOU 1398 OE2 GLU A 646 2692 3490 3139 36 252 -640 O
ATOM 1399 N HIS A 647 76.460 78.905 39.527 1.00 18.68 N
ANISOU 1399 N HIS A 647 2170 2660 2266 -38 45 -123 N
ATOM 1400 CA HIS A 647 76.553 77.607 38.904 1.00 18.85 C
ANISOU 1400 CA HIS A 647 2200 2679 2282 -56 50 -63 C
ATOM 1401 C HIS A 647 75.652 76.577 39.601 1.00 19.09 C
ANISOU 1401 C HIS A 647 2232 2744 2276 -107 124 -77 C
ATOM 1402 O HIS A 647 74.891 75.812 38.941 1.00 20.13 O
ANISOU 1402 O HIS A 647 2332 2876 2441 -123 146 -79 O
ATOM 1403 CB HIS A 647 77.982 77.091 38.886 1.00 18.73 C
ANISOU 1403 CB HIS A 647 2235 2649 2231 -59 15 8 C
ATOM 1404 CG HIS A 647 78.121 75.797 38.141 1.00 18.49 C
ANISOU 1404 CG HIS A 647 2216 2603 2206 -66 17 60 C
ATOM 1405 ND1 HIS A 647 77.728 74.585 38.671 1.00 18.56 N
ANISOU 1405 ND1 HIS A 647 2259 2619 2175 -102 57 83 N
ATOM 1406 CD2 HIS A 647 78.596 75.535 36.909 1.00 18.32 C
ANISOU 1406 CD2 HIS A 647 2187 2551 2221 -49 -9 89 C
ATOM 1407 CE1 HIS A 647 77.929 73.637 37.785 1.00 18.64 C
ANISOU 1407 CE1 HIS A 647 2277 2600 2207 -98 49 121 C
ATOM 1408 NE2 HIS A 647 78.482 74.185 36.704 1.00 19.21 N
ANISOU 1408 NE2 HIS A 647 2321 2653 2324 -65 11 122 N
ATOM 1409 N ARG A 648 75.734 76.581 40.938 1.00 18.85 N
ANISOU 1409 N ARG A 648 2247 2743 2172 -144 164 -91 N
ATOM 1410 CA ARG A 648 74.864 75.811 41.857 1.00 20.25 C
ANISOU 1410 CA ARG A 648 2448 2955 2292 -216 256 -115 C
ATOM 1411 C ARG A 648 75.109 74.284 41.883 1.00 20.08 C
ANISOU 1411 C ARG A 648 2501 2912 2217 -263 270 -36 C
ATOM 1412 O ARG A 648 74.460 73.621 42.655 1.00 22.78 O
ANISOU 1412 O ARG A 648 2886 3271 2497 -337 349 -47 O
ATOM 1413 CB ARG A 648 73.376 76.095 41.599 1.00 21.11 C
ANISOU 1413 CB ARG A 648 2454 3094 2472 -226 319 -212 C
ATOM 1414 CG ARG A 648 73.060 77.558 41.920 1.00 21.87 C
ANISOU 1414 CG ARG A 648 2494 3205 2610 -180 315 -303 C
ATOM 1415 CD ARG A 648 71.589 77.880 41.696 1.00 22.29 C
ANISOU 1415 CD ARG A 648 2426 3290 2753 -171 365 -416 C
ATOM 1416 NE ARG A 648 71.283 79.236 42.080 1.00 22.46 N
ANISOU 1416 NE ARG A 648 2400 3315 2818 -118 361 -511 N
ATOM 1417 CZ ARG A 648 70.075 79.780 42.025 1.00 23.23 C
ANISOU 1417 CZ ARG A 648 2381 3437 3009 -87 394 -633 C
ATOM 1418 NH1 ARG A 648 69.066 79.097 41.523 1.00 24.26 N
ANISOU 1418 NH1 ARG A 648 2418 3598 3203 -108 426 -674 N
ATOM 1419 NH2 ARG A 648 69.896 81.038 42.415 1.00 24.85 N
ANISOU 1419 NH2 ARG A 648 2555 3632 3256 -29 384 -721 N
ATOM 1420 N ASP A 649 76.081 73.797 41.153 1.00 20.66 N
ANISOU 1420 N ASP A 649 2599 2943 2306 -223 199 37 N
ATOM 1421 CA ASP A 649 76.405 72.344 41.202 1.00 21.49 C
ANISOU 1421 CA ASP A 649 2787 3011 2366 -253 200 110 C
ATOM 1422 C ASP A 649 77.826 72.093 40.813 1.00 19.96 C
ANISOU 1422 C ASP A 649 2623 2779 2181 -192 110 174 C
ATOM 1423 O ASP A 649 78.130 71.204 40.019 1.00 19.77 O
ANISOU 1423 O ASP A 649 2608 2714 2189 -176 90 213 O
ATOM 1424 CB ASP A 649 75.443 71.530 40.348 1.00 23.18 C
ANISOU 1424 CB ASP A 649 2964 3212 2630 -288 246 98 C
ATOM 1425 CG ASP A 649 75.468 70.023 40.704 1.00 26.10 C
ANISOU 1425 CG ASP A 649 3442 3536 2939 -345 275 160 C
ATOM 1426 OD1 ASP A 649 75.926 69.662 41.810 1.00 25.60 O
ANISOU 1426 OD1 ASP A 649 3489 3457 2780 -371 273 204 O
ATOM 1427 OD2 ASP A 649 75.077 69.240 39.823 1.00 29.35 O
ANISOU 1427 OD2 ASP A 649 3836 3918 3397 -361 287 165 O
ATOM 1428 N LEU A 650 78.751 72.884 41.350 1.00 20.27 N
ANISOU 1428 N LEU A 650 2670 2834 2200 -158 55 174 N
ATOM 1429 CA LEU A 650 80.120 72.832 40.874 1.00 20.19 C
ANISOU 1429 CA LEU A 650 2648 2800 2223 -100 -27 209 C
ATOM 1430 C LEU A 650 80.967 71.856 41.694 1.00 21.28 C
ANISOU 1430 C LEU A 650 2878 2910 2298 -87 -84 268 C
ATOM 1431 O LEU A 650 82.037 72.188 42.227 1.00 21.84 O
ANISOU 1431 O LEU A 650 2955 2989 2353 -51 -161 275 O
ATOM 1432 CB LEU A 650 80.715 74.212 40.834 1.00 21.23 C
ANISOU 1432 CB LEU A 650 2724 2958 2386 -74 -62 169 C
ATOM 1433 CG LEU A 650 81.938 74.481 39.985 1.00 24.40 C
ANISOU 1433 CG LEU A 650 3072 3346 2851 -31 -117 175 C
ATOM 1434 CD1 LEU A 650 82.128 73.782 38.711 1.00 25.28 C
ANISOU 1434 CD1 LEU A 650 3155 3427 3021 -12 -109 195 C
ATOM 1435 CD2 LEU A 650 82.107 75.994 39.816 1.00 25.63 C
ANISOU 1435 CD2 LEU A 650 3181 3519 3037 -33 -123 126 C
ATOM 1436 N HIS A 651 80.537 70.611 41.658 1.00 22.20 N
ANISOU 1436 N HIS A 651 3061 2983 2391 -110 -58 310 N
ATOM 1437 CA HIS A 651 81.306 69.517 42.211 1.00 22.63 C
ANISOU 1437 CA HIS A 651 3218 2984 2398 -83 -126 375 C
ATOM 1438 C HIS A 651 82.474 69.215 41.268 1.00 21.36 C
ANISOU 1438 C HIS A 651 2992 2795 2330 1 -196 382 C
ATOM 1439 O HIS A 651 82.575 69.739 40.172 1.00 21.07 O
ANISOU 1439 O HIS A 651 2852 2778 2377 18 -174 344 O
ATOM 1440 CB HIS A 651 80.436 68.288 42.480 1.00 23.84 C
ANISOU 1440 CB HIS A 651 3481 3084 2492 -146 -69 417 C
ATOM 1441 CG HIS A 651 79.794 67.714 41.262 1.00 22.95 C
ANISOU 1441 CG HIS A 651 3318 2946 2456 -161 -11 404 C
ATOM 1442 ND1 HIS A 651 80.454 66.897 40.362 1.00 24.59 N
ANISOU 1442 ND1 HIS A 651 3517 3095 2730 -103 -54 427 N
ATOM 1443 CD2 HIS A 651 78.526 67.805 40.814 1.00 24.99 C
ANISOU 1443 CD2 HIS A 651 3530 3230 2736 -228 83 361 C
ATOM 1444 CE1 HIS A 651 79.634 66.570 39.380 1.00 24.58 C
ANISOU 1444 CE1 HIS A 651 3475 3086 2778 -139 11 402 C
ATOM 1445 NE2 HIS A 651 78.451 67.079 39.647 1.00 25.10 N
ANISOU 1445 NE2 HIS A 651 3516 3202 2820 -214 88 364 N
ATOM 1446 N TRP A 652 83.418 68.405 41.748 1.00 21.10 N
ANISOU 1446 N TRP A 652 3023 2714 2280 56 -288 426 N
ATOM 1447 CA TRP A 652 84.674 68.239 41.018 1.00 21.50 C
ANISOU 1447 CA TRP A 652 2990 2751 2428 144 -358 411 C
ATOM 1448 C TRP A 652 84.595 67.411 39.743 1.00 21.53 C
ANISOU 1448 C TRP A 652 2961 2707 2511 164 -316 406 C
ATOM 1449 O TRP A 652 85.568 67.302 38.962 1.00 23.30 O
ANISOU 1449 O TRP A 652 3100 2927 2826 228 -346 374 O
ATOM 1450 CB TRP A 652 85.780 67.735 41.901 1.00 23.19 C
ANISOU 1450 CB TRP A 652 3258 2934 2620 217 -489 441 C
ATOM 1451 CG TRP A 652 85.624 66.406 42.559 1.00 24.26 C
ANISOU 1451 CG TRP A 652 3554 2978 2686 230 -537 515 C
ATOM 1452 CD1 TRP A 652 84.499 65.666 42.741 1.00 24.99 C
ANISOU 1452 CD1 TRP A 652 3771 3019 2705 156 -461 561 C
ATOM 1453 CD2 TRP A 652 86.693 65.697 43.209 1.00 25.69 C
ANISOU 1453 CD2 TRP A 652 3798 3101 2861 324 -685 550 C
ATOM 1454 NE1 TRP A 652 84.815 64.513 43.476 1.00 27.52 N
ANISOU 1454 NE1 TRP A 652 4252 3242 2962 190 -549 633 N
ATOM 1455 CE2 TRP A 652 86.148 64.554 43.799 1.00 26.98 C
ANISOU 1455 CE2 TRP A 652 4152 3168 2932 301 -697 629 C
ATOM 1456 CE3 TRP A 652 88.050 65.957 43.364 1.00 26.20 C
ANISOU 1456 CE3 TRP A 652 3774 3189 2993 423 -814 516 C
ATOM 1457 CZ2 TRP A 652 86.948 63.606 44.461 1.00 28.65 C
ANISOU 1457 CZ2 TRP A 652 4482 3288 3118 390 -848 685 C
ATOM 1458 CZ3 TRP A 652 88.843 65.066 44.076 1.00 28.17 C
ANISOU 1458 CZ3 TRP A 652 4116 3362 3224 517 -971 559 C
ATOM 1459 CH2 TRP A 652 88.289 63.901 44.619 1.00 29.23 C
ANISOU 1459 CH2 TRP A 652 4458 3386 3263 506 -993 649 C
ATOM 1460 N GLY A 653 83.444 66.840 39.492 1.00 21.55 N
ANISOU 1460 N GLY A 653 3023 2679 2484 103 -239 425 N
ATOM 1461 CA GLY A 653 83.193 66.279 38.184 1.00 21.25 C
ANISOU 1461 CA GLY A 653 2947 2611 2517 104 -188 405 C
ATOM 1462 C GLY A 653 82.900 67.309 37.087 1.00 20.76 C
ANISOU 1462 C GLY A 653 2772 2609 2505 80 -131 349 C
ATOM 1463 O GLY A 653 82.884 66.977 35.880 1.00 21.11 O
ANISOU 1463 O GLY A 653 2781 2636 2604 85 -98 326 O
ATOM 1464 N ASN A 654 82.582 68.550 37.526 1.00 19.83 N
ANISOU 1464 N ASN A 654 2617 2555 2361 50 -120 329 N
ATOM 1465 CA ASN A 654 82.201 69.631 36.638 1.00 19.65 C
ANISOU 1465 CA ASN A 654 2516 2576 2373 27 -80 284 C
ATOM 1466 C ASN A 654 83.310 70.664 36.375 1.00 20.13 C
ANISOU 1466 C ASN A 654 2504 2670 2474 58 -112 254 C
ATOM 1467 O ASN A 654 83.036 71.714 35.813 1.00 19.61 O
ANISOU 1467 O ASN A 654 2398 2630 2422 35 -87 225 O
ATOM 1468 CB ASN A 654 80.909 70.246 37.144 1.00 20.19 C
ANISOU 1468 CB ASN A 654 2594 2677 2400 -28 -37 270 C
ATOM 1469 CG ASN A 654 79.700 69.394 36.889 1.00 21.60 C
ANISOU 1469 CG ASN A 654 2804 2834 2569 -77 17 273 C
ATOM 1470 OD1 ASN A 654 79.721 68.477 36.044 1.00 22.98 O
ANISOU 1470 OD1 ASN A 654 2991 2967 2773 -73 24 282 O
ATOM 1471 ND2 ASN A 654 78.647 69.644 37.625 1.00 20.76 N
ANISOU 1471 ND2 ASN A 654 2708 2755 2424 -129 60 255 N
ATOM 1472 N VAL A 655 84.528 70.322 36.748 1.00 19.36 N
ANISOU 1472 N VAL A 655 2393 2566 2398 107 -168 258 N
ATOM 1473 CA VAL A 655 85.717 71.092 36.491 1.00 20.63 C
ANISOU 1473 CA VAL A 655 2471 2759 2610 129 -194 218 C
ATOM 1474 C VAL A 655 86.586 70.262 35.553 1.00 20.44 C
ANISOU 1474 C VAL A 655 2402 2708 2656 171 -188 197 C
ATOM 1475 O VAL A 655 87.092 69.219 35.950 1.00 21.17 O
ANISOU 1475 O VAL A 655 2513 2765 2765 229 -239 212 O
ATOM 1476 CB VAL A 655 86.488 71.389 37.771 1.00 20.41 C
ANISOU 1476 CB VAL A 655 2441 2755 2560 156 -275 219 C
ATOM 1477 CG1 VAL A 655 87.799 72.128 37.478 1.00 22.01 C
ANISOU 1477 CG1 VAL A 655 2537 2995 2831 169 -300 163 C
ATOM 1478 CG2 VAL A 655 85.596 72.193 38.719 1.00 22.15 C
ANISOU 1478 CG2 VAL A 655 2713 3001 2702 109 -267 229 C
ATOM 1479 N LEU A 656 86.736 70.713 34.317 1.00 19.43 N
ANISOU 1479 N LEU A 656 2227 2592 2565 142 -126 159 N
ATOM 1480 CA LEU A 656 87.575 70.017 33.340 1.00 20.14 C
ANISOU 1480 CA LEU A 656 2268 2664 2720 170 -98 120 C
ATOM 1481 C LEU A 656 88.898 70.686 33.158 1.00 20.67 C
ANISOU 1481 C LEU A 656 2231 2774 2849 173 -97 58 C
ATOM 1482 O LEU A 656 89.006 71.908 33.177 1.00 20.87 O
ANISOU 1482 O LEU A 656 2232 2836 2861 120 -81 43 O
ATOM 1483 CB LEU A 656 86.898 69.874 31.961 1.00 20.84 C
ANISOU 1483 CB LEU A 656 2388 2733 2798 125 -19 112 C
ATOM 1484 CG LEU A 656 85.483 69.296 31.993 1.00 21.43 C
ANISOU 1484 CG LEU A 656 2549 2774 2822 106 -13 157 C
ATOM 1485 CD1 LEU A 656 85.016 69.142 30.515 1.00 22.00 C
ANISOU 1485 CD1 LEU A 656 2642 2830 2888 67 49 136 C
ATOM 1486 CD2 LEU A 656 85.362 67.983 32.768 1.00 21.94 C
ANISOU 1486 CD2 LEU A 656 2663 2789 2884 152 -53 191 C
ATOM 1487 N LEU A 657 89.919 69.881 32.941 1.00 19.93 N
ANISOU 1487 N LEU A 657 2070 2671 2830 232 -109 13 N
ATOM 1488 CA LEU A 657 91.243 70.301 32.745 1.00 21.59 C
ANISOU 1488 CA LEU A 657 2157 2927 3120 238 -102 -65 C
ATOM 1489 C LEU A 657 91.786 69.860 31.413 1.00 22.00 C
ANISOU 1489 C LEU A 657 2155 2975 3229 227 -7 -134 C
ATOM 1490 O LEU A 657 91.735 68.688 31.080 1.00 23.01 O
ANISOU 1490 O LEU A 657 2303 3056 3384 285 -4 -139 O
ATOM 1491 CB LEU A 657 92.157 69.672 33.867 1.00 23.07 C
ANISOU 1491 CB LEU A 657 2285 3113 3366 340 -224 -80 C
ATOM 1492 CG LEU A 657 91.644 69.942 35.281 1.00 24.33 C
ANISOU 1492 CG LEU A 657 2523 3273 3450 351 -324 -10 C
ATOM 1493 CD1 LEU A 657 92.547 69.172 36.268 1.00 26.72 C
ANISOU 1493 CD1 LEU A 657 2792 3560 3800 461 -461 -19 C
ATOM 1494 CD2 LEU A 657 91.648 71.417 35.563 1.00 24.37 C
ANISOU 1494 CD2 LEU A 657 2501 3335 3423 273 -308 -25 C
ATOM 1495 N LYS A 658 92.402 70.780 30.710 1.00 23.11 N
ANISOU 1495 N LYS A 658 2229 3162 3390 151 74 -195 N
ATOM 1496 CA LYS A 658 93.083 70.497 29.440 1.00 26.70 C
ANISOU 1496 CA LYS A 658 2624 3625 3894 121 186 -280 C
ATOM 1497 C LYS A 658 94.423 71.116 29.386 1.00 26.54 C
ANISOU 1497 C LYS A 658 2457 3670 3959 90 223 -381 C
ATOM 1498 O LYS A 658 94.638 72.265 29.813 1.00 25.36 O
ANISOU 1498 O LYS A 658 2283 3557 3794 26 213 -380 O
ATOM 1499 CB LYS A 658 92.199 71.030 28.272 1.00 28.55 C
ANISOU 1499 CB LYS A 658 2974 3842 4031 16 285 -249 C
ATOM 1500 CG LYS A 658 92.736 70.712 26.889 1.00 34.31 C
ANISOU 1500 CG LYS A 658 3684 4577 4777 -32 412 -329 C
ATOM 1501 CD LYS A 658 91.862 71.377 25.797 1.00 38.86 C
ANISOU 1501 CD LYS A 658 4398 5131 5235 -141 486 -287 C
ATOM 1502 CE LYS A 658 90.773 70.422 25.334 1.00 43.23 C
ANISOU 1502 CE LYS A 658 5058 5631 5735 -108 470 -241 C
ATOM 1503 NZ LYS A 658 90.398 70.566 23.863 1.00 50.37 N
ANISOU 1503 NZ LYS A 658 6067 6519 6552 -200 564 -253 N
ATOM 1504 N LYS A 659 95.361 70.401 28.799 1.00 28.98 N
ANISOU 1504 N LYS A 659 2656 3991 4362 125 278 -482 N
ATOM 1505 CA LYS A 659 96.727 70.900 28.645 1.00 31.53 C
ANISOU 1505 CA LYS A 659 2807 4387 4788 89 333 -606 C
ATOM 1506 C LYS A 659 96.758 72.122 27.736 1.00 32.47 C
ANISOU 1506 C LYS A 659 2960 4535 4841 -80 475 -626 C
ATOM 1507 O LYS A 659 95.998 72.195 26.780 1.00 32.76 O
ANISOU 1507 O LYS A 659 3131 4535 4779 -150 559 -582 O
ATOM 1508 CB LYS A 659 97.658 69.823 28.079 1.00 38.13 C
ANISOU 1508 CB LYS A 659 3512 5229 5747 163 383 -728 C
ATOM 1509 CG LYS A 659 97.920 68.737 29.087 1.00 43.48 C
ANISOU 1509 CG LYS A 659 4136 5872 6512 338 222 -724 C
ATOM 1510 CD LYS A 659 99.191 67.944 28.793 1.00 48.89 C
ANISOU 1510 CD LYS A 659 4630 6580 7364 429 240 -878 C
ATOM 1511 CE LYS A 659 99.018 66.520 29.305 1.00 52.98 C
ANISOU 1511 CE LYS A 659 5188 7011 7931 604 109 -847 C
ATOM 1512 NZ LYS A 659 100.254 65.704 29.068 1.00 58.73 N
ANISOU 1512 NZ LYS A 659 5724 7750 8841 720 106 -1006 N
ATOM 1513 N THR A 660 97.535 73.108 28.103 1.00 32.45 N
ANISOU 1513 N THR A 660 2860 4588 4880 -148 483 -679 N
ATOM 1514 CA THR A 660 97.787 74.289 27.256 1.00 34.25 C
ANISOU 1514 CA THR A 660 3117 4839 5058 -322 626 -713 C
ATOM 1515 C THR A 660 99.259 74.606 27.280 1.00 36.41 C
ANISOU 1515 C THR A 660 3181 5193 5459 -372 688 -862 C
ATOM 1516 O THR A 660 99.929 74.437 28.313 1.00 36.20 O
ANISOU 1516 O THR A 660 3006 5208 5540 -284 572 -910 O
ATOM 1517 CB THR A 660 96.948 75.520 27.682 1.00 32.37 C
ANISOU 1517 CB THR A 660 3020 4569 4710 -395 579 -606 C
ATOM 1518 OG1 THR A 660 97.244 76.618 26.810 1.00 34.10 O
ANISOU 1518 OG1 THR A 660 3287 4792 4878 -566 715 -636 O
ATOM 1519 CG2 THR A 660 97.259 75.943 29.109 1.00 32.37 C
ANISOU 1519 CG2 THR A 660 2937 4599 4762 -344 443 -603 C
ATOM 1520 N SER A 661 99.808 75.083 26.156 1.00 39.38 N
ANISOU 1520 N SER A 661 3543 5595 5824 -520 871 -945 N
ATOM 1521 CA SER A 661 101.171 75.589 26.181 1.00 41.14 C
ANISOU 1521 CA SER A 661 3564 5901 6165 -604 950 -1095 C
ATOM 1522 C SER A 661 101.224 77.067 26.507 1.00 39.59 C
ANISOU 1522 C SER A 661 3417 5709 5917 -748 960 -1066 C
ATOM 1523 O SER A 661 102.292 77.594 26.638 1.00 41.03 O
ANISOU 1523 O SER A 661 3437 5958 6193 -831 1015 -1186 O
ATOM 1524 CB SER A 661 101.856 75.343 24.832 1.00 45.55 C
ANISOU 1524 CB SER A 661 4069 6493 6745 -710 1166 -1221 C
ATOM 1525 OG SER A 661 101.054 75.977 23.840 1.00 48.08 O
ANISOU 1525 OG SER A 661 4626 6753 6888 -853 1277 -1131 O
ATOM 1526 N LEU A 662 100.091 77.744 26.657 1.00 37.39 N
ANISOU 1526 N LEU A 662 3351 5357 5499 -776 904 -920 N
ATOM 1527 CA LEU A 662 100.097 79.136 27.137 1.00 37.95 C
ANISOU 1527 CA LEU A 662 3475 5416 5530 -889 886 -891 C
ATOM 1528 C LEU A 662 100.591 79.224 28.573 1.00 37.34 C
ANISOU 1528 C LEU A 662 3245 5389 5554 -801 730 -925 C
ATOM 1529 O LEU A 662 100.088 78.491 29.432 1.00 36.45 O
ANISOU 1529 O LEU A 662 3134 5265 5450 -639 576 -864 O
ATOM 1530 CB LEU A 662 98.694 79.735 27.093 1.00 37.66 C
ANISOU 1530 CB LEU A 662 3689 5283 5338 -898 833 -732 C
ATOM 1531 CG LEU A 662 98.076 79.883 25.689 1.00 39.77 C
ANISOU 1531 CG LEU A 662 4148 5485 5475 -996 959 -679 C
ATOM 1532 CD1 LEU A 662 96.602 80.179 25.844 1.00 39.07 C
ANISOU 1532 CD1 LEU A 662 4267 5310 5269 -942 854 -530 C
ATOM 1533 CD2 LEU A 662 98.776 81.004 24.939 1.00 42.48 C
ANISOU 1533 CD2 LEU A 662 4533 5824 5784 -1207 1116 -735 C
ATOM 1534 N LYS A 663 101.524 80.113 28.827 1.00 37.76 N
ANISOU 1534 N LYS A 663 3186 5491 5672 -917 768 -1019 N
ATOM 1535 CA LYS A 663 102.049 80.323 30.185 1.00 39.17 C
ANISOU 1535 CA LYS A 663 3224 5720 5939 -852 613 -1062 C
ATOM 1536 C LYS A 663 101.070 81.110 31.051 1.00 37.74 C
ANISOU 1536 C LYS A 663 3213 5475 5650 -840 494 -937 C
ATOM 1537 O LYS A 663 101.043 80.924 32.291 1.00 36.94 O
ANISOU 1537 O LYS A 663 3063 5396 5578 -728 326 -923 O
ATOM 1538 CB LYS A 663 103.414 81.018 30.164 1.00 43.37 C
ANISOU 1538 CB LYS A 663 3559 6333 6587 -991 694 -1224 C
ATOM 1539 CG LYS A 663 104.480 80.100 29.586 1.00 47.46 C
ANISOU 1539 CG LYS A 663 3850 6934 7250 -963 781 -1378 C
ATOM 1540 CD LYS A 663 105.819 80.784 29.503 1.00 52.51 C
ANISOU 1540 CD LYS A 663 4275 7662 8013 -1115 879 -1556 C
ATOM 1541 CE LYS A 663 106.863 79.820 28.978 1.00 56.15 C
ANISOU 1541 CE LYS A 663 4485 8212 8637 -1069 962 -1728 C
ATOM 1542 NZ LYS A 663 108.153 80.548 28.895 1.00 59.74 N
ANISOU 1542 NZ LYS A 663 4715 8762 9221 -1236 1071 -1915 N
ATOM 1543 N LYS A 664 100.304 82.011 30.417 1.00 35.80 N
ANISOU 1543 N LYS A 664 3170 5149 5282 -954 578 -854 N
ATOM 1544 CA LYS A 664 99.385 82.931 31.124 1.00 35.02 C
ANISOU 1544 CA LYS A 664 3234 4981 5089 -958 487 -754 C
ATOM 1545 C LYS A 664 98.042 82.858 30.415 1.00 31.64 C
ANISOU 1545 C LYS A 664 3026 4463 4535 -935 511 -625 C
ATOM 1546 O LYS A 664 97.983 82.788 29.192 1.00 32.27 O
ANISOU 1546 O LYS A 664 3178 4513 4570 -1010 637 -619 O
ATOM 1547 CB LYS A 664 99.845 84.380 31.038 1.00 38.48 C
ANISOU 1547 CB LYS A 664 3708 5396 5517 -1139 558 -796 C
ATOM 1548 CG LYS A 664 101.197 84.706 31.647 1.00 44.72 C
ANISOU 1548 CG LYS A 664 4284 6275 6433 -1205 549 -939 C
ATOM 1549 CD LYS A 664 101.366 86.214 31.742 1.00 49.61 C
ANISOU 1549 CD LYS A 664 4987 6844 7018 -1379 594 -955 C
ATOM 1550 CE LYS A 664 101.200 86.915 30.378 1.00 53.29 C
ANISOU 1550 CE LYS A 664 5622 7227 7398 -1553 775 -924 C
ATOM 1551 NZ LYS A 664 101.794 88.299 30.374 1.00 57.02 N
ANISOU 1551 NZ LYS A 664 6130 7662 7872 -1757 850 -982 N
ATOM 1552 N LEU A 665 96.981 82.854 31.176 1.00 28.81 N
ANISOU 1552 N LEU A 665 2768 4062 4117 -833 391 -531 N
ATOM 1553 CA LEU A 665 95.639 82.912 30.613 1.00 27.55 C
ANISOU 1553 CA LEU A 665 2803 3818 3848 -808 395 -419 C
ATOM 1554 C LEU A 665 95.058 84.280 30.933 1.00 28.47 C
ANISOU 1554 C LEU A 665 3056 3859 3901 -870 366 -375 C
ATOM 1555 O LEU A 665 95.503 84.936 31.847 1.00 29.80 O
ANISOU 1555 O LEU A 665 3171 4046 4105 -895 316 -418 O
ATOM 1556 CB LEU A 665 94.797 81.835 31.215 1.00 25.78 C
ANISOU 1556 CB LEU A 665 2581 3601 3612 -648 292 -358 C
ATOM 1557 CG LEU A 665 95.368 80.424 31.009 1.00 26.64 C
ANISOU 1557 CG LEU A 665 2563 3768 3791 -569 301 -401 C
ATOM 1558 CD1 LEU A 665 94.543 79.442 31.787 1.00 26.30 C
ANISOU 1558 CD1 LEU A 665 2542 3720 3730 -423 189 -336 C
ATOM 1559 CD2 LEU A 665 95.480 80.015 29.562 1.00 27.35 C
ANISOU 1559 CD2 LEU A 665 2683 3845 3864 -625 432 -417 C
ATOM 1560 N HIS A 666 94.112 84.738 30.095 1.00 27.47 N
ANISOU 1560 N HIS A 666 3112 3642 3684 -900 397 -297 N
ATOM 1561 CA HIS A 666 93.599 86.098 30.161 1.00 27.86 C
ANISOU 1561 CA HIS A 666 3312 3598 3678 -963 379 -260 C
ATOM 1562 C HIS A 666 92.111 86.097 30.482 1.00 24.41 C
ANISOU 1562 C HIS A 666 2987 3102 3185 -846 280 -175 C
ATOM 1563 O HIS A 666 91.387 85.225 30.008 1.00 24.54 O
ANISOU 1563 O HIS A 666 3029 3121 3173 -769 270 -127 O
ATOM 1564 CB HIS A 666 93.791 86.744 28.803 1.00 29.78 C
ANISOU 1564 CB HIS A 666 3690 3767 3858 -1106 493 -246 C
ATOM 1565 CG HIS A 666 95.215 86.929 28.427 1.00 32.85 C
ANISOU 1565 CG HIS A 666 3979 4206 4297 -1253 616 -341 C
ATOM 1566 ND1 HIS A 666 95.896 88.079 28.700 1.00 36.76 N
ANISOU 1566 ND1 HIS A 666 4483 4673 4811 -1385 650 -390 N
ATOM 1567 CD2 HIS A 666 96.114 86.073 27.898 1.00 34.05 C
ANISOU 1567 CD2 HIS A 666 3995 4443 4500 -1286 712 -413 C
ATOM 1568 CE1 HIS A 666 97.148 87.969 28.284 1.00 38.03 C
ANISOU 1568 CE1 HIS A 666 4520 4901 5028 -1509 773 -489 C
ATOM 1569 NE2 HIS A 666 97.308 86.751 27.806 1.00 37.75 N
ANISOU 1569 NE2 HIS A 666 4388 4938 5017 -1445 812 -508 N
ATOM 1570 N TYR A 667 91.666 87.049 31.291 1.00 23.85 N
ANISOU 1570 N TYR A 667 2973 2983 3107 -834 213 -169 N
ATOM 1571 CA TYR A 667 90.246 87.319 31.518 1.00 23.08 C
ANISOU 1571 CA TYR A 667 2986 2819 2965 -740 134 -107 C
ATOM 1572 C TYR A 667 90.108 88.851 31.608 1.00 23.40 C
ANISOU 1572 C TYR A 667 3153 2753 2986 -807 119 -109 C
ATOM 1573 O TYR A 667 91.078 89.591 31.891 1.00 23.66 O
ANISOU 1573 O TYR A 667 3163 2783 3046 -912 154 -164 O
ATOM 1574 CB TYR A 667 89.639 86.640 32.771 1.00 22.96 C
ANISOU 1574 CB TYR A 667 2887 2867 2971 -612 50 -109 C
ATOM 1575 CG TYR A 667 90.105 87.226 34.076 1.00 23.67 C
ANISOU 1575 CG TYR A 667 2920 2985 3089 -621 5 -166 C
ATOM 1576 CD1 TYR A 667 91.305 86.792 34.627 1.00 24.92 C
ANISOU 1576 CD1 TYR A 667 2940 3232 3296 -649 7 -224 C
ATOM 1577 CD2 TYR A 667 89.437 88.228 34.712 1.00 23.15 C
ANISOU 1577 CD2 TYR A 667 2932 2857 3006 -605 -42 -172 C
ATOM 1578 CE1 TYR A 667 91.761 87.315 35.783 1.00 25.69 C
ANISOU 1578 CE1 TYR A 667 2991 3359 3412 -662 -45 -279 C
ATOM 1579 CE2 TYR A 667 89.867 88.742 35.890 1.00 25.55 C
ANISOU 1579 CE2 TYR A 667 3193 3188 3327 -620 -81 -230 C
ATOM 1580 CZ TYR A 667 91.073 88.296 36.426 1.00 25.44 C
ANISOU 1580 CZ TYR A 667 3049 3266 3350 -655 -85 -282 C
ATOM 1581 OH TYR A 667 91.566 88.793 37.591 1.00 27.23 O
ANISOU 1581 OH TYR A 667 3234 3526 3588 -675 -137 -345 O
ATOM 1582 N THR A 668 88.872 89.310 31.409 1.00 22.42 N
ANISOU 1582 N THR A 668 3156 2538 2823 -740 61 -58 N
ATOM 1583 CA THR A 668 88.555 90.720 31.608 1.00 22.84 C
ANISOU 1583 CA THR A 668 3337 2474 2866 -768 24 -61 C
ATOM 1584 C THR A 668 87.332 90.805 32.475 1.00 22.43 C
