HEADER PROTEIN BINDING 15-JUN-20 6ZDV
TITLE CRYSTAL STRUCTURE OF STABILIZED A2A ADENOSINE RECEPTOR A2AR-STAR2-BRIL
TITLE 2 IN COMPLEX WITH CHROMONE 5D
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ADENOSINE RECEPTOR A2A,SOLUBLE CYTOCHROME B562,ADENOSINE
COMPND 3 RECEPTOR A2A;
COMPND 4 CHAIN: A;
COMPND 5 SYNONYM: CYTOCHROME B-562;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, ESCHERICHIA COLI;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606, 562;
SOURCE 5 GENE: ADORA2A, ADORA2, CYBC;
SOURCE 6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7111
KEYWDS G PROTEIN-COUPLED RECEPTOR, MEMBRANE PROTEIN, RECEPTOR, PROTEIN
KEYWDS 2 BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR G.VERDON,W.JESPERS,J.AZUAJE,M.MAJELLARO,H.KERANEN,X.GARCIA-MERA,
AUTHOR 2 M.CONGREVE,F.DEFLORIAN,C.DE GRAAF,A.ZHUKOV,A.DORE,J.MASON,J.AQVIST,
AUTHOR 3 R.COOKE,E.SOTELO,H.GUTIERREZ-DE-TERAN
REVDAT 2 16-DEC-20 6ZDV 1 JRNL
REVDAT 1 16-SEP-20 6ZDV 0
JRNL AUTH W.JESPERS,G.VERDON,J.AZUAJE,M.MAJELLARO,H.KERANEN,
JRNL AUTH 2 X.GARCIA-MERA,M.CONGREVE,F.DEFLORIAN,C.DE GRAAF,A.ZHUKOV,
JRNL AUTH 3 A.S.DORE,J.S.MASON,J.AQVIST,R.M.COOKE,E.SOTELO,
JRNL AUTH 4 H.GUTIERREZ-DE-TERAN
JRNL TITL X-RAY CRYSTALLOGRAPHY AND FREE ENERGY CALCULATIONS REVEAL
JRNL TITL 2 THE BINDING MECHANISM OF A 2A ADENOSINE RECEPTOR
JRNL TITL 3 ANTAGONISTS.
JRNL REF ANGEW.CHEM.INT.ED.ENGL. V. 59 16536 2020
JRNL REFN ESSN 1521-3773
JRNL PMID 32542862
JRNL DOI 10.1002/ANIE.202003788
REMARK 2
REMARK 2 RESOLUTION. 2.13 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.11.7
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.13
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.80
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 84.0
REMARK 3 NUMBER OF REFLECTIONS : 25511
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) : 0.216
REMARK 3 R VALUE (WORKING SET) : 0.215
REMARK 3 FREE R VALUE : 0.224
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 1260
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.13
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.20
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 11.29
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : NULL
REMARK 3 BIN R VALUE (WORKING + TEST SET) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.1961
REMARK 3 BIN FREE R VALUE : 0.2630
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 27
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2938
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 277
REMARK 3 SOLVENT ATOMS : 89
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 49.69
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.88180
REMARK 3 B22 (A**2) : 5.49510
REMARK 3 B33 (A**2) : -3.61330
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.300
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.247
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.176
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.248
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.178
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.925
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.947
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 3309 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 4479 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 1199 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES : 528 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 3282 ; 10.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 441 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 3059 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.023
REMARK 3 BOND ANGLES (DEGREES) : 1.59
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.56
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 20.16
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|-1 - A|208 A|219 - A|305 A|1201 - A|1201 }
REMARK 3 ORIGIN FOR THE GROUP (A): 22.0383 187.0307 17.8505
REMARK 3 T TENSOR
REMARK 3 T11: -0.0034 T22: 0.0306
REMARK 3 T33: -0.053 T12: -0.006
REMARK 3 T13: -0.0007 T23: -0.0029
REMARK 3 L TENSOR
REMARK 3 L11: 0.1356 L22: 0.2505
REMARK 3 L33: 0.0821 L12: 0.0971
REMARK 3 L13: -0.2004 L23: 0.0303
REMARK 3 S TENSOR
REMARK 3 S11: -0 S12: -0.0555 S13: -0.0355
REMARK 3 S21: -0.0555 S22: -0.0138 S23: 0.0447
REMARK 3 S31: -0.0355 S32: 0.0447 S33: 0.0139
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: { A|1001 - A|1106 }
REMARK 3 ORIGIN FOR THE GROUP (A): -1.8344 234.8934 19.9907
REMARK 3 T TENSOR
REMARK 3 T11: -0.1015 T22: -0.2021
REMARK 3 T33: 0.2514 T12: 0.0925
REMARK 3 T13: 0.0346 T23: 0.0495
REMARK 3 L TENSOR
REMARK 3 L11: 0.2998 L22: 0.5443
REMARK 3 L33: 0 L12: -0.7667
REMARK 3 L13: -0.0761 L23: -0.5405
REMARK 3 S TENSOR
REMARK 3 S11: 0.107 S12: -0.5054 S13: -0.2474
REMARK 3 S21: -0.5054 S22: 0.1966 S23: -0.0644
REMARK 3 S31: -0.2474 S32: -0.0644 S33: -0.3036
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6ZDV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-JUN-20.
REMARK 100 THE DEPOSITION ID IS D_1292109402.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-MAR-18
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25511
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.130
REMARK 200 RESOLUTION RANGE LOW (A) : 42.808
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 91.8
REMARK 200 DATA REDUNDANCY : 9.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.13
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.24
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 5IU4
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.43
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.59
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 400, SODIUM CITRATE, SODIUM
REMARK 280 THIOCYANATE, 2,5 HEXANEDIOL, LIPIDIC CUBIC PHASE, TEMPERATURE
REMARK 280 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 70.04250
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 70.04250
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 19.70700
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 89.91650
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 19.70700
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 89.91650
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 70.04250
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 19.70700
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 89.91650
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 70.04250
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 19.70700
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 89.91650
REMARK 290 SMTRY3 8 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6830 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19620 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 3.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 ASP A -8
REMARK 465 TYR A -7
REMARK 465 LYS A -6
REMARK 465 ASP A -5
REMARK 465 ASP A -4
REMARK 465 ASP A -3
REMARK 465 ASP A -2
REMARK 465 GLY A -1
REMARK 465 THR A 1044
REMARK 465 PRO A 1045
REMARK 465 PRO A 1046
REMARK 465 LYS A 1047
REMARK 465 LEU A 1048
REMARK 465 GLU A 1049
REMARK 465 ASP A 1050
REMARK 465 LYS A 1051
REMARK 465 SER A 1052
REMARK 465 PRO A 1053
REMARK 465 ASP A 1054
REMARK 465 SER A 1055
REMARK 465 PRO A 1056
REMARK 465 GLU A 1057
REMARK 465 MET A 1058
REMARK 465 LYS A 1059
REMARK 465 ASP A 1060
REMARK 465 PHE A 1061
REMARK 465 ARG A 1062
REMARK 465 HIS A 1063
REMARK 465 HIS A 306
REMARK 465 VAL A 307
REMARK 465 LEU A 308
REMARK 465 ARG A 309
REMARK 465 GLN A 310
REMARK 465 GLN A 311
REMARK 465 GLU A 312
REMARK 465 PRO A 313
REMARK 465 PHE A 314
REMARK 465 LYS A 315
REMARK 465 ALA A 316
REMARK 465 ALA A 317
REMARK 465 ALA A 318
REMARK 465 HIS A 319
REMARK 465 HIS A 320
REMARK 465 HIS A 321
REMARK 465 HIS A 322
REMARK 465 HIS A 323
REMARK 465 HIS A 324
REMARK 465 HIS A 325
REMARK 465 HIS A 326
REMARK 465 HIS A 327
REMARK 465 HIS A 328
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A1042 CG CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OE2 GLU A 1018 NZ LYS A 1095 1.90
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 LEU A 208 C ALA A1001 N 0.194
REMARK 500 GLU A 219 C ARG A 220 N 0.238
REMARK 500
REMARK 500 REMARK: NULL
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 SER A 6 CA - C - O ANGL. DEV. = 12.7 DEGREES
REMARK 500 TRP A 29 CA - C - O ANGL. DEV. = 12.7 DEGREES
REMARK 500 LEU A 208 O - C - N ANGL. DEV. = -33.8 DEGREES
REMARK 500 ALA A1001 C - N - CA ANGL. DEV. = 29.8 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 ASN A1022 -168.30 -123.99
REMARK 500 TYR A1101 -62.01 -133.38
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 TRP A 29 -11.32
REMARK 500 TRP A 29 -10.70
REMARK 500 LEU A 208 -33.49
REMARK 500 GLU A 219 11.57
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 OLB A 1206
REMARK 610 OLA A 1207
REMARK 610 OLA A 1208
REMARK 610 OLA A 1209
REMARK 610 OLA A 1210
REMARK 610 OLA A 1211
REMARK 610 OLA A 1212
REMARK 610 OLA A 1213
REMARK 610 OLA A 1214
REMARK 610 OLA A 1215
REMARK 610 OLA A 1216
REMARK 610 OLA A 1217
REMARK 610 OLA A 1218
REMARK 610 OLA A 1219
REMARK 610 OLA A 1220
REMARK 610 OLC A 1221
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 A1202 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 52 OD1
REMARK 620 2 SER A 91 OG 117.8
REMARK 620 3 HOH A1338 O 101.4 108.6
REMARK 620 4 HOH A1354 O 72.8 65.5 74.1
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue QGW A 1201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 1202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLR A 1203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLR A 1204
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLR A 1205
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLB A 1206
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1207
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1208
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1210
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1212
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1213
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1215
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1216
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1217
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1218
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1221
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6ZRD RELATED DB: PDB
REMARK 900 COMPLEX WITH CHROMONE 4D
DBREF 6ZDV A 2 208 UNP P29274 AA2AR_HUMAN 2 208
DBREF 6ZDV A 1001 1105 UNP P0ABE7 C562_ECOLX 23 127
DBREF 6ZDV A 219 317 UNP P29274 AA2AR_HUMAN 219 317
SEQADV 6ZDV ASP A -8 UNP P29274 EXPRESSION TAG
SEQADV 6ZDV TYR A -7 UNP P29274 EXPRESSION TAG
SEQADV 6ZDV LYS A -6 UNP P29274 EXPRESSION TAG
SEQADV 6ZDV ASP A -5 UNP P29274 EXPRESSION TAG
SEQADV 6ZDV ASP A -4 UNP P29274 EXPRESSION TAG
SEQADV 6ZDV ASP A -3 UNP P29274 EXPRESSION TAG
SEQADV 6ZDV ASP A -2 UNP P29274 EXPRESSION TAG
SEQADV 6ZDV GLY A -1 UNP P29274 EXPRESSION TAG
SEQADV 6ZDV ALA A 0 UNP P29274 EXPRESSION TAG
SEQADV 6ZDV PRO A 1 UNP P29274 EXPRESSION TAG
SEQADV 6ZDV LEU A 54 UNP P29274 ALA 54 CONFLICT
SEQADV 6ZDV ALA A 88 UNP P29274 THR 88 CONFLICT
SEQADV 6ZDV ALA A 107 UNP P29274 ARG 107 CONFLICT
SEQADV 6ZDV ALA A 122 UNP P29274 LYS 122 CONFLICT
SEQADV 6ZDV ALA A 154 UNP P29274 ASN 154 CONFLICT
SEQADV 6ZDV ALA A 202 UNP P29274 LEU 202 CONFLICT
SEQADV 6ZDV TRP A 1007 UNP P0ABE7 MET 29 CONFLICT
SEQADV 6ZDV ILE A 1102 UNP P0ABE7 HIS 124 CONFLICT
SEQADV 6ZDV LEU A 1106 UNP P0ABE7 LINKER
SEQADV 6ZDV ALA A 235 UNP P29274 LEU 235 CONFLICT
SEQADV 6ZDV ALA A 239 UNP P29274 VAL 239 CONFLICT
SEQADV 6ZDV ALA A 277 UNP P29274 SER 277 CONFLICT
SEQADV 6ZDV ALA A 318 UNP P29274 EXPRESSION TAG
SEQADV 6ZDV HIS A 319 UNP P29274 EXPRESSION TAG
SEQADV 6ZDV HIS A 320 UNP P29274 EXPRESSION TAG
SEQADV 6ZDV HIS A 321 UNP P29274 EXPRESSION TAG
SEQADV 6ZDV HIS A 322 UNP P29274 EXPRESSION TAG
SEQADV 6ZDV HIS A 323 UNP P29274 EXPRESSION TAG
SEQADV 6ZDV HIS A 324 UNP P29274 EXPRESSION TAG
SEQADV 6ZDV HIS A 325 UNP P29274 EXPRESSION TAG
SEQADV 6ZDV HIS A 326 UNP P29274 EXPRESSION TAG
SEQADV 6ZDV HIS A 327 UNP P29274 EXPRESSION TAG
SEQADV 6ZDV HIS A 328 UNP P29274 EXPRESSION TAG
SEQRES 1 A 433 ASP TYR LYS ASP ASP ASP ASP GLY ALA PRO PRO ILE MET
SEQRES 2 A 433 GLY SER SER VAL TYR ILE THR VAL GLU LEU ALA ILE ALA
SEQRES 3 A 433 VAL LEU ALA ILE LEU GLY ASN VAL LEU VAL CYS TRP ALA
SEQRES 4 A 433 VAL TRP LEU ASN SER ASN LEU GLN ASN VAL THR ASN TYR
SEQRES 5 A 433 PHE VAL VAL SER LEU ALA ALA ALA ASP ILE LEU VAL GLY
SEQRES 6 A 433 VAL LEU ALA ILE PRO PHE ALA ILE THR ILE SER THR GLY
SEQRES 7 A 433 PHE CYS ALA ALA CYS HIS GLY CYS LEU PHE ILE ALA CYS
SEQRES 8 A 433 PHE VAL LEU VAL LEU ALA GLN SER SER ILE PHE SER LEU
SEQRES 9 A 433 LEU ALA ILE ALA ILE ASP ARG TYR ILE ALA ILE ALA ILE
SEQRES 10 A 433 PRO LEU ARG TYR ASN GLY LEU VAL THR GLY THR ARG ALA
SEQRES 11 A 433 ALA GLY ILE ILE ALA ILE CYS TRP VAL LEU SER PHE ALA
SEQRES 12 A 433 ILE GLY LEU THR PRO MET LEU GLY TRP ASN ASN CYS GLY
SEQRES 13 A 433 GLN PRO LYS GLU GLY LYS ALA HIS SER GLN GLY CYS GLY
SEQRES 14 A 433 GLU GLY GLN VAL ALA CYS LEU PHE GLU ASP VAL VAL PRO
SEQRES 15 A 433 MET ASN TYR MET VAL TYR PHE ASN PHE PHE ALA CYS VAL
SEQRES 16 A 433 LEU VAL PRO LEU LEU LEU MET LEU GLY VAL TYR LEU ARG
SEQRES 17 A 433 ILE PHE ALA ALA ALA ARG ARG GLN LEU ALA ASP LEU GLU
SEQRES 18 A 433 ASP ASN TRP GLU THR LEU ASN ASP ASN LEU LYS VAL ILE
SEQRES 19 A 433 GLU LYS ALA ASP ASN ALA ALA GLN VAL LYS ASP ALA LEU
SEQRES 20 A 433 THR LYS MET ARG ALA ALA ALA LEU ASP ALA GLN LYS ALA
SEQRES 21 A 433 THR PRO PRO LYS LEU GLU ASP LYS SER PRO ASP SER PRO
SEQRES 22 A 433 GLU MET LYS ASP PHE ARG HIS GLY PHE ASP ILE LEU VAL
SEQRES 23 A 433 GLY GLN ILE ASP ASP ALA LEU LYS LEU ALA ASN GLU GLY
SEQRES 24 A 433 LYS VAL LYS GLU ALA GLN ALA ALA ALA GLU GLN LEU LYS
SEQRES 25 A 433 THR THR ARG ASN ALA TYR ILE GLN LYS TYR LEU GLU ARG
SEQRES 26 A 433 ALA ARG SER THR LEU GLN LYS GLU VAL HIS ALA ALA LYS
SEQRES 27 A 433 SER ALA ALA ILE ILE ALA GLY LEU PHE ALA LEU CYS TRP
SEQRES 28 A 433 LEU PRO LEU HIS ILE ILE ASN CYS PHE THR PHE PHE CYS
SEQRES 29 A 433 PRO ASP CYS SER HIS ALA PRO LEU TRP LEU MET TYR LEU
SEQRES 30 A 433 ALA ILE VAL LEU ALA HIS THR ASN SER VAL VAL ASN PRO
SEQRES 31 A 433 PHE ILE TYR ALA TYR ARG ILE ARG GLU PHE ARG GLN THR
SEQRES 32 A 433 PHE ARG LYS ILE ILE ARG SER HIS VAL LEU ARG GLN GLN
SEQRES 33 A 433 GLU PRO PHE LYS ALA ALA ALA HIS HIS HIS HIS HIS HIS
SEQRES 34 A 433 HIS HIS HIS HIS
HET QGW A1201 25
HET NA A1202 1
HET CLR A1203 28
HET CLR A1204 28
HET CLR A1205 28
HET OLB A1206 15
HET OLA A1207 11
HET OLA A1208 12
HET OLA A1209 7
HET OLA A1210 15
HET OLA A1211 6
HET OLA A1212 7
HET OLA A1213 5
HET OLA A1214 7
HET OLA A1215 15
HET OLA A1216 11
HET OLA A1217 17
HET OLA A1218 10
HET OLA A1219 7
HET OLA A1220 5
HET OLC A1221 17
HETNAM QGW [2-METHYL-3-(4-METHYL-1,3-THIAZOL-2-YL)-4-
HETNAM 2 QGW OXIDANYLIDENE-6-PROPYL-CHROMEN-7-YL] ETHANOATE
HETNAM NA SODIUM ION
HETNAM CLR CHOLESTEROL
HETNAM OLB (2S)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE
HETNAM OLA OLEIC ACID
HETNAM OLC (2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE
HETSYN OLC 1-OLEOYL-R-GLYCEROL
FORMUL 2 QGW C19 H19 N O4 S
FORMUL 3 NA NA 1+
FORMUL 4 CLR 3(C27 H46 O)
FORMUL 7 OLB C21 H40 O4
FORMUL 8 OLA 14(C18 H34 O2)
FORMUL 22 OLC C21 H40 O4
FORMUL 23 HOH *89(H2 O)
HELIX 1 AA1 PRO A 1 ASN A 34 1 34
HELIX 2 AA2 SER A 35 GLN A 38 5 4
HELIX 3 AA3 ASN A 39 LEU A 58 1 20
HELIX 4 AA4 LEU A 58 SER A 67 1 10
HELIX 5 AA5 CYS A 74 ILE A 108 1 35
HELIX 6 AA6 ILE A 108 VAL A 116 1 9
HELIX 7 AA7 THR A 117 LEU A 137 1 21
HELIX 8 AA8 THR A 138 GLY A 142 5 5
HELIX 9 AA9 LYS A 150 GLN A 157 1 8
HELIX 10 AB1 LEU A 167 VAL A 172 1 6
HELIX 11 AB2 PRO A 173 TYR A 179 1 7
HELIX 12 AB3 VAL A 186 LYS A 1019 1 42
HELIX 13 AB4 ASN A 1022 ALA A 1043 1 22
HELIX 14 AB5 PHE A 1065 GLU A 1081 1 17
HELIX 15 AB6 LYS A 1083 GLN A 1093 1 11
HELIX 16 AB7 GLN A 1093 TYR A 1101 1 9
HELIX 17 AB8 TYR A 1101 CYS A 259 1 47
HELIX 18 AB9 PRO A 266 ILE A 292 1 27
HELIX 19 AC1 ILE A 292 SER A 305 1 14
SHEET 1 AA1 2 CYS A 71 ALA A 73 0
SHEET 2 AA1 2 GLN A 163 ALA A 165 -1 O VAL A 164 N ALA A 72
SSBOND 1 CYS A 71 CYS A 159 1555 1555 2.04
SSBOND 2 CYS A 74 CYS A 146 1555 1555 1.98
SSBOND 3 CYS A 77 CYS A 166 1555 1555 2.02
SSBOND 4 CYS A 259 CYS A 262 1555 1555 1.98
LINK OD1 ASP A 52 NA NA A1202 1555 1555 2.43
LINK OG SER A 91 NA NA A1202 1555 1555 2.72
LINK NA NA A1202 O HOH A1338 1555 1555 2.67
LINK NA NA A1202 O HOH A1354 1555 1555 2.82
SITE 1 AC1 13 TYR A 9 ALA A 63 ILE A 66 SER A 67
SITE 2 AC1 13 LEU A 85 LEU A 167 PHE A 168 MET A 177
SITE 3 AC1 13 LEU A 249 HIS A 250 ASN A 253 TYR A 271
SITE 4 AC1 13 HOH A1320
SITE 1 AC2 5 ASP A 52 SER A 91 ASN A 280 HOH A1338
SITE 2 AC2 5 HOH A1354
SITE 1 AC3 3 LEU A 247 PRO A 248 SER A 263
SITE 1 AC4 6 ALA A 72 ALA A 73 GLY A 76 ILE A 80
SITE 2 AC4 6 CLR A1205 OLB A1206
SITE 1 AC5 5 PHE A 255 CLR A1204 OLB A1206 OLA A1215
SITE 2 AC5 5 HOH A1312
SITE 1 AC6 3 PHE A 258 CLR A1204 CLR A1205
SITE 1 AC7 5 CYS A 28 VAL A 31 TRP A 32 VAL A 46
SITE 2 AC7 5 ALA A 50
SITE 1 AC8 5 THR A 65 THR A 68 PHE A 70 OLA A1215
SITE 2 AC8 5 OLA A1217
SITE 1 AC9 1 PRO A 266
SITE 1 AD1 2 SER A 7 THR A 11
SITE 1 AD2 1 TRP A 29
SITE 1 AD3 5 CYS A 71 CLR A1205 OLA A1208 OLA A1217
SITE 2 AD3 5 HOH A1318
SITE 1 AD4 3 GLY A 5 TYR A 271 HOH A1345
SITE 1 AD5 4 PHE A 255 CYS A 262 OLA A1208 OLA A1215
SITE 1 AD6 3 MET A 140 LEU A 141 TYR A 179
SITE 1 AD7 3 TYR A 43 ALA A 122 TRP A 129
CRYST1 39.414 179.833 140.085 90.00 90.00 90.00 C 2 2 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.025372 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005561 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007139 0.00000
ATOM 1 N ALA A 0 22.939 157.309 1.010 1.00 75.43 N
ANISOU 1 N ALA A 0 9679 9664 9319 -177 568 -95 N
ATOM 2 CA ALA A 0 23.695 158.361 0.351 1.00 75.87 C
ANISOU 2 CA ALA A 0 9763 9719 9343 -192 536 -90 C
ATOM 3 C ALA A 0 24.752 158.844 1.310 1.00 74.54 C
ANISOU 3 C ALA A 0 9577 9565 9178 -167 539 -59 C
ATOM 4 O ALA A 0 24.414 159.218 2.408 1.00 73.85 O
ANISOU 4 O ALA A 0 9466 9496 9099 -140 519 -49 O
ATOM 5 CB ALA A 0 22.774 159.488 -0.034 1.00 76.15 C
ANISOU 5 CB ALA A 0 9818 9762 9355 -198 469 -108 C
ATOM 6 N PRO A 1 26.025 158.827 0.884 1.00 74.01 N
ANISOU 6 N PRO A 1 9524 9491 9105 -179 565 -43 N
ATOM 7 CA PRO A 1 27.147 159.209 1.741 1.00 72.24 C
ANISOU 7 CA PRO A 1 9282 9281 8885 -158 571 -13 C
ATOM 8 C PRO A 1 26.894 160.508 2.473 1.00 70.04 C
ANISOU 8 C PRO A 1 8998 9025 8590 -139 515 -9 C
ATOM 9 O PRO A 1 26.451 161.501 1.933 1.00 70.19 O
ANISOU 9 O PRO A 1 9041 9045 8585 -151 468 -24 O
ATOM 10 CB PRO A 1 28.336 159.323 0.786 1.00 74.04 C
ANISOU 10 CB PRO A 1 9538 9494 9101 -182 591 -9 C
ATOM 11 CG PRO A 1 27.914 158.656 -0.460 1.00 76.25 C
ANISOU 11 CG PRO A 1 9845 9749 9377 -215 611 -33 C
ATOM 12 CD PRO A 1 26.423 158.738 -0.528 1.00 74.76 C
ANISOU 12 CD PRO A 1 9657 9564 9182 -216 576 -57 C
ATOM 13 N PRO A 2 27.156 160.470 3.761 1.00 67.80 N
ANISOU 13 N PRO A 2 8681 8761 8321 -110 522 13 N
ATOM 14 CA PRO A 2 26.939 161.606 4.628 1.00 65.30 C
ANISOU 14 CA PRO A 2 8353 8465 7992 -92 475 19 C
ATOM 15 C PRO A 2 27.818 162.789 4.268 1.00 62.93 C
ANISOU 15 C PRO A 2 8075 8171 7666 -101 448 24 C
ATOM 16 O PRO A 2 27.349 163.847 4.436 1.00 62.24 O
ANISOU 16 O PRO A 2 7994 8093 7561 -98 403 16 O
ATOM 17 CB PRO A 2 27.273 161.041 5.997 1.00 65.77 C
ANISOU 17 CB PRO A 2 8373 8541 8074 -62 503 44 C
ATOM 18 CG PRO A 2 26.910 159.613 5.888 1.00 67.26 C
ANISOU 18 CG PRO A 2 8551 8715 8290 -62 551 41 C
ATOM 19 CD PRO A 2 27.392 159.238 4.525 1.00 67.14 C
ANISOU 19 CD PRO A 2 8565 8677 8269 -92 574 31 C
ATOM 20 N ILE A 3 28.984 162.603 3.679 1.00 62.03 N
ANISOU 20 N ILE A 3 7973 8047 7548 -115 475 33 N
ATOM 21 CA ILE A 3 29.852 163.647 3.228 1.00 61.25 C
ANISOU 21 CA ILE A 3 7896 7949 7425 -127 455 36 C
ATOM 22 C ILE A 3 29.322 164.494 2.068 1.00 60.34 C
ANISOU 22 C ILE A 3 7824 7821 7282 -151 416 11 C
ATOM 23 O ILE A 3 29.911 165.461 1.773 1.00 60.43 O
ANISOU 23 O ILE A 3 7855 7834 7273 -159 396 12 O
ATOM 24 CB ILE A 3 31.201 163.066 2.816 1.00 62.50 C
ANISOU 24 CB ILE A 3 8058 8096 7593 -138 501 50 C
ATOM 25 CG1 ILE A 3 32.187 164.175 2.473 1.00 63.29 C
ANISOU 25 CG1 ILE A 3 8179 8199 7670 -148 482 53 C
ATOM 26 CG2 ILE A 3 31.013 162.077 1.686 1.00 64.14 C
ANISOU 26 CG2 ILE A 3 8288 8276 7809 -163 536 36 C
ATOM 27 CD1 ILE A 3 33.616 163.733 2.353 1.00 65.54 C
ANISOU 27 CD1 ILE A 3 8458 8477 7968 -153 526 72 C
ATOM 28 N MET A 4 28.273 164.126 1.374 1.00 59.21 N
ANISOU 28 N MET A 4 7695 7664 7137 -164 408 -10 N
ATOM 29 CA MET A 4 27.738 164.989 0.333 1.00 58.55 C
ANISOU 29 CA MET A 4 7651 7570 7026 -185 367 -31 C
ATOM 30 C MET A 4 26.669 165.930 0.832 1.00 56.43 C
ANISOU 30 C MET A 4 7376 7316 6749 -170 314 -39 C
ATOM 31 O MET A 4 26.705 167.100 0.584 1.00 56.54 O
ANISOU 31 O MET A 4 7410 7333 6740 -174 276 -42 O
ATOM 32 CB MET A 4 27.152 164.166 -0.798 1.00 59.99 C
ANISOU 32 CB MET A 4 7855 7731 7207 -211 381 -51 C
ATOM 33 CG MET A 4 28.075 163.127 -1.359 1.00 62.42 C
ANISOU 33 CG MET A 4 8170 8021 7526 -228 438 -46 C
ATOM 34 SD MET A 4 27.233 162.104 -2.534 1.00 66.50 S
ANISOU 34 SD MET A 4 8708 8514 8043 -259 457 -72 S
ATOM 35 CE MET A 4 26.743 163.317 -3.716 1.00 64.32 C
ANISOU 35 CE MET A 4 8481 8232 7725 -283 398 -93 C
ATOM 36 N GLY A 5 25.697 165.377 1.527 1.00 54.25 N
ANISOU 36 N GLY A 5 7073 7047 6494 -154 314 -42 N
ATOM 37 CA GLY A 5 24.809 166.154 2.331 1.00 51.73 C
ANISOU 37 CA GLY A 5 6737 6742 6175 -135 273 -45 C
ATOM 38 C GLY A 5 25.524 167.056 3.283 1.00 48.96 C
ANISOU 38 C GLY A 5 6373 6410 5819 -118 262 -27 C
ATOM 39 O GLY A 5 25.231 168.220 3.342 1.00 48.48 O
ANISOU 39 O GLY A 5 6322 6356 5742 -116 222 -30 O
ATOM 40 N SER A 6 26.531 166.557 4.008 1.00 47.03 N
ANISOU 40 N SER A 6 6106 6176 5587 -107 299 -6 N
ATOM 41 CA ASER A 6 27.430 167.395 4.852 0.38 45.97 C
ANISOU 41 CA ASER A 6 5961 6063 5445 -94 291 13 C
ATOM 42 CA BSER A 6 27.339 167.428 4.847 0.62 46.01 C
ANISOU 42 CA BSER A 6 5966 6067 5449 -94 289 11 C
ATOM 43 C SER A 6 28.308 168.576 4.281 1.00 45.64 C
ANISOU 43 C SER A 6 5947 6021 5375 -108 272 13 C
ATOM 44 O SER A 6 28.450 169.809 4.629 1.00 45.01 O
ANISOU 44 O SER A 6 5871 5952 5277 -104 241 14 O
ATOM 45 CB ASER A 6 28.445 166.583 5.658 0.38 46.91 C
ANISOU 45 CB ASER A 6 6050 6193 5581 -81 335 37 C
ATOM 46 CB BSER A 6 28.055 166.614 5.921 0.62 46.86 C
ANISOU 46 CB BSER A 6 6038 6189 5578 -76 328 35 C
ATOM 47 OG ASER A 6 27.845 165.906 6.729 0.38 48.00 O
ANISOU 47 OG ASER A 6 6155 6341 5742 -59 347 44 O
ATOM 48 OG BSER A 6 29.254 166.089 5.453 0.62 49.30 O
ANISOU 48 OG BSER A 6 6352 6491 5888 -85 364 47 O
ATOM 49 N SER A 7 28.697 168.274 3.046 1.00 45.54 N
ANISOU 49 N SER A 7 5964 5986 5352 -131 286 5 N
ATOM 50 CA ASER A 7 29.345 169.237 2.143 0.50 45.56 C
ANISOU 50 CA ASER A 7 6004 5980 5328 -150 270 -1 C
ATOM 51 CA BSER A 7 29.386 169.267 2.232 0.50 45.52 C
ANISOU 51 CA BSER A 7 5997 5976 5324 -148 270 0 C
ATOM 52 C SER A 7 28.669 170.581 1.629 1.00 43.62 C
ANISOU 52 C SER A 7 5787 5730 5056 -157 218 -17 C
ATOM 53 O SER A 7 29.049 171.801 1.658 1.00 43.98 O
ANISOU 53 O SER A 7 5847 5782 5082 -157 195 -16 O
ATOM 54 CB ASER A 7 29.896 168.544 0.905 0.50 49.43 C
ANISOU 54 CB ASER A 7 6523 6445 5815 -175 300 -8 C
ATOM 55 CB BSER A 7 30.266 168.602 1.185 0.50 49.31 C
ANISOU 55 CB BSER A 7 6500 6435 5802 -171 306 -1 C
ATOM 56 OG ASER A 7 31.096 167.883 1.203 0.50 53.62 O
ANISOU 56 OG ASER A 7 7037 6977 6361 -173 344 9 O
ATOM 57 OG BSER A 7 29.471 168.036 0.193 0.50 53.98 O
ANISOU 57 OG BSER A 7 7113 7006 6391 -189 305 -19 O
ATOM 58 N VAL A 8 27.395 170.374 1.349 1.00 41.72 N
ANISOU 58 N VAL A 8 5550 5484 4819 -157 197 -30 N
ATOM 59 CA VAL A 8 26.487 171.478 1.114 1.00 40.65 C
ANISOU 59 CA VAL A 8 5430 5348 4667 -157 148 -42 C
ATOM 60 C VAL A 8 26.249 172.352 2.347 1.00 39.05 C
ANISOU 60 C VAL A 8 5202 5167 4470 -134 126 -34 C
ATOM 61 O VAL A 8 26.373 173.535 2.287 1.00 39.11 O
ANISOU 61 O VAL A 8 5225 5177 4459 -135 100 -35 O
ATOM 62 CB VAL A 8 25.151 171.014 0.566 1.00 41.63 C
ANISOU 62 CB VAL A 8 5560 5462 4797 -162 129 -58 C
ATOM 63 CG1 VAL A 8 24.217 172.169 0.380 1.00 41.20 C
ANISOU 63 CG1 VAL A 8 5517 5407 4728 -159 78 -67 C
ATOM 64 CG2 VAL A 8 25.323 170.250 -0.706 1.00 43.35 C
ANISOU 64 CG2 VAL A 8 5806 5659 5006 -188 148 -69 C
ATOM 65 N TYR A 9 25.887 171.722 3.450 1.00 37.10 N
ANISOU 65 N TYR A 9 4917 4933 4247 -116 140 -27 N
ATOM 66 CA TYR A 9 25.745 172.381 4.700 1.00 35.12 C
ANISOU 66 CA TYR A 9 4641 4702 4003 -96 127 -18 C
ATOM 67 C TYR A 9 26.990 173.172 5.088 1.00 33.50 C
ANISOU 67 C TYR A 9 4436 4510 3782 -96 133 -5 C
ATOM 68 O TYR A 9 26.887 174.304 5.423 1.00 33.01 O
ANISOU 68 O TYR A 9 4378 4456 3708 -93 108 -7 O
ATOM 69 CB TYR A 9 25.301 171.388 5.780 1.00 34.90 C
ANISOU 69 CB TYR A 9 4574 4684 4003 -78 148 -11 C
ATOM 70 CG TYR A 9 25.491 171.917 7.141 1.00 33.67 C
ANISOU 70 CG TYR A 9 4390 4550 3851 -60 145 1 C
ATOM 71 CD1 TYR A 9 24.666 172.892 7.637 1.00 33.61 C
ANISOU 71 CD1 TYR A 9 4380 4547 3843 -53 112 -5 C
ATOM 72 CD2 TYR A 9 26.534 171.503 7.908 1.00 33.13 C
ANISOU 72 CD2 TYR A 9 4302 4499 3788 -53 175 20 C
ATOM 73 CE1 TYR A 9 24.875 173.418 8.857 1.00 33.45 C
ANISOU 73 CE1 TYR A 9 4338 4547 3824 -41 111 5 C
ATOM 74 CE2 TYR A 9 26.728 172.020 9.133 1.00 33.24 C
ANISOU 74 CE2 TYR A 9 4293 4535 3803 -39 171 31 C
ATOM 75 CZ TYR A 9 25.892 172.969 9.589 1.00 34.30 C
ANISOU 75 CZ TYR A 9 4425 4672 3933 -34 140 23 C
ATOM 76 OH TYR A 9 26.135 173.491 10.766 1.00 36.38 O
ANISOU 76 OH TYR A 9 4669 4957 4196 -24 138 33 O
ATOM 77 N ILE A 10 28.145 172.546 5.012 1.00 32.72 N
ANISOU 77 N ILE A 10 4334 4413 3684 -101 168 6 N
ATOM 78 CA ILE A 10 29.402 173.143 5.377 1.00 32.47 C
ANISOU 78 CA ILE A 10 4300 4395 3641 -102 178 18 C
ATOM 79 C ILE A 10 29.790 174.300 4.483 1.00 33.37 C
ANISOU 79 C ILE A 10 4453 4499 3729 -118 158 8 C
ATOM 80 O ILE A 10 30.213 175.288 4.969 1.00 33.75 O
ANISOU 80 O ILE A 10 4499 4560 3765 -115 146 11 O
ATOM 81 CB ILE A 10 30.549 172.111 5.435 1.00 33.50 C
ANISOU 81 CB ILE A 10 4417 4527 3784 -103 222 33 C
ATOM 82 CG1 ILE A 10 30.443 171.251 6.665 1.00 34.74 C
ANISOU 82 CG1 ILE A 10 4532 4702 3965 -82 242 49 C
ATOM 83 CG2 ILE A 10 31.886 172.758 5.572 1.00 33.13 C
ANISOU 83 CG2 ILE A 10 4373 4491 3725 -107 231 42 C
ATOM 84 CD1 ILE A 10 31.228 169.985 6.578 1.00 36.41 C
ANISOU 84 CD1 ILE A 10 4730 4909 4194 -82 287 63 C
ATOM 85 N THR A 11 29.627 174.166 3.177 1.00 33.29 N
ANISOU 85 N THR A 11 4478 4464 3708 -136 154 -5 N
ATOM 86 CA THR A 11 29.962 175.229 2.254 1.00 33.77 C
ANISOU 86 CA THR A 11 4578 4511 3741 -151 136 -14 C
ATOM 87 C THR A 11 29.126 176.467 2.548 1.00 32.51 C
ANISOU 87 C THR A 11 4423 4358 3571 -144 95 -20 C
ATOM 88 O THR A 11 29.625 177.544 2.590 1.00 32.29 O
ANISOU 88 O THR A 11 4408 4335 3527 -146 86 -21 O
ATOM 89 CB THR A 11 29.800 174.791 0.794 1.00 36.60 C
ANISOU 89 CB THR A 11 4974 4842 4089 -173 138 -26 C
ATOM 90 OG1 THR A 11 30.639 173.675 0.557 1.00 37.76 O
ANISOU 90 OG1 THR A 11 5117 4983 4248 -182 181 -20 O
ATOM 91 CG2 THR A 11 30.163 175.865 -0.119 1.00 37.43 C
ANISOU 91 CG2 THR A 11 5122 4935 4166 -188 121 -35 C
ATOM 92 N VAL A 12 27.847 176.255 2.772 1.00 31.57 N
ANISOU 92 N VAL A 12 4291 4239 3464 -134 74 -25 N
ATOM 93 CA VAL A 12 26.917 177.293 3.106 1.00 31.24 C
ANISOU 93 CA VAL A 12 4249 4201 3419 -125 38 -30 C
ATOM 94 C VAL A 12 27.309 177.969 4.414 1.00 30.37 C
ANISOU 94 C VAL A 12 4113 4115 3314 -112 40 -21 C
ATOM 95 O VAL A 12 27.293 179.153 4.481 1.00 31.12 O
ANISOU 95 O VAL A 12 4219 4211 3395 -112 21 -24 O
ATOM 96 CB VAL A 12 25.485 176.775 3.152 1.00 32.12 C
ANISOU 96 CB VAL A 12 4348 4308 3550 -117 19 -38 C
ATOM 97 CG1 VAL A 12 24.562 177.780 3.786 1.00 32.00 C
ANISOU 97 CG1 VAL A 12 4322 4298 3538 -105 -13 -40 C
ATOM 98 CG2 VAL A 12 25.009 176.422 1.769 1.00 33.74 C
ANISOU 98 CG2 VAL A 12 4585 4491 3744 -134 7 -49 C
ATOM 99 N GLU A 13 27.682 177.194 5.422 1.00 28.58 N
ANISOU 99 N GLU A 13 3850 3905 3104 -101 66 -10 N
ATOM 100 CA GLU A 13 28.103 177.741 6.686 1.00 27.48 C
ANISOU 100 CA GLU A 13 3685 3790 2967 -90 70 0 C
ATOM 101 C GLU A 13 29.318 178.618 6.488 1.00 28.41 C
ANISOU 101 C GLU A 13 3819 3913 3062 -101 76 2 C
ATOM 102 O GLU A 13 29.398 179.659 7.048 1.00 27.78 O
ANISOU 102 O GLU A 13 3737 3845 2974 -99 65 1 O
ATOM 103 CB GLU A 13 28.424 176.650 7.690 1.00 27.98 C
ANISOU 103 CB GLU A 13 3711 3870 3049 -78 98 14 C
ATOM 104 CG GLU A 13 27.217 175.966 8.272 1.00 29.73 C
ANISOU 104 CG GLU A 13 3910 4092 3295 -64 94 12 C
ATOM 105 CD GLU A 13 26.592 176.713 9.421 1.00 34.42 C
ANISOU 105 CD GLU A 13 4484 4700 3893 -53 77 13 C
ATOM 106 OE1 GLU A 13 26.408 176.120 10.457 1.00 33.86 O
ANISOU 106 OE1 GLU A 13 4384 4643 3839 -40 90 21 O
ATOM 107 OE2 GLU A 13 26.280 177.880 9.294 1.00 34.18 O
ANISOU 107 OE2 GLU A 13 4469 4667 3852 -57 52 5 O
ATOM 108 N LEU A 14 30.252 178.171 5.665 1.00 29.30 N
ANISOU 108 N LEU A 14 3950 4016 3168 -113 97 3 N
ATOM 109 CA LEU A 14 31.435 178.952 5.399 1.00 31.29 C
ANISOU 109 CA LEU A 14 4219 4270 3400 -124 106 2 C
ATOM 110 C LEU A 14 31.136 180.243 4.640 1.00 31.47 C
ANISOU 110 C LEU A 14 4279 4278 3401 -133 79 -11 C
ATOM 111 O LEU A 14 31.707 181.219 4.918 1.00 32.27 O
ANISOU 111 O LEU A 14 4384 4387 3489 -136 78 -13 O
ATOM 112 CB LEU A 14 32.541 178.143 4.748 1.00 33.61 C
ANISOU 112 CB LEU A 14 4521 4554 3695 -135 138 7 C
ATOM 113 CG LEU A 14 33.017 176.928 5.503 1.00 35.87 C
ANISOU 113 CG LEU A 14 4770 4855 4003 -125 168 23 C
ATOM 114 CD1 LEU A 14 33.817 176.002 4.626 1.00 38.08 C
ANISOU 114 CD1 LEU A 14 5063 5118 4289 -137 199 25 C
ATOM 115 CD2 LEU A 14 33.759 177.316 6.747 1.00 35.57 C
ANISOU 115 CD2 LEU A 14 4700 4848 3967 -116 175 35 C
ATOM 116 N ALA A 15 30.207 180.223 3.715 1.00 31.20 N
ANISOU 116 N ALA A 15 4270 4221 3362 -138 58 -20 N
ATOM 117 CA ALA A 15 29.819 181.403 2.992 1.00 31.54 C
ANISOU 117 CA ALA A 15 4348 4250 3386 -144 32 -30 C
ATOM 118 C ALA A 15 29.234 182.439 3.968 1.00 30.40 C
ANISOU 118 C ALA A 15 4186 4121 3245 -132 12 -30 C
ATOM 119 O ALA A 15 29.540 183.602 3.888 1.00 29.98 O
ANISOU 119 O ALA A 15 4150 4066 3175 -136 5 -34 O
ATOM 120 CB ALA A 15 28.818 181.039 1.941 1.00 31.99 C
ANISOU 120 CB ALA A 15 4428 4284 3441 -149 11 -38 C
ATOM 121 N ILE A 16 28.398 181.962 4.888 1.00 29.20 N
ANISOU 121 N ILE A 16 4000 3981 3115 -118 6 -26 N
ATOM 122 CA ILE A 16 27.771 182.768 5.923 1.00 28.50 C
ANISOU 122 CA ILE A 16 3890 3905 3033 -106 -8 -25 C
ATOM 123 C ILE A 16 28.806 183.405 6.849 1.00 28.69 C
ANISOU 123 C ILE A 16 3900 3952 3050 -108 10 -20 C
ATOM 124 O ILE A 16 28.745 184.572 7.085 1.00 28.50 O
ANISOU 124 O ILE A 16 3883 3930 3016 -109 0 -25 O
ATOM 125 CB ILE A 16 26.698 182.001 6.716 1.00 27.99 C
ANISOU 125 CB ILE A 16 3793 3846 2995 -92 -14 -22 C
ATOM 126 CG1 ILE A 16 25.504 181.705 5.832 1.00 29.83 C
ANISOU 126 CG1 ILE A 16 4042 4058 3236 -92 -39 -30 C
ATOM 127 CG2 ILE A 16 26.237 182.789 7.918 1.00 26.48 C
ANISOU 127 CG2 ILE A 16 3578 3669 2812 -83 -22 -21 C
ATOM 128 CD1 ILE A 16 24.745 180.478 6.215 1.00 31.21 C
ANISOU 128 CD1 ILE A 16 4189 4233 3436 -82 -33 -29 C
ATOM 129 N ALA A 17 29.753 182.614 7.338 1.00 28.74 N
ANISOU 129 N ALA A 17 3885 3974 3059 -108 37 -11 N
ATOM 130 CA ALA A 17 30.812 183.102 8.183 1.00 28.96 C
ANISOU 130 CA ALA A 17 3897 4027 3080 -110 54 -6 C
ATOM 131 C ALA A 17 31.593 184.239 7.513 1.00 31.04 C
ANISOU 131 C ALA A 17 4192 4282 3318 -124 54 -16 C
ATOM 132 O ALA A 17 31.813 185.237 8.118 1.00 31.47 O
ANISOU 132 O ALA A 17 4242 4350 3364 -126 53 -19 O
ATOM 133 CB ALA A 17 31.719 181.986 8.585 1.00 28.46 C
ANISOU 133 CB ALA A 17 3810 3980 3025 -108 81 6 C
ATOM 134 N VAL A 18 31.978 184.064 6.256 1.00 32.14 N
ANISOU 134 N VAL A 18 4365 4399 3448 -134 58 -21 N
ATOM 135 CA VAL A 18 32.697 185.054 5.482 1.00 32.79 C
ANISOU 135 CA VAL A 18 4481 4469 3507 -148 61 -30 C
ATOM 136 C VAL A 18 31.948 186.352 5.462 1.00 32.13 C
ANISOU 136 C VAL A 18 4415 4380 3415 -146 38 -38 C
ATOM 137 O VAL A 18 32.475 187.362 5.777 1.00 31.72 O
ANISOU 137 O VAL A 18 4367 4336 3351 -151 44 -43 O
ATOM 138 CB VAL A 18 32.918 184.613 4.026 1.00 34.92 C
ANISOU 138 CB VAL A 18 4790 4711 3768 -159 64 -35 C
ATOM 139 CG1 VAL A 18 33.460 185.752 3.214 1.00 35.41 C
ANISOU 139 CG1 VAL A 18 4893 4756 3806 -172 63 -47 C
ATOM 140 CG2 VAL A 18 33.882 183.462 3.947 1.00 36.53 C
ANISOU 140 CG2 VAL A 18 4982 4918 3981 -164 93 -28 C
ATOM 141 N LEU A 19 30.697 186.284 5.074 1.00 31.95 N
ANISOU 141 N LEU A 19 4400 4340 3398 -139 12 -40 N
ATOM 142 CA LEU A 19 29.856 187.437 5.018 1.00 32.28 C
ANISOU 142 CA LEU A 19 4456 4373 3436 -136 -11 -45 C
ATOM 143 C LEU A 19 29.585 188.094 6.394 1.00 31.56 C
ANISOU 143 C LEU A 19 4334 4305 3355 -128 -10 -43 C
ATOM 144 O LEU A 19 29.525 189.289 6.489 1.00 31.78 O
ANISOU 144 O LEU A 19 4373 4329 3373 -131 -14 -49 O
ATOM 145 CB LEU A 19 28.562 187.124 4.287 1.00 32.90 C
ANISOU 145 CB LEU A 19 4547 4430 3522 -130 -40 -45 C
ATOM 146 CG LEU A 19 28.664 186.768 2.804 1.00 35.31 C
ANISOU 146 CG LEU A 19 4893 4712 3813 -141 -46 -49 C
ATOM 147 CD1 LEU A 19 27.375 186.199 2.276 1.00 36.21 C
ANISOU 147 CD1 LEU A 19 5010 4812 3938 -135 -73 -49 C
ATOM 148 CD2 LEU A 19 29.184 187.880 1.936 1.00 36.21 C
ANISOU 148 CD2 LEU A 19 5049 4808 3900 -151 -47 -56 C
ATOM 149 N ALA A 20 29.459 187.294 7.436 1.00 29.85 N
ANISOU 149 N ALA A 20 4078 4108 3155 -121 -2 -36 N
ATOM 150 CA ALA A 20 29.189 187.805 8.769 1.00 29.14 C
ANISOU 150 CA ALA A 20 3958 4039 3075 -116 0 -34 C
ATOM 151 C ALA A 20 30.355 188.610 9.259 1.00 29.47 C
ANISOU 151 C ALA A 20 3998 4099 3099 -126 20 -37 C
ATOM 152 O ALA A 20 30.191 189.639 9.822 1.00 29.58 O
ANISOU 152 O ALA A 20 4011 4120 3110 -129 19 -42 O
ATOM 153 CB ALA A 20 28.910 186.679 9.727 1.00 27.87 C
ANISOU 153 CB ALA A 20 3759 3895 2934 -106 6 -25 C
ATOM 154 N ILE A 21 31.536 188.088 9.031 1.00 29.19 N
ANISOU 154 N ILE A 21 3964 4073 3055 -133 39 -35 N
ATOM 155 CA ILE A 21 32.755 188.721 9.413 1.00 30.63 C
ANISOU 155 CA ILE A 21 4143 4274 3221 -144 60 -39 C
ATOM 156 C ILE A 21 32.972 190.034 8.665 1.00 32.14 C
ANISOU 156 C ILE A 21 4372 4448 3393 -154 58 -52 C
ATOM 157 O ILE A 21 33.173 191.047 9.255 1.00 32.24 O
ANISOU 157 O ILE A 21 4380 4472 3398 -160 65 -59 O
ATOM 158 CB ILE A 21 33.936 187.770 9.233 1.00 32.19 C
ANISOU 158 CB ILE A 21 4333 4481 3417 -148 80 -32 C
ATOM 159 CG1 ILE A 21 33.924 186.700 10.297 1.00 32.23 C
ANISOU 159 CG1 ILE A 21 4295 4511 3439 -138 87 -18 C
ATOM 160 CG2 ILE A 21 35.235 188.522 9.301 1.00 34.16 C
ANISOU 160 CG2 ILE A 21 4587 4743 3649 -162 100 -40 C
ATOM 161 CD1 ILE A 21 34.640 185.448 9.916 1.00 33.72 C
ANISOU 161 CD1 ILE A 21 4477 4699 3635 -137 103 -8 C
ATOM 162 N LEU A 22 32.857 189.981 7.352 1.00 33.12 N
ANISOU 162 N LEU A 22 4532 4542 3510 -157 50 -56 N
ATOM 163 CA LEU A 22 33.070 191.117 6.493 1.00 33.91 C
ANISOU 163 CA LEU A 22 4672 4622 3591 -165 50 -67 C
ATOM 164 C LEU A 22 32.169 192.287 6.782 1.00 33.77 C
ANISOU 164 C LEU A 22 4659 4597 3573 -161 35 -71 C
ATOM 165 O LEU A 22 32.624 193.358 6.998 1.00 34.00 O
ANISOU 165 O LEU A 22 4697 4632 3591 -169 48 -80 O
ATOM 166 CB LEU A 22 32.957 190.712 5.025 1.00 35.35 C
ANISOU 166 CB LEU A 22 4893 4772 3765 -168 41 -68 C
ATOM 167 CG LEU A 22 34.049 189.873 4.371 1.00 38.86 C
ANISOU 167 CG LEU A 22 5348 5213 4205 -178 61 -68 C
ATOM 168 CD1 LEU A 22 33.778 189.676 2.907 1.00 39.86 C