ANISOU 1584 C THR A 668 3284 2411 2829 -632 -67 -62 C
ATOM 1585 O THR A 668 86.337 90.119 32.198 1.00 20.61 O
ANISOU 1585 O THR A 668 3051 2193 2587 -533 -102 -25 O
ATOM 1586 CB THR A 668 88.315 91.421 30.252 1.00 24.01 C
ANISOU 1586 CB THR A 668 3679 2491 2952 -835 44 -1 C
ATOM 1587 OG1 THR A 668 89.421 91.196 29.385 1.00 25.51 O
ANISOU 1587 OG1 THR A 668 3867 2707 3119 -973 153 -6 O
ATOM 1588 CG2 THR A 668 88.116 92.917 30.441 1.00 25.33 C
ANISOU 1588 CG2 THR A 668 3994 2516 3113 -872 4 -5 C
ATOM 1589 N LEU A 669 87.451 91.554 33.573 1.00 21.76 N
ANISOU 1589 N LEU A 669 3181 2315 2770 -632 -96 -117 N
ATOM 1590 CA LEU A 669 86.361 91.771 34.515 1.00 23.22 C
ANISOU 1590 CA LEU A 669 3362 2490 2969 -517 -164 -142 C
ATOM 1591 C LEU A 669 86.019 93.276 34.555 1.00 25.23 C
ANISOU 1591 C LEU A 669 3757 2600 3231 -531 -201 -162 C
ATOM 1592 O LEU A 669 86.855 94.091 34.953 1.00 25.43 O
ANISOU 1592 O LEU A 669 3805 2592 3265 -625 -182 -206 O
ATOM 1593 CB LEU A 669 86.742 91.295 35.896 1.00 23.48 C
ANISOU 1593 CB LEU A 669 3265 2638 3019 -498 -171 -199 C
ATOM 1594 CG LEU A 669 85.703 91.492 36.999 1.00 24.29 C
ANISOU 1594 CG LEU A 669 3359 2745 3124 -400 -217 -241 C
ATOM 1595 CD1 LEU A 669 84.499 90.601 36.793 1.00 24.64 C
ANISOU 1595 CD1 LEU A 669 3376 2821 3164 -293 -231 -206 C
ATOM 1596 CD2 LEU A 669 86.338 91.234 38.357 1.00 25.66 C
ANISOU 1596 CD2 LEU A 669 3442 3017 3290 -417 -224 -299 C
ATOM 1597 N ASN A 670 84.755 93.595 34.182 1.00 25.12 N
ANISOU 1597 N ASN A 670 3827 2498 3219 -429 -262 -138 N
ATOM 1598 CA ASN A 670 84.280 94.968 34.098 1.00 26.62 C
ANISOU 1598 CA ASN A 670 4163 2528 3423 -412 -315 -152 C
ATOM 1599 C ASN A 670 85.294 95.893 33.469 1.00 27.38 C
ANISOU 1599 C ASN A 670 4393 2518 3493 -559 -279 -132 C
ATOM 1600 O ASN A 670 85.587 96.982 33.983 1.00 28.68 O
ANISOU 1600 O ASN A 670 4626 2595 3675 -606 -288 -180 O
ATOM 1601 CB ASN A 670 83.863 95.454 35.475 1.00 28.02 C
ANISOU 1601 CB ASN A 670 4288 2717 3641 -348 -341 -242 C
ATOM 1602 CG ASN A 670 82.676 94.701 36.010 1.00 28.30 C
ANISOU 1602 CG ASN A 670 4220 2833 3699 -211 -368 -267 C
ATOM 1603 OD1 ASN A 670 81.710 94.414 35.278 1.00 28.79 O
ANISOU 1603 OD1 ASN A 670 4301 2865 3772 -124 -411 -230 O
ATOM 1604 ND2 ASN A 670 82.746 94.335 37.284 1.00 29.05 N
ANISOU 1604 ND2 ASN A 670 4206 3036 3796 -199 -342 -332 N
ATOM 1605 N GLY A 671 85.865 95.446 32.375 1.00 27.65 N
ANISOU 1605 N GLY A 671 4463 2561 3482 -645 -228 -70 N
ATOM 1606 CA GLY A 671 86.736 96.236 31.559 1.00 29.05 C
ANISOU 1606 CA GLY A 671 4785 2633 3618 -800 -176 -42 C
ATOM 1607 C GLY A 671 88.201 96.166 31.921 1.00 30.78 C
ANISOU 1607 C GLY A 671 4906 2939 3850 -955 -77 -95 C
ATOM 1608 O GLY A 671 88.999 96.743 31.209 1.00 32.60 O
ANISOU 1608 O GLY A 671 5242 3097 4048 -1108 -10 -81 O
ATOM 1609 N LYS A 672 88.555 95.533 33.034 1.00 29.79 N
ANISOU 1609 N LYS A 672 4588 2958 3771 -922 -71 -160 N
ATOM 1610 CA LYS A 672 89.943 95.465 33.475 1.00 31.63 C
ANISOU 1610 CA LYS A 672 4705 3281 4031 -1052 -1 -225 C
ATOM 1611 C LYS A 672 90.485 94.091 33.165 1.00 30.33 C
ANISOU 1611 C LYS A 672 4385 3266 3873 -1051 50 -217 C
ATOM 1612 O LYS A 672 89.967 93.105 33.673 1.00 27.96 O
ANISOU 1612 O LYS A 672 3977 3062 3584 -927 8 -211 O
ATOM 1613 CB LYS A 672 90.025 95.690 34.957 1.00 35.72 C
ANISOU 1613 CB LYS A 672 5126 3856 4591 -1012 -50 -307 C
ATOM 1614 CG LYS A 672 91.479 95.657 35.444 1.00 42.22 C
ANISOU 1614 CG LYS A 672 5819 4774 5450 -1143 -2 -384 C
ATOM 1615 CD LYS A 672 91.570 96.206 36.861 1.00 48.09 C
ANISOU 1615 CD LYS A 672 6519 5536 6216 -1128 -61 -468 C
ATOM 1616 CE LYS A 672 93.015 96.201 37.336 1.00 53.11 C
ANISOU 1616 CE LYS A 672 7018 6268 6893 -1256 -33 -554 C
ATOM 1617 NZ LYS A 672 93.073 96.755 38.718 1.00 57.25 N
ANISOU 1617 NZ LYS A 672 7518 6809 7427 -1244 -103 -637 N
ATOM 1618 N SER A 673 91.502 94.023 32.345 1.00 31.05 N
ANISOU 1618 N SER A 673 4468 3372 3957 -1190 146 -223 N
ATOM 1619 CA SER A 673 92.052 92.735 31.980 1.00 30.95 C
ANISOU 1619 CA SER A 673 4308 3492 3960 -1185 201 -228 C
ATOM 1620 C SER A 673 93.162 92.333 32.940 1.00 31.21 C
ANISOU 1620 C SER A 673 4133 3658 4066 -1215 208 -321 C
ATOM 1621 O SER A 673 93.935 93.188 33.372 1.00 30.55 O
ANISOU 1621 O SER A 673 4036 3559 4013 -1326 225 -388 O
ATOM 1622 CB SER A 673 92.602 92.816 30.602 1.00 34.20 C
ANISOU 1622 CB SER A 673 4804 3861 4329 -1320 311 -203 C
ATOM 1623 OG SER A 673 91.543 92.895 29.705 1.00 35.44 O
ANISOU 1623 OG SER A 673 5139 3916 4412 -1266 282 -111 O
ATOM 1624 N SER A 674 93.250 91.034 33.229 1.00 29.37 N
ANISOU 1624 N SER A 674 3749 3550 3862 -1119 188 -327 N
ATOM 1625 CA SER A 674 94.308 90.477 34.056 1.00 31.31 C
ANISOU 1625 CA SER A 674 3795 3924 4178 -1125 173 -411 C
ATOM 1626 C SER A 674 94.739 89.134 33.511 1.00 29.80 C
ANISOU 1626 C SER A 674 3479 3828 4017 -1085 214 -413 C
ATOM 1627 O SER A 674 94.152 88.610 32.542 1.00 27.67 O
ANISOU 1627 O SER A 674 3281 3527 3704 -1054 255 -348 O
ATOM 1628 CB SER A 674 93.836 90.259 35.459 1.00 33.20 C
ANISOU 1628 CB SER A 674 3985 4208 4420 -1005 56 -422 C
ATOM 1629 OG SER A 674 93.689 91.458 36.170 1.00 38.00 O
ANISOU 1629 OG SER A 674 4670 4751 5018 -1046 18 -454 O
ATOM 1630 N THR A 675 95.798 88.594 34.124 1.00 29.02 N
ANISOU 1630 N THR A 675 3191 3840 3995 -1086 195 -495 N
ATOM 1631 CA THR A 675 96.283 87.292 33.706 1.00 29.80 C
ANISOU 1631 CA THR A 675 3156 4026 4140 -1032 223 -513 C
ATOM 1632 C THR A 675 96.420 86.328 34.897 1.00 28.17 C
ANISOU 1632 C THR A 675 2818 3911 3975 -894 99 -533 C
ATOM 1633 O THR A 675 96.462 86.746 36.055 1.00 29.41 O
ANISOU 1633 O THR A 675 2958 4085 4133 -872 5 -558 O
ATOM 1634 CB THR A 675 97.640 87.360 33.018 1.00 32.43 C
ANISOU 1634 CB THR A 675 3365 4411 4547 -1167 336 -611 C
ATOM 1635 OG1 THR A 675 98.595 87.918 33.911 1.00 33.99 O
ANISOU 1635 OG1 THR A 675 3437 4662 4817 -1228 293 -710 O
ATOM 1636 CG2 THR A 675 97.558 88.264 31.806 1.00 34.65 C
ANISOU 1636 CG2 THR A 675 3801 4596 4768 -1322 469 -586 C
ATOM 1637 N ILE A 676 96.435 85.057 34.563 1.00 27.36 N
ANISOU 1637 N ILE A 676 2646 3853 3895 -804 101 -517 N
ATOM 1638 CA ILE A 676 96.573 83.986 35.546 1.00 27.82 C
ANISOU 1638 CA ILE A 676 2602 3981 3986 -668 -16 -523 C
ATOM 1639 C ILE A 676 97.639 83.023 35.037 1.00 28.20 C
ANISOU 1639 C ILE A 676 2481 4101 4134 -651 19 -596 C
ATOM 1640 O ILE A 676 97.484 82.473 33.953 1.00 27.68 O
ANISOU 1640 O ILE A 676 2435 4018 4065 -654 113 -576 O
ATOM 1641 CB ILE A 676 95.276 83.188 35.713 1.00 26.34 C
ANISOU 1641 CB ILE A 676 2524 3759 3725 -545 -63 -419 C
ATOM 1642 CG1 ILE A 676 94.128 84.118 36.094 1.00 26.49 C
ANISOU 1642 CG1 ILE A 676 2699 3708 3658 -556 -83 -361 C
ATOM 1643 CG2 ILE A 676 95.491 82.111 36.793 1.00 26.96 C
ANISOU 1643 CG2 ILE A 676 2522 3896 3825 -420 -187 -422 C
ATOM 1644 CD1 ILE A 676 92.761 83.501 36.143 1.00 26.36 C
ANISOU 1644 CD1 ILE A 676 2785 3655 3574 -460 -106 -273 C
ATOM 1645 N PRO A 677 98.683 82.719 35.847 1.00 29.48 N
ANISOU 1645 N PRO A 677 2474 4343 4384 -614 -70 -683 N
ATOM 1646 CA PRO A 677 99.593 81.657 35.377 1.00 29.98 C
ANISOU 1646 CA PRO A 677 2369 4468 4555 -563 -50 -756 C
ATOM 1647 C PRO A 677 98.905 80.321 35.262 1.00 28.92 C
ANISOU 1647 C PRO A 677 2285 4310 4394 -419 -88 -678 C
ATOM 1648 O PRO A 677 98.138 79.920 36.156 1.00 29.67 O
ANISOU 1648 O PRO A 677 2469 4381 4422 -318 -203 -597 O
ATOM 1649 CB PRO A 677 100.678 81.604 36.485 1.00 31.91 C
ANISOU 1649 CB PRO A 677 2436 4794 4894 -522 -186 -855 C
ATOM 1650 CG PRO A 677 100.624 82.953 37.093 1.00 32.27 C
ANISOU 1650 CG PRO A 677 2541 4826 4894 -630 -206 -866 C
ATOM 1651 CD PRO A 677 99.159 83.315 37.103 1.00 30.40 C
ANISOU 1651 CD PRO A 677 2536 4498 4518 -621 -189 -734 C
ATOM 1652 N SER A 678 99.072 79.662 34.140 1.00 29.24 N
ANISOU 1652 N SER A 678 2291 4348 4469 -421 20 -699 N
ATOM 1653 CA SER A 678 98.261 78.506 33.813 1.00 28.17 C
ANISOU 1653 CA SER A 678 2238 4171 4294 -312 11 -619 C
ATOM 1654 C SER A 678 98.753 77.243 34.533 1.00 28.25 C
ANISOU 1654 C SER A 678 2141 4211 4381 -155 -119 -644 C
ATOM 1655 O SER A 678 97.984 76.311 34.667 1.00 27.20 O
ANISOU 1655 O SER A 678 2101 4033 4202 -56 -167 -563 O
ATOM 1656 CB SER A 678 98.301 78.177 32.301 1.00 28.43 C
ANISOU 1656 CB SER A 678 2281 4188 4333 -370 174 -641 C
ATOM 1657 OG SER A 678 99.613 77.828 31.938 1.00 29.40 O
ANISOU 1657 OG SER A 678 2207 4378 4586 -382 226 -776 O
ATOM 1658 N CYS A 679 100.047 77.170 34.833 1.00 30.03 N
ANISOU 1658 N CYS A 679 2171 4507 4734 -139 -164 -765 N
ATOM 1659 CA CYS A 679 100.673 75.889 35.231 1.00 33.66 C
ANISOU 1659 CA CYS A 679 2511 4986 5292 19 -278 -809 C
ATOM 1660 C CYS A 679 100.398 74.772 34.203 1.00 34.28 C
ANISOU 1660 C CYS A 679 2613 5023 5389 77 -190 -798 C
ATOM 1661 O CYS A 679 100.214 73.589 34.552 1.00 34.28 O
ANISOU 1661 O CYS A 679 2636 4984 5404 221 -289 -760 O
ATOM 1662 CB CYS A 679 100.184 75.491 36.641 1.00 34.91 C
ANISOU 1662 CB CYS A 679 2763 5118 5385 137 -476 -719 C
ATOM 1663 SG CYS A 679 100.805 76.603 37.887 1.00 38.47 S
ANISOU 1663 SG CYS A 679 3149 5630 5839 89 -602 -770 S
ATOM 1664 N GLY A 680 100.287 75.158 32.924 1.00 32.83 N
ANISOU 1664 N GLY A 680 2452 4835 5187 -44 -2 -822 N
ATOM 1665 CA GLY A 680 100.030 74.224 31.854 1.00 31.54 C
ANISOU 1665 CA GLY A 680 2321 4637 5028 -13 99 -823 C
ATOM 1666 C GLY A 680 98.653 73.671 31.672 1.00 29.31 C
ANISOU 1666 C GLY A 680 2242 4271 4623 29 92 -686 C
ATOM 1667 O GLY A 680 98.456 72.738 30.880 1.00 29.10 O
ANISOU 1667 O GLY A 680 2240 4211 4606 70 153 -691 O
ATOM 1668 N LEU A 681 97.671 74.202 32.385 1.00 27.57 N
ANISOU 1668 N LEU A 681 2165 4017 4292 16 21 -573 N
ATOM 1669 CA LEU A 681 96.330 73.724 32.273 1.00 27.30 C
ANISOU 1669 CA LEU A 681 2308 3914 4152 47 14 -455 C
ATOM 1670 C LEU A 681 95.321 74.862 32.105 1.00 26.40 C
ANISOU 1670 C LEU A 681 2335 3776 3921 -58 61 -379 C
ATOM 1671 O LEU A 681 95.465 75.950 32.675 1.00 26.32 O
ANISOU 1671 O LEU A 681 2319 3787 3894 -117 35 -384 O
ATOM 1672 CB LEU A 681 95.945 72.975 33.564 1.00 28.91 C
ANISOU 1672 CB LEU A 681 2558 4091 4337 172 -149 -386 C
ATOM 1673 CG LEU A 681 96.637 71.645 33.865 1.00 31.11 C
ANISOU 1673 CG LEU A 681 2754 4356 4710 312 -237 -426 C
ATOM 1674 CD1 LEU A 681 96.110 71.184 35.243 1.00 32.48 C
ANISOU 1674 CD1 LEU A 681 3029 4492 4820 400 -399 -333 C
ATOM 1675 CD2 LEU A 681 96.312 70.613 32.797 1.00 31.67 C
ANISOU 1675 CD2 LEU A 681 2863 4376 4793 341 -151 -427 C
ATOM 1676 N GLN A 682 94.322 74.570 31.328 1.00 24.75 N
ANISOU 1676 N GLN A 682 2248 3517 3639 -73 119 -317 N
ATOM 1677 CA AGLN A 682 93.192 75.455 31.130 0.50 25.15 C
ANISOU 1677 CA AGLN A 682 2440 3531 3585 -142 142 -241 C
ATOM 1678 CA BGLN A 682 93.206 75.457 31.155 0.50 25.26 C
ANISOU 1678 CA BGLN A 682 2452 3546 3600 -141 140 -242 C
ATOM 1679 C GLN A 682 91.969 74.794 31.709 1.00 22.50 C
ANISOU 1679 C GLN A 682 2203 3155 3189 -66 67 -153 C
ATOM 1680 O GLN A 682 91.657 73.643 31.349 1.00 22.62 O
ANISOU 1680 O GLN A 682 2241 3145 3210 -10 73 -137 O
ATOM 1681 CB AGLN A 682 92.978 75.715 29.632 0.50 26.80 C
ANISOU 1681 CB AGLN A 682 2717 3715 3752 -232 268 -248 C
ATOM 1682 CB BGLN A 682 93.023 75.796 29.676 0.50 27.26 C
ANISOU 1682 CB BGLN A 682 2771 3776 3811 -236 267 -250 C
ATOM 1683 CG AGLN A 682 91.587 76.223 29.296 0.50 28.06 C
ANISOU 1683 CG AGLN A 682 3036 3820 3807 -262 263 -161 C
ATOM 1684 CG BGLN A 682 92.011 76.897 29.487 0.50 29.31 C
ANISOU 1684 CG BGLN A 682 3168 3991 3976 -302 270 -183 C
ATOM 1685 CD AGLN A 682 91.411 77.713 29.558 0.50 29.14 C
ANISOU 1685 CD AGLN A 682 3226 3943 3903 -337 255 -143 C
ATOM 1686 CD BGLN A 682 92.212 77.658 28.183 0.50 32.02 C
ANISOU 1686 CD BGLN A 682 3578 4313 4275 -425 383 -201 C
ATOM 1687 OE1AGLN A 682 90.450 78.128 30.199 0.50 28.65 O
ANISOU 1687 OE1AGLN A 682 3233 3854 3797 -308 186 -87 O
ATOM 1688 OE1BGLN A 682 93.150 77.403 27.410 0.50 33.17 O
ANISOU 1688 OE1BGLN A 682 3661 4487 4457 -478 482 -274 O
ATOM 1689 NE2AGLN A 682 92.321 78.528 29.003 0.50 32.16 N
ANISOU 1689 NE2AGLN A 682 3583 4336 4300 -441 335 -198 N
ATOM 1690 NE2BGLN A 682 91.360 78.654 27.974 0.50 33.82 N
ANISOU 1690 NE2BGLN A 682 3938 4488 4423 -473 370 -142 N
ATOM 1691 N VAL A 683 91.259 75.487 32.573 1.00 20.86 N
ANISOU 1691 N VAL A 683 2057 2941 2927 -71 9 -104 N
ATOM 1692 CA VAL A 683 90.066 74.983 33.241 1.00 20.24 C
ANISOU 1692 CA VAL A 683 2067 2833 2790 -18 -47 -32 C
ATOM 1693 C VAL A 683 88.788 75.354 32.477 1.00 20.61 C
ANISOU 1693 C VAL A 683 2216 2842 2772 -60 0 12 C
ATOM 1694 O VAL A 683 88.673 76.502 31.983 1.00 21.93 O
ANISOU 1694 O VAL A 683 2415 2999 2918 -126 34 6 O
ATOM 1695 CB VAL A 683 89.954 75.552 34.674 1.00 21.15 C
ANISOU 1695 CB VAL A 683 2191 2968 2877 -4 -130 -17 C
ATOM 1696 CG1 VAL A 683 88.712 75.063 35.353 1.00 22.33 C
ANISOU 1696 CG1 VAL A 683 2431 3093 2959 31 -164 46 C
ATOM 1697 CG2 VAL A 683 91.125 75.145 35.498 1.00 22.60 C
ANISOU 1697 CG2 VAL A 683 2285 3188 3115 47 -207 -56 C
ATOM 1698 N SER A 684 87.854 74.412 32.373 1.00 19.32 N
ANISOU 1698 N SER A 684 2107 2651 2582 -22 -7 54 N
ATOM 1699 CA SER A 684 86.509 74.685 31.867 1.00 19.08 C
ANISOU 1699 CA SER A 684 2160 2592 2499 -46 10 89 C
ATOM 1700 C SER A 684 85.450 74.186 32.830 1.00 19.38 C
ANISOU 1700 C SER A 684 2233 2625 2505 -11 -32 127 C
ATOM 1701 O SER A 684 85.455 73.032 33.264 1.00 20.79 O
ANISOU 1701 O SER A 684 2416 2796 2689 28 -49 144 O
ATOM 1702 CB SER A 684 86.284 73.987 30.526 1.00 19.09 C
ANISOU 1702 CB SER A 684 2191 2567 2495 -60 62 87 C
ATOM 1703 OG SER A 684 87.141 74.471 29.518 1.00 20.13 O
ANISOU 1703 OG SER A 684 2309 2702 2637 -112 123 50 O
ATOM 1704 N ILE A 685 84.565 75.067 33.213 1.00 18.25 N
ANISOU 1704 N ILE A 685 2121 2482 2331 -28 -44 135 N
ATOM 1705 CA ILE A 685 83.449 74.776 34.087 1.00 17.75 C
ANISOU 1705 CA ILE A 685 2087 2423 2236 -14 -61 154 C
ATOM 1706 C ILE A 685 82.278 74.326 33.192 1.00 18.54 C
ANISOU 1706 C ILE A 685 2215 2500 2330 -23 -38 163 C
ATOM 1707 O ILE A 685 81.943 75.046 32.265 1.00 18.75 O
ANISOU 1707 O ILE A 685 2256 2511 2358 -40 -34 153 O
ATOM 1708 CB ILE A 685 83.017 76.032 34.842 1.00 18.33 C
ANISOU 1708 CB ILE A 685 2165 2509 2291 -25 -78 137 C
ATOM 1709 CG1 ILE A 685 84.115 76.442 35.804 1.00 19.28 C
ANISOU 1709 CG1 ILE A 685 2261 2655 2411 -23 -110 122 C
ATOM 1710 CG2 ILE A 685 81.695 75.847 35.578 1.00 18.42 C
ANISOU 1710 CG2 ILE A 685 2196 2529 2273 -22 -72 137 C
ATOM 1711 CD1 ILE A 685 83.913 77.862 36.368 1.00 19.73 C
ANISOU 1711 CD1 ILE A 685 2326 2716 2456 -43 -123 92 C
ATOM 1712 N ILE A 686 81.694 73.186 33.508 1.00 17.90 N
ANISOU 1712 N ILE A 686 2151 2413 2238 -16 -30 180 N
ATOM 1713 CA ILE A 686 80.634 72.575 32.705 1.00 18.00 C
ANISOU 1713 CA ILE A 686 2181 2407 2251 -31 -11 179 C
ATOM 1714 C ILE A 686 79.405 72.280 33.535 1.00 19.80 C
ANISOU 1714 C ILE A 686 2413 2649 2462 -48 0 175 C
ATOM 1715 O ILE A 686 79.397 72.385 34.750 1.00 18.94 O
ANISOU 1715 O ILE A 686 2310 2558 2328 -51 1 179 O
ATOM 1716 CB ILE A 686 81.168 71.265 32.037 1.00 18.10 C
ANISOU 1716 CB ILE A 686 2211 2390 2277 -24 7 191 C
ATOM 1717 CG1 ILE A 686 81.607 70.262 33.095 1.00 21.01 C
ANISOU 1717 CG1 ILE A 686 2598 2745 2640 -2 -3 216 C
ATOM 1718 CG2 ILE A 686 82.276 71.594 31.068 1.00 18.98 C
ANISOU 1718 CG2 ILE A 686 2307 2496 2407 -20 18 174 C
ATOM 1719 CD1 ILE A 686 81.549 68.802 32.787 1.00 22.25 C
ANISOU 1719 CD1 ILE A 686 2794 2854 2805 3 10 229 C
ATOM 1720 N ASP A 687 78.336 71.851 32.836 1.00 19.02 N
ANISOU 1720 N ASP A 687 2311 2543 2374 -69 12 160 N
ATOM 1721 CA ASP A 687 77.099 71.305 33.352 1.00 20.28 C
ANISOU 1721 CA ASP A 687 2461 2714 2529 -104 40 142 C
ATOM 1722 C ASP A 687 76.230 72.341 34.088 1.00 20.35 C
ANISOU 1722 C ASP A 687 2425 2763 2544 -106 44 99 C
ATOM 1723 O ASP A 687 76.300 72.495 35.283 1.00 20.41 O
ANISOU 1723 O ASP A 687 2442 2790 2522 -117 67 99 O
ATOM 1724 CB ASP A 687 77.282 70.060 34.280 1.00 21.75 C
ANISOU 1724 CB ASP A 687 2699 2882 2683 -130 73 175 C
ATOM 1725 CG ASP A 687 75.964 69.396 34.604 1.00 24.48 C
ANISOU 1725 CG ASP A 687 3042 3236 3024 -192 122 151 C
ATOM 1726 OD1 ASP A 687 74.935 69.826 34.078 1.00 24.19 O
ANISOU 1726 OD1 ASP A 687 2943 3226 3022 -206 124 100 O
ATOM 1727 OD2 ASP A 687 75.929 68.393 35.380 1.00 29.28 O
ANISOU 1727 OD2 ASP A 687 3713 3817 3593 -232 157 180 O
ATOM 1728 N TYR A 688 75.324 72.971 33.330 1.00 19.86 N
ANISOU 1728 N TYR A 688 2317 2708 2521 -95 17 56 N
ATOM 1729 CA TYR A 688 74.514 74.060 33.813 1.00 19.14 C
ANISOU 1729 CA TYR A 688 2171 2644 2456 -77 9 0 C
ATOM 1730 C TYR A 688 73.080 73.684 34.159 1.00 20.29 C
ANISOU 1730 C TYR A 688 2248 2828 2634 -110 47 -65 C
ATOM 1731 O TYR A 688 72.196 74.542 34.251 1.00 20.39 O
ANISOU 1731 O TYR A 688 2191 2863 2695 -83 30 -134 O
ATOM 1732 CB TYR A 688 74.626 75.254 32.861 1.00 18.63 C
ANISOU 1732 CB TYR A 688 2108 2553 2418 -26 -64 -8 C
ATOM 1733 CG TYR A 688 76.017 75.440 32.359 1.00 17.37 C
ANISOU 1733 CG TYR A 688 2013 2360 2227 -20 -80 48 C
ATOM 1734 CD1 TYR A 688 77.095 75.555 33.239 1.00 17.79 C
ANISOU 1734 CD1 TYR A 688 2086 2421 2253 -25 -56 73 C
ATOM 1735 CD2 TYR A 688 76.290 75.545 30.991 1.00 17.69 C
ANISOU 1735 CD2 TYR A 688 2095 2365 2262 -15 -119 69 C
ATOM 1736 CE1 TYR A 688 78.394 75.634 32.745 1.00 17.16 C
ANISOU 1736 CE1 TYR A 688 2041 2320 2159 -26 -63 108 C
ATOM 1737 CE2 TYR A 688 77.571 75.677 30.486 1.00 17.10 C
ANISOU 1737 CE2 TYR A 688 2071 2266 2161 -25 -111 106 C
ATOM 1738 CZ TYR A 688 78.628 75.749 31.387 1.00 17.27 C
ANISOU 1738 CZ TYR A 688 2088 2302 2174 -30 -81 120 C
ATOM 1739 OH TYR A 688 79.863 75.866 30.868 1.00 18.89 O
ANISOU 1739 OH TYR A 688 2318 2491 2366 -45 -68 140 O
ATOM 1740 N THR A 689 72.886 72.395 34.460 1.00 21.29 N
ANISOU 1740 N THR A 689 2395 2957 2736 -172 105 -50 N
ATOM 1741 CA THR A 689 71.595 71.850 34.820 1.00 23.22 C
ANISOU 1741 CA THR A 689 2578 3237 3006 -233 164 -113 C
ATOM 1742 C THR A 689 70.901 72.592 35.948 1.00 23.21 C
ANISOU 1742 C THR A 689 2517 3287 3015 -244 218 -184 C
ATOM 1743 O THR A 689 69.699 72.794 35.916 1.00 24.58 O
ANISOU 1743 O THR A 689 2586 3501 3251 -257 238 -275 O
ATOM 1744 CB THR A 689 71.743 70.347 35.197 1.00 25.11 C
ANISOU 1744 CB THR A 689 2890 3454 3197 -312 230 -68 C
ATOM 1745 OG1 THR A 689 72.323 69.642 34.092 1.00 26.23 O
ANISOU 1745 OG1 THR A 689 3080 3547 3342 -297 185 -21 O
ATOM 1746 CG2 THR A 689 70.415 69.752 35.482 1.00 28.78 C
ANISOU 1746 CG2 THR A 689 3294 3953 3689 -397 303 -139 C
ATOM 1747 N LEU A 690 71.665 72.974 36.995 1.00 21.28 N
ANISOU 1747 N LEU A 690 2333 3044 2709 -241 243 -153 N
ATOM 1748 CA LEU A 690 71.070 73.626 38.143 1.00 22.55 C
ANISOU 1748 CA LEU A 690 2454 3252 2861 -262 307 -225 C
ATOM 1749 C LEU A 690 71.343 75.164 38.172 1.00 21.34 C
ANISOU 1749 C LEU A 690 2270 3097 2740 -176 248 -259 C
ATOM 1750 O LEU A 690 70.959 75.821 39.120 1.00 22.46 O
ANISOU 1750 O LEU A 690 2385 3273 2876 -182 298 -326 O
ATOM 1751 CB LEU A 690 71.600 73.016 39.450 1.00 24.28 C
ANISOU 1751 CB LEU A 690 2779 3473 2971 -330 379 -178 C
ATOM 1752 CG LEU A 690 71.177 71.606 39.848 1.00 28.55 C
ANISOU 1752 CG LEU A 690 3377 4010 3461 -435 463 -156 C
ATOM 1753 CD1 LEU A 690 71.630 71.362 41.268 1.00 29.84 C
ANISOU 1753 CD1 LEU A 690 3660 4174 3504 -492 519 -119 C
ATOM 1754 CD2 LEU A 690 69.688 71.391 39.706 1.00 30.82 C
ANISOU 1754 CD2 LEU A 690 3552 4344 3814 -500 541 -259 C
ATOM 1755 N SER A 691 71.980 75.669 37.142 1.00 19.41 N
ANISOU 1755 N SER A 691 2042 2810 2525 -109 153 -217 N
ATOM 1756 CA SER A 691 72.456 77.053 37.149 1.00 19.97 C
ANISOU 1756 CA SER A 691 2119 2857 2611 -42 96 -229 C
ATOM 1757 C SER A 691 71.369 78.111 37.022 1.00 20.04 C
ANISOU 1757 C SER A 691 2037 2873 2706 14 70 -330 C
ATOM 1758 O SER A 691 70.190 77.825 36.691 1.00 20.65 O
ANISOU 1758 O SER A 691 2020 2977 2848 15 78 -399 O
ATOM 1759 CB SER A 691 73.516 77.222 36.101 1.00 19.50 C
ANISOU 1759 CB SER A 691 2121 2744 2545 -9 18 -152 C
ATOM 1760 OG SER A 691 74.564 76.268 36.190 1.00 20.14 O
ANISOU 1760 OG SER A 691 2269 2817 2566 -45 36 -73 O
ATOM 1761 N ARG A 692 71.767 79.336 37.354 1.00 19.53 N
ANISOU 1761 N ARG A 692 1993 2781 2646 63 38 -350 N
ATOM 1762 CA ARG A 692 70.856 80.481 37.347 1.00 21.01 C
ANISOU 1762 CA ARG A 692 2106 2958 2918 134 3 -451 C
ATOM 1763 C ARG A 692 71.606 81.700 36.764 1.00 20.56 C
ANISOU 1763 C ARG A 692 2121 2818 2871 200 -94 -415 C
ATOM 1764 O ARG A 692 72.789 81.916 37.062 1.00 20.98 O
ANISOU 1764 O ARG A 692 2260 2851 2861 173 -90 -353 O
ATOM 1765 CB ARG A 692 70.421 80.779 38.775 1.00 21.59 C
ANISOU 1765 CB ARG A 692 2140 3084 2981 108 101 -541 C
ATOM 1766 CG ARG A 692 69.617 82.040 38.990 1.00 22.42 C
ANISOU 1766 CG ARG A 692 2169 3174 3175 189 79 -662 C
ATOM 1767 CD ARG A 692 70.427 83.253 39.467 1.00 22.52 C
ANISOU 1767 CD ARG A 692 2260 3133 3163 224 49 -660 C
ATOM 1768 NE ARG A 692 69.480 84.263 39.901 1.00 23.99 N
ANISOU 1768 NE ARG A 692 2363 3314 3437 294 55 -799 N
ATOM 1769 CZ ARG A 692 69.415 85.537 39.490 1.00 24.52 C
ANISOU 1769 CZ ARG A 692 2443 3296 3577 393 -40 -836 C
ATOM 1770 NH1 ARG A 692 70.388 86.069 38.776 1.00 23.75 N
ANISOU 1770 NH1 ARG A 692 2461 3112 3452 413 -134 -738 N