ANISOU 168 CD1 LEU A 22 5518 5306 4321 -183 50 -72 C
ATOM 169 CD2 LEU A 22 35.395 190.504 4.541 1.00 41.14 C
ANISOU 169 CD2 LEU A 22 5640 5512 4480 -190 88 -77 C
ATOM 170 N GLY A 23 30.882 192.052 6.791 1.00 32.70 N
ANISOU 170 N GLY A 23 4518 4452 3453 -149 11 -65 N
ATOM 171 CA GLY A 23 29.943 193.102 7.017 1.00 32.65 C
ANISOU 171 CA GLY A 23 4516 4437 3453 -144 -3 -68 C
ATOM 172 C GLY A 23 30.071 193.708 8.374 1.00 32.43 C
ANISOU 172 C GLY A 23 4459 4434 3430 -147 12 -70 C
ATOM 173 O GLY A 23 30.027 194.881 8.507 1.00 33.45 O
ANISOU 173 O GLY A 23 4598 4558 3552 -152 18 -77 O
ATOM 174 N ASN A 24 30.252 192.877 9.367 1.00 30.64 N
ANISOU 174 N ASN A 24 4195 4233 3214 -145 20 -64 N
ATOM 175 CA ASN A 24 30.356 193.350 10.717 1.00 30.23 C
ANISOU 175 CA ASN A 24 4114 4206 3166 -149 34 -66 C
ATOM 176 C ASN A 24 31.673 194.011 11.093 1.00 32.17 C
ANISOU 176 C ASN A 24 4359 4473 3391 -165 60 -75 C
ATOM 177 O ASN A 24 31.707 194.820 11.971 1.00 32.62 O
ANISOU 177 O ASN A 24 4403 4545 3446 -173 71 -80 O
ATOM 178 CB ASN A 24 29.869 192.305 11.698 1.00 28.31 C
ANISOU 178 CB ASN A 24 3834 3982 2943 -141 30 -56 C
ATOM 179 CG ASN A 24 28.395 192.103 11.588 1.00 28.70 C
ANISOU 179 CG ASN A 24 3881 4010 3014 -127 7 -53 C
ATOM 180 OD1 ASN A 24 27.655 192.909 12.013 1.00 28.33 O
ANISOU 180 OD1 ASN A 24 3832 3957 2977 -127 2 -57 O
ATOM 181 ND2 ASN A 24 27.988 191.062 10.960 1.00 29.22 N
ANISOU 181 ND2 ASN A 24 3949 4064 3090 -118 -7 -47 N
ATOM 182 N VAL A 25 32.751 193.648 10.426 1.00 33.40 N
ANISOU 182 N VAL A 25 4528 4629 3533 -171 71 -76 N
ATOM 183 CA VAL A 25 34.002 194.351 10.590 1.00 35.83 C
ANISOU 183 CA VAL A 25 4841 4953 3822 -186 95 -87 C
ATOM 184 C VAL A 25 33.893 195.759 10.037 1.00 37.72 C
ANISOU 184 C VAL A 25 5113 5171 4048 -193 99 -100 C
ATOM 185 O VAL A 25 34.448 196.653 10.552 1.00 38.97 O
ANISOU 185 O VAL A 25 5268 5343 4196 -205 118 -110 O
ATOM 186 CB VAL A 25 35.167 193.602 9.958 1.00 36.93 C
ANISOU 186 CB VAL A 25 4986 5094 3953 -191 108 -86 C
ATOM 187 CG1 VAL A 25 36.334 194.519 9.734 1.00 38.22 C
ANISOU 187 CG1 VAL A 25 5165 5260 4095 -207 131 -100 C
ATOM 188 CG2 VAL A 25 35.541 192.395 10.765 1.00 36.79 C
ANISOU 188 CG2 VAL A 25 4929 5103 3945 -187 112 -73 C
ATOM 189 N LEU A 26 33.108 195.914 9.003 1.00 37.38 N
ANISOU 189 N LEU A 26 5101 5095 4008 -185 81 -98 N
ATOM 190 CA LEU A 26 32.853 197.185 8.424 1.00 38.36 C
ANISOU 190 CA LEU A 26 5258 5196 4122 -188 82 -107 C
ATOM 191 C LEU A 26 31.955 198.083 9.265 1.00 37.64 C
ANISOU 191 C LEU A 26 5152 5106 4041 -186 81 -108 C
ATOM 192 O LEU A 26 32.156 199.243 9.313 1.00 37.71 O
ANISOU 192 O LEU A 26 5176 5112 4042 -194 96 -118 O
ATOM 193 CB LEU A 26 32.283 196.975 7.038 1.00 39.53 C
ANISOU 193 CB LEU A 26 5443 5310 4268 -179 61 -102 C
ATOM 194 CG LEU A 26 31.955 198.115 6.104 1.00 43.40 C
ANISOU 194 CG LEU A 26 5975 5769 4747 -179 56 -107 C
ATOM 195 CD1 LEU A 26 33.209 198.799 5.633 1.00 44.93 C
ANISOU 195 CD1 LEU A 26 6195 5958 4916 -193 84 -121 C
ATOM 196 CD2 LEU A 26 31.146 197.628 4.928 1.00 44.62 C
ANISOU 196 CD2 LEU A 26 6156 5895 4903 -168 27 -99 C
ATOM 197 N VAL A 27 30.962 197.530 9.922 1.00 36.52 N
ANISOU 197 N VAL A 27 4984 4970 3921 -176 64 -99 N
ATOM 198 CA VAL A 27 30.233 198.256 10.921 1.00 36.30 C
ANISOU 198 CA VAL A 27 4937 4949 3907 -176 68 -100 C
ATOM 199 C VAL A 27 31.195 198.826 11.962 1.00 37.29 C
ANISOU 199 C VAL A 27 5044 5104 4019 -194 98 -111 C
ATOM 200 O VAL A 27 31.173 199.986 12.209 1.00 37.25 O
ANISOU 200 O VAL A 27 5047 5096 4011 -203 114 -121 O
ATOM 201 CB VAL A 27 29.133 197.394 11.579 1.00 35.66 C
ANISOU 201 CB VAL A 27 4825 4870 3852 -164 48 -89 C
ATOM 202 CG1 VAL A 27 28.490 198.099 12.728 1.00 35.24 C
ANISOU 202 CG1 VAL A 27 4751 4825 3813 -168 57 -92 C
ATOM 203 CG2 VAL A 27 28.093 197.002 10.580 1.00 35.94 C
ANISOU 203 CG2 VAL A 27 4879 4876 3901 -148 19 -81 C
ATOM 204 N CYS A 28 32.040 197.974 12.529 1.00 37.60 N
ANISOU 204 N CYS A 28 5060 5174 4054 -199 106 -109 N
ATOM 205 CA CYS A 28 32.908 198.295 13.634 1.00 38.98 C
ANISOU 205 CA CYS A 28 5210 5384 4217 -216 130 -117 C
ATOM 206 C CYS A 28 33.941 199.275 13.224 1.00 41.87 C
ANISOU 206 C CYS A 28 5597 5749 4561 -231 153 -132 C
ATOM 207 O CYS A 28 34.242 200.196 13.926 1.00 42.03 O
ANISOU 207 O CYS A 28 5611 5784 4572 -246 174 -144 O
ATOM 208 CB CYS A 28 33.603 197.070 14.155 1.00 38.40 C
ANISOU 208 CB CYS A 28 5107 5340 4143 -215 130 -107 C
ATOM 209 SG CYS A 28 32.604 195.962 15.075 1.00 36.98 S
ANISOU 209 SG CYS A 28 4893 5171 3986 -202 113 -91 S
ATOM 210 N TRP A 29 34.441 199.128 12.005 1.00 43.97 N
ANISOU 210 N TRP A 29 5894 5996 4818 -228 151 -134 N
ATOM 211 CA ATRP A 29 35.359 200.104 11.393 0.50 47.59 C
ANISOU 211 CA ATRP A 29 6381 6445 5255 -241 174 -150 C
ATOM 212 CA BTRP A 29 35.315 200.111 11.349 0.50 47.59 C
ANISOU 212 CA BTRP A 29 6382 6443 5256 -240 173 -150 C
ATOM 213 C TRP A 29 34.871 201.611 11.028 1.00 47.40 C
ANISOU 213 C TRP A 29 6388 6395 5227 -244 184 -161 C
ATOM 214 O TRP A 29 35.296 202.748 11.431 1.00 48.17 O
ANISOU 214 O TRP A 29 6489 6499 5314 -260 211 -177 O
ATOM 215 CB ATRP A 29 36.111 199.387 10.241 0.50 50.53 C
ANISOU 215 CB ATRP A 29 6776 6804 5620 -238 171 -149 C
ATOM 216 CB BTRP A 29 35.890 199.494 10.077 0.50 50.58 C
ANISOU 216 CB BTRP A 29 6789 6803 5627 -236 168 -148 C
ATOM 217 CG ATRP A 29 37.335 200.020 9.656 0.50 56.09 C
ANISOU 217 CG ATRP A 29 7504 7503 6303 -252 197 -165 C
ATOM 218 CG BTRP A 29 37.105 200.159 9.579 0.50 55.82 C
ANISOU 218 CG BTRP A 29 7475 7464 6271 -250 194 -165 C
ATOM 219 CD1ATRP A 29 38.080 201.006 10.196 0.50 59.05 C
ANISOU 219 CD1ATRP A 29 7876 7895 6666 -269 225 -183 C
ATOM 220 CD1BTRP A 29 37.271 200.795 8.397 0.50 58.24 C
ANISOU 220 CD1BTRP A 29 7827 7738 6565 -251 200 -173 C
ATOM 221 CD2ATRP A 29 37.980 199.670 8.419 0.50 58.58 C
ANISOU 221 CD2ATRP A 29 7852 7796 6610 -252 199 -168 C
ATOM 222 CD2BTRP A 29 38.363 200.229 10.246 0.50 58.55 C
ANISOU 222 CD2BTRP A 29 7799 7841 6605 -267 219 -176 C
ATOM 223 NE1ATRP A 29 39.119 201.323 9.377 0.50 60.91 N
ANISOU 223 NE1ATRP A 29 8139 8119 6886 -278 244 -196 N
ATOM 224 NE1BTRP A 29 38.552 201.248 8.276 0.50 60.01 N
ANISOU 224 NE1BTRP A 29 8059 7968 6773 -267 229 -190 N
ATOM 225 CE2ATRP A 29 39.084 200.517 8.275 0.50 61.06 C
ANISOU 225 CE2ATRP A 29 8181 8113 6908 -268 229 -187 C
ATOM 226 CE2BTRP A 29 39.237 200.930 9.414 0.50 60.64 C
ANISOU 226 CE2BTRP A 29 8097 8089 6854 -277 241 -193 C
ATOM 227 CE3ATRP A 29 37.722 198.723 7.415 0.50 59.93 C
ANISOU 227 CE3ATRP A 29 8042 7944 6786 -242 180 -157 C
ATOM 228 CE3BTRP A 29 38.832 199.772 11.477 0.50 60.37 C
ANISOU 228 CE3BTRP A 29 7985 8114 6839 -274 225 -173 C
ATOM 229 CZ2ATRP A 29 39.937 200.452 7.179 0.50 63.33 C
ANISOU 229 CZ2ATRP A 29 8501 8378 7183 -274 241 -196 C
ATOM 230 CZ2BTRP A 29 40.553 201.190 9.771 0.50 63.03 C
ANISOU 230 CZ2BTRP A 29 8388 8415 7145 -294 268 -208 C
ATOM 231 CZ3ATRP A 29 38.569 198.657 6.331 0.50 62.20 C
ANISOU 231 CZ3ATRP A 29 8362 8211 7061 -248 192 -165 C
ATOM 232 CZ3BTRP A 29 40.134 200.029 11.823 0.50 62.75 C
ANISOU 232 CZ3BTRP A 29 8275 8439 7126 -291 249 -187 C
ATOM 233 CH2ATRP A 29 39.661 199.520 6.218 0.50 63.44 C
ANISOU 233 CH2ATRP A 29 8534 8369 7202 -264 223 -184 C
ATOM 234 CH2BTRP A 29 40.979 200.730 10.978 0.50 63.65 C
ANISOU 234 CH2BTRP A 29 8421 8536 7227 -301 271 -205 C
ATOM 235 N ALA A 30 33.620 201.602 10.631 1.00 46.29 N
ANISOU 235 N ALA A 30 6258 6228 5102 -229 161 -150 N
ATOM 236 CA ALA A 30 32.816 202.774 10.506 1.00 46.66 C
ANISOU 236 CA ALA A 30 6322 6251 5154 -227 164 -153 C
ATOM 237 C ALA A 30 32.561 203.515 11.804 1.00 47.66 C
ANISOU 237 C ALA A 30 6423 6397 5288 -238 183 -160 C
ATOM 238 O ALA A 30 32.571 204.701 11.833 1.00 48.32 O
ANISOU 238 O ALA A 30 6522 6471 5368 -246 205 -171 O
ATOM 239 CB ALA A 30 31.517 202.430 9.836 1.00 46.08 C
ANISOU 239 CB ALA A 30 6260 6149 5098 -206 131 -138 C
ATOM 240 N VAL A 31 32.297 202.808 12.874 1.00 47.36 N
ANISOU 240 N VAL A 31 6347 6385 5262 -239 177 -154 N
ATOM 241 CA VAL A 31 32.061 203.464 14.130 1.00 48.11 C
ANISOU 241 CA VAL A 31 6418 6498 5363 -252 196 -161 C
ATOM 242 C VAL A 31 33.365 204.004 14.667 1.00 50.70 C
ANISOU 242 C VAL A 31 6740 6857 5668 -276 229 -179 C
ATOM 243 O VAL A 31 33.394 205.070 15.166 1.00 50.96 O
ANISOU 243 O VAL A 31 6774 6892 5697 -291 254 -192 O
ATOM 244 CB VAL A 31 31.320 202.569 15.139 1.00 47.18 C
ANISOU 244 CB VAL A 31 6264 6398 5265 -247 180 -150 C
ATOM 245 CG1 VAL A 31 31.209 203.241 16.473 1.00 47.57 C
ANISOU 245 CG1 VAL A 31 6290 6467 5316 -265 203 -159 C
ATOM 246 CG2 VAL A 31 29.933 202.265 14.645 1.00 46.52 C
ANISOU 246 CG2 VAL A 31 6186 6281 5206 -225 152 -136 C
ATOM 247 N TRP A 32 34.449 203.277 14.497 1.00 52.33 N
ANISOU 247 N TRP A 32 6941 7083 5859 -280 229 -180 N
ATOM 248 CA TRP A 32 35.749 203.766 14.874 1.00 55.23 C
ANISOU 248 CA TRP A 32 7303 7478 6205 -301 258 -197 C
ATOM 249 C TRP A 32 36.166 205.071 14.187 1.00 56.36 C
ANISOU 249 C TRP A 32 7481 7600 6335 -311 284 -216 C
ATOM 250 O TRP A 32 36.722 205.927 14.807 1.00 56.96 O
ANISOU 250 O TRP A 32 7550 7693 6398 -332 314 -233 O
ATOM 251 CB TRP A 32 36.794 202.707 14.658 1.00 56.79 C
ANISOU 251 CB TRP A 32 7489 7695 6393 -300 252 -193 C
ATOM 252 CG TRP A 32 38.123 203.108 15.132 1.00 60.72 C
ANISOU 252 CG TRP A 32 7975 8224 6870 -322 279 -210 C
ATOM 253 CD1 TRP A 32 38.965 203.969 14.539 1.00 63.09 C
ANISOU 253 CD1 TRP A 32 8301 8516 7155 -335 304 -229 C
ATOM 254 CD2 TRP A 32 38.791 202.647 16.302 1.00 62.45 C
ANISOU 254 CD2 TRP A 32 8155 8490 7083 -335 285 -210 C
ATOM 255 NE1 TRP A 32 40.105 204.090 15.254 1.00 64.80 N
ANISOU 255 NE1 TRP A 32 8494 8770 7357 -355 324 -242 N
ATOM 256 CE2 TRP A 32 40.025 203.277 16.347 1.00 64.69 C
ANISOU 256 CE2 TRP A 32 8439 8792 7347 -356 312 -230 C
ATOM 257 CE3 TRP A 32 38.466 201.752 17.317 1.00 63.15 C
ANISOU 257 CE3 TRP A 32 8207 8606 7180 -332 269 -194 C
ATOM 258 CZ2 TRP A 32 40.925 203.054 17.373 1.00 66.32 C
ANISOU 258 CZ2 TRP A 32 8610 9045 7542 -372 321 -234 C
ATOM 259 CZ3 TRP A 32 39.364 201.534 18.318 1.00 64.88 C
ANISOU 259 CZ3 TRP A 32 8393 8871 7386 -348 279 -197 C
ATOM 260 CH2 TRP A 32 40.571 202.171 18.340 1.00 66.07 C
ANISOU 260 CH2 TRP A 32 8544 9041 7518 -368 303 -216 C
ATOM 261 N LEU A 33 35.864 205.215 12.912 1.00 56.51 N
ANISOU 261 N LEU A 33 7537 7580 6354 -297 274 -212 N
ATOM 262 CA LEU A 33 36.378 206.283 12.113 1.00 57.95 C
ANISOU 262 CA LEU A 33 7756 7740 6522 -304 298 -228 C
ATOM 263 C LEU A 33 35.487 207.499 12.149 1.00 58.31 C
ANISOU 263 C LEU A 33 7817 7761 6576 -303 310 -231 C
ATOM 264 O LEU A 33 35.976 208.578 12.306 1.00 60.07 O
ANISOU 264 O LEU A 33 8051 7985 6788 -319 344 -249 O
ATOM 265 CB LEU A 33 36.634 205.827 10.677 1.00 58.72 C
ANISOU 265 CB LEU A 33 7888 7808 6613 -291 284 -222 C
ATOM 266 CG LEU A 33 37.753 204.817 10.429 1.00 61.49 C
ANISOU 266 CG LEU A 33 8232 8177 6954 -294 282 -223 C
ATOM 267 CD1 LEU A 33 37.733 204.299 9.014 1.00 62.55 C
ANISOU 267 CD1 LEU A 33 8403 8278 7086 -281 265 -215 C
ATOM 268 CD2 LEU A 33 39.142 205.300 10.773 1.00 63.20 C
ANISOU 268 CD2 LEU A 33 8443 8418 7154 -316 316 -245 C
ATOM 269 N ASN A 34 34.187 207.334 12.030 1.00 56.42 N
ANISOU 269 N ASN A 34 7579 7501 6358 -285 285 -214 N
ATOM 270 CA ASN A 34 33.294 208.465 12.053 1.00 56.21 C
ANISOU 270 CA ASN A 34 7565 7448 6343 -283 296 -214 C
ATOM 271 C ASN A 34 32.812 208.887 13.436 1.00 56.47 C
ANISOU 271 C ASN A 34 7565 7500 6389 -296 313 -218 C
ATOM 272 O ASN A 34 32.119 208.163 14.110 1.00 56.00 O
ANISOU 272 O ASN A 34 7478 7453 6348 -291 292 -207 O
ATOM 273 CB ASN A 34 32.113 208.239 11.116 1.00 56.13 C
ANISOU 273 CB ASN A 34 7575 7401 6350 -257 262 -194 C
ATOM 274 CG ASN A 34 31.326 209.496 10.853 1.00 58.73 C
ANISOU 274 CG ASN A 34 7926 7698 6691 -252 275 -193 C
ATOM 275 OD1 ASN A 34 31.544 210.507 11.480 1.00 60.78 O
ANISOU 275 OD1 ASN A 34 8182 7963 6949 -268 311 -207 O
ATOM 276 ND2 ASN A 34 30.402 209.429 9.931 1.00 57.98 N
ANISOU 276 ND2 ASN A 34 7852 7570 6608 -230 246 -176 N
ATOM 277 N SER A 35 33.139 210.112 13.821 1.00 56.96 N
ANISOU 277 N SER A 35 7634 7564 6445 -315 352 -236 N
ATOM 278 CA SER A 35 32.726 210.642 15.115 1.00 57.11 C
ANISOU 278 CA SER A 35 7626 7599 6476 -332 373 -243 C
ATOM 279 C SER A 35 31.226 210.967 15.229 1.00 56.01 C
ANISOU 279 C SER A 35 7484 7429 6367 -318 363 -228 C
ATOM 280 O SER A 35 30.707 211.075 16.325 1.00 55.66 O
ANISOU 280 O SER A 35 7414 7397 6338 -329 372 -230 O
ATOM 281 CB SER A 35 33.608 211.800 15.565 1.00 59.97 C
ANISOU 281 CB SER A 35 7992 7975 6819 -360 422 -269 C
ATOM 282 OG SER A 35 33.271 212.994 14.910 1.00 63.28 O
ANISOU 282 OG SER A 35 8444 8357 7242 -357 445 -274 O
ATOM 283 N ASN A 36 30.520 211.071 14.103 1.00 55.26 N
ANISOU 283 N ASN A 36 7418 7296 6284 -294 341 -214 N
ATOM 284 CA ASN A 36 29.071 211.281 14.104 1.00 55.23 C
ANISOU 284 CA ASN A 36 7410 7262 6313 -277 325 -198 C
ATOM 285 C ASN A 36 28.318 209.959 14.350 1.00 53.25 C
ANISOU 285 C ASN A 36 7134 7019 6081 -262 284 -180 C
ATOM 286 O ASN A 36 27.141 209.966 14.572 1.00 53.34 O
ANISOU 286 O ASN A 36 7135 7011 6122 -250 270 -169 O
ATOM 287 CB ASN A 36 28.575 211.901 12.800 1.00 58.14 C
ANISOU 287 CB ASN A 36 7817 7587 6686 -257 316 -187 C
ATOM 288 CG ASN A 36 29.122 213.280 12.557 1.00 64.04 C
ANISOU 288 CG ASN A 36 8591 8321 7421 -269 360 -202 C
ATOM 289 OD1 ASN A 36 29.215 214.079 13.466 1.00 67.08 O
ANISOU 289 OD1 ASN A 36 8962 8714 7809 -289 398 -216 O
ATOM 290 ND2 ASN A 36 29.495 213.560 11.323 1.00 64.55 N
ANISOU 290 ND2 ASN A 36 8694 8363 7469 -258 356 -200 N
ATOM 291 N LEU A 37 29.057 208.859 14.351 1.00 51.47 N
ANISOU 291 N LEU A 37 6898 6819 5838 -263 267 -180 N
ATOM 292 CA LEU A 37 28.517 207.545 14.600 1.00 50.10 C
ANISOU 292 CA LEU A 37 6701 6657 5679 -250 233 -166 C
ATOM 293 C LEU A 37 28.967 207.101 15.973 1.00 49.79 C
ANISOU 293 C LEU A 37 6626 6658 5635 -269 247 -174 C
ATOM 294 O LEU A 37 28.746 206.004 16.355 1.00 48.99 O
ANISOU 294 O LEU A 37 6502 6571 5541 -262 225 -164 O
ATOM 295 CB LEU A 37 28.973 206.536 13.540 1.00 49.27 C
ANISOU 295 CB LEU A 37 6611 6550 5560 -235 204 -158 C
ATOM 296 CG LEU A 37 28.379 206.582 12.139 1.00 49.63 C
ANISOU 296 CG LEU A 37 6689 6557 5610 -214 178 -146 C
ATOM 297 CD1 LEU A 37 29.081 205.646 11.196 1.00 49.51 C
ANISOU 297 CD1 LEU A 37 6690 6546 5576 -207 159 -142 C
ATOM 298 CD2 LEU A 37 26.895 206.350 12.122 1.00 49.49 C
ANISOU 298 CD2 LEU A 37 6661 6517 5625 -195 150 -130 C
ATOM 299 N GLN A 38 29.632 207.978 16.697 1.00 50.37 N
ANISOU 299 N GLN A 38 6695 6749 5694 -294 284 -191 N
ATOM 300 CA GLN A 38 30.091 207.682 18.035 1.00 50.45 C
ANISOU 300 CA GLN A 38 6672 6800 5697 -315 299 -199 C
ATOM 301 C GLN A 38 29.142 208.223 19.086 1.00 50.55 C
ANISOU 301 C GLN A 38 6668 6808 5732 -325 315 -201 C
ATOM 302 O GLN A 38 29.263 209.323 19.546 1.00 52.04 O
ANISOU 302 O GLN A 38 6859 6995 5917 -345 350 -216 O
ATOM 303 CB GLN A 38 31.478 208.215 18.238 1.00 52.32 C
ANISOU 303 CB GLN A 38 6913 7065 5903 -339 330 -219 C
ATOM 304 CG GLN A 38 32.497 207.436 17.481 1.00 55.43 C
ANISOU 304 CG GLN A 38 7314 7471 6276 -332 315 -217 C
ATOM 305 CD GLN A 38 33.843 208.065 17.514 1.00 60.02 C
ANISOU 305 CD GLN A 38 7902 8073 6828 -354 347 -238 C
ATOM 306 OE1 GLN A 38 34.076 208.994 18.230 1.00 61.97 O
ANISOU 306 OE1 GLN A 38 8143 8333 7068 -377 379 -255 O
ATOM 307 NE2 GLN A 38 34.721 207.562 16.733 1.00 60.22 N
ANISOU 307 NE2 GLN A 38 7939 8103 6840 -349 338 -238 N
ATOM 308 N ASN A 39 28.173 207.408 19.412 1.00 49.05 N
ANISOU 308 N ASN A 39 6460 6611 5567 -311 289 -187 N
ATOM 309 CA ASN A 39 27.158 207.688 20.376 1.00 48.39 C
ANISOU 309 CA ASN A 39 6358 6519 5509 -318 299 -187 C
ATOM 310 C ASN A 39 26.803 206.396 21.090 1.00 47.49 C
ANISOU 310 C ASN A 39 6215 6423 5404 -311 276 -176 C
ATOM 311 O ASN A 39 27.239 205.335 20.715 1.00 47.04 O
ANISOU 311 O ASN A 39 6155 6382 5337 -298 251 -167 O
ATOM 312 CB ASN A 39 25.948 208.332 19.718 1.00 49.54 C
ANISOU 312 CB ASN A 39 6520 6617 5687 -300 293 -178 C
ATOM 313 CG ASN A 39 25.476 207.593 18.500 1.00 52.63 C
ANISOU 313 CG ASN A 39 6925 6985 6087 -269 252 -161 C
ATOM 314 OD1 ASN A 39 25.018 206.489 18.583 1.00 53.10 O
ANISOU 314 OD1 ASN A 39 6969 7049 6159 -255 223 -150 O
ATOM 315 ND2 ASN A 39 25.569 208.222 17.369 1.00 53.59 N
ANISOU 315 ND2 ASN A 39 7076 7082 6204 -258 250 -159 N
ATOM 316 N VAL A 40 26.005 206.504 22.135 1.00 47.02 N
ANISOU 316 N VAL A 40 6138 6362 5366 -321 287 -177 N
ATOM 317 CA VAL A 40 25.636 205.365 22.963 1.00 46.30 C
ANISOU 317 CA VAL A 40 6020 6288 5284 -317 270 -169 C
ATOM 318 C VAL A 40 24.898 204.265 22.235 1.00 44.60 C
ANISOU 318 C VAL A 40 5803 6053 5089 -285 231 -152 C
ATOM 319 O VAL A 40 25.177 203.115 22.423 1.00 44.47 O
ANISOU 319 O VAL A 40 5772 6057 5065 -278 213 -144 O
ATOM 320 CB VAL A 40 24.881 205.802 24.210 1.00 47.64 C
ANISOU 320 CB VAL A 40 6173 6455 5473 -336 294 -176 C
ATOM 321 CG1 VAL A 40 24.125 204.642 24.779 1.00 47.86 C
ANISOU 321 CG1 VAL A 40 6179 6483 5521 -323 272 -165 C
ATOM 322 CG2 VAL A 40 25.855 206.323 25.216 1.00 49.13 C
ANISOU 322 CG2 VAL A 40 6354 6682 5632 -370 327 -192 C
ATOM 323 N THR A 41 23.978 204.646 21.383 1.00 43.36 N
ANISOU 323 N THR A 41 5662 5856 4958 -267 218 -146 N
ATOM 324 CA THR A 41 23.230 203.713 20.587 1.00 42.46 C
ANISOU 324 CA THR A 41 5548 5721 4863 -238 180 -131 C
ATOM 325 C THR A 41 24.162 202.841 19.775 1.00 40.53 C
ANISOU 325 C THR A 41 5313 5494 4592 -228 160 -126 C
ATOM 326 O THR A 41 24.021 201.657 19.728 1.00 40.61 O
ANISOU 326 O THR A 41 5311 5511 4607 -215 138 -117 O
ATOM 327 CB THR A 41 22.324 204.456 19.609 1.00 44.35 C
ANISOU 327 CB THR A 41 5807 5917 5127 -222 170 -126 C
ATOM 328 OG1 THR A 41 21.628 205.483 20.294 1.00 46.57 O
ANISOU 328 OG1 THR A 41 6084 6180 5432 -234 195 -132 O
ATOM 329 CG2 THR A 41 21.365 203.545 18.981 1.00 44.01 C
ANISOU 329 CG2 THR A 41 5761 5853 5109 -196 132 -113 C
ATOM 330 N ASN A 42 25.129 203.464 19.149 1.00 38.67 N
ANISOU 330 N ASN A 42 5098 5264 4330 -236 172 -132 N
ATOM 331 CA ASN A 42 26.067 202.773 18.326 1.00 37.49 C
ANISOU 331 CA ASN A 42 4960 5127 4156 -229 158 -129 C
ATOM 332 C ASN A 42 27.091 201.928 19.082 1.00 36.50 C
ANISOU 332 C ASN A 42 4813 5045 4009 -240 164 -130 C
ATOM 333 O ASN A 42 27.747 201.136 18.498 1.00 36.18 O
ANISOU 333 O ASN A 42 4777 5015 3955 -232 151 -124 O
ATOM 334 CB ASN A 42 26.699 203.729 17.323 1.00 38.85 C
ANISOU 334 CB ASN A 42 5165 5287 4310 -232 168 -135 C
ATOM 335 CG ASN A 42 25.785 204.059 16.165 1.00 42.20 C
ANISOU 335 CG ASN A 42 5613 5668 4751 -211 147 -127 C
ATOM 336 OD1 ASN A 42 24.689 203.585 16.065 1.00 43.04 O
ANISOU 336 OD1 ASN A 42 5712 5757 4885 -195 124 -116 O
ATOM 337 ND2 ASN A 42 26.260 204.866 15.286 1.00 43.81 N
ANISOU 337 ND2 ASN A 42 5848 5859 4940 -213 156 -131 N
ATOM 338 N TYR A 43 27.222 202.097 20.381 1.00 36.39 N
ANISOU 338 N TYR A 43 4778 5057 3993 -259 185 -136 N
ATOM 339 CA TYR A 43 28.104 201.238 21.138 1.00 37.19 C
ANISOU 339 CA TYR A 43 4857 5199 4075 -267 187 -134 C
ATOM 340 C TYR A 43 27.426 199.878 21.324 1.00 34.83 C
ANISOU 340 C TYR A 43 4540 4899 3795 -248 162 -119 C
ATOM 341 O TYR A 43 28.067 198.885 21.373 1.00 35.08 O
ANISOU 341 O TYR A 43 4560 4954 3816 -243 154 -111 O
ATOM 342 CB TYR A 43 28.497 201.850 22.461 1.00 39.58 C
ANISOU 342 CB TYR A 43 5142 5531 4364 -296 216 -146 C
ATOM 343 CG TYR A 43 29.196 203.153 22.280 1.00 43.69 C
ANISOU 343 CG TYR A 43 5680 6055 4867 -316 243 -163 C
ATOM 344 CD1 TYR A 43 29.976 203.393 21.160 1.00 45.38 C
ANISOU 344 CD1 TYR A 43 5916 6261 5064 -311 242 -166 C
ATOM 345 CD2 TYR A 43 29.057 204.152 23.195 1.00 46.31 C
ANISOU 345 CD2 TYR A 43 6007 6392 5197 -340 273 -176 C
ATOM 346 CE1 TYR A 43 30.604 204.590 20.970 1.00 47.57 C
ANISOU 346 CE1 TYR A 43 6211 6539 5325 -329 269 -183 C
ATOM 347 CE2 TYR A 43 29.676 205.354 23.014 1.00 48.50 C
ANISOU 347 CE2 TYR A 43 6300 6670 5458 -359 301 -193 C
ATOM 348 CZ TYR A 43 30.451 205.564 21.903 1.00 49.83 C
ANISOU 348 CZ TYR A 43 6490 6832 5610 -353 299 -196 C
ATOM 349 OH TYR A 43 31.050 206.758 21.746 1.00 53.40 O
ANISOU 349 OH TYR A 43 6959 7284 6048 -371 330 -214 O
ATOM 350 N PHE A 44 26.116 199.876 21.409 1.00 32.45 N
ANISOU 350 N PHE A 44 4235 4569 3524 -237 153 -115 N
ATOM 351 CA PHE A 44 25.352 198.664 21.514 1.00 31.79 C
ANISOU 351 CA PHE A 44 4137 4479 3463 -218 131 -103 C
ATOM 352 C PHE A 44 25.348 198.015 20.145 1.00 31.64 C
ANISOU 352 C PHE A 44 4134 4441 3445 -197 105 -95 C
ATOM 353 O PHE A 44 25.403 196.849 20.055 1.00 32.33 O
ANISOU 353 O PHE A 44 4212 4537 3535 -185 91 -86 O
ATOM 354 CB PHE A 44 23.955 198.934 22.025 1.00 31.41 C
ANISOU 354 CB PHE A 44 4081 4404 3449 -215 131 -105 C
ATOM 355 CG PHE A 44 23.904 199.251 23.488 1.00 32.52 C
ANISOU 355 CG PHE A 44 4203 4563 3589 -236 155 -112 C
ATOM 356 CD1 PHE A 44 24.209 198.302 24.414 1.00 33.53 C
ANISOU 356 CD1 PHE A 44 4309 4721 3709 -239 157 -106 C
ATOM 357 CD2 PHE A 44 23.557 200.487 23.920 1.00 33.63 C
ANISOU 357 CD2 PHE A 44 4348 4691 3737 -254 178 -123 C
ATOM 358 CE1 PHE A 44 24.177 198.586 25.745 1.00 34.98 C
ANISOU 358 CE1 PHE A 44 4479 4923 3890 -261 179 -113 C
ATOM 359 CE2 PHE A 44 23.526 200.780 25.243 1.00 35.04 C
ANISOU 359 CE2 PHE A 44 4512 4887 3914 -276 203 -131 C
ATOM 360 CZ PHE A 44 23.837 199.833 26.155 1.00 35.06 C
ANISOU 360 CZ PHE A 44 4495 4921 3907 -280 202 -126 C
ATOM 361 N VAL A 45 25.320 198.818 19.093 1.00 30.59 N
ANISOU 361 N VAL A 45 4029 4285 3310 -194 101 -98 N
ATOM 362 CA VAL A 45 25.409 198.340 17.732 1.00 30.59 C
ANISOU 362 CA VAL A 45 4048 4267 3305 -177 79 -92 C
ATOM 363 C VAL A 45 26.729 197.622 17.530 1.00 30.39 C
ANISOU 363 C VAL A 45 4023 4271 3254 -181 83 -90 C
ATOM 364 O VAL A 45 26.759 196.590 16.939 1.00 30.72 O
ANISOU 364 O VAL A 45 4065 4309 3297 -168 66 -81 O
ATOM 365 CB VAL A 45 25.306 199.473 16.711 1.00 31.33 C
ANISOU 365 CB VAL A 45 4174 4334 3396 -176 78 -96 C
ATOM 366 CG1 VAL A 45 25.867 199.058 15.377 1.00 31.56 C
ANISOU 366 CG1 VAL A 45 4228 4355 3409 -167 62 -92 C
ATOM 367 CG2 VAL A 45 23.890 199.916 16.547 1.00 31.61 C
ANISOU 367 CG2 VAL A 45 4212 4336 3464 -165 65 -93 C
ATOM 368 N VAL A 46 27.814 198.187 18.041 1.00 30.25 N
ANISOU 368 N VAL A 46 4003 4280 3212 -200 106 -98 N
ATOM 369 CA VAL A 46 29.134 197.586 17.954 1.00 29.84 C
ANISOU 369 CA VAL A 46 3946 4255 3135 -206 112 -97 C
ATOM 370 C VAL A 46 29.223 196.288 18.729 1.00 28.55 C
ANISOU 370 C VAL A 46 3753 4117 2977 -200 107 -85 C
ATOM 371 O VAL A 46 29.804 195.367 18.270 1.00 27.62 O
ANISOU 371 O VAL A 46 3635 4007 2854 -192 100 -77 O
ATOM 372 CB VAL A 46 30.251 198.557 18.341 1.00 31.31 C
ANISOU 372 CB VAL A 46 4135 4465 3296 -228 139 -110 C
ATOM 373 CG1 VAL A 46 31.535 197.822 18.605 1.00 31.87 C
ANISOU 373 CG1 VAL A 46 4192 4572 3347 -235 146 -107 C
ATOM 374 CG2 VAL A 46 30.452 199.574 17.248 1.00 31.67 C
ANISOU 374 CG2 VAL A 46 4216 4485 3332 -231 145 -120 C
ATOM 375 N SER A 47 28.600 196.230 19.891 1.00 27.92 N
ANISOU 375 N SER A 47 3651 4047 2909 -204 112 -84 N
ATOM 376 CA SER A 47 28.558 195.018 20.692 1.00 28.19 C
ANISOU 376 CA SER A 47 3658 4103 2950 -197 108 -72 C
ATOM 377 C SER A 47 27.839 193.905 19.934 1.00 27.85 C
ANISOU 377 C SER A 47 3618 4037 2928 -173 86 -61 C
ATOM 378 O SER A 47 28.229 192.789 19.970 1.00 27.36 O
ANISOU 378 O SER A 47 3543 3989 2865 -164 82 -51 O
ATOM 379 CB SER A 47 27.883 195.270 22.035 1.00 28.72 C
ANISOU 379 CB SER A 47 3706 4179 3028 -206 118 -75 C
ATOM 380 OG SER A 47 27.864 194.120 22.802 1.00 29.91 O
ANISOU 380 OG SER A 47 3832 4349 3182 -199 115 -63 O
ATOM 381 N LEU A 48 26.753 194.268 19.286 1.00 27.88 N
ANISOU 381 N LEU A 48 3636 4004 2952 -164 72 -65 N
ATOM 382 CA LEU A 48 25.966 193.405 18.460 1.00 27.57 C
ANISOU 382 CA LEU A 48 3603 3941 2933 -144 50 -58 C
ATOM 383 C LEU A 48 26.796 192.941 17.253 1.00 27.80 C
ANISOU 383 C LEU A 48 3650 3966 2945 -139 43 -54 C
ATOM 384 O LEU A 48 26.772 191.811 16.918 1.00 28.04 O
ANISOU 384 O LEU A 48 3675 3996 2982 -128 35 -46 O
ATOM 385 CB LEU A 48 24.707 194.135 18.058 1.00 27.46 C
ANISOU 385 CB LEU A 48 3601 3891 2941 -138 37 -63 C
ATOM 386 CG LEU A 48 23.667 193.500 17.193 1.00 29.26 C
ANISOU 386 CG LEU A 48 3836 4090 3193 -119 12 -59 C
ATOM 387 CD1 LEU A 48 23.173 192.222 17.831 1.00 29.08 C
ANISOU 387 CD1 LEU A 48 3788 4074 3188 -108 9 -52 C
ATOM 388 CD2 LEU A 48 22.544 194.482 16.981 1.00 30.14 C
ANISOU 388 CD2 LEU A 48 3956 4171 3325 -116 2 -64 C
ATOM 389 N ALA A 49 27.547 193.837 16.639 1.00 27.46 N
ANISOU 389 N ALA A 49 3629 3922 2881 -149 50 -61 N
ATOM 390 CA ALA A 49 28.432 193.485 15.545 1.00 27.77 C
ANISOU 390 CA ALA A 49 3688 3958 2904 -148 48 -60 C
ATOM 391 C ALA A 49 29.551 192.529 15.991 1.00 27.93 C
ANISOU 391 C ALA A 49 3689 4011 2913 -151 60 -52 C
ATOM 392 O ALA A 49 29.955 191.679 15.256 1.00 28.79 O
ANISOU 392 O ALA A 49 3804 4115 3020 -144 56 -46 O
ATOM 393 CB ALA A 49 29.009 194.713 14.902 1.00 28.02 C
ANISOU 393 CB ALA A 49 3748 3981 2916 -160 57 -70 C
ATOM 394 N ALA A 50 30.032 192.694 17.207 1.00 26.59 N
ANISOU 394 N ALA A 50 3495 3872 2735 -161 76 -52 N
ATOM 395 CA ALA A 50 31.056 191.858 17.782 1.00 26.58 C
ANISOU 395 CA ALA A 50 3470 3903 2724 -164 87 -43 C
ATOM 396 C ALA A 50 30.555 190.430 17.944 1.00 26.24 C
ANISOU 396 C ALA A 50 3410 3860 2700 -146 78 -28 C
ATOM 397 O ALA A 50 31.234 189.492 17.644 1.00 26.11 O
ANISOU 397 O ALA A 50 3388 3852 2681 -141 81 -18 O
ATOM 398 CB ALA A 50 31.531 192.424 19.093 1.00 26.23 C
ANISOU 398 CB ALA A 50 3405 3894 2667 -180 103 -46 C
ATOM 399 N ALA A 51 29.330 190.299 18.384 1.00 25.47 N
ANISOU 399 N ALA A 51 3304 3749 2623 -138 69 -28 N
ATOM 400 CA ALA A 51 28.723 189.023 18.550 1.00 25.18 C
ANISOU 400 CA ALA A 51 3252 3709 2606 -122 62 -17 C
ATOM 401 C ALA A 51 28.590 188.305 17.208 1.00 26.37 C
ANISOU 401 C ALA A 51 3421 3834 2764 -111 51 -14 C
ATOM 402 O ALA A 51 28.811 187.135 17.122 1.00 26.88 O
ANISOU 402 O ALA A 51 3475 3904 2835 -101 54 -3 O
ATOM 403 CB ALA A 51 27.392 189.166 19.225 1.00 24.07 C
ANISOU 403 CB ALA A 51 3103 3555 2487 -117 56 -20 C
ATOM 404 N ASP A 52 28.262 189.049 16.170 1.00 25.95 N
ANISOU 404 N ASP A 52 3396 3754 2708 -113 39 -23 N
ATOM 405 CA ASP A 52 28.120 188.483 14.847 1.00 25.73 C
ANISOU 405 CA ASP A 52 3390 3702 2684 -105 27 -23 C
ATOM 406 C ASP A 52 29.470 188.061 14.246 1.00 26.68 C
ANISOU 406 C ASP A 52 3518 3832 2785 -111 40 -19 C
ATOM 407 O ASP A 52 29.567 187.054 13.617 1.00 26.79 O
ANISOU 407 O ASP A 52 3535 3838 2805 -104 40 -13 O
ATOM 408 CB ASP A 52 27.273 189.377 13.948 1.00 26.04 C
ANISOU 408 CB ASP A 52 3458 3711 2727 -105 9 -32 C
ATOM 409 CG ASP A 52 25.843 189.472 14.415 1.00 30.85 C
ANISOU 409 CG ASP A 52 4056 4305 3361 -96 -5 -34 C
ATOM 410 OD1 ASP A 52 25.350 188.569 15.087 1.00 31.49 O
ANISOU 410 OD1 ASP A 52 4113 4392 3460 -87 -4 -29 O
ATOM 411 OD2 ASP A 52 25.205 190.459 14.146 1.00 32.56 O
ANISOU 411 OD2 ASP A 52 4287 4504 3582 -97 -15 -41 O
ATOM 412 N ILE A 53 30.497 188.847 14.499 1.00 27.38 N
ANISOU 412 N ILE A 53 3610 3940 2855 -124 54 -23 N
ATOM 413 CA ILE A 53 31.839 188.527 14.085 1.00 28.05 C
ANISOU 413 CA ILE A 53 3699 4036 2924 -131 69 -20 C
ATOM 414 C ILE A 53 32.238 187.198 14.719 1.00 28.03 C
ANISOU 414 C ILE A 53 3665 4054 2931 -123 78 -4 C
ATOM 415 O ILE A 53 32.773 186.371 14.056 1.00 29.40 O
ANISOU 415 O ILE A 53 3843 4223 3107 -120 85 2 O
ATOM 416 CB ILE A 53 32.846 189.636 14.423 1.00 29.27 C
ANISOU 416 CB ILE A 53 3855 4208 3056 -147 83 -29 C
ATOM 417 CG1 ILE A 53 32.643 190.852 13.547 1.00 30.29 C
ANISOU 417 CG1 ILE A 53 4021 4313 3176 -155 78 -44 C
ATOM 418 CG2 ILE A 53 34.257 189.138 14.263 1.00 30.68 C
ANISOU 418 CG2 ILE A 53 4028 4405 3225 -153 100 -24 C
ATOM 419 CD1 ILE A 53 33.251 192.118 14.067 1.00 31.33 C
ANISOU 419 CD1 ILE A 53 4153 4460 3290 -170 92 -55 C
ATOM 420 N LEU A 54 31.924 187.011 15.991 1.00 26.70 N
ANISOU 420 N LEU A 54 3467 3909 2770 -119 81 3 N
ATOM 421 CA LEU A 54 32.217 185.788 16.721 1.00 26.02 C
ANISOU 421 CA LEU A 54 3350 3843 2692 -109 90 20 C
ATOM 422 C LEU A 54 31.401 184.576 16.271 1.00 25.45 C
ANISOU 422 C LEU A 54 3277 3750 2642 -93 85 27 C
ATOM 423 O LEU A 54 31.799 183.486 16.456 1.00 25.60 O
ANISOU 423 O LEU A 54 3279 3779 2669 -85 96 41 O
ATOM 424 CB LEU A 54 32.126 185.999 18.227 1.00 25.48 C
ANISOU 424 CB LEU A 54 3255 3806 2622 -112 95 24 C
ATOM 425 CG LEU A 54 33.179 186.871 18.890 1.00 27.29 C
ANISOU 425 CG LEU A 54 3475 4066 2828 -129 105 21 C
ATOM 426 CD1 LEU A 54 32.891 187.142 20.336 1.00 27.26 C
ANISOU 426 CD1 LEU A 54 3447 4089 2821 -134 108 23 C
ATOM 427 CD2 LEU A 54 34.542 186.284 18.756 1.00 28.84 C
ANISOU 427 CD2 LEU A 54 3660 4284 3016 -130 118 32 C
ATOM 428 N VAL A 55 30.252 184.808 15.669 1.00 24.44 N
ANISOU 428 N VAL A 55 3167 3593 2525 -89 69 17 N
ATOM 429 CA VAL A 55 29.458 183.739 15.115 1.00 23.77 C
ANISOU 429 CA VAL A 55 3084 3487 2460 -77 63 20 C
ATOM 430 C VAL A 55 30.216 183.191 13.896 1.00 25.21 C
ANISOU 430 C VAL A 55 3286 3657 2637 -80 70 22 C
ATOM 431 O VAL A 55 30.277 182.033 13.678 1.00 26.07 O
ANISOU 431 O VAL A 55 3386 3762 2757 -72 79 30 O
ATOM 432 CB VAL A 55 28.036 184.207 14.710 1.00 23.19 C
ANISOU 432 CB VAL A 55 3025 3385 2400 -73 41 8 C
ATOM 433 CG1 VAL A 55 27.406 183.287 13.690 1.00 22.60 C
ANISOU 433 CG1 VAL A 55 2962 3285 2339 -65 33 7 C
ATOM 434 CG2 VAL A 55 27.140 184.374 15.915 1.00 22.74 C
ANISOU 434 CG2 VAL A 55 2947 3336 2358 -68 38 7 C
ATOM 435 N GLY A 56 30.816 184.060 13.123 1.00 25.98 N
ANISOU 435 N GLY A 56 3409 3746 2716 -92 67 13 N
ATOM 436 CA GLY A 56 31.561 183.619 11.973 1.00 27.48 C
ANISOU 436 CA GLY A 56 3619 3922 2900 -97 76 13 C
ATOM 437 C GLY A 56 32.890 182.981 12.298 1.00 28.45 C
ANISOU 437 C GLY A 56 3724 4067 3019 -99 100 25 C
ATOM 438 O GLY A 56 33.230 181.972 11.802 1.00 29.07 O
ANISOU 438 O GLY A 56 3802 4138 3106 -97 112 33 O
ATOM 439 N VAL A 57 33.612 183.584 13.200 1.00 28.82 N
ANISOU 439 N VAL A 57 3753 4142 3055 -104 107 28 N
ATOM 440 CA VAL A 57 34.919 183.117 13.602 1.00 29.73 C
ANISOU 440 CA VAL A 57 3848 4282 3167 -107 128 40 C
ATOM 441 C VAL A 57 34.890 181.866 14.484 1.00 29.87 C
ANISOU 441 C VAL A 57 3830 4317 3201 -92 138 60 C
ATOM 442 O VAL A 57 35.685 180.999 14.335 1.00 30.63 O
ANISOU 442 O VAL A 57 3915 4419 3305 -89 155 73 O
ATOM 443 CB VAL A 57 35.681 184.267 14.294 1.00 30.46 C
ANISOU 443 CB VAL A 57 3934 4401 3240 -119 131 34 C
ATOM 444 CG1 VAL A 57 36.925 183.799 14.959 1.00 32.40 C
ANISOU 444 CG1 VAL A 57 4150 4677 3483 -120 148 48 C
ATOM 445 CG2 VAL A 57 36.007 185.369 13.339 1.00 30.91 C
ANISOU 445 CG2 VAL A 57 4026 4438 3280 -133 128 16 C
ATOM 446 N LEU A 58 33.929 181.785 15.377 1.00 28.36 N
ANISOU 446 N LEU A 58 3622 4134 3018 -83 129 62 N
ATOM 447 CA LEU A 58 33.823 180.696 16.320 1.00 28.10 C
ANISOU 447 CA LEU A 58 3557 4119 3000 -69 139 81 C
ATOM 448 C LEU A 58 32.569 179.801 16.277 1.00 26.52 C
ANISOU 448 C LEU A 58 3355 3899 2822 -55 135 83 C
ATOM 449 O LEU A 58 32.699 178.624 16.131 1.00 26.97 O
ANISOU 449 O LEU A 58 3402 3952 2894 -45 150 95 O
ATOM 450 CB LEU A 58 34.062 181.216 17.730 1.00 28.88 C
ANISOU 450 CB LEU A 58 3631 4253 3088 -72 138 87 C
ATOM 451 CG LEU A 58 35.453 181.668 18.134 1.00 30.45 C
ANISOU 451 CG LEU A 58 3818 4484 3269 -82 147 92 C
ATOM 452 CD1 LEU A 58 35.468 182.095 19.565 1.00 29.99 C
ANISOU 452 CD1 LEU A 58 3734 4460 3199 -85 145 97 C
ATOM 453 CD2 LEU A 58 36.436 180.575 17.896 1.00 31.22 C
ANISOU 453 CD2 LEU A 58 3899 4588 3374 -75 165 111 C
ATOM 454 N ALA A 59 31.381 180.372 16.410 1.00 24.60 N
ANISOU 454 N ALA A 59 3120 3642 2583 -54 117 69 N
ATOM 455 CA ALA A 59 30.153 179.609 16.387 1.00 24.26 C
ANISOU 455 CA ALA A 59 3074 3580 2562 -42 113 68 C
ATOM 456 C ALA A 59 29.956 178.738 15.144 1.00 25.11 C
ANISOU 456 C ALA A 59 3199 3661 2682 -39 117 66 C
ATOM 457 O ALA A 59 29.508 177.641 15.258 1.00 25.59 O
ANISOU 457 O ALA A 59 3247 3715 2760 -27 127 72 O
ATOM 458 CB ALA A 59 28.961 180.502 16.584 1.00 23.28 C
ANISOU 458 CB ALA A 59 2960 3444 2441 -44 92 53 C
ATOM 459 N ILE A 60 30.274 179.254 13.977 1.00 24.52 N
ANISOU 459 N ILE A 60 3153 3569 2595 -50 110 55 N
ATOM 460 CA ILE A 60 30.144 178.496 12.752 1.00 24.63 C
ANISOU 460 CA ILE A 60 3186 3556 2615 -52 114 52 C
ATOM 461 C ILE A 60 31.144 177.338 12.654 1.00 25.51 C
ANISOU 461 C ILE A 60 3284 3675 2734 -49 143 68 C
ATOM 462 O ILE A 60 30.760 176.254 12.400 1.00 25.59 O
ANISOU 462 O ILE A 60 3289 3673 2761 -42 154 71 O
ATOM 463 CB ILE A 60 30.049 179.390 11.533 1.00 25.03 C
ANISOU 463 CB ILE A 60 3275 3585 2652 -65 96 36 C
ATOM 464 CG1 ILE A 60 28.656 180.011 11.509 1.00 25.17 C
ANISOU 464 CG1 ILE A 60 3300 3588 2675 -62 69 23 C
ATOM 465 CG2 ILE A 60 30.324 178.598 10.285 1.00 26.76 C
ANISOU 465 CG2 ILE A 60 3514 3782 2872 -71 107 34 C
ATOM 466 CD1 ILE A 60 28.442 181.102 10.490 1.00 25.98 C
ANISOU 466 CD1 ILE A 60 3438 3670 2761 -73 48 9 C
ATOM 467 N PRO A 61 32.428 177.586 12.903 1.00 26.37 N
ANISOU 467 N PRO A 61 3385 3802 2830 -54 156 77 N
ATOM 468 CA PRO A 61 33.360 176.470 12.960 1.00 27.24 C
ANISOU 468 CA PRO A 61 3477 3920 2951 -49 184 95 C
ATOM 469 C PRO A 61 32.937 175.436 14.021 1.00 27.27 C
ANISOU 469 C PRO A 61 3448 3938 2974 -31 196 112 C
ATOM 470 O PRO A 61 33.053 174.293 13.737 1.00 28.02 O
ANISOU 470 O PRO A 61 3536 4024 3086 -25 218 121 O
ATOM 471 CB PRO A 61 34.667 177.138 13.310 1.00 28.45 C
ANISOU 471 CB PRO A 61 3623 4098 3088 -57 190 101 C
ATOM 472 CG PRO A 61 34.534 178.461 12.721 1.00 28.71 C
ANISOU 472 CG PRO A 61 3686 4120 3102 -72 170 81 C
ATOM 473 CD PRO A 61 33.133 178.859 12.950 1.00 26.36 C
ANISOU 473 CD PRO A 61 3395 3814 2808 -67 147 70 C
ATOM 474 N PHE A 62 32.409 175.847 15.165 1.00 26.45 N
ANISOU 474 N PHE A 62 3326 3854 2868 -24 184 113 N
ATOM 475 CA PHE A 62 31.954 174.923 16.173 1.00 26.54 C
ANISOU 475 CA PHE A 62 3311 3877 2897 -7 196 128 C
ATOM 476 C PHE A 62 30.774 174.097 15.652 1.00 26.50 C
ANISOU 476 C PHE A 62 3313 3843 2913 0 198 119 C
ATOM 477 O PHE A 62 30.708 172.932 15.882 1.00 26.81 O
ANISOU 477 O PHE A 62 3336 3881 2969 12 219 131 O
ATOM 478 CB PHE A 62 31.524 175.633 17.468 1.00 26.03 C
ANISOU 478 CB PHE A 62 3230 3835 2825 -5 182 128 C
ATOM 479 CG PHE A 62 32.641 176.243 18.280 1.00 27.23 C
ANISOU 479 CG PHE A 62 3366 4022 2957 -10 183 139 C
ATOM 480 CD1 PHE A 62 33.945 176.128 17.908 1.00 28.72 C
ANISOU 480 CD1 PHE A 62 3552 4221 3138 -16 196 149 C
ATOM 481 CD2 PHE A 62 32.358 176.946 19.439 1.00 27.72 C
ANISOU 481 CD2 PHE A 62 3416 4106 3009 -12 172 138 C
ATOM 482 CE1 PHE A 62 34.940 176.701 18.654 1.00 30.19 C
ANISOU 482 CE1 PHE A 62 3722 4441 3307 -22 196 158 C
ATOM 483 CE2 PHE A 62 33.345 177.511 20.192 1.00 28.71 C
ANISOU 483 CE2 PHE A 62 3527 4266 3115 -20 173 147 C
ATOM 484 CZ PHE A 62 34.643 177.387 19.797 1.00 29.67 C
ANISOU 484 CZ PHE A 62 3644 4399 3230 -24 184 157 C
ATOM 485 N ALA A 63 29.851 174.708 14.945 1.00 25.85 N
ANISOU 485 N ALA A 63 3255 3738 2828 -7 176 98 N
ATOM 486 CA ALA A 63 28.707 173.992 14.440 1.00 26.15 C
ANISOU 486 CA ALA A 63 3299 3751 2885 -2 175 87 C
ATOM 487 C ALA A 63 29.068 172.983 13.354 1.00 27.48 C
ANISOU 487 C ALA A 63 3478 3900 3062 -5 196 89 C
ATOM 488 O ALA A 63 28.539 171.947 13.286 1.00 27.93 O
ANISOU 488 O ALA A 63 3528 3947 3139 2 211 90 O
ATOM 489 CB ALA A 63 27.645 174.939 13.960 1.00 25.66 C
ANISOU 489 CB ALA A 63 3259 3672 2820 -9 144 66 C
ATOM 490 N ILE A 64 30.023 173.329 12.539 1.00 27.70 N
ANISOU 490 N ILE A 64 3524 3925 3075 -19 198 89 N
ATOM 491 CA ILE A 64 30.520 172.445 11.514 1.00 29.65 C
ANISOU 491 CA ILE A 64 3783 4154 3329 -25 221 91 C
ATOM 492 C ILE A 64 31.134 171.218 12.211 1.00 32.40 C
ANISOU 492 C ILE A 64 4100 4515 3695 -12 257 114 C
ATOM 493 O ILE A 64 30.868 170.109 11.839 1.00 33.38 O
ANISOU 493 O ILE A 64 4222 4624 3838 -8 279 116 O
ATOM 494 CB ILE A 64 31.536 173.173 10.605 1.00 29.61 C
ANISOU 494 CB ILE A 64 3804 4143 3304 -43 219 86 C
ATOM 495 CG1 ILE A 64 30.836 174.157 9.674 1.00 29.44 C
ANISOU 495 CG1 ILE A 64 3817 4102 3266 -56 188 64 C
ATOM 496 CG2 ILE A 64 32.374 172.205 9.809 1.00 30.57 C
ANISOU 496 CG2 ILE A 64 3930 4250 3433 -50 251 94 C
ATOM 497 CD1 ILE A 64 31.749 175.187 9.089 1.00 30.41 C
ANISOU 497 CD1 ILE A 64 3964 4224 3366 -71 181 59 C
ATOM 498 N THR A 65 31.864 171.485 13.278 1.00 33.09 N
ANISOU 498 N THR A 65 4164 4632 3778 -4 260 131 N
ATOM 499 CA THR A 65 32.546 170.506 14.065 1.00 34.68 C
ANISOU 499 CA THR A 65 4334 4850 3992 11 289 157 C
ATOM 500 C THR A 65 31.587 169.538 14.693 1.00 35.74 C
ANISOU 500 C THR A 65 4451 4982 4148 28 301 161 C
ATOM 501 O THR A 65 31.746 168.376 14.579 1.00 36.60 O
ANISOU 501 O THR A 65 4549 5082 4276 36 331 173 O
ATOM 502 CB THR A 65 33.422 171.182 15.132 1.00 36.14 C
ANISOU 502 CB THR A 65 4498 5070 4163 14 282 172 C
ATOM 503 OG1 THR A 65 34.547 171.748 14.521 1.00 37.88 O
ANISOU 503 OG1 THR A 65 4730 5294 4370 0 283 172 O
ATOM 504 CG2 THR A 65 33.938 170.233 16.074 1.00 36.82 C
ANISOU 504 CG2 THR A 65 4551 5177 4262 31 307 200 C
ATOM 505 N ILE A 66 30.633 170.061 15.408 1.00 35.89 N
ANISOU 505 N ILE A 66 4467 5007 4165 33 279 152 N
ATOM 506 CA AILE A 66 29.614 169.196 15.980 0.50 37.20 C
ANISOU 506 CA AILE A 66 4618 5166 4351 48 290 153 C
ATOM 507 CA BILE A 66 29.564 169.236 15.967 0.50 37.20 C
ANISOU 507 CA BILE A 66 4618 5165 4350 48 289 151 C
ATOM 508 C ILE A 66 28.600 168.356 15.078 1.00 38.06 C
ANISOU 508 C ILE A 66 4740 5242 4480 47 300 135 C
ATOM 509 O ILE A 66 27.936 167.266 15.325 1.00 39.18 O
ANISOU 509 O ILE A 66 4870 5373 4644 60 322 137 O
ATOM 510 CB AILE A 66 28.924 169.869 17.189 0.50 37.88 C
ANISOU 510 CB AILE A 66 4693 5268 4432 55 270 150 C
ATOM 511 CB BILE A 66 28.628 170.019 16.888 0.50 37.84 C
ANISOU 511 CB BILE A 66 4696 5255 4428 52 263 141 C
ATOM 512 CG1AILE A 66 28.013 168.924 17.925 0.50 40.34 C
ANISOU 512 CG1AILE A 66 4987 5575 4766 72 286 153 C
ATOM 513 CG1BILE A 66 29.340 170.590 18.073 0.50 40.39 C
ANISOU 513 CG1BILE A 66 5000 5612 4735 55 258 158 C
ATOM 514 CG2AILE A 66 28.079 171.025 16.762 0.50 38.26 C
ANISOU 514 CG2AILE A 66 4763 5304 4471 43 235 124 C
ATOM 515 CG2BILE A 66 27.555 169.112 17.416 0.50 38.54 C
ANISOU 515 CG2BILE A 66 4771 5332 4539 67 276 139 C
ATOM 516 CD1AILE A 66 27.368 169.571 19.123 0.50 42.03 C
ANISOU 516 CD1AILE A 66 5192 5803 4976 78 269 150 C
ATOM 517 CD1BILE A 66 28.356 171.022 19.131 0.50 42.04 C
ANISOU 517 CD1BILE A 66 5201 5827 4946 61 244 151 C
ATOM 518 N SER A 67 28.601 168.805 13.822 1.00 37.06 N
ANISOU 518 N SER A 67 4642 5096 4343 30 286 118 N
ATOM 519 CA SER A 67 27.833 168.121 12.799 1.00 36.44 C
ANISOU 519 CA SER A 67 4579 4989 4277 23 293 101 C
ATOM 520 C SER A 67 28.453 166.795 12.387 1.00 37.85 C
ANISOU 520 C SER A 67 4751 5158 4472 25 336 114 C
ATOM 521 O SER A 67 27.797 165.970 11.836 1.00 38.28 O
ANISOU 521 O SER A 67 4810 5192 4541 23 351 103 O
ATOM 522 CB SER A 67 27.553 169.032 11.592 1.00 35.18 C
ANISOU 522 CB SER A 67 4454 4813 4101 3 263 79 C
ATOM 523 OG SER A 67 28.608 169.154 10.698 1.00 35.79 O
ANISOU 523 OG SER A 67 4549 4884 4165 -12 272 83 O
ATOM 524 N THR A 68 29.715 166.625 12.708 1.00 38.28 N
ANISOU 524 N THR A 68 4792 5228 4524 28 356 137 N
ATOM 525 CA THR A 68 30.413 165.416 12.388 1.00 39.36 C
ANISOU 525 CA THR A 68 4921 5356 4678 30 400 153 C
ATOM 526 C THR A 68 30.155 164.336 13.410 1.00 40.53 C
ANISOU 526 C THR A 68 5038 5512 4849 53 428 171 C
ATOM 527 O THR A 68 30.329 163.191 13.123 1.00 41.96 O
ANISOU 527 O THR A 68 5212 5680 5050 57 467 179 O
ATOM 528 CB THR A 68 31.927 165.635 12.201 1.00 40.21 C
ANISOU 528 CB THR A 68 5027 5475 4778 24 411 171 C
ATOM 529 OG1 THR A 68 32.534 165.946 13.445 1.00 40.90 O
ANISOU 529 OG1 THR A 68 5086 5594 4859 39 407 193 O
ATOM 530 CG2 THR A 68 32.191 166.727 11.251 1.00 39.52 C
ANISOU 530 CG2 THR A 68 4970 5379 4667 2 385 153 C
ATOM 531 N GLY A 69 29.732 164.724 14.608 1.00 40.03 N
ANISOU 531 N GLY A 69 4958 5470 4783 68 411 176 N
ATOM 532 CA GLY A 69 29.497 163.805 15.689 1.00 40.43 C
ANISOU 532 CA GLY A 69 4981 5530 4852 90 437 194 C
ATOM 533 C GLY A 69 30.759 163.183 16.245 1.00 41.49 C
ANISOU 533 C GLY A 69 5091 5682 4991 103 467 229 C
ATOM 534 O GLY A 69 30.714 162.127 16.798 1.00 42.89 O
ANISOU 534 O GLY A 69 5248 5859 5188 120 499 246 O
ATOM 535 N PHE A 70 31.874 163.882 16.109 1.00 40.61 N
ANISOU 535 N PHE A 70 4980 5586 4863 94 455 239 N
ATOM 536 CA PHE A 70 33.182 163.460 16.534 1.00 41.59 C
ANISOU 536 CA PHE A 70 5081 5728 4991 103 478 271 C
ATOM 537 C PHE A 70 33.250 163.159 18.011 1.00 41.77 C
ANISOU 537 C PHE A 70 5074 5780 5017 126 483 297 C
ATOM 538 O PHE A 70 32.613 163.775 18.793 1.00 41.34 O
ANISOU 538 O PHE A 70 5018 5739 4949 130 457 290 O
ATOM 539 CB PHE A 70 34.236 164.515 16.151 1.00 41.71 C
ANISOU 539 CB PHE A 70 5105 5757 4985 87 457 271 C
ATOM 540 CG PHE A 70 34.290 165.670 17.079 1.00 42.04 C
ANISOU 540 CG PHE A 70 5141 5829 5002 87 421 271 C
ATOM 541 CD1 PHE A 70 33.246 166.535 17.168 1.00 41.64 C
ANISOU 541 CD1 PHE A 70 5107 5776 4939 81 389 246 C
ATOM 542 CD2 PHE A 70 35.375 165.873 17.882 1.00 43.55 C
ANISOU 542 CD2 PHE A 70 5308 6053 5185 94 421 296 C
ATOM 543 CE1 PHE A 70 33.263 167.561 18.056 1.00 42.16 C
ANISOU 543 CE1 PHE A 70 5167 5869 4984 80 360 246 C
ATOM 544 CE2 PHE A 70 35.411 166.912 18.756 1.00 43.68 C
ANISOU 544 CE2 PHE A 70 5319 6098 5179 92 390 295 C
ATOM 545 CZ PHE A 70 34.347 167.750 18.852 1.00 42.55 C
ANISOU 545 CZ PHE A 70 5194 5951 5023 84 361 270 C
ATOM 546 N CYS A 71 34.064 162.203 18.376 1.00 42.38 N
ANISOU 546 N CYS A 71 5127 5865 5110 142 517 329 N
ATOM 547 CA CYS A 71 34.218 161.841 19.756 1.00 42.95 C
ANISOU 547 CA CYS A 71 5170 5965 5183 164 523 357 C
ATOM 548 C CYS A 71 34.854 162.945 20.551 1.00 42.53 C
ANISOU 548 C CYS A 71 5107 5949 5102 160 489 366 C
ATOM 549 O CYS A 71 35.813 163.533 20.122 1.00 43.18 O
ANISOU 549 O CYS A 71 5192 6041 5174 148 479 368 O
ATOM 550 CB CYS A 71 35.051 160.588 19.849 1.00 45.40 C
ANISOU 550 CB CYS A 71 5457 6275 5518 181 567 391 C
ATOM 551 SG CYS A 71 34.314 159.227 19.007 1.00 50.22 S
ANISOU 551 SG CYS A 71 6077 6843 6162 184 614 381 S
ATOM 552 N ALA A 72 34.304 163.222 21.713 1.00 40.86 N
ANISOU 552 N ALA A 72 4887 5758 4880 170 472 369 N
ATOM 553 CA ALA A 72 34.831 164.242 22.567 1.00 40.61 C
ANISOU 553 CA ALA A 72 4845 5763 4821 165 442 377 C
ATOM 554 C ALA A 72 34.408 164.051 23.985 1.00 40.72 C
ANISOU 554 C ALA A 72 4843 5800 4830 181 440 392 C
ATOM 555 O ALA A 72 33.389 163.486 24.258 1.00 40.49 O
ANISOU 555 O ALA A 72 4817 5753 4813 192 451 386 O
ATOM 556 CB ALA A 72 34.389 165.609 22.107 1.00 39.74 C
ANISOU 556 CB ALA A 72 4761 5649 4689 142 405 343 C
ATOM 557 N ALA A 73 35.200 164.582 24.899 1.00 40.89 N
ANISOU 557 N ALA A 73 4846 5860 4829 181 423 412 N
ATOM 558 CA ALA A 73 34.855 164.598 26.290 1.00 40.96 C
ANISOU 558 CA ALA A 73 4843 5895 4827 192 416 425 C
ATOM 559 C ALA A 73 33.588 165.415 26.377 1.00 40.00 C
ANISOU 559 C ALA A 73 4743 5758 4696 180 393 390 C
ATOM 560 O ALA A 73 33.517 166.496 25.831 1.00 40.26 O
ANISOU 560 O ALA A 73 4795 5789 4716 159 368 365 O
ATOM 561 CB ALA A 73 35.939 165.265 27.079 1.00 41.81 C
ANISOU 561 CB ALA A 73 4931 6047 4908 187 396 446 C
ATOM 562 N CYS A 74 32.591 164.907 27.075 1.00 39.04 N
ANISOU 562 N CYS A 74 4622 5627 4584 192 403 389 N
ATOM 563 CA CYS A 74 31.312 165.581 27.160 1.00 38.21 C
ANISOU 563 CA CYS A 74 4537 5504 4476 182 385 356 C
ATOM 564 C CYS A 74 31.303 167.071 27.491 1.00 37.68 C
ANISOU 564 C CYS A 74 4480 5457 4381 160 349 338 C
ATOM 565 O CYS A 74 30.629 167.801 26.845 1.00 36.72 O
ANISOU 565 O CYS A 74 4379 5314 4260 146 332 308 O
ATOM 566 CB CYS A 74 30.318 164.798 28.011 1.00 40.34 C
ANISOU 566 CB CYS A 74 4804 5764 4761 199 404 358 C
ATOM 567 SG CYS A 74 28.623 165.353 27.883 1.00 42.99 S
ANISOU 567 SG CYS A 74 5162 6065 5105 189 390 316 S
ATOM 568 N HIS A 75 32.089 167.517 28.455 1.00 38.18 N
ANISOU 568 N HIS A 75 4528 5559 4420 157 338 357 N
ATOM 569 CA HIS A 75 32.126 168.922 28.799 1.00 38.74 C
ANISOU 569 CA HIS A 75 4607 5649 4464 134 308 340 C
ATOM 570 C HIS A 75 32.764 169.832 27.761 1.00 38.04 C
ANISOU 570 C HIS A 75 4530 5559 4365 115 291 325 C
ATOM 571 O HIS A 75 32.456 170.982 27.693 1.00 37.41 O
ANISOU 571 O HIS A 75 4464 5478 4270 96 269 301 O
ATOM 572 CB HIS A 75 32.697 169.146 30.179 1.00 41.61 C
ANISOU 572 CB HIS A 75 4953 6056 4803 134 301 363 C
ATOM 573 CG HIS A 75 31.755 168.758 31.264 1.00 45.79 C
ANISOU 573 CG HIS A 75 5481 6582 5334 143 309 365 C
ATOM 574 ND1 HIS A 75 31.584 167.456 31.660 1.00 48.69 N
ANISOU 574 ND1 HIS A 75 5837 6943 5720 168 336 388 N
ATOM 575 CD2 HIS A 75 30.895 169.491 32.000 1.00 47.15 C
ANISOU 575 CD2 HIS A 75 5665 6754 5497 131 297 346 C
ATOM 576 CE1 HIS A 75 30.670 167.403 32.601 1.00 49.09 C
ANISOU 576 CE1 HIS A 75 5893 6990 5771 171 339 383 C
ATOM 577 NE2 HIS A 75 30.240 168.626 32.829 1.00 48.85 N
ANISOU 577 NE2 HIS A 75 5876 6962 5723 148 316 358 N
ATOM 578 N GLY A 76 33.643 169.272 26.955 1.00 37.51 N
ANISOU 578 N GLY A 76 4457 5489 4308 121 304 338 N
ATOM 579 CA GLY A 76 34.265 169.993 25.886 1.00 37.09 C
ANISOU 579 CA GLY A 76 4416 5430 4248 104 293 324 C
ATOM 580 C GLY A 76 33.267 170.091 24.773 1.00 34.66 C
ANISOU 580 C GLY A 76 4135 5079 3955 99 290 294 C
ATOM 581 O GLY A 76 33.144 171.092 24.165 1.00 34.59 O
ANISOU 581 O GLY A 76 4146 5062 3936 81 271 271 O
ATOM 582 N CYS A 77 32.524 169.022 24.579 1.00 33.07 N
ANISOU 582 N CYS A 77 3934 4852 3778 114 311 296 N
ATOM 583 CA CYS A 77 31.479 168.942 23.593 1.00 32.14 C
ANISOU 583 CA CYS A 77 3839 4694 3677 111 310 269 C
ATOM 584 C CYS A 77 30.423 169.968 23.927 1.00 29.79 C
ANISOU 584 C CYS A 77 3557 4392 3372 100 284 243 C
ATOM 585 O CYS A 77 29.921 170.674 23.091 1.00 28.18 O
ANISOU 585 O CYS A 77 3374 4167 3166 87 267 218 O
ATOM 586 CB CYS A 77 30.846 167.582 23.559 1.00 32.89 C
ANISOU 586 CB CYS A 77 3929 4769 3801 129 339 275 C
ATOM 587 SG CYS A 77 29.442 167.572 22.480 1.00 35.96 S
ANISOU 587 SG CYS A 77 4344 5113 4208 123 333 239 S
ATOM 588 N LEU A 78 30.119 170.041 25.209 1.00 29.25 N
ANISOU 588 N LEU A 78 3476 4342 3297 105 283 251 N
ATOM 589 CA ALEU A 78 29.164 171.042 25.724 0.70 28.62 C
ANISOU 589 CA ALEU A 78 3406 4258 3209 94 262 228 C
ATOM 590 CA BLEU A 78 29.161 171.031 25.724 0.30 28.88 C
ANISOU 590 CA BLEU A 78 3439 4291 3242 94 262 229 C
ATOM 591 C LEU A 78 29.404 172.580 25.382 1.00 28.90 C
ANISOU 591 C LEU A 78 3457 4301 3222 71 234 209 C
ATOM 592 O LEU A 78 28.626 173.508 24.969 1.00 29.19 O
ANISOU 592 O LEU A 78 3513 4318 3259 58 215 183 O
ATOM 593 CB ALEU A 78 28.999 170.952 27.245 0.70 28.49 C
ANISOU 593 CB ALEU A 78 3375 4266 3185 100 266 242 C
ATOM 594 CB BLEU A 78 29.033 170.871 27.240 0.30 29.37 C
ANISOU 594 CB BLEU A 78 3485 4377 3297 101 268 244 C
ATOM 595 CG ALEU A 78 27.780 170.344 27.904 0.70 28.31 C
ANISOU 595 CG ALEU A 78 3351 4224 3181 113 278 236 C
ATOM 596 CG BLEU A 78 27.721 171.051 27.989 0.30 29.89 C
ANISOU 596 CG BLEU A 78 3556 4428 3372 102 265 227 C
ATOM 597 CD1ALEU A 78 27.853 170.468 29.404 0.70 28.80 C
ANISOU 597 CD1ALEU A 78 3401 4314 3228 113 280 251 C
ATOM 598 CD1BLEU A 78 26.504 170.588 27.206 0.30 29.39 C
ANISOU 598 CD1BLEU A 78 3505 4322 3338 109 270 205 C
ATOM 599 CD2ALEU A 78 26.478 170.886 27.349 0.70 27.23 C
ANISOU 599 CD2ALEU A 78 3234 4052 3060 105 265 203 C
ATOM 600 CD2BLEU A 78 27.806 170.344 29.327 0.30 31.29 C
ANISOU 600 CD2BLEU A 78 3716 4626 3546 115 282 251 C
ATOM 601 N PHE A 79 30.688 172.836 25.593 1.00 29.12 N
ANISOU 601 N PHE A 79 3474 4360 3230 65 233 227 N
ATOM 602 CA PHE A 79 31.197 174.162 25.322 1.00 29.45 C
ANISOU 602 CA PHE A 79 3526 4413 3249 44 213 213 C
ATOM 603 C PHE A 79 31.014 174.555 23.876 1.00 28.08 C
ANISOU 603 C PHE A 79 3378 4210 3082 36 204 192 C
ATOM 604 O PHE A 79 30.547 175.597 23.605 1.00 28.57 O
ANISOU 604 O PHE A 79 3457 4262 3137 22 187 171 O
ATOM 605 CB PHE A 79 32.645 174.403 25.760 1.00 30.90 C
ANISOU 605 CB PHE A 79 3694 4637 3410 38 214 233 C
ATOM 606 CG PHE A 79 33.124 175.797 25.473 1.00 32.41 C
ANISOU 606 CG PHE A 79 3897 4839 3579 15 196 215 C
ATOM 607 CD1 PHE A 79 32.777 176.840 26.274 1.00 33.80 C
ANISOU 607 CD1 PHE A 79 4076 5029 3738 0 183 203 C
ATOM 608 CD2 PHE A 79 33.874 176.062 24.377 1.00 33.01 C
ANISOU 608 CD2 PHE A 79 3984 4907 3652 8 195 210 C
ATOM 609 CE1 PHE A 79 33.179 178.107 25.996 1.00 34.64 C
ANISOU 609 CE1 PHE A 79 4194 5142 3824 -21 170 186 C
ATOM 610 CE2 PHE A 79 34.284 177.323 24.098 1.00 34.37 C
ANISOU 610 CE2 PHE A 79 4169 5086 3804 -12 181 193 C
ATOM 611 CZ PHE A 79 33.939 178.352 24.908 1.00 34.54 C
ANISOU 611 CZ PHE A 79 4192 5123 3809 -26 169 181 C
ATOM 612 N ILE A 80 31.369 173.681 22.968 1.00 27.47 N
ANISOU 612 N ILE A 80 3302 4117 3018 44 219 199 N
ATOM 613 CA ILE A 80 31.216 173.961 21.556 1.00 27.27 C
ANISOU 613 CA ILE A 80 3303 4063 2998 35 212 181 C
ATOM 614 C ILE A 80 29.760 173.971 21.099 1.00 25.09 C
ANISOU 614 C ILE A 80 3043 3752 2738 37 202 158 C
ATOM 615 O ILE A 80 29.463 174.607 20.154 1.00 24.83 O
ANISOU 615 O ILE A 80 3032 3699 2702 26 188 140 O
ATOM 616 CB ILE A 80 32.129 173.147 20.614 1.00 29.37 C
ANISOU 616 CB ILE A 80 3568 4320 3271 38 230 192 C
ATOM 617 CG1 ILE A 80 31.753 171.695 20.591 1.00 31.02 C
ANISOU 617 CG1 ILE A 80 3766 4515 3505 56 255 205 C
ATOM 618 CG2 ILE A 80 33.595 173.367 20.915 1.00 31.00 C
ANISOU 618 CG2 ILE A 80 3759 4558 3461 34 235 210 C
ATOM 619 CD1 ILE A 80 32.426 170.928 19.503 1.00 34.50 C
ANISOU 619 CD1 ILE A 80 4212 4940 3957 57 275 211 C
ATOM 620 N ALA A 81 28.892 173.273 21.805 1.00 23.72 N
ANISOU 620 N ALA A 81 2858 3574 2581 50 211 161 N
ATOM 621 CA ALA A 81 27.486 173.272 21.535 1.00 23.82 C
ANISOU 621 CA ALA A 81 2883 3557 2612 53 202 140 C
ATOM 622 C ALA A 81 26.834 174.556 22.040 1.00 24.58 C
ANISOU 622 C ALA A 81 2986 3654 2699 42 179 123 C
ATOM 623 O ALA A 81 26.024 175.101 21.382 1.00 24.83 O
ANISOU 623 O ALA A 81 3035 3662 2737 36 163 103 O
ATOM 624 CB ALA A 81 26.825 172.073 22.169 1.00 22.91 C
ANISOU 624 CB ALA A 81 2752 3435 2519 71 223 148 C
ATOM 625 N CYS A 82 27.270 175.049 23.184 1.00 24.72 N
ANISOU 625 N CYS A 82 2990 3700 2700 38 179 133 N
ATOM 626 CA CYS A 82 26.664 176.198 23.825 1.00 24.74 C
ANISOU 626 CA CYS A 82 2999 3706 2696 26 163 119 C
ATOM 627 C CYS A 82 27.231 177.573 23.580 1.00 24.34 C
ANISOU 627 C CYS A 82 2960 3665 2622 7 147 109 C
ATOM 628 O CYS A 82 26.612 178.521 23.951 1.00 23.89 O
ANISOU 628 O CYS A 82 2910 3604 2563 -3 136 95 O
ATOM 629 CB CYS A 82 26.607 175.988 25.343 1.00 26.46 C
ANISOU 629 CB CYS A 82 3197 3946 2910 30 174 131 C
ATOM 630 SG CYS A 82 25.680 174.614 25.974 1.00 28.64 S
ANISOU 630 SG CYS A 82 3461 4208 3214 51 194 138 S
ATOM 631 N PHE A 83 28.415 177.680 23.005 1.00 24.61 N
ANISOU 631 N PHE A 83 2997 3713 2639 1 149 117 N
ATOM 632 CA PHE A 83 28.995 178.987 22.803 1.00 24.28 C
ANISOU 632 CA PHE A 83 2968 3683 2576 -18 136 108 C
ATOM 633 C PHE A 83 28.096 179.921 21.993 1.00 23.02 C
ANISOU 633 C PHE A 83 2833 3493 2422 -26 118 84 C
ATOM 634 O PHE A 83 27.987 181.056 22.306 1.00 22.27 O
ANISOU 634 O PHE A 83 2744 3402 2315 -39 110 73 O
ATOM 635 CB PHE A 83 30.410 178.941 22.246 1.00 24.35 C
ANISOU 635 CB PHE A 83 2976 3708 2568 -23 142 118 C
ATOM 636 CG PHE A 83 31.054 180.273 22.203 1.00 25.19 C
ANISOU 636 CG PHE A 83 3092 3829 2650 -42 133 108 C
ATOM 637 CD1 PHE A 83 31.347 180.943 23.364 1.00 26.34 C
ANISOU 637 CD1 PHE A 83 3224 4005 2779 -53 133 109 C
ATOM 638 CD2 PHE A 83 31.294 180.897 21.013 1.00 24.46 C
ANISOU 638 CD2 PHE A 83 3023 3717 2552 -51 126 94 C
ATOM 639 CE1 PHE A 83 31.903 182.184 23.335 1.00 26.88 C
ANISOU 639 CE1 PHE A 83 3301 4085 2825 -72 128 97 C
ATOM 640 CE2 PHE A 83 31.847 182.139 20.983 1.00 25.19 C
ANISOU 640 CE2 PHE A 83 3126 3821 2624 -68 120 83 C
ATOM 641 CZ PHE A 83 32.164 182.785 22.140 1.00 26.13 C
ANISOU 641 CZ PHE A 83 3230 3971 2727 -79 122 84 C
ATOM 642 N VAL A 84 27.414 179.385 20.995 1.00 22.48 N
ANISOU 642 N VAL A 84 2777 3393 2371 -17 114 77 N
ATOM 643 CA VAL A 84 26.482 180.148 20.192 1.00 22.23 C
ANISOU 643 CA VAL A 84 2767 3332 2347 -22 95 56 C
ATOM 644 C VAL A 84 25.336 180.773 21.031 1.00 22.01 C
ANISOU 644 C VAL A 84 2736 3297 2332 -24 87 45 C
ATOM 645 O VAL A 84 24.862 181.813 20.727 1.00 21.18 O
ANISOU 645 O VAL A 84 2645 3178 2226 -32 73 31 O
ATOM 646 CB VAL A 84 25.948 179.351 18.994 1.00 22.26 C
ANISOU 646 CB VAL A 84 2784 3307 2368 -14 91 52 C
ATOM 647 CG1 VAL A 84 25.125 178.169 19.405 1.00 21.90 C
ANISOU 647 CG1 VAL A 84 2723 3252 2348 2 101 55 C
ATOM 648 CG2 VAL A 84 25.186 180.242 18.072 1.00 22.90 C
ANISOU 648 CG2 VAL A 84 2889 3360 2451 -20 68 33 C
ATOM 649 N LEU A 85 24.950 180.108 22.105 1.00 22.17 N
ANISOU 649 N LEU A 85 2736 3325 2363 -15 99 53 N
ATOM 650 CA LEU A 85 23.929 180.605 23.011 1.00 21.74 C
ANISOU 650 CA LEU A 85 2675 3263 2321 -17 96 43 C
ATOM 651 C LEU A 85 24.370 181.883 23.691 1.00 21.13 C
ANISOU 651 C LEU A 85 2600 3205 2222 -35 95 39 C
ATOM 652 O LEU A 85 23.597 182.740 23.898 1.00 21.52 O
ANISOU 652 O LEU A 85 2656 3241 2281 -43 88 25 O
ATOM 653 CB LEU A 85 23.524 179.540 24.018 1.00 21.88 C
ANISOU 653 CB LEU A 85 2674 3286 2355 -5 113 52 C
ATOM 654 CG LEU A 85 23.031 178.252 23.393 1.00 23.58 C
ANISOU 654 CG LEU A 85 2887 3481 2593 13 119 54 C
ATOM 655 CD1 LEU A 85 22.767 177.165 24.406 1.00 24.10 C
ANISOU 655 CD1 LEU A 85 2933 3553 2671 26 140 65 C
ATOM 656 CD2 LEU A 85 21.840 178.495 22.514 1.00 23.40 C
ANISOU 656 CD2 LEU A 85 2877 3422 2592 14 102 34 C
ATOM 657 N VAL A 86 25.641 181.966 24.026 1.00 21.03 N
ANISOU 657 N VAL A 86 2581 3225 2184 -43 103 51 N
ATOM 658 CA VAL A 86 26.244 183.137 24.610 1.00 21.39 C
ANISOU 658 CA VAL A 86 2628 3294 2207 -62 103 48 C
ATOM 659 C VAL A 86 26.130 184.285 23.619 1.00 21.46 C
ANISOU 659 C VAL A 86 2660 3283 2211 -73 90 31 C
ATOM 660 O VAL A 86 25.737 185.362 23.961 1.00 22.69 O
ANISOU 660 O VAL A 86 2822 3434 2365 -85 88 19 O
ATOM 661 CB VAL A 86 27.724 182.911 24.881 1.00 21.44 C
ANISOU 661 CB VAL A 86 2623 3338 2186 -67 112 64 C
ATOM 662 CG1 VAL A 86 28.401 184.177 25.319 1.00 21.48 C
ANISOU 662 CG1 VAL A 86 2630 3366 2165 -89 113 56 C
ATOM 663 CG2 VAL A 86 27.940 181.771 25.813 1.00 21.15 C
ANISOU 663 CG2 VAL A 86 2563 3323 2152 -55 125 83 C
ATOM 664 N LEU A 87 26.465 184.014 22.376 1.00 19.82 N
ANISOU 664 N LEU A 87 2465 3062 2002 -67 83 32 N
ATOM 665 CA LEU A 87 26.395 185.005 21.338 1.00 19.85 C
ANISOU 665 CA LEU A 87 2494 3046 2001 -75 71 18 C
ATOM 666 C LEU A 87 24.964 185.462 21.066 1.00 20.21 C
ANISOU 666 C LEU A 87 2550 3057 2070 -71 57 4 C
ATOM 667 O LEU A 87 24.734 186.605 20.909 1.00 22.03 O
ANISOU 667 O LEU A 87 2794 3279 2298 -81 51 -6 O
ATOM 668 CB LEU A 87 27.143 184.575 20.067 1.00 18.95 C
ANISOU 668 CB LEU A 87 2395 2927 1880 -71 68 22 C
ATOM 669 CG LEU A 87 28.602 184.128 20.148 1.00 20.26 C
ANISOU 669 CG LEU A 87 2551 3121 2026 -74 82 35 C
ATOM 670 CD1 LEU A 87 29.170 183.755 18.799 1.00 21.11 C
ANISOU 670 CD1 LEU A 87 2677 3214 2130 -72 80 36 C
ATOM 671 CD2 LEU A 87 29.481 185.115 20.858 1.00 19.95 C
ANISOU 671 CD2 LEU A 87 2507 3111 1962 -92 89 33 C
ATOM 672 N ALA A 88 24.019 184.548 21.054 1.00 18.82 N
ANISOU 672 N ALA A 88 2366 2864 1920 -57 53 5 N
ATOM 673 CA ALA A 88 22.647 184.904 20.850 1.00 19.07 C
ANISOU 673 CA ALA A 88 2404 2864 1977 -52 40 -7 C
ATOM 674 C ALA A 88 22.099 185.714 22.025 1.00 20.42 C
ANISOU 674 C ALA A 88 2566 3038 2156 -61 47 -14 C
ATOM 675 O ALA A 88 21.320 186.578 21.826 1.00 21.50 O
ANISOU 675 O ALA A 88 2711 3153 2305 -65 37 -25 O
ATOM 676 CB ALA A 88 21.818 183.682 20.625 1.00 18.73 C
ANISOU 676 CB ALA A 88 2352 2804 1960 -36 38 -6 C
ATOM 677 N GLN A 89 22.532 185.401 23.235 1.00 20.59 N
ANISOU 677 N GLN A 89 2570 3086 2169 -66 64 -6 N
ATOM 678 CA GLN A 89 22.096 186.092 24.428 1.00 20.56 C
ANISOU 678 CA GLN A 89 2558 3087 2168 -77 74 -12 C
ATOM 679 C GLN A 89 22.625 187.493 24.478 1.00 21.40 C
ANISOU 679 C GLN A 89 2675 3203 2254 -97 76 -19 C
ATOM 680 O GLN A 89 21.933 188.383 24.822 1.00 21.48 O
ANISOU 680 O GLN A 89 2689 3198 2276 -106 78 -30 O
ATOM 681 CB GLN A 89 22.487 185.345 25.672 1.00 21.14 C
ANISOU 681 CB GLN A 89 2611 3187 2233 -78 91 -1 C
ATOM 682 CG GLN A 89 21.618 185.669 26.846 1.00 24.75 C
ANISOU 682 CG GLN A 89 3060 3638 2706 -85 102 -8 C
ATOM 683 CD GLN A 89 20.171 185.406 26.593 1.00 26.03 C
ANISOU 683 CD GLN A 89 3224 3761 2907 -73 95 -19 C
ATOM 684 OE1 GLN A 89 19.807 184.366 26.172 1.00 25.42 O
ANISOU 684 OE1 GLN A 89 3141 3671 2845 -55 91 -16 O
ATOM 685 NE2 GLN A 89 19.351 186.362 26.880 1.00 26.87 N
ANISOU 685 NE2 GLN A 89 3334 3847 3030 -83 95 -33 N
ATOM 686 N SER A 90 23.874 187.651 24.092 1.00 21.37 N
ANISOU 686 N SER A 90 2676 3221 2221 -104 78 -14 N
ATOM 687 CA SER A 90 24.496 188.932 24.045 1.00 21.98 C
ANISOU 687 CA SER A 90 2765 3309 2277 -123 82 -22 C
ATOM 688 C SER A 90 23.754 189.826 23.085 1.00 22.91 C
ANISOU 688 C SER A 90 2903 3392 2408 -122 69 -34 C
ATOM 689 O SER A 90 23.552 190.968 23.344 1.00 24.13 O
ANISOU 689 O SER A 90 3065 3541 2562 -136 75 -44 O
ATOM 690 CB SER A 90 25.950 188.792 23.662 1.00 22.79 C
ANISOU 690 CB SER A 90 2870 3440 2350 -127 85 -14 C
ATOM 691 OG SER A 90 26.523 190.032 23.562 1.00 23.94 O
ANISOU 691 OG SER A 90 3027 3593 2476 -146 91 -24 O
ATOM 692 N SER A 91 23.350 189.251 21.977 1.00 22.61 N
ANISOU 692 N SER A 91 2876 3331 2384 -106 52 -32 N
ATOM 693 CA SER A 91 22.601 189.963 20.966 1.00 22.98 C
ANISOU 693 CA SER A 91 2943 3345 2445 -102 36 -40 C
ATOM 694 C SER A 91 21.253 190.471 21.480 1.00 23.98 C
ANISOU 694 C SER A 91 3064 3446 2602 -101 34 -49 C
ATOM 695 O SER A 91 20.859 191.548 21.172 1.00 24.66 O
ANISOU 695 O SER A 91 3163 3515 2694 -107 31 -56 O
ATOM 696 CB SER A 91 22.380 189.087 19.742 1.00 22.88 C
ANISOU 696 CB SER A 91 2939 3314 2440 -86 18 -36 C
ATOM 697 OG SER A 91 23.561 188.724 19.120 1.00 25.03 O
ANISOU 697 OG SER A 91 3220 3603 2687 -88 21 -30 O
ATOM 698 N ILE A 92 20.568 189.655 22.263 1.00 23.96 N
ANISOU 698 N ILE A 92 3042 3442 2620 -94 38 -47 N
ATOM 699 CA ILE A 92 19.284 189.984 22.846 1.00 24.54 C
ANISOU 699 CA ILE A 92 3107 3491 2726 -93 39 -56 C
ATOM 700 C ILE A 92 19.425 191.161 23.774 1.00 25.41 C
ANISOU 700 C ILE A 92 3217 3609 2829 -114 58 -62 C
ATOM 701 O ILE A 92 18.641 192.044 23.723 1.00 25.78 O
ANISOU 701 O ILE A 92 3269 3631 2895 -118 57 -71 O
ATOM 702 CB ILE A 92 18.648 188.775 23.547 1.00 24.57 C
ANISOU 702 CB ILE A 92 3091 3493 2751 -82 44 -53 C
ATOM 703 CG1 ILE A 92 18.080 187.836 22.503 1.00 25.62 C
ANISOU 703 CG1 ILE A 92 3227 3605 2902 -62 25 -52 C
ATOM 704 CG2 ILE A 92 17.593 189.199 24.544 1.00 25.05 C
ANISOU 704 CG2 ILE A 92 3142 3536 2841 -87 55 -63 C
ATOM 705 CD1 ILE A 92 17.962 186.417 22.948 1.00 27.28 C
ANISOU 705 CD1 ILE A 92 3420 3822 3122 -50 32 -46 C
ATOM 706 N PHE A 93 20.457 191.143 24.598 1.00 25.65 N
ANISOU 706 N PHE A 93 3241 3675 2831 -128 76 -58 N
ATOM 707 CA PHE A 93 20.752 192.230 25.513 1.00 27.90 C
ANISOU 707 CA PHE A 93 3525 3972 3102 -152 96 -66 C
ATOM 708 C PHE A 93 21.040 193.521 24.722 1.00 28.77 C
ANISOU 708 C PHE A 93 3655 4073 3203 -161 94 -73 C
ATOM 709 O PHE A 93 20.521 194.544 25.032 1.00 29.03 O
ANISOU 709 O PHE A 93 3692 4091 3248 -172 105 -82 O
ATOM 710 CB PHE A 93 21.902 191.884 26.464 1.00 28.81 C
ANISOU 710 CB PHE A 93 3629 4133 3186 -165 112 -59 C
ATOM 711 CG PHE A 93 21.550 190.886 27.538 1.00 31.26 C
ANISOU 711 CG PHE A 93 3920 4452 3504 -160 120 -53 C
ATOM 712 CD1 PHE A 93 20.344 190.937 28.196 1.00 34.59 C
ANISOU 712 CD1 PHE A 93 4336 4849 3958 -161 126 -60 C
ATOM 713 CD2 PHE A 93 22.419 189.900 27.885 1.00 32.14 C
ANISOU 713 CD2 PHE A 93 4020 4596 3596 -156 122 -39 C
ATOM 714 CE1 PHE A 93 20.036 190.029 29.182 1.00 35.83 C
ANISOU 714 CE1 PHE A 93 4479 5014 4122 -157 136 -55 C
ATOM 715 CE2 PHE A 93 22.122 188.991 28.868 1.00 33.86 C
ANISOU 715 CE2 PHE A 93 4222 4823 3820 -151 130 -32 C
ATOM 716 CZ PHE A 93 20.925 189.049 29.516 1.00 34.79 C
ANISOU 716 CZ PHE A 93 4337 4915 3967 -152 138 -41 C
ATOM 717 N SER A 94 21.872 193.433 23.697 1.00 27.93 N
ANISOU 717 N SER A 94 3562 3975 3076 -155 84 -68 N
ATOM 718 CA SER A 94 22.169 194.557 22.849 1.00 28.87 C
ANISOU 718 CA SER A 94 3702 4082 3184 -162 82 -74 C
ATOM 719 C SER A 94 20.901 195.130 22.204 1.00 29.55 C
ANISOU 719 C SER A 94 3799 4126 3302 -151 69 -79 C
ATOM 720 O SER A 94 20.692 196.300 22.222 1.00 30.58 O
ANISOU 720 O SER A 94 3938 4243 3436 -162 78 -86 O
ATOM 721 CB SER A 94 23.159 194.173 21.774 1.00 29.32 C
ANISOU 721 CB SER A 94 3773 4150 3217 -155 71 -68 C
ATOM 722 OG SER A 94 24.457 194.258 22.234 1.00 32.14 O
ANISOU 722 OG SER A 94 4127 4544 3543 -170 87 -68 O
ATOM 723 N LEU A 95 20.061 194.278 21.653 1.00 28.13 N
ANISOU 723 N LEU A 95 3616 3925 3147 -131 47 -74 N
ATOM 724 CA LEU A 95 18.832 194.723 21.031 1.00 28.13 C
ANISOU 724 CA LEU A 95 3622 3886 3179 -120 31 -77 C
ATOM 725 C LEU A 95 17.885 195.363 22.025 1.00 28.93 C
ANISOU 725 C LEU A 95 3711 3971 3309 -128 46 -84 C
ATOM 726 O LEU A 95 17.280 196.330 21.727 1.00 29.30 O
ANISOU 726 O LEU A 95 3766 3993 3373 -129 45 -88 O
ATOM 727 CB LEU A 95 18.141 193.608 20.265 1.00 27.25 C
ANISOU 727 CB LEU A 95 3509 3760 3087 -98 5 -72 C
ATOM 728 CG LEU A 95 18.777 193.064 19.002 1.00 27.13 C
ANISOU 728 CG LEU A 95 3510 3748 3051 -89 -14 -65 C
ATOM 729 CD1 LEU A 95 18.237 191.705 18.660 1.00 27.15 C
ANISOU 729 CD1 LEU A 95 3503 3744 3070 -73 -30 -62 C
ATOM 730 CD2 LEU A 95 18.596 194.000 17.853 1.00 26.90 C
ANISOU 730 CD2 LEU A 95 3506 3697 3019 -87 -29 -66 C
ATOM 731 N LEU A 96 17.792 194.818 23.216 1.00 28.91 N
ANISOU 731 N LEU A 96 3690 3984 3313 -135 62 -86 N
ATOM 732 CA LEU A 96 16.941 195.381 24.229 1.00 30.39 C
ANISOU 732 CA LEU A 96 3867 4155 3527 -145 80 -94 C
ATOM 733 C LEU A 96 17.432 196.769 24.642 1.00 31.89 C
ANISOU 733 C LEU A 96 4065 4350 3701 -169 104 -101 C
ATOM 734 O LEU A 96 16.659 197.656 24.816 1.00 32.49 O
ANISOU 734 O LEU A 96 4142 4400 3802 -175 114 -107 O
ATOM 735 CB LEU A 96 16.813 194.434 25.423 1.00 30.52 C
ANISOU 735 CB LEU A 96 3863 4186 3548 -148 93 -94 C
ATOM 736 CG LEU A 96 15.936 194.794 26.619 1.00 32.32 C
ANISOU 736 CG LEU A 96 4079 4398 3803 -161 115 -103 C
ATOM 737 CD1 LEU A 96 14.543 195.194 26.219 1.00 32.75 C
ANISOU 737 CD1 LEU A 96 4132 4407 3906 -150 105 -108 C
ATOM 738 CD2 LEU A 96 15.922 193.710 27.672 1.00 32.98 C
ANISOU 738 CD2 LEU A 96 4146 4498 3886 -161 125 -101 C
ATOM 739 N ALA A 97 18.735 196.931 24.751 1.00 32.01 N
ANISOU 739 N ALA A 97 4087 4401 3675 -183 115 -100 N
ATOM 740 CA ALA A 97 19.336 198.177 25.127 1.00 32.82 C
ANISOU 740 CA ALA A 97 4198 4514 3759 -207 140 -108 C
ATOM 741 C ALA A 97 19.111 199.254 24.093 1.00 33.00 C
ANISOU 741 C ALA A 97 4241 4509 3789 -203 135 -110 C
ATOM 742 O ALA A 97 18.875 200.367 24.429 1.00 33.34 O
ANISOU 742 O ALA A 97 4288 4539 3840 -218 156 -118 O
ATOM 743 CB ALA A 97 20.805 198.002 25.404 1.00 32.64 C
ANISOU 743 CB ALA A 97 4176 4536 3692 -221 150 -107 C
ATOM 744 N ILE A 98 19.181 198.893 22.829 1.00 32.38 N
ANISOU 744 N ILE A 98 4175 4421 3707 -183 108 -103 N
ATOM 745 CA ILE A 98 18.948 199.820 21.756 1.00 31.56 C
ANISOU 745 CA ILE A 98 4092 4290 3609 -176 100 -102 C
ATOM 746 C ILE A 98 17.512 200.311 21.833 1.00 32.99 C
ANISOU 746 C ILE A 98 4267 4431 3835 -168 97 -103 C
ATOM 747 O ILE A 98 17.286 201.465 21.702 1.00 34.36 O
ANISOU 747 O ILE A 98 4451 4587 4018 -175 110 -106 O
ATOM 748 CB ILE A 98 19.292 199.202 20.386 1.00 30.26 C
ANISOU 748 CB ILE A 98 3943 4123 3430 -157 70 -93 C
ATOM 749 CG1 ILE A 98 20.789 199.037 20.262 1.00 31.07 C
ANISOU 749 CG1 ILE A 98 4055 4261 3490 -167 79 -94 C
ATOM 750 CG2 ILE A 98 18.774 200.049 19.263 1.00 30.10 C
ANISOU 750 CG2 ILE A 98 3944 4071 3421 -146 56 -90 C
ATOM 751 CD1 ILE A 98 21.244 198.079 19.205 1.00 31.32 C
ANISOU 751 CD1 ILE A 98 4097 4298 3507 -152 54 -86 C
ATOM 752 N ALA A 99 16.560 199.419 22.064 1.00 32.79 N
ANISOU 752 N ALA A 99 4224 4393 3840 -155 82 -100 N
ATOM 753 CA ALA A 99 15.171 199.786 22.195 1.00 33.76 C
ANISOU 753 CA ALA A 99 4338 4478 4010 -147 79 -101 C
ATOM 754 C ALA A 99 14.943 200.748 23.344 1.00 36.04 C
ANISOU 754 C ALA A 99 4620 4761 4313 -170 116 -111 C
ATOM 755 O ALA A 99 14.270 201.710 23.186 1.00 37.01 O
ANISOU 755 O ALA A 99 4746 4854 4462 -170 123 -112 O
ATOM 756 CB ALA A 99 14.300 198.568 22.338 1.00 32.63 C
ANISOU 756 CB ALA A 99 4176 4326 3895 -131 59 -99 C
ATOM 757 N ILE A 100 15.534 200.466 24.490 1.00 36.31 N
ANISOU 757 N ILE A 100 4644 4823 4327 -190 139 -117 N
ATOM 758 CA ILE A 100 15.402 201.307 25.670 1.00 37.41 C
ANISOU 758 CA ILE A 100 4778 4962 4475 -216 177 -128 C
ATOM 759 C ILE A 100 16.029 202.693 25.477 1.00 38.46 C
ANISOU 759 C ILE A 100 4928 5096 4590 -234 201 -133 C
ATOM 760 O ILE A 100 15.453 203.687 25.808 1.00 38.76 O
ANISOU 760 O ILE A 100 4966 5109 4652 -245 224 -139 O
ATOM 761 CB ILE A 100 15.932 200.607 26.925 1.00 37.15 C
ANISOU 761 CB ILE A 100 4731 4962 4421 -233 194 -133 C
ATOM 762 CG1 ILE A 100 15.032 199.438 27.264 1.00 37.60 C
ANISOU 762 CG1 ILE A 100 4772 5007 4508 -217 180 -130 C
ATOM 763 CG2 ILE A 100 15.967 201.562 28.087 1.00 37.31 C
ANISOU 763 CG2 ILE A 100 4750 4985 4442 -265 235 -145 C
ATOM 764 CD1 ILE A 100 15.553 198.540 28.324 1.00 38.60 C
ANISOU 764 CD1 ILE A 100 4887 5167 4614 -228 190 -131 C
ATOM 765 N ASP A 101 17.214 202.706 24.910 1.00 38.35 N
ANISOU 765 N ASP A 101 4927 5110 4533 -235 196 -131 N
ATOM 766 CA ASP A 101 17.924 203.901 24.586 1.00 39.25 C
ANISOU 766 CA ASP A 101 5059 5227 4626 -250 216 -137 C
ATOM 767 C ASP A 101 17.068 204.803 23.694 1.00 40.32 C
ANISOU 767 C ASP A 101 5208 5319 4793 -236 210 -132 C
ATOM 768 O ASP A 101 16.943 205.956 23.955 1.00 40.85 O
ANISOU 768 O ASP A 101 5281 5372 4870 -251 239 -139 O
ATOM 769 CB ASP A 101 19.219 203.532 23.893 1.00 40.06 C
ANISOU 769 CB ASP A 101 5175 5361 4684 -247 203 -134 C
ATOM 770 CG ASP A 101 20.015 204.716 23.509 1.00 44.36 C
ANISOU 770 CG ASP A 101 5739 5910 5205 -261 225 -141 C
ATOM 771 OD1 ASP A 101 20.637 205.294 24.364 1.00 45.92 O
ANISOU 771 OD1 ASP A 101 5934 6130 5384 -289 257 -153 O
ATOM 772 OD2 ASP A 101 20.008 205.086 22.361 1.00 46.13 O
ANISOU 772 OD2 ASP A 101 5983 6115 5429 -246 211 -135 O
ATOM 773 N ARG A 102 16.490 204.259 22.638 1.00 40.46 N
ANISOU 773 N ARG A 102 5230 5318 4827 -207 173 -120 N
ATOM 774 CA ARG A 102 15.634 205.021 21.754 1.00 42.04 C
ANISOU 774 CA ARG A 102 5439 5477 5056 -191 162 -113 C
ATOM 775 C ARG A 102 14.360 205.521 22.478 1.00 45.03 C
ANISOU 775 C ARG A 102 5801 5822 5486 -194 178 -115 C
ATOM 776 O ARG A 102 13.857 206.567 22.180 1.00 46.52 O
ANISOU 776 O ARG A 102 5996 5980 5697 -192 189 -112 O
ATOM 777 CB ARG A 102 15.293 204.228 20.487 1.00 41.42 C
ANISOU 777 CB ARG A 102 5368 5388 4982 -161 115 -100 C
ATOM 778 CG ARG A 102 16.410 204.088 19.464 1.00 42.47 C
ANISOU 778 CG ARG A 102 5525 5542 5071 -156 101 -96 C
ATOM 779 CD ARG A 102 16.916 205.417 18.932 1.00 44.78 C
ANISOU 779 CD ARG A 102 5842 5824 5347 -163 120 -97 C
ATOM 780 NE ARG A 102 17.861 206.041 19.841 1.00 48.29 N
ANISOU 780 NE ARG A 102 6287 6294 5768 -192 162 -111 N
ATOM 781 CZ ARG A 102 18.133 207.331 19.931 1.00 49.72 C
ANISOU 781 CZ ARG A 102 6481 6466 5944 -207 194 -117 C
ATOM 782 NH1 ARG A 102 17.553 208.198 19.147 1.00 49.78 N
ANISOU 782 NH1 ARG A 102 6504 6440 5971 -194 192 -109 N
ATOM 783 NH2 ARG A 102 18.998 207.740 20.817 1.00 48.63 N
ANISOU 783 NH2 ARG A 102 6340 6355 5782 -235 231 -132 N
ATOM 784 N TYR A 103 13.857 204.758 23.432 1.00 45.42 N
ANISOU 784 N TYR A 103 5828 5874 5554 -198 181 -120 N
ATOM 785 CA TYR A 103 12.710 205.169 24.171 1.00 47.79 C
ANISOU 785 CA TYR A 103 6113 6142 5902 -203 199 -124 C
ATOM 786 C TYR A 103 13.051 206.345 25.091 1.00 49.06 C
ANISOU 786 C TYR A 103 6277 6304 6059 -235 250 -136 C
ATOM 787 O TYR A 103 12.292 207.248 25.234 1.00 50.22 O
ANISOU 787 O TYR A 103 6423 6418 6242 -239 269 -137 O
ATOM 788 CB TYR A 103 12.122 204.024 24.972 1.00 48.40 C
ANISOU 788 CB TYR A 103 6169 6222 6000 -201 192 -128 C
ATOM 789 CG TYR A 103 11.028 204.487 25.857 1.00 51.14 C
ANISOU 789 CG TYR A 103 6500 6536 6395 -211 218 -135 C
ATOM 790 CD1 TYR A 103 9.838 204.902 25.335 1.00 52.88 C
ANISOU 790 CD1 TYR A 103 6714 6712 6665 -194 206 -128 C
ATOM 791 CD2 TYR A 103 11.206 204.575 27.205 1.00 53.08 C
ANISOU 791 CD2 TYR A 103 6739 6794 6637 -240 255 -147 C
ATOM 792 CE1 TYR A 103 8.836 205.367 26.137 1.00 55.11 C
ANISOU 792 CE1 TYR A 103 6982 6961 6996 -203 232 -135 C
ATOM 793 CE2 TYR A 103 10.218 205.050 28.014 1.00 55.12 C
ANISOU 793 CE2 TYR A 103 6985 7019 6940 -252 282 -155 C
ATOM 794 CZ TYR A 103 9.028 205.430 27.473 1.00 56.59 C
ANISOU 794 CZ TYR A 103 7164 7159 7179 -233 271 -149 C
ATOM 795 OH TYR A 103 8.038 205.885 28.275 1.00 59.47 O
ANISOU 795 OH TYR A 103 7515 7487 7592 -245 300 -156 O
ATOM 796 N ILE A 104 14.215 206.322 25.694 1.00 48.40 N
ANISOU 796 N ILE A 104 6199 6261 5931 -259 270 -145 N
ATOM 797 CA ILE A 104 14.628 207.388 26.560 1.00 49.38 C
ANISOU 797 CA ILE A 104 6326 6390 6045 -292 318 -158 C
ATOM 798 C ILE A 104 14.776 208.674 25.773 1.00 50.59 C
ANISOU 798 C ILE A 104 6499 6524 6199 -292 332 -156 C
ATOM 799 O ILE A 104 14.357 209.706 26.210 1.00 51.58 O
ANISOU 799 O ILE A 104 6624 6626 6348 -308 368 -162 O
ATOM 800 CB ILE A 104 15.938 207.047 27.259 1.00 49.32 C
ANISOU 800 CB ILE A 104 6320 6435 5986 -317 332 -168 C
ATOM 801 CG1 ILE A 104 15.723 205.963 28.293 1.00 49.30 C
ANISOU 801 CG1 ILE A 104 6298 6448 5985 -322 329 -170 C
ATOM 802 CG2 ILE A 104 16.514 208.268 27.917 1.00 50.76 C
ANISOU 802 CG2 ILE A 104 6510 6626 6151 -352 380 -182 C
ATOM 803 CD1 ILE A 104 16.986 205.458 28.897 1.00 49.63 C
ANISOU 803 CD1 ILE A 104 6338 6542 5976 -341 334 -175 C
ATOM 804 N ALA A 105 15.347 208.572 24.593 1.00 50.24 N
ANISOU 804 N ALA A 105 6470 6487 6130 -273 305 -147 N
ATOM 805 CA ALA A 105 15.568 209.689 23.722 1.00 51.52 C
ANISOU 805 CA ALA A 105 6654 6632 6288 -269 315 -144 C
ATOM 806 C ALA A 105 14.301 210.377 23.273 1.00 53.98 C
ANISOU 806 C ALA A 105 6964 6893 6651 -252 313 -133 C
ATOM 807 O ALA A 105 14.290 211.559 23.114 1.00 54.76 O
ANISOU 807 O ALA A 105 7076 6973 6758 -259 341 -134 O
ATOM 808 CB ALA A 105 16.378 209.262 22.527 1.00 50.82 C
ANISOU 808 CB ALA A 105 6585 6561 6163 -250 282 -136 C
ATOM 809 N ILE A 106 13.233 209.636 23.069 1.00 54.92 N
ANISOU 809 N ILE A 106 7068 6991 6807 -228 280 -123 N
ATOM 810 CA ILE A 106 11.998 210.249 22.657 1.00 57.44 C
ANISOU 810 CA ILE A 106 7383 7263 7178 -211 275 -112 C
ATOM 811 C ILE A 106 11.088 210.665 23.808 1.00 59.86 C
ANISOU 811 C ILE A 106 7668 7543 7531 -228 310 -120 C
ATOM 812 O ILE A 106 10.369 211.609 23.685 1.00 61.47 O
ANISOU 812 O ILE A 106 7872 7710 7773 -225 328 -115 O
ATOM 813 CB ILE A 106 11.237 209.410 21.616 1.00 58.21 C
ANISOU 813 CB ILE A 106 7476 7345 7295 -175 219 -96 C
ATOM 814 CG1 ILE A 106 10.235 210.262 20.881 1.00 60.73 C
ANISOU 814 CG1 ILE A 106 7797 7619 7657 -155 212 -81 C
ATOM 815 CG2 ILE A 106 10.473 208.280 22.239 1.00 58.79 C
ANISOU 815 CG2 ILE A 106 7524 7417 7396 -170 202 -99 C
ATOM 816 CD1 ILE A 106 9.756 209.641 19.610 1.00 62.37 C
ANISOU 816 CD1 ILE A 106 8009 7818 7871 -122 156 -64 C