ATOM 1771 NH2 ARG A 692 68.421 86.273 39.855 1.00 26.37 N
ANISOU 1771 NH2 ARG A 692 2582 3530 3907 465 -32 -975 N
ATOM 1772 N LEU A 693 70.895 82.527 35.980 1.00 20.83 N
ANISOU 1772 N LEU A 693 2124 2803 2989 284 -185 -461 N
ATOM 1773 CA LEU A 693 71.458 83.796 35.559 1.00 21.69 C
ANISOU 1773 CA LEU A 693 2317 2820 3106 340 -271 -438 C
ATOM 1774 C LEU A 693 70.354 84.698 35.176 1.00 22.73 C
ANISOU 1774 C LEU A 693 2391 2906 3340 444 -358 -525 C
ATOM 1775 O LEU A 693 69.188 84.301 35.228 1.00 23.04 O
ANISOU 1775 O LEU A 693 2307 2998 3451 471 -349 -610 O
ATOM 1776 CB LEU A 693 72.461 83.594 34.415 1.00 22.23 C
ANISOU 1776 CB LEU A 693 2494 2834 3117 313 -326 -320 C
ATOM 1777 CG LEU A 693 71.970 82.986 33.109 1.00 23.12 C
ANISOU 1777 CG LEU A 693 2607 2935 3244 328 -394 -288 C
ATOM 1778 CD1 LEU A 693 71.012 83.778 32.250 1.00 25.52 C
ANISOU 1778 CD1 LEU A 693 2903 3174 3619 423 -521 -330 C
ATOM 1779 CD2 LEU A 693 73.270 82.701 32.317 1.00 23.98 C
ANISOU 1779 CD2 LEU A 693 2832 3008 3270 271 -396 -178 C
ATOM 1780 N GLU A 694 70.666 85.943 34.819 1.00 23.11 N
ANISOU 1780 N GLU A 694 2525 2851 3406 505 -445 -516 N
ATOM 1781 CA GLU A 694 69.640 86.804 34.341 1.00 25.10 C
ANISOU 1781 CA GLU A 694 2738 3038 3760 623 -556 -591 C
ATOM 1782 C GLU A 694 70.187 87.788 33.328 1.00 25.92 C
ANISOU 1782 C GLU A 694 2999 3003 3845 666 -683 -515 C
ATOM 1783 O GLU A 694 71.399 88.121 33.350 1.00 25.71 O
ANISOU 1783 O GLU A 694 3098 2933 3739 600 -655 -434 O
ATOM 1784 CB GLU A 694 69.030 87.549 35.515 1.00 28.87 C
ANISOU 1784 CB GLU A 694 3129 3530 4310 674 -507 -725 C
ATOM 1785 CG GLU A 694 69.943 88.493 36.189 1.00 31.52 C
ANISOU 1785 CG GLU A 694 3567 3807 4603 657 -481 -714 C
ATOM 1786 CD GLU A 694 69.233 89.221 37.346 1.00 34.92 C
ANISOU 1786 CD GLU A 694 3908 4252 5106 711 -428 -866 C
ATOM 1787 OE1 GLU A 694 69.360 88.727 38.492 1.00 33.56 O
ANISOU 1787 OE1 GLU A 694 3689 4177 4885 634 -293 -907 O
ATOM 1788 OE2 GLU A 694 68.581 90.279 37.113 1.00 37.60 O
ANISOU 1788 OE2 GLU A 694 4237 4501 5547 831 -522 -945 O
ATOM 1789 N ARG A 695 69.298 88.295 32.483 1.00 25.89 N
ANISOU 1789 N ARG A 695 2993 2930 3916 773 -824 -546 N
ATOM 1790 CA ARG A 695 69.638 89.433 31.588 1.00 28.23 C
ANISOU 1790 CA ARG A 695 3462 3068 4197 829 -961 -484 C
ATOM 1791 C ARG A 695 68.440 90.313 31.513 1.00 28.10 C
ANISOU 1791 C ARG A 695 3388 2981 4309 984 -1091 -590 C
ATOM 1792 O ARG A 695 67.331 89.833 31.276 1.00 28.10 O
ANISOU 1792 O ARG A 695 3247 3038 4392 1051 -1144 -665 O
ATOM 1793 CB ARG A 695 70.023 88.981 30.151 1.00 30.45 C
ANISOU 1793 CB ARG A 695 3870 3308 4393 789 -1040 -362 C
ATOM 1794 CG ARG A 695 71.362 88.251 30.120 1.00 32.21 C
ANISOU 1794 CG ARG A 695 4165 3579 4495 643 -917 -261 C
ATOM 1795 CD ARG A 695 71.948 88.078 28.696 1.00 33.69 C
ANISOU 1795 CD ARG A 695 4515 3703 4584 592 -978 -145 C
ATOM 1796 NE ARG A 695 72.241 89.357 28.059 1.00 37.65 N
ANISOU 1796 NE ARG A 695 5203 4046 5057 620 -1081 -97 N
ATOM 1797 CZ ARG A 695 72.830 89.505 26.859 1.00 41.93 C
ANISOU 1797 CZ ARG A 695 5931 4506 5496 564 -1130 4 C
ATOM 1798 NH1 ARG A 695 73.279 88.446 26.186 1.00 40.58 N
ANISOU 1798 NH1 ARG A 695 5772 4402 5244 477 -1074 61 N
ATOM 1799 NH2 ARG A 695 72.978 90.730 26.318 1.00 43.31 N
ANISOU 1799 NH2 ARG A 695 6293 4520 5642 590 -1231 46 N
ATOM 1800 N ASP A 696 68.687 91.597 31.677 1.00 29.59 N
ANISOU 1800 N ASP A 696 3684 3040 4518 1041 -1148 -600 N
ATOM 1801 CA ASP A 696 67.667 92.616 31.620 1.00 31.68 C
ANISOU 1801 CA ASP A 696 3920 3206 4912 1206 -1287 -702 C
ATOM 1802 C ASP A 696 66.484 92.292 32.520 1.00 32.00 C
ANISOU 1802 C ASP A 696 3708 3364 5087 1278 -1231 -876 C
ATOM 1803 O ASP A 696 65.329 92.568 32.169 1.00 33.94 O
ANISOU 1803 O ASP A 696 3853 3583 5459 1418 -1359 -973 O
ATOM 1804 CB ASP A 696 67.234 92.825 30.183 1.00 33.38 C
ANISOU 1804 CB ASP A 696 4242 3313 5127 1289 -1491 -638 C
ATOM 1805 CG ASP A 696 68.355 93.439 29.340 1.00 35.11 C
ANISOU 1805 CG ASP A 696 4740 3386 5214 1221 -1544 -482 C
ATOM 1806 OD1 ASP A 696 68.828 94.545 29.738 1.00 38.70 O
ANISOU 1806 OD1 ASP A 696 5312 3722 5672 1233 -1547 -483 O
ATOM 1807 OD2 ASP A 696 68.747 92.803 28.318 1.00 34.13 O
ANISOU 1807 OD2 ASP A 696 4715 3269 4985 1147 -1571 -369 O
ATOM 1808 N GLY A 697 66.797 91.735 33.707 1.00 30.59 N
ANISOU 1808 N GLY A 697 3434 3313 4878 1176 -1038 -920 N
ATOM 1809 CA GLY A 697 65.720 91.528 34.692 1.00 31.75 C
ANISOU 1809 CA GLY A 697 3355 3567 5140 1223 -953 -1098 C
ATOM 1810 C GLY A 697 64.976 90.224 34.483 1.00 31.96 C
ANISOU 1810 C GLY A 697 3218 3736 5191 1182 -910 -1128 C
ATOM 1811 O GLY A 697 64.025 89.963 35.186 1.00 35.32 O
ANISOU 1811 O GLY A 697 3450 4258 5713 1204 -833 -1278 O
ATOM 1812 N ILE A 698 65.335 89.437 33.479 1.00 30.49 N
ANISOU 1812 N ILE A 698 3104 3557 4925 1124 -961 -1001 N
ATOM 1813 CA ILE A 698 64.646 88.182 33.190 1.00 30.40 C
ANISOU 1813 CA ILE A 698 2951 3667 4935 1079 -931 -1027 C
ATOM 1814 C ILE A 698 65.523 87.083 33.713 1.00 28.79 C
ANISOU 1814 C ILE A 698 2781 3558 4601 911 -758 -941 C
ATOM 1815 O ILE A 698 66.700 86.957 33.285 1.00 26.23 O
ANISOU 1815 O ILE A 698 2625 3187 4155 841 -759 -796 O
ATOM 1816 CB ILE A 698 64.435 87.966 31.687 1.00 31.64 C
ANISOU 1816 CB ILE A 698 3173 3766 5083 1124 -1109 -949 C
ATOM 1817 CG1 ILE A 698 63.685 89.133 31.031 1.00 34.27 C
ANISOU 1817 CG1 ILE A 698 3521 3974 5528 1304 -1324 -1007 C
ATOM 1818 CG2 ILE A 698 63.701 86.647 31.407 1.00 31.86 C
ANISOU 1818 CG2 ILE A 698 3049 3919 5136 1069 -1076 -988 C
ATOM 1819 CD1 ILE A 698 62.295 89.389 31.586 1.00 36.26 C
ANISOU 1819 CD1 ILE A 698 3529 4280 5968 1423 -1345 -1212 C
ATOM 1820 N VAL A 699 64.988 86.262 34.629 1.00 27.88 N
ANISOU 1820 N VAL A 699 2513 3572 4509 842 -609 -1031 N
ATOM 1821 CA VAL A 699 65.815 85.235 35.331 1.00 26.87 C
ANISOU 1821 CA VAL A 699 2430 3525 4255 687 -444 -955 C
ATOM 1822 C VAL A 699 65.547 83.868 34.727 1.00 26.37 C
ANISOU 1822 C VAL A 699 2321 3530 4167 612 -426 -913 C
ATOM 1823 O VAL A 699 64.411 83.512 34.416 1.00 26.88 O
ANISOU 1823 O VAL A 699 2239 3643 4329 642 -456 -1009 O
ATOM 1824 CB VAL A 699 65.527 85.176 36.866 1.00 28.11 C
ANISOU 1824 CB VAL A 699 2496 3770 4415 633 -271 -1066 C
ATOM 1825 CG1 VAL A 699 66.459 84.176 37.565 1.00 27.67 C
ANISOU 1825 CG1 VAL A 699 2523 3775 4216 485 -132 -971 C
ATOM 1826 CG2 VAL A 699 65.708 86.566 37.511 1.00 29.72 C
ANISOU 1826 CG2 VAL A 699 2737 3904 4651 710 -285 -1131 C
ATOM 1827 N VAL A 700 66.609 83.147 34.498 1.00 24.41 N
ANISOU 1827 N VAL A 700 2197 3279 3798 521 -389 -778 N
ATOM 1828 CA VAL A 700 66.581 81.771 34.015 1.00 25.99 C
ANISOU 1828 CA VAL A 700 2386 3533 3956 435 -354 -725 C
ATOM 1829 C VAL A 700 67.236 80.876 35.084 1.00 25.45 C
ANISOU 1829 C VAL A 700 2350 3527 3792 312 -191 -684 C
ATOM 1830 O VAL A 700 68.364 81.120 35.477 1.00 23.19 O
ANISOU 1830 O VAL A 700 2179 3211 3422 287 -164 -605 O
ATOM 1831 CB VAL A 700 67.390 81.708 32.722 1.00 26.85 C
ANISOU 1831 CB VAL A 700 2637 3566 3999 442 -463 -596 C
ATOM 1832 CG1 VAL A 700 67.443 80.313 32.209 1.00 27.48 C
ANISOU 1832 CG1 VAL A 700 2717 3690 4032 357 -427 -545 C
ATOM 1833 CG2 VAL A 700 66.715 82.601 31.663 1.00 30.84 C
ANISOU 1833 CG2 VAL A 700 3139 3997 4581 563 -641 -627 C
ATOM 1834 N PHE A 701 66.506 79.841 35.541 1.00 26.31 N
ANISOU 1834 N PHE A 701 2362 3720 3914 233 -89 -741 N
ATOM 1835 CA PHE A 701 67.021 79.008 36.646 1.00 26.01 C
ANISOU 1835 CA PHE A 701 2374 3731 3779 117 60 -705 C
ATOM 1836 C PHE A 701 66.283 77.694 36.709 1.00 29.07 C
ANISOU 1836 C PHE A 701 2692 4182 4171 19 145 -736 C
ATOM 1837 O PHE A 701 65.227 77.527 36.065 1.00 28.86 O
ANISOU 1837 O PHE A 701 2542 4181 4242 39 104 -817 O
ATOM 1838 CB PHE A 701 66.910 79.755 37.972 1.00 26.72 C
ANISOU 1838 CB PHE A 701 2440 3849 3862 116 148 -786 C
ATOM 1839 CG PHE A 701 65.518 79.935 38.499 1.00 28.02 C
ANISOU 1839 CG PHE A 701 2436 4082 4128 119 219 -955 C
ATOM 1840 CD1 PHE A 701 64.609 80.841 37.917 1.00 29.20 C
ANISOU 1840 CD1 PHE A 701 2460 4215 4419 239 119 -1065 C
ATOM 1841 CD2 PHE A 701 65.083 79.215 39.633 1.00 29.12 C
ANISOU 1841 CD2 PHE A 701 2540 4302 4222 0 390 -1015 C
ATOM 1842 CE1 PHE A 701 63.323 81.012 38.439 1.00 32.20 C
ANISOU 1842 CE1 PHE A 701 2657 4665 4910 248 190 -1243 C
ATOM 1843 CE2 PHE A 701 63.791 79.375 40.148 1.00 30.46 C
ANISOU 1843 CE2 PHE A 701 2540 4545 4488 -12 480 -1189 C
ATOM 1844 CZ PHE A 701 62.899 80.261 39.561 1.00 32.50 C
ANISOU 1844 CZ PHE A 701 2646 4797 4906 114 384 -1312 C
ATOM 1845 N CYS A 702 66.845 76.798 37.509 1.00 28.77 N
ANISOU 1845 N CYS A 702 2739 4164 4029 -87 256 -674 N
ATOM 1846 CA CYS A 702 66.179 75.531 37.864 1.00 29.94 C
ANISOU 1846 CA CYS A 702 2849 4364 4161 -208 370 -703 C
ATOM 1847 C CYS A 702 65.541 75.601 39.249 1.00 30.93 C
ANISOU 1847 C CYS A 702 2924 4557 4271 -284 522 -804 C
ATOM 1848 O CYS A 702 66.209 75.752 40.295 1.00 29.13 O
ANISOU 1848 O CYS A 702 2799 4327 3941 -319 589 -767 O
ATOM 1849 CB CYS A 702 67.205 74.430 37.805 1.00 28.76 C
ANISOU 1849 CB CYS A 702 2851 4175 3902 -274 385 -564 C
ATOM 1850 SG CYS A 702 66.444 72.819 38.045 1.00 33.81 S
ANISOU 1850 SG CYS A 702 3478 4847 4520 -426 507 -582 S
ATOM 1851 N ASP A 703 64.225 75.572 39.278 1.00 31.65 N
ANISOU 1851 N ASP A 703 2850 4712 4464 -308 578 -948 N
ATOM 1852 CA ASP A 703 63.511 75.704 40.545 1.00 35.02 C
ANISOU 1852 CA ASP A 703 3210 5212 4885 -387 741 -1071 C
ATOM 1853 C ASP A 703 63.510 74.363 41.293 1.00 36.17 C
ANISOU 1853 C ASP A 703 3448 5381 4915 -566 895 -1027 C
ATOM 1854 O ASP A 703 62.703 73.500 41.011 1.00 36.55 O
ANISOU 1854 O ASP A 703 3419 5463 5008 -655 954 -1077 O
ATOM 1855 CB ASP A 703 62.058 76.149 40.326 1.00 37.95 C
ANISOU 1855 CB ASP A 703 3344 5650 5424 -353 756 -1263 C
ATOM 1856 CG ASP A 703 61.343 76.417 41.625 1.00 41.99 C
ANISOU 1856 CG ASP A 703 3775 6241 5936 -430 938 -1412 C
ATOM 1857 OD1 ASP A 703 61.952 76.325 42.732 1.00 42.16 O
ANISOU 1857 OD1 ASP A 703 3940 6264 5814 -511 1049 -1362 O
ATOM 1858 OD2 ASP A 703 60.146 76.772 41.550 1.00 46.93 O
ANISOU 1858 OD2 ASP A 703 4189 6933 6711 -405 968 -1591 O
ATOM 1859 N VAL A 704 64.405 74.216 42.269 1.00 34.60 N
ANISOU 1859 N VAL A 704 3423 5160 4565 -619 955 -937 N
ATOM 1860 CA VAL A 704 64.513 72.953 43.033 1.00 34.59 C
ANISOU 1860 CA VAL A 704 3555 5157 4430 -784 1084 -875 C
ATOM 1861 C VAL A 704 63.838 73.083 44.403 1.00 36.93 C
ANISOU 1861 C VAL A 704 3842 5524 4666 -901 1273 -987 C
ATOM 1862 O VAL A 704 64.119 72.301 45.298 1.00 36.88 O
ANISOU 1862 O VAL A 704 3997 5506 4509 -1032 1377 -924 O
ATOM 1863 CB VAL A 704 65.990 72.504 43.197 1.00 33.44 C
ANISOU 1863 CB VAL A 704 3632 4931 4145 -772 1012 -690 C
ATOM 1864 CG1 VAL A 704 66.591 72.158 41.881 1.00 33.32 C
ANISOU 1864 CG1 VAL A 704 3629 4852 4180 -690 865 -592 C
ATOM 1865 CG2 VAL A 704 66.804 73.591 43.865 1.00 33.46 C
ANISOU 1865 CG2 VAL A 704 3698 4926 4089 -694 969 -673 C
ATOM 1866 N SER A 705 62.934 74.042 44.576 1.00 38.23 N
ANISOU 1866 N SER A 705 3825 5757 4943 -858 1319 -1159 N
ATOM 1867 CA SER A 705 62.371 74.331 45.904 1.00 41.29 C
ANISOU 1867 CA SER A 705 4203 6217 5270 -960 1506 -1282 C
ATOM 1868 C SER A 705 61.562 73.147 46.478 1.00 45.33 C
ANISOU 1868 C SER A 705 4727 6776 5721 -1174 1706 -1329 C
ATOM 1869 O SER A 705 61.407 73.072 47.687 1.00 45.83 O
ANISOU 1869 O SER A 705 4877 6877 5660 -1300 1872 -1373 O
ATOM 1870 CB SER A 705 61.466 75.573 45.872 1.00 42.73 C
ANISOU 1870 CB SER A 705 4158 6462 5617 -859 1517 -1482 C
ATOM 1871 OG SER A 705 60.456 75.442 44.864 1.00 42.68 O
ANISOU 1871 OG SER A 705 3931 6488 5795 -821 1474 -1585 O
ATOM 1872 N MET A 706 61.044 72.280 45.607 1.00 47.16 N
ANISOU 1872 N MET A 706 4879 7003 6035 -1218 1689 -1327 N
ATOM 1873 CA MET A 706 60.248 71.107 46.011 1.00 52.44 C
ANISOU 1873 CA MET A 706 5557 7707 6661 -1433 1873 -1372 C
ATOM 1874 C MET A 706 61.017 69.797 45.863 1.00 52.16 C
ANISOU 1874 C MET A 706 5754 7575 6490 -1520 1843 -1178 C
ATOM 1875 O MET A 706 60.453 68.736 46.052 1.00 51.90 O
ANISOU 1875 O MET A 706 5757 7544 6419 -1697 1974 -1191 O
ATOM 1876 CB MET A 706 58.959 71.014 45.156 1.00 55.70 C
ANISOU 1876 CB MET A 706 5691 8190 7282 -1439 1886 -1539 C
ATOM 1877 CG MET A 706 58.126 72.279 45.108 1.00 59.50 C
ANISOU 1877 CG MET A 706 5911 8758 7938 -1322 1881 -1744 C
ATOM 1878 SD MET A 706 57.544 72.780 46.731 1.00 73.38 S
ANISOU 1878 SD MET A 706 7648 10609 9623 -1447 2142 -1911 S
ATOM 1879 CE MET A 706 57.780 74.567 46.625 1.00 73.00 C
ANISOU 1879 CE MET A 706 7486 10561 9688 -1193 1997 -1991 C
ATOM 1880 N ASP A 707 62.290 69.841 45.513 1.00 48.41 N
ANISOU 1880 N ASP A 707 5435 7011 5949 -1401 1676 -1006 N
ATOM 1881 CA ASP A 707 63.085 68.618 45.380 1.00 51.20 C
ANISOU 1881 CA ASP A 707 6007 7263 6185 -1461 1635 -829 C
ATOM 1882 C ASP A 707 63.365 68.184 46.824 1.00 53.66 C
ANISOU 1882 C ASP A 707 6542 7556 6289 -1608 1773 -775 C
ATOM 1883 O ASP A 707 63.609 69.015 47.688 1.00 56.95 O
ANISOU 1883 O ASP A 707 6995 8009 6635 -1583 1804 -805 O
ATOM 1884 CB ASP A 707 64.372 68.919 44.596 1.00 50.48 C
ANISOU 1884 CB ASP A 707 5986 7093 6100 -1280 1419 -687 C
ATOM 1885 CG ASP A 707 65.039 67.674 44.006 1.00 54.11 C
ANISOU 1885 CG ASP A 707 6596 7452 6513 -1302 1347 -538 C
ATOM 1886 OD1 ASP A 707 65.334 66.693 44.729 1.00 56.55 O
ANISOU 1886 OD1 ASP A 707 7105 7701 6680 -1421 1417 -450 O
ATOM 1887 OD2 ASP A 707 65.315 67.686 42.784 1.00 57.63 O
ANISOU 1887 OD2 ASP A 707 6972 7868 7058 -1192 1212 -508 O
ATOM 1888 N GLU A 708 63.212 66.904 47.108 1.00 57.60 N
ANISOU 1888 N GLU A 708 7193 8001 6690 -1774 1866 -711 N
ATOM 1889 CA GLU A 708 63.547 66.359 48.435 1.00 59.32 C
ANISOU 1889 CA GLU A 708 7675 8178 6685 -1919 1978 -632 C
ATOM 1890 C GLU A 708 64.984 65.899 48.439 1.00 55.71 C
ANISOU 1890 C GLU A 708 7457 7598 6112 -1829 1809 -427 C
ATOM 1891 O GLU A 708 65.840 66.390 49.233 1.00 49.78 O
ANISOU 1891 O GLU A 708 6846 6832 5235 -1775 1754 -360 O
ATOM 1892 CB GLU A 708 62.637 65.177 48.756 1.00 65.45 C
ANISOU 1892 CB GLU A 708 8518 8943 7408 -2157 2167 -664 C
ATOM 1893 CG GLU A 708 61.219 65.602 49.108 1.00 71.73 C
ANISOU 1893 CG GLU A 708 9097 9871 8284 -2286 2378 -885 C
ATOM 1894 CD GLU A 708 60.183 64.533 48.787 1.00 77.27 C
ANISOU 1894 CD GLU A 708 9741 10577 9041 -2481 2521 -954 C
ATOM 1895 OE1 GLU A 708 59.773 64.420 47.606 1.00 79.11 O
ANISOU 1895 OE1 GLU A 708 9774 10826 9460 -2414 2437 -1007 O
ATOM 1896 OE2 GLU A 708 59.777 63.809 49.716 1.00 81.47 O
ANISOU 1896 OE2 GLU A 708 10434 11095 9425 -2709 2717 -957 O
ATOM 1897 N ASP A 709 65.232 64.985 47.489 1.00 51.59 N
ANISOU 1897 N ASP A 709 6960 6993 5647 -1806 1720 -342 N
ATOM 1898 CA ASP A 709 66.444 64.206 47.434 1.00 49.12 C
ANISOU 1898 CA ASP A 709 6875 6550 5239 -1749 1583 -159 C
ATOM 1899 C ASP A 709 67.712 65.009 47.264 1.00 44.44 C
ANISOU 1899 C ASP A 709 6291 5941 4651 -1546 1395 -84 C
ATOM 1900 O ASP A 709 68.726 64.639 47.820 1.00 43.07 O
ANISOU 1900 O ASP A 709 6326 5688 4351 -1518 1312 44 O
ATOM 1901 CB ASP A 709 66.366 63.221 46.305 1.00 50.35 C
ANISOU 1901 CB ASP A 709 7008 6632 5489 -1747 1530 -119 C
ATOM 1902 CG ASP A 709 65.318 62.143 46.556 1.00 53.57 C
ANISOU 1902 CG ASP A 709 7474 7019 5863 -1972 1706 -160 C
ATOM 1903 OD1 ASP A 709 64.758 62.071 47.682 1.00 57.06 O
ANISOU 1903 OD1 ASP A 709 8008 7491 6182 -2139 1875 -200 O
ATOM 1904 OD2 ASP A 709 65.089 61.377 45.623 1.00 55.99 O
ANISOU 1904 OD2 ASP A 709 7741 7275 6257 -1988 1678 -154 O
ATOM 1905 N LEU A 710 67.649 66.099 46.501 1.00 39.41 N
ANISOU 1905 N LEU A 710 5433 5379 4164 -1411 1325 -165 N
ATOM 1906 CA LEU A 710 68.797 66.974 46.372 1.00 36.17 C
ANISOU 1906 CA LEU A 710 5020 4960 3760 -1239 1168 -111 C
ATOM 1907 C LEU A 710 69.412 67.394 47.737 1.00 34.93 C
ANISOU 1907 C LEU A 710 5025 4808 3438 -1257 1175 -73 C
ATOM 1908 O LEU A 710 70.623 67.618 47.807 1.00 34.20 O
ANISOU 1908 O LEU A 710 5015 4672 3306 -1146 1032 19 O
ATOM 1909 CB LEU A 710 68.413 68.231 45.592 1.00 35.22 C
ANISOU 1909 CB LEU A 710 4657 4922 3802 -1125 1128 -225 C
ATOM 1910 CG LEU A 710 69.587 69.121 45.174 1.00 33.45 C
ANISOU 1910 CG LEU A 710 4416 4681 3612 -953 962 -171 C
ATOM 1911 CD1 LEU A 710 70.656 68.330 44.450 1.00 32.09 C
ANISOU 1911 CD1 LEU A 710 4336 4417 3440 -884 834 -41 C
ATOM 1912 CD2 LEU A 710 69.053 70.225 44.285 1.00 33.54 C
ANISOU 1912 CD2 LEU A 710 4210 4751 3782 -857 926 -278 C
ATOM 1913 N PHE A 711 68.592 67.544 48.766 1.00 35.47 N
ANISOU 1913 N PHE A 711 5125 4934 3417 -1394 1339 -154 N
ATOM 1914 CA PHE A 711 69.018 68.081 50.061 1.00 36.93 C
ANISOU 1914 CA PHE A 711 5450 5139 3441 -1421 1361 -146 C
ATOM 1915 C PHE A 711 69.218 67.009 51.155 1.00 39.16 C
ANISOU 1915 C PHE A 711 6026 5349 3504 -1568 1419 -42 C
ATOM 1916 O PHE A 711 69.483 67.345 52.288 1.00 40.78 O
ANISOU 1916 O PHE A 711 6375 5570 3550 -1615 1446 -35 O
ATOM 1917 CB PHE A 711 68.043 69.158 50.503 1.00 38.36 C
ANISOU 1917 CB PHE A 711 5473 5437 3664 -1461 1502 -321 C
ATOM 1918 CG PHE A 711 67.852 70.218 49.462 1.00 38.09 C
ANISOU 1918 CG PHE A 711 5179 5454 3837 -1309 1426 -414 C
ATOM 1919 CD1 PHE A 711 68.869 71.124 49.182 1.00 36.24 C
ANISOU 1919 CD1 PHE A 711 4925 5206 3640 -1148 1264 -374 C
ATOM 1920 CD2 PHE A 711 66.673 70.268 48.714 1.00 39.73 C
ANISOU 1920 CD2 PHE A 711 5173 5718 4206 -1331 1506 -539 C
ATOM 1921 CE1 PHE A 711 68.710 72.076 48.198 1.00 34.53 C
ANISOU 1921 CE1 PHE A 711 4502 5018 3600 -1016 1189 -446 C
ATOM 1922 CE2 PHE A 711 66.520 71.215 47.715 1.00 38.62 C
ANISOU 1922 CE2 PHE A 711 4819 5607 4247 -1182 1411 -611 C
ATOM 1923 CZ PHE A 711 67.532 72.108 47.460 1.00 35.91 C
ANISOU 1923 CZ PHE A 711 4484 5238 3924 -1029 1257 -559 C
ATOM 1924 N THR A 712 69.152 65.737 50.788 1.00 40.29 N
ANISOU 1924 N THR A 712 6272 5403 3633 -1634 1422 44 N
ATOM 1925 CA THR A 712 69.304 64.684 51.781 1.00 43.12 C
ANISOU 1925 CA THR A 712 6932 5671 3780 -1776 1470 150 C
ATOM 1926 C THR A 712 70.471 63.741 51.478 1.00 43.04 C
ANISOU 1926 C THR A 712 7101 5517 3735 -1682 1280 324 C
ATOM 1927 O THR A 712 70.542 62.642 52.028 1.00 43.89 O
ANISOU 1927 O THR A 712 7461 5518 3698 -1789 1300 425 O
ATOM 1928 CB THR A 712 67.988 63.909 51.895 1.00 45.21 C
ANISOU 1928 CB THR A 712 7205 5945 4029 -1992 1689 82 C
ATOM 1929 OG1 THR A 712 67.625 63.428 50.608 1.00 45.59 O
ANISOU 1929 OG1 THR A 712 7088 5973 4260 -1956 1665 62 O
ATOM 1930 CG2 THR A 712 66.910 64.843 52.446 1.00 47.08 C
ANISOU 1930 CG2 THR A 712 7285 6325 4277 -2091 1885 -100 C
ATOM 1931 N GLY A 713 71.440 64.208 50.704 1.00 40.51 N
ANISOU 1931 N GLY A 713 6668 5191 3533 -1482 1095 357 N
ATOM 1932 CA GLY A 713 72.651 63.431 50.443 1.00 40.38 C
ANISOU 1932 CA GLY A 713 6794 5049 3500 -1369 907 500 C
ATOM 1933 C GLY A 713 73.555 63.403 51.664 1.00 41.45 C
ANISOU 1933 C GLY A 713 7170 5135 3442 -1356 808 596 C
ATOM 1934 O GLY A 713 73.408 64.218 52.559 1.00 40.58 O
ANISOU 1934 O GLY A 713 7083 5104 3232 -1402 861 544 O
ATOM 1935 N ASP A 714 74.458 62.413 51.693 1.00 44.03 N
ANISOU 1935 N ASP A 714 7686 5327 3718 -1294 659 730 N
ATOM 1936 CA AASP A 714 75.400 62.214 52.803 0.50 45.76 C
ANISOU 1936 CA AASP A 714 8157 5476 3753 -1265 522 836 C
ATOM 1937 CA BASP A 714 75.409 62.206 52.800 0.50 46.04 C
ANISOU 1937 CA BASP A 714 8193 5510 3789 -1264 521 837 C
ATOM 1938 C ASP A 714 76.719 61.619 52.277 1.00 44.62 C
ANISOU 1938 C ASP A 714 8050 5222 3682 -1079 289 938 C
ATOM 1939 O ASP A 714 76.764 61.070 51.170 1.00 47.17 O
ANISOU 1939 O ASP A 714 8268 5496 4158 -1017 268 941 O
ATOM 1940 CB AASP A 714 74.759 61.298 53.850 0.50 49.04 C
ANISOU 1940 CB AASP A 714 8876 5810 3949 -1464 638 902 C
ATOM 1941 CB BASP A 714 74.812 61.300 53.895 0.50 49.89 C
ANISOU 1941 CB BASP A 714 8993 5914 4048 -1461 629 906 C
ATOM 1942 CG AASP A 714 75.470 61.332 55.172 0.50 51.41 C
ANISOU 1942 CG AASP A 714 9445 6068 4022 -1470 529 987 C
ATOM 1943 CG BASP A 714 74.254 59.963 53.352 0.50 51.44 C
ANISOU 1943 CG BASP A 714 9283 5989 4273 -1553 701 958 C
ATOM 1944 OD1AASP A 714 76.133 62.347 55.466 0.50 52.15 O
ANISOU 1944 OD1AASP A 714 9453 6244 4118 -1365 428 951 O
ATOM 1945 OD1BASP A 714 74.442 59.604 52.176 0.50 53.23 O
ANISOU 1945 OD1BASP A 714 9363 6181 4683 -1452 643 955 O
ATOM 1946 OD2AASP A 714 75.363 60.339 55.926 0.50 54.62 O
ANISOU 1946 OD2AASP A 714 10162 6352 4241 -1585 541 1092 O
ATOM 1947 OD2BASP A 714 73.599 59.270 54.127 0.50 56.88 O
ANISOU 1947 OD2BASP A 714 10205 6616 4791 -1742 827 998 O
ATOM 1948 N GLY A 715 77.783 61.747 53.058 1.00 46.24 N
ANISOU 1948 N GLY A 715 8392 5394 3783 -990 113 1007 N
ATOM 1949 CA GLY A 715 79.052 61.092 52.750 1.00 45.84 C
ANISOU 1949 CA GLY A 715 8399 5231 3788 -817 -116 1098 C
ATOM 1950 C GLY A 715 80.095 61.900 52.016 1.00 45.39 C
ANISOU 1950 C GLY A 715 8096 5243 3907 -626 -260 1047 C
ATOM 1951 O GLY A 715 81.160 61.382 51.699 1.00 46.77 O
ANISOU 1951 O GLY A 715 8283 5337 4151 -477 -441 1101 O
ATOM 1952 N ASP A 716 79.783 63.152 51.685 1.00 41.72 N
ANISOU 1952 N ASP A 716 7401 4923 3526 -629 -174 935 N
ATOM 1953 CA ASP A 716 80.716 64.044 50.999 1.00 39.32 C
ANISOU 1953 CA ASP A 716 6868 4691 3382 -475 -287 878 C
ATOM 1954 C ASP A 716 80.232 65.450 51.316 1.00 36.23 C