ATOM 817 N ALA A 107 11.138 209.974 24.925 1.00 60.25 N
ANISOU 817 N ALA A 107 7703 7612 7578 -247 323 -133 N
ATOM 818 CA ALA A 107 10.277 210.285 26.033 1.00 62.33 C
ANISOU 818 CA ALA A 107 7949 7850 7885 -264 356 -142 C
ATOM 819 C ALA A 107 10.808 211.405 26.876 1.00 64.70 C
ANISOU 819 C ALA A 107 8257 8154 8173 -301 414 -156 C
ATOM 820 O ALA A 107 10.073 212.231 27.328 1.00 66.35 O
ANISOU 820 O ALA A 107 8459 8328 8423 -312 448 -159 O
ATOM 821 CB ALA A 107 10.030 209.063 26.879 1.00 61.72 C
ANISOU 821 CB ALA A 107 7854 7787 7811 -268 346 -149 C
ATOM 822 N ILE A 108 12.095 211.424 27.119 1.00 64.71 N
ANISOU 822 N ILE A 108 8270 8198 8118 -322 428 -166 N
ATOM 823 CA ILE A 108 12.667 212.471 27.920 1.00 66.01 C
ANISOU 823 CA ILE A 108 8442 8372 8268 -360 483 -182 C
ATOM 824 C ILE A 108 13.942 213.005 27.318 1.00 65.54 C
ANISOU 824 C ILE A 108 8404 8340 8157 -366 490 -185 C
ATOM 825 O ILE A 108 14.993 212.872 27.887 1.00 64.96 O
ANISOU 825 O ILE A 108 8334 8309 8039 -391 505 -198 O
ATOM 826 CB ILE A 108 12.985 211.980 29.324 1.00 67.41 C
ANISOU 826 CB ILE A 108 8608 8577 8427 -393 507 -198 C
ATOM 827 CG1 ILE A 108 13.804 210.720 29.259 1.00 67.57 C
ANISOU 827 CG1 ILE A 108 8627 8644 8403 -384 470 -196 C
ATOM 828 CG2 ILE A 108 11.726 211.729 30.119 1.00 69.01 C
ANISOU 828 CG2 ILE A 108 8791 8746 8683 -395 517 -200 C
ATOM 829 CD1 ILE A 108 14.313 210.314 30.605 1.00 69.27 C
ANISOU 829 CD1 ILE A 108 8834 8894 8592 -418 493 -211 C
ATOM 830 N PRO A 109 13.849 213.689 26.178 1.00 66.07 N
ANISOU 830 N PRO A 109 8487 8384 8233 -345 481 -173 N
ATOM 831 CA PRO A 109 15.011 214.248 25.484 1.00 66.78 C
ANISOU 831 CA PRO A 109 8600 8495 8277 -348 488 -176 C
ATOM 832 C PRO A 109 15.844 215.256 26.305 1.00 69.78 C
ANISOU 832 C PRO A 109 8987 8893 8632 -390 548 -197 C
ATOM 833 O PRO A 109 17.024 215.392 26.083 1.00 69.66 O
ANISOU 833 O PRO A 109 8987 8912 8570 -400 554 -205 O
ATOM 834 CB PRO A 109 14.405 214.887 24.248 1.00 67.19 C
ANISOU 834 CB PRO A 109 8666 8508 8357 -317 473 -158 C
ATOM 835 CG PRO A 109 12.963 214.994 24.511 1.00 67.96 C
ANISOU 835 CG PRO A 109 8744 8561 8517 -306 473 -149 C
ATOM 836 CD PRO A 109 12.612 213.900 25.435 1.00 65.97 C
ANISOU 836 CD PRO A 109 8470 8324 8273 -314 461 -155 C
ATOM 837 N LEU A 110 15.191 215.969 27.214 1.00 72.19 N
ANISOU 837 N LEU A 110 9284 9175 8972 -413 592 -206 N
ATOM 838 CA LEU A 110 15.786 216.904 28.133 1.00 74.52 C
ANISOU 838 CA LEU A 110 9582 9482 9248 -457 652 -227 C
ATOM 839 C LEU A 110 16.834 216.209 28.993 1.00 74.64 C
ANISOU 839 C LEU A 110 9593 9555 9214 -484 653 -244 C
ATOM 840 O LEU A 110 17.951 216.656 29.090 1.00 75.13 O
ANISOU 840 O LEU A 110 9665 9648 9232 -507 676 -258 O
ATOM 841 CB LEU A 110 14.674 217.417 29.039 1.00 76.39 C
ANISOU 841 CB LEU A 110 9805 9681 9538 -474 690 -232 C
ATOM 842 CG LEU A 110 14.170 218.842 28.908 1.00 79.90 C
ANISOU 842 CG LEU A 110 10257 10082 10019 -482 738 -232 C
ATOM 843 CD1 LEU A 110 13.209 219.027 27.753 1.00 80.80 C
ANISOU 843 CD1 LEU A 110 10373 10149 10178 -438 709 -207 C
ATOM 844 CD2 LEU A 110 13.537 219.263 30.218 1.00 81.60 C
ANISOU 844 CD2 LEU A 110 10459 10278 10266 -518 789 -247 C
ATOM 845 N ARG A 111 16.456 215.104 29.614 1.00 74.00 N
ANISOU 845 N ARG A 111 9494 9485 9139 -482 627 -241 N
ATOM 846 CA ARG A 111 17.365 214.376 30.482 1.00 74.17 C
ANISOU 846 CA ARG A 111 9508 9559 9114 -506 626 -253 C
ATOM 847 C ARG A 111 18.238 213.296 29.833 1.00 71.82 C
ANISOU 847 C ARG A 111 9211 9300 8775 -484 577 -244 C
ATOM 848 O ARG A 111 19.077 212.722 30.495 1.00 71.31 O
ANISOU 848 O ARG A 111 9141 9282 8673 -502 575 -252 O
ATOM 849 CB ARG A 111 16.585 213.746 31.627 1.00 77.40 C
ANISOU 849 CB ARG A 111 9899 9964 9548 -519 630 -256 C
ATOM 850 CG ARG A 111 16.014 214.724 32.635 1.00 83.70 C
ANISOU 850 CG ARG A 111 10694 10736 10373 -555 688 -271 C
ATOM 851 CD ARG A 111 15.532 214.012 33.899 1.00 90.69 C
ANISOU 851 CD ARG A 111 11563 11627 11267 -575 694 -278 C
ATOM 852 NE ARG A 111 14.426 213.063 33.673 1.00 96.11 N
ANISOU 852 NE ARG A 111 12237 12284 11996 -541 656 -262 N
ATOM 853 CZ ARG A 111 13.126 213.376 33.655 1.00100.16 C
ANISOU 853 CZ ARG A 111 12743 12743 12571 -530 666 -258 C
ATOM 854 NH1 ARG A 111 12.717 214.620 33.841 1.00100.88 N
ANISOU 854 NH1 ARG A 111 12839 12799 12691 -550 714 -265 N
ATOM 855 NH2 ARG A 111 12.224 212.433 33.445 1.00100.45 N
ANISOU 855 NH2 ARG A 111 12767 12759 12642 -500 630 -246 N
ATOM 856 N TYR A 112 18.063 213.049 28.538 1.00 70.06 N
ANISOU 856 N TYR A 112 8998 9060 8561 -445 539 -227 N
ATOM 857 CA TYR A 112 18.804 211.986 27.862 1.00 68.64 C
ANISOU 857 CA TYR A 112 8821 8912 8348 -423 494 -218 C
ATOM 858 C TYR A 112 20.323 212.042 27.907 1.00 68.64 C
ANISOU 858 C TYR A 112 8829 8960 8292 -443 503 -230 C
ATOM 859 O TYR A 112 20.944 211.081 28.301 1.00 68.33 O
ANISOU 859 O TYR A 112 8779 8959 8224 -446 484 -229 O
ATOM 860 CB TYR A 112 18.324 211.775 26.430 1.00 67.49 C
ANISOU 860 CB TYR A 112 8685 8736 8221 -382 453 -199 C
ATOM 861 CG TYR A 112 19.125 210.766 25.660 1.00 66.53 C
ANISOU 861 CG TYR A 112 8569 8644 8065 -362 411 -191 C
ATOM 862 CD1 TYR A 112 20.288 211.118 25.048 1.00 67.03 C
ANISOU 862 CD1 TYR A 112 8651 8730 8089 -366 416 -196 C
ATOM 863 CD2 TYR A 112 18.715 209.474 25.546 1.00 66.34 C
ANISOU 863 CD2 TYR A 112 8533 8624 8050 -339 371 -179 C
ATOM 864 CE1 TYR A 112 21.034 210.211 24.351 1.00 67.01 C
ANISOU 864 CE1 TYR A 112 8653 8751 8057 -349 381 -189 C
ATOM 865 CE2 TYR A 112 19.453 208.557 24.841 1.00 66.20 C
ANISOU 865 CE2 TYR A 112 8520 8632 8002 -322 336 -172 C
ATOM 866 CZ TYR A 112 20.604 208.929 24.249 1.00 67.10 C
ANISOU 866 CZ TYR A 112 8651 8765 8077 -328 342 -176 C
ATOM 867 OH TYR A 112 21.348 208.047 23.547 1.00 67.79 O
ANISOU 867 OH TYR A 112 8744 8875 8138 -312 311 -169 O
ATOM 868 N ASN A 113 20.920 213.159 27.528 1.00 68.86 N
ANISOU 868 N ASN A 113 8874 8985 8304 -456 533 -239 N
ATOM 869 CA ASN A 113 22.373 213.263 27.505 1.00 69.33 C
ANISOU 869 CA ASN A 113 8941 9089 8312 -474 543 -252 C
ATOM 870 C ASN A 113 23.086 213.040 28.831 1.00 69.69 C
ANISOU 870 C ASN A 113 8971 9182 8328 -511 564 -268 C
ATOM 871 O ASN A 113 24.193 212.545 28.854 1.00 69.92 O
ANISOU 871 O ASN A 113 8998 9253 8316 -517 552 -272 O
ATOM 872 CB ASN A 113 22.821 214.576 26.858 1.00 71.22 C
ANISOU 872 CB ASN A 113 9203 9314 8544 -481 576 -262 C
ATOM 873 CG ASN A 113 22.964 214.459 25.363 1.00 74.33 C
ANISOU 873 CG ASN A 113 9617 9690 8935 -446 544 -248 C
ATOM 874 OD1 ASN A 113 23.038 213.367 24.826 1.00 74.63 O
ANISOU 874 OD1 ASN A 113 9652 9737 8966 -421 498 -234 O
ATOM 875 ND2 ASN A 113 22.993 215.584 24.687 1.00 75.91 N
ANISOU 875 ND2 ASN A 113 9838 9863 9140 -444 569 -251 N
ATOM 876 N GLY A 114 22.447 213.395 29.926 1.00 69.80 N
ANISOU 876 N GLY A 114 8974 9186 8360 -537 595 -277 N
ATOM 877 CA GLY A 114 23.062 213.220 31.211 1.00 70.58 C
ANISOU 877 CA GLY A 114 9060 9329 8429 -574 615 -292 C
ATOM 878 C GLY A 114 22.746 211.890 31.838 1.00 70.04 C
ANISOU 878 C GLY A 114 8972 9277 8362 -565 583 -280 C
ATOM 879 O GLY A 114 23.376 211.485 32.792 1.00 71.06 O
ANISOU 879 O GLY A 114 9090 9449 8461 -590 588 -288 O
ATOM 880 N LEU A 115 21.756 211.205 31.308 1.00 68.19 N
ANISOU 880 N LEU A 115 8735 9010 8165 -530 549 -262 N
ATOM 881 CA LEU A 115 21.385 209.919 31.851 1.00 67.49 C
ANISOU 881 CA LEU A 115 8630 8934 8081 -519 521 -252 C
ATOM 882 C LEU A 115 22.087 208.795 31.103 1.00 65.47 C
ANISOU 882 C LEU A 115 8372 8704 7800 -490 475 -237 C
ATOM 883 O LEU A 115 22.564 207.867 31.700 1.00 65.42 O
ANISOU 883 O LEU A 115 8352 8733 7770 -494 461 -234 O
ATOM 884 CB LEU A 115 19.861 209.769 31.842 1.00 68.08 C
ANISOU 884 CB LEU A 115 8699 8957 8211 -500 514 -243 C
ATOM 885 CG LEU A 115 19.072 208.467 31.663 1.00 70.10 C
ANISOU 885 CG LEU A 115 8943 9200 8493 -467 473 -226 C
ATOM 886 CD1 LEU A 115 19.167 207.535 32.852 1.00 71.41 C
ANISOU 886 CD1 LEU A 115 9094 9396 8644 -481 472 -228 C
ATOM 887 CD2 LEU A 115 17.619 208.791 31.390 1.00 71.06 C
ANISOU 887 CD2 LEU A 115 9064 9264 8673 -450 474 -221 C
ATOM 888 N VAL A 116 22.174 208.918 29.791 1.00 63.45 N
ANISOU 888 N VAL A 116 8130 8430 7549 -462 454 -229 N
ATOM 889 CA VAL A 116 22.774 207.900 28.985 1.00 61.57 C
ANISOU 889 CA VAL A 116 7892 8211 7291 -435 414 -216 C
ATOM 890 C VAL A 116 24.097 208.376 28.473 1.00 61.23 C
ANISOU 890 C VAL A 116 7861 8195 7207 -445 422 -224 C
ATOM 891 O VAL A 116 24.162 209.071 27.503 1.00 61.42 O
ANISOU 891 O VAL A 116 7904 8197 7235 -435 425 -225 O
ATOM 892 CB VAL A 116 21.832 207.502 27.838 1.00 60.88 C
ANISOU 892 CB VAL A 116 7812 8082 7239 -396 380 -199 C
ATOM 893 CG1 VAL A 116 22.350 206.307 27.088 1.00 60.12 C
ANISOU 893 CG1 VAL A 116 7714 8003 7124 -369 339 -186 C
ATOM 894 CG2 VAL A 116 20.471 207.176 28.388 1.00 61.10 C
ANISOU 894 CG2 VAL A 116 7826 8079 7311 -388 377 -195 C
ATOM 895 N THR A 117 25.157 207.990 29.152 1.00 60.77 N
ANISOU 895 N THR A 117 7793 8186 7112 -465 426 -230 N
ATOM 896 CA THR A 117 26.492 208.377 28.762 1.00 60.85 C
ANISOU 896 CA THR A 117 7811 8226 7083 -477 435 -239 C
ATOM 897 C THR A 117 27.237 207.199 28.236 1.00 59.97 C
ANISOU 897 C THR A 117 7694 8140 6952 -455 399 -226 C
ATOM 898 O THR A 117 26.821 206.082 28.380 1.00 59.43 O
ANISOU 898 O THR A 117 7613 8074 6894 -437 371 -211 O
ATOM 899 CB THR A 117 27.299 208.942 29.939 1.00 63.58 C
ANISOU 899 CB THR A 117 8146 8612 7397 -520 470 -258 C
ATOM 900 OG1 THR A 117 27.447 207.943 30.941 1.00 65.37 O
ANISOU 900 OG1 THR A 117 8352 8875 7611 -527 457 -252 O
ATOM 901 CG2 THR A 117 26.613 210.126 30.541 1.00 64.30 C
ANISOU 901 CG2 THR A 117 8244 8680 7508 -546 512 -273 C
ATOM 902 N GLY A 118 28.366 207.476 27.625 1.00 59.57 N
ANISOU 902 N GLY A 118 7653 8109 6873 -459 402 -232 N
ATOM 903 CA GLY A 118 29.206 206.448 27.072 1.00 58.63 C
ANISOU 903 CA GLY A 118 7529 8013 6734 -441 372 -221 C
ATOM 904 C GLY A 118 29.848 205.582 28.112 1.00 58.54 C
ANISOU 904 C GLY A 118 7492 8049 6700 -454 366 -217 C
ATOM 905 O GLY A 118 30.132 204.436 27.856 1.00 58.70 O
ANISOU 905 O GLY A 118 7503 8083 6716 -433 338 -202 O
ATOM 906 N THR A 119 30.096 206.142 29.278 1.00 58.22 N
ANISOU 906 N THR A 119 7442 8036 6644 -488 394 -231 N
ATOM 907 CA THR A 119 30.707 205.433 30.386 1.00 58.61 C
ANISOU 907 CA THR A 119 7467 8135 6669 -504 391 -228 C
ATOM 908 C THR A 119 29.737 204.434 30.999 1.00 57.20 C
ANISOU 908 C THR A 119 7274 7947 6511 -490 372 -211 C
ATOM 909 O THR A 119 30.109 203.330 31.290 1.00 57.44 O
ANISOU 909 O THR A 119 7288 8004 6531 -479 350 -197 O
ATOM 910 CB THR A 119 31.244 206.426 31.438 1.00 61.63 C
ANISOU 910 CB THR A 119 7844 8548 7026 -549 428 -250 C
ATOM 911 OG1 THR A 119 32.589 206.747 31.128 1.00 63.63 O
ANISOU 911 OG1 THR A 119 8097 8833 7246 -562 435 -261 O
ATOM 912 CG2 THR A 119 31.222 205.835 32.794 1.00 62.77 C
ANISOU 912 CG2 THR A 119 7967 8727 7157 -567 427 -245 C
ATOM 913 N ARG A 120 28.490 204.845 31.171 1.00 55.71 N
ANISOU 913 N ARG A 120 7092 7719 6355 -489 382 -214 N
ATOM 914 CA ARG A 120 27.448 203.986 31.699 1.00 54.74 C
ANISOU 914 CA ARG A 120 6959 7581 6258 -475 368 -201 C
ATOM 915 C ARG A 120 27.121 202.892 30.691 1.00 52.87 C
ANISOU 915 C ARG A 120 6723 7324 6040 -433 330 -181 C
ATOM 916 O ARG A 120 26.856 201.791 31.061 1.00 52.87 O
ANISOU 916 O ARG A 120 6711 7333 6047 -419 312 -168 O
ATOM 917 CB ARG A 120 26.189 204.779 32.031 1.00 56.25 C
ANISOU 917 CB ARG A 120 7158 7731 6484 -484 390 -210 C
ATOM 918 CG ARG A 120 26.348 205.713 33.210 1.00 60.58 C
ANISOU 918 CG ARG A 120 7704 8297 7017 -528 430 -229 C
ATOM 919 CD ARG A 120 25.099 206.459 33.566 1.00 63.43 C
ANISOU 919 CD ARG A 120 8071 8614 7415 -538 455 -237 C
ATOM 920 NE ARG A 120 25.412 207.469 34.549 1.00 68.34 N
ANISOU 920 NE ARG A 120 8694 9254 8019 -583 497 -258 N
ATOM 921 CZ ARG A 120 24.727 208.580 34.731 1.00 70.72 C
ANISOU 921 CZ ARG A 120 9006 9522 8344 -602 532 -272 C
ATOM 922 NH1 ARG A 120 23.669 208.837 34.010 1.00 68.53 N
ANISOU 922 NH1 ARG A 120 8737 9192 8111 -578 529 -266 N
ATOM 923 NH2 ARG A 120 25.108 209.431 35.649 1.00 72.17 N
ANISOU 923 NH2 ARG A 120 9189 9725 8507 -646 572 -292 N
ATOM 924 N ALA A 121 27.152 203.234 29.415 1.00 51.01 N
ANISOU 924 N ALA A 121 6505 7063 5813 -415 321 -181 N
ATOM 925 CA ALA A 121 26.884 202.309 28.338 1.00 49.00 C
ANISOU 925 CA ALA A 121 6256 6789 5574 -378 288 -165 C
ATOM 926 C ALA A 121 27.919 201.211 28.261 1.00 48.71 C
ANISOU 926 C ALA A 121 6206 6789 5512 -369 269 -153 C
ATOM 927 O ALA A 121 27.572 200.082 28.134 1.00 48.69 O
ANISOU 927 O ALA A 121 6195 6783 5521 -347 246 -138 O
ATOM 928 CB ALA A 121 26.793 203.035 27.024 1.00 48.04 C
ANISOU 928 CB ALA A 121 6157 6634 5461 -366 285 -168 C
ATOM 929 N ALA A 122 29.197 201.532 28.363 1.00 48.43 N
ANISOU 929 N ALA A 122 6170 6790 5443 -387 280 -160 N
ATOM 930 CA ALA A 122 30.229 200.509 28.322 1.00 47.89 C
ANISOU 930 CA ALA A 122 6087 6758 5352 -379 264 -148 C
ATOM 931 C ALA A 122 30.203 199.544 29.506 1.00 47.43 C
ANISOU 931 C ALA A 122 6003 6729 5288 -382 258 -136 C
ATOM 932 O ALA A 122 30.640 198.433 29.385 1.00 47.20 O
ANISOU 932 O ALA A 122 5963 6718 5254 -365 240 -119 O
ATOM 933 CB ALA A 122 31.595 201.124 28.183 1.00 48.80 C
ANISOU 933 CB ALA A 122 6204 6904 5434 -399 278 -159 C
ATOM 934 N GLY A 123 29.704 200.022 30.635 1.00 46.53 N
ANISOU 934 N GLY A 123 5884 6621 5175 -405 277 -144 N
ATOM 935 CA GLY A 123 29.582 199.233 31.826 1.00 46.04 C
ANISOU 935 CA GLY A 123 5801 6585 5106 -410 275 -134 C
ATOM 936 C GLY A 123 28.437 198.275 31.667 1.00 44.20 C
ANISOU 936 C GLY A 123 5567 6319 4908 -381 257 -120 C
ATOM 937 O GLY A 123 28.508 197.155 32.077 1.00 44.47 O
ANISOU 937 O GLY A 123 5587 6371 4940 -369 244 -104 O
ATOM 938 N ILE A 124 27.369 198.757 31.070 1.00 42.13 N
ANISOU 938 N ILE A 124 5320 6011 4678 -371 258 -127 N
ATOM 939 CA ILE A 124 26.235 197.944 30.798 1.00 40.65 C
ANISOU 939 CA ILE A 124 5132 5789 4526 -344 241 -117 C
ATOM 940 C ILE A 124 26.593 196.831 29.817 1.00 38.06 C
ANISOU 940 C ILE A 124 4802 5460 4198 -313 214 -100 C
ATOM 941 O ILE A 124 26.216 195.731 30.032 1.00 37.95 O
ANISOU 941 O ILE A 124 4777 5446 4196 -296 202 -87 O
ATOM 942 CB ILE A 124 25.085 198.767 30.269 1.00 41.27 C
ANISOU 942 CB ILE A 124 5226 5818 4638 -340 246 -127 C
ATOM 943 CG1 ILE A 124 24.480 199.542 31.397 1.00 44.14 C
ANISOU 943 CG1 ILE A 124 5587 6176 5010 -367 273 -140 C
ATOM 944 CG2 ILE A 124 24.028 197.890 29.667 1.00 40.06 C
ANISOU 944 CG2 ILE A 124 5072 5629 4520 -308 223 -116 C
ATOM 945 CD1 ILE A 124 23.638 200.691 30.931 1.00 45.87 C
ANISOU 945 CD1 ILE A 124 5821 6351 5256 -371 286 -152 C
ATOM 946 N ILE A 125 27.355 197.141 28.777 1.00 35.89 N
ANISOU 946 N ILE A 125 4539 5187 3911 -309 208 -102 N
ATOM 947 CA ILE A 125 27.772 196.179 27.781 1.00 34.73 C
ANISOU 947 CA ILE A 125 4393 5039 3763 -283 186 -88 C
ATOM 948 C ILE A 125 28.596 195.045 28.375 1.00 34.51 C
ANISOU 948 C ILE A 125 4344 5050 3717 -279 181 -73 C
ATOM 949 O ILE A 125 28.397 193.919 28.050 1.00 33.29 O
ANISOU 949 O ILE A 125 4184 4890 3575 -256 166 -58 O
ATOM 950 CB ILE A 125 28.521 196.861 26.637 1.00 35.11 C
ANISOU 950 CB ILE A 125 4461 5082 3798 -284 185 -95 C
ATOM 951 CG1 ILE A 125 27.561 197.714 25.846 1.00 35.84 C
ANISOU 951 CG1 ILE A 125 4575 5129 3914 -278 184 -105 C
ATOM 952 CG2 ILE A 125 29.217 195.849 25.756 1.00 34.12 C
ANISOU 952 CG2 ILE A 125 4335 4962 3666 -264 167 -82 C
ATOM 953 CD1 ILE A 125 28.213 198.549 24.793 1.00 37.59 C
ANISOU 953 CD1 ILE A 125 4818 5342 4122 -281 187 -113 C
ATOM 954 N ALA A 126 29.512 195.391 29.258 1.00 35.26 N
ANISOU 954 N ALA A 126 4428 5187 3782 -303 195 -76 N
ATOM 955 CA ALA A 126 30.363 194.448 29.951 1.00 35.94 C
ANISOU 955 CA ALA A 126 4492 5316 3849 -302 191 -60 C
ATOM 956 C ALA A 126 29.570 193.472 30.822 1.00 36.24 C
ANISOU 956 C ALA A 126 4516 5352 3901 -292 187 -47 C
ATOM 957 O ALA A 126 29.806 192.305 30.812 1.00 35.11 O
ANISOU 957 O ALA A 126 4360 5219 3759 -272 176 -29 O
ATOM 958 CB ALA A 126 31.363 195.199 30.790 1.00 36.64 C
ANISOU 958 CB ALA A 126 4572 5448 3903 -334 207 -69 C
ATOM 959 N ILE A 127 28.623 194.014 31.560 1.00 37.01 N
ANISOU 959 N ILE A 127 4616 5434 4010 -305 199 -58 N
ATOM 960 CA ILE A 127 27.749 193.280 32.442 1.00 37.57 C
ANISOU 960 CA ILE A 127 4679 5499 4098 -299 200 -50 C
ATOM 961 C ILE A 127 26.913 192.301 31.641 1.00 35.37 C
ANISOU 961 C ILE A 127 4402 5183 3852 -265 184 -41 C
ATOM 962 O ILE A 127 26.780 191.175 31.991 1.00 34.90 O
ANISOU 962 O ILE A 127 4331 5131 3799 -249 178 -26 O
ATOM 963 CB ILE A 127 26.862 194.256 33.240 1.00 39.23 C
ANISOU 963 CB ILE A 127 4896 5692 4318 -323 219 -68 C
ATOM 964 CG1 ILE A 127 27.634 194.847 34.400 1.00 42.33 C
ANISOU 964 CG1 ILE A 127 5280 6128 4675 -357 237 -74 C
ATOM 965 CG2 ILE A 127 25.639 193.580 33.772 1.00 39.30 C
ANISOU 965 CG2 ILE A 127 4901 5675 4357 -311 220 -64 C
ATOM 966 CD1 ILE A 127 27.008 196.071 34.989 1.00 44.57 C
ANISOU 966 CD1 ILE A 127 5574 6396 4965 -387 261 -95 C
ATOM 967 N CYS A 128 26.399 192.776 30.526 1.00 33.84 N
ANISOU 967 N CYS A 128 4226 4954 3680 -255 176 -50 N
ATOM 968 CA CYS A 128 25.597 191.995 29.634 1.00 32.59 C
ANISOU 968 CA CYS A 128 4071 4760 3552 -226 160 -44 C
ATOM 969 C CYS A 128 26.375 190.830 29.032 1.00 31.55 C
ANISOU 969 C CYS A 128 3932 4644 3410 -206 147 -26 C
ATOM 970 O CYS A 128 25.836 189.785 28.897 1.00 31.14 O
ANISOU 970 O CYS A 128 3874 4578 3378 -185 139 -17 O
ATOM 971 CB CYS A 128 24.938 192.888 28.580 1.00 32.74 C
ANISOU 971 CB CYS A 128 4110 4740 3590 -223 154 -57 C
ATOM 972 SG CYS A 128 23.598 193.912 29.175 1.00 35.63 S
ANISOU 972 SG CYS A 128 4482 5072 3984 -237 168 -74 S
ATOM 973 N TRP A 129 27.649 191.020 28.732 1.00 30.53 N
ANISOU 973 N TRP A 129 3802 4543 3253 -213 147 -23 N
ATOM 974 CA TRP A 129 28.465 189.957 28.201 1.00 29.87 C
ANISOU 974 CA TRP A 129 3711 4476 3163 -196 139 -6 C
ATOM 975 C TRP A 129 28.705 188.887 29.248 1.00 30.32 C
ANISOU 975 C TRP A 129 3745 4561 3213 -190 142 12 C
ATOM 976 O TRP A 129 28.669 187.740 28.944 1.00 30.12 O
ANISOU 976 O TRP A 129 3713 4531 3200 -169 137 26 O
ATOM 977 CB TRP A 129 29.768 190.472 27.603 1.00 29.58 C
ANISOU 977 CB TRP A 129 3680 4460 3100 -206 140 -8 C
ATOM 978 CG TRP A 129 29.678 190.868 26.153 1.00 28.89 C
ANISOU 978 CG TRP A 129 3615 4340 3022 -198 131 -17 C
ATOM 979 CD1 TRP A 129 29.578 192.103 25.675 1.00 29.83 C
ANISOU 979 CD1 TRP A 129 3753 4443 3137 -211 134 -34 C
ATOM 980 CD2 TRP A 129 29.696 190.007 25.021 1.00 28.35 C
ANISOU 980 CD2 TRP A 129 3554 4252 2966 -176 119 -9 C
ATOM 981 NE1 TRP A 129 29.531 192.096 24.336 1.00 29.72 N
ANISOU 981 NE1 TRP A 129 3759 4402 3131 -199 124 -36 N
ATOM 982 CE2 TRP A 129 29.596 190.812 23.897 1.00 28.99 C
ANISOU 982 CE2 TRP A 129 3661 4307 3048 -178 114 -21 C
ATOM 983 CE3 TRP A 129 29.777 188.633 24.850 1.00 28.06 C
ANISOU 983 CE3 TRP A 129 3506 4217 2939 -156 114 9 C
ATOM 984 CZ2 TRP A 129 29.581 190.296 22.631 1.00 28.74 C
ANISOU 984 CZ2 TRP A 129 3643 4251 3025 -162 102 -18 C
ATOM 985 CZ3 TRP A 129 29.763 188.136 23.605 1.00 28.29 C
ANISOU 985 CZ3 TRP A 129 3549 4223 2979 -142 104 11 C
ATOM 986 CH2 TRP A 129 29.661 188.949 22.511 1.00 28.27 C
ANISOU 986 CH2 TRP A 129 3572 4195 2975 -145 98 -2 C
ATOM 987 N VAL A 130 28.941 189.297 30.487 1.00 31.13 N
ANISOU 987 N VAL A 130 3838 4693 3298 -211 154 10 N
ATOM 988 CA VAL A 130 29.120 188.375 31.595 1.00 32.37 C
ANISOU 988 CA VAL A 130 3974 4878 3446 -208 158 28 C
ATOM 989 C VAL A 130 27.832 187.564 31.791 1.00 32.13 C
ANISOU 989 C VAL A 130 3944 4816 3448 -189 157 31 C
ATOM 990 O VAL A 130 27.878 186.393 31.926 1.00 32.66 O
ANISOU 990 O VAL A 130 4000 4888 3522 -169 156 49 O
ATOM 991 CB VAL A 130 29.524 189.091 32.910 1.00 35.07 C
ANISOU 991 CB VAL A 130 4309 5257 3760 -238 170 23 C
ATOM 992 CG1 VAL A 130 29.523 188.132 34.068 1.00 36.00 C
ANISOU 992 CG1 VAL A 130 4409 5399 3871 -233 173 42 C
ATOM 993 CG2 VAL A 130 30.859 189.776 32.789 1.00 35.66 C
ANISOU 993 CG2 VAL A 130 4379 5367 3802 -257 171 20 C
ATOM 994 N LEU A 131 26.687 188.227 31.781 1.00 31.11 N
ANISOU 994 N LEU A 131 3828 4652 3341 -194 160 13 N
ATOM 995 CA LEU A 131 25.408 187.587 31.918 1.00 30.27 C
ANISOU 995 CA LEU A 131 3722 4512 3267 -178 161 12 C
ATOM 996 C LEU A 131 25.144 186.601 30.786 1.00 27.61 C
ANISOU 996 C LEU A 131 3387 4150 2952 -149 148 20 C
ATOM 997 O LEU A 131 24.601 185.577 31.020 1.00 27.02 O
ANISOU 997 O LEU A 131 3305 4066 2896 -131 150 28 O
ATOM 998 CB LEU A 131 24.308 188.612 31.997 1.00 31.11 C
ANISOU 998 CB LEU A 131 3842 4585 3395 -191 166 -9 C
ATOM 999 CG LEU A 131 24.196 189.414 33.274 1.00 35.39 C
ANISOU 999 CG LEU A 131 4382 5141 3924 -220 184 -18 C
ATOM 1000 CD1 LEU A 131 23.065 190.411 33.211 1.00 35.34 C
ANISOU 1000 CD1 LEU A 131 4388 5094 3944 -230 191 -39 C
ATOM 1001 CD2 LEU A 131 24.044 188.521 34.477 1.00 36.72 C
ANISOU 1001 CD2 LEU A 131 4538 5325 4089 -218 193 -7 C
ATOM 1002 N SER A 132 25.565 186.957 29.581 1.00 25.98 N
ANISOU 1002 N SER A 132 3192 3936 2744 -145 137 16 N
ATOM 1003 CA SER A 132 25.439 186.136 28.392 1.00 24.67 C
ANISOU 1003 CA SER A 132 3030 3749 2595 -122 126 22 C
ATOM 1004 C SER A 132 26.213 184.835 28.522 1.00 24.98 C
ANISOU 1004 C SER A 132 3054 3812 2626 -107 129 43 C
ATOM 1005 O SER A 132 25.759 183.809 28.105 1.00 24.55 O
ANISOU 1005 O SER A 132 2997 3739 2591 -87 127 50 O
ATOM 1006 CB SER A 132 25.867 186.889 27.129 1.00 24.38 C
ANISOU 1006 CB SER A 132 3012 3701 2551 -126 115 13 C
ATOM 1007 OG SER A 132 25.096 188.011 26.896 1.00 24.74 O
ANISOU 1007 OG SER A 132 3072 3721 2608 -136 112 -5 O
ATOM 1008 N PHE A 133 27.389 184.907 29.117 1.00 25.82 N
ANISOU 1008 N PHE A 133 3149 3959 2702 -118 135 55 N
ATOM 1009 CA PHE A 133 28.201 183.735 29.370 1.00 27.13 C
ANISOU 1009 CA PHE A 133 3297 4151 2860 -104 139 78 C
ATOM 1010 C PHE A 133 27.508 182.835 30.403 1.00 28.24 C
ANISOU 1010 C PHE A 133 3425 4291 3013 -93 149 88 C
ATOM 1011 O PHE A 133 27.424 181.669 30.215 1.00 28.79 O
ANISOU 1011 O PHE A 133 3487 4354 3097 -72 152 102 O
ATOM 1012 CB PHE A 133 29.626 184.115 29.771 1.00 27.27 C
ANISOU 1012 CB PHE A 133 3304 4214 2844 -119 142 88 C
ATOM 1013 CG PHE A 133 30.569 184.267 28.609 1.00 27.74 C
ANISOU 1013 CG PHE A 133 3371 4275 2896 -118 136 88 C
ATOM 1014 CD1 PHE A 133 31.245 183.192 28.116 1.00 28.25 C
ANISOU 1014 CD1 PHE A 133 3424 4345 2964 -101 138 106 C
ATOM 1015 CD2 PHE A 133 30.775 185.485 28.029 1.00 27.52 C
ANISOU 1015 CD2 PHE A 133 3358 4239 2857 -136 132 69 C
ATOM 1016 CE1 PHE A 133 32.097 183.325 27.065 1.00 28.58 C
ANISOU 1016 CE1 PHE A 133 3474 4385 3000 -102 135 105 C
ATOM 1017 CE2 PHE A 133 31.622 185.623 26.974 1.00 27.92 C
ANISOU 1017 CE2 PHE A 133 3418 4289 2901 -135 129 68 C
ATOM 1018 CZ PHE A 133 32.286 184.542 26.489 1.00 27.97 C
ANISOU 1018 CZ PHE A 133 3415 4301 2912 -119 130 86 C
ATOM 1019 N ALA A 134 27.003 183.428 31.471 1.00 27.70 N
ANISOU 1019 N ALA A 134 3357 4228 2940 -109 155 80 N
ATOM 1020 CA ALA A 134 26.270 182.737 32.500 1.00 28.44 C
ANISOU 1020 CA ALA A 134 3443 4319 3045 -102 165 86 C
ATOM 1021 C ALA A 134 25.022 182.020 31.969 1.00 28.17 C
ANISOU 1021 C ALA A 134 3414 4240 3050 -81 166 79 C
ATOM 1022 O ALA A 134 24.812 180.901 32.283 1.00 28.35 O
ANISOU 1022 O ALA A 134 3428 4261 3084 -63 174 92 O
ATOM 1023 CB ALA A 134 25.902 183.691 33.607 1.00 29.34 C
ANISOU 1023 CB ALA A 134 3559 4440 3147 -128 173 74 C
ATOM 1024 N ILE A 135 24.228 182.685 31.153 1.00 26.92 N
ANISOU 1024 N ILE A 135 3270 4046 2911 -83 157 59 N
ATOM 1025 CA ILE A 135 23.023 182.115 30.590 1.00 25.63 C
ANISOU 1025 CA ILE A 135 3112 3842 2785 -65 155 50 C
ATOM 1026 C ILE A 135 23.331 181.036 29.548 1.00 24.53 C
ANISOU 1026 C ILE A 135 2971 3696 2655 -43 151 61 C
ATOM 1027 O ILE A 135 22.885 179.939 29.661 1.00 23.56 O
ANISOU 1027 O ILE A 135 2840 3562 2550 -26 159 67 O
ATOM 1028 CB ILE A 135 22.082 183.200 30.032 1.00 25.83 C
ANISOU 1028 CB ILE A 135 3152 3832 2829 -75 145 26 C
ATOM 1029 CG1 ILE A 135 21.462 184.023 31.146 1.00 27.37 C
ANISOU 1029 CG1 ILE A 135 3348 4024 3028 -94 155 14 C
ATOM 1030 CG2 ILE A 135 20.958 182.603 29.229 1.00 25.46 C
ANISOU 1030 CG2 ILE A 135 3109 3746 2820 -56 138 17 C
ATOM 1031 CD1 ILE A 135 20.860 185.315 30.691 1.00 27.72 C
ANISOU 1031 CD1 ILE A 135 3406 4043 3084 -107 148 -6 C
ATOM 1032 N GLY A 136 24.148 181.366 28.571 1.00 24.15 N
ANISOU 1032 N GLY A 136 2929 3654 2592 -46 140 62 N
ATOM 1033 CA GLY A 136 24.509 180.447 27.517 1.00 24.03 C
ANISOU 1033 CA GLY A 136 2914 3633 2584 -29 138 71 C
ATOM 1034 C GLY A 136 25.292 179.235 27.938 1.00 25.03 C
ANISOU 1034 C GLY A 136 3024 3783 2703 -16 152 96 C
ATOM 1035 O GLY A 136 25.157 178.205 27.357 1.00 24.69 O
ANISOU 1035 O GLY A 136 2978 3726 2676 1 157 102 O
ATOM 1036 N LEU A 137 26.119 179.391 28.953 1.00 25.45 N
ANISOU 1036 N LEU A 137 3065 3874 2732 -25 158 109 N
ATOM 1037 CA LEU A 137 26.904 178.304 29.440 1.00 26.68 C
ANISOU 1037 CA LEU A 137 3202 4055 2879 -12 171 135 C
ATOM 1038 C LEU A 137 26.377 177.656 30.696 1.00 27.28 C
ANISOU 1038 C LEU A 137 3267 4137 2961 -4 185 145 C
ATOM 1039 O LEU A 137 27.043 176.914 31.287 1.00 28.16 O
ANISOU 1039 O LEU A 137 3363 4274 3062 4 195 168 O
ATOM 1040 CB LEU A 137 28.378 178.659 29.534 1.00 27.69 C
ANISOU 1040 CB LEU A 137 3322 4223 2977 -22 168 150 C
ATOM 1041 CG LEU A 137 29.073 179.223 28.312 1.00 28.17 C
ANISOU 1041 CG LEU A 137 3394 4280 3030 -29 158 142 C
ATOM 1042 CD1 LEU A 137 30.531 179.469 28.592 1.00 29.30 C
ANISOU 1042 CD1 LEU A 137 3524 4464 3145 -39 159 157 C
ATOM 1043 CD2 LEU A 137 28.887 178.357 27.086 1.00 27.89 C
ANISOU 1043 CD2 LEU A 137 3365 4215 3017 -12 161 143 C
ATOM 1044 N THR A 138 25.118 177.899 31.006 1.00 26.67 N
ANISOU 1044 N THR A 138 3198 4032 2903 -6 186 127 N
ATOM 1045 CA THR A 138 24.404 177.301 32.128 1.00 27.19 C
ANISOU 1045 CA THR A 138 3257 4093 2979 1 201 131 C
ATOM 1046 C THR A 138 24.452 175.768 32.105 1.00 27.30 C
ANISOU 1046 C THR A 138 3260 4105 3008 27 217 150 C
ATOM 1047 O THR A 138 24.607 175.179 33.116 1.00 27.64 O
ANISOU 1047 O THR A 138 3293 4166 3044 33 231 167 O
ATOM 1048 CB THR A 138 22.950 177.843 32.269 1.00 28.28 C
ANISOU 1048 CB THR A 138 3407 4194 3143 -6 200 104 C
ATOM 1049 OG1 THR A 138 22.957 178.982 33.089 1.00 30.79 O
ANISOU 1049 OG1 THR A 138 3730 4526 3444 -30 198 95 O
ATOM 1050 CG2 THR A 138 22.026 176.864 32.881 1.00 28.10 C
ANISOU 1050 CG2 THR A 138 3380 4152 3145 10 217 104 C
ATOM 1051 N PRO A 139 24.355 175.140 30.939 1.00 26.34 N
ANISOU 1051 N PRO A 139 3140 3961 2905 41 217 148 N
ATOM 1052 CA PRO A 139 24.482 173.702 30.884 1.00 26.62 C
ANISOU 1052 CA PRO A 139 3165 3994 2955 65 236 167 C
ATOM 1053 C PRO A 139 25.813 173.192 31.465 1.00 28.24 C
ANISOU 1053 C PRO A 139 3353 4240 3135 70 245 199 C
ATOM 1054 O PRO A 139 25.841 172.129 32.011 1.00 28.63 O
ANISOU 1054 O PRO A 139 3392 4295 3192 88 264 218 O
ATOM 1055 CB PRO A 139 24.397 173.424 29.403 1.00 26.41 C
ANISOU 1055 CB PRO A 139 3146 3942 2945 71 231 157 C
ATOM 1056 CG PRO A 139 23.539 174.497 28.909 1.00 25.99 C
ANISOU 1056 CG PRO A 139 3110 3865 2900 57 212 128 C
ATOM 1057 CD PRO A 139 24.016 175.686 29.631 1.00 24.83 C
ANISOU 1057 CD PRO A 139 2964 3744 2726 37 201 128 C
ATOM 1058 N MET A 140 26.872 173.975 31.329 1.00 28.53 N
ANISOU 1058 N MET A 140 3388 4306 3145 55 231 205 N
ATOM 1059 CA MET A 140 28.209 173.645 31.852 1.00 30.52 C
ANISOU 1059 CA MET A 140 3622 4601 3373 58 235 236 C
ATOM 1060 C MET A 140 28.298 173.669 33.371 1.00 32.72 C
ANISOU 1060 C MET A 140 3890 4908 3632 54 239 250 C
ATOM 1061 O MET A 140 29.160 173.090 33.935 1.00 34.03 O
ANISOU 1061 O MET A 140 4040 5106 3784 62 246 278 O
ATOM 1062 CB MET A 140 29.302 174.509 31.236 1.00 30.77 C
ANISOU 1062 CB MET A 140 3654 4653 3383 42 219 235 C
ATOM 1063 CG MET A 140 29.491 174.287 29.761 1.00 31.69 C
ANISOU 1063 CG MET A 140 3779 4746 3515 48 218 228 C
ATOM 1064 SD MET A 140 30.869 175.119 29.032 1.00 42.05 S
ANISOU 1064 SD MET A 140 5092 6080 4804 31 205 229 S
ATOM 1065 CE MET A 140 32.089 173.853 29.203 1.00 34.91 C
ANISOU 1065 CE MET A 140 4162 5203 3900 51 222 267 C
ATOM 1066 N LEU A 141 27.345 174.307 34.023 1.00 33.21 N
ANISOU 1066 N LEU A 141 3964 4959 3695 41 237 230 N
ATOM 1067 CA LEU A 141 27.244 174.326 35.466 1.00 35.34 C
ANISOU 1067 CA LEU A 141 4229 5251 3948 35 243 240 C
ATOM 1068 C LEU A 141 26.481 173.095 36.037 1.00 36.13 C
ANISOU 1068 C LEU A 141 4327 5333 4070 58 266 250 C
ATOM 1069 O LEU A 141 26.273 173.003 37.222 1.00 37.66 O
ANISOU 1069 O LEU A 141 4519 5539 4252 54 274 258 O
ATOM 1070 CB LEU A 141 26.677 175.649 35.960 1.00 35.75 C
ANISOU 1070 CB LEU A 141 4295 5300 3990 7 233 214 C
ATOM 1071 CG LEU A 141 27.272 176.952 35.448 1.00 38.24 C
ANISOU 1071 CG LEU A 141 4615 5629 4285 -17 215 200 C
ATOM 1072 CD1 LEU A 141 26.705 178.135 36.170 1.00 39.07 C
ANISOU 1072 CD1 LEU A 141 4733 5733 4381 -45 212 178 C
ATOM 1073 CD2 LEU A 141 28.766 177.002 35.507 1.00 39.41 C
ANISOU 1073 CD2 LEU A 141 4748 5822 4403 -22 208 222 C
ATOM 1074 N GLY A 142 26.154 172.156 35.165 1.00 34.34 N
ANISOU 1074 N GLY A 142 4099 5077 3872 80 277 251 N
ATOM 1075 CA GLY A 142 25.483 170.952 35.568 1.00 34.86 C
ANISOU 1075 CA GLY A 142 4163 5124 3961 102 301 259 C
ATOM 1076 C GLY A 142 24.188 170.558 34.893 1.00 33.76 C
ANISOU 1076 C GLY A 142 4034 4934 3859 112 311 233 C
ATOM 1077 O GLY A 142 23.779 169.432 34.993 1.00 34.59 O
ANISOU 1077 O GLY A 142 4135 5023 3985 133 334 241 O
ATOM 1078 N TRP A 143 23.527 171.487 34.232 1.00 31.18 N
ANISOU 1078 N TRP A 143 3720 4583 3542 97 295 203 N
ATOM 1079 CA TRP A 143 22.291 171.168 33.549 1.00 29.19 C
ANISOU 1079 CA TRP A 143 3477 4286 3327 105 300 178 C
ATOM 1080 C TRP A 143 22.594 170.616 32.156 1.00 27.73 C
ANISOU 1080 C TRP A 143 3291 4089 3156 116 299 179 C
ATOM 1081 O TRP A 143 22.463 171.276 31.184 1.00 26.60 O
ANISOU 1081 O TRP A 143 3157 3933 3017 107 281 161 O
ATOM 1082 CB TRP A 143 21.353 172.366 33.523 1.00 27.78 C
ANISOU 1082 CB TRP A 143 3312 4086 3157 86 284 147 C
ATOM 1083 CG TRP A 143 19.898 172.112 33.178 1.00 26.92 C
ANISOU 1083 CG TRP A 143 3210 3931 3087 92 290 120 C
ATOM 1084 CD1 TRP A 143 19.322 170.945 32.845 1.00 26.89 C
ANISOU 1084 CD1 TRP A 143 3203 3903 3111 113 309 117 C
ATOM 1085 CD2 TRP A 143 18.860 173.085 33.142 1.00 25.38 C
ANISOU 1085 CD2 TRP A 143 3026 3709 2908 78 278 91 C
ATOM 1086 NE1 TRP A 143 18.014 171.117 32.604 1.00 26.59 N
ANISOU 1086 NE1 TRP A 143 3172 3826 3104 112 307 89 N
ATOM 1087 CE2 TRP A 143 17.697 172.429 32.775 1.00 25.78 C
ANISOU 1087 CE2 TRP A 143 3078 3721 2997 91 288 72 C
ATOM 1088 CE3 TRP A 143 18.811 174.451 33.376 1.00 25.44 C
ANISOU 1088 CE3 TRP A 143 3042 3722 2903 54 261 78 C
ATOM 1089 CZ2 TRP A 143 16.496 173.088 32.640 1.00 26.21 C
ANISOU 1089 CZ2 TRP A 143 3140 3742 3078 82 279 44 C
ATOM 1090 CZ3 TRP A 143 17.627 175.095 33.246 1.00 26.06 C
ANISOU 1090 CZ3 TRP A 143 3128 3766 3008 46 255 51 C
ATOM 1091 CH2 TRP A 143 16.486 174.426 32.883 1.00 26.18 C
ANISOU 1091 CH2 TRP A 143 3142 3743 3062 61 263 34 C
ATOM 1092 N ASN A 144 23.003 169.374 32.122 1.00 28.19 N
ANISOU 1092 N ASN A 144 3339 4151 3221 137 321 200 N
ATOM 1093 CA ASN A 144 23.372 168.674 30.920 1.00 28.95 C
ANISOU 1093 CA ASN A 144 3432 4236 3330 148 328 204 C
ATOM 1094 C ASN A 144 23.091 167.178 30.993 1.00 31.17 C
ANISOU 1094 C ASN A 144 3706 4502 3635 172 361 216 C
ATOM 1095 O ASN A 144 22.672 166.667 31.994 1.00 32.14 O
ANISOU 1095 O ASN A 144 3825 4625 3764 182 380 223 O
ATOM 1096 CB ASN A 144 24.839 168.930 30.614 1.00 29.34 C
ANISOU 1096 CB ASN A 144 3475 4320 3353 142 318 227 C
ATOM 1097 CG ASN A 144 25.755 168.417 31.694 1.00 32.55 C
ANISOU 1097 CG ASN A 144 3864 4762 3741 152 331 262 C
ATOM 1098 OD1 ASN A 144 25.854 167.258 31.916 1.00 34.69 O
ANISOU 1098 OD1 ASN A 144 4125 5031 4024 172 357 281 O
ATOM 1099 ND2 ASN A 144 26.419 169.295 32.343 1.00 32.89 N
ANISOU 1099 ND2 ASN A 144 3904 4838 3754 137 314 270 N
ATOM 1100 N ASN A 145 23.334 166.484 29.903 1.00 32.01 N
ANISOU 1100 N ASN A 145 3811 4595 3756 180 371 218 N
ATOM 1101 CA ASN A 145 23.126 165.063 29.825 1.00 33.88 C
ANISOU 1101 CA ASN A 145 4040 4816 4016 202 406 228 C
ATOM 1102 C ASN A 145 24.440 164.294 29.862 1.00 36.37 C
ANISOU 1102 C ASN A 145 4340 5157 4322 214 425 265 C
ATOM 1103 O ASN A 145 24.501 163.184 29.446 1.00 37.02 O
ANISOU 1103 O ASN A 145 4417 5225 4423 230 453 274 O
ATOM 1104 CB ASN A 145 22.348 164.670 28.571 1.00 33.76 C
ANISOU 1104 CB ASN A 145 4034 4764 4029 202 411 201 C
ATOM 1105 CG ASN A 145 21.028 165.378 28.434 1.00 36.18 C
ANISOU 1105 CG ASN A 145 4353 5043 4349 191 393 165 C
ATOM 1106 OD1 ASN A 145 20.324 165.586 29.375 1.00 36.98 O
ANISOU 1106 OD1 ASN A 145 4456 5141 4455 191 394 157 O
ATOM 1107 ND2 ASN A 145 20.704 165.745 27.237 1.00 37.72 N
ANISOU 1107 ND2 ASN A 145 4560 5221 4552 180 375 143 N
ATOM 1108 N CYS A 146 25.489 164.917 30.352 1.00 37.69 N
ANISOU 1108 N CYS A 146 4500 5360 4459 207 408 286 N
ATOM 1109 CA CYS A 146 26.787 164.292 30.425 1.00 39.84 C
ANISOU 1109 CA CYS A 146 4755 5660 4722 218 422 322 C
ATOM 1110 C CYS A 146 26.776 163.144 31.415 1.00 42.79 C
ANISOU 1110 C CYS A 146 5115 6039 5104 242 454 350 C
ATOM 1111 O CYS A 146 27.535 162.225 31.311 1.00 43.76 O
ANISOU 1111 O CYS A 146 5224 6170 5234 259 477 378 O
ATOM 1112 CB CYS A 146 27.861 165.311 30.773 1.00 40.65 C
ANISOU 1112 CB CYS A 146 4852 5802 4791 203 394 336 C
ATOM 1113 SG CYS A 146 28.340 166.468 29.498 1.00 43.82 S
ANISOU 1113 SG CYS A 146 5266 6202 5182 179 364 315 S
ATOM 1114 N GLY A 147 25.847 163.184 32.350 1.00 44.13 N
ANISOU 1114 N GLY A 147 5291 6201 5276 245 457 340 N
ATOM 1115 CA GLY A 147 25.682 162.129 33.317 1.00 46.78 C
ANISOU 1115 CA GLY A 147 5618 6538 5620 267 489 362 C
ATOM 1116 C GLY A 147 25.024 160.875 32.773 1.00 48.70 C
ANISOU 1116 C GLY A 147 5862 6744 5899 286 527 355 C
ATOM 1117 O GLY A 147 25.065 159.850 33.390 1.00 50.77 O
ANISOU 1117 O GLY A 147 6115 7006 6170 308 559 378 O
ATOM 1118 N GLN A 148 24.391 160.967 31.620 1.00 47.88 N
ANISOU 1118 N GLN A 148 5768 6609 5815 277 524 324 N
ATOM 1119 CA GLN A 148 23.732 159.841 30.985 1.00 48.09 C
ANISOU 1119 CA GLN A 148 5796 6600 5875 291 559 313 C
ATOM 1120 C GLN A 148 24.152 159.705 29.519 1.00 47.07 C
ANISOU 1120 C GLN A 148 5669 6460 5756 284 558 305 C
ATOM 1121 O GLN A 148 23.362 159.897 28.624 1.00 45.98 O
ANISOU 1121 O GLN A 148 5543 6294 5633 272 551 272 O
ATOM 1122 CB GLN A 148 22.219 160.006 31.078 1.00 50.91 C
ANISOU 1122 CB GLN A 148 6167 6924 6252 286 558 274 C
ATOM 1123 CG GLN A 148 21.596 159.867 32.468 1.00 58.81 C
ANISOU 1123 CG GLN A 148 7169 7925 7252 296 570 277 C
ATOM 1124 CD GLN A 148 20.436 158.876 32.543 1.00 68.68 C
ANISOU 1124 CD GLN A 148 8422 9137 8536 310 607 258 C
ATOM 1125 OE1 GLN A 148 20.630 157.658 32.512 1.00 70.90 O
ANISOU 1125 OE1 GLN A 148 8695 9410 8833 330 647 275 O
ATOM 1126 NE2 GLN A 148 19.219 159.401 32.626 1.00 71.23 N
ANISOU 1126 NE2 GLN A 148 8756 9435 8873 299 596 221 N
ATOM 1127 N PRO A 149 25.415 159.356 29.277 1.00 47.27 N
ANISOU 1127 N PRO A 149 5681 6505 5772 289 567 337 N
ATOM 1128 CA PRO A 149 25.899 159.239 27.916 1.00 46.91 C
ANISOU 1128 CA PRO A 149 5639 6449 5735 280 569 331 C
ATOM 1129 C PRO A 149 25.341 158.086 27.139 1.00 48.45 C
ANISOU 1129 C PRO A 149 5837 6609 5963 289 607 319 C
ATOM 1130 O PRO A 149 24.974 157.077 27.675 1.00 49.53 O
ANISOU 1130 O PRO A 149 5967 6736 6118 308 644 329 O
ATOM 1131 CB PRO A 149 27.392 159.037 28.097 1.00 47.94 C
ANISOU 1131 CB PRO A 149 5752 6610 5852 288 575 372 C
ATOM 1132 CG PRO A 149 27.554 158.506 29.440 1.00 48.86 C