ANISOU 1954 C ASP A 716 6351 4438 2976 -530 -188 776 C
ATOM 1955 O ASP A 716 79.016 65.739 51.364 1.00 36.40 O
ANISOU 1955 O ASP A 716 6340 4515 2975 -656 -2 715 O
ATOM 1956 CB ASP A 716 80.666 63.742 49.494 1.00 37.83 C
ANISOU 1956 CB ASP A 716 6491 4487 3395 -409 -259 847 C
ATOM 1957 CG ASP A 716 81.704 64.541 48.621 1.00 38.79 C
ANISOU 1957 CG ASP A 716 6383 4668 3686 -257 -365 792 C
ATOM 1958 OD1 ASP A 716 81.940 65.738 48.764 1.00 35.45 O
ANISOU 1958 OD1 ASP A 716 5841 4345 3284 -238 -372 727 O
ATOM 1959 OD2 ASP A 716 82.185 63.955 47.640 1.00 44.05 O
ANISOU 1959 OD2 ASP A 716 6976 5282 4480 -169 -415 801 O
ATOM 1960 N TYR A 717 81.176 66.338 51.514 1.00 34.09 N
ANISOU 1960 N TYR A 717 5999 4222 2731 -435 -310 747 N
ATOM 1961 CA TYR A 717 80.884 67.758 51.670 1.00 31.97 C
ANISOU 1961 CA TYR A 717 5593 4074 2480 -462 -239 642 C
ATOM 1962 C TYR A 717 80.012 68.329 50.549 1.00 29.39 C
ANISOU 1962 C TYR A 717 5048 3808 2311 -479 -94 554 C
ATOM 1963 O TYR A 717 79.201 69.243 50.801 1.00 29.13 O
ANISOU 1963 O TYR A 717 4949 3855 2264 -548 27 466 O
ATOM 1964 CB TYR A 717 82.198 68.538 51.818 1.00 31.63 C
ANISOU 1964 CB TYR A 717 5475 4067 2478 -344 -412 624 C
ATOM 1965 CG TYR A 717 82.058 70.006 52.143 1.00 30.75 C
ANISOU 1965 CG TYR A 717 5259 4060 2365 -370 -364 523 C
ATOM 1966 CD1 TYR A 717 81.118 70.473 53.088 1.00 31.60 C
ANISOU 1966 CD1 TYR A 717 5460 4216 2332 -493 -234 476 C
ATOM 1967 CD2 TYR A 717 82.915 70.936 51.584 1.00 29.62 C
ANISOU 1967 CD2 TYR A 717 4938 3964 2354 -277 -449 468 C
ATOM 1968 CE1 TYR A 717 81.031 71.825 53.422 1.00 31.61 C
ANISOU 1968 CE1 TYR A 717 5374 4301 2334 -507 -197 375 C
ATOM 1969 CE2 TYR A 717 82.841 72.280 51.929 1.00 29.23 C
ANISOU 1969 CE2 TYR A 717 4813 3992 2299 -301 -415 377 C
ATOM 1970 CZ TYR A 717 81.866 72.735 52.815 1.00 30.12 C
ANISOU 1970 CZ TYR A 717 5015 4147 2284 -410 -289 328 C
ATOM 1971 OH TYR A 717 81.801 74.090 53.141 1.00 30.52 O
ANISOU 1971 OH TYR A 717 4992 4267 2339 -426 -258 227 O
ATOM 1972 N GLN A 718 80.123 67.775 49.351 1.00 29.12 N
ANISOU 1972 N GLN A 718 4914 3733 2419 -419 -108 571 N
ATOM 1973 CA GLN A 718 79.235 68.153 48.221 1.00 28.25 C
ANISOU 1973 CA GLN A 718 4621 3666 2446 -437 14 497 C
ATOM 1974 C GLN A 718 77.785 68.246 48.682 1.00 28.67 C
ANISOU 1974 C GLN A 718 4700 3761 2432 -577 192 443 C
ATOM 1975 O GLN A 718 77.042 69.180 48.327 1.00 27.65 O
ANISOU 1975 O GLN A 718 4420 3707 2377 -595 283 346 O
ATOM 1976 CB GLN A 718 79.353 67.121 47.105 1.00 29.08 C
ANISOU 1976 CB GLN A 718 4697 3698 2654 -393 -7 540 C
ATOM 1977 CG GLN A 718 78.426 67.361 45.917 1.00 28.64 C
ANISOU 1977 CG GLN A 718 4477 3678 2725 -416 100 472 C
ATOM 1978 CD GLN A 718 78.535 66.291 44.865 1.00 29.26 C
ANISOU 1978 CD GLN A 718 4548 3683 2888 -383 81 511 C
ATOM 1979 OE1 GLN A 718 79.473 65.504 44.854 1.00 30.55 O
ANISOU 1979 OE1 GLN A 718 4791 3768 3047 -315 -23 578 O
ATOM 1980 NE2 GLN A 718 77.597 66.280 43.961 1.00 29.19 N
ANISOU 1980 NE2 GLN A 718 4436 3696 2961 -424 173 459 N
ATOM 1981 N PHE A 719 77.361 67.262 49.445 1.00 31.28 N
ANISOU 1981 N PHE A 719 5221 4036 2628 -677 244 500 N
ATOM 1982 CA PHE A 719 75.945 67.155 49.789 1.00 32.97 C
ANISOU 1982 CA PHE A 719 5451 4286 2790 -829 435 441 C
ATOM 1983 C PHE A 719 75.538 68.168 50.799 1.00 32.34 C
ANISOU 1983 C PHE A 719 5379 4292 2615 -893 514 362 C
ATOM 1984 O PHE A 719 74.354 68.549 50.848 1.00 33.50 O
ANISOU 1984 O PHE A 719 5439 4506 2783 -986 678 261 O
ATOM 1985 CB PHE A 719 75.609 65.712 50.159 1.00 36.21 C
ANISOU 1985 CB PHE A 719 6068 4598 3092 -934 480 527 C
ATOM 1986 CG PHE A 719 75.844 64.796 49.013 1.00 36.43 C
ANISOU 1986 CG PHE A 719 6056 4545 3240 -872 423 576 C
ATOM 1987 CD1 PHE A 719 75.065 64.928 47.851 1.00 36.36 C
ANISOU 1987 CD1 PHE A 719 5850 4577 3388 -877 505 499 C
ATOM 1988 CD2 PHE A 719 76.885 63.873 49.017 1.00 38.76 C
ANISOU 1988 CD2 PHE A 719 6494 4725 3508 -791 274 688 C
ATOM 1989 CE1 PHE A 719 75.302 64.154 46.741 1.00 37.16 C
ANISOU 1989 CE1 PHE A 719 5910 4610 3598 -819 452 533 C
ATOM 1990 CE2 PHE A 719 77.127 63.094 47.893 1.00 38.46 C
ANISOU 1990 CE2 PHE A 719 6403 4616 3595 -725 227 716 C
ATOM 1991 CZ PHE A 719 76.339 63.231 46.766 1.00 38.62 C
ANISOU 1991 CZ PHE A 719 6240 4681 3754 -745 321 639 C
ATOM 1992 N ASP A 720 76.487 68.625 51.623 1.00 31.63 N
ANISOU 1992 N ASP A 720 5386 4205 2427 -845 401 394 N
ATOM 1993 CA ASP A 720 76.236 69.728 52.511 1.00 32.85 C
ANISOU 1993 CA ASP A 720 5536 4443 2503 -888 460 307 C
ATOM 1994 C ASP A 720 76.030 71.041 51.710 1.00 30.21 C
ANISOU 1994 C ASP A 720 4948 4186 2343 -809 479 191 C
ATOM 1995 O ASP A 720 75.277 71.901 52.150 1.00 30.71 O
ANISOU 1995 O ASP A 720 4953 4321 2393 -862 594 82 O
ATOM 1996 CB ASP A 720 77.384 69.944 53.516 1.00 34.63 C
ANISOU 1996 CB ASP A 720 5918 4652 2586 -847 310 363 C
ATOM 1997 CG ASP A 720 77.623 68.740 54.431 1.00 40.19 C
ANISOU 1997 CG ASP A 720 6908 5270 3094 -918 267 482 C
ATOM 1998 OD1 ASP A 720 76.632 68.161 54.949 1.00 41.55 O
ANISOU 1998 OD1 ASP A 720 7207 5430 3150 -1070 426 482 O
ATOM 1999 OD2 ASP A 720 78.831 68.419 54.684 1.00 42.73 O
ANISOU 1999 OD2 ASP A 720 7331 5532 3371 -824 68 572 O
ATOM 2000 N ILE A 721 76.738 71.192 50.602 1.00 29.49 N
ANISOU 2000 N ILE A 721 4727 4074 2404 -685 364 216 N
ATOM 2001 CA ILE A 721 76.665 72.446 49.816 1.00 27.40 C
ANISOU 2001 CA ILE A 721 4256 3863 2292 -608 360 124 C
ATOM 2002 C ILE A 721 75.215 72.689 49.374 1.00 27.79 C
ANISOU 2002 C ILE A 721 4179 3956 2422 -665 517 24 C
ATOM 2003 O ILE A 721 74.711 73.799 49.475 1.00 26.60 O
ANISOU 2003 O ILE A 721 3926 3862 2318 -658 572 -82 O
ATOM 2004 CB ILE A 721 77.620 72.476 48.645 1.00 27.13 C
ANISOU 2004 CB ILE A 721 4121 3795 2394 -488 231 168 C
ATOM 2005 CG1 ILE A 721 79.079 72.295 49.125 1.00 27.48 C
ANISOU 2005 CG1 ILE A 721 4259 3807 2377 -425 71 243 C
ATOM 2006 CG2 ILE A 721 77.454 73.803 47.902 1.00 25.83 C
ANISOU 2006 CG2 ILE A 721 3779 3673 2361 -430 238 78 C
ATOM 2007 CD1 ILE A 721 79.552 73.319 50.097 1.00 28.09 C
ANISOU 2007 CD1 ILE A 721 4368 3928 2375 -426 28 198 C
ATOM 2008 N TYR A 722 74.525 71.645 48.948 1.00 27.56 N
ANISOU 2008 N TYR A 722 4160 3901 2412 -724 588 50 N
ATOM 2009 CA TYR A 722 73.108 71.836 48.555 1.00 28.66 C
ANISOU 2009 CA TYR A 722 4162 4090 2637 -783 731 -59 C
ATOM 2010 C TYR A 722 72.300 72.420 49.693 1.00 29.55 C
ANISOU 2010 C TYR A 722 4294 4270 2662 -878 870 -164 C
ATOM 2011 O TYR A 722 71.501 73.354 49.522 1.00 29.23 O
ANISOU 2011 O TYR A 722 4099 4292 2717 -863 941 -292 O
ATOM 2012 CB TYR A 722 72.498 70.517 48.034 1.00 28.20 C
ANISOU 2012 CB TYR A 722 4126 3991 2596 -856 790 -18 C
ATOM 2013 CG TYR A 722 73.236 69.935 46.880 1.00 27.44 C
ANISOU 2013 CG TYR A 722 4008 3829 2589 -764 667 68 C
ATOM 2014 CD1 TYR A 722 73.469 70.665 45.715 1.00 26.35 C
ANISOU 2014 CD1 TYR A 722 3710 3704 2598 -651 589 38 C
ATOM 2015 CD2 TYR A 722 73.718 68.645 46.921 1.00 28.76 C
ANISOU 2015 CD2 TYR A 722 4324 3912 2690 -790 628 178 C
ATOM 2016 CE1 TYR A 722 74.169 70.132 44.657 1.00 25.16 C
ANISOU 2016 CE1 TYR A 722 3545 3496 2517 -576 491 108 C
ATOM 2017 CE2 TYR A 722 74.461 68.116 45.903 1.00 27.85 C
ANISOU 2017 CE2 TYR A 722 4189 3736 2656 -700 519 244 C
ATOM 2018 CZ TYR A 722 74.651 68.829 44.741 1.00 26.42 C
ANISOU 2018 CZ TYR A 722 3841 3580 2617 -600 461 205 C
ATOM 2019 OH TYR A 722 75.323 68.252 43.665 1.00 28.42 O
ANISOU 2019 OH TYR A 722 4075 3777 2947 -526 376 259 O
ATOM 2020 N ARG A 723 72.481 71.887 50.909 1.00 30.53 N
ANISOU 2020 N ARG A 723 4620 4382 2598 -978 913 -117 N
ATOM 2021 CA ARG A 723 71.745 72.379 52.037 1.00 32.12 C
ANISOU 2021 CA ARG A 723 4862 4649 2694 -1085 1061 -220 C
ATOM 2022 C ARG A 723 72.158 73.774 52.436 1.00 31.33 C
ANISOU 2022 C ARG A 723 4710 4593 2602 -1008 1013 -295 C
ATOM 2023 O ARG A 723 71.339 74.555 52.867 1.00 32.12 O
ANISOU 2023 O ARG A 723 4730 4759 2715 -1047 1137 -433 O
ATOM 2024 CB ARG A 723 71.929 71.433 53.236 1.00 34.02 C
ANISOU 2024 CB ARG A 723 5371 4853 2704 -1218 1105 -135 C
ATOM 2025 CG ARG A 723 71.301 70.072 53.095 1.00 35.31 C
ANISOU 2025 CG ARG A 723 5619 4968 2830 -1338 1199 -80 C
ATOM 2026 CD ARG A 723 71.452 69.238 54.387 1.00 38.28 C
ANISOU 2026 CD ARG A 723 6297 5296 2952 -1482 1247 4 C
ATOM 2027 NE ARG A 723 72.746 68.546 54.458 1.00 38.94 N
ANISOU 2027 NE ARG A 723 6566 5276 2954 -1403 1046 172 N
ATOM 2028 CZ ARG A 723 73.050 67.359 53.908 1.00 40.15 C
ANISOU 2028 CZ ARG A 723 6801 5327 3126 -1390 974 289 C
ATOM 2029 NH1 ARG A 723 72.164 66.675 53.191 1.00 41.07 N
ANISOU 2029 NH1 ARG A 723 6839 5430 3337 -1460 1086 266 N
ATOM 2030 NH2 ARG A 723 74.282 66.863 54.060 1.00 41.53 N
ANISOU 2030 NH2 ARG A 723 7132 5412 3236 -1297 778 423 N
ATOM 2031 N LEU A 724 73.449 74.071 52.345 1.00 30.20 N
ANISOU 2031 N LEU A 724 4614 4411 2448 -905 838 -213 N
ATOM 2032 CA LEU A 724 73.934 75.405 52.663 1.00 30.65 C
ANISOU 2032 CA LEU A 724 4626 4501 2519 -836 781 -282 C
ATOM 2033 C LEU A 724 73.429 76.468 51.652 1.00 29.21 C
ANISOU 2033 C LEU A 724 4214 4341 2542 -743 789 -387 C
ATOM 2034 O LEU A 724 73.157 77.601 52.067 1.00 31.58 O
ANISOU 2034 O LEU A 724 4461 4680 2860 -728 829 -501 O
ATOM 2035 CB LEU A 724 75.445 75.425 52.717 1.00 29.75 C
ANISOU 2035 CB LEU A 724 4597 4342 2365 -755 588 -177 C
ATOM 2036 CG LEU A 724 75.960 74.662 53.948 1.00 32.34 C
ANISOU 2036 CG LEU A 724 5168 4649 2471 -834 557 -94 C
ATOM 2037 CD1 LEU A 724 77.439 74.445 53.768 1.00 32.34 C
ANISOU 2037 CD1 LEU A 724 5218 4599 2471 -735 346 14 C
ATOM 2038 CD2 LEU A 724 75.639 75.402 55.237 1.00 34.17 C
ANISOU 2038 CD2 LEU A 724 5493 4936 2554 -917 643 -187 C
ATOM 2039 N MET A 725 73.275 76.089 50.391 1.00 28.59 N
ANISOU 2039 N MET A 725 4021 4235 2607 -685 750 -352 N
ATOM 2040 CA MET A 725 72.715 77.023 49.402 1.00 28.08 C
ANISOU 2040 CA MET A 725 3762 4182 2725 -599 746 -443 C
ATOM 2041 C MET A 725 71.271 77.312 49.738 1.00 29.97 C
ANISOU 2041 C MET A 725 3905 4481 3001 -659 909 -590 C
ATOM 2042 O MET A 725 70.843 78.453 49.672 1.00 30.34 O
ANISOU 2042 O MET A 725 3841 4550 3138 -601 924 -706 O
ATOM 2043 CB MET A 725 72.744 76.442 48.007 1.00 27.10 C
ANISOU 2043 CB MET A 725 3554 4018 2724 -542 679 -378 C
ATOM 2044 CG MET A 725 74.097 76.490 47.336 1.00 25.96 C
ANISOU 2044 CG MET A 725 3437 3821 2606 -455 522 -273 C
ATOM 2045 SD MET A 725 73.984 76.062 45.599 1.00 25.20 S
ANISOU 2045 SD MET A 725 3229 3685 2660 -388 462 -230 S
ATOM 2046 CE MET A 725 73.441 74.363 45.652 1.00 25.60 C
ANISOU 2046 CE MET A 725 3348 3725 2655 -483 537 -171 C
ATOM 2047 N LYS A 726 70.530 76.274 50.125 1.00 31.61 N
ANISOU 2047 N LYS A 726 4156 4712 3140 -779 1034 -591 N
ATOM 2048 CA LYS A 726 69.123 76.425 50.519 1.00 34.46 C
ANISOU 2048 CA LYS A 726 4416 5143 3535 -860 1213 -746 C
ATOM 2049 C LYS A 726 68.941 77.272 51.757 1.00 35.72 C
ANISOU 2049 C LYS A 726 4621 5352 3599 -904 1310 -858 C
ATOM 2050 O LYS A 726 68.000 78.062 51.870 1.00 38.13 O
ANISOU 2050 O LYS A 726 4781 5709 3996 -893 1409 -1023 O
ATOM 2051 CB LYS A 726 68.497 75.042 50.695 1.00 36.00 C
ANISOU 2051 CB LYS A 726 4674 5344 3660 -1004 1332 -712 C
ATOM 2052 CG LYS A 726 67.018 75.064 51.040 1.00 40.56 C
ANISOU 2052 CG LYS A 726 5127 6002 4283 -1108 1534 -881 C
ATOM 2053 CD LYS A 726 66.506 73.634 51.220 1.00 43.46 C
ANISOU 2053 CD LYS A 726 5582 6364 4568 -1272 1651 -833 C
ATOM 2054 CE LYS A 726 65.091 73.624 51.710 1.00 48.27 C
ANISOU 2054 CE LYS A 726 6075 7061 5204 -1405 1876 -1012 C
ATOM 2055 NZ LYS A 726 64.435 72.374 51.244 1.00 49.57 N
ANISOU 2055 NZ LYS A 726 6223 7216 5395 -1522 1952 -987 N
ATOM 2056 N LYS A 727 69.867 77.149 52.694 1.00 35.64 N
ANISOU 2056 N LYS A 727 4812 5323 3407 -947 1272 -776 N
ATOM 2057 CA LYS A 727 69.883 78.004 53.831 1.00 38.07 C
ANISOU 2057 CA LYS A 727 5183 5670 3610 -981 1337 -872 C
ATOM 2058 C LYS A 727 70.138 79.464 53.440 1.00 37.15 C
ANISOU 2058 C LYS A 727 4942 5545 3629 -840 1248 -956 C
ATOM 2059 O LYS A 727 69.448 80.345 53.939 1.00 36.63 O
ANISOU 2059 O LYS A 727 4803 5523 3591 -844 1352 -1116 O
ATOM 2060 CB LYS A 727 70.945 77.545 54.812 1.00 40.24 C
ANISOU 2060 CB LYS A 727 5709 5917 3661 -1042 1272 -752 C
ATOM 2061 CG LYS A 727 71.001 78.443 56.019 1.00 45.59 C
ANISOU 2061 CG LYS A 727 6471 6637 4213 -1085 1333 -854 C
ATOM 2062 CD LYS A 727 71.416 77.687 57.263 1.00 50.33 C
ANISOU 2062 CD LYS A 727 7341 7236 4547 -1218 1361 -775 C
ATOM 2063 CE LYS A 727 71.680 78.671 58.390 1.00 53.21 C
ANISOU 2063 CE LYS A 727 7800 7637 4781 -1244 1382 -869 C
ATOM 2064 NZ LYS A 727 72.826 79.545 57.984 1.00 54.35 N
ANISOU 2064 NZ LYS A 727 7901 7743 5007 -1099 1175 -833 N
ATOM 2065 N GLU A 728 71.149 79.689 52.595 1.00 34.34 N
ANISOU 2065 N GLU A 728 4573 5128 3346 -726 1064 -850 N
ATOM 2066 CA GLU A 728 71.507 81.028 52.084 1.00 34.54 C
ANISOU 2066 CA GLU A 728 4501 5123 3499 -598 963 -906 C
ATOM 2067 C GLU A 728 70.339 81.729 51.369 1.00 34.40 C
ANISOU 2067 C GLU A 728 4281 5116 3673 -527 1019 -1045 C
ATOM 2068 O GLU A 728 70.132 82.931 51.584 1.00 34.23 O
ANISOU 2068 O GLU A 728 4203 5091 3713 -468 1025 -1164 O
ATOM 2069 CB GLU A 728 72.746 80.964 51.163 1.00 33.40 C
ANISOU 2069 CB GLU A 728 4375 4913 3403 -510 776 -763 C
ATOM 2070 CG GLU A 728 72.976 82.208 50.302 1.00 33.82 C
ANISOU 2070 CG GLU A 728 4319 4919 3611 -389 680 -806 C
ATOM 2071 CD GLU A 728 73.294 83.443 51.088 1.00 35.50 C
ANISOU 2071 CD GLU A 728 4570 5129 3790 -374 673 -897 C
ATOM 2072 OE1 GLU A 728 73.675 83.347 52.275 1.00 38.54 O
ANISOU 2072 OE1 GLU A 728 5082 5545 4015 -450 706 -903 O
ATOM 2073 OE2 GLU A 728 73.169 84.557 50.535 1.00 35.45 O
ANISOU 2073 OE2 GLU A 728 4478 5079 3911 -286 630 -965 O
ATOM 2074 N ASN A 729 69.592 80.988 50.548 1.00 33.17 N
ANISOU 2074 N ASN A 729 4021 4969 3612 -531 1049 -1034 N
ATOM 2075 CA ASN A 729 68.556 81.618 49.691 1.00 33.21 C
ANISOU 2075 CA ASN A 729 3823 4977 3817 -440 1056 -1155 C
ATOM 2076 C ASN A 729 67.137 81.449 50.206 1.00 36.49 C
ANISOU 2076 C ASN A 729 4125 5472 4266 -513 1240 -1319 C
ATOM 2077 O ASN A 729 66.203 81.867 49.530 1.00 36.74 O
ANISOU 2077 O ASN A 729 3973 5513 4472 -438 1242 -1431 O
ATOM 2078 CB ASN A 729 68.664 81.164 48.226 1.00 31.60 C
ANISOU 2078 CB ASN A 729 3549 4727 3730 -368 934 -1056 C
ATOM 2079 CG ASN A 729 68.396 79.675 48.043 1.00 30.01 C
ANISOU 2079 CG ASN A 729 3373 4550 3480 -467 991 -979 C
ATOM 2080 OD1 ASN A 729 67.649 79.055 48.807 1.00 32.08 O
ANISOU 2080 OD1 ASN A 729 3641 4871 3676 -586 1145 -1041 O
ATOM 2081 ND2 ASN A 729 69.001 79.109 47.051 1.00 29.16 N
ANISOU 2081 ND2 ASN A 729 3288 4393 3400 -428 876 -850 N
ATOM 2082 N ASN A 730 66.963 80.820 51.381 1.00 37.34 N
ANISOU 2082 N ASN A 730 4342 5637 4210 -664 1393 -1338 N
ATOM 2083 CA ASN A 730 65.629 80.620 51.967 1.00 40.14 C
ANISOU 2083 CA ASN A 730 4592 6076 4581 -764 1602 -1508 C
ATOM 2084 C ASN A 730 64.715 79.861 51.051 1.00 38.88 C
ANISOU 2084 C ASN A 730 4275 5939 4557 -776 1629 -1528 C
ATOM 2085 O ASN A 730 63.479 80.068 51.050 1.00 39.78 O
ANISOU 2085 O ASN A 730 4202 6119 4796 -788 1749 -1708 O
ATOM 2086 CB ASN A 730 65.011 81.954 52.365 1.00 42.28 C
ANISOU 2086 CB ASN A 730 4740 6375 4950 -690 1661 -1711 C
ATOM 2087 CG ASN A 730 65.780 82.635 53.470 1.00 44.49 C
ANISOU 2087 CG ASN A 730 5186 6646 5073 -714 1672 -1718 C
ATOM 2088 OD1 ASN A 730 65.746 82.194 54.596 1.00 50.30 O
ANISOU 2088 OD1 ASN A 730 6054 7431 5625 -860 1812 -1736 O
ATOM 2089 ND2 ASN A 730 66.453 83.720 53.161 1.00 45.50 N
ANISOU 2089 ND2 ASN A 730 5316 6707 5264 -580 1526 -1710 N
ATOM 2090 N ASN A 731 65.324 78.936 50.325 1.00 36.13 N
ANISOU 2090 N ASN A 731 4003 5542 4183 -781 1523 -1354 N
ATOM 2091 CA ASN A 731 64.665 78.129 49.332 1.00 36.79 C
ANISOU 2091 CA ASN A 731 3966 5631 4381 -791 1515 -1343 C
ATOM 2092 C ASN A 731 63.984 78.929 48.198 1.00 37.39 C
ANISOU 2092 C ASN A 731 3812 5702 4691 -637 1418 -1446 C
ATOM 2093 O ASN A 731 63.017 78.430 47.597 1.00 38.41 O
ANISOU 2093 O ASN A 731 3788 5870 4937 -659 1455 -1516 O
ATOM 2094 CB ASN A 731 63.619 77.205 50.011 1.00 39.03 C
ANISOU 2094 CB ASN A 731 4227 5992 4611 -977 1735 -1433 C
ATOM 2095 CG ASN A 731 63.363 75.929 49.210 1.00 38.17 C
ANISOU 2095 CG ASN A 731 4103 5866 4532 -1043 1724 -1348 C
ATOM 2096 OD1 ASN A 731 64.231 75.413 48.523 1.00 36.61 O
ANISOU 2096 OD1 ASN A 731 4006 5596 4310 -996 1580 -1180 O
ATOM 2097 ND2 ASN A 731 62.138 75.434 49.296 1.00 40.67 N
ANISOU 2097 ND2 ASN A 731 4285 6254 4913 -1156 1884 -1481 N
ATOM 2098 N ARG A 732 64.473 80.148 47.917 1.00 36.07 N
ANISOU 2098 N ARG A 732 3630 5485 4589 -487 1289 -1456 N
ATOM 2099 CA ARG A 732 63.978 80.936 46.799 1.00 35.72 C
ANISOU 2099 CA ARG A 732 3414 5410 4747 -329 1162 -1524 C
ATOM 2100 C ARG A 732 65.086 80.983 45.728 1.00 32.65 C
ANISOU 2100 C ARG A 732 3122 4926 4357 -236 961 -1344 C
ATOM 2101 O ARG A 732 65.982 81.792 45.825 1.00 32.49 O
ANISOU 2101 O ARG A 732 3196 4848 4300 -169 876 -1292 O
ATOM 2102 CB ARG A 732 63.572 82.310 47.291 1.00 37.92 C
ANISOU 2102 CB ARG A 732 3608 5692 5108 -237 1182 -1690 C
ATOM 2103 CG ARG A 732 62.330 82.241 48.196 1.00 41.80 C
ANISOU 2103 CG ARG A 732 3964 6287 5632 -325 1393 -1898 C
ATOM 2104 CD ARG A 732 61.751 83.614 48.447 1.00 45.75 C
ANISOU 2104 CD ARG A 732 4333 6784 6266 -200 1396 -2091 C
ATOM 2105 NE ARG A 732 62.597 84.387 49.350 1.00 47.75 N
ANISOU 2105 NE ARG A 732 4746 7003 6395 -199 1408 -2075 N
ATOM 2106 CZ ARG A 732 62.435 84.510 50.681 1.00 50.73 C
ANISOU 2106 CZ ARG A 732 5176 7443 6657 -306 1591 -2182 C
ATOM 2107 NH1 ARG A 732 63.302 85.257 51.387 1.00 50.86 N
ANISOU 2107 NH1 ARG A 732 5348 7416 6561 -293 1567 -2158 N
ATOM 2108 NH2 ARG A 732 61.437 83.899 51.316 1.00 52.81 N
ANISOU 2108 NH2 ARG A 732 5346 7811 6908 -436 1800 -2317 N
ATOM 2109 N TRP A 733 64.968 80.082 44.750 1.00 30.17 N
ANISOU 2109 N TRP A 733 2780 4603 4082 -248 905 -1265 N
ATOM 2110 CA TRP A 733 65.989 79.798 43.740 1.00 28.54 C
ANISOU 2110 CA TRP A 733 2672 4320 3852 -197 751 -1093 C
ATOM 2111 C TRP A 733 66.007 80.824 42.595 1.00 27.78 C
ANISOU 2111 C TRP A 733 2512 4156 3886 -39 584 -1101 C
ATOM 2112 O TRP A 733 66.979 80.871 41.855 1.00 25.97 O
ANISOU 2112 O TRP A 733 2380 3859 3627 4 465 -971 O
ATOM 2113 CB TRP A 733 65.874 78.343 43.229 1.00 28.48 C
ANISOU 2113 CB TRP A 733 2681 4325 3814 -288 773 -1011 C
ATOM 2114 CG TRP A 733 66.075 77.405 44.394 1.00 29.70 C
ANISOU 2114 CG TRP A 733 2955 4516 3814 -440 918 -974 C
ATOM 2115 CD1 TRP A 733 65.116 77.021 45.319 1.00 31.70 C
ANISOU 2115 CD1 TRP A 733 3160 4845 4040 -561 1096 -1088 C
ATOM 2116 CD2 TRP A 733 67.329 76.946 44.917 1.00 28.37 C
ANISOU 2116 CD2 TRP A 733 2984 4309 3488 -483 898 -828 C
ATOM 2117 NE1 TRP A 733 65.701 76.266 46.307 1.00 32.61 N
ANISOU 2117 NE1 TRP A 733 3456 4958 3975 -684 1182 -1002 N
ATOM 2118 CE2 TRP A 733 67.050 76.204 46.088 1.00 30.77 C
ANISOU 2118 CE2 TRP A 733 3372 4655 3665 -629 1052 -843 C
ATOM 2119 CE3 TRP A 733 68.632 76.972 44.443 1.00 27.39 C
ANISOU 2119 CE3 TRP A 733 2969 4117 3322 -420 765 -688 C
ATOM 2120 CZ2 TRP A 733 68.053 75.548 46.811 1.00 31.15 C
ANISOU 2120 CZ2 TRP A 733 3622 4670 3543 -695 1050 -715 C
ATOM 2121 CZ3 TRP A 733 69.638 76.349 45.190 1.00 27.12 C
ANISOU 2121 CZ3 TRP A 733 3107 4062 3137 -481 769 -577 C
ATOM 2122 CH2 TRP A 733 69.329 75.609 46.324 1.00 28.55 C
ANISOU 2122 CH2 TRP A 733 3379 4276 3192 -611 899 -585 C
ATOM 2123 N GLY A 734 64.955 81.623 42.463 1.00 29.68 N
ANISOU 2123 N GLY A 734 2597 4413 4269 43 575 -1255 N
ATOM 2124 CA GLY A 734 64.987 82.713 41.471 1.00 30.21 C
ANISOU 2124 CA GLY A 734 2635 4395 4447 200 403 -1260 C
ATOM 2125 C GLY A 734 65.866 83.891 41.876 1.00 30.47 C
ANISOU 2125 C GLY A 734 2779 4357 4440 261 355 -1237 C
ATOM 2126 O GLY A 734 66.359 84.587 41.018 1.00 29.88 O
ANISOU 2126 O GLY A 734 2762 4191 4400 353 211 -1172 O
ATOM 2127 N GLU A 735 66.087 84.086 43.182 1.00 30.02 N
ANISOU 2127 N GLU A 735 2768 4339 4299 195 478 -1287 N
ATOM 2128 CA GLU A 735 66.905 85.192 43.657 1.00 30.26 C
ANISOU 2128 CA GLU A 735 2902 4306 4289 239 439 -1279 C
ATOM 2129 C GLU A 735 68.370 85.014 43.303 1.00 27.20 C
ANISOU 2129 C GLU A 735 2679 3863 3794 211 356 -1100 C
ATOM 2130 O GLU A 735 68.846 83.905 43.029 1.00 26.61 O
ANISOU 2130 O GLU A 735 2654 3811 3644 139 362 -983 O
ATOM 2131 CB GLU A 735 66.764 85.343 45.169 1.00 32.59 C
ANISOU 2131 CB GLU A 735 3212 4666 4502 161 596 -1383 C
ATOM 2132 CG GLU A 735 65.335 85.661 45.612 1.00 35.63 C
ANISOU 2132 CG GLU A 735 3422 5112 5003 187 701 -1592 C
ATOM 2133 CD GLU A 735 65.199 85.764 47.099 1.00 37.96 C
ANISOU 2133 CD GLU A 735 3746 5476 5199 93 875 -1699 C
ATOM 2134 OE1 GLU A 735 66.197 85.530 47.832 1.00 37.61 O
ANISOU 2134 OE1 GLU A 735 3870 5435 4985 4 905 -1603 O
ATOM 2135 OE2 GLU A 735 64.078 86.064 47.538 1.00 39.79 O
ANISOU 2135 OE2 GLU A 735 3833 5764 5524 106 982 -1887 O
ATOM 2136 N TYR A 736 69.108 86.103 43.357 1.00 27.13 N
ANISOU 2136 N TYR A 736 2751 3778 3780 264 285 -1086 N
ATOM 2137 CA TYR A 736 70.545 86.045 43.131 1.00 25.65 C
ANISOU 2137 CA TYR A 736 2703 3545 3499 229 218 -940 C
ATOM 2138 C TYR A 736 71.287 86.003 44.457 1.00 26.03 C
ANISOU 2138 C TYR A 736 2840 3634 3416 144 295 -939 C
ATOM 2139 O TYR A 736 71.255 86.965 45.243 1.00 26.15 O
ANISOU 2139 O TYR A 736 2872 3635 3428 160 321 -1034 O
ATOM 2140 CB TYR A 736 70.998 87.296 42.372 1.00 25.45 C
ANISOU 2140 CB TYR A 736 2728 3404 3540 320 92 -923 C
ATOM 2141 CG TYR A 736 72.448 87.378 42.059 1.00 24.51 C
ANISOU 2141 CG TYR A 736 2732 3236 3344 279 31 -795 C
ATOM 2142 CD1 TYR A 736 73.139 86.310 41.526 1.00 23.73 C
ANISOU 2142 CD1 TYR A 736 2667 3164 3186 223 19 -671 C
ATOM 2143 CD2 TYR A 736 73.125 88.574 42.234 1.00 25.58 C
ANISOU 2143 CD2 TYR A 736 2946 3293 3481 300 -17 -809 C
ATOM 2144 CE1 TYR A 736 74.515 86.422 41.231 1.00 22.62 C
ANISOU 2144 CE1 TYR A 736 2619 2985 2990 187 -32 -572 C
ATOM 2145 CE2 TYR A 736 74.464 88.717 41.889 1.00 24.87 C
ANISOU 2145 CE2 TYR A 736 2954 3160 3335 254 -70 -706 C
ATOM 2146 CZ TYR A 736 75.147 87.649 41.368 1.00 24.55 C
ANISOU 2146 CZ TYR A 736 2928 3158 3242 201 -76 -592 C
ATOM 2147 OH TYR A 736 76.490 87.773 41.019 1.00 23.47 O
ANISOU 2147 OH TYR A 736 2866 2988 3063 153 -118 -507 O
ATOM 2148 N HIS A 737 72.002 84.911 44.665 1.00 25.02 N
ANISOU 2148 N HIS A 737 2778 3548 3179 59 316 -831 N
ATOM 2149 CA HIS A 737 72.834 84.719 45.888 1.00 26.12 C
ANISOU 2149 CA HIS A 737 3023 3724 3176 -23 360 -808 C
ATOM 2150 C HIS A 737 74.190 84.228 45.475 1.00 24.07 C
ANISOU 2150 C HIS A 737 2846 3440 2859 -44 273 -665 C
ATOM 2151 O HIS A 737 74.456 83.012 45.439 1.00 24.11 O
ANISOU 2151 O HIS A 737 2880 3477 2804 -93 286 -579 O
ATOM 2152 CB HIS A 737 72.166 83.735 46.850 1.00 27.60 C
ANISOU 2152 CB HIS A 737 3213 3998 3275 -114 491 -843 C
ATOM 2153 CG HIS A 737 70.920 84.265 47.466 1.00 28.96 C
ANISOU 2153 CG HIS A 737 3300 4211 3495 -111 602 -1009 C
ATOM 2154 ND1 HIS A 737 70.917 84.950 48.654 1.00 31.34 N
ANISOU 2154 ND1 HIS A 737 3648 4535 3726 -141 672 -1106 N
ATOM 2155 CD2 HIS A 737 69.634 84.258 47.032 1.00 30.39 C
ANISOU 2155 CD2 HIS A 737 3338 4414 3796 -75 653 -1109 C
ATOM 2156 CE1 HIS A 737 69.683 85.341 48.935 1.00 32.80 C
ANISOU 2156 CE1 HIS A 737 3722 4754 3988 -125 773 -1265 C
ATOM 2157 NE2 HIS A 737 68.886 84.911 47.975 1.00 32.24 N
ANISOU 2157 NE2 HIS A 737 3526 4686 4037 -84 762 -1270 N
ATOM 2158 N PRO A 738 75.073 85.149 45.080 1.00 23.77 N
ANISOU 2158 N PRO A 738 2843 3339 2850 -7 185 -641 N
ATOM 2159 CA PRO A 738 76.392 84.707 44.591 1.00 22.80 C
ANISOU 2159 CA PRO A 738 2774 3198 2693 -27 109 -522 C
ATOM 2160 C PRO A 738 77.271 84.050 45.655 1.00 22.25 C
ANISOU 2160 C PRO A 738 2779 3178 2496 -94 113 -479 C
ATOM 2161 O PRO A 738 78.311 83.458 45.325 1.00 21.91 O
ANISOU 2161 O PRO A 738 2763 3132 2430 -106 53 -388 O
ATOM 2162 CB PRO A 738 77.018 86.004 44.069 1.00 23.18 C
ANISOU 2162 CB PRO A 738 2840 3167 2799 10 34 -534 C
ATOM 2163 CG PRO A 738 76.345 87.059 44.862 1.00 24.19 C
ANISOU 2163 CG PRO A 738 2966 3283 2944 32 72 -657 C
ATOM 2164 CD PRO A 738 74.923 86.603 44.987 1.00 24.71 C
ANISOU 2164 CD PRO A 738 2954 3393 3043 53 151 -725 C
ATOM 2165 N TYR A 739 76.850 84.098 46.919 1.00 23.60 N
ANISOU 2165 N TYR A 739 2988 3396 2583 -136 182 -547 N
ATOM 2166 CA TYR A 739 77.494 83.299 47.953 1.00 23.82 C
ANISOU 2166 CA TYR A 739 3109 3471 2472 -202 182 -499 C
ATOM 2167 C TYR A 739 77.468 81.814 47.632 1.00 23.65 C
ANISOU 2167 C TYR A 739 3101 3465 2419 -224 189 -401 C
ATOM 2168 O TYR A 739 78.376 81.087 48.019 1.00 23.76 O
ANISOU 2168 O TYR A 739 3189 3486 2351 -247 133 -323 O
ATOM 2169 CB TYR A 739 76.830 83.542 49.298 1.00 25.77 C
ANISOU 2169 CB TYR A 739 3408 3765 2620 -255 275 -594 C
ATOM 2170 CG TYR A 739 77.599 82.932 50.450 1.00 26.97 C
ANISOU 2170 CG TYR A 739 3689 3953 2606 -322 251 -546 C
ATOM 2171 CD1 TYR A 739 78.856 83.457 50.830 1.00 28.16 C
ANISOU 2171 CD1 TYR A 739 3893 4093 2715 -319 142 -529 C
ATOM 2172 CD2 TYR A 739 77.056 81.911 51.226 1.00 27.76 C
ANISOU 2172 CD2 TYR A 739 3869 4095 2585 -395 333 -528 C
ATOM 2173 CE1 TYR A 739 79.534 82.937 51.947 1.00 29.59 C
ANISOU 2173 CE1 TYR A 739 4199 4306 2738 -373 98 -493 C
ATOM 2174 CE2 TYR A 739 77.750 81.405 52.333 1.00 29.94 C
ANISOU 2174 CE2 TYR A 739 4292 4393 2692 -454 294 -481 C
ATOM 2175 CZ TYR A 739 78.998 81.904 52.653 1.00 30.54 C
ANISOU 2175 CZ TYR A 739 4413 4459 2734 -434 165 -461 C
ATOM 2176 OH TYR A 739 79.703 81.394 53.745 1.00 33.19 O
ANISOU 2176 OH TYR A 739 4898 4814 2900 -482 101 -414 O
ATOM 2177 N SER A 740 76.520 81.346 46.811 1.00 21.89 N
ANISOU 2177 N SER A 740 2806 3238 2273 -208 239 -402 N
ATOM 2178 CA SER A 740 76.616 79.941 46.349 1.00 22.25 C
ANISOU 2178 CA SER A 740 2870 3284 2302 -228 234 -305 C
ATOM 2179 C SER A 740 77.872 79.608 45.602 1.00 20.13 C
ANISOU 2179 C SER A 740 2611 2979 2059 -192 128 -210 C
ATOM 2180 O SER A 740 78.439 78.533 45.748 1.00 21.51 O
ANISOU 2180 O SER A 740 2844 3152 2177 -209 99 -130 O
ATOM 2181 CB SER A 740 75.375 79.556 45.543 1.00 22.57 C
ANISOU 2181 CB SER A 740 2821 3327 2428 -222 299 -335 C
ATOM 2182 OG SER A 740 75.374 80.210 44.298 1.00 22.90 O
ANISOU 2182 OG SER A 740 2782 3327 2591 -149 238 -340 O
ATOM 2183 N ASN A 741 78.398 80.562 44.826 1.00 19.49 N
ANISOU 2183 N ASN A 741 2479 2864 2061 -143 68 -221 N
ATOM 2184 CA ASN A 741 79.648 80.353 44.134 1.00 19.46 C
ANISOU 2184 CA ASN A 741 2473 2834 2085 -120 -15 -151 C
ATOM 2185 C ASN A 741 80.828 80.210 45.132 1.00 19.95 C
ANISOU 2185 C ASN A 741 2598 2918 2064 -140 -78 -127 C
ATOM 2186 O ASN A 741 81.722 79.369 44.915 1.00 21.50 O
ANISOU 2186 O ASN A 741 2804 3110 2255 -128 -136 -60 O
ATOM 2187 CB ASN A 741 79.915 81.457 43.131 1.00 20.13 C
ANISOU 2187 CB ASN A 741 2508 2875 2264 -86 -50 -173 C
ATOM 2188 CG ASN A 741 78.916 81.487 41.985 1.00 20.13 C
ANISOU 2188 CG ASN A 741 2458 2847 2345 -55 -24 -180 C
ATOM 2189 OD1 ASN A 741 78.470 80.445 41.471 1.00 20.64 O
ANISOU 2189 OD1 ASN A 741 2506 2919 2417 -56 -2 -141 O
ATOM 2190 ND2 ASN A 741 78.621 82.685 41.523 1.00 20.56 N
ANISOU 2190 ND2 ASN A 741 2494 2857 2460 -25 -40 -228 N
ATOM 2191 N VAL A 742 80.766 80.974 46.203 1.00 20.51 N
ANISOU 2191 N VAL A 742 2710 3010 2072 -165 -70 -188 N
ATOM 2192 CA VAL A 742 81.756 80.895 47.272 1.00 22.68 C
ANISOU 2192 CA VAL A 742 3054 3309 2252 -187 -140 -177 C
ATOM 2193 C VAL A 742 81.719 79.520 47.912 1.00 22.84 C
ANISOU 2193 C VAL A 742 3162 3346 2172 -208 -145 -109 C
ATOM 2194 O VAL A 742 82.774 78.937 48.183 1.00 22.93 O
ANISOU 2194 O VAL A 742 3208 3356 2147 -192 -242 -54 O
ATOM 2195 CB VAL A 742 81.564 81.997 48.316 1.00 23.50 C
ANISOU 2195 CB VAL A 742 3199 3433 2297 -218 -121 -267 C
ATOM 2196 CG1 VAL A 742 82.576 81.841 49.469 1.00 24.82 C
ANISOU 2196 CG1 VAL A 742 3451 3629 2349 -245 -210 -255 C
ATOM 2197 CG2 VAL A 742 81.712 83.358 47.653 1.00 24.30 C
ANISOU 2197 CG2 VAL A 742 3233 3496 2502 -196 -131 -327 C
ATOM 2198 N LEU A 743 80.504 79.045 48.225 1.00 22.47 N
ANISOU 2198 N LEU A 743 3151 3310 2076 -246 -41 -120 N
ATOM 2199 CA LEU A 743 80.338 77.733 48.808 1.00 23.59 C
ANISOU 2199 CA LEU A 743 3398 3451 2113 -284 -29 -52 C
ATOM 2200 C LEU A 743 80.953 76.654 47.930 1.00 22.85 C
ANISOU 2200 C LEU A 743 3286 3318 2076 -239 -94 39 C
ATOM 2201 O LEU A 743 81.713 75.817 48.417 1.00 23.73 O
ANISOU 2201 O LEU A 743 3486 3413 2119 -230 -176 107 O
ATOM 2202 CB LEU A 743 78.861 77.458 49.080 1.00 24.33 C
ANISOU 2202 CB LEU A 743 3508 3564 2171 -348 116 -94 C
ATOM 2203 CG LEU A 743 78.237 78.236 50.193 1.00 25.37 C
ANISOU 2203 CG LEU A 743 3686 3739 2216 -405 197 -188 C
ATOM 2204 CD1 LEU A 743 76.704 78.131 50.143 1.00 26.11 C
ANISOU 2204 CD1 LEU A 743 3731 3858 2333 -456 355 -261 C
ATOM 2205 CD2 LEU A 743 78.713 77.738 51.543 1.00 27.42 C
ANISOU 2205 CD2 LEU A 743 4119 4010 2289 -465 167 -149 C
ATOM 2206 N TRP A 744 80.688 76.686 46.634 1.00 21.26 N
ANISOU 2206 N TRP A 744 2979 3098 2001 -204 -69 38 N
ATOM 2207 CA TRP A 744 81.317 75.674 45.772 1.00 21.54 C
ANISOU 2207 CA TRP A 744 2997 3095 2091 -162 -124 112 C
ATOM 2208 C TRP A 744 82.832 75.813 45.736 1.00 21.71 C
ANISOU 2208 C TRP A 744 2997 3112 2139 -111 -245 133 C
ATOM 2209 O TRP A 744 83.527 74.834 45.744 1.00 20.83 O
ANISOU 2209 O TRP A 744 2920 2976 2019 -78 -314 191 O
ATOM 2210 CB TRP A 744 80.696 75.612 44.359 1.00 22.31 C
ANISOU 2210 CB TRP A 744 3000 3174 2303 -144 -71 105 C
ATOM 2211 CG TRP A 744 79.357 75.007 44.377 1.00 21.61 C
ANISOU 2211 CG TRP A 744 2929 3087 2194 -193 28 97 C
ATOM 2212 CD1 TRP A 744 78.176 75.645 44.305 1.00 22.21 C
ANISOU 2212 CD1 TRP A 744 2952 3190 2299 -218 111 24 C
ATOM 2213 CD2 TRP A 744 79.069 73.640 44.590 1.00 22.49 C
ANISOU 2213 CD2 TRP A 744 3122 3173 2251 -228 53 155 C
ATOM 2214 NE1 TRP A 744 77.138 74.745 44.393 1.00 22.42 N
ANISOU 2214 NE1 TRP A 744 2999 3219 2301 -274 195 25 N
ATOM 2215 CE2 TRP A 744 77.669 73.511 44.627 1.00 22.52 C
ANISOU 2215 CE2 TRP A 744 3110 3197 2252 -290 165 109 C
ATOM 2216 CE3 TRP A 744 79.860 72.508 44.807 1.00 22.43 C
ANISOU 2216 CE3 TRP A 744 3204 3120 2197 -213 -13 236 C
ATOM 2217 CZ2 TRP A 744 77.051 72.309 44.844 1.00 24.28 C
ANISOU 2217 CZ2 TRP A 744 3406 3397 2423 -355 226 145 C
ATOM 2218 CZ3 TRP A 744 79.259 71.342 45.046 1.00 23.99 C
ANISOU 2218 CZ3 TRP A 744 3492 3283 2338 -265 35 279 C
ATOM 2219 CH2 TRP A 744 77.843 71.230 45.037 1.00 24.55 C
ANISOU 2219 CH2 TRP A 744 3548 3376 2404 -345 162 234 C
ATOM 2220 N LEU A 745 83.323 77.039 45.723 1.00 22.05 N
ANISOU 2220 N LEU A 745 2981 3178 2220 -104 -272 76 N
ATOM 2221 CA LEU A 745 84.784 77.240 45.701 1.00 22.03 C
ANISOU 2221 CA LEU A 745 2935 3180 2253 -68 -382 77 C
ATOM 2222 C LEU A 745 85.393 76.706 46.971 1.00 22.53 C
ANISOU 2222 C LEU A 745 3095 3255 2209 -64 -477 104 C
ATOM 2223 O LEU A 745 86.503 76.181 46.971 1.00 22.73 O
ANISOU 2223 O LEU A 745 3101 3275 2260 -16 -584 130 O
ATOM 2224 CB LEU A 745 85.103 78.709 45.450 1.00 22.22 C
ANISOU 2224 CB LEU A 745 2888 3218 2335 -83 -379 6 C
ATOM 2225 CG LEU A 745 84.842 79.194 44.031 1.00 22.26 C
ANISOU 2225 CG LEU A 745 2811 3197 2451 -77 -321 -7 C
ATOM 2226 CD1 LEU A 745 84.910 80.737 43.988 1.00 22.46 C
ANISOU 2226 CD1 LEU A 745 2810 3217 2508 -104 -310 -76 C
ATOM 2227 CD2 LEU A 745 85.885 78.563 43.065 1.00 22.11 C
ANISOU 2227 CD2 LEU A 745 2723 3167 2511 -45 -360 24 C
ATOM 2228 N HIS A 746 84.672 76.843 48.073 1.00 22.83 N
ANISOU 2228 N HIS A 746 3240 3309 2123 -115 -441 93 N
ATOM 2229 CA HIS A 746 85.137 76.271 49.366 1.00 24.65 C
ANISOU 2229 CA HIS A 746 3606 3544 2216 -121 -535 130 C
ATOM 2230 C HIS A 746 85.168 74.760 49.320 1.00 25.05 C
ANISOU 2230 C HIS A 746 3739 3545 2234 -94 -570 222 C
ATOM 2231 O HIS A 746 86.161 74.136 49.727 1.00 24.68 O
ANISOU 2231 O HIS A 746 3739 3478 2161 -41 -710 266 O
ATOM 2232 CB HIS A 746 84.279 76.803 50.520 1.00 26.36 C
ANISOU 2232 CB HIS A 746 3932 3790 2293 -198 -463 88 C
ATOM 2233 CG HIS A 746 84.780 76.412 51.871 1.00 27.58 C
ANISOU 2233 CG HIS A 746 4245 3950 2286 -217 -564 119 C
ATOM 2234 ND1 HIS A 746 84.152 75.474 52.651 1.00 29.26 N
ANISOU 2234 ND1 HIS A 746 4629 4140 2348 -268 -529 178 N
ATOM 2235 CD2 HIS A 746 85.869 76.819 52.577 1.00 28.34 C
ANISOU 2235 CD2 HIS A 746 4363 4068 2338 -195 -709 101 C
ATOM 2236 CE1 HIS A 746 84.813 75.314 53.779 1.00 30.74 C
ANISOU 2236 CE1 HIS A 746 4956 4330 2395 -273 -651 202 C
ATOM 2237 NE2 HIS A 746 85.876 76.101 53.747 1.00 30.90 N
ANISOU 2237 NE2 HIS A 746 4880 4380 2482 -223 -771 155 N
ATOM 2238 N TYR A 747 84.118 74.154 48.757 1.00 23.37 N
ANISOU 2238 N TYR A 747 3537 3306 2037 -122 -454 248 N
ATOM 2239 CA TYR A 747 84.100 72.709 48.565 1.00 23.35 C
ANISOU 2239 CA TYR A 747 3612 3241 2019 -101 -476 332 C
ATOM 2240 C TYR A 747 85.275 72.254 47.668 1.00 23.05 C
ANISOU 2240 C TYR A 747 3476 3174 2109 -2 -582 353 C
ATOM 2241 O TYR A 747 85.893 71.218 47.940 1.00 25.95 O
ANISOU 2241 O TYR A 747 3921 3489 2450 50 -685 415 O
ATOM 2242 CB TYR A 747 82.758 72.297 47.974 1.00 23.18 C
ANISOU 2242 CB TYR A 747 3588 3205 2016 -158 -325 334 C
ATOM 2243 CG TYR A 747 82.799 71.046 47.086 1.00 23.05 C
ANISOU 2243 CG TYR A 747 3571 3122 2066 -122 -331 396 C
ATOM 2244 CD1 TYR A 747 83.172 71.136 45.763 1.00 23.02 C
ANISOU 2244 CD1 TYR A 747 3425 3113 2208 -64 -336 376 C
ATOM 2245 CD2 TYR A 747 82.553 69.785 47.618 1.00 24.11 C
ANISOU 2245 CD2 TYR A 747 3865 3190 2104 -150 -338 471 C
ATOM 2246 CE1 TYR A 747 83.301 70.035 44.977 1.00 22.98 C
ANISOU 2246 CE1 TYR A 747 3422 3048 2261 -28 -345 420 C
ATOM 2247 CE2 TYR A 747 82.645 68.648 46.815 1.00 24.35 C
ANISOU 2247 CE2 TYR A 747 3902 3149 2200 -113 -350 521 C
ATOM 2248 CZ TYR A 747 83.020 68.767 45.501 1.00 24.39 C
ANISOU 2248 CZ TYR A 747 3753 3158 2358 -49 -354 491 C
ATOM 2249 OH TYR A 747 83.115 67.667 44.661 1.00 24.01 O
ANISOU 2249 OH TYR A 747 3708 3039 2375 -13 -359 527 O
ATOM 2250 N LEU A 748 85.594 73.042 46.644 1.00 23.00 N
ANISOU 2250 N LEU A 748 3308 3197 2234 22 -557 297 N
ATOM 2251 CA LEU A 748 86.683 72.653 45.732 1.00 22.89 C
ANISOU 2251 CA LEU A 748 3188 3165 2346 102 -629 298 C
ATOM 2252 C LEU A 748 88.031 72.786 46.381 1.00 25.04 C
ANISOU 2252 C LEU A 748 3439 3456 2621 158 -783 283 C
ATOM 2253 O LEU A 748 88.896 71.947 46.210 1.00 24.96 O
ANISOU 2253 O LEU A 748 3407 3412 2663 236 -880 304 O
ATOM 2254 CB LEU A 748 86.582 73.427 44.436 1.00 23.17 C
ANISOU 2254 CB LEU A 748 3081 3222 2501 92 -545 245 C
ATOM 2255 CG LEU A 748 85.418 73.066 43.530 1.00 22.31 C
ANISOU 2255 CG LEU A 748 2974 3087 2417 62 -426 261 C
ATOM 2256 CD1 LEU A 748 85.097 74.154 42.514 1.00 23.06 C
ANISOU 2256 CD1 LEU A 748 2967 3205 2589 38 -351 208 C
ATOM 2257 CD2 LEU A 748 85.699 71.729 42.843 1.00 22.75 C
ANISOU 2257 CD2 LEU A 748 3036 3088 2521 111 -444 306 C
ATOM 2258 N THR A 749 88.201 73.833 47.180 1.00 25.16 N
ANISOU 2258 N THR A 749 3458 3521 2580 121 -811 237 N
ATOM 2259 CA THR A 749 89.443 74.076 47.921 1.00 26.56 C
ANISOU 2259 CA THR A 749 3614 3727 2752 163 -969 210 C
ATOM 2260 C THR A 749 89.683 72.931 48.920 1.00 27.85 C
ANISOU 2260 C THR A 749 3934 3844 2805 210 -1099 284 C
ATOM 2261 O THR A 749 90.790 72.459 49.107 1.00 27.80 O
ANISOU 2261 O THR A 749 3896 3827 2840 295 -1254 286 O
ATOM 2262 CB THR A 749 89.361 75.425 48.660 1.00 26.22 C
ANISOU 2262 CB THR A 749 3575 3739 2647 97 -960 145 C
ATOM 2263 OG1 THR A 749 89.179 76.473 47.737 1.00 25.23 O
ANISOU 2263 OG1 THR A 749 3327 3636 2623 59 -855 83 O
ATOM 2264 CG2 THR A 749 90.666 75.710 49.452 1.00 28.04 C
ANISOU 2264 CG2 THR A 749 3778 4006 2871 133 -1136 106 C
ATOM 2265 N ASP A 750 88.591 72.488 49.542 1.00 27.60 N
ANISOU 2265 N ASP A 750 4074 3780 2631 151 -1030 343 N
ATOM 2266 CA ASP A 750 88.587 71.386 50.450 1.00 30.93 C
ANISOU 2266 CA ASP A 750 4690 4140 2923 170 -1124 428 C
ATOM 2267 C ASP A 750 89.043 70.099 49.744 1.00 30.92 C
ANISOU 2267 C ASP A 750 4675 4059 3013 264 -1187 483 C
ATOM 2268 O ASP A 750 89.847 69.361 50.266 1.00 32.14 O
ANISOU 2268 O ASP A 750 4904 4166 3143 346 -1355 524 O
ATOM 2269 CB ASP A 750 87.181 71.264 51.033 1.00 31.37 C
ANISOU 2269 CB ASP A 750 4910 4184 2826 57 -981 463 C
ATOM 2270 CG ASP A 750 87.084 70.246 52.094 1.00 34.07 C
ANISOU 2270 CG ASP A 750 5491 4457 2995 44 -1060 554 C
ATOM 2271 OD1 ASP A 750 87.527 70.557 53.232 1.00 38.96 O
ANISOU 2271 OD1 ASP A 750 6220 5096 3484 35 -1171 555 O
ATOM 2272 OD2 ASP A 750 86.598 69.151 51.826 1.00 34.42 O
ANISOU 2272 OD2 ASP A 750 5628 4425 3026 38 -1018 624 O
ATOM 2273 N LYS A 751 88.523 69.849 48.547 1.00 29.05 N
ANISOU 2273 N LYS A 751 4348 3806 2884 257 -1057 477 N
ATOM 2274 CA LYS A 751 88.992 68.692 47.771 1.00 29.58 C
ANISOU 2274 CA LYS A 751 4386 3798 3053 348 -1105 510 C
ATOM 2275 C LYS A 751 90.468 68.785 47.463 1.00 30.21 C
ANISOU 2275 C LYS A 751 4312 3899 3269 462 -1248 454 C
ATOM 2276 O LYS A 751 91.141 67.782 47.518 1.00 31.35 O
ANISOU 2276 O LYS A 751 4488 3975 3448 562 -1373 486 O
ATOM 2277 CB LYS A 751 88.224 68.509 46.465 1.00 28.30 C
ANISOU 2277 CB LYS A 751 4144 3625 2985 315 -943 497 C
ATOM 2278 CG LYS A 751 86.796 68.059 46.676 1.00 28.10 C
ANISOU 2278 CG LYS A 751 4262 3563 2851 216 -814 550 C
ATOM 2279 CD LYS A 751 86.725 66.570 46.937 1.00 30.54 C
ANISOU 2279 CD LYS A 751 4738 3759 3108 245 -868 637 C
ATOM 2280 CE LYS A 751 85.295 66.064 47.183 1.00 31.35 C
ANISOU 2280 CE LYS A 751 4988 3824 3100 124 -728 684 C
ATOM 2281 NZ LYS A 751 84.847 66.328 48.586 1.00 33.31 N
ANISOU 2281 NZ LYS A 751 5405 4087 3163 39 -727 714 N
ATOM 2282 N AMET A 752 90.929 69.994 47.106 0.50 28.92 N
ANISOU 2282 N AMET A 752 3977 3825 3186 440 -1221 366 N
ATOM 2283 N BMET A 752 90.975 69.958 47.160 0.50 30.42 N
ANISOU 2283 N BMET A 752 4172 4014 3373 445 -1232 367 N
ATOM 2284 CA AMET A 752 92.355 70.265 46.765 0.50 29.48 C
ANISOU 2284 CA AMET A 752 3865 3938 3401 524 -1332 286 C
ATOM 2285 CA BMET A 752 92.397 70.066 46.826 0.50 32.02 C
ANISOU 2285 CA BMET A 752 4202 4246 3718 538 -1350 296 C
ATOM 2286 C AMET A 752 93.289 69.915 47.942 0.50 31.83 C
ANISOU 2286 C AMET A 752 4224 4223 3647 606 -1556 299 C
ATOM 2287 C BMET A 752 93.314 69.836 47.992 0.50 33.31 C
ANISOU 2287 C BMET A 752 4420 4405 3830 613 -1567 303 C
ATOM 2288 O AMET A 752 94.372 69.334 47.735 0.50 33.00 O
ANISOU 2288 O AMET A 752 4275 4353 3910 723 -1688 267 O
ATOM 2289 O BMET A 752 94.419 69.288 47.832 0.50 34.11 O
ANISOU 2289 O BMET A 752 4425 4491 4044 729 -1706 270 O
ATOM 2290 CB AMET A 752 92.595 71.747 46.348 0.50 27.86 C
ANISOU 2290 CB AMET A 752 3499 3826 3261 454 -1254 192 C
ATOM 2291 CB BMET A 752 92.669 71.405 46.266 0.50 32.25 C
ANISOU 2291 CB BMET A 752 4060 4364 3829 478 -1269 203 C
ATOM 2292 CG AMET A 752 92.067 72.214 44.987 0.50 26.24 C
ANISOU 2292 CG AMET A 752 3193 3634 3143 395 -1072 160 C
ATOM 2293 CG BMET A 752 91.829 71.573 45.067 0.50 32.64 C
ANISOU 2293 CG BMET A 752 4067 4407 3928 419 -1083 201 C
ATOM 2294 SD AMET A 752 92.697 71.227 43.612 0.50 25.42 S
ANISOU 2294 SD AMET A 752 2964 3492 3200 477 -1047 138 S
ATOM 2295 SD BMET A 752 92.180 73.161 44.475 0.50 33.09 S
ANISOU 2295 SD BMET A 752 3962 4546 4063 345 -1003 103 S
ATOM 2296 CE AMET A 752 92.128 72.171 42.236 0.50 24.42 C
ANISOU 2296 CE AMET A 752 2748 3399 3132 380 -852 95 C
ATOM 2297 CE BMET A 752 91.347 73.023 42.897 0.50 31.45 C
ANISOU 2297 CE BMET A 752 3719 4311 3921 307 -820 112 C
ATOM 2298 N LEU A 753 92.869 70.246 49.173 1.00 32.74 N
ANISOU 2298 N LEU A 753 4504 4348 3589 550 -1604 338 N
ATOM 2299 CA LEU A 753 93.664 70.039 50.364 1.00 34.59 C
ANISOU 2299 CA LEU A 753 4825 4575 3744 614 -1824 352 C
ATOM 2300 C LEU A 753 93.568 68.647 50.917 1.00 36.45 C
ANISOU 2300 C LEU A 753 5267 4697 3887 686 -1941 460 C
ATOM 2301 O LEU A 753 94.456 68.219 51.682 1.00 37.28 O
ANISOU 2301 O LEU A 753 5426 4773 3966 784 -2167 474 O
ATOM 2302 CB LEU A 753 93.265 71.085 51.414 1.00 34.24 C
ANISOU 2302 CB LEU A 753 4876 4593 3542 509 -1814 338 C
ATOM 2303 CG LEU A 753 93.669 72.494 51.050 1.00 33.85 C
ANISOU 2303 CG LEU A 753 4630 4644 3589 457 -1758 223 C
ATOM 2304 CD1 LEU A 753 92.977 73.424 52.032 1.00 34.57 C
ANISOU 2304 CD1 LEU A 753 4848 4775 3511 345 -1710 214 C
ATOM 2305 CD2 LEU A 753 95.179 72.644 51.107 1.00 36.29 C
ANISOU 2305 CD2 LEU A 753 4771 4996 4022 547 -1946 142 C
ATOM 2306 N LYS A 754 92.509 67.917 50.575 1.00 36.48 N
ANISOU 2306 N LYS A 754 5398 4626 3836 639 -1805 537 N
ATOM 2307 CA LYS A 754 92.246 66.630 51.246 1.00 39.22 C
ANISOU 2307 CA LYS A 754 5997 4848 4056 674 -1899 654 C
ATOM 2308 C LYS A 754 92.235 65.382 50.370 1.00 39.86 C
ANISOU 2308 C LYS A 754 6080 4821 4243 754 -1885 694 C
ATOM 2309 O LYS A 754 92.539 64.293 50.847 1.00 42.75 O
ANISOU 2309 O LYS A 754 6611 5072 4562 839 -2036 770 O
ATOM 2310 CB LYS A 754 90.923 66.713 51.984 1.00 39.83 C
ANISOU 2310 CB LYS A 754 6298 4913 3921 524 -1764 722 C
ATOM 2311 CG LYS A 754 90.948 67.662 53.142 1.00 42.21 C
ANISOU 2311 CG LYS A 754 6677 5289 4071 455 -1813 700 C
ATOM 2312 CD LYS A 754 89.588 67.780 53.792 1.00 43.51 C
ANISOU 2312 CD LYS A 754 7041 5452 4039 296 -1644 746 C
ATOM 2313 CE LYS A 754 89.697 68.564 55.065 1.00 46.04 C
ANISOU 2313 CE LYS A 754 7476 5831 4185 236 -1714 727 C
ATOM 2314 NZ LYS A 754 88.513 69.414 55.302 1.00 45.76 N
ANISOU 2314 NZ LYS A 754 7466 5864 4056 83 -1494 684 N
ATOM 2315 N GLN A 755 91.858 65.515 49.115 1.00 38.82 N
ANISOU 2315 N GLN A 755 5789 4715 4244 726 -1711 646 N
ATOM 2316 CA GLN A 755 91.599 64.348 48.304 1.00 39.98 C
ANISOU 2316 CA GLN A 755 5968 4758 4463 771 -1664 684 C
ATOM 2317 C GLN A 755 92.484 64.276 47.064 1.00 39.66 C
ANISOU 2317 C GLN A 755 5680 4738 4649 875 -1665 591 C
ATOM 2318 O GLN A 755 92.257 63.407 46.243 1.00 41.30 O
ANISOU 2318 O GLN A 755 5893 4870 4930 905 -1603 603 O
ATOM 2319 CB GLN A 755 90.080 64.259 47.996 1.00 40.65 C
ANISOU 2319 CB GLN A 755 6156 4828 4462 624 -1443 729 C
ATOM 2320 CG GLN A 755 89.289 63.852 49.249 1.00 44.86 C
ANISOU 2320 CG GLN A 755 6974 5300 4771 535 -1453 831 C
ATOM 2321 CD GLN A 755 87.770 63.851 49.065 1.00 47.55 C
ANISOU 2321 CD GLN A 755 7394 5644 5028 375 -1230 855 C
ATOM 2322 OE1 GLN A 755 87.021 64.651 49.687 1.00 49.51 O
ANISOU 2322 OE1 GLN A 755 7687 5966 5158 256 -1132 843 O
ATOM 2323 NE2 GLN A 755 87.298 62.963 48.218 1.00 47.88 N
ANISOU 2323 NE2 GLN A 755 7447 5609 5136 371 -1147 877 N
ATOM 2324 N MET A 756 93.498 65.147 46.926 1.00 38.04 N