ANISOU 1132 CG PRO A 149 5853 6746 5964 308 592 402 C
ATOM 1133 CD PRO A 149 26.487 159.130 30.250 1.00 47.59 C
ANISOU 1133 CD PRO A 149 5705 6582 5796 303 573 380 C
ATOM 1134 N LYS A 150 25.276 158.271 25.843 1.00 48.49 N
ANISOU 1134 N LYS A 150 5854 6597 5974 273 600 298 N
ATOM 1135 CA LYS A 150 24.834 157.239 24.958 1.00 49.29 C
ANISOU 1135 CA LYS A 150 5958 6667 6103 275 635 284 C
ATOM 1136 C LYS A 150 26.058 156.396 24.675 1.00 50.48 C
ANISOU 1136 C LYS A 150 6096 6826 6260 285 668 319 C
ATOM 1137 O LYS A 150 26.801 156.697 23.804 1.00 49.70 O
ANISOU 1137 O LYS A 150 6000 6729 6154 272 658 321 O
ATOM 1138 CB LYS A 150 24.274 157.862 23.698 1.00 49.90 C
ANISOU 1138 CB LYS A 150 6055 6723 6181 252 610 247 C
ATOM 1139 CG LYS A 150 23.106 158.750 23.989 1.00 52.14 C
ANISOU 1139 CG LYS A 150 6350 7000 6461 243 576 216 C
ATOM 1140 CD LYS A 150 22.043 158.699 22.939 1.00 56.20 C
ANISOU 1140 CD LYS A 150 6879 7483 6992 230 571 177 C
ATOM 1141 CE LYS A 150 20.929 159.639 23.331 1.00 60.13 C
ANISOU 1141 CE LYS A 150 7384 7974 7488 222 537 150 C
ATOM 1142 NZ LYS A 150 19.969 159.848 22.239 1.00 63.19 N
ANISOU 1142 NZ LYS A 150 7786 8336 7888 207 520 113 N
ATOM 1143 N GLU A 151 26.258 155.342 25.451 1.00 52.17 N
ANISOU 1143 N GLU A 151 6293 7042 6488 310 708 347 N
ATOM 1144 CA GLU A 151 27.429 154.483 25.302 1.00 54.36 C
ANISOU 1144 CA GLU A 151 6554 7327 6774 322 743 384 C
ATOM 1145 C GLU A 151 27.358 153.613 24.068 1.00 55.31 C
ANISOU 1145 C GLU A 151 6680 7415 6920 316 780 371 C
ATOM 1146 O GLU A 151 28.346 153.269 23.513 1.00 56.57 O
ANISOU 1146 O GLU A 151 6832 7577 7084 315 797 391 O
ATOM 1147 CB GLU A 151 27.690 153.651 26.556 1.00 57.72 C
ANISOU 1147 CB GLU A 151 6960 7766 7205 352 774 421 C
ATOM 1148 CG GLU A 151 27.994 154.431 27.826 1.00 62.12 C
ANISOU 1148 CG GLU A 151 7510 8360 7734 357 740 441 C
ATOM 1149 CD GLU A 151 29.263 155.249 27.761 1.00 70.29 C
ANISOU 1149 CD GLU A 151 8537 9428 8744 347 708 462 C
ATOM 1150 OE1 GLU A 151 29.820 155.418 26.685 1.00 73.19 O
ANISOU 1150 OE1 GLU A 151 8907 9789 9114 333 704 456 O
ATOM 1151 OE2 GLU A 151 29.719 155.738 28.788 1.00 72.68 O
ANISOU 1151 OE2 GLU A 151 8829 9764 9023 352 686 484 O
ATOM 1152 N GLY A 152 26.173 153.282 23.623 1.00 54.74 N
ANISOU 1152 N GLY A 152 6620 7313 6864 310 792 336 N
ATOM 1153 CA GLY A 152 26.027 152.489 22.431 1.00 54.83 C
ANISOU 1153 CA GLY A 152 6640 7295 6899 301 826 320 C
ATOM 1154 C GLY A 152 26.439 153.273 21.211 1.00 54.30 C
ANISOU 1154 C GLY A 152 6588 7227 6818 273 796 303 C
ATOM 1155 O GLY A 152 26.976 152.739 20.277 1.00 55.30 O
ANISOU 1155 O GLY A 152 6717 7339 6955 264 822 306 O
ATOM 1156 N LYS A 153 26.155 154.561 21.220 1.00 52.27 N
ANISOU 1156 N LYS A 153 6343 6981 6536 258 741 285 N
ATOM 1157 CA LYS A 153 26.511 155.433 20.133 1.00 50.86 C
ANISOU 1157 CA LYS A 153 6182 6803 6342 233 708 269 C
ATOM 1158 C LYS A 153 27.997 155.758 20.194 1.00 50.58 C
ANISOU 1158 C LYS A 153 6135 6791 6291 233 703 302 C
ATOM 1159 O LYS A 153 28.632 155.908 19.185 1.00 50.50 O
ANISOU 1159 O LYS A 153 6136 6775 6278 216 702 299 O
ATOM 1160 CB LYS A 153 25.681 156.703 20.187 1.00 50.82 C
ANISOU 1160 CB LYS A 153 6191 6801 6317 219 655 239 C
ATOM 1161 CG LYS A 153 25.770 157.582 18.976 1.00 52.06 C
ANISOU 1161 CG LYS A 153 6370 6952 6459 192 621 217 C
ATOM 1162 CD LYS A 153 24.954 158.839 19.140 1.00 54.97 C
ANISOU 1162 CD LYS A 153 6752 7325 6811 182 570 191 C
ATOM 1163 CE LYS A 153 23.466 158.575 19.150 1.00 57.53 C
ANISOU 1163 CE LYS A 153 7080 7626 7152 183 570 160 C
ATOM 1164 NZ LYS A 153 22.662 159.691 18.616 1.00 58.57 N
ANISOU 1164 NZ LYS A 153 7230 7751 7274 165 523 129 N
ATOM 1165 N ALA A 154 28.541 155.859 21.391 1.00 50.60 N
ANISOU 1165 N ALA A 154 6119 6822 6285 251 699 333 N
ATOM 1166 CA ALA A 154 29.944 156.146 21.558 1.00 52.15 C
ANISOU 1166 CA ALA A 154 6303 7045 6469 253 693 366 C
ATOM 1167 C ALA A 154 30.808 154.935 21.239 1.00 54.54 C
ANISOU 1167 C ALA A 154 6590 7338 6796 265 745 395 C
ATOM 1168 O ALA A 154 31.864 155.077 20.706 1.00 54.87 O
ANISOU 1168 O ALA A 154 6628 7385 6835 256 747 409 O
ATOM 1169 CB ALA A 154 30.236 156.648 22.951 1.00 52.09 C
ANISOU 1169 CB ALA A 154 6279 7072 6442 268 671 389 C
ATOM 1170 N HIS A 155 30.330 153.735 21.528 1.00 55.76 N
ANISOU 1170 N HIS A 155 6735 7475 6975 283 791 402 N
ATOM 1171 CA HIS A 155 31.094 152.542 21.237 1.00 58.13 C
ANISOU 1171 CA HIS A 155 7021 7764 7302 294 845 430 C
ATOM 1172 C HIS A 155 31.067 152.243 19.781 1.00 58.96 C
ANISOU 1172 C HIS A 155 7143 7838 7421 271 865 406 C
ATOM 1173 O HIS A 155 32.014 151.735 19.240 1.00 60.25 O
ANISOU 1173 O HIS A 155 7300 7995 7598 269 896 425 O
ATOM 1174 CB HIS A 155 30.609 151.360 22.026 1.00 59.80 C
ANISOU 1174 CB HIS A 155 7218 7966 7536 321 891 446 C
ATOM 1175 CG HIS A 155 30.980 151.427 23.461 1.00 63.58 C
ANISOU 1175 CG HIS A 155 7676 8477 8003 346 881 481 C
ATOM 1176 ND1 HIS A 155 30.194 150.907 24.453 1.00 66.04 N
ANISOU 1176 ND1 HIS A 155 7982 8787 8321 367 898 485 N
ATOM 1177 CD2 HIS A 155 32.027 152.008 24.075 1.00 65.71 C
ANISOU 1177 CD2 HIS A 155 7930 8783 8254 352 855 513 C
ATOM 1178 CE1 HIS A 155 30.756 151.136 25.620 1.00 67.64 C
ANISOU 1178 CE1 HIS A 155 8168 9024 8508 385 882 520 C
ATOM 1179 NE2 HIS A 155 31.874 151.802 25.417 1.00 67.76 N
ANISOU 1179 NE2 HIS A 155 8176 9062 8507 376 856 537 N
ATOM 1180 N SER A 156 29.995 152.617 19.124 1.00 58.12 N
ANISOU 1180 N SER A 156 7061 7713 7310 252 847 363 N
ATOM 1181 CA SER A 156 29.928 152.395 17.720 1.00 58.98 C
ANISOU 1181 CA SER A 156 7189 7793 7427 228 862 339 C
ATOM 1182 C SER A 156 30.919 153.256 16.949 1.00 59.91 C
ANISOU 1182 C SER A 156 7318 7919 7527 207 835 340 C
ATOM 1183 O SER A 156 31.406 152.841 15.936 1.00 61.30 O
ANISOU 1183 O SER A 156 7502 8075 7714 191 861 337 O
ATOM 1184 CB SER A 156 28.502 152.483 17.203 1.00 59.40 C
ANISOU 1184 CB SER A 156 7263 7824 7481 213 850 294 C
ATOM 1185 OG SER A 156 28.124 153.784 16.930 1.00 61.34 O
ANISOU 1185 OG SER A 156 7527 8079 7700 196 792 269 O
ATOM 1186 N GLN A 157 31.234 154.446 17.423 1.00 59.39 N
ANISOU 1186 N GLN A 157 7251 7880 7433 205 784 344 N
ATOM 1187 CA GLN A 157 32.201 155.265 16.740 1.00 59.61 C
ANISOU 1187 CA GLN A 157 7289 7915 7444 186 761 345 C
ATOM 1188 C GLN A 157 33.569 155.152 17.349 1.00 60.04 C
ANISOU 1188 C GLN A 157 7318 7994 7502 201 772 387 C
ATOM 1189 O GLN A 157 34.387 156.001 17.148 1.00 60.49 O
ANISOU 1189 O GLN A 157 7377 8065 7540 189 746 391 O
ATOM 1190 CB GLN A 157 31.853 156.723 16.782 1.00 60.92 C
ANISOU 1190 CB GLN A 157 7471 8097 7579 172 700 323 C
ATOM 1191 CG GLN A 157 30.418 157.093 16.785 1.00 65.74 C
ANISOU 1191 CG GLN A 157 8097 8697 8183 167 675 289 C
ATOM 1192 CD GLN A 157 30.284 158.562 16.574 1.00 72.42 C
ANISOU 1192 CD GLN A 157 8962 9554 8999 150 619 269 C
ATOM 1193 OE1 GLN A 157 29.267 159.032 16.130 1.00 74.10 O
ANISOU 1193 OE1 GLN A 157 9195 9755 9207 137 594 237 O
ATOM 1194 NE2 GLN A 157 31.326 159.296 16.874 1.00 73.76 N
ANISOU 1194 NE2 GLN A 157 9125 9749 9152 148 600 287 N
ATOM 1195 N GLY A 158 33.815 154.132 18.132 1.00 59.89 N
ANISOU 1195 N GLY A 158 7272 7979 7503 226 811 419 N
ATOM 1196 CA GLY A 158 35.122 153.970 18.701 1.00 60.41 C
ANISOU 1196 CA GLY A 158 7312 8068 7573 241 821 462 C
ATOM 1197 C GLY A 158 35.619 155.074 19.595 1.00 59.80 C
ANISOU 1197 C GLY A 158 7223 8031 7466 245 772 475 C
ATOM 1198 O GLY A 158 36.795 155.315 19.668 1.00 61.45 O
ANISOU 1198 O GLY A 158 7418 8259 7673 246 769 499 O
ATOM 1199 N CYS A 159 34.733 155.713 20.323 1.00 57.27 N
ANISOU 1199 N CYS A 159 6909 7725 7126 248 738 459 N
ATOM 1200 CA CYS A 159 35.126 156.763 21.238 1.00 56.60 C
ANISOU 1200 CA CYS A 159 6815 7679 7011 250 693 470 C
ATOM 1201 C CYS A 159 35.797 156.181 22.454 1.00 58.60 C
ANISOU 1201 C CYS A 159 7036 7961 7270 277 709 515 C
ATOM 1202 O CYS A 159 35.574 155.059 22.802 1.00 59.87 O
ANISOU 1202 O CYS A 159 7184 8111 7453 298 748 533 O
ATOM 1203 CB CYS A 159 33.935 157.622 21.669 1.00 53.91 C
ANISOU 1203 CB CYS A 159 6492 7343 6650 243 654 439 C
ATOM 1204 SG CYS A 159 33.025 158.458 20.385 1.00 50.71 S
ANISOU 1204 SG CYS A 159 6124 6909 6235 213 627 387 S
ATOM 1205 N GLY A 160 36.603 156.975 23.113 1.00 59.22 N
ANISOU 1205 N GLY A 160 7100 8075 7325 277 677 532 N
ATOM 1206 CA GLY A 160 37.280 156.515 24.283 1.00 61.67 C
ANISOU 1206 CA GLY A 160 7378 8417 7635 302 685 576 C
ATOM 1207 C GLY A 160 36.498 156.650 25.564 1.00 63.12 C
ANISOU 1207 C GLY A 160 7559 8620 7802 315 669 580 C
ATOM 1208 O GLY A 160 35.347 156.992 25.556 1.00 62.39 O
ANISOU 1208 O GLY A 160 7488 8514 7703 307 655 547 O
ATOM 1209 N GLU A 161 37.165 156.392 26.674 1.00 65.01 N
ANISOU 1209 N GLU A 161 7771 8894 8035 335 669 620 N
ATOM 1210 CA GLU A 161 36.559 156.455 27.968 1.00 65.96 C
ANISOU 1210 CA GLU A 161 7889 9035 8139 348 656 628 C
ATOM 1211 C GLU A 161 36.324 157.874 28.315 1.00 64.47 C
ANISOU 1211 C GLU A 161 7712 8869 7914 326 605 603 C
ATOM 1212 O GLU A 161 37.192 158.700 28.171 1.00 65.57 O
ANISOU 1212 O GLU A 161 7847 9032 8036 312 578 606 O
ATOM 1213 CB GLU A 161 37.471 155.850 29.015 1.00 71.87 C
ANISOU 1213 CB GLU A 161 8604 9816 8887 373 668 681 C
ATOM 1214 CG GLU A 161 37.716 154.370 28.840 1.00 81.08 C
ANISOU 1214 CG GLU A 161 9754 10961 10090 399 723 712 C
ATOM 1215 CD GLU A 161 36.453 153.551 28.853 1.00 88.87 C
ANISOU 1215 CD GLU A 161 10757 11913 11097 410 757 695 C
ATOM 1216 OE1 GLU A 161 35.571 153.851 29.655 1.00 91.01 O
ANISOU 1216 OE1 GLU A 161 11038 12190 11350 412 740 682 O
ATOM 1217 OE2 GLU A 161 36.341 152.603 28.070 1.00 90.88 O
ANISOU 1217 OE2 GLU A 161 11013 12133 11384 416 801 694 O
ATOM 1218 N GLY A 162 35.114 158.161 28.752 1.00 61.89 N
ANISOU 1218 N GLY A 162 7404 8533 7579 323 594 578 N
ATOM 1219 CA GLY A 162 34.735 159.506 29.114 1.00 59.95 C
ANISOU 1219 CA GLY A 162 7172 8304 7302 302 548 552 C
ATOM 1220 C GLY A 162 34.274 160.363 27.960 1.00 56.89 C
ANISOU 1220 C GLY A 162 6810 7892 6912 276 529 508 C
ATOM 1221 O GLY A 162 33.924 161.507 28.159 1.00 57.35 O
ANISOU 1221 O GLY A 162 6882 7961 6947 258 493 485 O
ATOM 1222 N GLN A 163 34.256 159.802 26.763 1.00 53.69 N
ANISOU 1222 N GLN A 163 6414 7455 6532 274 552 498 N
ATOM 1223 CA GLN A 163 33.867 160.518 25.575 1.00 50.63 C
ANISOU 1223 CA GLN A 163 6052 7043 6143 250 535 459 C
ATOM 1224 C GLN A 163 32.521 160.113 25.047 1.00 47.40 C
ANISOU 1224 C GLN A 163 5663 6595 5752 249 549 428 C
ATOM 1225 O GLN A 163 32.074 159.027 25.244 1.00 48.47 O
ANISOU 1225 O GLN A 163 5792 6714 5910 266 583 437 O
ATOM 1226 CB GLN A 163 34.890 160.316 24.461 1.00 51.41 C
ANISOU 1226 CB GLN A 163 6149 7132 6252 242 549 466 C
ATOM 1227 CG GLN A 163 36.284 160.739 24.778 1.00 54.45 C
ANISOU 1227 CG GLN A 163 6514 7552 6623 240 537 493 C
ATOM 1228 CD GLN A 163 37.153 160.746 23.571 1.00 58.89 C
ANISOU 1228 CD GLN A 163 7080 8100 7196 228 547 490 C
ATOM 1229 OE1 GLN A 163 36.973 159.976 22.660 1.00 59.85 O
ANISOU 1229 OE1 GLN A 163 7211 8188 7342 228 578 484 O
ATOM 1230 NE2 GLN A 163 38.094 161.631 23.559 1.00 59.74 N
ANISOU 1230 NE2 GLN A 163 7183 8232 7284 215 523 494 N
ATOM 1231 N VAL A 164 31.918 161.033 24.347 1.00 43.75 N
ANISOU 1231 N VAL A 164 5224 6119 5281 227 521 392 N
ATOM 1232 CA VAL A 164 30.661 160.818 23.710 1.00 41.11 C
ANISOU 1232 CA VAL A 164 4910 5749 4962 222 526 359 C
ATOM 1233 C VAL A 164 30.767 161.269 22.267 1.00 38.29 C
ANISOU 1233 C VAL A 164 4573 5371 4604 200 515 335 C
ATOM 1234 O VAL A 164 31.640 162.004 21.916 1.00 37.41 O
ANISOU 1234 O VAL A 164 4465 5274 4476 187 497 338 O
ATOM 1235 CB VAL A 164 29.550 161.651 24.378 1.00 41.17 C
ANISOU 1235 CB VAL A 164 4928 5758 4957 217 496 335 C
ATOM 1236 CG1 VAL A 164 29.284 161.201 25.792 1.00 41.57 C
ANISOU 1236 CG1 VAL A 164 4963 5825 5008 237 508 355 C
ATOM 1237 CG2 VAL A 164 29.886 163.126 24.366 1.00 41.67 C
ANISOU 1237 CG2 VAL A 164 5000 5841 4991 197 453 324 C
ATOM 1238 N ALA A 165 29.858 160.794 21.444 1.00 36.81 N
ANISOU 1238 N ALA A 165 4402 5150 4435 196 528 310 N
ATOM 1239 CA ALA A 165 29.741 161.245 20.097 1.00 36.35 C
ANISOU 1239 CA ALA A 165 4367 5070 4374 174 515 283 C
ATOM 1240 C ALA A 165 29.194 162.650 20.315 1.00 34.93 C
ANISOU 1240 C ALA A 165 4201 4899 4170 161 467 261 C
ATOM 1241 O ALA A 165 28.177 162.798 20.914 1.00 34.50 O
ANISOU 1241 O ALA A 165 4147 4842 4119 166 457 248 O
ATOM 1242 CB ALA A 165 28.758 160.392 19.359 1.00 36.54 C
ANISOU 1242 CB ALA A 165 4402 5060 4421 173 539 262 C
ATOM 1243 N CYS A 166 29.893 163.680 19.880 1.00 33.97 N
ANISOU 1243 N CYS A 166 4089 4789 4027 144 441 258 N
ATOM 1244 CA CYS A 166 29.458 165.046 20.139 1.00 33.47 C
ANISOU 1244 CA CYS A 166 4038 4736 3942 132 399 239 C
ATOM 1245 C CYS A 166 28.365 165.561 19.224 1.00 32.63 C
ANISOU 1245 C CYS A 166 3957 4602 3838 118 377 203 C
ATOM 1246 O CYS A 166 28.618 165.911 18.090 1.00 33.34 O
ANISOU 1246 O CYS A 166 4066 4678 3921 102 368 191 O
ATOM 1247 CB CYS A 166 30.621 166.014 20.165 1.00 34.54 C
ANISOU 1247 CB CYS A 166 4173 4897 4053 121 379 249 C
ATOM 1248 SG CYS A 166 30.197 167.684 20.606 1.00 37.40 S
ANISOU 1248 SG CYS A 166 4548 5274 4390 106 334 229 S
ATOM 1249 N LEU A 167 27.156 165.577 19.763 1.00 30.87 N
ANISOU 1249 N LEU A 167 3734 4370 3624 124 369 189 N
ATOM 1250 CA LEU A 167 25.938 165.999 19.093 1.00 29.83 C
ANISOU 1250 CA LEU A 167 3621 4213 3498 114 348 156 C
ATOM 1251 C LEU A 167 25.110 166.884 20.004 1.00 29.22 C
ANISOU 1251 C LEU A 167 3543 4143 3416 115 322 145 C
ATOM 1252 O LEU A 167 24.915 166.546 21.131 1.00 30.09 O
ANISOU 1252 O LEU A 167 3637 4264 3533 128 334 156 O
ATOM 1253 CB LEU A 167 25.137 164.788 18.664 1.00 29.96 C
ANISOU 1253 CB LEU A 167 3637 4204 3542 121 376 146 C
ATOM 1254 CG LEU A 167 25.846 163.842 17.721 1.00 31.82 C
ANISOU 1254 CG LEU A 167 3875 4428 3786 118 407 155 C
ATOM 1255 CD1 LEU A 167 25.250 162.465 17.706 1.00 32.34 C
ANISOU 1255 CD1 LEU A 167 3932 4475 3879 130 445 153 C
ATOM 1256 CD2 LEU A 167 25.954 164.434 16.344 1.00 31.65 C
ANISOU 1256 CD2 LEU A 167 3881 4393 3753 96 386 136 C
ATOM 1257 N PHE A 168 24.567 167.967 19.485 1.00 27.79 N
ANISOU 1257 N PHE A 168 3380 3953 3226 100 289 123 N
ATOM 1258 CA PHE A 168 23.891 168.989 20.241 1.00 26.63 C
ANISOU 1258 CA PHE A 168 3233 3811 3074 97 264 112 C
ATOM 1259 C PHE A 168 22.814 168.446 21.146 1.00 27.01 C
ANISOU 1259 C PHE A 168 3270 3850 3144 111 275 106 C
ATOM 1260 O PHE A 168 22.857 168.671 22.307 1.00 26.98 O
ANISOU 1260 O PHE A 168 3253 3863 3135 116 277 116 O
ATOM 1261 CB PHE A 168 23.284 170.048 19.334 1.00 25.59 C
ANISOU 1261 CB PHE A 168 3124 3662 2936 82 230 87 C
ATOM 1262 CG PHE A 168 22.714 171.220 20.075 1.00 24.36 C
ANISOU 1262 CG PHE A 168 2969 3512 2775 77 205 77 C
ATOM 1263 CD1 PHE A 168 21.460 171.159 20.651 1.00 24.50 C
ANISOU 1263 CD1 PHE A 168 2980 3514 2813 84 203 63 C
ATOM 1264 CD2 PHE A 168 23.443 172.351 20.238 1.00 24.14 C
ANISOU 1264 CD2 PHE A 168 2947 3504 2723 66 188 81 C
ATOM 1265 CE1 PHE A 168 20.958 172.215 21.345 1.00 24.78 C
ANISOU 1265 CE1 PHE A 168 3017 3553 2846 78 184 54 C
ATOM 1266 CE2 PHE A 168 22.939 173.410 20.921 1.00 24.53 C
ANISOU 1266 CE2 PHE A 168 2997 3556 2767 60 170 72 C
ATOM 1267 CZ PHE A 168 21.696 173.347 21.473 1.00 23.80 C
ANISOU 1267 CZ PHE A 168 2899 3447 2696 66 168 59 C
ATOM 1268 N GLU A 169 21.884 167.701 20.598 1.00 26.83 N
ANISOU 1268 N GLU A 169 3249 3800 3144 115 285 89 N
ATOM 1269 CA GLU A 169 20.788 167.145 21.351 1.00 26.94 C
ANISOU 1269 CA GLU A 169 3252 3801 3182 127 298 80 C
ATOM 1270 C GLU A 169 21.135 165.989 22.293 1.00 27.66 C
ANISOU 1270 C GLU A 169 3325 3902 3283 146 337 102 C
ATOM 1271 O GLU A 169 20.342 165.639 23.098 1.00 27.32 O
ANISOU 1271 O GLU A 169 3274 3851 3256 156 349 97 O
ATOM 1272 CB GLU A 169 19.624 166.797 20.424 1.00 28.28 C
ANISOU 1272 CB GLU A 169 3431 3939 3376 124 294 52 C
ATOM 1273 CG GLU A 169 18.960 168.007 19.803 1.00 32.07 C
ANISOU 1273 CG GLU A 169 3927 4408 3851 110 253 30 C
ATOM 1274 CD GLU A 169 17.787 167.717 18.905 1.00 34.72 C
ANISOU 1274 CD GLU A 169 4269 4714 4208 106 245 3 C
ATOM 1275 OE1 GLU A 169 16.956 166.919 19.234 1.00 33.53 O
ANISOU 1275 OE1 GLU A 169 4108 4549 4082 116 263 -8 O
ATOM 1276 OE2 GLU A 169 17.677 168.351 17.883 1.00 35.43 O
ANISOU 1276 OE2 GLU A 169 4376 4798 4290 93 218 -9 O
ATOM 1277 N ASP A 170 22.314 165.408 22.165 1.00 27.68 N
ANISOU 1277 N ASP A 170 3320 3920 3275 150 357 127 N
ATOM 1278 CA ASP A 170 22.726 164.363 23.060 1.00 28.92 C
ANISOU 1278 CA ASP A 170 3460 4089 3440 169 393 152 C
ATOM 1279 C ASP A 170 23.292 164.947 24.367 1.00 29.29 C
ANISOU 1279 C ASP A 170 3496 4167 3467 172 384 173 C
ATOM 1280 O ASP A 170 23.194 164.340 25.376 1.00 30.57 O
ANISOU 1280 O ASP A 170 3645 4335 3634 187 405 188 O
ATOM 1281 CB ASP A 170 23.731 163.403 22.430 1.00 31.31 C
ANISOU 1281 CB ASP A 170 3757 4394 3746 174 422 173 C
ATOM 1282 CG ASP A 170 23.144 162.525 21.374 1.00 36.37 C
ANISOU 1282 CG ASP A 170 4405 5004 4409 173 442 155 C
ATOM 1283 OD1 ASP A 170 21.957 162.565 21.125 1.00 37.72 O
ANISOU 1283 OD1 ASP A 170 4584 5153 4595 169 434 127 O
ATOM 1284 OD2 ASP A 170 23.894 161.786 20.772 1.00 37.95 O
ANISOU 1284 OD2 ASP A 170 4604 5203 4614 174 467 169 O
ATOM 1285 N VAL A 171 23.867 166.133 24.305 1.00 27.58 N
ANISOU 1285 N VAL A 171 3285 3968 3225 157 354 174 N
ATOM 1286 CA VAL A 171 24.464 166.806 25.442 1.00 26.83 C
ANISOU 1286 CA VAL A 171 3182 3905 3107 156 343 191 C
ATOM 1287 C VAL A 171 23.667 167.960 26.064 1.00 25.92 C
ANISOU 1287 C VAL A 171 3074 3790 2984 144 317 171 C
ATOM 1288 O VAL A 171 23.664 168.105 27.244 1.00 26.73 O
ANISOU 1288 O VAL A 171 3169 3910 3079 147 320 181 O
ATOM 1289 CB VAL A 171 25.929 167.216 25.170 1.00 27.61 C
ANISOU 1289 CB VAL A 171 3277 4032 3181 148 335 211 C
ATOM 1290 CG1 VAL A 171 26.736 166.034 24.721 1.00 29.38 C
ANISOU 1290 CG1 VAL A 171 3491 4257 3415 160 366 234 C
ATOM 1291 CG2 VAL A 171 26.060 168.360 24.186 1.00 25.79 C
ANISOU 1291 CG2 VAL A 171 3065 3796 2937 127 306 192 C
ATOM 1292 N VAL A 172 22.987 168.756 25.270 1.00 24.15 N
ANISOU 1292 N VAL A 172 2866 3545 2764 131 293 144 N
ATOM 1293 CA VAL A 172 22.213 169.863 25.782 1.00 24.42 C
ANISOU 1293 CA VAL A 172 2908 3576 2796 120 271 126 C
ATOM 1294 C VAL A 172 20.776 169.413 26.012 1.00 25.82 C
ANISOU 1294 C VAL A 172 3084 3722 3004 128 279 105 C
ATOM 1295 O VAL A 172 20.135 168.990 25.101 1.00 26.55 O
ANISOU 1295 O VAL A 172 3182 3789 3116 130 280 89 O
ATOM 1296 CB VAL A 172 22.260 171.105 24.864 1.00 23.93 C
ANISOU 1296 CB VAL A 172 2862 3509 2722 101 239 109 C
ATOM 1297 CG1 VAL A 172 21.576 172.289 25.491 1.00 23.13 C
ANISOU 1297 CG1 VAL A 172 2766 3405 2617 89 220 93 C
ATOM 1298 CG2 VAL A 172 23.674 171.448 24.495 1.00 23.47 C
ANISOU 1298 CG2 VAL A 172 2805 3477 2637 93 234 126 C
ATOM 1299 N PRO A 173 20.292 169.487 27.256 1.00 25.30 N
ANISOU 1299 N PRO A 173 3012 3659 2940 131 287 106 N
ATOM 1300 CA PRO A 173 18.926 169.086 27.601 1.00 25.57 C
ANISOU 1300 CA PRO A 173 3046 3664 3006 138 298 86 C
ATOM 1301 C PRO A 173 17.884 169.946 26.911 1.00 26.17 C
ANISOU 1301 C PRO A 173 3134 3713 3098 127 272 55 C
ATOM 1302 O PRO A 173 18.011 171.129 26.901 1.00 27.17 O
ANISOU 1302 O PRO A 173 3267 3847 3209 112 248 50 O
ATOM 1303 CB PRO A 173 18.869 169.271 29.109 1.00 25.67 C
ANISOU 1303 CB PRO A 173 3052 3691 3010 139 308 95 C
ATOM 1304 CG PRO A 173 20.250 169.461 29.545 1.00 26.35 C
ANISOU 1304 CG PRO A 173 3133 3817 3063 136 306 124 C
ATOM 1305 CD PRO A 173 20.998 170.027 28.411 1.00 24.49 C
ANISOU 1305 CD PRO A 173 2904 3589 2813 125 285 124 C
ATOM 1306 N MET A 174 16.875 169.330 26.338 1.00 25.61 N
ANISOU 1306 N MET A 174 3063 3612 3057 134 278 36 N
ATOM 1307 CA MET A 174 15.842 170.057 25.651 1.00 25.61 C
ANISOU 1307 CA MET A 174 3071 3585 3074 125 252 8 C
ATOM 1308 C MET A 174 14.984 170.924 26.561 1.00 25.55 C
ANISOU 1308 C MET A 174 3063 3568 3078 118 244 -6 C
ATOM 1309 O MET A 174 14.485 171.901 26.131 1.00 25.85 O
ANISOU 1309 O MET A 174 3108 3594 3121 107 218 -22 O
ATOM 1310 CB MET A 174 15.007 169.139 24.796 1.00 26.93 C
ANISOU 1310 CB MET A 174 3238 3726 3271 133 260 -10 C
ATOM 1311 CG MET A 174 14.458 169.799 23.569 1.00 31.59 C
ANISOU 1311 CG MET A 174 3837 4297 3866 122 228 -30 C
ATOM 1312 SD MET A 174 15.618 170.696 22.555 1.00 39.46 S
ANISOU 1312 SD MET A 174 4850 5315 4828 108 201 -18 S
ATOM 1313 CE MET A 174 15.977 169.501 21.327 1.00 41.80 C
ANISOU 1313 CE MET A 174 5150 5606 5126 112 215 -16 C
ATOM 1314 N ASN A 175 14.838 170.551 27.823 1.00 25.17 N
ANISOU 1314 N ASN A 175 3007 3522 3033 124 267 0 N
ATOM 1315 CA ASN A 175 14.102 171.356 28.781 1.00 25.57 C
ANISOU 1315 CA ASN A 175 3059 3564 3094 116 264 -12 C
ATOM 1316 C ASN A 175 14.799 172.695 29.019 1.00 24.48 C
ANISOU 1316 C ASN A 175 2927 3448 2925 98 242 -4 C
ATOM 1317 O ASN A 175 14.149 173.675 29.159 1.00 24.65 O
ANISOU 1317 O ASN A 175 2953 3456 2957 86 228 -20 O
ATOM 1318 CB ASN A 175 13.716 170.615 30.074 1.00 27.83 C
ANISOU 1318 CB ASN A 175 3337 3845 3391 125 296 -9 C
ATOM 1319 CG ASN A 175 14.889 169.951 30.783 1.00 30.66 C
ANISOU 1319 CG ASN A 175 3692 4237 3722 133 316 23 C
ATOM 1320 OD1 ASN A 175 16.025 170.211 30.519 1.00 32.15 O
ANISOU 1320 OD1 ASN A 175 3880 4455 3880 129 306 42 O
ATOM 1321 ND2 ASN A 175 14.584 169.098 31.687 1.00 30.06 N
ANISOU 1321 ND2 ASN A 175 3610 4155 3655 145 346 27 N
ATOM 1322 N TYR A 176 16.128 172.696 29.010 1.00 23.71 N
ANISOU 1322 N TYR A 176 2830 3385 2794 96 242 20 N
ATOM 1323 CA TYR A 176 16.909 173.906 29.125 1.00 22.99 C
ANISOU 1323 CA TYR A 176 2745 3318 2673 78 223 27 C
ATOM 1324 C TYR A 176 16.691 174.752 27.880 1.00 22.65 C
ANISOU 1324 C TYR A 176 2713 3261 2633 69 195 12 C
ATOM 1325 O TYR A 176 16.477 175.903 27.969 1.00 23.27 O
ANISOU 1325 O TYR A 176 2798 3336 2708 55 180 2 O
ATOM 1326 CB TYR A 176 18.410 173.644 29.349 1.00 22.47 C
ANISOU 1326 CB TYR A 176 2675 3293 2572 79 230 55 C
ATOM 1327 CG TYR A 176 19.250 174.820 28.966 1.00 21.97 C
ANISOU 1327 CG TYR A 176 2618 3250 2480 61 208 58 C
ATOM 1328 CD1 TYR A 176 19.542 175.810 29.872 1.00 22.83 C
ANISOU 1328 CD1 TYR A 176 2728 3378 2568 44 204 60 C
ATOM 1329 CD2 TYR A 176 19.706 174.966 27.697 1.00 21.26 C
ANISOU 1329 CD2 TYR A 176 2536 3158 2384 60 193 57 C
ATOM 1330 CE1 TYR A 176 20.269 176.903 29.522 1.00 22.59 C
ANISOU 1330 CE1 TYR A 176 2706 3365 2514 28 187 60 C
ATOM 1331 CE2 TYR A 176 20.436 176.053 27.334 1.00 21.42 C
ANISOU 1331 CE2 TYR A 176 2565 3194 2380 44 175 58 C
ATOM 1332 CZ TYR A 176 20.710 177.026 28.248 1.00 22.33 C
ANISOU 1332 CZ TYR A 176 2679 3328 2475 29 172 59 C
ATOM 1333 OH TYR A 176 21.415 178.100 27.898 1.00 22.80 O
ANISOU 1333 OH TYR A 176 2748 3403 2513 13 158 57 O
ATOM 1334 N MET A 177 16.723 174.124 26.725 1.00 22.45 N
ANISOU 1334 N MET A 177 2689 3225 2614 78 191 10 N
ATOM 1335 CA MET A 177 16.556 174.783 25.437 1.00 22.57 C
ANISOU 1335 CA MET A 177 2717 3227 2631 71 164 -3 C
ATOM 1336 C MET A 177 15.208 175.454 25.285 1.00 23.27 C
ANISOU 1336 C MET A 177 2809 3284 2748 67 148 -27 C
ATOM 1337 O MET A 177 15.146 176.551 24.884 1.00 23.02 O
ANISOU 1337 O MET A 177 2787 3249 2711 56 126 -33 O
ATOM 1338 CB MET A 177 16.828 173.820 24.280 1.00 22.30 C
ANISOU 1338 CB MET A 177 2685 3188 2600 80 166 0 C
ATOM 1339 CG MET A 177 18.297 173.549 23.983 1.00 23.40 C
ANISOU 1339 CG MET A 177 2826 3355 2708 79 173 23 C
ATOM 1340 SD MET A 177 19.368 174.950 23.999 1.00 21.86 S
ANISOU 1340 SD MET A 177 2641 3187 2478 61 154 32 S
ATOM 1341 CE MET A 177 18.582 175.968 22.846 1.00 20.47 C
ANISOU 1341 CE MET A 177 2482 2984 2310 51 122 9 C
ATOM 1342 N VAL A 178 14.152 174.766 25.686 1.00 23.54 N
ANISOU 1342 N VAL A 178 2835 3296 2815 77 161 -39 N
ATOM 1343 CA VAL A 178 12.790 175.253 25.574 1.00 23.53 C
ANISOU 1343 CA VAL A 178 2832 3262 2848 75 148 -63 C
ATOM 1344 C VAL A 178 12.330 176.215 26.686 1.00 23.55 C
ANISOU 1344 C VAL A 178 2832 3258 2856 65 151 -69 C
ATOM 1345 O VAL A 178 11.959 177.304 26.397 1.00 23.37 O
ANISOU 1345 O VAL A 178 2816 3224 2839 55 131 -79 O
ATOM 1346 CB VAL A 178 11.805 174.100 25.330 1.00 23.77 C
ANISOU 1346 CB VAL A 178 2854 3266 2912 89 160 -78 C
ATOM 1347 CG1 VAL A 178 10.392 174.563 25.393 1.00 24.53 C
ANISOU 1347 CG1 VAL A 178 2945 3329 3046 88 149 -102 C
ATOM 1348 CG2 VAL A 178 12.071 173.483 23.999 1.00 23.94 C
ANISOU 1348 CG2 VAL A 178 2880 3288 2929 93 151 -77 C
ATOM 1349 N TYR A 179 12.401 175.802 27.938 1.00 24.27 N
ANISOU 1349 N TYR A 179 2918 3358 2948 67 177 -63 N
ATOM 1350 CA TYR A 179 11.957 176.620 29.051 1.00 25.83 C
ANISOU 1350 CA TYR A 179 3114 3549 3151 55 184 -70 C
ATOM 1351 C TYR A 179 12.893 177.739 29.474 1.00 26.13 C
ANISOU 1351 C TYR A 179 3160 3614 3154 37 177 -58 C
ATOM 1352 O TYR A 179 12.481 178.839 29.644 1.00 26.76 O
ANISOU 1352 O TYR A 179 3243 3682 3240 23 169 -69 O
ATOM 1353 CB TYR A 179 11.661 175.768 30.266 1.00 26.71 C
ANISOU 1353 CB TYR A 179 3219 3657 3273 61 215 -69 C
ATOM 1354 CG TYR A 179 10.523 174.802 30.157 1.00 28.07 C
ANISOU 1354 CG TYR A 179 3383 3796 3486 76 228 -86 C
ATOM 1355 CD1 TYR A 179 9.322 175.159 29.609 1.00 29.64 C
ANISOU 1355 CD1 TYR A 179 3579 3960 3722 76 214 -110 C
ATOM 1356 CD2 TYR A 179 10.650 173.534 30.641 1.00 29.09 C
ANISOU 1356 CD2 TYR A 179 3506 3929 3617 91 256 -78 C
ATOM 1357 CE1 TYR A 179 8.298 174.263 29.529 1.00 31.14 C
ANISOU 1357 CE1 TYR A 179 3761 4122 3950 89 226 -127 C
ATOM 1358 CE2 TYR A 179 9.630 172.641 30.579 1.00 30.44 C
ANISOU 1358 CE2 TYR A 179 3670 4070 3825 104 271 -95 C
ATOM 1359 CZ TYR A 179 8.458 173.014 30.021 1.00 32.63 C
ANISOU 1359 CZ TYR A 179 3945 4314 4139 102 256 -121 C
ATOM 1360 OH TYR A 179 7.467 172.118 29.957 1.00 36.26 O
ANISOU 1360 OH TYR A 179 4397 4746 4636 114 272 -140 O
ATOM 1361 N PHE A 180 14.157 177.423 29.641 1.00 25.63 N
ANISOU 1361 N PHE A 180 3097 3587 3055 36 183 -36 N
ATOM 1362 CA PHE A 180 15.144 178.377 30.085 1.00 25.55 C
ANISOU 1362 CA PHE A 180 3091 3607 3008 19 180 -25 C
ATOM 1363 C PHE A 180 15.655 179.263 28.975 1.00 25.38 C
ANISOU 1363 C PHE A 180 3080 3591 2972 11 155 -26 C
ATOM 1364 O PHE A 180 15.513 180.424 29.041 1.00 26.24 O
ANISOU 1364 O PHE A 180 3196 3696 3078 -4 146 -34 O
ATOM 1365 CB PHE A 180 16.273 177.662 30.804 1.00 25.52 C
ANISOU 1365 CB PHE A 180 3082 3641 2975 22 196 -1 C
ATOM 1366 CG PHE A 180 17.162 178.551 31.633 1.00 26.18 C
ANISOU 1366 CG PHE A 180 3168 3757 3023 2 197 9 C
ATOM 1367 CD1 PHE A 180 18.214 179.237 31.063 1.00 26.14 C
ANISOU 1367 CD1 PHE A 180 3168 3777 2989 -8 183 17 C
ATOM 1368 CD2 PHE A 180 16.991 178.641 32.987 1.00 26.76 C
ANISOU 1368 CD2 PHE A 180 3239 3838 3092 -7 215 10 C
ATOM 1369 CE1 PHE A 180 19.061 180.001 31.813 1.00 27.25 C
ANISOU 1369 CE1 PHE A 180 3309 3950 3097 -27 185 25 C
ATOM 1370 CE2 PHE A 180 17.822 179.424 33.732 1.00 27.88 C
ANISOU 1370 CE2 PHE A 180 3382 4012 3199 -27 216 18 C
ATOM 1371 CZ PHE A 180 18.857 180.106 33.149 1.00 27.23 C
ANISOU 1371 CZ PHE A 180 3302 3955 3088 -37 201 25 C
ATOM 1372 N ASN A 181 16.229 178.688 27.948 1.00 24.42 N
ANISOU 1372 N ASN A 181 2961 3477 2841 21 146 -18 N
ATOM 1373 CA ASN A 181 16.721 179.471 26.848 1.00 25.02 C
ANISOU 1373 CA ASN A 181 3048 3555 2901 14 124 -18 C
ATOM 1374 C ASN A 181 15.661 180.169 25.965 1.00 26.29 C
ANISOU 1374 C ASN A 181 3218 3683 3089 13 102 -38 C
ATOM 1375 O ASN A 181 15.717 181.344 25.802 1.00 28.05 O
ANISOU 1375 O ASN A 181 3450 3904 3304 0 90 -42 O
ATOM 1376 CB ASN A 181 17.691 178.674 26.011 1.00 24.85 C
ANISOU 1376 CB ASN A 181 3029 3551 2863 23 123 -4 C
ATOM 1377 CG ASN A 181 18.528 179.544 25.104 1.00 26.23 C
ANISOU 1377 CG ASN A 181 3217 3736 3011 12 105 -1 C
ATOM 1378 OD1 ASN A 181 18.102 179.888 24.048 1.00 26.84 O
ANISOU 1378 OD1 ASN A 181 3306 3794 3099 12 87 -12 O
ATOM 1379 ND2 ASN A 181 19.715 179.879 25.531 1.00 25.67 N
ANISOU 1379 ND2 ASN A 181 3145 3698 2909 2 111 12 N
ATOM 1380 N PHE A 182 14.711 179.451 25.421 1.00 25.65 N
ANISOU 1380 N PHE A 182 3133 3574 3038 26 98 -48 N
ATOM 1381 CA PHE A 182 13.696 180.050 24.575 1.00 26.88 C
ANISOU 1381 CA PHE A 182 3295 3700 3219 26 75 -65 C
ATOM 1382 C PHE A 182 12.668 180.911 25.310 1.00 27.76 C
ANISOU 1382 C PHE A 182 3402 3789 3357 19 76 -79 C
ATOM 1383 O PHE A 182 12.631 182.063 25.113 1.00 28.04 O
ANISOU 1383 O PHE A 182 3446 3820 3389 8 63 -82 O
ATOM 1384 CB PHE A 182 13.000 178.992 23.715 1.00 27.01 C
ANISOU 1384 CB PHE A 182 3307 3696 3259 41 69 -73 C
ATOM 1385 CG PHE A 182 12.027 179.542 22.690 1.00 28.33 C
ANISOU 1385 CG PHE A 182 3480 3835 3448 41 41 -88 C
ATOM 1386 CD1 PHE A 182 12.284 180.705 22.004 1.00 28.72 C
ANISOU 1386 CD1 PHE A 182 3544 3885 3483 32 18 -87 C
ATOM 1387 CD2 PHE A 182 10.862 178.872 22.406 1.00 29.17 C
ANISOU 1387 CD2 PHE A 182 3576 3915 3591 51 37 -103 C
ATOM 1388 CE1 PHE A 182 11.409 181.187 21.069 1.00 29.27 C
ANISOU 1388 CE1 PHE A 182 3618 3930 3572 34 -9 -98 C
ATOM 1389 CE2 PHE A 182 9.989 179.349 21.468 1.00 30.07 C
ANISOU 1389 CE2 PHE A 182 3694 4005 3724 52 9 -116 C
ATOM 1390 CZ PHE A 182 10.263 180.511 20.800 1.00 29.56 C
ANISOU 1390 CZ PHE A 182 3645 3943 3645 44 -15 -112 C
ATOM 1391 N PHE A 183 11.876 180.328 26.183 1.00 28.01 N
ANISOU 1391 N PHE A 183 3421 3806 3415 24 94 -87 N
ATOM 1392 CA PHE A 183 10.828 181.052 26.882 1.00 28.82 C
ANISOU 1392 CA PHE A 183 3519 3883 3549 18 98 -102 C
ATOM 1393 C PHE A 183 11.315 182.240 27.715 1.00 28.22 C
ANISOU 1393 C PHE A 183 3449 3821 3453 -2 106 -98 C
ATOM 1394 O PHE A 183 10.942 183.342 27.459 1.00 28.47 O
ANISOU 1394 O PHE A 183 3486 3838 3495 -11 94 -105 O
ATOM 1395 CB PHE A 183 9.918 180.122 27.703 1.00 29.21 C
ANISOU 1395 CB PHE A 183 3556 3913 3631 27 120 -112 C
ATOM 1396 CG PHE A 183 9.060 179.167 26.892 1.00 30.62 C
ANISOU 1396 CG PHE A 183 3727 4068 3840 43 112 -124 C
ATOM 1397 CD1 PHE A 183 9.018 179.207 25.530 1.00 31.36 C
ANISOU 1397 CD1 PHE A 183 3826 4157 3933 48 84 -126 C
ATOM 1398 CD2 PHE A 183 8.311 178.219 27.524 1.00 32.27 C
ANISOU 1398 CD2 PHE A 183 3924 4259 4077 53 133 -134 C
ATOM 1399 CE1 PHE A 183 8.242 178.334 24.820 1.00 32.32 C
ANISOU 1399 CE1 PHE A 183 3940 4259 4081 61 78 -138 C
ATOM 1400 CE2 PHE A 183 7.534 177.345 26.824 1.00 33.32 C
ANISOU 1400 CE2 PHE A 183 4050 4372 4239 66 129 -147 C
ATOM 1401 CZ PHE A 183 7.504 177.404 25.467 1.00 33.08 C
ANISOU 1401 CZ PHE A 183 4023 4339 4206 70 100 -149 C
ATOM 1402 N ALA A 184 12.175 181.983 28.670 1.00 26.87 N
ANISOU 1402 N ALA A 184 3276 3678 3253 -9 126 -86 N
ATOM 1403 CA ALA A 184 12.703 182.990 29.558 1.00 26.35 C
ANISOU 1403 CA ALA A 184 3216 3630 3167 -30 137 -82 C
ATOM 1404 C ALA A 184 13.730 183.984 29.002 1.00 25.84 C
ANISOU 1404 C ALA A 184 3162 3588 3066 -42 124 -74 C
ATOM 1405 O ALA A 184 13.589 185.144 29.153 1.00 25.62 O
ANISOU 1405 O ALA A 184 3141 3554 3040 -57 123 -81 O
ATOM 1406 CB ALA A 184 13.256 182.330 30.788 1.00 25.63 C
ANISOU 1406 CB ALA A 184 3119 3563 3055 -33 162 -72 C
ATOM 1407 N CYS A 185 14.737 183.481 28.329 1.00 25.13 N
ANISOU 1407 N CYS A 185 3076 3523 2949 -35 115 -61 N
ATOM 1408 CA CYS A 185 15.828 184.285 27.840 1.00 24.87 C
ANISOU 1408 CA CYS A 185 3054 3515 2882 -46 106 -53 C
ATOM 1409 C CYS A 185 15.726 184.846 26.435 1.00 25.37 C
ANISOU 1409 C CYS A 185 3129 3562 2948 -43 81 -57 C
ATOM 1410 O CYS A 185 16.412 185.742 26.121 1.00 25.79 O
ANISOU 1410 O CYS A 185 3193 3628 2979 -54 76 -55 O
ATOM 1411 CB CYS A 185 17.144 183.556 28.078 1.00 24.10 C
ANISOU 1411 CB CYS A 185 2952 3456 2748 -45 114 -34 C
ATOM 1412 SG CYS A 185 17.478 183.084 29.772 1.00 28.28 S
ANISOU 1412 SG CYS A 185 3469 4011 3264 -52 141 -25 S
ATOM 1413 N VAL A 186 14.844 184.316 25.616 1.00 25.23 N
ANISOU 1413 N VAL A 186 3110 3517 2959 -27 67 -64 N
ATOM 1414 CA VAL A 186 14.653 184.818 24.267 1.00 25.56 C
ANISOU 1414 CA VAL A 186 3165 3543 3004 -24 41 -68 C
ATOM 1415 C VAL A 186 13.260 185.458 24.069 1.00 27.20 C
ANISOU 1415 C VAL A 186 3371 3712 3251 -22 29 -83 C
ATOM 1416 O VAL A 186 13.160 186.605 23.797 1.00 27.47 O
ANISOU 1416 O VAL A 186 3414 3737 3285 -30 20 -86 O
ATOM 1417 CB VAL A 186 14.957 183.746 23.203 1.00 25.14 C
ANISOU 1417 CB VAL A 186 3115 3492 2944 -10 30 -62 C
ATOM 1418 CG1 VAL A 186 14.490 184.171 21.834 1.00 24.91 C
ANISOU 1418 CG1 VAL A 186 3099 3442 2924 -6 2 -68 C
ATOM 1419 CG2 VAL A 186 16.423 183.414 23.178 1.00 24.59 C
ANISOU 1419 CG2 VAL A 186 3050 3457 2836 -14 39 -47 C
ATOM 1420 N LEU A 187 12.213 184.677 24.226 1.00 27.93 N
ANISOU 1420 N LEU A 187 3451 3782 3378 -10 30 -91 N
ATOM 1421 CA LEU A 187 10.853 185.100 24.071 1.00 30.28 C
ANISOU 1421 CA LEU A 187 3743 4044 3718 -6 19 -105 C
ATOM 1422 C LEU A 187 10.468 186.253 24.956 1.00 30.58 C
ANISOU 1422 C LEU A 187 3780 4071 3770 -20 31 -111 C
ATOM 1423 O LEU A 187 9.941 187.196 24.490 1.00 30.31 O
ANISOU 1423 O LEU A 187 3750 4016 3751 -22 17 -116 O
ATOM 1424 CB LEU A 187 9.916 183.943 24.330 1.00 32.16 C
ANISOU 1424 CB LEU A 187 3965 4264 3990 7 25 -115 C
ATOM 1425 CG LEU A 187 8.735 183.766 23.420 1.00 36.49 C
ANISOU 1425 CG LEU A 187 4508 4781 4574 19 1 -127 C
ATOM 1426 CD1 LEU A 187 9.169 183.933 21.995 1.00 37.75 C
ANISOU 1426 CD1 LEU A 187 4683 4948 4713 22 -27 -120 C
ATOM 1427 CD2 LEU A 187 8.112 182.410 23.615 1.00 37.38 C
ANISOU 1427 CD2 LEU A 187 4608 4885 4712 32 12 -135 C
ATOM 1428 N VAL A 188 10.719 186.146 26.238 1.00 30.99 N
ANISOU 1428 N VAL A 188 3825 4134 3815 -30 59 -111 N
ATOM 1429 CA VAL A 188 10.388 187.222 27.145 1.00 31.69 C
ANISOU 1429 CA VAL A 188 3913 4213 3915 -47 75 -117 C
ATOM 1430 C VAL A 188 11.091 188.532 26.779 1.00 32.41 C
ANISOU 1430 C VAL A 188 4019 4315 3980 -62 70 -113 C
ATOM 1431 O VAL A 188 10.439 189.524 26.678 1.00 34.24 O
ANISOU 1431 O VAL A 188 4252 4522 4235 -67 67 -119 O
ATOM 1432 CB VAL A 188 10.503 186.843 28.627 1.00 31.81 C
ANISOU 1432 CB VAL A 188 3921 4239 3926 -58 107 -119 C
ATOM 1433 CG1 VAL A 188 10.513 188.075 29.489 1.00 32.65 C
ANISOU 1433 CG1 VAL A 188 4032 4343 4031 -81 125 -124 C
ATOM 1434 CG2 VAL A 188 9.362 185.945 29.020 1.00 31.72 C
ANISOU 1434 CG2 VAL A 188 3896 4199 3956 -45 114 -130 C
ATOM 1435 N PRO A 189 12.416 188.525 26.569 1.00 30.82 N
ANISOU 1435 N PRO A 189 3827 4149 3734 -67 70 -101 N
ATOM 1436 CA PRO A 189 13.045 189.772 26.145 1.00 29.98 C
ANISOU 1436 CA PRO A 189 3735 4050 3605 -80 66 -98 C
ATOM 1437 C PRO A 189 12.525 190.269 24.802 1.00 29.22 C
ANISOU 1437 C PRO A 189 3648 3929 3524 -69 38 -100 C
ATOM 1438 O PRO A 189 12.446 191.433 24.645 1.00 30.45 O
ANISOU 1438 O PRO A 189 3813 4076 3683 -78 38 -102 O
ATOM 1439 CB PRO A 189 14.522 189.419 26.066 1.00 30.07 C
ANISOU 1439 CB PRO A 189 3753 4103 3568 -85 69 -86 C
ATOM 1440 CG PRO A 189 14.666 188.300 26.989 1.00 30.60 C
ANISOU 1440 CG PRO A 189 3807 4187 3633 -81 84 -82 C
ATOM 1441 CD PRO A 189 13.416 187.511 26.899 1.00 29.29 C
ANISOU 1441 CD PRO A 189 3630 3990 3508 -65 78 -90 C
ATOM 1442 N LEU A 190 12.167 189.413 23.870 1.00 27.85 N
ANISOU 1442 N LEU A 190 3473 3746 3360 -51 16 -98 N
ATOM 1443 CA LEU A 190 11.621 189.891 22.620 1.00 28.74 C
ANISOU 1443 CA LEU A 190 3596 3837 3488 -41 -13 -99 C
ATOM 1444 C LEU A 190 10.255 190.556 22.793 1.00 31.02 C
ANISOU 1444 C LEU A 190 3875 4088 3823 -39 -16 -108 C
ATOM 1445 O LEU A 190 9.989 191.518 22.165 1.00 32.04 O
ANISOU 1445 O LEU A 190 4013 4201 3959 -39 -29 -107 O
ATOM 1446 CB LEU A 190 11.576 188.801 21.567 1.00 28.06 C
ANISOU 1446 CB LEU A 190 3512 3751 3399 -25 -35 -96 C
ATOM 1447 CG LEU A 190 12.877 188.257 21.005 1.00 28.40 C
ANISOU 1447 CG LEU A 190 3567 3824 3399 -25 -37 -86 C
ATOM 1448 CD1 LEU A 190 12.622 187.060 20.133 1.00 29.61 C
ANISOU 1448 CD1 LEU A 190 3719 3973 3558 -10 -54 -86 C