ANISOU 2324 N MET A 756 5265 4633 4554 921 -1728 490 N
ATOM 2325 CA MET A 756 94.413 65.094 45.789 1.00 39.15 C
ANISOU 2325 CA MET A 756 5166 4802 4906 1008 -1719 387 C
ATOM 2326 C MET A 756 95.758 64.570 46.168 1.00 40.81 C
ANISOU 2326 C MET A 756 5305 4984 5217 1173 -1946 345 C
ATOM 2327 O MET A 756 96.222 64.825 47.295 1.00 41.85 O
ANISOU 2327 O MET A 756 5498 5132 5271 1205 -2120 360 O
ATOM 2328 CB MET A 756 94.707 66.468 45.174 1.00 39.82 C
ANISOU 2328 CB MET A 756 5030 5024 5077 934 -1609 280 C
ATOM 2329 CG MET A 756 93.564 67.355 45.018 1.00 41.97 C
ANISOU 2329 CG MET A 756 5346 5345 5253 783 -1430 301 C
ATOM 2330 SD MET A 756 92.698 67.123 43.500 1.00 41.59 S
ANISOU 2330 SD MET A 756 5255 5278 5271 723 -1212 295 S
ATOM 2331 CE MET A 756 91.168 67.933 43.865 1.00 40.56 C
ANISOU 2331 CE MET A 756 5248 5179 4984 569 -1069 348 C
ATOM 2332 N THR A 757 96.394 63.886 45.214 1.00 41.24 N
ANISOU 2332 N THR A 757 5221 5002 5447 1278 -1946 280 N
ATOM 2333 CA ATHR A 757 97.777 63.390 45.348 0.50 43.71 C
ANISOU 2333 CA ATHR A 757 5402 5296 5909 1456 -2151 202 C
ATOM 2334 CA BTHR A 757 97.793 63.434 45.378 0.50 44.42 C
ANISOU 2334 CA BTHR A 757 5489 5390 5997 1454 -2154 201 C
ATOM 2335 C THR A 757 98.653 64.082 44.308 1.00 44.11 C
ANISOU 2335 C THR A 757 5135 5464 6161 1460 -2062 41 C
ATOM 2336 O THR A 757 98.485 63.853 43.102 1.00 45.80 O
ANISOU 2336 O THR A 757 5258 5673 6469 1440 -1894 -6 O
ATOM 2337 CB ATHR A 757 97.859 61.866 45.108 0.50 44.94 C
ANISOU 2337 CB ATHR A 757 5662 5293 6120 1594 -2231 245 C
ATOM 2338 CB BTHR A 757 97.971 61.892 45.373 0.50 46.68 C
ANISOU 2338 CB BTHR A 757 5898 5513 6326 1607 -2278 251 C
ATOM 2339 OG1ATHR A 757 96.899 61.183 45.930 0.50 44.65 O
ANISOU 2339 OG1ATHR A 757 5944 5134 5885 1556 -2269 402 O
ATOM 2340 OG1BTHR A 757 97.584 61.330 44.112 0.50 47.07 O
ANISOU 2340 OG1BTHR A 757 5900 5518 6467 1596 -2101 225 O
ATOM 2341 CG2ATHR A 757 99.265 61.348 45.389 0.50 47.42 C
ANISOU 2341 CG2ATHR A 757 5849 5580 6590 1798 -2474 163 C
ATOM 2342 CG2BTHR A 757 97.153 61.268 46.478 0.50 47.55 C
ANISOU 2342 CG2BTHR A 757 6343 5504 6220 1582 -2367 414 C
ATOM 2343 N PHE A 758 99.541 64.952 44.750 1.00 44.14 N
ANISOU 2343 N PHE A 758 4980 5575 6218 1468 -2159 -47 N
ATOM 2344 CA PHE A 758 100.379 65.683 43.831 1.00 43.31 C
ANISOU 2344 CA PHE A 758 4579 5584 6292 1444 -2061 -204 C
ATOM 2345 C PHE A 758 101.628 64.904 43.491 1.00 45.30 C
ANISOU 2345 C PHE A 758 4639 5818 6754 1621 -2187 -322 C
ATOM 2346 O PHE A 758 102.190 64.150 44.313 1.00 45.48 O
ANISOU 2346 O PHE A 758 4712 5771 6796 1779 -2431 -305 O
ATOM 2347 CB PHE A 758 100.694 67.064 44.392 1.00 42.58 C
ANISOU 2347 CB PHE A 758 4398 5618 6164 1344 -2079 -256 C
ATOM 2348 CG PHE A 758 99.483 67.856 44.667 1.00 42.00 C
ANISOU 2348 CG PHE A 758 4495 5560 5904 1181 -1947 -160 C
ATOM 2349 CD1 PHE A 758 98.764 68.423 43.612 1.00 39.53 C
ANISOU 2349 CD1 PHE A 758 4152 5277 5590 1052 -1702 -167 C
ATOM 2350 CD2 PHE A 758 99.016 68.019 45.952 1.00 42.82 C
ANISOU 2350 CD2 PHE A 758 4798 5644 5828 1158 -2063 -66 C
ATOM 2351 CE1 PHE A 758 97.612 69.138 43.844 1.00 38.78 C
ANISOU 2351 CE1 PHE A 758 4204 5191 5339 917 -1587 -88 C
ATOM 2352 CE2 PHE A 758 97.849 68.744 46.183 1.00 40.51 C
ANISOU 2352 CE2 PHE A 758 4651 5367 5374 1011 -1925 7 C
ATOM 2353 CZ PHE A 758 97.164 69.311 45.134 1.00 39.52 C
ANISOU 2353 CZ PHE A 758 4473 5272 5270 898 -1693 -9 C
ATOM 2354 N LYS A 759 102.076 65.075 42.256 1.00 45.06 N
ANISOU 2354 N LYS A 759 4389 5846 6885 1597 -2022 -449 N
ATOM 2355 CA LYS A 759 103.312 64.434 41.812 1.00 49.05 C
ANISOU 2355 CA LYS A 759 4665 6354 7617 1755 -2107 -598 C
ATOM 2356 C LYS A 759 104.500 64.938 42.600 1.00 48.80 C
ANISOU 2356 C LYS A 759 4446 6412 7684 1826 -2310 -705 C
ATOM 2357 O LYS A 759 105.372 64.182 42.921 1.00 51.35 O
ANISOU 2357 O LYS A 759 4678 6695 8137 2010 -2511 -771 O
ATOM 2358 CB LYS A 759 103.548 64.687 40.337 1.00 50.90 C
ANISOU 2358 CB LYS A 759 4700 6655 7985 1679 -1859 -725 C
ATOM 2359 CG LYS A 759 102.434 64.150 39.456 1.00 52.18 C
ANISOU 2359 CG LYS A 759 5031 6732 8063 1616 -1668 -637 C
ATOM 2360 CD LYS A 759 102.772 62.802 38.841 1.00 57.83 C
ANISOU 2360 CD LYS A 759 5718 7345 8910 1771 -1687 -689 C
ATOM 2361 CE LYS A 759 101.598 62.301 38.010 1.00 58.79 C
ANISOU 2361 CE LYS A 759 6021 7385 8933 1692 -1503 -599 C
ATOM 2362 NZ LYS A 759 101.193 63.285 36.964 1.00 60.39 N
ANISOU 2362 NZ LYS A 759 6156 7687 9102 1502 -1247 -638 N
ATOM 2363 N THR A 760 104.535 66.236 42.854 1.00 47.41 N
ANISOU 2363 N THR A 760 4204 6355 7455 1678 -2254 -733 N
ATOM 2364 CA THR A 760 105.537 66.844 43.683 1.00 50.29 C
ANISOU 2364 CA THR A 760 4412 6810 7885 1713 -2443 -828 C
ATOM 2365 C THR A 760 104.889 67.187 44.994 1.00 49.48 C
ANISOU 2365 C THR A 760 4559 6681 7560 1673 -2583 -684 C
ATOM 2366 O THR A 760 103.881 67.883 45.055 1.00 46.85 O
ANISOU 2366 O THR A 760 4385 6358 7058 1513 -2437 -588 O
ATOM 2367 CB THR A 760 106.102 68.113 43.022 1.00 51.56 C
ANISOU 2367 CB THR A 760 4319 7123 8149 1556 -2270 -979 C
ATOM 2368 OG1 THR A 760 106.632 67.741 41.754 1.00 54.87 O
ANISOU 2368 OG1 THR A 760 4531 7563 8756 1577 -2111 -1110 O
ATOM 2369 CG2 THR A 760 107.206 68.756 43.840 1.00 54.29 C
ANISOU 2369 CG2 THR A 760 4474 7571 8582 1582 -2463 -1099 C
ATOM 2370 N LYS A 761 105.482 66.700 46.062 1.00 51.62 N
ANISOU 2370 N LYS A 761 4867 6918 7830 1822 -2876 -675 N
ATOM 2371 CA LYS A 761 105.051 67.133 47.373 1.00 53.25 C
ANISOU 2371 CA LYS A 761 5289 7117 7824 1776 -3022 -565 C
ATOM 2372 C LYS A 761 105.508 68.564 47.648 1.00 54.24 C
ANISOU 2372 C LYS A 761 5256 7393 7962 1642 -3000 -668 C
ATOM 2373 O LYS A 761 106.357 69.139 46.954 1.00 55.08 O
ANISOU 2373 O LYS A 761 5066 7604 8256 1607 -2921 -834 O
ATOM 2374 CB LYS A 761 105.572 66.199 48.461 1.00 55.29 C
ANISOU 2374 CB LYS A 761 5661 7288 8060 1974 -3362 -519 C
ATOM 2375 CG LYS A 761 105.309 64.721 48.199 1.00 56.45 C
ANISOU 2375 CG LYS A 761 5953 7270 8225 2128 -3415 -435 C
ATOM 2376 CD LYS A 761 103.895 64.413 47.797 1.00 55.04 C
ANISOU 2376 CD LYS A 761 6027 7004 7883 2012 -3189 -282 C
ATOM 2377 CE LYS A 761 103.782 62.950 47.484 1.00 56.58 C
ANISOU 2377 CE LYS A 761 6338 7034 8124 2165 -3247 -223 C
ATOM 2378 NZ LYS A 761 102.490 62.664 46.853 1.00 55.29 N
ANISOU 2378 NZ LYS A 761 6359 6803 7848 2044 -2999 -112 N
ATOM 2379 N CYS A 762 104.932 69.096 48.710 1.00 55.20 N
ANISOU 2379 N CYS A 762 5589 7514 7871 1563 -3072 -569 N
ATOM 2380 CA ACYS A 762 105.193 70.467 49.145 0.50 55.40 C
ANISOU 2380 CA ACYS A 762 5526 7660 7865 1425 -3061 -645 C
ATOM 2381 CA BCYS A 762 105.162 70.456 49.168 0.50 55.38 C
ANISOU 2381 CA BCYS A 762 5533 7655 7855 1425 -3062 -640 C
ATOM 2382 C CYS A 762 106.369 70.497 50.130 1.00 57.15 C
ANISOU 2382 C CYS A 762 5635 7933 8147 1537 -3376 -737 C
ATOM 2383 O CYS A 762 106.263 70.984 51.244 1.00 58.36 O
ANISOU 2383 O CYS A 762 5928 8104 8141 1497 -3517 -697 O
ATOM 2384 CB ACYS A 762 103.905 71.074 49.740 0.50 54.59 C
ANISOU 2384 CB ACYS A 762 5707 7533 7503 1276 -2954 -507 C
ATOM 2385 CB BCYS A 762 103.837 70.946 49.812 0.50 54.56 C
ANISOU 2385 CB BCYS A 762 5733 7515 7482 1288 -2968 -490 C
ATOM 2386 SG ACYS A 762 103.423 70.430 51.366 0.50 57.52 S
ANISOU 2386 SG ACYS A 762 6429 7811 7614 1348 -3209 -350 S
ATOM 2387 SG BCYS A 762 103.844 72.518 50.701 0.50 56.29 S
ANISOU 2387 SG BCYS A 762 5966 7842 7582 1125 -2984 -538 S
ATOM 2388 N ASN A 763 107.523 69.971 49.697 1.00 57.51 N
ANISOU 2388 N ASN A 763 5414 8005 8433 1681 -3489 -875 N
ATOM 2389 CA ASN A 763 108.730 69.892 50.539 1.00 58.73 C
ANISOU 2389 CA ASN A 763 5420 8209 8685 1815 -3812 -984 C
ATOM 2390 C ASN A 763 109.813 70.894 50.233 1.00 58.69 C
ANISOU 2390 C ASN A 763 5059 8363 8878 1739 -3790 -1200 C
ATOM 2391 O ASN A 763 110.965 70.657 50.572 1.00 58.74 O
ANISOU 2391 O ASN A 763 4851 8419 9049 1874 -4030 -1334 O
ATOM 2392 CB ASN A 763 109.333 68.492 50.446 1.00 61.95 C
ANISOU 2392 CB ASN A 763 5779 8524 9235 2064 -4013 -999 C
ATOM 2393 CG ASN A 763 108.367 67.432 50.888 1.00 62.48 C
ANISOU 2393 CG ASN A 763 6217 8420 9103 2144 -4076 -786 C
ATOM 2394 OD1 ASN A 763 107.476 67.704 51.713 1.00 63.74 O
ANISOU 2394 OD1 ASN A 763 6676 8540 9001 2047 -4083 -636 O
ATOM 2395 ND2 ASN A 763 108.523 66.231 50.344 1.00 63.50 N
ANISOU 2395 ND2 ASN A 763 6331 8442 9353 2311 -4112 -778 N
ATOM 2396 N THR A 764 109.462 71.985 49.562 1.00 55.79 N
ANISOU 2396 N THR A 764 4623 8069 8504 1526 -3506 -1240 N
ATOM 2397 CA THR A 764 110.343 73.127 49.432 1.00 57.24 C
ANISOU 2397 CA THR A 764 4528 8397 8824 1404 -3470 -1425 C
ATOM 2398 C THR A 764 109.662 74.306 50.099 1.00 55.02 C
ANISOU 2398 C THR A 764 4430 8141 8332 1217 -3411 -1358 C
ATOM 2399 O THR A 764 108.435 74.297 50.225 1.00 53.90 O
ANISOU 2399 O THR A 764 4581 7919 7981 1157 -3295 -1188 O
ATOM 2400 CB THR A 764 110.609 73.457 47.962 1.00 57.61 C
ANISOU 2400 CB THR A 764 4330 8502 9059 1298 -3168 -1546 C
ATOM 2401 OG1 THR A 764 109.392 73.878 47.342 1.00 55.87 O
ANISOU 2401 OG1 THR A 764 4313 8230 8685 1143 -2883 -1418 O
ATOM 2402 CG2 THR A 764 111.203 72.234 47.240 1.00 59.51 C
ANISOU 2402 CG2 THR A 764 4399 8709 9504 1485 -3199 -1618 C
ATOM 2403 N PRO A 765 110.429 75.326 50.497 1.00 56.28 N
ANISOU 2403 N PRO A 765 4417 8413 8553 1120 -3479 -1500 N
ATOM 2404 CA PRO A 765 109.806 76.464 51.181 1.00 55.48 C
ANISOU 2404 CA PRO A 765 4497 8329 8253 948 -3432 -1447 C
ATOM 2405 C PRO A 765 108.779 77.186 50.294 1.00 53.47 C
ANISOU 2405 C PRO A 765 4347 8045 7923 764 -3082 -1379 C
ATOM 2406 O PRO A 765 107.624 77.468 50.736 1.00 52.09 O
ANISOU 2406 O PRO A 765 4460 7807 7524 696 -3012 -1234 O
ATOM 2407 CB PRO A 765 111.004 77.353 51.542 1.00 57.33 C
ANISOU 2407 CB PRO A 765 4464 8694 8626 881 -3555 -1648 C
ATOM 2408 CG PRO A 765 112.187 76.424 51.581 1.00 59.96 C
ANISOU 2408 CG PRO A 765 4547 9063 9171 1082 -3795 -1769 C
ATOM 2409 CD PRO A 765 111.912 75.376 50.561 1.00 58.97 C
ANISOU 2409 CD PRO A 765 4406 8863 9136 1189 -3657 -1715 C
ATOM 2410 N ALA A 766 109.120 77.364 49.020 1.00 53.48 N
ANISOU 2410 N ALA A 766 4135 8082 8103 697 -2863 -1473 N
ATOM 2411 CA ALA A 766 108.192 77.983 48.062 1.00 51.93 C
ANISOU 2411 CA ALA A 766 4038 7849 7845 536 -2544 -1408 C
ATOM 2412 C ALA A 766 106.826 77.272 47.962 1.00 48.87 C
ANISOU 2412 C ALA A 766 3942 7344 7282 588 -2461 -1207 C
ATOM 2413 O ALA A 766 105.713 77.908 47.973 1.00 44.78 O
ANISOU 2413 O ALA A 766 3634 6780 6599 472 -2312 -1104 O
ATOM 2414 CB ALA A 766 108.862 78.048 46.688 1.00 53.41 C
ANISOU 2414 CB ALA A 766 3960 8086 8248 478 -2344 -1540 C
ATOM 2415 N MET A 767 106.883 75.953 47.830 1.00 48.50 N
ANISOU 2415 N MET A 767 3907 7243 7279 762 -2552 -1159 N
ATOM 2416 CA MET A 767 105.669 75.174 47.749 1.00 47.99 C
ANISOU 2416 CA MET A 767 4104 7067 7063 812 -2485 -981 C
ATOM 2417 C MET A 767 104.927 75.176 49.081 1.00 47.69 C
ANISOU 2417 C MET A 767 4347 6981 6792 824 -2631 -852 C
ATOM 2418 O MET A 767 103.707 75.257 49.103 1.00 44.88 O
ANISOU 2418 O MET A 767 4218 6564 6271 758 -2500 -725 O
ATOM 2419 CB MET A 767 105.953 73.742 47.281 1.00 49.94 C
ANISOU 2419 CB MET A 767 4300 7254 7419 992 -2549 -968 C
ATOM 2420 CG MET A 767 104.743 73.071 46.616 1.00 49.70 C
ANISOU 2420 CG MET A 767 4470 7121 7293 992 -2374 -823 C
ATOM 2421 SD MET A 767 104.235 73.888 45.083 1.00 51.07 S
ANISOU 2421 SD MET A 767 4570 7320 7514 810 -2017 -855 S
ATOM 2422 CE MET A 767 105.609 73.543 43.974 1.00 50.99 C
ANISOU 2422 CE MET A 767 4212 7376 7784 862 -1968 -1046 C
ATOM 2423 N LYS A 768 105.650 75.048 50.190 1.00 50.80 N
ANISOU 2423 N LYS A 768 4729 7404 7168 909 -2905 -890 N
ATOM 2424 CA LYS A 768 105.045 75.214 51.531 1.00 52.26 C
ANISOU 2424 CA LYS A 768 5185 7559 7114 893 -3043 -787 C
ATOM 2425 C LYS A 768 104.218 76.479 51.658 1.00 49.31 C
ANISOU 2425 C LYS A 768 4922 7208 6606 702 -2861 -769 C
ATOM 2426 O LYS A 768 103.138 76.475 52.276 1.00 48.97 O
ANISOU 2426 O LYS A 768 5147 7108 6350 663 -2826 -646 O
ATOM 2427 CB LYS A 768 106.129 75.175 52.630 1.00 55.66 C
ANISOU 2427 CB LYS A 768 5545 8040 7562 984 -3366 -868 C
ATOM 2428 CG LYS A 768 106.198 73.848 53.357 1.00 59.07 C
ANISOU 2428 CG LYS A 768 6140 8385 7920 1175 -3620 -768 C
ATOM 2429 CD LYS A 768 107.548 73.659 54.079 1.00 63.25 C
ANISOU 2429 CD LYS A 768 6507 8969 8556 1308 -3956 -884 C
ATOM 2430 CE LYS A 768 108.512 72.762 53.292 1.00 65.19 C
ANISOU 2430 CE LYS A 768 6487 9213 9070 1479 -4032 -981 C
ATOM 2431 NZ LYS A 768 109.957 72.951 53.654 1.00 69.41 N
ANISOU 2431 NZ LYS A 768 6735 9847 9791 1566 -4288 -1165 N
ATOM 2432 N GLN A 769 104.793 77.567 51.135 1.00 49.66 N
ANISOU 2432 N GLN A 769 4756 7334 6779 584 -2758 -905 N
ATOM 2433 CA GLN A 769 104.180 78.893 51.173 1.00 48.40 C
ANISOU 2433 CA GLN A 769 4669 7192 6527 404 -2593 -915 C
ATOM 2434 C GLN A 769 102.850 78.882 50.418 1.00 44.16 C
ANISOU 2434 C GLN A 769 4288 6581 5910 345 -2341 -799 C
ATOM 2435 O GLN A 769 101.847 79.425 50.885 1.00 41.95 O
ANISOU 2435 O GLN A 769 4206 6268 5463 267 -2264 -730 O
ATOM 2436 CB GLN A 769 105.134 79.930 50.574 1.00 52.70 C
ANISOU 2436 CB GLN A 769 4949 7822 7251 290 -2520 -1084 C
ATOM 2437 CG GLN A 769 104.571 81.340 50.376 1.00 55.33 C
ANISOU 2437 CG GLN A 769 5344 8156 7524 100 -2327 -1104 C
ATOM 2438 CD GLN A 769 104.224 82.059 51.682 1.00 61.29 C
ANISOU 2438 CD GLN A 769 6274 8915 8098 44 -2436 -1094 C
ATOM 2439 OE1 GLN A 769 104.689 81.688 52.772 1.00 69.05 O
ANISOU 2439 OE1 GLN A 769 7292 9927 9018 124 -2678 -1106 O
ATOM 2440 NE2 GLN A 769 103.408 83.116 51.575 1.00 65.27 N
ANISOU 2440 NE2 GLN A 769 6896 9387 8517 -93 -2263 -1077 N
ATOM 2441 N ILE A 770 102.844 78.222 49.265 1.00 40.98 N
ANISOU 2441 N ILE A 770 3791 6152 5629 391 -2220 -786 N
ATOM 2442 CA ILE A 770 101.598 78.101 48.510 1.00 39.34 C
ANISOU 2442 CA ILE A 770 3723 5872 5350 348 -2003 -678 C
ATOM 2443 C ILE A 770 100.592 77.306 49.309 1.00 37.71 C
ANISOU 2443 C ILE A 770 3776 5594 4957 414 -2065 -534 C
ATOM 2444 O ILE A 770 99.436 77.680 49.380 1.00 35.84 O
ANISOU 2444 O ILE A 770 3706 5320 4590 339 -1935 -459 O
ATOM 2445 CB ILE A 770 101.798 77.454 47.137 1.00 38.94 C
ANISOU 2445 CB ILE A 770 3537 5806 5453 386 -1873 -693 C
ATOM 2446 CG1 ILE A 770 102.617 78.408 46.270 1.00 40.87 C
ANISOU 2446 CG1 ILE A 770 3557 6117 5854 274 -1755 -831 C
ATOM 2447 CG2 ILE A 770 100.446 77.152 46.503 1.00 37.70 C
ANISOU 2447 CG2 ILE A 770 3550 5570 5203 361 -1693 -570 C
ATOM 2448 CD1 ILE A 770 103.079 77.830 44.933 1.00 41.68 C
ANISOU 2448 CD1 ILE A 770 3493 6224 6121 301 -1632 -883 C
ATOM 2449 N LYS A 771 101.030 76.230 49.945 1.00 39.82 N
ANISOU 2449 N LYS A 771 4081 5838 5209 551 -2268 -499 N
ATOM 2450 CA LYS A 771 100.120 75.451 50.763 1.00 40.57 C
ANISOU 2450 CA LYS A 771 4445 5858 5113 599 -2328 -360 C
ATOM 2451 C LYS A 771 99.491 76.284 51.876 1.00 41.11 C
ANISOU 2451 C LYS A 771 4695 5941 4982 500 -2341 -335 C
ATOM 2452 O LYS A 771 98.269 76.235 52.087 1.00 39.61 O
ANISOU 2452 O LYS A 771 4706 5704 4641 446 -2222 -241 O
ATOM 2453 CB LYS A 771 100.833 74.283 51.411 1.00 45.26 C
ANISOU 2453 CB LYS A 771 5069 6417 5711 760 -2582 -333 C
ATOM 2454 CG LYS A 771 99.810 73.376 52.078 1.00 47.66 C
ANISOU 2454 CG LYS A 771 5673 6622 5813 791 -2607 -175 C
ATOM 2455 CD LYS A 771 100.397 72.105 52.612 1.00 52.65 C
ANISOU 2455 CD LYS A 771 6377 7186 6441 956 -2850 -125 C
ATOM 2456 CE LYS A 771 99.261 71.155 52.924 1.00 54.01 C
ANISOU 2456 CE LYS A 771 6841 7244 6436 960 -2803 35 C
ATOM 2457 NZ LYS A 771 99.761 69.932 53.547 1.00 58.02 N
ANISOU 2457 NZ LYS A 771 7472 7662 6910 1115 -3051 102 N
ATOM 2458 N ARG A 772 100.332 77.039 52.593 1.00 42.23 N
ANISOU 2458 N ARG A 772 4763 6154 5131 475 -2484 -431 N
ATOM 2459 CA ARG A 772 99.821 77.908 53.651 1.00 43.51 C
ANISOU 2459 CA ARG A 772 5089 6335 5108 376 -2495 -429 C
ATOM 2460 C ARG A 772 98.782 78.889 53.120 1.00 40.71 C
ANISOU 2460 C ARG A 772 4771 5972 4723 241 -2237 -429 C
ATOM 2461 O ARG A 772 97.774 79.150 53.785 1.00 39.62 O
ANISOU 2461 O ARG A 772 4835 5810 4408 181 -2172 -375 O
ATOM 2462 CB ARG A 772 100.957 78.687 54.361 1.00 47.35 C
ANISOU 2462 CB ARG A 772 5458 6903 5629 355 -2679 -556 C
ATOM 2463 CG ARG A 772 101.660 77.875 55.432 1.00 52.83 C
ANISOU 2463 CG ARG A 772 6225 7596 6251 475 -2978 -536 C
ATOM 2464 CD ARG A 772 102.595 78.748 56.277 1.00 57.98 C
ANISOU 2464 CD ARG A 772 6797 8333 6900 435 -3161 -660 C
ATOM 2465 NE ARG A 772 103.577 79.499 55.464 1.00 61.22 N
ANISOU 2465 NE ARG A 772 6893 8821 7548 389 -3119 -815 N
ATOM 2466 CZ ARG A 772 104.814 79.073 55.124 1.00 64.52 C
ANISOU 2466 CZ ARG A 772 7063 9286 8167 487 -3268 -910 C
ATOM 2467 NH1 ARG A 772 105.278 77.870 55.488 1.00 65.97 N
ANISOU 2467 NH1 ARG A 772 7266 9439 8361 659 -3493 -866 N
ATOM 2468 NH2 ARG A 772 105.598 79.857 54.380 1.00 65.26 N
ANISOU 2468 NH2 ARG A 772 6882 9454 8462 409 -3186 -1057 N
ATOM 2469 N LYS A 773 99.024 79.420 51.917 1.00 39.44 N
ANISOU 2469 N LYS A 773 4421 5830 4734 196 -2090 -493 N
ATOM 2470 CA LYS A 773 98.116 80.357 51.293 1.00 37.61 C
ANISOU 2470 CA LYS A 773 4218 5579 4494 83 -1865 -495 C
ATOM 2471 C LYS A 773 96.771 79.700 50.969 1.00 35.36 C
ANISOU 2471 C LYS A 773 4089 5225 4121 99 -1726 -375 C
ATOM 2472 O LYS A 773 95.722 80.322 51.140 1.00 33.72 O
ANISOU 2472 O LYS A 773 4001 4996 3816 26 -1601 -354 O
ATOM 2473 CB LYS A 773 98.749 81.010 50.040 1.00 39.61 C
ANISOU 2473 CB LYS A 773 4253 5857 4941 26 -1750 -584 C
ATOM 2474 CG LYS A 773 99.870 82.023 50.323 1.00 44.89 C
ANISOU 2474 CG LYS A 773 4772 6594 5691 -46 -1829 -721 C
ATOM 2475 CD LYS A 773 99.258 83.287 50.939 1.00 50.38 C
ANISOU 2475 CD LYS A 773 5590 7279 6272 -161 -1771 -747 C
ATOM 2476 CE LYS A 773 100.113 84.543 50.746 1.00 55.66 C
ANISOU 2476 CE LYS A 773 6115 7989 7046 -279 -1754 -882 C
ATOM 2477 NZ LYS A 773 99.603 85.712 51.562 1.00 57.82 N
ANISOU 2477 NZ LYS A 773 6523 8247 7198 -376 -1736 -918 N
ATOM 2478 N ILE A 774 96.807 78.450 50.470 1.00 33.38 N
ANISOU 2478 N ILE A 774 3827 4939 3918 196 -1745 -308 N
ATOM 2479 CA ILE A 774 95.569 77.747 50.154 1.00 31.73 C
ANISOU 2479 CA ILE A 774 3758 4664 3633 206 -1621 -201 C
ATOM 2480 C ILE A 774 94.812 77.397 51.447 1.00 32.29 C
ANISOU 2480 C ILE A 774 4065 4711 3493 200 -1679 -127 C
ATOM 2481 O ILE A 774 93.568 77.510 51.496 1.00 30.44 O
ANISOU 2481 O ILE A 774 3958 4448 3161 141 -1535 -79 O
ATOM 2482 CB ILE A 774 95.808 76.510 49.255 1.00 31.80 C
ANISOU 2482 CB ILE A 774 3701 4633 3749 302 -1620 -156 C
ATOM 2483 CG1 ILE A 774 96.379 77.001 47.913 1.00 32.13 C
ANISOU 2483 CG1 ILE A 774 3529 4703 3977 276 -1513 -236 C
ATOM 2484 CG2 ILE A 774 94.480 75.765 49.031 1.00 30.53 C
ANISOU 2484 CG2 ILE A 774 3699 4403 3497 299 -1499 -48 C
ATOM 2485 CD1 ILE A 774 96.891 75.893 47.026 1.00 32.68 C
ANISOU 2485 CD1 ILE A 774 3496 4748 4174 371 -1522 -229 C
ATOM 2486 N GLN A 775 95.534 76.968 52.465 1.00 33.48 N
ANISOU 2486 N GLN A 775 4276 4872 3573 257 -1884 -122 N
ATOM 2487 CA GLN A 775 94.922 76.759 53.769 1.00 35.98 C
ANISOU 2487 CA GLN A 775 4834 5170 3667 231 -1944 -61 C
ATOM 2488 C GLN A 775 94.265 78.004 54.361 1.00 36.08 C
ANISOU 2488 C GLN A 775 4919 5219 3570 111 -1844 -114 C
ATOM 2489 O GLN A 775 93.190 77.919 54.950 1.00 35.71 O
ANISOU 2489 O GLN A 775 5058 5149 3362 55 -1754 -65 O
ATOM 2490 CB GLN A 775 95.971 76.304 54.777 1.00 38.96 C
ANISOU 2490 CB GLN A 775 5257 5558 3988 308 -2212 -63 C
ATOM 2491 CG GLN A 775 96.320 74.867 54.540 1.00 40.03 C
ANISOU 2491 CG GLN A 775 5416 5627 4167 437 -2325 17 C
ATOM 2492 CD GLN A 775 97.508 74.433 55.330 1.00 42.70 C
ANISOU 2492 CD GLN A 775 5752 5972 4498 542 -2614 0 C
ATOM 2493 OE1 GLN A 775 98.393 75.221 55.684 1.00 44.25 O
ANISOU 2493 OE1 GLN A 775 5827 6244 4744 534 -2733 -103 O
ATOM 2494 NE2 GLN A 775 97.553 73.166 55.593 1.00 44.34 N
ANISOU 2494 NE2 GLN A 775 6096 6097 4655 644 -2738 97 N
ATOM 2495 N GLU A 776 94.915 79.152 54.186 1.00 37.72 N
ANISOU 2495 N GLU A 776 4978 5482 3874 66 -1852 -224 N
ATOM 2496 CA GLU A 776 94.377 80.451 54.608 1.00 39.50 C
ANISOU 2496 CA GLU A 776 5249 5732 4028 -43 -1753 -294 C
ATOM 2497 C GLU A 776 93.093 80.798 53.835 1.00 36.96 C
ANISOU 2497 C GLU A 776 4943 5374 3727 -95 -1515 -273 C
ATOM 2498 O GLU A 776 92.101 81.228 54.416 1.00 35.22 O
ANISOU 2498 O GLU A 776 4855 5147 3380 -157 -1417 -278 O
ATOM 2499 CB GLU A 776 95.465 81.527 54.442 1.00 45.84 C
ANISOU 2499 CB GLU A 776 5875 6587 4954 -79 -1818 -416 C
ATOM 2500 CG GLU A 776 95.031 82.975 54.620 1.00 50.61 C
ANISOU 2500 CG GLU A 776 6496 7201 5533 -190 -1706 -502 C
ATOM 2501 CD GLU A 776 96.219 83.906 54.864 1.00 56.84 C
ANISOU 2501 CD GLU A 776 7159 8042 6397 -235 -1821 -623 C
ATOM 2502 OE1 GLU A 776 96.051 84.928 55.580 1.00 58.96 O
ANISOU 2502 OE1 GLU A 776 7499 8322 6582 -317 -1813 -696 O
ATOM 2503 OE2 GLU A 776 97.337 83.609 54.367 1.00 65.54 O
ANISOU 2503 OE2 GLU A 776 8084 9174 7643 -192 -1920 -656 O
ATOM 2504 N PHE A 777 93.111 80.533 52.530 1.00 32.90 N
ANISOU 2504 N PHE A 777 4295 4838 3369 -63 -1428 -254 N
ATOM 2505 CA PHE A 777 91.930 80.658 51.673 1.00 30.67 C
ANISOU 2505 CA PHE A 777 4021 4516 3117 -91 -1231 -225 C
ATOM 2506 C PHE A 777 90.776 79.824 52.217 1.00 29.78 C
ANISOU 2506 C PHE A 777 4083 4373 2859 -90 -1173 -142 C
ATOM 2507 O PHE A 777 89.674 80.335 52.421 1.00 29.30 O
ANISOU 2507 O PHE A 777 4096 4305 2730 -148 -1042 -158 O
ATOM 2508 CB PHE A 777 92.317 80.197 50.278 1.00 29.75 C
ANISOU 2508 CB PHE A 777 3754 4380 3168 -45 -1190 -205 C
ATOM 2509 CG PHE A 777 91.324 80.528 49.167 1.00 27.71 C
ANISOU 2509 CG PHE A 777 3470 4085 2971 -76 -1007 -192 C
ATOM 2510 CD1 PHE A 777 90.994 81.831 48.854 1.00 26.47 C
ANISOU 2510 CD1 PHE A 777 3286 3924 2850 -142 -916 -256 C
ATOM 2511 CD2 PHE A 777 90.851 79.537 48.323 1.00 27.87 C
ANISOU 2511 CD2 PHE A 777 3485 4071 3033 -32 -944 -122 C
ATOM 2512 CE1 PHE A 777 90.164 82.146 47.807 1.00 25.91 C
ANISOU 2512 CE1 PHE A 777 3194 3812 2840 -158 -779 -244 C
ATOM 2513 CE2 PHE A 777 90.024 79.852 47.266 1.00 26.18 C
ANISOU 2513 CE2 PHE A 777 3241 3826 2878 -56 -801 -115 C
ATOM 2514 CZ PHE A 777 89.692 81.131 46.990 1.00 26.34 C
ANISOU 2514 CZ PHE A 777 3240 3841 2927 -114 -726 -173 C
ATOM 2515 N HIS A 778 91.032 78.550 52.442 1.00 31.01 N
ANISOU 2515 N HIS A 778 4302 4506 2972 -27 -1266 -62 N
ATOM 2516 CA HIS A 778 90.030 77.624 53.006 1.00 31.74 C
ANISOU 2516 CA HIS A 778 4581 4562 2917 -39 -1218 23 C
ATOM 2517 C HIS A 778 89.391 78.142 54.281 1.00 32.44 C
ANISOU 2517 C HIS A 778 4837 4673 2816 -119 -1191 -2 C
ATOM 2518 O HIS A 778 88.150 78.113 54.429 1.00 32.11 O
ANISOU 2518 O HIS A 778 4886 4620 2696 -180 -1036 10 O
ATOM 2519 CB HIS A 778 90.653 76.267 53.250 1.00 32.97 C
ANISOU 2519 CB HIS A 778 4804 4678 3043 44 -1368 108 C
ATOM 2520 CG HIS A 778 89.692 75.197 53.640 1.00 33.78 C
ANISOU 2520 CG HIS A 778 5099 4725 3011 25 -1311 205 C
ATOM 2521 ND1 HIS A 778 89.413 74.897 54.957 1.00 37.41 N
ANISOU 2521 ND1 HIS A 778 5781 5174 3258 -19 -1365 246 N
ATOM 2522 CD2 HIS A 778 89.053 74.266 52.907 1.00 34.25 C
ANISOU 2522 CD2 HIS A 778 5171 4730 3111 40 -1219 272 C
ATOM 2523 CE1 HIS A 778 88.588 73.871 55.010 1.00 36.47 C
ANISOU 2523 CE1 HIS A 778 5805 4995 3057 -42 -1291 333 C
ATOM 2524 NE2 HIS A 778 88.384 73.445 53.786 1.00 34.75 N
ANISOU 2524 NE2 HIS A 778 5459 4748 2995 -3 -1210 350 N
ATOM 2525 N ARG A 779 90.219 78.750 55.121 1.00 33.54 N
ANISOU 2525 N ARG A 779 4993 4851 2899 -128 -1325 -57 N
ATOM 2526 CA ARG A 779 89.790 79.219 56.411 1.00 35.21 C
ANISOU 2526 CA ARG A 779 5375 5086 2916 -204 -1322 -89 C
ATOM 2527 C ARG A 779 88.994 80.497 56.406 1.00 32.68 C
ANISOU 2527 C ARG A 779 5025 4790 2601 -284 -1160 -186 C
ATOM 2528 O ARG A 779 88.313 80.799 57.404 1.00 36.69 O
ANISOU 2528 O ARG A 779 5685 5313 2943 -356 -1099 -217 O
ATOM 2529 CB ARG A 779 91.057 79.367 57.335 1.00 38.10 C
ANISOU 2529 CB ARG A 779 5775 5486 3217 -180 -1556 -118 C
ATOM 2530 CG ARG A 779 90.810 79.869 58.714 1.00 42.75 C
ANISOU 2530 CG ARG A 779 6550 6104 3591 -259 -1583 -158 C
ATOM 2531 CD ARG A 779 92.070 79.934 59.555 1.00 46.13 C
ANISOU 2531 CD ARG A 779 7007 6563 3958 -227 -1836 -184 C
ATOM 2532 NE ARG A 779 92.804 81.186 59.287 1.00 47.96 N
ANISOU 2532 NE ARG A 779 7056 6843 4322 -247 -1867 -309 N
ATOM 2533 CZ ARG A 779 94.033 81.270 58.773 1.00 49.79 C
ANISOU 2533 CZ ARG A 779 7098 7098 4721 -185 -2012 -347 C
ATOM 2534 NH1 ARG A 779 94.749 80.180 58.481 1.00 51.16 N
ANISOU 2534 NH1 ARG A 779 7223 7254 4963 -79 -2157 -278 N
ATOM 2535 NH2 ARG A 779 94.571 82.459 58.581 1.00 51.62 N
ANISOU 2535 NH2 ARG A 779 7187 7369 5056 -232 -2011 -464 N
ATOM 2536 N THR A 780 89.192 81.334 55.418 1.00 30.03 N
ANISOU 2536 N THR A 780 4511 4457 2444 -274 -1106 -246 N
ATOM 2537 CA THR A 780 88.669 82.688 55.429 1.00 29.10 C
ANISOU 2537 CA THR A 780 4362 4347 2348 -335 -993 -349 C
ATOM 2538 C THR A 780 87.633 82.967 54.324 1.00 27.85 C
ANISOU 2538 C THR A 780 4120 4154 2310 -332 -813 -354 C
ATOM 2539 O THR A 780 86.848 83.919 54.408 1.00 27.76 O
ANISOU 2539 O THR A 780 4114 4135 2298 -372 -699 -431 O
ATOM 2540 CB THR A 780 89.798 83.702 55.237 1.00 29.69 C
ANISOU 2540 CB THR A 780 4314 4440 2528 -341 -1088 -432 C
ATOM 2541 OG1 THR A 780 90.540 83.404 54.041 1.00 28.45 O
ANISOU 2541 OG1 THR A 780 3991 4270 2547 -288 -1122 -402 O
ATOM 2542 CG2 THR A 780 90.724 83.781 56.444 1.00 32.18 C
ANISOU 2542 CG2 THR A 780 4706 4797 2722 -357 -1266 -466 C
ATOM 2543 N MET A 781 87.637 82.152 53.268 1.00 26.96 N
ANISOU 2543 N MET A 781 3926 4016 2302 -279 -796 -278 N
ATOM 2544 CA MET A 781 86.853 82.459 52.066 1.00 25.45 C
ANISOU 2544 CA MET A 781 3639 3791 2240 -269 -660 -284 C
ATOM 2545 C MET A 781 85.323 82.514 52.298 1.00 25.70 C
ANISOU 2545 C MET A 781 3739 3815 2210 -302 -506 -303 C
ATOM 2546 O MET A 781 84.611 83.254 51.639 1.00 25.17 O
ANISOU 2546 O MET A 781 3607 3725 2232 -301 -408 -351 O
ATOM 2547 CB MET A 781 87.205 81.487 50.926 1.00 25.61 C
ANISOU 2547 CB MET A 781 3573 3789 2370 -211 -680 -203 C
ATOM 2548 CG MET A 781 86.852 80.054 51.210 1.00 25.63 C
ANISOU 2548 CG MET A 781 3667 3781 2289 -189 -689 -112 C
ATOM 2549 SD MET A 781 87.628 78.914 50.013 1.00 26.03 S
ANISOU 2549 SD MET A 781 3617 3803 2470 -109 -750 -34 S
ATOM 2550 CE MET A 781 86.886 79.458 48.535 1.00 24.78 C
ANISOU 2550 CE MET A 781 3345 3620 2451 -115 -607 -56 C
ATOM 2551 N LEU A 782 84.842 81.778 53.267 1.00 27.21 N
ANISOU 2551 N LEU A 782 4065 4025 2249 -333 -488 -273 N
ATOM 2552 CA LEU A 782 83.405 81.793 53.559 1.00 27.65 C
ANISOU 2552 CA LEU A 782 4173 4085 2247 -378 -328 -309 C
ATOM 2553 C LEU A 782 82.961 83.100 54.179 1.00 27.79 C
ANISOU 2553 C LEU A 782 4205 4120 2236 -418 -262 -433 C
ATOM 2554 O LEU A 782 81.756 83.343 54.342 1.00 27.92 O
ANISOU 2554 O LEU A 782 4229 4143 2238 -447 -119 -495 O
ATOM 2555 CB LEU A 782 83.031 80.618 54.440 1.00 28.53 C
ANISOU 2555 CB LEU A 782 4442 4207 2189 -423 -312 -244 C
ATOM 2556 CG LEU A 782 83.111 79.249 53.761 1.00 29.17 C
ANISOU 2556 CG LEU A 782 4521 4255 2307 -386 -339 -127 C
ATOM 2557 CD1 LEU A 782 82.766 78.211 54.842 1.00 31.17 C
ANISOU 2557 CD1 LEU A 782 4975 4507 2364 -448 -327 -66 C
ATOM 2558 CD2 LEU A 782 82.210 79.137 52.569 1.00 27.75 C
ANISOU 2558 CD2 LEU A 782 4222 4056 2267 -367 -220 -130 C
ATOM 2559 N ASN A 783 83.911 83.981 54.503 1.00 26.95 N
ANISOU 2559 N ASN A 783 4090 4018 2133 -420 -361 -484 N
ATOM 2560 CA ASN A 783 83.536 85.341 54.872 1.00 28.52 C
ANISOU 2560 CA ASN A 783 4283 4212 2340 -448 -300 -610 C
ATOM 2561 C ASN A 783 83.397 86.344 53.737 1.00 27.66 C
ANISOU 2561 C ASN A 783 4043 4050 2415 -407 -265 -656 C
ATOM 2562 O ASN A 783 83.239 87.536 54.009 1.00 28.91 O
ANISOU 2562 O ASN A 783 4204 4188 2593 -422 -237 -761 O
ATOM 2563 CB ASN A 783 84.526 85.860 55.944 1.00 30.59 C
ANISOU 2563 CB ASN A 783 4629 4502 2493 -488 -417 -657 C
ATOM 2564 CG ASN A 783 84.352 85.154 57.247 1.00 33.26 C
ANISOU 2564 CG ASN A 783 5138 4883 2614 -542 -426 -639 C
ATOM 2565 OD1 ASN A 783 83.249 84.763 57.606 1.00 34.79 O
ANISOU 2565 OD1 ASN A 783 5402 5090 2728 -578 -291 -648 O
ATOM 2566 ND2 ASN A 783 85.432 85.007 57.995 1.00 34.82 N
ANISOU 2566 ND2 ASN A 783 5412 5106 2711 -556 -585 -621 N
ATOM 2567 N PHE A 784 83.488 85.870 52.485 1.00 26.30 N
ANISOU 2567 N PHE A 784 3775 3850 2369 -358 -274 -580 N
ATOM 2568 CA PHE A 784 83.380 86.694 51.296 1.00 25.33 C
ANISOU 2568 CA PHE A 784 3551 3667 2406 -322 -251 -602 C
ATOM 2569 C PHE A 784 81.991 86.484 50.674 1.00 26.34 C
ANISOU 2569 C PHE A 784 3641 3776 2592 -288 -135 -605 C
ATOM 2570 O PHE A 784 81.396 85.427 50.844 1.00 26.99 O
ANISOU 2570 O PHE A 784 3745 3892 2619 -293 -86 -559 O
ATOM 2571 CB PHE A 784 84.474 86.344 50.289 1.00 24.31 C
ANISOU 2571 CB PHE A 784 3344 3522 2369 -301 -337 -524 C
ATOM 2572 CG PHE A 784 85.851 86.788 50.712 1.00 24.97 C
ANISOU 2572 CG PHE A 784 3424 3622 2440 -333 -451 -548 C
ATOM 2573 CD1 PHE A 784 86.466 86.231 51.792 1.00 25.68 C
ANISOU 2573 CD1 PHE A 784 3578 3767 2412 -352 -537 -537 C
ATOM 2574 CD2 PHE A 784 86.521 87.751 50.000 1.00 25.20 C
ANISOU 2574 CD2 PHE A 784 3390 3608 2578 -349 -475 -583 C
ATOM 2575 CE1 PHE A 784 87.719 86.668 52.190 1.00 25.91 C
ANISOU 2575 CE1 PHE A 784 3587 3817 2440 -380 -655 -574 C
ATOM 2576 CE2 PHE A 784 87.758 88.188 50.363 1.00 26.14 C
ANISOU 2576 CE2 PHE A 784 3488 3747 2699 -391 -571 -620 C
ATOM 2577 CZ PHE A 784 88.357 87.656 51.483 1.00 26.18 C
ANISOU 2577 CZ PHE A 784 3537 3816 2593 -403 -666 -621 C
ATOM 2578 N SER A 785 81.522 87.475 49.946 1.00 26.16 N
ANISOU 2578 N SER A 785 3564 3694 2683 -255 -102 -659 N
ATOM 2579 CA ASER A 785 80.119 87.521 49.529 0.50 26.24 C
ANISOU 2579 CA ASER A 785 3531 3686 2754 -215 -5 -698 C
ATOM 2580 CA BSER A 785 80.125 87.540 49.503 0.50 26.79 C
ANISOU 2580 CA BSER A 785 3599 3754 2826 -213 -6 -698 C
ATOM 2581 C SER A 785 79.863 86.965 48.115 1.00 25.00 C
ANISOU 2581 C SER A 785 3298 3498 2702 -167 -11 -618 C
ATOM 2582 O SER A 785 78.722 86.729 47.757 1.00 25.72 O
ANISOU 2582 O SER A 785 3345 3589 2838 -135 55 -639 O
ATOM 2583 CB ASER A 785 79.597 88.956 49.643 0.50 27.41 C
ANISOU 2583 CB ASER A 785 3675 3777 2964 -189 25 -819 C
ATOM 2584 CB BSER A 785 79.653 88.989 49.539 0.50 28.55 C
ANISOU 2584 CB BSER A 785 3816 3915 3118 -187 18 -813 C
ATOM 2585 OG ASER A 785 80.246 89.803 48.722 0.50 27.30 O
ANISOU 2585 OG ASER A 785 3642 3680 3048 -167 -45 -802 O
ATOM 2586 OG BSER A 785 79.536 89.397 50.869 0.50 31.69 O
ANISOU 2586 OG BSER A 785 4280 4348 3413 -229 57 -908 O
ATOM 2587 N SER A 786 80.919 86.743 47.331 1.00 23.61 N
ANISOU 2587 N SER A 786 3106 3302 2564 -167 -88 -536 N
ATOM 2588 CA SER A 786 80.802 86.354 45.938 1.00 23.38 C
ANISOU 2588 CA SER A 786 3021 3237 2626 -130 -97 -467 C
ATOM 2589 C SER A 786 82.165 85.963 45.411 1.00 22.27 C
ANISOU 2589 C SER A 786 2869 3098 2496 -150 -168 -392 C
ATOM 2590 O SER A 786 83.187 86.292 46.001 1.00 21.87 O
ANISOU 2590 O SER A 786 2837 3062 2411 -185 -221 -407 O
ATOM 2591 CB SER A 786 80.265 87.507 45.084 1.00 23.07 C
ANISOU 2591 CB SER A 786 2961 3113 2689 -87 -96 -512 C
ATOM 2592 OG SER A 786 81.192 88.619 45.097 1.00 23.52 O
ANISOU 2592 OG SER A 786 3052 3118 2765 -114 -145 -539 O
ATOM 2593 N ALA A 787 82.190 85.340 44.243 1.00 21.92 N
ANISOU 2593 N ALA A 787 2784 3035 2508 -128 -170 -324 N
ATOM 2594 CA ALA A 787 83.460 85.068 43.571 1.00 21.54 C
ANISOU 2594 CA ALA A 787 2708 2984 2490 -146 -221 -271 C
ATOM 2595 C ALA A 787 84.187 86.359 43.200 1.00 21.61 C
ANISOU 2595 C ALA A 787 2722 2941 2550 -179 -246 -309 C
ATOM 2596 O ALA A 787 85.424 86.414 43.247 1.00 21.83 O
ANISOU 2596 O ALA A 787 2725 2985 2583 -218 -288 -307 O
ATOM 2597 CB ALA A 787 83.280 84.198 42.331 1.00 21.79 C
ANISOU 2597 CB ALA A 787 2707 3004 2570 -121 -204 -202 C
ATOM 2598 N THR A 788 83.425 87.364 42.829 1.00 21.23 N
ANISOU 2598 N THR A 788 2702 2824 2541 -163 -223 -347 N
ATOM 2599 CA THR A 788 83.960 88.672 42.518 1.00 23.04 C
ANISOU 2599 CA THR A 788 2963 2980 2811 -199 -242 -383 C
ATOM 2600 C THR A 788 84.725 89.254 43.727 1.00 23.74 C
ANISOU 2600 C THR A 788 3067 3096 2856 -248 -272 -449 C
ATOM 2601 O THR A 788 85.855 89.761 43.579 1.00 24.66 O
ANISOU 2601 O THR A 788 3176 3198 2994 -311 -302 -461 O
ATOM 2602 CB THR A 788 82.885 89.647 42.029 1.00 23.31 C
ANISOU 2602 CB THR A 788 3044 2920 2893 -155 -229 -416 C
ATOM 2603 OG1 THR A 788 82.175 89.093 40.892 1.00 22.23 O
ANISOU 2603 OG1 THR A 788 2894 2762 2792 -108 -220 -358 O
ATOM 2604 CG2 THR A 788 83.516 90.957 41.632 1.00 24.03 C
ANISOU 2604 CG2 THR A 788 3195 2916 3021 -202 -252 -441 C
ATOM 2605 N ASP A 789 84.129 89.143 44.917 1.00 23.97 N
ANISOU 2605 N ASP A 789 3118 3170 2821 -230 -261 -497 N
ATOM 2606 CA ASP A 789 84.767 89.658 46.171 1.00 25.73 C
ANISOU 2606 CA ASP A 789 3371 3424 2982 -277 -296 -566 C
ATOM 2607 C ASP A 789 86.053 88.850 46.388 1.00 25.13 C
ANISOU 2607 C ASP A 789 3252 3419 2878 -312 -360 -524 C
ATOM 2608 O ASP A 789 87.100 89.412 46.760 1.00 25.74 O
ANISOU 2608 O ASP A 789 3321 3504 2956 -367 -414 -566 O
ATOM 2609 CB ASP A 789 83.721 89.481 47.310 1.00 27.70 C
ANISOU 2609 CB ASP A 789 3661 3714 3151 -252 -252 -618 C
ATOM 2610 CG ASP A 789 84.146 90.002 48.671 1.00 32.23 C
ANISOU 2610 CG ASP A 789 4288 4319 3637 -299 -279 -697 C
ATOM 2611 OD1 ASP A 789 85.035 90.897 48.746 1.00 36.13 O
ANISOU 2611 OD1 ASP A 789 4791 4781 4154 -346 -328 -740 O
ATOM 2612 OD2 ASP A 789 83.518 89.560 49.709 1.00 31.99 O
ANISOU 2612 OD2 ASP A 789 4301 4345 3507 -298 -243 -727 O
ATOM 2613 N LEU A 790 86.004 87.523 46.209 1.00 24.32 N
ANISOU 2613 N LEU A 790 3119 3367 2753 -279 -363 -449 N
ATOM 2614 CA LEU A 790 87.200 86.721 46.387 1.00 23.88 C
ANISOU 2614 CA LEU A 790 3018 3370 2686 -290 -437 -415 C
ATOM 2615 C LEU A 790 88.303 87.130 45.436 1.00 23.45 C
ANISOU 2615 C LEU A 790 2890 3293 2727 -329 -456 -419 C
ATOM 2616 O LEU A 790 89.478 87.292 45.833 1.00 24.08 O
ANISOU 2616 O LEU A 790 2924 3409 2816 -369 -525 -455 O
ATOM 2617 CB LEU A 790 86.905 85.223 46.226 1.00 24.01 C
ANISOU 2617 CB LEU A 790 3025 3422 2676 -241 -434 -334 C
ATOM 2618 CG LEU A 790 86.136 84.496 47.327 1.00 25.13 C
ANISOU 2618 CG LEU A 790 3246 3601 2703 -225 -425 -320 C
ATOM 2619 CD1 LEU A 790 85.751 83.127 46.801 1.00 25.26 C
ANISOU 2619 CD1 LEU A 790 3254 3623 2722 -185 -403 -236 C
ATOM 2620 CD2 LEU A 790 86.964 84.315 48.579 1.00 26.01 C
ANISOU 2620 CD2 LEU A 790 3400 3762 2721 -244 -522 -337 C
ATOM 2621 N LEU A 791 87.961 87.235 44.156 1.00 22.35 N
ANISOU 2621 N LEU A 791 2737 3099 2656 -323 -396 -383 N
ATOM 2622 CA LEU A 791 88.952 87.514 43.153 1.00 23.18 C
ANISOU 2622 CA LEU A 791 2784 3184 2839 -373 -390 -382 C
ATOM 2623 C LEU A 791 89.634 88.861 43.421 1.00 24.85 C
ANISOU 2623 C LEU A 791 3008 3362 3073 -455 -404 -459 C
ATOM 2624 O LEU A 791 90.874 88.983 43.312 1.00 24.79 O
ANISOU 2624 O LEU A 791 2926 3384 3109 -517 -431 -492 O
ATOM 2625 CB LEU A 791 88.335 87.519 41.762 1.00 22.87 C
ANISOU 2625 CB LEU A 791 2765 3081 2843 -362 -322 -331 C
ATOM 2626 CG LEU A 791 89.344 87.725 40.646 1.00 23.46 C
ANISOU 2626 CG LEU A 791 2796 3136 2983 -429 -293 -328 C
ATOM 2627 CD1 LEU A 791 90.204 86.496 40.436 1.00 23.76 C
ANISOU 2627 CD1 LEU A 791 2733 3250 3047 -413 -308 -308 C
ATOM 2628 CD2 LEU A 791 88.587 88.049 39.356 1.00 22.79 C
ANISOU 2628 CD2 LEU A 791 2779 2966 2914 -428 -235 -282 C
ATOM 2629 N CYS A 792 88.822 89.850 43.773 1.00 26.30 N
ANISOU 2629 N CYS A 792 3276 3482 3234 -456 -385 -495 N
ATOM 2630 CA CYS A 792 89.297 91.236 43.880 1.00 29.55 C
ANISOU 2630 CA CYS A 792 3725 3830 3672 -536 -388 -566 C
ATOM 2631 C CYS A 792 89.948 91.505 45.232 1.00 30.39 C
ANISOU 2631 C CYS A 792 3820 3995 3733 -572 -455 -643 C
ATOM 2632 O CYS A 792 90.770 92.423 45.330 1.00 31.60 O
ANISOU 2632 O CYS A 792 3968 4121 3916 -659 -472 -707 O
ATOM 2633 CB CYS A 792 88.169 92.244 43.636 1.00 30.80 C
ANISOU 2633 CB CYS A 792 3988 3877 3838 -511 -349 -582 C
ATOM 2634 SG CYS A 792 87.504 92.147 41.927 1.00 33.16 S
ANISOU 2634 SG CYS A 792 4322 4089 4188 -479 -296 -495 S
ATOM 2635 N GLN A 793 89.601 90.757 46.265 1.00 29.33 N
ANISOU 2635 N GLN A 793 3692 3934 3519 -517 -494 -640 N
ATOM 2636 CA GLN A 793 90.070 91.099 47.610 1.00 31.87 C
ANISOU 2636 CA GLN A 793 4034 4302 3773 -551 -564 -716 C
ATOM 2637 C GLN A 793 90.857 90.033 48.353 1.00 31.29 C
ANISOU 2637 C GLN A 793 3907 4334 3649 -533 -661 -700 C
ATOM 2638 O GLN A 793 91.542 90.354 49.301 1.00 31.33 O
ANISOU 2638 O GLN A 793 3914 4380 3610 -573 -742 -765 O
ATOM 2639 CB GLN A 793 88.898 91.535 48.467 1.00 35.22 C
ANISOU 2639 CB GLN A 793 4561 4703 4119 -520 -530 -757 C
ATOM 2640 CG GLN A 793 88.067 92.605 47.807 1.00 38.35 C
ANISOU 2640 CG GLN A 793 5011 4985 4575 -514 -456 -783 C
ATOM 2641 CD GLN A 793 87.585 93.590 48.805 1.00 46.58 C
ANISOU 2641 CD GLN A 793 6136 5993 5570 -527 -448 -884 C
ATOM 2642 OE1 GLN A 793 88.370 94.417 49.278 1.00 53.40 O
ANISOU 2642 OE1 GLN A 793 7017 6841 6431 -601 -490 -957 O
ATOM 2643 NE2 GLN A 793 86.301 93.506 49.175 1.00 50.64 N
ANISOU 2643 NE2 GLN A 793 6695 6500 6046 -461 -389 -902 N
ATOM 2644 N HIS A 794 90.770 88.776 47.960 1.00 27.70 N
ANISOU 2644 N HIS A 794 3413 3917 3196 -471 -664 -617 N
ATOM 2645 CA HIS A 794 91.397 87.769 48.757 1.00 27.29 C
ANISOU 2645 CA HIS A 794 3338 3945 3085 -438 -769 -598 C
ATOM 2646 C HIS A 794 92.889 87.784 48.526 1.00 28.92 C
ANISOU 2646 C HIS A 794 3418 4192 3377 -473 -852 -638 C
ATOM 2647 O HIS A 794 93.361 87.851 47.388 1.00 28.96 O
ANISOU 2647 O HIS A 794 3333 4179 3492 -496 -803 -633 O
ATOM 2648 CB HIS A 794 90.854 86.359 48.514 1.00 25.83 C
ANISOU 2648 CB HIS A 794 3164 3777 2872 -358 -756 -501 C
ATOM 2649 CG HIS A 794 91.146 85.446 49.658 1.00 26.61 C
ANISOU 2649 CG HIS A 794 3310 3934 2865 -322 -866 -479 C
ATOM 2650 ND1 HIS A 794 92.409 85.006 49.934 1.00 27.86 N
ANISOU 2650 ND1 HIS A 794 3394 4142 3050 -307 -999 -492 N
ATOM 2651 CD2 HIS A 794 90.370 84.986 50.660 1.00 26.71 C
ANISOU 2651 CD2 HIS A 794 3450 3960 2740 -305 -870 -453 C
ATOM 2652 CE1 HIS A 794 92.419 84.309 51.052 1.00 28.86 C
ANISOU 2652 CE1 HIS A 794 3610 4302 3055 -274 -1099 -466 C
ATOM 2653 NE2 HIS A 794 91.178 84.255 51.503 1.00 28.43 N
ANISOU 2653 NE2 HIS A 794 3688 4225 2890 -279 -1013 -437 N
ATOM 2654 N SER A 795 93.657 87.651 49.609 1.00 29.96 N
ANISOU 2654 N SER A 795 3541 4386 3455 -477 -983 -683 N
ATOM 2655 CA SER A 795 95.111 87.674 49.515 1.00 32.87 C
ANISOU 2655 CA SER A 795 3768 4807 3915 -508 -1080 -743 C
ATOM 2656 C SER A 795 95.722 86.515 48.638 1.00 32.65 C
ANISOU 2656 C SER A 795 3612 4808 3985 -444 -1095 -694 C
ATOM 2657 O SER A 795 96.825 86.652 48.137 1.00 32.99 O
ANISOU 2657 O SER A 795 3507 4884 4145 -480 -1119 -754 O
ATOM 2658 CB SER A 795 95.687 87.668 50.936 1.00 34.67 C
ANISOU 2658 CB SER A 795 4025 5096 4050 -508 -1241 -797 C
ATOM 2659 OG SER A 795 95.420 86.437 51.568 1.00 35.33 O
ANISOU 2659 OG SER A 795 4178 5209 4036 -414 -1324 -720 O
ATOM 2660 N LEU A 796 95.019 85.403 48.458 1.00 31.00 N
ANISOU 2660 N LEU A 796 3457 4587 3735 -356 -1075 -597 N
ATOM 2661 CA LEU A 796 95.501 84.307 47.627 1.00 32.15 C
ANISOU 2661 CA LEU A 796 3498 4748 3971 -291 -1081 -556 C
ATOM 2662 C LEU A 796 95.872 84.798 46.213 1.00 32.72 C
ANISOU 2662 C LEU A 796 3460 4798 4176 -353 -959 -587 C
ATOM 2663 O LEU A 796 96.833 84.298 45.628 1.00 32.75 O
ANISOU 2663 O LEU A 796 3320 4837 4287 -338 -980 -617 O
ATOM 2664 CB LEU A 796 94.479 83.192 47.485 1.00 31.14 C
ANISOU 2664 CB LEU A 796 3467 4587 3777 -209 -1041 -447 C
ATOM 2665 CG LEU A 796 94.960 81.949 46.728 1.00 30.98 C
ANISOU 2665 CG LEU A 796 3357 4574 3842 -131 -1059 -407 C
ATOM 2666 CD1 LEU A 796 96.210 81.377 47.346 1.00 32.77 C
ANISOU 2666 CD1 LEU A 796 3488 4854 4107 -74 -1231 -449 C
ATOM 2667 CD2 LEU A 796 93.860 80.921 46.686 1.00 29.91 C
ANISOU 2667 CD2 LEU A 796 3339 4397 3628 -68 -1017 -303 C
ATOM 2668 N PHE A 797 95.132 85.764 45.698 1.00 33.10 N
ANISOU 2668 N PHE A 797 3579 4785 4214 -421 -839 -584 N
ATOM 2669 CA PHE A 797 95.308 86.210 44.306 1.00 35.84 C
ANISOU 2669 CA PHE A 797 3870 5091 4655 -486 -716 -592 C
ATOM 2670 C PHE A 797 96.184 87.437 44.125 1.00 41.52 C
ANISOU 2670 C PHE A 797 4527 5807 5442 -611 -693 -688 C
ATOM 2671 O PHE A 797 96.400 87.881 43.000 1.00 45.85 O
ANISOU 2671 O PHE A 797 5048 6317 6056 -686 -586 -698 O
ATOM 2672 CB PHE A 797 93.946 86.405 43.682 1.00 33.26 C
ANISOU 2672 CB PHE A 797 3669 4686 4283 -474 -607 -519 C
ATOM 2673 CG PHE A 797 93.060 85.211 43.844 1.00 29.82 C
ANISOU 2673 CG PHE A 797 3289 4255 3786 -371 -617 -434 C
ATOM 2674 CD1 PHE A 797 93.467 83.942 43.413 1.00 29.76 C
ANISOU 2674 CD1 PHE A 797 3209 4279 3819 -306 -638 -397 C
ATOM 2675 CD2 PHE A 797 91.852 85.337 44.495 1.00 30.35 C
ANISOU 2675 CD2 PHE A 797 3479 4295 3759 -342 -605 -402 C
ATOM 2676 CE1 PHE A 797 92.663 82.827 43.599 1.00 27.80 C
ANISOU 2676 CE1 PHE A 797 3025 4025 3512 -222 -648 -319 C
ATOM 2677 CE2 PHE A 797 91.015 84.257 44.647 1.00 27.72 C
ANISOU 2677 CE2 PHE A 797 3199 3965 3369 -268 -600 -330 C
ATOM 2678 CZ PHE A 797 91.417 82.995 44.229 1.00 28.70 C
ANISOU 2678 CZ PHE A 797 3267 4113 3527 -211 -625 -284 C
ATOM 2679 N LYS A 798 96.713 87.961 45.213 1.00 44.04 N
ANISOU 2679 N LYS A 798 4832 6164 5739 -643 -792 -761 N
ATOM 2680 CA LYS A 798 97.517 89.162 45.153 1.00 49.53 C
ANISOU 2680 CA LYS A 798 5475 6851 6493 -774 -775 -862 C
ATOM 2681 C LYS A 798 98.976 88.803 44.953 1.00 54.48 C
ANISOU 2681 C LYS A 798 5899 7563 7237 -806 -825 -945 C
ATOM 2682 O LYS A 798 99.410 87.645 45.122 1.00 55.68 O
ANISOU 2682 O LYS A 798 5954 7783 7417 -707 -910 -934 O
ATOM 2683 CB LYS A 798 97.329 89.984 46.422 1.00 49.48 C
ANISOU 2683 CB LYS A 798 5556 6839 6404 -803 -854 -914 C
ATOM 2684 CG LYS A 798 95.958 90.594 46.411 1.00 49.13 C
ANISOU 2684 CG LYS A 798 5688 6700 6278 -793 -772 -862 C
ATOM 2685 CD LYS A 798 95.651 91.363 47.663 1.00 51.01 C
ANISOU 2685 CD LYS A 798 6026 6929 6427 -814 -833 -919 C
ATOM 2686 CE LYS A 798 94.181 91.658 47.694 1.00 50.84 C
ANISOU 2686 CE LYS A 798 6157 6828 6331 -767 -756 -869 C
ATOM 2687 NZ LYS A 798 93.604 92.049 46.375 1.00 49.69 N
ANISOU 2687 NZ LYS A 798 6047 6587 6246 -781 -633 -819 N
ATOM 2688 OXT LYS A 798 99.745 89.703 44.607 1.00 61.12 O
ANISOU 2688 OXT LYS A 798 6669 8402 8153 -936 -777 -1033 O
TER 2689 LYS A 798
HETATM 2690 N1 S1Z A 801 76.807 68.148 31.427 1.00 20.93 N