ATOM 1449 CD2 LEU A 190 13.689 189.283 20.266 1.00 28.08 C
ANISOU 1449 CD2 LEU A 190 3549 3792 3329 -33 -45 -80 C
ATOM 1450 N LEU A 191 9.408 190.027 23.658 1.00 31.63 N
ANISOU 1450 N LEU A 191 3934 4149 3933 -37 -3 -117 N
ATOM 1451 CA LEU A 191 8.118 190.609 23.933 1.00 34.23 C
ANISOU 1451 CA LEU A 191 4253 4442 4312 -35 -2 -127 C
ATOM 1452 C LEU A 191 8.310 191.974 24.608 1.00 35.49 C
ANISOU 1452 C LEU A 191 4417 4597 4468 -55 19 -127 C
ATOM 1453 O LEU A 191 7.615 192.887 24.329 1.00 36.17 O
ANISOU 1453 O LEU A 191 4504 4657 4582 -55 13 -129 O
ATOM 1454 CB LEU A 191 7.249 189.683 24.771 1.00 35.49 C
ANISOU 1454 CB LEU A 191 4392 4586 4505 -30 11 -138 C
ATOM 1455 CG LEU A 191 6.882 188.319 24.204 1.00 38.29 C
ANISOU 1455 CG LEU A 191 4739 4940 4871 -12 -5 -141 C
ATOM 1456 CD1 LEU A 191 6.176 187.410 25.173 1.00 39.30 C
ANISOU 1456 CD1 LEU A 191 4849 5054 5027 -9 16 -153 C
ATOM 1457 CD2 LEU A 191 6.167 188.372 22.885 1.00 39.77 C
ANISOU 1457 CD2 LEU A 191 4927 5107 5078 3 -41 -142 C
ATOM 1458 N LEU A 192 9.299 192.078 25.469 1.00 35.07 N
ANISOU 1458 N LEU A 192 4370 4574 4382 -72 45 -125 N
ATOM 1459 CA LEU A 192 9.625 193.307 26.124 1.00 35.85 C
ANISOU 1459 CA LEU A 192 4475 4675 4472 -93 68 -127 C
ATOM 1460 C LEU A 192 10.019 194.348 25.089 1.00 36.70 C
ANISOU 1460 C LEU A 192 4599 4781 4564 -93 53 -120 C
ATOM 1461 O LEU A 192 9.592 195.446 25.177 1.00 37.78 O
ANISOU 1461 O LEU A 192 4738 4896 4720 -101 62 -123 O
ATOM 1462 CB LEU A 192 10.736 193.107 27.133 1.00 35.74 C
ANISOU 1462 CB LEU A 192 4464 4699 4418 -112 94 -125 C
ATOM 1463 CG LEU A 192 10.412 192.428 28.451 1.00 37.96 C
ANISOU 1463 CG LEU A 192 4732 4981 4710 -119 119 -132 C
ATOM 1464 CD1 LEU A 192 11.643 192.116 29.238 1.00 37.49 C
ANISOU 1464 CD1 LEU A 192 4676 4964 4604 -134 136 -125 C
ATOM 1465 CD2 LEU A 192 9.482 193.234 29.310 1.00 39.78 C
ANISOU 1465 CD2 LEU A 192 4957 5181 4978 -134 142 -144 C
ATOM 1466 N MET A 193 10.822 193.969 24.105 1.00 36.16 N
ANISOU 1466 N MET A 193 4543 4733 4463 -84 32 -111 N
ATOM 1467 CA MET A 193 11.248 194.850 23.037 1.00 35.90 C
ANISOU 1467 CA MET A 193 4529 4699 4412 -83 17 -105 C
ATOM 1468 C MET A 193 10.046 195.339 22.260 1.00 36.65 C
ANISOU 1468 C MET A 193 4622 4755 4547 -69 -6 -105 C
ATOM 1469 O MET A 193 9.968 196.473 21.923 1.00 37.19 O
ANISOU 1469 O MET A 193 4701 4810 4620 -73 -4 -102 O
ATOM 1470 CB MET A 193 12.171 194.148 22.076 1.00 35.03 C
ANISOU 1470 CB MET A 193 4431 4613 4264 -74 -3 -97 C
ATOM 1471 CG MET A 193 13.602 194.037 22.501 1.00 36.35 C
ANISOU 1471 CG MET A 193 4606 4820 4385 -88 15 -93 C
ATOM 1472 SD MET A 193 14.567 193.121 21.322 1.00 36.79 S
ANISOU 1472 SD MET A 193 4675 4897 4405 -77 -7 -84 S
ATOM 1473 CE MET A 193 15.426 191.987 22.376 1.00 34.50 C
ANISOU 1473 CE MET A 193 4371 4644 4093 -82 13 -81 C
ATOM 1474 N LEU A 194 9.126 194.442 21.960 1.00 36.80 N
ANISOU 1474 N LEU A 194 4627 4757 4596 -52 -26 -107 N
ATOM 1475 CA LEU A 194 7.902 194.768 21.250 1.00 38.56 C
ANISOU 1475 CA LEU A 194 4844 4945 4862 -37 -50 -107 C
ATOM 1476 C LEU A 194 7.167 195.867 21.979 1.00 39.33 C
ANISOU 1476 C LEU A 194 4933 5014 4996 -46 -29 -112 C
ATOM 1477 O LEU A 194 6.722 196.797 21.389 1.00 39.61 O
ANISOU 1477 O LEU A 194 4974 5028 5049 -42 -40 -107 O
ATOM 1478 CB LEU A 194 7.018 193.547 21.129 1.00 39.24 C
ANISOU 1478 CB LEU A 194 4912 5019 4977 -21 -67 -113 C
ATOM 1479 CG LEU A 194 5.679 193.734 20.478 1.00 42.84 C
ANISOU 1479 CG LEU A 194 5358 5440 5481 -6 -94 -115 C
ATOM 1480 CD1 LEU A 194 5.894 194.207 19.073 1.00 44.29 C
ANISOU 1480 CD1 LEU A 194 5559 5624 5645 3 -127 -103 C
ATOM 1481 CD2 LEU A 194 4.887 192.462 20.480 1.00 43.61 C
ANISOU 1481 CD2 LEU A 194 5436 5529 5605 6 -106 -124 C
ATOM 1482 N GLY A 195 7.072 195.722 23.282 1.00 38.99 N
ANISOU 1482 N GLY A 195 4879 4973 4965 -60 3 -121 N
ATOM 1483 CA GLY A 195 6.426 196.680 24.122 1.00 40.40 C
ANISOU 1483 CA GLY A 195 5048 5124 5177 -73 30 -128 C
ATOM 1484 C GLY A 195 7.099 198.029 24.173 1.00 40.52 C
ANISOU 1484 C GLY A 195 5080 5145 5171 -90 50 -123 C
ATOM 1485 O GLY A 195 6.444 199.024 24.227 1.00 42.75 O
ANISOU 1485 O GLY A 195 5360 5398 5486 -93 59 -124 O
ATOM 1486 N VAL A 196 8.412 198.046 24.172 1.00 38.15 N
ANISOU 1486 N VAL A 196 4795 4881 4818 -101 58 -120 N
ATOM 1487 CA VAL A 196 9.172 199.268 24.198 1.00 37.63 C
ANISOU 1487 CA VAL A 196 4746 4824 4727 -118 78 -118 C
ATOM 1488 C VAL A 196 8.962 199.998 22.872 1.00 38.46 C
ANISOU 1488 C VAL A 196 4865 4911 4838 -103 52 -107 C
ATOM 1489 O VAL A 196 8.730 201.160 22.865 1.00 39.04 O
ANISOU 1489 O VAL A 196 4943 4964 4926 -109 67 -106 O
ATOM 1490 CB VAL A 196 10.657 199.009 24.529 1.00 36.41 C
ANISOU 1490 CB VAL A 196 4604 4716 4515 -133 91 -118 C
ATOM 1491 CG1 VAL A 196 11.520 200.184 24.176 1.00 36.52 C
ANISOU 1491 CG1 VAL A 196 4637 4740 4499 -146 104 -115 C
ATOM 1492 CG2 VAL A 196 10.833 198.631 25.980 1.00 35.58 C
ANISOU 1492 CG2 VAL A 196 4486 4626 4405 -153 122 -127 C
ATOM 1493 N TYR A 197 9.004 199.283 21.765 1.00 38.12 N
ANISOU 1493 N TYR A 197 4827 4872 4783 -82 15 -100 N
ATOM 1494 CA TYR A 197 8.768 199.890 20.472 1.00 39.54 C
ANISOU 1494 CA TYR A 197 5022 5036 4966 -67 -13 -89 C
ATOM 1495 C TYR A 197 7.345 200.462 20.333 1.00 43.05 C
ANISOU 1495 C TYR A 197 5451 5437 5468 -55 -22 -86 C
ATOM 1496 O TYR A 197 7.166 201.492 19.770 1.00 44.37 O
ANISOU 1496 O TYR A 197 5628 5585 5643 -52 -25 -78 O
ATOM 1497 CB TYR A 197 9.164 198.968 19.322 1.00 38.30 C
ANISOU 1497 CB TYR A 197 4875 4895 4781 -51 -50 -82 C
ATOM 1498 CG TYR A 197 10.654 198.905 19.112 1.00 37.85 C
ANISOU 1498 CG TYR A 197 4839 4873 4667 -62 -41 -80 C
ATOM 1499 CD1 TYR A 197 11.366 200.019 18.749 1.00 38.52 C
ANISOU 1499 CD1 TYR A 197 4947 4962 4728 -70 -30 -76 C
ATOM 1500 CD2 TYR A 197 11.350 197.739 19.309 1.00 37.37 C
ANISOU 1500 CD2 TYR A 197 4777 4843 4581 -63 -42 -83 C
ATOM 1501 CE1 TYR A 197 12.722 199.973 18.576 1.00 38.43 C
ANISOU 1501 CE1 TYR A 197 4953 4982 4668 -81 -20 -77 C
ATOM 1502 CE2 TYR A 197 12.702 197.688 19.145 1.00 37.22 C
ANISOU 1502 CE2 TYR A 197 4774 4855 4513 -73 -34 -81 C
ATOM 1503 CZ TYR A 197 13.386 198.807 18.779 1.00 38.56 C
ANISOU 1503 CZ TYR A 197 4964 5027 4659 -82 -23 -79 C
ATOM 1504 OH TYR A 197 14.725 198.753 18.619 1.00 39.90 O
ANISOU 1504 OH TYR A 197 5150 5227 4784 -92 -14 -78 O
ATOM 1505 N LEU A 198 6.350 199.786 20.861 1.00 44.36 N
ANISOU 1505 N LEU A 198 5593 5585 5675 -50 -25 -94 N
ATOM 1506 CA LEU A 198 5.000 200.297 20.829 1.00 46.68 C
ANISOU 1506 CA LEU A 198 5870 5838 6028 -40 -31 -92 C
ATOM 1507 C LEU A 198 4.916 201.617 21.576 1.00 47.91 C
ANISOU 1507 C LEU A 198 6027 5975 6202 -57 9 -94 C
ATOM 1508 O LEU A 198 4.306 202.528 21.122 1.00 48.68 O
ANISOU 1508 O LEU A 198 6124 6044 6329 -49 4 -86 O
ATOM 1509 CB LEU A 198 4.036 199.313 21.443 1.00 47.74 C
ANISOU 1509 CB LEU A 198 5979 5959 6203 -34 -33 -104 C
ATOM 1510 CG LEU A 198 3.665 198.125 20.593 1.00 50.86 C
ANISOU 1510 CG LEU A 198 6367 6358 6599 -13 -75 -103 C
ATOM 1511 CD1 LEU A 198 2.655 197.259 21.299 1.00 51.82 C
ANISOU 1511 CD1 LEU A 198 6462 6462 6765 -9 -70 -116 C
ATOM 1512 CD2 LEU A 198 3.178 198.548 19.225 1.00 52.92 C
ANISOU 1512 CD2 LEU A 198 6634 6604 6869 6 -115 -89 C
ATOM 1513 N ARG A 199 5.551 201.696 22.723 1.00 48.02 N
ANISOU 1513 N ARG A 199 6042 6007 6198 -81 48 -105 N
ATOM 1514 CA ARG A 199 5.579 202.895 23.512 1.00 49.36 C
ANISOU 1514 CA ARG A 199 6213 6162 6380 -103 91 -109 C
ATOM 1515 C ARG A 199 6.346 204.005 22.808 1.00 49.37 C
ANISOU 1515 C ARG A 199 6238 6169 6350 -106 96 -99 C
ATOM 1516 O ARG A 199 6.028 205.157 22.958 1.00 50.78 O
ANISOU 1516 O ARG A 199 6418 6323 6553 -113 120 -97 O
ATOM 1517 CB ARG A 199 6.241 202.621 24.831 1.00 51.36 C
ANISOU 1517 CB ARG A 199 6465 6439 6610 -130 129 -123 C
ATOM 1518 CG ARG A 199 5.442 201.805 25.803 1.00 56.66 C
ANISOU 1518 CG ARG A 199 7114 7097 7315 -132 139 -134 C
ATOM 1519 CD ARG A 199 5.950 202.115 27.187 1.00 62.90 C
ANISOU 1519 CD ARG A 199 7907 7902 8091 -165 186 -146 C
ATOM 1520 NE ARG A 199 5.807 201.020 28.121 1.00 69.47 N
ANISOU 1520 NE ARG A 199 8727 8743 8924 -170 194 -157 N
ATOM 1521 CZ ARG A 199 4.957 201.013 29.140 1.00 74.85 C
ANISOU 1521 CZ ARG A 199 9395 9398 9647 -182 221 -168 C
ATOM 1522 NH1 ARG A 199 4.172 202.045 29.343 1.00 77.05 N
ANISOU 1522 NH1 ARG A 199 9668 9637 9970 -190 243 -171 N
ATOM 1523 NH2 ARG A 199 4.887 199.975 29.952 1.00 74.82 N
ANISOU 1523 NH2 ARG A 199 9383 9404 9641 -186 228 -177 N
ATOM 1524 N ILE A 200 7.365 203.646 22.046 1.00 47.33 N
ANISOU 1524 N ILE A 200 5999 5943 6041 -101 75 -94 N
ATOM 1525 CA ILE A 200 8.136 204.620 21.316 1.00 46.77 C
ANISOU 1525 CA ILE A 200 5952 5878 5939 -103 79 -86 C
ATOM 1526 C ILE A 200 7.298 205.227 20.216 1.00 48.73 C
ANISOU 1526 C ILE A 200 6204 6093 6218 -80 52 -71 C
ATOM 1527 O ILE A 200 7.253 206.410 20.068 1.00 49.30 O
ANISOU 1527 O ILE A 200 6286 6147 6299 -83 71 -65 O
ATOM 1528 CB ILE A 200 9.408 204.037 20.699 1.00 44.77 C
ANISOU 1528 CB ILE A 200 5720 5665 5627 -102 63 -84 C
ATOM 1529 CG1 ILE A 200 10.489 203.834 21.746 1.00 44.33 C
ANISOU 1529 CG1 ILE A 200 5665 5645 5533 -129 96 -96 C
ATOM 1530 CG2 ILE A 200 9.926 204.953 19.625 1.00 44.40 C
ANISOU 1530 CG2 ILE A 200 5698 5614 5556 -97 56 -73 C
ATOM 1531 CD1 ILE A 200 11.683 203.063 21.263 1.00 44.03 C
ANISOU 1531 CD1 ILE A 200 5641 5646 5443 -127 80 -94 C
ATOM 1532 N PHE A 201 6.626 204.397 19.450 1.00 49.66 N
ANISOU 1532 N PHE A 201 6313 6203 6351 -56 8 -64 N
ATOM 1533 CA PHE A 201 5.802 204.870 18.367 1.00 51.93 C
ANISOU 1533 CA PHE A 201 6603 6462 6666 -33 -24 -48 C
ATOM 1534 C PHE A 201 4.566 205.641 18.817 1.00 55.15 C
ANISOU 1534 C PHE A 201 6990 6827 7138 -30 -10 -45 C
ATOM 1535 O PHE A 201 4.150 206.534 18.152 1.00 56.82 O
ANISOU 1535 O PHE A 201 7206 7014 7368 -18 -18 -31 O
ATOM 1536 CB PHE A 201 5.450 203.735 17.421 1.00 51.15 C
ANISOU 1536 CB PHE A 201 6502 6370 6564 -12 -76 -43 C
ATOM 1537 CG PHE A 201 6.622 203.197 16.667 1.00 49.83 C
ANISOU 1537 CG PHE A 201 6360 6237 6337 -12 -92 -41 C
ATOM 1538 CD1 PHE A 201 7.449 204.029 15.978 1.00 50.23 C
ANISOU 1538 CD1 PHE A 201 6439 6294 6351 -14 -88 -32 C
ATOM 1539 CD2 PHE A 201 6.907 201.870 16.680 1.00 49.60 C
ANISOU 1539 CD2 PHE A 201 6325 6231 6288 -11 -108 -48 C
ATOM 1540 CE1 PHE A 201 8.530 203.555 15.298 1.00 49.86 C
ANISOU 1540 CE1 PHE A 201 6416 6276 6251 -16 -101 -31 C
ATOM 1541 CE2 PHE A 201 7.988 201.385 15.999 1.00 49.36 C
ANISOU 1541 CE2 PHE A 201 6318 6231 6206 -12 -120 -46 C
ATOM 1542 CZ PHE A 201 8.803 202.230 15.312 1.00 48.91 C
ANISOU 1542 CZ PHE A 201 6291 6180 6115 -15 -117 -38 C
ATOM 1543 N ALA A 202 4.017 205.297 19.963 1.00 55.86 N
ANISOU 1543 N ALA A 202 7055 6907 7261 -42 14 -59 N
ATOM 1544 CA ALA A 202 2.864 205.974 20.495 1.00 58.16 C
ANISOU 1544 CA ALA A 202 7326 7156 7616 -41 33 -59 C
ATOM 1545 C ALA A 202 3.240 207.333 21.059 1.00 60.08 C
ANISOU 1545 C ALA A 202 7579 7388 7860 -62 83 -59 C
ATOM 1546 O ALA A 202 2.507 208.272 20.923 1.00 61.92 O
ANISOU 1546 O ALA A 202 7806 7586 8136 -56 92 -50 O
ATOM 1547 CB ALA A 202 2.192 205.139 21.548 1.00 57.67 C
ANISOU 1547 CB ALA A 202 7237 7086 7588 -49 45 -75 C
ATOM 1548 N ALA A 203 4.400 207.423 21.677 1.00 59.31 N
ANISOU 1548 N ALA A 203 7498 7322 7716 -87 115 -70 N
ATOM 1549 CA ALA A 203 4.902 208.648 22.236 1.00 60.16 C
ANISOU 1549 CA ALA A 203 7617 7425 7816 -110 164 -74 C
ATOM 1550 C ALA A 203 5.264 209.612 21.131 1.00 62.26 C
ANISOU 1550 C ALA A 203 7905 7685 8065 -98 156 -58 C
ATOM 1551 O ALA A 203 5.241 210.781 21.313 1.00 63.46 O
ANISOU 1551 O ALA A 203 8063 7817 8231 -108 191 -56 O
ATOM 1552 CB ALA A 203 6.112 208.351 23.058 1.00 58.63 C
ANISOU 1552 CB ALA A 203 7434 7272 7570 -138 193 -90 C
ATOM 1553 N ALA A 204 5.623 209.082 19.985 1.00 62.54 N
ANISOU 1553 N ALA A 204 7955 7739 8069 -78 111 -47 N
ATOM 1554 CA ALA A 204 5.976 209.873 18.856 1.00 64.05 C
ANISOU 1554 CA ALA A 204 8171 7925 8241 -65 98 -31 C
ATOM 1555 C ALA A 204 4.707 210.424 18.294 1.00 66.87 C
ANISOU 1555 C ALA A 204 8515 8238 8654 -41 80 -14 C
ATOM 1556 O ALA A 204 4.634 211.568 17.998 1.00 67.69 O
ANISOU 1556 O ALA A 204 8630 8321 8770 -39 98 -3 O
ATOM 1557 CB ALA A 204 6.665 209.028 17.826 1.00 63.06 C
ANISOU 1557 CB ALA A 204 8063 7829 8066 -51 55 -26 C
ATOM 1558 N ARG A 205 3.712 209.579 18.147 1.00 68.12 N
ANISOU 1558 N ARG A 205 8650 8385 8848 -24 43 -11 N
ATOM 1559 CA ARG A 205 2.418 209.982 17.631 1.00 71.29 C
ANISOU 1559 CA ARG A 205 9034 8746 9307 0 20 6 C
ATOM 1560 C ARG A 205 1.794 211.073 18.497 1.00 72.96 C
ANISOU 1560 C ARG A 205 9230 8920 9571 -12 69 5 C
ATOM 1561 O ARG A 205 1.276 212.034 17.996 1.00 74.60 O
ANISOU 1561 O ARG A 205 9439 9098 9809 1 71 23 O
ATOM 1562 CB ARG A 205 1.487 208.774 17.545 1.00 73.68 C
ANISOU 1562 CB ARG A 205 9310 9045 9639 15 -21 3 C
ATOM 1563 CG ARG A 205 0.402 208.869 16.496 1.00 79.63 C
ANISOU 1563 CG ARG A 205 10053 9773 10431 46 -69 24 C
ATOM 1564 CD ARG A 205 -0.594 207.733 16.612 1.00 83.76 C
ANISOU 1564 CD ARG A 205 10545 10289 10992 57 -101 16 C
ATOM 1565 NE ARG A 205 -1.029 207.523 17.984 1.00 86.28 N
ANISOU 1565 NE ARG A 205 10839 10594 11349 40 -62 -3 N
ATOM 1566 CZ ARG A 205 -0.975 206.365 18.613 1.00 87.79 C
ANISOU 1566 CZ ARG A 205 11020 10804 11533 31 -62 -22 C
ATOM 1567 NH1 ARG A 205 -0.509 205.301 18.001 1.00 86.50 N
ANISOU 1567 NH1 ARG A 205 10866 10672 11328 38 -98 -25 N
ATOM 1568 NH2 ARG A 205 -1.369 206.277 19.863 1.00 88.48 N
ANISOU 1568 NH2 ARG A 205 11088 10876 11655 14 -24 -39 N
ATOM 1569 N ARG A 206 1.876 210.903 19.803 1.00 72.31 N
ANISOU 1569 N ARG A 206 9136 8841 9498 -38 111 -15 N
ATOM 1570 CA ARG A 206 1.339 211.837 20.756 1.00 73.66 C
ANISOU 1570 CA ARG A 206 9293 8978 9718 -55 163 -20 C
ATOM 1571 C ARG A 206 2.025 213.174 20.681 1.00 73.34 C
ANISOU 1571 C ARG A 206 9276 8933 9658 -68 204 -15 C
ATOM 1572 O ARG A 206 1.414 214.171 20.866 1.00 74.54 O
ANISOU 1572 O ARG A 206 9419 9047 9854 -69 234 -7 O
ATOM 1573 CB ARG A 206 1.521 211.311 22.156 1.00 75.37 C
ANISOU 1573 CB ARG A 206 9498 9206 9932 -85 200 -45 C
ATOM 1574 CG ARG A 206 0.979 212.186 23.247 1.00 82.68 C
ANISOU 1574 CG ARG A 206 10410 10096 10906 -108 258 -54 C
ATOM 1575 CD ARG A 206 1.130 211.564 24.624 1.00 89.71 C
ANISOU 1575 CD ARG A 206 11292 11001 11794 -137 290 -79 C
ATOM 1576 NE ARG A 206 0.581 212.403 25.699 1.00 96.25 N
ANISOU 1576 NE ARG A 206 12109 11793 12669 -163 349 -89 N
ATOM 1577 CZ ARG A 206 0.419 212.008 26.957 1.00100.21 C
ANISOU 1577 CZ ARG A 206 12600 12293 13182 -189 382 -109 C
ATOM 1578 NH1 ARG A 206 0.748 210.785 27.320 1.00 99.21 N
ANISOU 1578 NH1 ARG A 206 12472 12198 13026 -192 362 -121 N
ATOM 1579 NH2 ARG A 206 -0.081 212.839 27.854 1.00102.04 N
ANISOU 1579 NH2 ARG A 206 12824 12489 13458 -213 436 -118 N
ATOM 1580 N GLN A 207 3.302 213.190 20.397 1.00 71.43 N
ANISOU 1580 N GLN A 207 9062 8728 9350 -78 208 -19 N
ATOM 1581 CA GLN A 207 4.010 214.432 20.329 1.00 71.13 C
ANISOU 1581 CA GLN A 207 9046 8687 9291 -91 249 -17 C
ATOM 1582 C GLN A 207 3.828 215.156 19.023 1.00 72.83 C
ANISOU 1582 C GLN A 207 9277 8883 9510 -63 225 9 C
ATOM 1583 O GLN A 207 3.763 216.334 19.022 1.00 74.03 O
ANISOU 1583 O GLN A 207 9436 9011 9680 -67 261 16 O
ATOM 1584 CB GLN A 207 5.479 214.209 20.599 1.00 69.36 C
ANISOU 1584 CB GLN A 207 8846 8511 8998 -115 266 -33 C
ATOM 1585 CG GLN A 207 5.770 213.885 22.031 1.00 69.50 C
ANISOU 1585 CG GLN A 207 8851 8544 9010 -149 306 -58 C
ATOM 1586 CD GLN A 207 7.176 213.409 22.253 1.00 69.71 C
ANISOU 1586 CD GLN A 207 8896 8622 8968 -168 311 -73 C
ATOM 1587 OE1 GLN A 207 8.100 213.866 21.635 1.00 70.08 O
ANISOU 1587 OE1 GLN A 207 8968 8687 8973 -169 314 -70 O
ATOM 1588 NE2 GLN A 207 7.328 212.486 23.144 1.00 68.96 N
ANISOU 1588 NE2 GLN A 207 8788 8550 8862 -184 313 -88 N
ATOM 1589 N LEU A 208 3.730 214.439 17.923 1.00 73.34 N
ANISOU 1589 N LEU A 208 9348 8959 9558 -36 164 22 N
ATOM 1590 CA LEU A 208 3.601 215.023 16.608 1.00 75.44 C
ANISOU 1590 CA LEU A 208 9632 9211 9820 -9 135 48 C
ATOM 1591 C LEU A 208 2.223 215.525 16.347 1.00 78.78 C
ANISOU 1591 C LEU A 208 10032 9589 10313 14 122 69 C
ATOM 1592 O LEU A 208 1.942 216.694 16.434 1.00 79.47 O
ANISOU 1592 O LEU A 208 10120 9645 10430 14 158 79 O
ATOM 1593 CB LEU A 208 3.862 213.991 15.551 1.00 75.29 C
ANISOU 1593 CB LEU A 208 9626 9219 9763 11 73 55 C
ATOM 1594 CG LEU A 208 5.257 213.645 15.065 1.00 76.16 C
ANISOU 1594 CG LEU A 208 9768 9369 9798 3 66 47 C
ATOM 1595 CD1 LEU A 208 5.214 212.338 14.274 1.00 76.36 C
ANISOU 1595 CD1 LEU A 208 9795 9418 9801 19 5 50 C
ATOM 1596 CD2 LEU A 208 5.794 214.770 14.204 1.00 77.54 C
ANISOU 1596 CD2 LEU A 208 9977 9536 9949 9 78 62 C
ATOM 1597 N ALA A1001 0.929 215.190 17.091 1.00 79.60 N
ANISOU 1597 N ALA A1001 8092 7565 14585 558 -795 1635 N
ATOM 1598 CA ALA A1001 -0.445 215.491 17.470 1.00 84.90 C
ANISOU 1598 CA ALA A1001 8650 8285 15324 616 -927 1731 C
ATOM 1599 C ALA A1001 -0.417 216.694 18.361 1.00 83.15 C
ANISOU 1599 C ALA A1001 8353 8245 14995 637 -797 1694 C
ATOM 1600 O ALA A1001 -1.051 217.653 18.085 1.00 81.62 O
ANISOU 1600 O ALA A1001 8282 8004 14726 671 -825 1651 O
ATOM 1601 CB ALA A1001 -1.099 214.348 18.205 1.00 92.56 C
ANISOU 1601 CB ALA A1001 9321 9357 16490 635 -1042 1914 C
ATOM 1602 N ASP A1002 0.264 216.610 19.475 1.00 84.80 N
ANISOU 1602 N ASP A1002 8347 8670 15205 621 -664 1718 N
ATOM 1603 CA ASP A1002 0.503 217.788 20.273 1.00 83.13 C
ANISOU 1603 CA ASP A1002 8092 8621 14872 636 -526 1655 C
ATOM 1604 C ASP A1002 1.132 218.992 19.576 1.00 77.49 C
ANISOU 1604 C ASP A1002 7661 7802 13981 612 -413 1474 C
ATOM 1605 O ASP A1002 0.804 220.105 19.885 1.00 75.93 O
ANISOU 1605 O ASP A1002 7494 7665 13691 643 -370 1429 O
ATOM 1606 CB ASP A1002 1.370 217.405 21.454 1.00 87.80 C
ANISOU 1606 CB ASP A1002 8435 9438 15485 616 -393 1688 C
ATOM 1607 CG ASP A1002 0.589 216.819 22.578 1.00103.65 C
ANISOU 1607 CG ASP A1002 10123 11634 17627 674 -460 1862 C
ATOM 1608 OD1 ASP A1002 -0.565 216.456 22.368 1.00109.82 O
ANISOU 1608 OD1 ASP A1002 10862 12351 18514 718 -622 1974 O
ATOM 1609 OD2 ASP A1002 1.124 216.696 23.685 1.00110.80 O
ANISOU 1609 OD2 ASP A1002 10810 12751 18538 680 -351 1894 O
ATOM 1610 N LEU A1003 2.071 218.790 18.682 1.00 74.94 N
ANISOU 1610 N LEU A1003 7538 7328 13609 562 -355 1374 N
ATOM 1611 CA LEU A1003 2.660 219.926 18.026 1.00 70.97 C
ANISOU 1611 CA LEU A1003 7292 6722 12950 548 -243 1212 C
ATOM 1612 C LEU A1003 1.595 220.540 17.172 1.00 71.15 C
ANISOU 1612 C LEU A1003 7509 6587 12937 596 -361 1190 C
ATOM 1613 O LEU A1003 1.429 221.729 17.139 1.00 68.34 O
ANISOU 1613 O LEU A1003 7259 6236 12473 617 -303 1109 O
ATOM 1614 CB LEU A1003 3.819 219.527 17.126 1.00 70.10 C
ANISOU 1614 CB LEU A1003 7373 6458 12803 499 -167 1126 C
ATOM 1615 CG LEU A1003 5.254 219.496 17.621 1.00 71.15 C
ANISOU 1615 CG LEU A1003 7447 6693 12893 441 19 1071 C
ATOM 1616 CD1 LEU A1003 6.079 219.214 16.397 1.00 71.15 C
ANISOU 1616 CD1 LEU A1003 7706 6475 12851 414 57 994 C
ATOM 1617 CD2 LEU A1003 5.684 220.823 18.212 1.00 69.29 C
ANISOU 1617 CD2 LEU A1003 7213 6572 12542 438 165 971 C
ATOM 1618 N GLU A1004 0.878 219.697 16.465 1.00 75.28 N
ANISOU 1618 N GLU A1004 8080 6966 13557 614 -531 1262 N
ATOM 1619 CA GLU A1004 -0.152 220.154 15.573 1.00 78.21 C
ANISOU 1619 CA GLU A1004 8639 7170 13905 660 -660 1246 C
ATOM 1620 C GLU A1004 -1.288 220.845 16.302 1.00 79.75 C
ANISOU 1620 C GLU A1004 8703 7492 14107 709 -713 1319 C
ATOM 1621 O GLU A1004 -1.792 221.841 15.827 1.00 79.09 O
ANISOU 1621 O GLU A1004 8787 7334 13929 739 -718 1253 O
ATOM 1622 CB GLU A1004 -0.666 219.005 14.718 1.00 86.50 C
ANISOU 1622 CB GLU A1004 9752 8043 15073 669 -845 1315 C
ATOM 1623 CG GLU A1004 -1.529 219.418 13.534 1.00 96.06 C
ANISOU 1623 CG GLU A1004 11216 9036 16246 714 -975 1270 C
ATOM 1624 CD GLU A1004 -0.855 220.400 12.594 1.00100.16 C
ANISOU 1624 CD GLU A1004 12044 9416 16597 719 -855 1098 C
ATOM 1625 OE1 GLU A1004 0.369 220.306 12.385 1.00 99.75 O
ANISOU 1625 OE1 GLU A1004 12074 9338 16488 684 -719 1018 O
ATOM 1626 OE2 GLU A1004 -1.555 221.267 12.061 1.00103.33 O
ANISOU 1626 OE2 GLU A1004 12603 9733 16927 761 -894 1050 O
ATOM 1627 N ASP A1005 -1.671 220.329 17.455 1.00 82.10 N
ANISOU 1627 N ASP A1005 8702 7982 14511 721 -744 1457 N
ATOM 1628 CA ASP A1005 -2.737 220.924 18.204 1.00 84.12 C
ANISOU 1628 CA ASP A1005 8821 8365 14777 778 -791 1544 C
ATOM 1629 C ASP A1005 -2.379 222.342 18.549 1.00 78.45 C
ANISOU 1629 C ASP A1005 8182 7733 13892 784 -636 1428 C
ATOM 1630 O ASP A1005 -3.081 223.257 18.181 1.00 78.08 O
ANISOU 1630 O ASP A1005 8270 7626 13769 818 -663 1394 O
ATOM 1631 CB ASP A1005 -3.014 220.147 19.474 1.00 90.88 C
ANISOU 1631 CB ASP A1005 9333 9431 15768 800 -817 1709 C
ATOM 1632 CG ASP A1005 -3.771 218.861 19.219 1.00103.88 C
ANISOU 1632 CG ASP A1005 10871 10997 17603 812 -1005 1857 C
ATOM 1633 OD1 ASP A1005 -4.287 218.663 18.110 1.00107.31 O
ANISOU 1633 OD1 ASP A1005 11493 11219 18063 812 -1138 1841 O
ATOM 1634 OD2 ASP A1005 -3.842 218.033 20.142 1.00110.96 O
ANISOU 1634 OD2 ASP A1005 11490 12044 18627 825 -1021 1990 O
ATOM 1635 N ASN A1006 -1.271 222.530 19.238 1.00 74.63 N
ANISOU 1635 N ASN A1006 7617 7385 13352 749 -473 1364 N
ATOM 1636 CA ASN A1006 -0.828 223.850 19.656 1.00 70.53 C
ANISOU 1636 CA ASN A1006 7155 6957 12684 752 -322 1251 C
ATOM 1637 C ASN A1006 -0.802 224.907 18.545 1.00 66.78 C
ANISOU 1637 C ASN A1006 6996 6300 12079 749 -286 1105 C
ATOM 1638 O ASN A1006 -1.095 226.052 18.775 1.00 64.88 O
ANISOU 1638 O ASN A1006 6807 6108 11736 777 -231 1053 O
ATOM 1639 CB ASN A1006 0.518 223.746 20.346 1.00 70.41 C
ANISOU 1639 CB ASN A1006 7037 7073 12641 703 -161 1190 C
ATOM 1640 CG ASN A1006 0.386 223.455 21.814 1.00 77.30 C
ANISOU 1640 CG ASN A1006 7596 8201 13574 735 -143 1303 C
ATOM 1641 OD1 ASN A1006 -0.657 223.663 22.395 1.00 81.73 O
ANISOU 1641 OD1 ASN A1006 8035 8856 14164 800 -218 1406 O
ATOM 1642 ND2 ASN A1006 1.446 222.991 22.420 1.00 78.65 N
ANISOU 1642 ND2 ASN A1006 7637 8486 13762 695 -39 1287 N
ATOM 1643 N TRP A1007 -0.466 224.488 17.345 1.00 66.06 N
ANISOU 1643 N TRP A1007 7112 5998 11992 723 -318 1045 N
ATOM 1644 CA TRP A1007 -0.402 225.344 16.206 1.00 64.58 C
ANISOU 1644 CA TRP A1007 7224 5623 11691 730 -286 913 C
ATOM 1645 C TRP A1007 -1.799 225.691 15.792 1.00 68.11 C
ANISOU 1645 C TRP A1007 7741 5996 12142 786 -427 967 C
ATOM 1646 O TRP A1007 -2.077 226.815 15.457 1.00 67.60 O
ANISOU 1646 O TRP A1007 7831 5888 11967 811 -380 886 O
ATOM 1647 CB TRP A1007 0.292 224.597 15.101 1.00 64.88 C
ANISOU 1647 CB TRP A1007 7439 5463 11749 702 -299 861 C
ATOM 1648 CG TRP A1007 0.291 225.211 13.753 1.00 66.13 C
ANISOU 1648 CG TRP A1007 7917 5395 11814 725 -294 745 C
ATOM 1649 CD1 TRP A1007 -0.397 224.782 12.680 1.00 71.26 C
ANISOU 1649 CD1 TRP A1007 8729 5850 12494 760 -441 762 C
ATOM 1650 CD2 TRP A1007 1.072 226.319 13.302 1.00 64.22 C
ANISOU 1650 CD2 TRP A1007 7873 5091 11436 721 -130 594 C
ATOM 1651 NE1 TRP A1007 -0.120 225.548 11.603 1.00 72.74 N
ANISOU 1651 NE1 TRP A1007 9203 5865 12569 784 -379 632 N
ATOM 1652 CE2 TRP A1007 0.780 226.506 11.960 1.00 68.60 C
ANISOU 1652 CE2 TRP A1007 8703 5418 11945 761 -184 530 C
ATOM 1653 CE3 TRP A1007 1.985 227.175 13.911 1.00 61.46 C
ANISOU 1653 CE3 TRP A1007 7490 4855 11007 692 53 507 C
ATOM 1654 CZ2 TRP A1007 1.355 227.504 11.219 1.00 69.83 C
ANISOU 1654 CZ2 TRP A1007 9093 5459 11979 777 -54 391 C
ATOM 1655 CZ3 TRP A1007 2.549 228.147 13.176 1.00 62.83 C
ANISOU 1655 CZ3 TRP A1007 7893 4910 11070 700 174 370 C
ATOM 1656 CH2 TRP A1007 2.243 228.308 11.848 1.00 66.63 C
ANISOU 1656 CH2 TRP A1007 8640 5168 11508 744 127 315 C
ATOM 1657 N GLU A1008 -2.701 224.729 15.820 1.00 72.45 N
ANISOU 1657 N GLU A1008 8173 6530 12825 807 -601 1109 N
ATOM 1658 CA GLU A1008 -4.067 225.016 15.441 1.00 77.30 C
ANISOU 1658 CA GLU A1008 8843 7072 13456 860 -745 1174 C
ATOM 1659 C GLU A1008 -4.655 225.988 16.421 1.00 76.29 C
ANISOU 1659 C GLU A1008 8592 7124 13270 896 -695 1214 C
ATOM 1660 O GLU A1008 -5.289 226.925 16.024 1.00 77.72 O
ANISOU 1660 O GLU A1008 8915 7250 13365 929 -701 1174 O
ATOM 1661 CB GLU A1008 -4.912 223.766 15.388 1.00 86.28 C
ANISOU 1661 CB GLU A1008 9848 8167 14767 875 -945 1331 C
ATOM 1662 CG GLU A1008 -4.973 223.132 14.026 1.00 95.71 C
ANISOU 1662 CG GLU A1008 11258 9110 15995 871 -1064 1292 C
ATOM 1663 CD GLU A1008 -5.115 221.642 14.135 1.00109.12 C
ANISOU 1663 CD GLU A1008 12796 10793 17873 856 -1202 1417 C
ATOM 1664 OE1 GLU A1008 -5.874 221.190 15.013 1.00114.80 O
ANISOU 1664 OE1 GLU A1008 13260 11643 18716 876 -1288 1574 O
ATOM 1665 OE2 GLU A1008 -4.467 220.926 13.357 1.00112.77 O
ANISOU 1665 OE2 GLU A1008 13383 11111 18354 830 -1222 1364 O
ATOM 1666 N THR A1009 -4.414 225.772 17.701 1.00 74.34 N
ANISOU 1666 N THR A1009 8085 7095 13066 895 -639 1290 N
ATOM 1667 CA THR A1009 -4.884 226.649 18.745 1.00 73.73 C
ANISOU 1667 CA THR A1009 7877 7205 12931 939 -584 1332 C
ATOM 1668 C THR A1009 -4.468 228.110 18.512 1.00 68.83 C
ANISOU 1668 C THR A1009 7453 6569 12129 935 -437 1169 C
ATOM 1669 O THR A1009 -5.242 229.012 18.686 1.00 69.26 O
ANISOU 1669 O THR A1009 7540 6661 12114 980 -441 1183 O
ATOM 1670 CB THR A1009 -4.356 226.197 20.105 1.00 75.22 C
ANISOU 1670 CB THR A1009 7781 7624 13173 938 -514 1403 C
ATOM 1671 OG1 THR A1009 -5.071 225.042 20.519 1.00 82.74 O
ANISOU 1671 OG1 THR A1009 8516 8625 14295 967 -654 1588 O
ATOM 1672 CG2 THR A1009 -4.537 227.257 21.110 1.00 74.28 C
ANISOU 1672 CG2 THR A1009 7576 7688 12957 983 -422 1401 C
ATOM 1673 N LEU A1010 -3.225 228.326 18.139 1.00 64.79 N
ANISOU 1673 N LEU A1010 7067 6003 11548 883 -306 1020 N
ATOM 1674 CA LEU A1010 -2.724 229.624 17.846 1.00 62.42 C
ANISOU 1674 CA LEU A1010 6952 5670 11096 875 -165 863 C
ATOM 1675 C LEU A1010 -3.497 230.226 16.675 1.00 64.30 C
ANISOU 1675 C LEU A1010 7440 5718 11272 905 -225 817 C
ATOM 1676 O LEU A1010 -3.849 231.374 16.704 1.00 63.94 O
ANISOU 1676 O LEU A1010 7483 5693 11120 932 -167 763 O
ATOM 1677 CB LEU A1010 -1.252 229.500 17.489 1.00 60.19 C
ANISOU 1677 CB LEU A1010 6760 5327 10785 814 -34 733 C
ATOM 1678 CG LEU A1010 -0.349 230.705 17.333 1.00 60.90 C
ANISOU 1678 CG LEU A1010 7001 5398 10741 792 142 565 C
ATOM 1679 CD1 LEU A1010 1.084 230.245 17.246 1.00 61.78 C
ANISOU 1679 CD1 LEU A1010 7119 5487 10870 731 251 492 C
ATOM 1680 CD2 LEU A1010 -0.716 231.503 16.104 1.00 60.91 C
ANISOU 1680 CD2 LEU A1010 7286 5201 10654 817 144 472 C
ATOM 1681 N ASN A1011 -3.758 229.447 15.643 1.00 67.00 N
ANISOU 1681 N ASN A1011 7900 5877 11681 903 -342 836 N
ATOM 1682 CA ASN A1011 -4.455 229.950 14.481 1.00 70.65 C
ANISOU 1682 CA ASN A1011 8606 6152 12086 937 -404 788 C
ATOM 1683 C ASN A1011 -5.953 230.131 14.614 1.00 74.60 C
ANISOU 1683 C ASN A1011 9057 6675 12614 990 -542 910 C
ATOM 1684 O ASN A1011 -6.520 230.949 13.939 1.00 77.37 O
ANISOU 1684 O ASN A1011 9589 6928 12879 1021 -547 859 O
ATOM 1685 CB ASN A1011 -4.165 229.073 13.290 1.00 75.18 C
ANISOU 1685 CB ASN A1011 9340 6511 12711 925 -483 757 C
ATOM 1686 CG ASN A1011 -2.815 229.339 12.716 1.00 76.74 C
ANISOU 1686 CG ASN A1011 9707 6619 12831 893 -328 604 C
ATOM 1687 OD1 ASN A1011 -2.154 230.277 13.117 1.00 74.62 O
ANISOU 1687 OD1 ASN A1011 9451 6431 12468 878 -165 512 O
ATOM 1688 ND2 ASN A1011 -2.389 228.511 11.786 1.00 80.34 N
ANISOU 1688 ND2 ASN A1011 10291 6905 13330 886 -378 580 N
ATOM 1689 N ASP A1012 -6.591 229.360 15.469 1.00 75.89 N
ANISOU 1689 N ASP A1012 8972 6962 12900 1004 -651 1077 N
ATOM 1690 CA ASP A1012 -8.013 229.469 15.643 1.00 81.01 C
ANISOU 1690 CA ASP A1012 9555 7634 13591 1057 -784 1214 C
ATOM 1691 C ASP A1012 -8.317 230.544 16.605 1.00 78.22 C
ANISOU 1691 C ASP A1012 9116 7461 13145 1090 -688 1231 C
ATOM 1692 O ASP A1012 -9.330 231.177 16.509 1.00 81.50 O
ANISOU 1692 O ASP A1012 9579 7868 13519 1134 -737 1281 O
ATOM 1693 CB ASP A1012 -8.620 228.171 16.125 1.00 87.73 C
ANISOU 1693 CB ASP A1012 10172 8532 14629 1067 -946 1401 C
ATOM 1694 CG ASP A1012 -8.511 227.102 15.103 1.00 97.56 C
ANISOU 1694 CG ASP A1012 11514 9581 15972 1042 -1070 1395 C
ATOM 1695 OD1 ASP A1012 -8.195 227.442 13.960 1.00 99.80 O
ANISOU 1695 OD1 ASP A1012 12062 9684 16172 1033 -1050 1260 O
ATOM 1696 OD2 ASP A1012 -8.709 225.938 15.437 1.00102.81 O
ANISOU 1696 OD2 ASP A1012 11997 10272 16795 1037 -1183 1522 O
ATOM 1697 N ASN A1013 -7.409 230.800 17.521 1.00 72.67 N
ANISOU 1697 N ASN A1013 8296 6918 12398 1070 -547 1184 N
ATOM 1698 CA ASN A1013 -7.612 231.858 18.475 1.00 70.94 C
ANISOU 1698 CA ASN A1013 8002 6873 12079 1106 -450 1187 C
ATOM 1699 C ASN A1013 -7.324 233.235 17.862 1.00 68.35 C
ANISOU 1699 C ASN A1013 7923 6468 11581 1100 -323 1016 C
ATOM 1700 O ASN A1013 -7.739 234.232 18.383 1.00 67.80 O
ANISOU 1700 O ASN A1013 7848 6497 11416 1137 -265 1017 O
ATOM 1701 CB ASN A1013 -6.798 231.621 19.733 1.00 69.43 C
ANISOU 1701 CB ASN A1013 7587 6888 11908 1096 -357 1203 C
ATOM 1702 CG ASN A1013 -7.548 230.842 20.781 1.00 76.74 C
ANISOU 1702 CG ASN A1013 8229 7972 12958 1148 -459 1409 C
ATOM 1703 OD1 ASN A1013 -8.719 231.029 20.971 1.00 81.97 O
ANISOU 1703 OD1 ASN A1013 8845 8662 13640 1208 -547 1535 O
ATOM 1704 ND2 ASN A1013 -6.859 229.978 21.477 1.00 77.53 N
ANISOU 1704 ND2 ASN A1013 8135 8179 13143 1129 -438 1448 N
ATOM 1705 N LEU A1014 -6.605 233.267 16.760 1.00 67.46 N
ANISOU 1705 N LEU A1014 8024 6176 11431 1060 -277 875 N
ATOM 1706 CA LEU A1014 -6.360 234.484 16.071 1.00 66.94 C
ANISOU 1706 CA LEU A1014 8195 6017 11221 1060 -163 721 C
ATOM 1707 C LEU A1014 -7.671 234.871 15.403 1.00 72.69 C
ANISOU 1707 C LEU A1014 9047 6649 11924 1110 -267 775 C
ATOM 1708 O LEU A1014 -8.121 235.978 15.550 1.00 73.06 O
ANISOU 1708 O LEU A1014 9157 6739 11862 1140 -204 748 O
ATOM 1709 CB LEU A1014 -5.274 234.283 15.028 1.00 66.33 C
ANISOU 1709 CB LEU A1014 8308 5765 11130 1017 -95 577 C
ATOM 1710 CG LEU A1014 -3.890 234.757 15.427 1.00 63.33 C
ANISOU 1710 CG LEU A1014 7924 5449 10691 973 86 446 C
ATOM 1711 CD1 LEU A1014 -2.847 234.337 14.424 1.00 64.37 C
ANISOU 1711 CD1 LEU A1014 8219 5406 10834 937 137 340 C
ATOM 1712 CD2 LEU A1014 -3.867 236.252 15.614 1.00 63.19 C
ANISOU 1712 CD2 LEU A1014 7998 5478 10534 991 219 345 C
ATOM 1713 N LYS A1015 -8.292 233.946 14.680 1.00 77.97 N
ANISOU 1713 N LYS A1015 9748 7185 12694 1118 -429 855 N
ATOM 1714 CA LYS A1015 -9.534 234.226 13.985 1.00 85.59 C
ANISOU 1714 CA LYS A1015 10831 8044 13646 1163 -543 910 C
ATOM 1715 C LYS A1015 -10.588 234.686 14.970 1.00 86.33 C
ANISOU 1715 C LYS A1015 10764 8305 13732 1208 -575 1052 C
ATOM 1716 O LYS A1015 -11.229 235.690 14.769 1.00 88.59 O
ANISOU 1716 O LYS A1015 11163 8583 13915 1241 -543 1034 O
ATOM 1717 CB LYS A1015 -9.989 233.015 13.214 1.00 94.36 C
ANISOU 1717 CB LYS A1015 11961 9002 14890 1163 -729 987 C
ATOM 1718 CG LYS A1015 -8.906 232.487 12.312 1.00 98.92 C
ANISOU 1718 CG LYS A1015 12689 9422 15474 1127 -696 859 C
ATOM 1719 CD LYS A1015 -9.454 231.710 11.138 1.00112.49 C
ANISOU 1719 CD LYS A1015 14546 10929 17266 1145 -869 882 C
ATOM 1720 CE LYS A1015 -10.032 230.381 11.580 1.00120.05 C
ANISOU 1720 CE LYS A1015 15287 11919 18407 1139 -1054 1057 C
ATOM 1721 NZ LYS A1015 -10.231 229.461 10.428 1.00130.86 N
ANISOU 1721 NZ LYS A1015 16794 13070 19858 1146 -1214 1054 N
ATOM 1722 N VAL A1016 -10.718 233.979 16.076 1.00 84.35 N
ANISOU 1722 N VAL A1016 10248 8215 13586 1214 -626 1194 N
ATOM 1723 CA VAL A1016 -11.664 234.321 17.108 1.00 86.01 C
ANISOU 1723 CA VAL A1016 10285 8595 13799 1270 -654 1347 C
ATOM 1724 C VAL A1016 -11.490 235.758 17.594 1.00 82.41 C
ANISOU 1724 C VAL A1016 9893 8248 13170 1290 -490 1257 C
ATOM 1725 O VAL A1016 -12.439 236.424 17.952 1.00 85.12 O
ANISOU 1725 O VAL A1016 10219 8661 13461 1343 -504 1343 O
ATOM 1726 CB VAL A1016 -11.461 233.388 18.295 1.00 85.16 C
ANISOU 1726 CB VAL A1016 9883 8658 13816 1276 -686 1478 C
ATOM 1727 CG1 VAL A1016 -12.200 233.847 19.518 1.00 86.98 C
ANISOU 1727 CG1 VAL A1016 9930 9091 14028 1345 -675 1621 C
ATOM 1728 CG2 VAL A1016 -11.825 231.975 17.923 1.00 90.89 C
ANISOU 1728 CG2 VAL A1016 10518 9289 14726 1265 -862 1597 C
ATOM 1729 N ILE A1017 -10.259 236.224 17.603 1.00 76.93 N
ANISOU 1729 N ILE A1017 9273 7565 12393 1247 -335 1086 N
ATOM 1730 CA ILE A1017 -9.930 237.542 18.082 1.00 74.42 C
ANISOU 1730 CA ILE A1017 9009 7344 11921 1258 -176 984 C
ATOM 1731 C ILE A1017 -10.258 238.539 17.017 1.00 78.14 C
ANISOU 1731 C ILE A1017 9746 7669 12276 1265 -132 877 C
ATOM 1732 O ILE A1017 -10.739 239.609 17.291 1.00 78.56 O
ANISOU 1732 O ILE A1017 9846 7785 12216 1300 -68 870 O
ATOM 1733 CB ILE A1017 -8.451 237.630 18.434 1.00 69.11 C
ANISOU 1733 CB ILE A1017 8316 6723 11220 1206 -34 840 C
ATOM 1734 CG1 ILE A1017 -8.245 237.085 19.819 1.00 68.02 C
ANISOU 1734 CG1 ILE A1017 7901 6795 11148 1222 -41 944 C
ATOM 1735 CG2 ILE A1017 -7.959 239.057 18.352 1.00 67.79 C
ANISOU 1735 CG2 ILE A1017 8305 6558 10893 1202 131 676 C
ATOM 1736 CD1 ILE A1017 -6.825 237.165 20.267 1.00 65.67 C
ANISOU 1736 CD1 ILE A1017 7563 6562 10825 1172 92 814 C
ATOM 1737 N GLU A1018 -10.032 238.140 15.779 1.00 81.63 N
ANISOU 1737 N GLU A1018 10361 7910 12746 1237 -171 801 N
ATOM 1738 CA GLU A1018 -10.287 238.965 14.632 1.00 87.40 C
ANISOU 1738 CA GLU A1018 11353 8479 13374 1249 -131 694 C
ATOM 1739 C GLU A1018 -11.730 239.413 14.522 1.00 94.95 C
ANISOU 1739 C GLU A1018 12341 9437 14299 1304 -218 808 C
ATOM 1740 O GLU A1018 -11.992 240.542 14.140 1.00 97.68 O
ANISOU 1740 O GLU A1018 12847 9751 14516 1325 -130 731 O
ATOM 1741 CB GLU A1018 -9.883 238.240 13.371 1.00 92.66 C
ANISOU 1741 CB GLU A1018 12178 8932 14096 1226 -188 623 C
ATOM 1742 CG GLU A1018 -8.488 238.589 12.935 1.00 94.33 C
ANISOU 1742 CG GLU A1018 12520 9074 14248 1188 -28 437 C
ATOM 1743 CD GLU A1018 -7.943 237.630 11.928 1.00103.31 C
ANISOU 1743 CD GLU A1018 13764 10031 15459 1169 -88 392 C
ATOM 1744 OE1 GLU A1018 -8.717 236.855 11.376 1.00109.35 O
ANISOU 1744 OE1 GLU A1018 14549 10697 16303 1189 -253 481 O
ATOM 1745 OE2 GLU A1018 -6.739 237.668 11.681 1.00103.35 O
ANISOU 1745 OE2 GLU A1018 13837 9988 15444 1137 30 270 O
ATOM 1746 N LYS A1019 -12.659 238.534 14.867 1.00 99.03 N
ANISOU 1746 N LYS A1019 12699 9990 14937 1327 -386 996 N
ATOM 1747 CA LYS A1019 -14.067 238.853 14.791 1.00107.23 C
ANISOU 1747 CA LYS A1019 13750 11029 15966 1379 -481 1129 C
ATOM 1748 C LYS A1019 -14.451 238.560 16.217 1.00106.38 C
ANISOU 1748 C LYS A1019 13366 11132 15919 1410 -514 1301 C
ATOM 1749 O LYS A1019 -14.786 237.451 16.553 1.00110.61 O
ANISOU 1749 O LYS A1019 13727 11691 16607 1415 -649 1447 O
ATOM 1750 CB LYS A1019 -14.761 237.918 13.842 1.00117.87 C
ANISOU 1750 CB LYS A1019 15151 12204 17430 1382 -668 1203 C
ATOM 1751 CG LYS A1019 -14.754 236.472 14.272 1.00122.09 C
ANISOU 1751 CG LYS A1019 15473 12763 18151 1368 -812 1336 C
ATOM 1752 CD LYS A1019 -15.504 235.656 13.240 1.00135.46 C
ANISOU 1752 CD LYS A1019 17247 14268 19954 1374 -1004 1398 C
ATOM 1753 CE LYS A1019 -15.533 234.183 13.619 1.00141.21 C
ANISOU 1753 CE LYS A1019 17765 15009 20882 1359 -1156 1533 C
ATOM 1754 NZ LYS A1019 -16.260 233.353 12.631 1.00153.63 N
ANISOU 1754 NZ LYS A1019 19410 16391 22572 1364 -1358 1594 N
ATOM 1755 N ALA A1020 -14.511 239.598 17.011 1.00101.81 N
ANISOU 1755 N ALA A1020 12761 10702 15221 1440 -395 1293 N
ATOM 1756 CA ALA A1020 -14.922 239.496 18.382 1.00101.54 C
ANISOU 1756 CA ALA A1020 12486 10875 15219 1489 -410 1455 C
ATOM 1757 C ALA A1020 -15.784 240.717 18.654 1.00104.33 C
ANISOU 1757 C ALA A1020 12905 11300 15436 1547 -353 1498 C
ATOM 1758 O ALA A1020 -15.647 241.747 18.003 1.00104.15 O
ANISOU 1758 O ALA A1020 13095 11203 15277 1534 -250 1355 O
ATOM 1759 CB ALA A1020 -13.727 239.438 19.308 1.00 94.60 C
ANISOU 1759 CB ALA A1020 11479 10136 14328 1467 -297 1376 C
ATOM 1760 N ASP A1021 -16.686 240.589 19.610 1.00107.65 N
ANISOU 1760 N ASP A1021 13143 11862 15896 1616 -418 1702 N
ATOM 1761 CA ASP A1021 -17.596 241.678 19.932 1.00111.65 C
ANISOU 1761 CA ASP A1021 13700 12445 16279 1679 -373 1773 C
ATOM 1762 C ASP A1021 -16.921 242.684 20.833 1.00105.33 C
ANISOU 1762 C ASP A1021 12888 11800 15331 1698 -204 1673 C
ATOM 1763 O ASP A1021 -16.827 243.843 20.488 1.00105.16 O
ANISOU 1763 O ASP A1021 13047 11752 15156 1692 -88 1547 O
ATOM 1764 CB ASP A1021 -18.916 241.157 20.550 1.00122.11 C
ANISOU 1764 CB ASP A1021 14841 13848 17706 1757 -513 2051 C
ATOM 1765 CG ASP A1021 -20.132 242.066 20.244 1.00134.68 C
ANISOU 1765 CG ASP A1021 16554 15416 19201 1807 -520 2138 C
ATOM 1766 OD1 ASP A1021 -19.943 243.090 19.573 1.00133.74 O
ANISOU 1766 OD1 ASP A1021 16657 15226 18932 1781 -413 1978 O
ATOM 1767 OD2 ASP A1021 -21.275 241.766 20.675 1.00144.47 O
ANISOU 1767 OD2 ASP A1021 17666 16709 20516 1874 -627 2371 O
ATOM 1768 N ASN A1022 -16.421 242.237 21.972 1.00100.84 N
ANISOU 1768 N ASN A1022 12110 11392 14811 1721 -189 1724 N
ATOM 1769 CA ASN A1022 -15.798 243.155 22.898 1.00 96.21 C
ANISOU 1769 CA ASN A1022 11504 10959 14092 1747 -44 1634 C
ATOM 1770 C ASN A1022 -14.386 242.801 23.268 1.00 89.65 C
ANISOU 1770 C ASN A1022 10604 10172 13288 1694 28 1491 C
ATOM 1771 O ASN A1022 -13.776 241.933 22.689 1.00 88.37 O
ANISOU 1771 O ASN A1022 10439 9906 13230 1627 -14 1434 O
ATOM 1772 CB ASN A1022 -16.600 243.164 24.173 1.00100.99 C
ANISOU 1772 CB ASN A1022 11913 11758 14699 1855 -78 1845 C
ATOM 1773 CG ASN A1022 -17.051 241.790 24.552 1.00107.92 C
ANISOU 1773 CG ASN A1022 12565 12669 15770 1886 -225 2049 C
ATOM 1774 OD1 ASN A1022 -17.207 240.940 23.706 1.00110.96 O
ANISOU 1774 OD1 ASN A1022 12970 12910 16280 1836 -331 2072 O
ATOM 1775 ND2 ASN A1022 -17.249 241.569 25.821 1.00110.97 N
ANISOU 1775 ND2 ASN A1022 12739 13243 16182 1975 -232 2196 N
ATOM 1776 N ALA A1023 -13.912 243.494 24.288 1.00 86.22 N
ANISOU 1776 N ALA A1023 10107 9897 12754 1730 133 1442 N
ATOM 1777 CA ALA A1023 -12.595 243.340 24.824 1.00 81.50 C
ANISOU 1777 CA ALA A1023 9435 9370 12163 1691 213 1310 C
ATOM 1778 C ALA A1023 -12.463 242.062 25.620 1.00 82.18 C
ANISOU 1778 C ALA A1023 9264 9562 12397 1715 128 1447 C
ATOM 1779 O ALA A1023 -11.404 241.487 25.678 1.00 79.91 O
ANISOU 1779 O ALA A1023 8918 9273 12171 1657 155 1354 O
ATOM 1780 CB ALA A1023 -12.267 244.529 25.694 1.00 80.77 C
ANISOU 1780 CB ALA A1023 9359 9415 11915 1734 337 1227 C
ATOM 1781 N ALA A1024 -13.536 241.600 26.222 1.00 86.06 N
ANISOU 1781 N ALA A1024 9599 10145 12955 1804 27 1675 N
ATOM 1782 CA ALA A1024 -13.475 240.393 27.032 1.00 88.30 C
ANISOU 1782 CA ALA A1024 9624 10540 13388 1841 -50 1822 C
ATOM 1783 C ALA A1024 -13.337 239.116 26.235 1.00 87.41 C
ANISOU 1783 C ALA A1024 9477 10289 13446 1770 -154 1849 C
ATOM 1784 O ALA A1024 -12.901 238.121 26.742 1.00 88.83 O
ANISOU 1784 O ALA A1024 9471 10536 13744 1769 -189 1904 O
ATOM 1785 CB ALA A1024 -14.690 240.314 27.937 1.00 95.38 C
ANISOU 1785 CB ALA A1024 10358 11574 14308 1971 -120 2072 C
ATOM 1786 N GLN A1025 -13.752 239.146 24.992 1.00 85.92 N
ANISOU 1786 N GLN A1025 9469 9908 13269 1717 -208 1814 N
ATOM 1787 CA GLN A1025 -13.665 237.988 24.153 1.00 86.15 C
ANISOU 1787 CA GLN A1025 9493 9790 13451 1654 -315 1833 C
ATOM 1788 C GLN A1025 -12.233 237.881 23.711 1.00 79.51 C
ANISOU 1788 C GLN A1025 8740 8880 12591 1559 -224 1618 C
ATOM 1789 O GLN A1025 -11.647 236.831 23.680 1.00 78.80 O
ANISOU 1789 O GLN A1025 8549 8770 12620 1518 -264 1622 O
ATOM 1790 CB GLN A1025 -14.534 238.169 22.935 1.00 89.97 C
ANISOU 1790 CB GLN A1025 10166 10085 13933 1635 -396 1846 C
ATOM 1791 CG GLN A1025 -15.687 237.214 22.865 1.00101.20 C
ANISOU 1791 CG GLN A1025 11461 11474 15518 1677 -573 2075 C
ATOM 1792 CD GLN A1025 -16.916 237.857 22.288 1.00110.55 C
ANISOU 1792 CD GLN A1025 12778 12575 16650 1713 -629 2153 C
ATOM 1793 OE1 GLN A1025 -16.978 238.131 21.110 1.00112.35 O
ANISOU 1793 OE1 GLN A1025 13221 12627 16838 1662 -642 2045 O
ATOM 1794 NE2 GLN A1025 -17.892 238.110 23.126 1.00116.15 N
ANISOU 1794 NE2 GLN A1025 13360 13414 17357 1807 -657 2345 N
ATOM 1795 N VAL A1026 -11.669 239.022 23.388 1.00 75.02 N
ANISOU 1795 N VAL A1026 8359 8275 11869 1528 -94 1432 N
ATOM 1796 CA VAL A1026 -10.309 239.125 22.967 1.00 69.91 C
ANISOU 1796 CA VAL A1026 7813 7560 11189 1444 11 1225 C
ATOM 1797 C VAL A1026 -9.445 238.653 24.112 1.00 69.25 C
ANISOU 1797 C VAL A1026 7517 7647 11148 1448 57 1230 C
ATOM 1798 O VAL A1026 -8.591 237.826 23.922 1.00 67.85 O
ANISOU 1798 O VAL A1026 7294 7429 11055 1388 56 1180 O
ATOM 1799 CB VAL A1026 -10.012 240.556 22.595 1.00 67.86 C
ANISOU 1799 CB VAL A1026 7767 7257 10761 1430 144 1053 C
ATOM 1800 CG1 VAL A1026 -8.536 240.833 22.672 1.00 64.60 C
ANISOU 1800 CG1 VAL A1026 7391 6847 10306 1365 277 860 C
ATOM 1801 CG2 VAL A1026 -10.577 240.852 21.230 1.00 69.95 C
ANISOU 1801 CG2 VAL A1026 8262 7319 10997 1408 110 1012 C
ATOM 1802 N LYS A1027 -9.725 239.102 25.329 1.00 71.24 N
ANISOU 1802 N LYS A1027 7629 8094 11345 1527 88 1305 N
ATOM 1803 CA LYS A1027 -8.982 238.660 26.485 1.00 72.70 C
ANISOU 1803 CA LYS A1027 7603 8455 11566 1546 126 1320 C
ATOM 1804 C LYS A1027 -9.049 237.157 26.710 1.00 75.82 C
ANISOU 1804 C LYS A1027 7792 8877 12141 1548 20 1466 C
ATOM 1805 O LYS A1027 -8.099 236.561 27.162 1.00 76.04 O
ANISOU 1805 O LYS A1027 7700 8972 12222 1517 58 1424 O
ATOM 1806 CB LYS A1027 -9.424 239.372 27.742 1.00 77.91 C
ANISOU 1806 CB LYS A1027 8151 9315 12134 1653 161 1396 C
ATOM 1807 CG LYS A1027 -9.078 238.569 28.972 1.00 85.93 C
ANISOU 1807 CG LYS A1027 8899 10520 13231 1707 149 1495 C
ATOM 1808 CD LYS A1027 -9.719 239.116 30.215 1.00 96.24 C
ANISOU 1808 CD LYS A1027 10082 12024 14462 1839 159 1613 C
ATOM 1809 CE LYS A1027 -8.651 239.557 31.184 1.00102.87 C
ANISOU 1809 CE LYS A1027 10854 13013 15221 1853 266 1489 C
ATOM 1810 NZ LYS A1027 -8.992 239.148 32.560 1.00113.91 N
ANISOU 1810 NZ LYS A1027 12005 14628 16650 1983 239 1656 N
ATOM 1811 N ASP A1028 -10.190 236.553 26.432 1.00 78.95 N
ANISOU 1811 N ASP A1028 8139 9224 12636 1588 -112 1644 N
ATOM 1812 CA ASP A1028 -10.344 235.131 26.583 1.00 82.91 C
ANISOU 1812 CA ASP A1028 8447 9736 13319 1591 -221 1791 C
ATOM 1813 C ASP A1028 -9.424 234.419 25.626 1.00 78.26 C
ANISOU 1813 C ASP A1028 7948 8989 12797 1480 -223 1666 C
ATOM 1814 O ASP A1028 -8.658 233.593 26.036 1.00 79.21 O
ANISOU 1814 O ASP A1028 7926 9172 12999 1454 -209 1665 O
ATOM 1815 CB ASP A1028 -11.793 234.720 26.296 1.00 91.37 C
ANISOU 1815 CB ASP A1028 9480 10751 14487 1648 -370 1996 C
ATOM 1816 CG ASP A1028 -12.591 234.454 27.554 1.00105.51 C
ANISOU 1816 CG ASP A1028 11020 12735 16335 1771 -415 2220 C
ATOM 1817 OD1 ASP A1028 -12.610 235.308 28.464 1.00108.49 O
ANISOU 1817 OD1 ASP A1028 11362 13268 16593 1844 -329 2220 O
ATOM 1818 OD2 ASP A1028 -13.218 233.383 27.629 1.00113.34 O
ANISOU 1818 OD2 ASP A1028 11849 13719 17497 1801 -537 2402 O
ATOM 1819 N ALA A1029 -9.500 234.753 24.350 1.00 74.26 N
ANISOU 1819 N ALA A1029 7682 8280 12251 1422 -236 1563 N
ATOM 1820 CA ALA A1029 -8.685 234.097 23.351 1.00 71.27 C
ANISOU 1820 CA ALA A1029 7414 7736 11930 1329 -242 1451 C
ATOM 1821 C ALA A1029 -7.177 234.332 23.409 1.00 66.23 C
ANISOU 1821 C ALA A1029 6824 7111 11228 1260 -97 1263 C
ATOM 1822 O ALA A1029 -6.452 233.607 22.793 1.00 64.99 O
ANISOU 1822 O ALA A1029 6709 6848 11136 1194 -102 1202 O
ATOM 1823 CB ALA A1029 -9.197 234.399 21.974 1.00 71.15 C
ANISOU 1823 CB ALA A1029 7647 7501 11886 1301 -296 1396 C
ATOM 1824 N LEU A1030 -6.713 235.345 24.119 1.00 64.19 N
ANISOU 1824 N LEU A1030 6568 6975 10847 1278 27 1172 N
ATOM 1825 CA LEU A1030 -5.294 235.603 24.228 1.00 61.48 C
ANISOU 1825 CA LEU A1030 6260 6647 10453 1214 161 1001 C
ATOM 1826 C LEU A1030 -4.758 234.994 25.511 1.00 64.15 C
ANISOU 1826 C LEU A1030 6337 7188 10847 1236 183 1063 C
ATOM 1827 O LEU A1030 -3.588 234.768 25.655 1.00 63.06 O
ANISOU 1827 O LEU A1030 6172 7070 10718 1179 264 963 O
ATOM 1828 CB LEU A1030 -5.014 237.098 24.250 1.00 59.81 C
ANISOU 1828 CB LEU A1030 6204 6442 10077 1216 285 850 C
ATOM 1829 CG LEU A1030 -5.178 237.969 23.023 1.00 58.93 C
ANISOU 1829 CG LEU A1030 6372 6140 9878 1187 320 732 C
ATOM 1830 CD1 LEU A1030 -5.444 239.373 23.520 1.00 59.78 C
ANISOU 1830 CD1 LEU A1030 6541 6334 9841 1232 404 675 C
ATOM 1831 CD2 LEU A1030 -3.940 237.948 22.173 1.00 57.13 C
ANISOU 1831 CD2 LEU A1030 6292 5767 9647 1101 408 561 C
ATOM 1832 N THR A1031 -5.640 234.752 26.459 1.00 68.60 N
ANISOU 1832 N THR A1031 6707 7907 11449 1327 115 1236 N
ATOM 1833 CA THR A1031 -5.228 234.151 27.699 1.00 73.69 C
ANISOU 1833 CA THR A1031 7097 8753 12151 1367 133 1310 C
ATOM 1834 C THR A1031 -4.911 232.691 27.393 1.00 74.42 C
ANISOU 1834 C THR A1031 7080 8793 12404 1318 66 1378 C
ATOM 1835 O THR A1031 -3.955 232.129 27.899 1.00 75.88 O
ANISOU 1835 O THR A1031 7140 9062 12630 1288 121 1346 O
ATOM 1836 CB THR A1031 -6.270 234.311 28.821 1.00 81.71 C
ANISOU 1836 CB THR A1031 7935 9951 13161 1496 85 1487 C
ATOM 1837 OG1 THR A1031 -7.527 234.713 28.280 1.00 83.27 O
ANISOU 1837 OG1 THR A1031 8239 10060 13341 1537 4 1575 O
ATOM 1838 CG2 THR A1031 -5.836 235.357 29.804 1.00 83.69 C
ANISOU 1838 CG2 THR A1031 8165 10361 13273 1545 194 1402 C
ATOM 1839 N LYS A1032 -5.711 232.115 26.513 1.00 73.53 N
ANISOU 1839 N LYS A1032 7029 8531 12378 1308 -54 1466 N
ATOM 1840 CA LYS A1032 -5.555 230.760 26.072 1.00 74.81 C
ANISOU 1840 CA LYS A1032 7116 8614 12694 1263 -135 1533 C
ATOM 1841 C LYS A1032 -4.343 230.690 25.200 1.00 69.52 C
ANISOU 1841 C LYS A1032 6615 7803 11995 1157 -58 1353 C
ATOM 1842 O LYS A1032 -3.591 229.748 25.279 1.00 70.84 O
ANISOU 1842 O LYS A1032 6686 7983 12249 1112 -48 1356 O
ATOM 1843 CB LYS A1032 -6.745 230.335 25.219 1.00 78.53 C
ANISOU 1843 CB LYS A1032 7654 8933 13251 1279 -289 1650 C
ATOM 1844 CG LYS A1032 -7.980 229.862 25.960 1.00 90.29 C
ANISOU 1844 CG LYS A1032 8929 10533 14845 1377 -404 1882 C
ATOM 1845 CD LYS A1032 -9.154 229.800 24.994 1.00 96.45 C
ANISOU 1845 CD LYS A1032 9833 11140 15675 1386 -544 1963 C
ATOM 1846 CE LYS A1032 -10.253 228.876 25.473 1.00109.29 C
ANISOU 1846 CE LYS A1032 11233 12820 17471 1460 -688 2208 C
ATOM 1847 NZ LYS A1032 -11.115 228.393 24.354 1.00114.41 N
ANISOU 1847 NZ LYS A1032 11989 13262 18218 1438 -846 2272 N
ATOM 1848 N MET A1033 -4.166 231.679 24.337 1.00 64.24 N
ANISOU 1848 N MET A1033 6202 6996 11210 1121 -2 1204 N
ATOM 1849 CA MET A1033 -3.042 231.707 23.422 1.00 60.32 C
ANISOU 1849 CA MET A1033 5888 6349 10682 1032 78 1037 C
ATOM 1850 C MET A1033 -1.743 231.778 24.157 1.00 60.29 C
ANISOU 1850 C MET A1033 5792 6466 10649 994 210 944 C
ATOM 1851 O MET A1033 -0.777 231.195 23.747 1.00 59.19 O
ANISOU 1851 O MET A1033 5683 6257 10550 926 252 880 O
ATOM 1852 CB MET A1033 -3.119 232.895 22.498 1.00 57.79 C
ANISOU 1852 CB MET A1033 5842 5881 10235 1018 131 899 C
ATOM 1853 CG MET A1033 -3.558 232.580 21.105 1.00 59.06 C
ANISOU 1853 CG MET A1033 6202 5812 10427 997 45 890 C
ATOM 1854 SD MET A1033 -4.007 234.082 20.254 1.00 59.37 S
ANISOU 1854 SD MET A1033 6522 5723 10313 1015 98 769 S
ATOM 1855 CE MET A1033 -2.781 234.126 18.990 1.00 52.35 C
ANISOU 1855 CE MET A1033 5876 4623 9392 942 192 587 C
ATOM 1856 N ARG A1034 -1.732 232.533 25.228 1.00 61.96 N
ANISOU 1856 N ARG A1034 5901 6856 10786 1042 274 935 N
ATOM 1857 CA ARG A1034 -0.543 232.672 26.009 1.00 64.11 C
ANISOU 1857 CA ARG A1034 6078 7253 11027 1013 392 846 C
ATOM 1858 C ARG A1034 -0.103 231.339 26.561 1.00 68.51 C
ANISOU 1858 C ARG A1034 6414 7907 11711 1000 367 942 C
ATOM 1859 O ARG A1034 1.016 230.949 26.382 1.00 68.81 O
ANISOU 1859 O ARG A1034 6460 7913 11770 929 437 861 O
ATOM 1860 CB ARG A1034 -0.779 233.634 27.132 1.00 67.68 C
ANISOU 1860 CB ARG A1034 6444 7888 11383 1085 440 842 C
ATOM 1861 CG ARG A1034 0.409 234.488 27.417 1.00 70.60 C
ANISOU 1861 CG ARG A1034 6873 8293 11659 1042 579 666 C
ATOM 1862 CD ARG A1034 0.383 234.980 28.827 1.00 78.89 C
ANISOU 1862 CD ARG A1034 7753 9571 12652 1118 612 688 C
ATOM 1863 NE ARG A1034 1.646 235.594 29.120 1.00 84.35 N
ANISOU 1863 NE ARG A1034 8476 10293 13281 1066 734 522 N
ATOM 1864 CZ ARG A1034 2.287 235.447 30.254 1.00 94.32 C
ANISOU 1864 CZ ARG A1034 9555 11737 14546 1089 777 517 C
ATOM 1865 NH1 ARG A1034 1.762 234.712 31.203 1.00 99.55 N
ANISOU 1865 NH1 ARG A1034 9988 12570 15265 1170 715 672 N
ATOM 1866 NH2 ARG A1034 3.449 236.031 30.431 1.00 97.62 N
ANISOU 1866 NH2 ARG A1034 10014 12162 14913 1034 882 360 N
ATOM 1867 N ALA A1035 -1.003 230.640 27.223 1.00 72.77 N
ANISOU 1867 N ALA A1035 6752 8560 12337 1074 268 1122 N
ATOM 1868 CA ALA A1035 -0.711 229.333 27.790 1.00 78.24 C
ANISOU 1868 CA ALA A1035 7214 9353 13160 1073 238 1233 C
ATOM 1869 C ALA A1035 -0.198 228.326 26.779 1.00 76.23 C
ANISOU 1869 C ALA A1035 7036 8931 12999 986 209 1216 C
ATOM 1870 O ALA A1035 0.660 227.554 27.093 1.00 78.98 O
ANISOU 1870 O ALA A1035 7266 9337 13405 946 255 1215 O
ATOM 1871 CB ALA A1035 -1.932 228.785 28.490 1.00 83.76 C
ANISOU 1871 CB ALA A1035 7707 10169 13950 1175 125 1443 C
ATOM 1872 N ALA A1036 -0.733 228.340 25.571 1.00 72.31 N
ANISOU 1872 N ALA A1036 6739 8226 12510 962 133 1203 N
ATOM 1873 CA ALA A1036 -0.321 227.455 24.499 1.00 71.15 C
ANISOU 1873 CA ALA A1036 6699 7897 12437 890 95 1182 C
ATOM 1874 C ALA A1036 1.018 227.824 23.844 1.00 69.02 C
ANISOU 1874 C ALA A1036 6615 7518 12091 805 225 1001 C
ATOM 1875 O ALA A1036 1.562 227.051 23.071 1.00 67.99 O
ANISOU 1875 O ALA A1036 6561 7255 12015 749 215 981 O
ATOM 1876 CB ALA A1036 -1.395 227.403 23.441 1.00 69.35 C
ANISOU 1876 CB ALA A1036 6629 7483 12237 907 -37 1228 C
ATOM 1877 N ALA A1037 1.527 229.016 24.133 1.00 68.70 N
ANISOU 1877 N ALA A1037 6650 7525 11926 801 342 873 N
ATOM 1878 CA ALA A1037 2.792 229.451 23.593 1.00 68.16 C
ANISOU 1878 CA ALA A1037 6743 7362 11794 728 471 710 C
ATOM 1879 C ALA A1037 3.859 229.122 24.605 1.00 73.97 C
ANISOU 1879 C ALA A1037 7288 8268 12549 699 567 696 C
ATOM 1880 O ALA A1037 4.978 228.910 24.257 1.00 74.18 O
ANISOU 1880 O ALA A1037 7374 8232 12578 631 653 615 O
ATOM 1881 CB ALA A1037 2.772 230.930 23.291 1.00 66.17 C
ANISOU 1881 CB ALA A1037 6682 7052 11408 736 544 578 C
ATOM 1882 N LEU A1038 3.498 229.079 25.867 1.00 79.63 N
ANISOU 1882 N LEU A1038 7775 9203 13280 758 552 780 N
ATOM 1883 CA LEU A1038 4.432 228.724 26.908 1.00 87.43 C
ANISOU 1883 CA LEU A1038 8563 10369 14288 743 635 777 C
ATOM 1884 C LEU A1038 4.667 227.225 26.975 1.00 92.13 C
ANISOU 1884 C LEU A1038 9001 10991 15015 719 594 888 C
ATOM 1885 O LEU A1038 5.655 226.788 27.522 1.00 97.05 O
ANISOU 1885 O LEU A1038 9501 11712 15660 682 675 869 O
ATOM 1886 CB LEU A1038 3.920 229.183 28.252 1.00 93.02 C
ANISOU 1886 CB LEU A1038 9078 11304 14960 833 630 834 C
ATOM 1887 CG LEU A1038 3.868 230.680 28.367 1.00 93.24 C
ANISOU 1887 CG LEU A1038 9240 11335 14852 856 688 713 C
ATOM 1888 CD1 LEU A1038 3.976 231.093 29.815 1.00101.31 C
ANISOU 1888 CD1 LEU A1038 10067 12597 15828 925 729 724 C
ATOM 1889 CD2 LEU A1038 5.010 231.214 27.554 1.00 91.61 C
ANISOU 1889 CD2 LEU A1038 9237 10978 14594 761 795 540 C
ATOM 1890 N ASP A1039 3.746 226.442 26.447 1.00 91.53 N
ANISOU 1890 N ASP A1039 8922 10828 15028 740 467 1008 N
ATOM 1891 CA ASP A1039 3.891 225.008 26.436 1.00 96.25 C
ANISOU 1891 CA ASP A1039 9380 11434 15757 718 418 1117 C
ATOM 1892 C ASP A1039 4.728 224.629 25.258 1.00 94.09 C
ANISOU 1892 C ASP A1039 9303 10958 15489 629 453 1032 C
ATOM 1893 O ASP A1039 5.424 223.631 25.275 1.00 96.93 O
ANISOU 1893 O ASP A1039 9579 11329 15921 583 478 1065 O
ATOM 1894 CB ASP A1039 2.557 224.312 26.283 1.00 98.99 C
ANISOU 1894 CB ASP A1039 9651 11751 16210 777 258 1280 C
ATOM 1895 CG ASP A1039 1.982 223.895 27.582 1.00112.00 C
ANISOU 1895 CG ASP A1039 11003 13626 17928 861 224 1430 C
ATOM 1896 OD1 ASP A1039 2.507 222.958 28.206 1.00118.89 O
ANISOU 1896 OD1 ASP A1039 11674 14617 18882 853 254 1494 O
ATOM 1897 OD2 ASP A1039 0.998 224.504 28.002 1.00115.69 O
ANISOU 1897 OD2 ASP A1039 11434 14157 18367 943 172 1489 O
ATOM 1898 N ALA A1040 4.658 225.410 24.201 1.00 89.57 N
ANISOU 1898 N ALA A1040 8999 10195 14838 609 457 927 N
ATOM 1899 CA ALA A1040 5.471 225.104 23.036 1.00 88.07 C
ANISOU 1899 CA ALA A1040 9015 9803 14645 539 496 846 C
ATOM 1900 C ALA A1040 6.936 225.406 23.327 1.00 91.42 C
ANISOU 1900 C ALA A1040 9443 10276 15017 477 661 736 C
ATOM 1901 O ALA A1040 7.809 224.711 22.864 1.00 92.14 O
ANISOU 1901 O ALA A1040 9577 10290 15144 419 707 723 O
ATOM 1902 CB ALA A1040 4.979 225.855 21.825 1.00 83.39 C
ANISOU 1902 CB ALA A1040 8707 8995 13984 549 458 769 C
ATOM 1903 N GLN A1041 7.168 226.421 24.144 1.00 94.25 N
ANISOU 1903 N GLN A1041 9746 10768 15296 493 742 666 N
ATOM 1904 CA GLN A1041 8.494 226.867 24.545 1.00 99.32 C
ANISOU 1904 CA GLN A1041 10377 11471 15890 439 892 558 C
ATOM 1905 C GLN A1041 9.163 225.889 25.492 1.00106.68 C
ANISOU 1905 C GLN A1041 11060 12579 16896 417 930 629 C
ATOM 1906 O GLN A1041 10.377 225.869 25.602 1.00110.95 O
ANISOU 1906 O GLN A1041 11597 13134 17425 356 1044 562 O
ATOM 1907 CB GLN A1041 8.354 228.188 25.283 1.00103.08 C
ANISOU 1907 CB GLN A1041 10837 12058 16270 477 940 478 C
ATOM 1908 CG GLN A1041 9.432 229.220 25.057 1.00108.83 C
ANISOU 1908 CG GLN A1041 11710 12724 16918 426 1075 316 C
ATOM 1909 CD GLN A1041 9.258 230.380 26.012 1.00117.81 C
ANISOU 1909 CD GLN A1041 12781 14008 17973 470 1109 254 C
ATOM 1910 OE1 GLN A1041 9.513 231.537 25.686 1.00119.25 O
ANISOU 1910 OE1 GLN A1041 13123 14111 18076 460 1173 131 O
ATOM 1911 NE2 GLN A1041 8.795 230.068 27.198 1.00123.04 N
ANISOU 1911 NE2 GLN A1041 13208 14884 18656 528 1063 345 N
ATOM 1912 N LYS A1042 8.374 225.121 26.223 1.00109.25 N
ANISOU 1912 N LYS A1042 11167 13045 17296 472 839 769 N
ATOM 1913 CA LYS A1042 8.928 224.154 27.137 1.00117.14 C
ANISOU 1913 CA LYS A1042 11919 14221 18370 462 875 847 C
ATOM 1914 C LYS A1042 9.198 222.911 26.324 1.00115.76 C
ANISOU 1914 C LYS A1042 11781 13917 18285 409 844 910 C
ATOM 1915 O LYS A1042 10.279 222.345 26.375 1.00119.37 O
ANISOU 1915 O LYS A1042 12198 14392 18765 347 933 894 O
ATOM 1916 CB LYS A1042 7.953 223.859 28.254 1.00122.18 C
ANISOU 1916 CB LYS A1042 12306 15062 19057 555 796 979 C
ATOM 1917 N ALA A1043 8.204 222.515 25.544 1.00110.69 N
ANISOU 1917 N ALA A1043 11228 13138 17692 435 715 979 N
ATOM 1918 CA ALA A1043 8.314 221.341 24.706 1.00109.52 C
ANISOU 1918 CA ALA A1043 11133 12851 17631 396 662 1041 C
ATOM 1919 C ALA A1043 9.455 221.483 23.734 1.00107.05 C
ANISOU 1919 C ALA A1043 11048 12364 17263 320 761 926 C
ATOM 1920 O ALA A1043 9.300 221.166 22.563 1.00102.83 O
ANISOU 1920 O ALA A1043 10711 11618 16740 306 704 920 O
ATOM 1921 CB ALA A1043 7.015 221.093 23.961 1.00105.49 C
ANISOU 1921 CB ALA A1043 10711 12201 17170 441 497 1114 C
ATOM 1922 N GLY A1064 11.958 234.191 18.960 1.00 82.17 N
ANISOU 1922 N GLY A1064 9798 8191 13232 331 1539 -357 N
ATOM 1923 CA GLY A1064 10.631 234.095 18.414 1.00 74.87 C
ANISOU 1923 CA GLY A1064 8961 7205 12283 391 1417 -305 C
ATOM 1924 C GLY A1064 9.595 233.937 19.494 1.00 69.82 C
ANISOU 1924 C GLY A1064 8117 6768 11643 422 1307 -222 C
ATOM 1925 O GLY A1064 8.565 234.530 19.414 1.00 66.89 O
ANISOU 1925 O GLY A1064 7799 6396 11221 473 1247 -220 O
ATOM 1926 N PHE A1065 9.866 233.151 20.517 1.00 69.81 N
ANISOU 1926 N PHE A1065 7882 6944 11699 399 1285 -149 N
ATOM 1927 CA PHE A1065 8.878 232.962 21.565 1.00 67.45 C
ANISOU 1927 CA PHE A1065 7381 6840 11406 444 1184 -56 C
ATOM 1928 C PHE A1065 8.821 234.103 22.552 1.00 69.70 C
ANISOU 1928 C PHE A1065 7588 7275 11621 467 1232 -122 C
ATOM 1929 O PHE A1065 7.829 234.271 23.217 1.00 67.90 O
ANISOU 1929 O PHE A1065 7257 7172 11370 524 1153 -59 O
ATOM 1930 CB PHE A1065 9.075 231.632 22.288 1.00 68.47 C
ANISOU 1930 CB PHE A1065 7282 7107 11629 426 1137 61 C
ATOM 1931 CG PHE A1065 8.386 230.490 21.621 1.00 64.94 C
ANISOU 1931 CG PHE A1065 6854 6569 11252 440 1018 175 C
ATOM 1932 CD1 PHE A1065 7.040 230.373 21.674 1.00 62.33 C
ANISOU 1932 CD1 PHE A1065 6489 6263 10930 501 888 265 C
ATOM 1933 CD2 PHE A1065 9.097 229.550 20.928 1.00 65.91 C
ANISOU 1933 CD2 PHE A1065 7034 6575 11433 394 1035 193 C
ATOM 1934 CE1 PHE A1065 6.411 229.345 21.056 1.00 60.57 C
ANISOU 1934 CE1 PHE A1065 6284 5948 10782 513 770 366 C
ATOM 1935 CE2 PHE A1065 8.471 228.510 20.306 1.00 63.53 C
ANISOU 1935 CE2 PHE A1065 6757 6183 11198 408 918 291 C
ATOM 1936 CZ PHE A1065 7.122 228.413 20.367 1.00 60.54 C
ANISOU 1936 CZ PHE A1065 6340 5827 10836 466 781 375 C
ATOM 1937 N ASP A1066 9.921 234.846 22.643 1.00 74.12 N
ANISOU 1937 N ASP A1066 8194 7818 12151 423 1359 -243 N
ATOM 1938 CA ASP A1066 10.060 236.008 23.487 1.00 78.01 C
ANISOU 1938 CA ASP A1066 8638 8426 12577 437 1415 -330 C
ATOM 1939 C ASP A1066 9.178 237.061 22.884 1.00 72.65 C
ANISOU 1939 C ASP A1066 8140 7648 11816 484 1400 -380 C
ATOM 1940 O ASP A1066 8.470 237.757 23.565 1.00 73.34 O
ANISOU 1940 O ASP A1066 8174 7850 11842 535 1369 -380 O
ATOM 1941 CB ASP A1066 11.502 236.520 23.416 1.00 88.73 C
ANISOU 1941 CB ASP A1066 10045 9730 13941 372 1554 -453 C
ATOM 1942 CG ASP A1066 12.375 236.007 24.526 1.00103.30 C
ANISOU 1942 CG ASP A1066 11668 11750 15833 335 1586 -437 C
ATOM 1943 OD1 ASP A1066 11.889 235.260 25.384 1.00104.41 O
ANISOU 1943 OD1 ASP A1066 11612 12062 15998 366 1508 -334 O
ATOM 1944 OD2 ASP A1066 13.561 236.359 24.547 1.00113.79 O
ANISOU 1944 OD2 ASP A1066 13015 13044 17177 279 1692 -525 O
ATOM 1945 N ILE A1067 9.257 237.179 21.578 1.00 68.39 N
ANISOU 1945 N ILE A1067 7822 6890 11273 472 1428 -421 N
ATOM 1946 CA ILE A1067 8.473 238.115 20.854 1.00 64.94 C
ANISOU 1946 CA ILE A1067 7574 6339 10761 516 1422 -469 C
ATOM 1947 C ILE A1067 6.995 237.754 20.978 1.00 57.66 C
ANISOU 1947 C ILE A1067 6605 5476 9828 578 1280 -351 C
ATOM 1948 O ILE A1067 6.201 238.572 21.360 1.00 57.20 O
ANISOU 1948 O ILE A1067 6548 5485 9699 626 1258 -357 O
ATOM 1949 CB ILE A1067 8.898 238.142 19.391 1.00 66.19 C
ANISOU 1949 CB ILE A1067 7972 6249 10926 500 1479 -526 C
ATOM 1950 CG1 ILE A1067 10.355 238.587 19.266 1.00 74.41 C
ANISOU 1950 CG1 ILE A1067 9060 7226 11986 445 1628 -635 C
ATOM 1951 CG2 ILE A1067 8.006 239.048 18.579 1.00 65.26 C
ANISOU 1951 CG2 ILE A1067 8053 6010 10731 553 1469 -568 C
ATOM 1952 CD1 ILE A1067 10.852 238.709 17.852 1.00 78.25 C
ANISOU 1952 CD1 ILE A1067 9787 7467 12477 444 1702 -689 C
ATOM 1953 N LEU A1068 6.650 236.506 20.708 1.00 52.57 N
ANISOU 1953 N LEU A1068 5908 4809 9258 579 1183 -236 N
ATOM 1954 CA LEU A1068 5.275 236.043 20.753 1.00 47.18 C
ANISOU 1954 CA LEU A1068 5176 4163 8588 635 1040 -110 C
ATOM 1955 C LEU A1068 4.537 236.270 22.047 1.00 45.99 C
ANISOU 1955 C LEU A1068 4825 4233 8414 685 987 -36 C
ATOM 1956 O LEU A1068 3.481 236.827 22.041 1.00 43.78 O
ANISOU 1956 O LEU A1068 4588 3965 8082 740 933 -4 O
ATOM 1957 CB LEU A1068 5.188 234.588 20.366 1.00 45.28 C
ANISOU 1957 CB LEU A1068 4882 3871 8449 620 947 -1 C
ATOM 1958 CG LEU A1068 3.822 234.201 19.838 1.00 43.25 C
ANISOU 1958 CG LEU A1068 4673 3548 8211 672 801 103 C
ATOM 1959 CD1 LEU A1068 3.734 234.431 18.360 1.00 43.52 C
ANISOU 1959 CD1 LEU A1068 4980 3340 8215 674 803 37 C
ATOM 1960 CD2 LEU A1068 3.528 232.767 20.175 1.00 42.67 C
ANISOU 1960 CD2 LEU A1068 4420 3540 8252 671 688 249 C
ATOM 1961 N VAL A1069 5.085 235.810 23.152 1.00 48.13 N
ANISOU 1961 N VAL A1069 4880 4682 8727 672 1004 -2 N
ATOM 1962 CA VAL A1069 4.456 235.983 24.435 1.00 49.35 C
ANISOU 1962 CA VAL A1069 4838 5054 8860 734 960 72 C
ATOM 1963 C VAL A1069 4.338 237.461 24.735 1.00 50.30 C
ANISOU 1963 C VAL A1069 5042 5207 8862 763 1026 -32 C
ATOM 1964 O VAL A1069 3.315 237.936 25.176 1.00 49.42 O
ANISOU 1964 O VAL A1069 4901 5178 8698 833 972 25 O
ATOM 1965 CB VAL A1069 5.219 235.251 25.531 1.00 54.82 C
ANISOU 1965 CB VAL A1069 5292 5924 9611 718 982 110 C
ATOM 1966 CG1 VAL A1069 4.540 235.400 26.868 1.00 58.53 C
ANISOU 1966 CG1 VAL A1069 5558 6622 10058 800 936 196 C
ATOM 1967 CG2 VAL A1069 5.328 233.793 25.187 1.00 53.94 C
ANISOU 1967 CG2 VAL A1069 5105 5774 9616 687 922 214 C
ATOM 1968 N GLY A1070 5.396 238.190 24.449 1.00 52.44 N
ANISOU 1968 N GLY A1070 5425 5403 9098 709 1146 -183 N
ATOM 1969 CA GLY A1070 5.414 239.609 24.632 1.00 54.70 C
ANISOU 1969 CA GLY A1070 5805 5697 9282 727 1217 -298 C
ATOM 1970 C GLY A1070 4.281 240.273 23.886 1.00 50.54 C
ANISOU 1970 C GLY A1070 5450 5065 8687 773 1179 -288 C
ATOM 1971 O GLY A1070 3.618 241.097 24.439 1.00 51.44 O
ANISOU 1971 O GLY A1070 5553 5271 8721 828 1170 -287 O
ATOM 1972 N GLN A1071 4.051 239.888 22.651 1.00 46.28 N
ANISOU 1972 N GLN A1071 5067 4339 8177 756 1153 -276 N
ATOM 1973 CA GLN A1071 3.002 240.483 21.868 1.00 43.57 C
ANISOU 1973 CA GLN A1071 4895 3888 7771 799 1117 -269 C
ATOM 1974 C GLN A1071 1.591 240.123 22.297 1.00 41.52 C
ANISOU 1974 C GLN A1071 4537 3728 7513 868 984 -112 C
ATOM 1975 O GLN A1071 0.670 240.836 22.017 1.00 41.15 O
ANISOU 1975 O GLN A1071 4592 3649 7395 913 963 -103 O
ATOM 1976 CB GLN A1071 3.172 240.133 20.409 1.00 43.22 C
ANISOU 1976 CB GLN A1071 5051 3613 7759 770 1122 -301 C
ATOM 1977 CG GLN A1071 4.400 240.695 19.748 1.00 48.89 C
ANISOU 1977 CG GLN A1071 5917 4194 8465 720 1263 -452 C
ATOM 1978 CD GLN A1071 4.555 240.169 18.356 1.00 51.31 C
ANISOU 1978 CD GLN A1071 6407 4281 8808 708 1258 -461 C
ATOM 1979 OE1 GLN A1071 4.506 238.980 18.138 1.00 50.38 O
ANISOU 1979 OE1 GLN A1071 6237 4138 8767 697 1176 -372 O
ATOM 1980 NE2 GLN A1071 4.723 241.049 17.414 1.00 53.46 N
ANISOU 1980 NE2 GLN A1071 6894 4394 9024 717 1344 -567 N
ATOM 1981 N ILE A1072 1.434 238.979 22.929 1.00 41.31 N
ANISOU 1981 N ILE A1072 4310 3812 7574 877 898 17 N
ATOM 1982 CA ILE A1072 0.168 238.516 23.440 1.00 41.06 C
ANISOU 1982 CA ILE A1072 4150 3885 7568 946 771 184 C
ATOM 1983 C ILE A1072 -0.121 239.350 24.669 1.00 44.63 C
ANISOU 1983 C ILE A1072 4489 4531 7938 1007 799 193 C
ATOM 1984 O ILE A1072 -1.233 239.719 24.918 1.00 44.51 O
ANISOU 1984 O ILE A1072 4465 4569 7879 1076 740 279 O
ATOM 1985 CB ILE A1072 0.257 237.031 23.802 1.00 41.84 C
ANISOU 1985 CB ILE A1072 4053 4047 7796 937 688 312 C
ATOM 1986 CG1 ILE A1072 0.048 236.178 22.571 1.00 40.13 C
ANISOU 1986 CG1 ILE A1072 3954 3638 7656 905 614 348 C
ATOM 1987 CG2 ILE A1072 -0.727 236.654 24.878 1.00 44.03 C
ANISOU 1987 CG2 ILE A1072 4115 4511 8104 1018 593 481 C
ATOM 1988 CD1 ILE A1072 0.392 234.747 22.804 1.00 41.47 C
ANISOU 1988 CD1 ILE A1072 3956 3845 7954 879 555 443 C
ATOM 1989 N ASP A1073 0.930 239.644 25.405 1.00 48.69 N
ANISOU 1989 N ASP A1073 4923 5142 8432 981 890 100 N
ATOM 1990 CA ASP A1073 0.874 240.450 26.588 1.00 53.38 C
ANISOU 1990 CA ASP A1073 5419 5917 8946 1037 924 82 C
ATOM 1991 C ASP A1073 0.474 241.900 26.270 1.00 53.17 C
ANISOU 1991 C ASP A1073 5578 5832 8793 1060 980 -13 C
ATOM 1992 O ASP A1073 -0.263 242.509 27.001 1.00 55.02 O
ANISOU 1992 O ASP A1073 5767 6187 8951 1136 960 35 O
ATOM 1993 CB ASP A1073 2.232 240.427 27.268 1.00 60.41 C
ANISOU 1993 CB ASP A1073 6210 6891 9853 991 1010 -19 C
ATOM 1994 CG ASP A1073 2.413 239.247 28.173 1.00 68.18 C
ANISOU 1994 CG ASP A1073 6945 8032 10926 1009 958 97 C
ATOM 1995 OD1 ASP A1073 1.536 238.386 28.243 1.00 66.26 O
ANISOU 1995 OD1 ASP A1073 6604 7826 10747 1054 856 257 O
ATOM 1996 OD2 ASP A1073 3.457 239.196 28.829 1.00 76.69 O
ANISOU 1996 OD2 ASP A1073 7924 9199 12017 979 1021 27 O
ATOM 1997 N ASP A1074 0.994 242.440 25.182 1.00 51.54 N
ANISOU 1997 N ASP A1074 5580 5440 8564 998 1057 -147 N
ATOM 1998 CA ASP A1074 0.693 243.779 24.756 1.00 51.75 C
ANISOU 1998 CA ASP A1074 5791 5392 8479 1013 1122 -245 C
ATOM 1999 C ASP A1074 -0.784 243.851 24.449 1.00 49.51 C
ANISOU 1999 C ASP A1074 5560 5092 8158 1079 1033 -123 C
ATOM 2000 O ASP A1074 -1.443 244.798 24.793 1.00 50.79 O
ANISOU 2000 O ASP A1074 5763 5314 8221 1134 1046 -123 O
ATOM 2001 CB ASP A1074 1.435 244.105 23.473 1.00 52.02 C
ANISOU 2001 CB ASP A1074 6036 5207 8520 944 1210 -382 C
ATOM 2002 CG ASP A1074 2.880 244.303 23.667 1.00 58.71 C
ANISOU 2002 CG ASP A1074 6866 6046 9395 879 1315 -514 C
ATOM 2003 OD1 ASP A1074 3.370 244.150 24.772 1.00 63.06 O
ANISOU 2003 OD1 ASP A1074 7244 6757 9960 881 1318 -510 O
ATOM 2004 OD2 ASP A1074 3.531 244.621 22.696 1.00 60.55 O
ANISOU 2004 OD2 ASP A1074 7262 6108 9637 832 1397 -620 O
ATOM 2005 N ALA A1075 -1.276 242.842 23.753 1.00 46.92 N
ANISOU 2005 N ALA A1075 5239 4675 7913 1071 941 -21 N
ATOM 2006 CA ALA A1075 -2.653 242.781 23.366 1.00 46.44 C
ANISOU 2006 CA ALA A1075 5226 4580 7838 1126 844 103 C
ATOM 2007 C ALA A1075 -3.568 242.599 24.563 1.00 48.39 C
ANISOU 2007 C ALA A1075 5279 5028 8081 1211 763 265 C
ATOM 2008 O ALA A1075 -4.632 243.136 24.591 1.00 48.57 O
ANISOU 2008 O ALA A1075 5346 5071 8039 1272 728 337 O
ATOM 2009 CB ALA A1075 -2.867 241.684 22.358 1.00 44.61 C
ANISOU 2009 CB ALA A1075 5040 4199 7709 1096 757 167 C
ATOM 2010 N LEU A1076 -3.130 241.860 25.560 1.00 50.55 N
ANISOU 2010 N LEU A1076 5336 5452 8420 1221 741 325 N
ATOM 2011 CA LEU A1076 -3.937 241.625 26.737 1.00 54.33 C
ANISOU 2011 CA LEU A1076 5616 6125 8901 1316 670 487 C
ATOM 2012 C LEU A1076 -4.066 242.864 27.582 1.00 57.91 C
ANISOU 2012 C LEU A1076 6079 6705 9219 1378 736 438 C
ATOM 2013 O LEU A1076 -5.089 243.115 28.146 1.00 59.46 O
ANISOU 2013 O LEU A1076 6220 7001 9371 1469 687 563 O
ATOM 2014 CB LEU A1076 -3.365 240.493 27.570 1.00 57.19 C
ANISOU 2014 CB LEU A1076 5743 6616 9371 1316 639 558 C
ATOM 2015 CG LEU A1076 -4.029 239.158 27.351 1.00 58.88 C
ANISOU 2015 CG LEU A1076 5842 6808 9721 1328 514 734 C
ATOM 2016 CD1 LEU A1076 -3.187 238.098 28.001 1.00 62.39 C
ANISOU 2016 CD1 LEU A1076 6084 7353 10268 1306 514 761 C
ATOM 2017 CD2 LEU A1076 -5.407 239.163 27.959 1.00 62.29 C
ANISOU 2017 CD2 LEU A1076 6170 7348 10149 1439 423 924 C
ATOM 2018 N LYS A1077 -3.011 243.643 27.681 1.00 59.68 N
ANISOU 2018 N LYS A1077 6374 6922 9381 1332 848 258 N
ATOM 2019 CA LYS A1077 -3.095 244.846 28.453 1.00 63.78 C
ANISOU 2019 CA LYS A1077 6914 7550 9770 1389 907 198 C
ATOM 2020 C LYS A1077 -4.109 245.754 27.798 1.00 62.52 C
ANISOU 2020 C LYS A1077 6936 7302 9515 1419 911 209 C
ATOM 2021 O LYS A1077 -4.912 246.354 28.465 1.00 64.44 O
ANISOU 2021 O LYS A1077 7156 7656 9671 1507 896 283 O
ATOM 2022 CB LYS A1077 -1.760 245.549 28.548 1.00 68.28 C
ANISOU 2022 CB LYS A1077 7542 8100 10303 1324 1023 -7 C
ATOM 2023 CG LYS A1077 -1.782 246.648 29.571 1.00 77.20 C
ANISOU 2023 CG LYS A1077 8651 9369 11311 1392 1067 -59 C
ATOM 2024 CD LYS A1077 -0.633 247.614 29.434 1.00 85.82 C
ANISOU 2024 CD LYS A1077 9853 10399 12357 1325 1182 -275 C
ATOM 2025 CE LYS A1077 -1.098 249.046 29.592 1.00 92.42 C
ANISOU 2025 CE LYS A1077 10817 11246 13051 1374 1233 -343 C
ATOM 2026 NZ LYS A1077 -1.497 249.678 28.300 1.00 91.91 N
ANISOU 2026 NZ LYS A1077 10979 10992 12949 1334 1279 -397 N
ATOM 2027 N LEU A1078 -4.082 245.834 26.483 1.00 59.63 N
ANISOU 2027 N LEU A1078 6755 6738 9165 1352 931 141 N
ATOM 2028 CA LEU A1078 -5.017 246.681 25.796 1.00 59.39 C
ANISOU 2028 CA LEU A1078 6903 6618 9045 1379 940 146 C
ATOM 2029 C LEU A1078 -6.390 246.143 26.010 1.00 59.25 C
ANISOU 2029 C LEU A1078 6800 6661 9050 1456 819 361 C
ATOM 2030 O LEU A1078 -7.291 246.882 26.317 1.00 60.66 O
ANISOU 2030 O LEU A1078 7014 6900 9134 1527 816 424 O
ATOM 2031 CB LEU A1078 -4.721 246.755 24.314 1.00 58.06 C
ANISOU 2031 CB LEU A1078 6941 6222 8897 1303 980 40 C
ATOM 2032 CG LEU A1078 -3.554 247.603 23.865 1.00 61.58 C
ANISOU 2032 CG LEU A1078 7525 6570 9301 1237 1118 -173 C
ATOM 2033 CD1 LEU A1078 -3.548 247.568 22.363 1.00 61.77 C
ANISOU 2033 CD1 LEU A1078 7752 6372 9347 1191 1139 -233 C
ATOM 2034 CD2 LEU A1078 -3.625 249.027 24.368 1.00 65.10 C
ANISOU 2034 CD2 LEU A1078 8039 7084 9613 1273 1206 -261 C
ATOM 2035 N ALA A1079 -6.539 244.844 25.848 1.00 58.27 N
ANISOU 2035 N ALA A1079 6563 6518 9059 1443 719 477 N
ATOM 2036 CA ALA A1079 -7.824 244.196 26.038 1.00 60.12 C
ANISOU 2036 CA ALA A1079 6696 6800 9347 1514 593 695 C
ATOM 2037 C ALA A1079 -8.403 244.410 27.448 1.00 64.54 C
ANISOU 2037 C ALA A1079 7083 7580 9860 1626 571 828 C
ATOM 2038 O ALA A1079 -9.593 244.547 27.596 1.00 66.94 O
ANISOU 2038 O ALA A1079 7375 7921 10140 1702 510 981 O
ATOM 2039 CB ALA A1079 -7.737 242.730 25.699 1.00 59.26 C
ANISOU 2039 CB ALA A1079 6479 6636 9401 1478 493 786 C
ATOM 2040 N ASN A1080 -7.561 244.476 28.470 1.00 66.48 N
ANISOU 2040 N ASN A1080 7203 7968 10087 1641 625 770 N
ATOM 2041 CA ASN A1080 -7.997 244.717 29.833 1.00 71.80 C
ANISOU 2041 CA ASN A1080 7721 8853 10706 1759 613 880 C
ATOM 2042 C ASN A1080 -8.306 246.199 30.117 1.00 73.81 C
ANISOU 2042 C ASN A1080 8109 9149 10786 1810 690 810 C
ATOM 2043 O ASN A1080 -8.855 246.536 31.140 1.00 78.85 O
ANISOU 2043 O ASN A1080 8656 9946 11356 1922 679 912 O
ATOM 2044 CB ASN A1080 -6.975 244.165 30.815 1.00 75.97 C
ANISOU 2044 CB ASN A1080 8061 9519 11284 1762 635 845 C
ATOM 2045 CG ASN A1080 -7.068 242.669 30.964 1.00 79.89 C
ANISOU 2045 CG ASN A1080 8363 10048 11944 1766 541 994 C
ATOM 2046 OD1 ASN A1080 -8.097 242.081 30.727 1.00 81.12 O
ANISOU 2046 OD1 ASN A1080 8472 10178 12169 1806 446 1169 O
ATOM 2047 ND2 ASN A1080 -5.986 242.052 31.341 1.00 82.24 N
ANISOU 2047 ND2 ASN A1080 8544 10395 12307 1722 569 926 N
ATOM 2048 N GLU A1081 -7.937 247.064 29.195 1.00 70.60 N
ANISOU 2048 N GLU A1081 7920 8597 10310 1733 771 639 N
ATOM 2049 CA GLU A1081 -8.240 248.472 29.307 1.00 72.06 C
ANISOU 2049 CA GLU A1081 8249 8797 10335 1771 848 565 C
ATOM 2050 C GLU A1081 -9.496 248.777 28.501 1.00 71.06 C
ANISOU 2050 C GLU A1081 8256 8574 10170 1794 812 666 C
ATOM 2051 O GLU A1081 -9.861 249.921 28.358 1.00 72.35 O
ANISOU 2051 O GLU A1081 8565 8722 10204 1816 877 612 O
ATOM 2052 CB GLU A1081 -7.124 249.332 28.735 1.00 72.85 C
ANISOU 2052 CB GLU A1081 8512 8786 10383 1678 968 318 C
ATOM 2053 CG GLU A1081 -5.854 249.405 29.526 1.00 79.95 C
ANISOU 2053 CG GLU A1081 9317 9772 11287 1654 1023 187 C
ATOM 2054 CD GLU A1081 -4.778 250.139 28.768 1.00 86.82 C
ANISOU 2054 CD GLU A1081 10351 10498 12137 1552 1135 -42 C
ATOM 2055 OE1 GLU A1081 -4.593 249.870 27.578 1.00 84.43 O
ANISOU 2055 OE1 GLU A1081 10166 10020 11893 1473 1150 -90 O
ATOM 2056 OE2 GLU A1081 -4.126 250.997 29.349 1.00 93.97 O
ANISOU 2056 OE2 GLU A1081 11272 11462 12971 1556 1207 -170 O
ATOM 2057 N GLY A1082 -10.132 247.760 27.947 1.00 69.26 N
ANISOU 2057 N GLY A1082 7982 8277 10057 1785 710 807 N
ATOM 2058 CA GLY A1082 -11.319 247.942 27.158 1.00 69.29 C
ANISOU 2058 CA GLY A1082 8103 8185 10041 1803 662 909 C
ATOM 2059 C GLY A1082 -11.127 248.426 25.745 1.00 66.86 C
ANISOU 2059 C GLY A1082 8031 7670 9705 1715 717 761 C
ATOM 2060 O GLY A1082 -12.097 248.684 25.065 1.00 69.35 O
ANISOU 2060 O GLY A1082 8458 7903 9988 1732 686 831 O
ATOM 2061 N LYS A1083 -9.901 248.579 25.293 1.00 63.24 N
ANISOU 2061 N LYS A1083 7650 7124 9254 1629 801 561 N
ATOM 2062 CA LYS A1083 -9.698 249.037 23.945 1.00 62.37 C
ANISOU 2062 CA LYS A1083 7763 6815 9119 1560 861 424 C
ATOM 2063 C LYS A1083 -9.706 247.876 22.975 1.00 61.05 C
ANISOU 2063 C LYS A1083 7607 6502 9086 1508 771 464 C
ATOM 2064 O LYS A1083 -8.687 247.286 22.733 1.00 59.39 O
ANISOU 2064 O LYS A1083 7374 6236 8957 1443 788 374 O
ATOM 2065 CB LYS A1083 -8.405 249.816 23.856 1.00 63.86 C
ANISOU 2065 CB LYS A1083 8042 6965 9256 1500 999 198 C
ATOM 2066 CG LYS A1083 -8.196 250.787 24.990 1.00 69.07 C
ANISOU 2066 CG LYS A1083 8655 7784 9806 1549 1072 151 C