HETATM 2691 C7 S1Z A 801 77.532 67.166 31.956 1.00 19.90 C
HETATM 2692 C8 S1Z A 801 77.608 68.704 30.475 1.00 19.85 C
HETATM 2693 N2 S1Z A 801 83.974 68.310 27.236 1.00 19.13 N
HETATM 2694 C9 S1Z A 801 78.835 68.087 30.403 1.00 18.95 C
HETATM 2695 C1 S1Z A 801 82.356 64.271 31.437 1.00 21.50 C
HETATM 2696 C5 S1Z A 801 78.115 65.195 33.176 1.00 21.16 C
HETATM 2697 C6 S1Z A 801 77.219 66.186 32.933 1.00 21.61 C
HETATM 2698 N3 S1Z A 801 83.087 69.316 26.999 1.00 19.51 N
HETATM 2699 C4 S1Z A 801 79.388 65.291 32.589 1.00 20.89 C
HETATM 2700 C3 S1Z A 801 82.624 64.028 33.928 1.00 23.32 C
HETATM 2701 C2 S1Z A 801 81.843 64.688 32.801 1.00 21.40 C
HETATM 2702 N4 S1Z A 801 78.779 67.082 31.377 1.00 19.02 N
HETATM 2703 O S1Z A 801 82.201 64.454 35.223 1.00 22.95 O
HETATM 2704 C S1Z A 801 83.615 65.021 31.062 1.00 22.49 C
HETATM 2705 N S1Z A 801 80.416 64.532 33.043 1.00 21.69 N
HETATM 2706 N5 S1Z A 801 79.756 66.173 31.676 1.00 19.03 N
HETATM 2707 C10 S1Z A 801 79.945 68.392 29.478 1.00 18.32 C
HETATM 2708 C15 S1Z A 801 81.091 67.612 29.361 1.00 17.77 C
HETATM 2709 C14 S1Z A 801 82.106 67.985 28.468 1.00 18.17 C
HETATM 2710 C16 S1Z A 801 83.395 67.512 28.111 1.00 18.23 C
HETATM 2711 C13 S1Z A 801 81.946 69.158 27.712 1.00 19.93 C
HETATM 2712 C12 S1Z A 801 80.809 69.938 27.815 1.00 19.18 C
HETATM 2713 C11 S1Z A 801 79.809 69.546 28.680 1.00 18.87 C
HETATM 2714 NA NA A 802 86.875 76.659 28.580 1.00 21.69 NA
HETATM 2715 C1 GOL A 803 90.973 81.657 31.578 1.00 43.90 C
HETATM 2716 O1 GOL A 803 90.852 80.623 30.592 1.00 37.83 O
HETATM 2717 C2 GOL A 803 89.614 82.343 31.734 1.00 42.68 C
HETATM 2718 O2 GOL A 803 89.538 83.261 30.617 1.00 36.10 O
HETATM 2719 C3 GOL A 803 89.425 82.926 33.155 1.00 41.79 C
HETATM 2720 O3 GOL A 803 89.539 81.832 34.110 1.00 47.16 O
HETATM 2721 C1 GOL A 804 90.088 91.382 39.278 1.00 52.34 C
HETATM 2722 O1 GOL A 804 91.201 91.681 40.130 1.00 59.43 O
HETATM 2723 C2 GOL A 804 89.940 92.434 38.181 1.00 50.67 C
HETATM 2724 O2 GOL A 804 89.687 93.728 38.743 1.00 51.86 O
HETATM 2725 C3 GOL A 804 91.203 92.499 37.339 1.00 52.67 C
HETATM 2726 O3 GOL A 804 90.888 92.393 35.944 1.00 48.79 O
HETATM 2727 C1 MPD A 805 67.140 86.075 30.153 1.00 45.08 C
HETATM 2728 C2 MPD A 805 67.713 85.589 28.832 1.00 44.86 C
HETATM 2729 O2 MPD A 805 67.996 86.714 28.003 1.00 40.91 O
HETATM 2730 CM MPD A 805 69.068 84.924 29.093 1.00 42.47 C
HETATM 2731 C3 MPD A 805 66.680 84.702 28.119 1.00 48.36 C
HETATM 2732 C4 MPD A 805 66.003 85.352 26.899 1.00 54.96 C
HETATM 2733 O4 MPD A 805 65.560 84.283 26.055 1.00 57.79 O
HETATM 2734 C5 MPD A 805 64.820 86.259 27.269 1.00 56.19 C
HETATM 2735 O HOH A 901 59.777 53.938 25.816 1.00 44.63 O
HETATM 2736 O HOH A 902 92.228 80.856 28.068 1.00 43.47 O
HETATM 2737 O HOH A 903 79.996 90.435 46.437 1.00 39.59 O
HETATM 2738 O HOH A 904 87.376 66.763 50.768 1.00 49.06 O
HETATM 2739 O HOH A 905 58.952 60.521 31.824 1.00 35.49 O
HETATM 2740 O HOH A 906 86.726 63.082 32.476 1.00 38.92 O
HETATM 2741 O HOH A 907 60.904 49.088 22.749 1.00 47.85 O
HETATM 2742 O HOH A 908 86.492 70.933 20.632 1.00 28.26 O
HETATM 2743 O HOH A 909 87.061 59.628 25.166 1.00 54.17 O
HETATM 2744 O HOH A 910 81.279 70.819 15.260 1.00 49.56 O
HETATM 2745 O HOH A 911 80.246 56.852 36.683 1.00 42.40 O
HETATM 2746 O HOH A 912 93.350 87.869 39.160 1.00 27.50 O
HETATM 2747 O HOH A 913 77.114 70.206 15.640 1.00 47.39 O
HETATM 2748 O HOH A 914 67.510 61.400 29.371 1.00 25.87 O
HETATM 2749 O HOH A 915 88.532 92.026 26.884 1.00 29.07 O
HETATM 2750 O HOH A 916 82.094 65.434 45.455 1.00 28.77 O
HETATM 2751 O HOH A 917 95.251 67.015 48.739 1.00 44.36 O
HETATM 2752 O HOH A 918 77.314 89.734 22.325 1.00 38.36 O
HETATM 2753 O HOH A 919 67.889 49.511 34.979 1.00 40.30 O
HETATM 2754 O HOH A 920 94.759 73.835 25.205 1.00 47.30 O
HETATM 2755 O HOH A 921 92.885 75.026 26.416 1.00 50.72 O
HETATM 2756 O HOH A 922 70.903 95.636 28.632 1.00 44.65 O
HETATM 2757 O HOH A 923 83.660 61.670 12.943 1.00 42.25 O
HETATM 2758 O HOH A 924 67.398 80.477 55.631 1.00 51.03 O
HETATM 2759 O HOH A 925 67.677 55.795 16.166 1.00 30.90 O
HETATM 2760 O HOH A 926 54.482 56.803 21.941 1.00 46.56 O
HETATM 2761 O HOH A 927 77.474 90.190 41.037 1.00 37.19 O
HETATM 2762 O HOH A 928 74.546 88.891 23.939 1.00 50.24 O
HETATM 2763 O HOH A 929 65.778 84.701 50.283 1.00 56.14 O
HETATM 2764 O HOH A 930 82.437 90.695 51.810 1.00 45.23 O
HETATM 2765 O HOH A 931 100.892 71.956 36.492 1.00 39.24 O
HETATM 2766 O HOH A 932 75.641 47.132 30.172 1.00 37.95 O
HETATM 2767 O HOH A 933 89.622 78.352 25.707 1.00 38.27 O
HETATM 2768 O HOH A 934 105.135 67.693 52.912 1.00 31.81 O
HETATM 2769 O HOH A 935 93.677 92.164 39.377 1.00 58.02 O
HETATM 2770 O HOH A 936 104.160 72.476 39.749 1.00 47.46 O
HETATM 2771 O HOH A 937 93.794 63.182 52.881 1.00 43.42 O
HETATM 2772 O HOH A 938 77.279 88.562 28.425 1.00 37.80 O
HETATM 2773 O HOH A 939 75.071 72.545 30.294 1.00 21.81 O
HETATM 2774 O HOH A 940 74.652 92.441 40.102 1.00 44.81 O
HETATM 2775 O HOH A 941 69.623 85.579 26.250 1.00 46.87 O
HETATM 2776 O HOH A 942 86.124 77.185 26.387 1.00 26.24 O
HETATM 2777 O HOH A 943 56.655 72.296 30.635 1.00 46.43 O
HETATM 2778 O HOH A 944 57.714 56.611 23.090 1.00 36.79 O
HETATM 2779 O HOH A 945 80.206 90.715 40.170 1.00 32.63 O
HETATM 2780 O HOH A 946 64.699 64.747 30.718 1.00 31.54 O
HETATM 2781 O HOH A 947 79.114 94.398 35.843 1.00 48.65 O
HETATM 2782 O HOH A 948 93.056 90.599 51.473 1.00 46.55 O
HETATM 2783 O HOH A 949 68.648 76.876 39.905 1.00 25.54 O
HETATM 2784 O HOH A 950 65.948 60.785 39.581 1.00 42.19 O
HETATM 2785 O HOH A 951 85.580 67.253 53.387 1.00 45.30 O
HETATM 2786 O HOH A 952 70.886 68.333 32.176 1.00 25.46 O
HETATM 2787 O HOH A 953 88.615 71.180 57.294 1.00 49.27 O
HETATM 2788 O HOH A 954 90.086 78.884 32.795 1.00 30.06 O
HETATM 2789 O HOH A 955 68.511 82.029 45.012 1.00 31.94 O
HETATM 2790 O HOH A 956 76.708 64.345 36.480 1.00 44.39 O
HETATM 2791 O HOH A 957 61.686 57.580 14.004 1.00 47.30 O
HETATM 2792 O HOH A 958 88.815 74.431 21.359 1.00 48.22 O
HETATM 2793 O HOH A 959 80.944 74.829 55.569 1.00 36.07 O
HETATM 2794 O HOH A 960 77.229 49.250 37.190 1.00 44.82 O
HETATM 2795 O HOH A 961 94.557 89.972 30.044 1.00 44.60 O
HETATM 2796 O HOH A 962 97.541 64.100 49.516 1.00 47.45 O
HETATM 2797 O HOH A 963 68.503 55.834 31.214 1.00 31.66 O
HETATM 2798 O HOH A 964 84.663 61.831 37.867 1.00 42.31 O
HETATM 2799 O HOH A 965 82.330 54.135 26.091 1.00 24.18 O
HETATM 2800 O HOH A 966 82.160 62.695 37.256 1.00 39.26 O
HETATM 2801 O HOH A 967 68.668 46.520 29.717 1.00 48.20 O
HETATM 2802 O HOH A 968 67.048 49.672 30.772 1.00 33.33 O
HETATM 2803 O HOH A 969 68.345 70.755 32.050 1.00 36.57 O
HETATM 2804 O HOH A 970 88.312 73.211 25.372 1.00 45.55 O
HETATM 2805 O HOH A 971 100.012 86.152 35.369 1.00 44.87 O
HETATM 2806 O HOH A 972 95.775 88.323 38.129 1.00 37.09 O
HETATM 2807 O HOH A 973 86.170 79.816 55.093 1.00 29.17 O
HETATM 2808 O HOH A 974 76.452 67.675 37.938 1.00 45.33 O
HETATM 2809 O HOH A 975 74.461 69.947 56.000 1.00 45.71 O
HETATM 2810 O HOH A 976 71.339 92.547 27.606 1.00 36.83 O
HETATM 2811 O HOH A 977 79.322 80.939 21.723 1.00 35.11 O
HETATM 2812 O HOH A 978 83.175 79.678 24.000 1.00 25.04 O
HETATM 2813 O HOH A 979 76.828 87.707 25.368 1.00 42.02 O
HETATM 2814 O HOH A 980 75.153 66.582 40.329 1.00 44.06 O
HETATM 2815 O HOH A 981 87.478 94.825 37.483 1.00 36.15 O
HETATM 2816 O HOH A 982 85.219 57.461 30.032 1.00 47.20 O
HETATM 2817 O HOH A 983 89.452 73.014 29.665 1.00 21.60 O
HETATM 2818 O HOH A 984 92.864 89.587 45.364 1.00 30.46 O
HETATM 2819 O HOH A 985 76.692 86.118 27.499 1.00 26.89 O
HETATM 2820 O HOH A 986 98.617 85.073 43.737 1.00 46.27 O
HETATM 2821 O HOH A 987 66.729 91.448 27.113 1.00 26.36 O
HETATM 2822 O HOH A 988 76.372 87.605 48.793 1.00 33.73 O
HETATM 2823 O HOH A 989 73.627 67.111 36.035 1.00 46.86 O
HETATM 2824 O HOH A 990 85.206 60.148 31.850 1.00 44.46 O
HETATM 2825 O HOH A 991 72.255 66.919 49.869 1.00 32.68 O
HETATM 2826 O HOH A 992 67.938 51.183 21.153 1.00 36.40 O
HETATM 2827 O HOH A 993 92.910 89.199 41.514 1.00 33.68 O
HETATM 2828 O HOH A 994 88.025 62.118 27.801 1.00 28.81 O
HETATM 2829 O HOH A 995 73.852 59.180 36.840 1.00 38.43 O
HETATM 2830 O HOH A 996 97.559 82.384 40.632 1.00 33.34 O
HETATM 2831 O HOH A 997 93.473 60.383 39.345 1.00 41.27 O
HETATM 2832 O HOH A 998 72.842 90.420 33.722 1.00 42.43 O
HETATM 2833 O HOH A 999 68.070 89.120 40.955 1.00 54.10 O
HETATM 2834 O HOH A1000 79.661 65.736 36.087 1.00 34.26 O
HETATM 2835 O HOH A1001 105.673 80.512 47.103 1.00 42.49 O
HETATM 2836 O HOH A1002 76.760 58.949 38.066 1.00 51.47 O
HETATM 2837 O HOH A1003 91.463 68.226 22.889 1.00 54.18 O
HETATM 2838 O HOH A1004 64.000 87.621 49.804 1.00 57.44 O
HETATM 2839 O HOH A1005 70.697 59.976 26.829 1.00 23.74 O
HETATM 2840 O HOH A1006 67.526 71.379 34.997 1.00 47.16 O
HETATM 2841 O HOH A1007 71.012 80.715 45.529 1.00 27.68 O
HETATM 2842 O HOH A1008 85.098 68.907 49.532 1.00 28.60 O
HETATM 2843 O HOH A1009 61.133 72.044 42.740 1.00 41.52 O
HETATM 2844 O HOH A1010 70.203 57.682 30.473 1.00 27.46 O
HETATM 2845 O HOH A1011 61.187 53.789 12.716 1.00 26.90 O
HETATM 2846 O HOH A1012 67.058 73.225 31.756 1.00 29.23 O
HETATM 2847 O HOH A1013 85.246 83.070 21.307 1.00 48.78 O
HETATM 2848 O HOH A1014 92.044 67.623 16.255 1.00 48.05 O
HETATM 2849 O HOH A1015 58.620 66.999 33.378 1.00 39.84 O
HETATM 2850 O HOH A1016 65.873 61.703 33.669 1.00 32.74 O
HETATM 2851 O HOH A1017 94.265 61.387 45.108 1.00 43.04 O
HETATM 2852 O HOH A1018 59.510 57.788 27.037 1.00 35.86 O
HETATM 2853 O HOH A1019 74.137 81.603 54.376 1.00 43.99 O
HETATM 2854 O HOH A1020 69.254 91.965 34.966 1.00 33.74 O
HETATM 2855 O HOH A1021 77.133 53.292 31.255 1.00 25.42 O
HETATM 2856 O HOH A1022 82.177 60.190 34.347 1.00 33.06 O
HETATM 2857 O HOH A1023 83.503 80.887 28.485 1.00 21.31 O
HETATM 2858 O HOH A1024 90.634 62.883 24.316 1.00 48.73 O
HETATM 2859 O HOH A1025 57.218 61.861 20.159 1.00 49.37 O
HETATM 2860 O HOH A1026 76.677 91.552 38.824 1.00 37.61 O
HETATM 2861 O HOH A1027 73.794 69.179 18.499 1.00 24.16 O
HETATM 2862 O HOH A1028 83.166 76.041 20.671 1.00 49.88 O
HETATM 2863 O HOH A1029 63.706 51.515 16.580 1.00 33.36 O
HETATM 2864 O HOH A1030 86.823 59.992 44.017 1.00 49.58 O
HETATM 2865 O HOH A1031 76.874 78.510 42.680 1.00 19.90 O
HETATM 2866 O HOH A1032 100.084 78.816 40.425 1.00 35.32 O
HETATM 2867 O HOH A1033 62.397 78.792 43.949 1.00 35.07 O
HETATM 2868 O HOH A1034 95.683 70.226 24.832 1.00 54.11 O
HETATM 2869 O HOH A1035 74.499 47.785 20.924 1.00 43.06 O
HETATM 2870 O HOH A1036 70.506 85.119 53.279 1.00 48.08 O
HETATM 2871 O HOH A1037 67.028 96.243 31.036 1.00 34.74 O
HETATM 2872 O HOH A1038 64.704 57.998 13.847 1.00 48.83 O
HETATM 2873 O HOH A1039 88.122 81.918 59.960 1.00 52.17 O
HETATM 2874 O HOH A1040 59.466 62.030 23.356 1.00 27.86 O
HETATM 2875 O HOH A1041 71.359 92.319 32.088 1.00 36.99 O
HETATM 2876 O HOH A1042 96.732 65.560 41.701 1.00 34.80 O
HETATM 2877 O HOH A1043 69.047 73.749 54.266 1.00 39.46 O
HETATM 2878 O HOH A1044 60.218 56.092 24.058 1.00 25.12 O
HETATM 2879 O HOH A1045 80.779 86.697 22.174 1.00 28.87 O
HETATM 2880 O HOH A1046 80.484 47.445 24.572 1.00 37.82 O
HETATM 2881 O HOH A1047 62.632 75.146 36.999 1.00 41.07 O
HETATM 2882 O HOH A1048 54.294 59.154 18.338 1.00 49.55 O
HETATM 2883 O HOH A1049 74.711 78.975 53.980 1.00 41.05 O
HETATM 2884 O HOH A1050 80.048 89.700 28.914 1.00 21.77 O
HETATM 2885 O HOH A1051 85.822 90.138 20.959 1.00 50.93 O
HETATM 2886 O HOH A1052 86.267 59.502 20.998 1.00 47.85 O
HETATM 2887 O HOH A1053 74.556 73.118 37.431 1.00 23.31 O
HETATM 2888 O HOH A1054 70.308 57.547 38.246 1.00 46.49 O
HETATM 2889 O HOH A1055 90.716 88.847 28.458 1.00 30.80 O
HETATM 2890 O HOH A1056 66.437 89.124 28.677 1.00 29.43 O
HETATM 2891 O HOH A1057 92.905 96.382 31.617 1.00 38.78 O
HETATM 2892 O HOH A1058 90.573 95.506 29.137 1.00 50.77 O
HETATM 2893 O HOH A1059 98.362 80.378 38.959 1.00 30.60 O
HETATM 2894 O HOH A1060 64.573 67.393 51.582 1.00 48.64 O
HETATM 2895 O HOH A1061 82.950 64.729 10.706 1.00 40.62 O
HETATM 2896 O HOH A1062 72.506 63.478 38.301 1.00 34.51 O
HETATM 2897 O HOH A1063 87.329 78.202 34.735 1.00 27.27 O
HETATM 2898 O HOH A1064 86.590 63.691 29.548 1.00 29.82 O
HETATM 2899 O HOH A1065 78.182 76.061 27.052 1.00 20.06 O
HETATM 2900 O HOH A1066 94.874 67.716 27.931 1.00 37.95 O
HETATM 2901 O HOH A1067 80.018 47.285 36.465 1.00 54.15 O
HETATM 2902 O HOH A1068 72.440 80.010 47.871 1.00 29.16 O
HETATM 2903 O HOH A1069 77.106 65.220 53.439 1.00 34.56 O
HETATM 2904 O HOH A1070 95.606 83.188 51.050 1.00 38.17 O
HETATM 2905 O HOH A1071 102.395 70.065 46.184 1.00 38.24 O
HETATM 2906 O HOH A1072 66.930 58.273 14.689 1.00 43.23 O
HETATM 2907 O HOH A1073 64.504 47.524 27.414 1.00 52.56 O
HETATM 2908 O HOH A1074 69.535 61.968 48.515 1.00 57.60 O
HETATM 2909 O HOH A1075 102.256 78.892 33.932 1.00 39.27 O
HETATM 2910 O HOH A1076 87.278 62.797 20.743 1.00 38.43 O
HETATM 2911 O HOH A1077 92.060 94.048 47.763 1.00 51.93 O
HETATM 2912 O HOH A1078 83.951 65.559 51.576 1.00 36.31 O
HETATM 2913 O HOH A1079 91.579 93.776 42.915 1.00 50.57 O
HETATM 2914 O HOH A1080 74.621 85.637 48.287 1.00 27.34 O
HETATM 2915 O HOH A1081 69.631 75.806 34.666 1.00 29.17 O
HETATM 2916 O HOH A1082 63.904 55.155 36.100 1.00 41.07 O
HETATM 2917 O HOH A1083 66.222 52.878 22.806 1.00 26.06 O
HETATM 2918 O HOH A1084 80.792 61.761 46.352 1.00 54.17 O
HETATM 2919 O HOH A1085 79.768 58.757 8.383 1.00 33.89 O
HETATM 2920 O HOH A1086 100.695 71.411 29.591 1.00 47.32 O
HETATM 2921 O HOH A1087 77.901 72.206 29.986 1.00 19.99 O
HETATM 2922 O HOH A1088 82.026 82.866 21.995 1.00 46.93 O
HETATM 2923 O HOH A1089 62.226 86.709 35.424 1.00 38.32 O
HETATM 2924 O HOH A1090 61.828 65.934 35.877 1.00 49.67 O
HETATM 2925 O HOH A1091 66.966 70.161 15.615 1.00 37.25 O
HETATM 2926 O HOH A1092 72.637 68.679 38.308 1.00 44.12 O
HETATM 2927 O HOH A1093 58.012 64.677 29.581 1.00 48.32 O
HETATM 2928 O HOH A1094 67.600 88.595 43.683 1.00 35.79 O
HETATM 2929 O HOH A1095 99.989 65.021 47.647 1.00 48.39 O
HETATM 2930 O HOH A1096 86.685 76.239 56.564 1.00 49.11 O
HETATM 2931 O HOH A1097 65.916 77.740 53.929 1.00 49.23 O
HETATM 2932 O HOH A1098 80.651 93.260 39.062 1.00 31.91 O
HETATM 2933 O HOH A1099 86.099 63.950 11.219 1.00 32.81 O
HETATM 2934 O HOH A1100 72.409 74.818 16.923 1.00 33.79 O
HETATM 2935 O HOH A1101 64.929 64.142 34.211 1.00 38.14 O
HETATM 2936 O HOH A1102 97.319 90.455 35.852 1.00 49.51 O
HETATM 2937 O HOH A1103 83.753 54.633 28.322 1.00 36.38 O
HETATM 2938 O HOH A1104 63.813 79.520 34.346 1.00 33.33 O
HETATM 2939 O HOH A1105 80.676 53.717 19.438 1.00 44.68 O
HETATM 2940 O HOH A1106 93.800 83.099 27.636 1.00 32.09 O
HETATM 2941 O HOH A1107 73.733 60.532 8.192 1.00 47.85 O
HETATM 2942 O HOH A1108 60.315 63.524 38.143 1.00 48.16 O
HETATM 2943 O HOH A1109 62.489 82.537 43.862 1.00 36.97 O
HETATM 2944 O HOH A1110 65.002 55.325 15.396 1.00 30.06 O
HETATM 2945 O HOH A1111 95.404 95.325 31.901 1.00 55.75 O
HETATM 2946 O HOH A1112 82.690 62.523 44.132 1.00 51.19 O
HETATM 2947 O HOH A1113 72.515 46.513 22.151 1.00 53.56 O
HETATM 2948 O HOH A1114 99.151 83.859 47.468 1.00 49.21 O
HETATM 2949 O HOH A1115 85.750 83.188 60.353 1.00 49.63 O
HETATM 2950 O HOH A1116 99.703 69.339 36.440 1.00 31.72 O
HETATM 2951 O HOH A1117 94.540 95.851 34.631 1.00 59.99 O
HETATM 2952 O HOH A1118 74.350 60.760 49.182 1.00 56.72 O
HETATM 2953 O HOH A1119 56.183 61.553 16.087 1.00 56.44 O
HETATM 2954 O HOH A1120 97.350 83.432 57.848 1.00 50.73 O
HETATM 2955 O HOH A1121 85.116 95.117 38.972 1.00 40.17 O
HETATM 2956 O HOH A1122 78.029 46.667 30.739 1.00 43.11 O
HETATM 2957 O HOH A1123 98.789 58.617 43.571 1.00 46.95 O
HETATM 2958 O HOH A1124 67.544 74.138 34.281 1.00 33.51 O
HETATM 2959 O HOH A1125 79.662 62.132 34.861 1.00 24.22 O
HETATM 2960 O HOH A1126 71.054 82.283 25.486 1.00 40.42 O
HETATM 2961 O HOH A1127 84.968 77.890 22.604 1.00 47.86 O
HETATM 2962 O HOH A1128 61.632 52.929 32.133 1.00 50.74 O
HETATM 2963 O HOH A1129 99.896 70.225 31.846 1.00 59.91 O
HETATM 2964 O HOH A1130 73.897 56.547 9.535 1.00 39.99 O
HETATM 2965 O HOH A1131 76.923 64.563 41.516 1.00 39.24 O
HETATM 2966 O HOH A1132 84.664 54.211 19.898 1.00 59.27 O
HETATM 2967 O HOH A1133 62.301 78.342 36.517 1.00 58.93 O
HETATM 2968 O HOH A1134 73.350 66.196 42.489 1.00 49.74 O
HETATM 2969 O HOH A1135 81.258 64.444 42.048 1.00 42.85 O
HETATM 2970 O HOH A1136 75.307 58.276 8.391 1.00 40.62 O
HETATM 2971 O HOH A1137 68.488 58.003 12.574 1.00 36.53 O
HETATM 2972 O HOH A1138 62.444 71.294 35.624 1.00 57.68 O
HETATM 2973 O HOH A1139 101.560 82.879 27.432 1.00 46.30 O
HETATM 2974 O HOH A1140 82.933 81.748 58.248 1.00 56.47 O
HETATM 2975 O HOH A1141 70.661 65.715 35.987 1.00 32.02 O
HETATM 2976 O HOH A1142 89.031 76.585 27.815 1.00 30.19 O
HETATM 2977 O HOH A1143 101.582 80.574 42.284 1.00 52.04 O
HETATM 2978 O HOH A1144 72.216 71.333 11.346 1.00 53.76 O
HETATM 2979 O HOH A1145 111.708 77.012 47.275 1.00 47.65 O
HETATM 2980 O HOH A1146 76.089 78.439 19.527 1.00 51.79 O
HETATM 2981 O HOH A1147 71.333 73.349 14.886 1.00 50.18 O
HETATM 2982 O HOH A1148 84.712 72.577 19.208 1.00 35.60 O
HETATM 2983 O HOH A1149 58.143 59.618 24.008 1.00 39.79 O
HETATM 2984 O HOH A1150 78.154 93.700 37.904 1.00 45.33 O
HETATM 2985 O HOH A1151 81.157 46.286 27.553 1.00 51.23 O
HETATM 2986 O HOH A1152 75.393 67.064 17.267 1.00 38.84 O
HETATM 2987 O HOH A1153 89.093 91.185 24.126 1.00 41.94 O
HETATM 2988 O HOH A1154 67.112 69.331 36.851 1.00 46.24 O
HETATM 2989 O HOH A1155 87.456 60.410 30.247 1.00 57.13 O
HETATM 2990 O HOH A1156 101.622 68.401 48.460 1.00 34.26 O
HETATM 2991 O HOH A1157 75.535 67.506 14.531 1.00 52.61 O
HETATM 2992 O HOH A1158 62.538 61.746 12.502 1.00 50.00 O
HETATM 2993 O HOH A1159 65.322 61.945 30.873 1.00 30.01 O
HETATM 2994 O HOH A1160 81.950 51.702 21.937 1.00 53.18 O
HETATM 2995 O HOH A1161 92.916 90.330 27.827 1.00 48.91 O
HETATM 2996 O HOH A1162 99.016 69.102 50.255 1.00 51.42 O
HETATM 2997 O HOH A1163 65.826 65.816 36.134 1.00 40.28 O
HETATM 2998 O HOH A1164 84.021 78.952 26.506 1.00 26.69 O
HETATM 2999 O HOH A1165 58.582 73.564 42.004 1.00 56.35 O
HETATM 3000 O HOH A1166 85.001 85.388 61.549 1.00 49.79 O
HETATM 3001 O HOH A1167 92.240 85.154 59.107 1.00 46.41 O
HETATM 3002 O HOH A1168 76.995 92.285 29.101 1.00 45.76 O
HETATM 3003 O HOH A1169 94.698 66.610 30.504 1.00 59.55 O
HETATM 3004 O HOH A1170 56.228 66.093 22.223 1.00 53.32 O
HETATM 3005 O HOH A1171 97.782 68.924 56.516 1.00 52.64 O
HETATM 3006 O HOH A1172 79.035 63.311 37.331 1.00 53.60 O
HETATM 3007 O HOH A1173 79.817 95.463 31.032 1.00 40.48 O
HETATM 3008 O HOH A1174 103.538 76.993 32.509 1.00 50.79 O
HETATM 3009 O HOH A1175 90.108 74.129 27.212 1.00 33.41 O
HETATM 3010 O HOH A1176 89.325 94.834 26.888 1.00 52.51 O
HETATM 3011 O HOH A1177 83.609 53.104 23.809 1.00 43.37 O
HETATM 3012 O HOH A1178 66.700 65.643 32.230 1.00 31.32 O
HETATM 3013 O HOH A1179 86.969 79.345 23.761 1.00 51.10 O
HETATM 3014 O HOH A1180 59.353 45.804 22.764 1.00 43.74 O
HETATM 3015 O HOH A1181 96.619 91.781 30.850 1.00 50.69 O
HETATM 3016 O HOH A1182 91.315 65.015 22.650 1.00 52.00 O
HETATM 3017 O HOH A1183 76.521 90.082 47.257 1.00 47.31 O
HETATM 3018 O HOH A1184 57.197 63.136 22.251 1.00 38.56 O
HETATM 3019 O HOH A1185 99.126 84.650 40.504 1.00 50.39 O
HETATM 3020 O HOH A1186 68.228 68.021 32.692 1.00 32.48 O
HETATM 3021 O HOH A1187 74.544 65.250 37.672 1.00 41.65 O
HETATM 3022 O HOH A1188 68.117 67.050 35.407 1.00 36.13 O
HETATM 3023 O HOH A1189 90.697 62.700 27.116 1.00 45.79 O
HETATM 3024 O HOH A1190 91.906 65.399 27.447 1.00 47.15 O
HETATM 3025 O HOH A1191 79.324 60.370 37.781 1.00 53.50 O
HETATM 3026 O HOH A1192 68.812 59.048 28.448 1.00 28.41 O
HETATM 3027 O HOH A1193 73.310 59.620 39.318 1.00 51.35 O
HETATM 3028 O HOH A1194 79.270 77.011 56.391 1.00 45.37 O
CONECT 663 2714
CONECT 676 2714
CONECT 1703 2714
CONECT 2690 2691 2692
CONECT 2691 2690 2697 2702
CONECT 2692 2690 2694
CONECT 2693 2698 2710
CONECT 2694 2692 2702 2707
CONECT 2695 2701 2704
CONECT 2696 2697 2699
CONECT 2697 2691 2696
CONECT 2698 2693 2711
CONECT 2699 2696 2705 2706
CONECT 2700 2701 2703
CONECT 2701 2695 2700 2705
CONECT 2702 2691 2694 2706
CONECT 2703 2700
CONECT 2704 2695
CONECT 2705 2699 2701
CONECT 2706 2699 2702
CONECT 2707 2694 2708 2713
CONECT 2708 2707 2709
CONECT 2709 2708 2710 2711
CONECT 2710 2693 2709
CONECT 2711 2698 2709 2712
CONECT 2712 2711 2713
CONECT 2713 2707 2712
CONECT 2714 663 676 1703 2776
CONECT 2714 2976
CONECT 2715 2716 2717
CONECT 2716 2715
CONECT 2717 2715 2718 2719
CONECT 2718 2717
CONECT 2719 2717 2720
CONECT 2720 2719
CONECT 2721 2722 2723
CONECT 2722 2721
CONECT 2723 2721 2724 2725
CONECT 2724 2723
CONECT 2725 2723 2726
CONECT 2726 2725
CONECT 2727 2728
CONECT 2728 2727 2729 2730 2731
CONECT 2729 2728
CONECT 2730 2728
CONECT 2731 2728 2732
CONECT 2732 2731 2733 2734
CONECT 2733 2732
CONECT 2734 2732
CONECT 2776 2714
CONECT 2976 2714
MASTER 343 0 5 13 13 0 0 6 2966 1 51 28
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