ATOM 2067 CD LYS A1083 -6.889 251.521 24.826 1.00 74.20 C
ANISOU 2067 CD LYS A1083 9391 8375 10425 1482 1201 -75 C
ATOM 2068 CE LYS A1083 -6.462 252.186 26.119 1.00 79.31 C
ANISOU 2068 CE LYS A1083 9944 9193 10999 1525 1246 -123 C
ATOM 2069 NZ LYS A1083 -5.269 253.025 25.892 1.00 83.53 N
ANISOU 2069 NZ LYS A1083 10577 9654 11506 1459 1371 -343 N
ATOM 2070 N VAL A1084 -10.855 247.572 22.394 1.00 62.43 N
ANISOU 2070 N VAL A1084 7826 6611 9285 1536 676 598 N
ATOM 2071 CA VAL A1084 -10.993 246.440 21.488 1.00 62.70 C
ANISOU 2071 CA VAL A1084 7870 6505 9449 1497 570 649 C
ATOM 2072 C VAL A1084 -10.290 246.529 20.164 1.00 62.23 C
ANISOU 2072 C VAL A1084 8010 6240 9394 1425 627 479 C
ATOM 2073 O VAL A1084 -9.621 245.612 19.773 1.00 60.68 O
ANISOU 2073 O VAL A1084 7787 5967 9303 1376 591 448 O
ATOM 2074 CB VAL A1084 -12.442 246.151 21.163 1.00 67.74 C
ANISOU 2074 CB VAL A1084 8513 7112 10113 1548 446 833 C
ATOM 2075 CG1 VAL A1084 -12.575 244.735 20.662 1.00 68.91 C
ANISOU 2075 CG1 VAL A1084 8586 7170 10427 1521 304 926 C
ATOM 2076 CG2 VAL A1084 -13.291 246.385 22.383 1.00 69.94 C
ANISOU 2076 CG2 VAL A1084 8637 7583 10353 1638 414 1004 C
ATOM 2077 N LYS A1085 -10.458 247.627 19.455 1.00 64.22 N
ANISOU 2077 N LYS A1085 8468 6403 9532 1426 718 375 N
ATOM 2078 CA LYS A1085 -9.817 247.776 18.169 1.00 65.71 C
ANISOU 2078 CA LYS A1085 8855 6393 9719 1375 783 218 C
ATOM 2079 C LYS A1085 -8.294 247.756 18.230 1.00 62.18 C
ANISOU 2079 C LYS A1085 8402 5924 9299 1314 887 55 C
ATOM 2080 O LYS A1085 -7.650 247.240 17.355 1.00 62.86 O
ANISOU 2080 O LYS A1085 8571 5865 9449 1272 892 -20 O
ATOM 2081 CB LYS A1085 -10.329 249.026 17.474 1.00 72.16 C
ANISOU 2081 CB LYS A1085 9882 7134 10404 1399 873 144 C
ATOM 2082 CG LYS A1085 -11.726 248.866 16.926 1.00 80.53 C
ANISOU 2082 CG LYS A1085 11000 8140 11458 1443 763 284 C
ATOM 2083 CD LYS A1085 -11.717 248.344 15.508 1.00 89.51 C
ANISOU 2083 CD LYS A1085 12295 9066 12650 1420 716 236 C
ATOM 2084 CE LYS A1085 -13.113 248.270 14.911 1.00 99.85 C
ANISOU 2084 CE LYS A1085 13676 10314 13950 1464 606 364 C
ATOM 2085 NZ LYS A1085 -14.142 247.755 15.849 1.00100.78 N
ANISOU 2085 NZ LYS A1085 13601 10573 14118 1504 474 583 N
ATOM 2086 N GLU A1086 -7.745 248.306 19.289 1.00 59.19 N
ANISOU 2086 N GLU A1086 7923 5692 8874 1316 965 9 N
ATOM 2087 CA GLU A1086 -6.322 248.351 19.462 1.00 57.78 C
ANISOU 2087 CA GLU A1086 7724 5506 8723 1260 1063 -137 C
ATOM 2088 C GLU A1086 -5.772 246.996 19.839 1.00 53.83 C
ANISOU 2088 C GLU A1086 7052 5045 8358 1228 980 -73 C
ATOM 2089 O GLU A1086 -4.699 246.647 19.427 1.00 53.56 O
ANISOU 2089 O GLU A1086 7046 4925 8380 1171 1030 -173 O
ATOM 2090 CB GLU A1086 -5.949 249.352 20.521 1.00 59.85 C
ANISOU 2090 CB GLU A1086 7928 5916 8897 1276 1157 -204 C
ATOM 2091 CG GLU A1086 -4.941 250.357 20.061 1.00 68.33 C
ANISOU 2091 CG GLU A1086 9148 6896 9919 1234 1313 -406 C
ATOM 2092 CD GLU A1086 -4.954 251.579 20.919 1.00 78.23 C
ANISOU 2092 CD GLU A1086 10393 8272 11060 1265 1396 -464 C
ATOM 2093 OE1 GLU A1086 -5.544 252.589 20.503 1.00 83.61 O
ANISOU 2093 OE1 GLU A1086 11221 8909 11638 1293 1455 -498 O
ATOM 2094 OE2 GLU A1086 -4.371 251.527 22.002 1.00 78.86 O
ANISOU 2094 OE2 GLU A1086 10323 8490 11151 1263 1401 -477 O
ATOM 2095 N ALA A1087 -6.517 246.247 20.634 1.00 51.18 N
ANISOU 2095 N ALA A1087 6533 4840 8072 1269 859 101 N
ATOM 2096 CA ALA A1087 -6.112 244.915 21.021 1.00 48.90 C
ANISOU 2096 CA ALA A1087 6067 4597 7915 1245 775 181 C
ATOM 2097 C ALA A1087 -6.116 244.031 19.785 1.00 48.45 C
ANISOU 2097 C ALA A1087 6111 4351 7948 1208 708 187 C
ATOM 2098 O ALA A1087 -5.235 243.248 19.595 1.00 46.71 O
ANISOU 2098 O ALA A1087 5853 4083 7812 1158 709 149 O
ATOM 2099 CB ALA A1087 -7.029 244.350 22.086 1.00 48.55 C
ANISOU 2099 CB ALA A1087 5810 4726 7909 1312 662 379 C
ATOM 2100 N GLN A1088 -7.096 244.207 18.929 1.00 50.55 N
ANISOU 2100 N GLN A1088 6515 4505 8187 1236 652 231 N
ATOM 2101 CA GLN A1088 -7.192 243.409 17.741 1.00 52.13 C
ANISOU 2101 CA GLN A1088 6823 4520 8463 1213 575 238 C
ATOM 2102 C GLN A1088 -6.097 243.681 16.750 1.00 53.71 C
ANISOU 2102 C GLN A1088 7207 4555 8645 1165 687 58 C
ATOM 2103 O GLN A1088 -5.689 242.790 16.046 1.00 54.51 O
ANISOU 2103 O GLN A1088 7347 4534 8829 1137 640 49 O
ATOM 2104 CB GLN A1088 -8.519 243.631 17.071 1.00 57.02 C
ANISOU 2104 CB GLN A1088 7554 5062 9051 1259 491 322 C
ATOM 2105 CG GLN A1088 -9.632 242.783 17.613 1.00 59.93 C
ANISOU 2105 CG GLN A1088 7750 5515 9505 1300 326 534 C
ATOM 2106 CD GLN A1088 -10.972 243.305 17.190 1.00 68.44 C
ANISOU 2106 CD GLN A1088 8925 6552 10525 1352 267 619 C
ATOM 2107 OE1 GLN A1088 -11.183 244.488 17.173 1.00 69.80 O
ANISOU 2107 OE1 GLN A1088 9208 6744 10569 1373 366 555 O
ATOM 2108 NE2 GLN A1088 -11.871 242.423 16.839 1.00 72.40 N
ANISOU 2108 NE2 GLN A1088 9386 6995 11126 1370 106 763 N
ATOM 2109 N ALA A1089 -5.650 244.918 16.671 1.00 54.75 N
ANISOU 2109 N ALA A1089 7456 4676 8668 1163 834 -80 N
ATOM 2110 CA ALA A1089 -4.604 245.269 15.756 1.00 57.78 C
ANISOU 2110 CA ALA A1089 8012 4904 9038 1127 953 -245 C
ATOM 2111 C ALA A1089 -3.256 244.818 16.277 1.00 55.60 C
ANISOU 2111 C ALA A1089 7624 4674 8829 1071 1014 -306 C
ATOM 2112 O ALA A1089 -2.350 244.580 15.528 1.00 58.08 O
ANISOU 2112 O ALA A1089 8036 4853 9179 1039 1072 -395 O
ATOM 2113 CB ALA A1089 -4.589 246.764 15.513 1.00 61.38 C
ANISOU 2113 CB ALA A1089 8622 5333 9368 1146 1094 -366 C
ATOM 2114 N ALA A1090 -3.132 244.726 17.581 1.00 51.73 N
ANISOU 2114 N ALA A1090 6927 4377 8350 1067 1003 -254 N
ATOM 2115 CA ALA A1090 -1.900 244.312 18.182 1.00 50.76 C
ANISOU 2115 CA ALA A1090 6681 4317 8288 1016 1056 -304 C
ATOM 2116 C ALA A1090 -1.731 242.818 18.089 1.00 49.19 C
ANISOU 2116 C ALA A1090 6377 4100 8214 992 950 -209 C
ATOM 2117 O ALA A1090 -0.637 242.332 18.051 1.00 49.12 O
ANISOU 2117 O ALA A1090 6338 4063 8264 942 999 -264 O
ATOM 2118 CB ALA A1090 -1.848 244.752 19.617 1.00 49.62 C
ANISOU 2118 CB ALA A1090 6358 4389 8107 1031 1078 -285 C
ATOM 2119 N ALA A1091 -2.856 242.125 18.066 1.00 48.51 N
ANISOU 2119 N ALA A1091 6233 4031 8169 1029 806 -60 N
ATOM 2120 CA ALA A1091 -2.924 240.695 17.949 1.00 47.94 C
ANISOU 2120 CA ALA A1091 6059 3936 8220 1014 685 48 C
ATOM 2121 C ALA A1091 -2.680 240.307 16.526 1.00 51.37 C
ANISOU 2121 C ALA A1091 6693 4144 8682 995 674 -9 C
ATOM 2122 O ALA A1091 -2.312 239.201 16.272 1.00 50.56 O
ANISOU 2122 O ALA A1091 6547 3989 8676 969 613 31 O
ATOM 2123 CB ALA A1091 -4.269 240.180 18.379 1.00 47.52 C
ANISOU 2123 CB ALA A1091 5881 3967 8206 1066 533 229 C
ATOM 2124 N GLU A1092 -2.878 241.233 15.605 1.00 55.96 N
ANISOU 2124 N GLU A1092 7497 4591 9176 1016 737 -103 N
ATOM 2125 CA GLU A1092 -2.659 240.956 14.197 1.00 61.08 C
ANISOU 2125 CA GLU A1092 8356 5015 9836 1016 734 -164 C
ATOM 2126 C GLU A1092 -1.164 240.884 13.914 1.00 62.01 C
ANISOU 2126 C GLU A1092 8525 5060 9975 969 860 -284 C
ATOM 2127 O GLU A1092 -0.726 240.211 13.022 1.00 63.90 O
ANISOU 2127 O GLU A1092 8869 5149 10262 962 843 -303 O
ATOM 2128 CB GLU A1092 -3.357 242.001 13.338 1.00 69.45 C
ANISOU 2128 CB GLU A1092 9630 5964 10793 1064 770 -224 C
ATOM 2129 CG GLU A1092 -3.583 241.626 11.899 1.00 81.98 C
ANISOU 2129 CG GLU A1092 11427 7331 12391 1091 717 -247 C
ATOM 2130 CD GLU A1092 -4.508 240.454 11.731 1.00 90.97 C
ANISOU 2130 CD GLU A1092 12502 8445 13619 1107 518 -102 C
ATOM 2131 OE1 GLU A1092 -5.163 240.058 12.697 1.00 88.52 O
ANISOU 2131 OE1 GLU A1092 11990 8288 13355 1105 423 28 O
ATOM 2132 OE2 GLU A1092 -4.566 239.920 10.621 1.00 99.12 O
ANISOU 2132 OE2 GLU A1092 13684 9298 14677 1126 456 -116 O
ATOM 2133 N GLN A1093 -0.368 241.551 14.724 1.00 61.33 N
ANISOU 2133 N GLN A1093 8358 5088 9858 939 982 -357 N
ATOM 2134 CA GLN A1093 1.069 241.544 14.556 1.00 63.79 C
ANISOU 2134 CA GLN A1093 8700 5341 10196 892 1107 -462 C
ATOM 2135 C GLN A1093 1.662 240.195 14.900 1.00 61.43 C
ANISOU 2135 C GLN A1093 8252 5082 10007 850 1046 -389 C
ATOM 2136 O GLN A1093 2.800 239.915 14.597 1.00 63.60 O
ANISOU 2136 O GLN A1093 8561 5284 10319 812 1127 -450 O
ATOM 2137 CB GLN A1093 1.705 242.588 15.447 1.00 65.93 C
ANISOU 2137 CB GLN A1093 8900 5734 10415 870 1236 -550 C
ATOM 2138 CG GLN A1093 1.054 243.936 15.354 1.00 71.54 C
ANISOU 2138 CG GLN A1093 9720 6446 11015 911 1293 -609 C
ATOM 2139 CD GLN A1093 1.192 244.523 13.988 1.00 81.52 C
ANISOU 2139 CD GLN A1093 11240 7498 12237 936 1374 -707 C
ATOM 2140 OE1 GLN A1093 2.278 244.554 13.438 1.00 86.71 O
ANISOU 2140 OE1 GLN A1093 11983 8040 12922 912 1476 -796 O
ATOM 2141 NE2 GLN A1093 0.092 244.976 13.427 1.00 83.76 N
ANISOU 2141 NE2 GLN A1093 11645 7727 12453 989 1332 -686 N
ATOM 2142 N LEU A1094 0.861 239.376 15.560 1.00 57.44 N
ANISOU 2142 N LEU A1094 7574 4695 9556 859 906 -250 N
ATOM 2143 CA LEU A1094 1.247 238.053 15.952 1.00 55.39 C
ANISOU 2143 CA LEU A1094 7153 4489 9404 825 836 -163 C
ATOM 2144 C LEU A1094 1.483 237.236 14.708 1.00 58.45 C
ANISOU 2144 C LEU A1094 7696 4672 9841 822 794 -166 C
ATOM 2145 O LEU A1094 2.325 236.383 14.700 1.00 58.21 O
ANISOU 2145 O LEU A1094 7613 4624 9880 782 806 -157 O
ATOM 2146 CB LEU A1094 0.181 237.411 16.810 1.00 52.20 C
ANISOU 2146 CB LEU A1094 6546 4238 9051 852 691 -4 C
ATOM 2147 CG LEU A1094 0.188 237.777 18.270 1.00 51.57 C
ANISOU 2147 CG LEU A1094 6250 4391 8952 857 722 28 C
ATOM 2148 CD1 LEU A1094 -1.102 237.313 18.862 1.00 50.63 C
ANISOU 2148 CD1 LEU A1094 5982 4384 8871 908 578 193 C
ATOM 2149 CD2 LEU A1094 1.357 237.187 19.010 1.00 51.97 C
ANISOU 2149 CD2 LEU A1094 6140 4544 9064 805 781 15 C
ATOM 2150 N LYS A1095 0.779 237.538 13.627 1.00 62.16 N
ANISOU 2150 N LYS A1095 8368 4981 10268 868 752 -186 N
ATOM 2151 CA LYS A1095 0.976 236.807 12.383 1.00 66.30 C
ANISOU 2151 CA LYS A1095 9064 5300 10829 879 707 -196 C
ATOM 2152 C LYS A1095 2.400 236.927 11.836 1.00 69.13 C
ANISOU 2152 C LYS A1095 9540 5547 11180 853 857 -308 C
ATOM 2153 O LYS A1095 2.933 236.003 11.286 1.00 70.42 O
ANISOU 2153 O LYS A1095 9749 5608 11401 843 832 -291 O
ATOM 2154 CB LYS A1095 -0.046 237.209 11.329 1.00 73.89 C
ANISOU 2154 CB LYS A1095 10229 6112 11735 943 640 -206 C
ATOM 2155 CG LYS A1095 -1.463 236.774 11.656 1.00 78.63 C
ANISOU 2155 CG LYS A1095 10724 6780 12372 970 462 -69 C
ATOM 2156 CD LYS A1095 -2.454 237.142 10.570 1.00 90.84 C
ANISOU 2156 CD LYS A1095 12478 8172 13866 1032 390 -79 C
ATOM 2157 CE LYS A1095 -3.826 236.517 10.819 1.00 96.31 C
ANISOU 2157 CE LYS A1095 13062 8911 14622 1055 194 73 C
ATOM 2158 NZ LYS A1095 -4.914 237.478 11.183 1.00100.82 N
ANISOU 2158 NZ LYS A1095 13620 9567 15119 1091 184 107 N
ATOM 2159 N THR A1096 3.024 238.057 12.036 1.00 70.47 N
ANISOU 2159 N THR A1096 9751 5741 11284 843 1012 -415 N
ATOM 2160 CA THR A1096 4.356 238.237 11.540 1.00 74.30 C
ANISOU 2160 CA THR A1096 10342 6119 11771 822 1158 -512 C
ATOM 2161 C THR A1096 5.315 237.360 12.290 1.00 70.31 C
ANISOU 2161 C THR A1096 9655 5713 11348 757 1175 -471 C
ATOM 2162 O THR A1096 6.221 236.834 11.716 1.00 73.44 O
ANISOU 2162 O THR A1096 10126 5996 11781 742 1226 -490 O
ATOM 2163 CB THR A1096 4.756 239.711 11.650 1.00 79.86 C
ANISOU 2163 CB THR A1096 11115 6832 12397 826 1317 -633 C
ATOM 2164 OG1 THR A1096 3.939 240.462 10.752 1.00 85.33 O
ANISOU 2164 OG1 THR A1096 12005 7404 13012 892 1314 -674 O
ATOM 2165 CG2 THR A1096 6.215 239.913 11.305 1.00 85.46 C
ANISOU 2165 CG2 THR A1096 11896 7449 13126 799 1476 -722 C
ATOM 2166 N THR A1097 5.103 237.205 13.577 1.00 64.56 N
ANISOU 2166 N THR A1097 8688 5196 10645 723 1135 -411 N
ATOM 2167 CA THR A1097 5.969 236.381 14.370 1.00 62.25 C
ANISOU 2167 CA THR A1097 8207 5016 10428 664 1152 -369 C
ATOM 2168 C THR A1097 5.764 234.927 14.041 1.00 59.76 C
ANISOU 2168 C THR A1097 7855 4655 10197 661 1027 -261 C
ATOM 2169 O THR A1097 6.687 234.174 14.029 1.00 60.44 O
ANISOU 2169 O THR A1097 7901 4723 10339 621 1064 -249 O
ATOM 2170 CB THR A1097 5.708 236.585 15.852 1.00 60.16 C
ANISOU 2170 CB THR A1097 7696 4997 10165 646 1134 -327 C
ATOM 2171 OG1 THR A1097 5.825 237.962 16.139 1.00 64.03 O
ANISOU 2171 OG1 THR A1097 8231 5524 10574 654 1238 -430 O
ATOM 2172 CG2 THR A1097 6.703 235.868 16.672 1.00 60.32 C
ANISOU 2172 CG2 THR A1097 7529 5136 10255 588 1173 -301 C
ATOM 2173 N ARG A1098 4.540 234.552 13.751 1.00 57.71 N
ANISOU 2173 N ARG A1098 7613 4368 9947 704 879 -182 N
ATOM 2174 CA ARG A1098 4.218 233.184 13.429 1.00 57.10 C
ANISOU 2174 CA ARG A1098 7499 4240 9957 705 741 -76 C
ATOM 2175 C ARG A1098 4.916 232.724 12.165 1.00 61.07 C
ANISOU 2175 C ARG A1098 8216 4522 10466 712 772 -122 C
ATOM 2176 O ARG A1098 5.424 231.643 12.099 1.00 60.39 O
ANISOU 2176 O ARG A1098 8079 4415 10451 685 741 -69 O
ATOM 2177 CB ARG A1098 2.720 233.037 13.292 1.00 57.54 C
ANISOU 2177 CB ARG A1098 7551 4291 10020 754 576 10 C
ATOM 2178 CG ARG A1098 2.280 231.663 12.906 1.00 60.41 C
ANISOU 2178 CG ARG A1098 7884 4588 10483 760 417 119 C
ATOM 2179 CD ARG A1098 0.855 231.690 12.438 1.00 65.37 C
ANISOU 2179 CD ARG A1098 8577 5150 11110 815 263 179 C
ATOM 2180 NE ARG A1098 0.678 232.541 11.281 1.00 72.35 N
ANISOU 2180 NE ARG A1098 9737 5853 11900 862 301 77 N
ATOM 2181 CZ ARG A1098 -0.498 232.904 10.807 1.00 77.78 C
ANISOU 2181 CZ ARG A1098 10518 6478 12557 914 202 100 C
ATOM 2182 NH1 ARG A1098 -1.601 232.491 11.380 1.00 76.29 N
ANISOU 2182 NH1 ARG A1098 10171 6386 12430 924 55 227 N
ATOM 2183 NH2 ARG A1098 -0.570 233.667 9.749 1.00 83.53 N
ANISOU 2183 NH2 ARG A1098 11496 7044 13198 959 250 1 N
ATOM 2184 N ASN A1099 4.951 233.571 11.166 1.00 65.86 N
ANISOU 2184 N ASN A1099 9063 4966 10995 756 838 -219 N
ATOM 2185 CA ASN A1099 5.588 233.222 9.928 1.00 71.69 C
ANISOU 2185 CA ASN A1099 10021 5488 11729 783 874 -262 C
ATOM 2186 C ASN A1099 7.086 233.127 10.046 1.00 73.83 C
ANISOU 2186 C ASN A1099 10279 5753 12019 737 1028 -307 C
ATOM 2187 O ASN A1099 7.683 232.164 9.637 1.00 75.29 O
ANISOU 2187 O ASN A1099 10496 5857 12252 727 1016 -270 O
ATOM 2188 CB ASN A1099 5.265 234.260 8.874 1.00 79.26 C
ANISOU 2188 CB ASN A1099 11236 6284 12596 854 924 -357 C
ATOM 2189 CG ASN A1099 3.795 234.379 8.610 1.00 83.20 C
ANISOU 2189 CG ASN A1099 11776 6766 13071 904 776 -315 C
ATOM 2190 OD1 ASN A1099 3.046 233.436 8.786 1.00 82.43 O
ANISOU 2190 OD1 ASN A1099 11580 6700 13038 902 611 -212 O
ATOM 2191 ND2 ASN A1099 3.378 235.542 8.178 1.00 87.46 N
ANISOU 2191 ND2 ASN A1099 12458 7252 13522 951 835 -393 N
ATOM 2192 N ALA A1100 7.683 234.136 10.637 1.00 74.79 N
ANISOU 2192 N ALA A1100 10351 5962 12104 708 1170 -382 N
ATOM 2193 CA ALA A1100 9.114 234.234 10.741 1.00 78.50 C
ANISOU 2193 CA ALA A1100 10816 6420 12592 665 1327 -432 C
ATOM 2194 C ALA A1100 9.830 233.405 11.774 1.00 76.10 C
ANISOU 2194 C ALA A1100 10276 6275 12362 588 1336 -368 C
ATOM 2195 O ALA A1100 11.021 233.236 11.682 1.00 80.20 O
ANISOU 2195 O ALA A1100 10809 6754 12907 555 1449 -391 O
ATOM 2196 CB ALA A1100 9.489 235.686 10.903 1.00 82.63 C
ANISOU 2196 CB ALA A1100 11385 6955 13053 666 1473 -543 C
ATOM 2197 N TYR A1101 9.138 232.920 12.786 1.00 70.46 N
ANISOU 2197 N TYR A1101 9341 5746 11685 564 1226 -287 N
ATOM 2198 CA TYR A1101 9.802 232.122 13.799 1.00 69.07 C
ANISOU 2198 CA TYR A1101 8932 5731 11579 498 1239 -225 C
ATOM 2199 C TYR A1101 9.070 230.833 14.171 1.00 64.55 C
ANISOU 2199 C TYR A1101 8204 5240 11081 495 1079 -93 C
ATOM 2200 O TYR A1101 9.588 229.758 14.008 1.00 64.70 O
ANISOU 2200 O TYR A1101 8193 5229 11162 469 1063 -36 O
ATOM 2201 CB TYR A1101 10.027 232.926 15.073 1.00 69.38 C
ANISOU 2201 CB TYR A1101 8786 5974 11599 464 1310 -264 C
ATOM 2202 CG TYR A1101 10.809 234.197 14.931 1.00 75.91 C
ANISOU 2202 CG TYR A1101 9720 6750 12371 456 1467 -391 C
ATOM 2203 CD1 TYR A1101 10.194 235.364 14.539 1.00 77.90 C
ANISOU 2203 CD1 TYR A1101 10111 6941 12547 503 1485 -466 C
ATOM 2204 CD2 TYR A1101 12.152 234.240 15.226 1.00 82.01 C
ANISOU 2204 CD2 TYR A1101 10444 7541 13173 401 1598 -431 C
ATOM 2205 CE1 TYR A1101 10.900 236.529 14.432 1.00 84.71 C
ANISOU 2205 CE1 TYR A1101 11060 7757 13370 497 1629 -580 C
ATOM 2206 CE2 TYR A1101 12.866 235.407 15.119 1.00 89.31 C
ANISOU 2206 CE2 TYR A1101 11455 8415 14063 393 1737 -543 C
ATOM 2207 CZ TYR A1101 12.234 236.546 14.725 1.00 91.29 C
ANISOU 2207 CZ TYR A1101 11841 8602 14243 442 1752 -618 C
ATOM 2208 OH TYR A1101 12.932 237.714 14.607 1.00100.82 O
ANISOU 2208 OH TYR A1101 13130 9754 15424 437 1891 -728 O
ATOM 2209 N ILE A1102 7.868 230.976 14.694 1.00 61.09 N
ANISOU 2209 N ILE A1102 7664 4908 10640 524 965 -42 N
ATOM 2210 CA ILE A1102 7.067 229.867 15.148 1.00 58.63 C
ANISOU 2210 CA ILE A1102 7183 4686 10409 528 811 91 C
ATOM 2211 C ILE A1102 6.822 228.729 14.185 1.00 59.00 C
ANISOU 2211 C ILE A1102 7332 4571 10513 544 699 155 C
ATOM 2212 O ILE A1102 6.795 227.600 14.597 1.00 58.27 O
ANISOU 2212 O ILE A1102 7082 4549 10509 521 626 255 O
ATOM 2213 CB ILE A1102 5.710 230.346 15.617 1.00 57.28 C
ANISOU 2213 CB ILE A1102 6937 4608 10218 574 706 137 C
ATOM 2214 CG1 ILE A1102 5.867 231.659 16.374 1.00 58.68 C
ANISOU 2214 CG1 ILE A1102 7071 4910 10316 573 815 55 C
ATOM 2215 CG2 ILE A1102 5.058 229.263 16.443 1.00 56.12 C
ANISOU 2215 CG2 ILE A1102 6545 4607 10170 573 576 284 C
ATOM 2216 CD1 ILE A1102 6.580 231.537 17.690 1.00 60.45 C
ANISOU 2216 CD1 ILE A1102 7053 5346 10567 530 885 70 C
ATOM 2217 N GLN A1103 6.649 229.026 12.908 1.00 60.94 N
ANISOU 2217 N GLN A1103 7843 4601 10711 588 687 97 N
ATOM 2218 CA GLN A1103 6.411 228.011 11.911 1.00 62.81 C
ANISOU 2218 CA GLN A1103 8206 4666 10992 614 575 145 C
ATOM 2219 C GLN A1103 7.702 227.291 11.594 1.00 64.14 C
ANISOU 2219 C GLN A1103 8417 4767 11188 578 665 138 C
ATOM 2220 O GLN A1103 7.692 226.153 11.200 1.00 64.30 O
ANISOU 2220 O GLN A1103 8446 4714 11270 578 576 207 O
ATOM 2221 CB GLN A1103 5.800 228.609 10.652 1.00 68.22 C
ANISOU 2221 CB GLN A1103 9169 5144 11607 686 534 81 C
ATOM 2222 CG GLN A1103 5.753 227.661 9.469 1.00 75.18 C
ANISOU 2222 CG GLN A1103 10230 5817 12517 723 436 105 C
ATOM 2223 CD GLN A1103 4.865 228.135 8.344 1.00 85.03 C
ANISOU 2223 CD GLN A1103 11718 6884 13707 804 353 61 C
ATOM 2224 OE1 GLN A1103 4.485 229.285 8.280 1.00 88.41 O
ANISOU 2224 OE1 GLN A1103 12219 7316 14058 832 405 -6 O
ATOM 2225 NE2 GLN A1103 4.533 227.243 7.455 1.00 89.42 N
ANISOU 2225 NE2 GLN A1103 12398 7280 14297 844 221 98 N
ATOM 2226 N LYS A1104 8.818 227.975 11.755 1.00 65.62 N
ANISOU 2226 N LYS A1104 8631 4971 11329 548 843 57 N
ATOM 2227 CA LYS A1104 10.092 227.367 11.535 1.00 68.36 C
ANISOU 2227 CA LYS A1104 9006 5267 11702 511 944 58 C
ATOM 2228 C LYS A1104 10.364 226.394 12.651 1.00 65.75 C
ANISOU 2228 C LYS A1104 8397 5128 11456 446 921 153 C
ATOM 2229 O LYS A1104 10.954 225.372 12.432 1.00 66.40 O
ANISOU 2229 O LYS A1104 8473 5169 11588 423 921 207 O
ATOM 2230 CB LYS A1104 11.184 228.407 11.490 1.00 74.06 C
ANISOU 2230 CB LYS A1104 9810 5965 12366 495 1138 -46 C
ATOM 2231 CG LYS A1104 11.505 228.882 10.106 1.00 84.08 C
ANISOU 2231 CG LYS A1104 11384 6988 13573 558 1202 -120 C
ATOM 2232 CD LYS A1104 12.049 230.292 10.158 1.00 92.89 C
ANISOU 2232 CD LYS A1104 12567 8099 14628 560 1362 -230 C
ATOM 2233 CE LYS A1104 11.952 230.968 8.811 1.00102.46 C
ANISOU 2233 CE LYS A1104 14077 9081 15772 646 1401 -304 C
ATOM 2234 NZ LYS A1104 11.011 232.104 8.856 1.00104.19 N
ANISOU 2234 NZ LYS A1104 14333 9324 15929 682 1380 -368 N
ATOM 2235 N TYR A1105 9.889 226.748 13.894 1.00 47.57 N
ANISOU 2235 N TYR A1105 5860 3047 9167 424 903 177 N
ATOM 2236 CA TYR A1105 10.077 225.841 15.022 1.00 47.24 C
ANISOU 2236 CA TYR A1105 5538 3203 9207 376 882 272 C
ATOM 2237 C TYR A1105 9.183 224.614 14.887 1.00 47.42 C
ANISOU 2237 C TYR A1105 5490 3213 9317 395 706 392 C
ATOM 2238 O TYR A1105 9.633 223.483 15.091 1.00 47.77 O
ANISOU 2238 O TYR A1105 5424 3292 9434 360 693 468 O
ATOM 2239 CB TYR A1105 9.804 226.552 16.348 1.00 47.49 C
ANISOU 2239 CB TYR A1105 5351 3466 9225 365 910 266 C
ATOM 2240 CG TYR A1105 9.826 225.605 17.534 1.00 57.08 C
ANISOU 2240 CG TYR A1105 6268 4895 10526 334 874 374 C
ATOM 2241 CD1 TYR A1105 10.986 224.920 17.878 1.00 97.79 C
ANISOU 2241 CD1 TYR A1105 11327 10108 15721 276 968 392 C
ATOM 2242 CD2 TYR A1105 8.684 225.380 18.299 1.00 84.14 C
ANISOU 2242 CD2 TYR A1105 9509 8463 13996 369 751 466 C
ATOM 2243 CE1 TYR A1105 11.015 224.041 18.952 1.00 61.96 C
ANISOU 2243 CE1 TYR A1105 6513 5767 11260 253 943 491 C
ATOM 2244 CE2 TYR A1105 8.704 224.505 19.381 1.00 78.05 C
ANISOU 2244 CE2 TYR A1105 8460 7888 13307 353 726 570 C
ATOM 2245 CZ TYR A1105 9.874 223.841 19.703 1.00 68.04 C
ANISOU 2245 CZ TYR A1105 7100 6678 12074 295 823 578 C
ATOM 2246 OH TYR A1105 9.910 222.970 20.773 1.00 87.36 O
ANISOU 2246 OH TYR A1105 9268 9322 14601 284 807 681 O
ATOM 2247 N LEU A1106 7.909 224.824 14.546 1.00 52.20 N
ANISOU 2247 N LEU A1106 6152 3763 9918 449 568 414 N
ATOM 2248 CA LEU A1106 6.988 223.711 14.341 1.00 49.93 C
ANISOU 2248 CA LEU A1106 5808 3440 9722 472 386 528 C
ATOM 2249 C LEU A1106 7.539 222.714 13.326 1.00 48.93 C
ANISOU 2249 C LEU A1106 5835 3130 9627 467 362 540 C
ATOM 2250 O LEU A1106 7.552 221.501 13.567 1.00 49.37 O
ANISOU 2250 O LEU A1106 5757 3223 9779 444 290 639 O
ATOM 2251 CB LEU A1106 5.625 224.243 13.883 1.00 49.68 C
ANISOU 2251 CB LEU A1106 5875 3331 9669 534 253 530 C
ATOM 2252 CG LEU A1106 4.706 223.220 13.202 1.00 99.97 C
ANISOU 2252 CG LEU A1106 12288 9575 16123 567 56 619 C
ATOM 2253 CD1 LEU A1106 3.984 222.348 14.224 1.00 62.75 C
ANISOU 2253 CD1 LEU A1106 7277 5032 11533 558 -61 765 C
ATOM 2254 CD2 LEU A1106 3.715 223.892 12.253 1.00 53.75 C
ANISOU 2254 CD2 LEU A1106 6651 3558 10213 631 -38 575 C
ATOM 2255 N GLU A 219 8.007 223.217 12.183 1.00 55.58 N
ANISOU 2255 N GLU A 219 7351 6628 7141 9 333 118 N
ATOM 2256 CA GLU A 219 8.510 222.331 11.136 1.00 50.49 C
ANISOU 2256 CA GLU A 219 6729 6010 6446 24 273 123 C
ATOM 2257 C GLU A 219 9.805 221.633 11.532 1.00 47.89 C
ANISOU 2257 C GLU A 219 6412 5726 6057 -4 283 92 C
ATOM 2258 O GLU A 219 10.050 220.496 11.115 1.00 46.05 O
ANISOU 2258 O GLU A 219 6182 5521 5795 2 233 89 O
ATOM 2259 CB GLU A 219 8.722 223.116 9.840 1.00 35.32 C
ANISOU 2259 CB GLU A 219 4847 4071 4504 48 264 147 C
ATOM 2260 CG GLU A 219 7.438 223.638 9.213 1.00 35.74 C
ANISOU 2260 CG GLU A 219 4888 4082 4608 82 238 184 C
ATOM 2261 CD GLU A 219 7.695 224.471 7.972 1.00 36.02 C
ANISOU 2261 CD GLU A 219 4965 4100 4621 105 233 209 C
ATOM 2262 OE1 GLU A 219 8.870 224.801 7.708 1.00 35.90 O
ANISOU 2262 OE1 GLU A 219 4987 4100 4554 92 262 194 O
ATOM 2263 OE2 GLU A 219 6.721 224.799 7.262 1.00 36.38 O
ANISOU 2263 OE2 GLU A 219 5006 4117 4700 137 201 242 O
ATOM 2264 N ARG A 220 11.062 222.441 12.026 1.00 80.14 N
ANISOU 2264 N ARG A 220 10520 9824 10105 -35 351 67 N
ATOM 2265 CA ARG A 220 12.018 221.693 12.810 1.00 78.67 C
ANISOU 2265 CA ARG A 220 10328 9680 9881 -65 363 36 C
ATOM 2266 C ARG A 220 11.637 220.653 13.824 1.00 76.86 C
ANISOU 2266 C ARG A 220 10062 9470 9670 -79 348 22 C
ATOM 2267 O ARG A 220 12.160 219.588 13.778 1.00 76.28 O
ANISOU 2267 O ARG A 220 9989 9431 9563 -82 317 12 O
ATOM 2268 CB ARG A 220 12.997 222.650 13.429 1.00 80.96 C
ANISOU 2268 CB ARG A 220 10634 9978 10150 -96 434 13 C
ATOM 2269 CG ARG A 220 13.934 223.246 12.415 1.00 86.45 C
ANISOU 2269 CG ARG A 220 11373 10674 10801 -90 443 15 C
ATOM 2270 CD ARG A 220 14.850 224.272 13.052 1.00 91.69 C
ANISOU 2270 CD ARG A 220 12048 11342 11446 -122 518 -10 C
ATOM 2271 NE ARG A 220 15.639 225.001 12.059 1.00 96.38 N
ANISOU 2271 NE ARG A 220 12686 11929 12005 -114 534 -7 N
ATOM 2272 CZ ARG A 220 16.827 225.528 12.308 1.00 98.56 C
ANISOU 2272 CZ ARG A 220 12982 12223 12243 -140 584 -34 C
ATOM 2273 NH1 ARG A 220 17.349 225.418 13.516 1.00 97.44 N
ANISOU 2273 NH1 ARG A 220 12820 12109 12094 -177 621 -63 N
ATOM 2274 NH2 ARG A 220 17.484 226.158 11.355 1.00 99.24 N
ANISOU 2274 NH2 ARG A 220 13108 12299 12299 -131 596 -31 N
ATOM 2275 N ALA A 221 10.772 220.942 14.764 1.00 75.88 N
ANISOU 2275 N ALA A 221 9907 9325 9597 -87 374 21 N
ATOM 2276 CA ALA A 221 10.441 219.931 15.744 1.00 74.33 C
ANISOU 2276 CA ALA A 221 9679 9147 9415 -101 362 7 C
ATOM 2277 C ALA A 221 9.816 218.712 15.120 1.00 73.75 C
ANISOU 2277 C ALA A 221 9594 9080 9349 -74 291 21 C
ATOM 2278 O ALA A 221 10.036 217.619 15.570 1.00 72.86 O
ANISOU 2278 O ALA A 221 9468 8996 9220 -83 271 8 O
ATOM 2279 CB ALA A 221 9.535 220.479 16.808 1.00 74.97 C
ANISOU 2279 CB ALA A 221 9731 9199 9555 -114 403 4 C
ATOM 2280 N ARG A 222 9.028 218.913 14.085 1.00 74.19 N
ANISOU 2280 N ARG A 222 9654 9107 9427 -41 254 49 N
ATOM 2281 CA ARG A 222 8.364 217.838 13.425 1.00 74.12 C
ANISOU 2281 CA ARG A 222 9635 9102 9426 -16 187 62 C
ATOM 2282 C ARG A 222 9.362 216.974 12.707 1.00 72.10 C
ANISOU 2282 C ARG A 222 9403 8882 9108 -15 153 56 C
ATOM 2283 O ARG A 222 9.260 215.778 12.708 1.00 71.42 O
ANISOU 2283 O ARG A 222 9305 8817 9014 -12 115 51 O
ATOM 2284 CB ARG A 222 7.381 218.396 12.441 1.00 77.95 C
ANISOU 2284 CB ARG A 222 10122 9549 9945 17 158 94 C
ATOM 2285 CG ARG A 222 6.509 217.368 11.788 1.00 83.28 C
ANISOU 2285 CG ARG A 222 10781 10224 10637 43 88 108 C
ATOM 2286 CD ARG A 222 5.740 217.994 10.652 1.00 90.14 C
ANISOU 2286 CD ARG A 222 11659 11061 11528 75 57 141 C
ATOM 2287 NE ARG A 222 4.650 218.829 11.134 1.00 96.28 N
ANISOU 2287 NE ARG A 222 12410 11798 12373 82 81 155 N
ATOM 2288 CZ ARG A 222 4.206 219.919 10.516 1.00101.52 C
ANISOU 2288 CZ ARG A 222 13084 12429 13061 102 88 181 C
ATOM 2289 NH1 ARG A 222 4.760 220.334 9.388 1.00101.56 N
ANISOU 2289 NH1 ARG A 222 13127 12437 13025 116 72 196 N
ATOM 2290 NH2 ARG A 222 3.205 220.599 11.039 1.00103.51 N
ANISOU 2290 NH2 ARG A 222 13307 12643 13379 108 112 192 N
ATOM 2291 N SER A 223 10.338 217.612 12.099 1.00 70.97 N
ANISOU 2291 N SER A 223 9297 8746 8923 -18 171 55 N
ATOM 2292 CA SER A 223 11.366 216.941 11.360 1.00 69.29 C
ANISOU 2292 CA SER A 223 9112 8564 8652 -19 146 49 C
ATOM 2293 C SER A 223 12.200 216.069 12.263 1.00 66.81 C
ANISOU 2293 C SER A 223 8786 8289 8309 -45 159 23 C
ATOM 2294 O SER A 223 12.590 214.995 11.895 1.00 65.99 O
ANISOU 2294 O SER A 223 8686 8210 8176 -42 123 19 O
ATOM 2295 CB SER A 223 12.245 217.975 10.732 1.00 70.93 C
ANISOU 2295 CB SER A 223 9359 8766 8825 -21 176 50 C
ATOM 2296 OG SER A 223 13.047 217.426 9.744 1.00 73.58 O
ANISOU 2296 OG SER A 223 9725 9121 9110 -15 145 51 O
ATOM 2297 N THR A 224 12.476 216.549 13.453 1.00 65.52 N
ANISOU 2297 N THR A 224 8609 8131 8154 -72 212 4 N
ATOM 2298 CA THR A 224 13.268 215.791 14.381 1.00 64.07 C
ANISOU 2298 CA THR A 224 8413 7986 7944 -98 226 -20 C
ATOM 2299 C THR A 224 12.538 214.554 14.861 1.00 63.55 C
ANISOU 2299 C THR A 224 8315 7928 7901 -93 191 -20 C
ATOM 2300 O THR A 224 13.134 213.550 15.075 1.00 62.46 O
ANISOU 2300 O THR A 224 8174 7823 7735 -101 176 -31 O
ATOM 2301 CB THR A 224 13.657 216.651 15.568 1.00 64.76 C
ANISOU 2301 CB THR A 224 8494 8077 8037 -130 291 -39 C
ATOM 2302 OG1 THR A 224 14.476 217.701 15.110 1.00 66.44 O
ANISOU 2302 OG1 THR A 224 8736 8285 8221 -136 325 -42 O
ATOM 2303 CG2 THR A 224 14.420 215.879 16.536 1.00 63.76 C
ANISOU 2303 CG2 THR A 224 8354 7990 7884 -156 303 -61 C
ATOM 2304 N LEU A 225 11.234 214.657 15.038 1.00 64.30 N
ANISOU 2304 N LEU A 225 8388 7993 8052 -79 180 -8 N
ATOM 2305 CA LEU A 225 10.437 213.552 15.490 1.00 64.42 C
ANISOU 2305 CA LEU A 225 8372 8011 8095 -73 150 -9 C
ATOM 2306 C LEU A 225 10.270 212.527 14.396 1.00 64.38 C
ANISOU 2306 C LEU A 225 8373 8014 8074 -48 88 3 C
ATOM 2307 O LEU A 225 10.039 211.379 14.669 1.00 64.15 O
ANISOU 2307 O LEU A 225 8326 8001 8049 -47 63 -2 O
ATOM 2308 CB LEU A 225 9.063 214.009 15.932 1.00 66.04 C
ANISOU 2308 CB LEU A 225 8549 8176 8365 -65 157 0 C
ATOM 2309 CG LEU A 225 8.889 214.636 17.296 1.00 68.58 C
ANISOU 2309 CG LEU A 225 8853 8488 8716 -91 214 -14 C
ATOM 2310 CD1 LEU A 225 7.529 215.287 17.357 1.00 70.78 C
ANISOU 2310 CD1 LEU A 225 9112 8720 9062 -77 218 0 C
ATOM 2311 CD2 LEU A 225 9.009 213.591 18.370 1.00 68.50 C
ANISOU 2311 CD2 LEU A 225 8821 8504 8701 -110 217 -34 C
ATOM 2312 N GLN A 226 10.356 212.955 13.157 1.00 64.43 N
ANISOU 2312 N GLN A 226 8407 8009 8065 -30 65 20 N
ATOM 2313 CA GLN A 226 10.204 212.048 12.053 1.00 64.69 C
ANISOU 2313 CA GLN A 226 8449 8049 8081 -8 8 32 C
ATOM 2314 C GLN A 226 11.516 211.309 11.887 1.00 62.16 C
ANISOU 2314 C GLN A 226 8148 7766 7703 -22 6 17 C
ATOM 2315 O GLN A 226 11.539 210.170 11.515 1.00 61.30 O
ANISOU 2315 O GLN A 226 8036 7674 7580 -15 -30 17 O
ATOM 2316 CB GLN A 226 9.828 212.814 10.799 1.00 68.91 C
ANISOU 2316 CB GLN A 226 9008 8557 8619 15 -15 55 C
ATOM 2317 CG GLN A 226 9.293 211.984 9.656 1.00 75.90 C
ANISOU 2317 CG GLN A 226 9898 9442 9500 39 -79 71 C
ATOM 2318 CD GLN A 226 9.130 212.796 8.376 1.00 85.06 C
ANISOU 2318 CD GLN A 226 11088 10580 10651 59 -99 95 C
ATOM 2319 OE1 GLN A 226 8.998 214.022 8.423 1.00 88.76 O
ANISOU 2319 OE1 GLN A 226 11565 11024 11137 62 -69 104 O
ATOM 2320 NE2 GLN A 226 9.130 212.119 7.232 1.00 85.59 N
ANISOU 2320 NE2 GLN A 226 11174 10654 10692 73 -149 105 N
ATOM 2321 N LYS A 227 12.608 211.971 12.218 1.00 60.72 N
ANISOU 2321 N LYS A 227 7984 7598 7490 -42 50 5 N
ATOM 2322 CA LYS A 227 13.913 211.365 12.138 1.00 59.14 C
ANISOU 2322 CA LYS A 227 7800 7433 7237 -56 54 -9 C
ATOM 2323 C LYS A 227 14.031 210.285 13.187 1.00 57.49 C
ANISOU 2323 C LYS A 227 7562 7252 7030 -70 56 -24 C
ATOM 2324 O LYS A 227 14.646 209.280 12.943 1.00 57.15 O
ANISOU 2324 O LYS A 227 7523 7235 6957 -72 36 -29 O
ATOM 2325 CB LYS A 227 15.005 212.388 12.361 1.00 60.32 C
ANISOU 2325 CB LYS A 227 7971 7590 7357 -76 103 -21 C
ATOM 2326 CG LYS A 227 15.644 212.917 11.106 1.00 65.33 C
ANISOU 2326 CG LYS A 227 8648 8218 7957 -67 97 -13 C
ATOM 2327 CD LYS A 227 16.421 214.179 11.399 1.00 70.50 C
ANISOU 2327 CD LYS A 227 9320 8869 8597 -85 152 -24 C
ATOM 2328 CE LYS A 227 16.962 214.842 10.142 1.00 75.31 C
ANISOU 2328 CE LYS A 227 9973 9464 9176 -74 150 -16 C
ATOM 2329 NZ LYS A 227 15.931 215.119 9.106 1.00 79.14 N
ANISOU 2329 NZ LYS A 227 10470 9916 9684 -45 113 11 N
ATOM 2330 N GLU A 228 13.421 210.521 14.340 1.00 56.39 N
ANISOU 2330 N GLU A 228 7394 7104 6927 -81 81 -31 N
ATOM 2331 CA GLU A 228 13.429 209.595 15.457 1.00 55.24 C
ANISOU 2331 CA GLU A 228 7221 6982 6787 -95 88 -44 C
ATOM 2332 C GLU A 228 12.559 208.385 15.222 1.00 54.72 C
ANISOU 2332 C GLU A 228 7135 6912 6743 -76 42 -37 C
ATOM 2333 O GLU A 228 12.870 207.324 15.667 1.00 54.66 O
ANISOU 2333 O GLU A 228 7115 6930 6722 -82 35 -45 O
ATOM 2334 CB GLU A 228 12.988 210.279 16.735 1.00 57.23 C
ANISOU 2334 CB GLU A 228 7451 7222 7072 -113 131 -53 C
ATOM 2335 CG GLU A 228 14.070 211.052 17.414 1.00 61.35 C
ANISOU 2335 CG GLU A 228 7984 7763 7564 -142 182 -69 C
ATOM 2336 CD GLU A 228 13.598 211.674 18.683 1.00 67.57 C
ANISOU 2336 CD GLU A 228 8751 8539 8383 -163 225 -80 C
ATOM 2337 OE1 GLU A 228 12.948 212.704 18.628 1.00 69.85 O
ANISOU 2337 OE1 GLU A 228 9041 8794 8705 -160 245 -73 O
ATOM 2338 OE2 GLU A 228 13.878 211.131 19.739 1.00 69.88 O
ANISOU 2338 OE2 GLU A 228 9027 8856 8670 -183 240 -93 O
ATOM 2339 N VAL A 229 11.451 208.572 14.540 1.00 54.37 N
ANISOU 2339 N VAL A 229 7088 6837 6734 -53 13 -21 N
ATOM 2340 CA VAL A 229 10.563 207.487 14.222 1.00 53.92 C
ANISOU 2340 CA VAL A 229 7013 6776 6700 -35 -31 -15 C
ATOM 2341 C VAL A 229 11.215 206.575 13.188 1.00 52.82 C
ANISOU 2341 C VAL A 229 6893 6657 6518 -27 -67 -12 C
ATOM 2342 O VAL A 229 11.112 205.394 13.264 1.00 51.77 O
ANISOU 2342 O VAL A 229 6748 6540 6383 -24 -88 -17 O
ATOM 2343 CB VAL A 229 9.214 208.010 13.728 1.00 55.36 C
ANISOU 2343 CB VAL A 229 7185 6919 6931 -14 -53 1 C
ATOM 2344 CG1 VAL A 229 8.463 206.965 12.948 1.00 55.45 C
ANISOU 2344 CG1 VAL A 229 7188 6928 6954 7 -108 10 C
ATOM 2345 CG2 VAL A 229 8.387 208.453 14.896 1.00 56.07 C
ANISOU 2345 CG2 VAL A 229 7246 6988 7072 -22 -23 -4 C
ATOM 2346 N HIS A 230 11.911 207.165 12.240 1.00 52.95 N
ANISOU 2346 N HIS A 230 6944 6674 6501 -24 -69 -5 N
ATOM 2347 CA HIS A 230 12.588 206.435 11.205 1.00 53.30 C
ANISOU 2347 CA HIS A 230 7012 6736 6504 -19 -98 -3 C
ATOM 2348 C HIS A 230 13.729 205.623 11.804 1.00 50.88 C
ANISOU 2348 C HIS A 230 6703 6465 6162 -37 -80 -19 C
ATOM 2349 O HIS A 230 13.906 204.489 11.469 1.00 50.01 O
ANISOU 2349 O HIS A 230 6592 6371 6038 -34 -104 -20 O
ATOM 2350 CB HIS A 230 13.105 207.406 10.150 1.00 56.37 C
ANISOU 2350 CB HIS A 230 7440 7113 6866 -15 -98 7 C
ATOM 2351 CG HIS A 230 13.550 206.756 8.881 1.00 62.38 C
ANISOU 2351 CG HIS A 230 8228 7882 7590 -6 -133 13 C
ATOM 2352 ND1 HIS A 230 14.867 206.477 8.610 1.00 64.81 N
ANISOU 2352 ND1 HIS A 230 8561 8214 7851 -19 -120 3 N
ATOM 2353 CD2 HIS A 230 12.855 206.351 7.800 1.00 65.14 C
ANISOU 2353 CD2 HIS A 230 8587 8220 7945 12 -180 27 C
ATOM 2354 CE1 HIS A 230 14.966 205.922 7.421 1.00 65.79 C
ANISOU 2354 CE1 HIS A 230 8708 8338 7952 -10 -156 11 C
ATOM 2355 NE2 HIS A 230 13.758 205.835 6.907 1.00 66.50 N
ANISOU 2355 NE2 HIS A 230 8789 8407 8071 9 -193 25 N
ATOM 2356 N ALA A 231 14.485 206.231 12.697 1.00 49.23 N
ANISOU 2356 N ALA A 231 6494 6270 5942 -58 -36 -31 N
ATOM 2357 CA ALA A 231 15.592 205.555 13.325 1.00 48.17 C
ANISOU 2357 CA ALA A 231 6355 6171 5776 -76 -17 -44 C
ATOM 2358 C ALA A 231 15.114 204.431 14.236 1.00 47.39 C
ANISOU 2358 C ALA A 231 6223 6085 5698 -77 -23 -50 C
ATOM 2359 O ALA A 231 15.818 203.481 14.458 1.00 46.32 O
ANISOU 2359 O ALA A 231 6083 5976 5539 -83 -24 -56 O
ATOM 2360 CB ALA A 231 16.445 206.532 14.095 1.00 47.92 C
ANISOU 2360 CB ALA A 231 6329 6150 5728 -98 31 -56 C
ATOM 2361 N ALA A 232 13.907 204.574 14.766 1.00 47.19 N
ANISOU 2361 N ALA A 232 6174 6036 5718 -70 -25 -47 N
ATOM 2362 CA ALA A 232 13.328 203.585 15.644 1.00 46.07 C
ANISOU 2362 CA ALA A 232 6001 5901 5601 -71 -29 -53 C
ATOM 2363 C ALA A 232 12.788 202.435 14.835 1.00 45.83 C
ANISOU 2363 C ALA A 232 5967 5868 5577 -51 -73 -46 C
ATOM 2364 O ALA A 232 12.800 201.327 15.284 1.00 45.41 O
ANISOU 2364 O ALA A 232 5897 5831 5524 -52 -78 -52 O
ATOM 2365 CB ALA A 232 12.263 204.185 16.515 1.00 46.58 C
ANISOU 2365 CB ALA A 232 6044 5941 5714 -73 -12 -55 C
ATOM 2366 N LYS A 233 12.332 202.715 13.631 1.00 45.99 N
ANISOU 2366 N LYS A 233 6004 5868 5600 -35 -104 -34 N
ATOM 2367 CA LYS A 233 11.861 201.689 12.741 1.00 46.14 C
ANISOU 2367 CA LYS A 233 6023 5887 5622 -18 -147 -29 C
ATOM 2368 C LYS A 233 13.029 200.865 12.266 1.00 44.64 C
ANISOU 2368 C LYS A 233 5851 5725 5385 -24 -151 -32 C
ATOM 2369 O LYS A 233 12.917 199.695 12.140 1.00 44.81 O
ANISOU 2369 O LYS A 233 5863 5757 5406 -20 -168 -34 O
ATOM 2370 CB LYS A 233 11.143 202.270 11.547 1.00 50.11 C
ANISOU 2370 CB LYS A 233 6541 6362 6135 -1 -179 -14 C
ATOM 2371 CG LYS A 233 9.702 202.592 11.833 1.00 56.62 C
ANISOU 2371 CG LYS A 233 7341 7158 7016 11 -191 -9 C
ATOM 2372 CD LYS A 233 8.896 202.882 10.583 1.00 62.21 C
ANISOU 2372 CD LYS A 233 8059 7842 7735 31 -233 7 C
ATOM 2373 CE LYS A 233 7.588 203.563 10.939 1.00 67.24 C
ANISOU 2373 CE LYS A 233 8672 8448 8430 42 -235 14 C
ATOM 2374 NZ LYS A 233 7.169 204.524 9.888 1.00 71.04 N
ANISOU 2374 NZ LYS A 233 9171 8905 8915 58 -258 34 N
ATOM 2375 N SER A 234 14.149 201.500 12.018 1.00 43.28 N
ANISOU 2375 N SER A 234 5705 5564 5176 -35 -131 -33 N
ATOM 2376 CA SER A 234 15.319 200.801 11.573 1.00 42.67 C
ANISOU 2376 CA SER A 234 5645 5512 5056 -42 -131 -37 C
ATOM 2377 C SER A 234 15.822 199.838 12.632 1.00 41.92 C
ANISOU 2377 C SER A 234 5526 5444 4956 -53 -112 -46 C
ATOM 2378 O SER A 234 16.215 198.755 12.306 1.00 42.63 O
ANISOU 2378 O SER A 234 5617 5550 5031 -51 -124 -47 O
ATOM 2379 CB SER A 234 16.388 201.777 11.166 1.00 43.25 C
ANISOU 2379 CB SER A 234 5749 5589 5095 -52 -111 -37 C
ATOM 2380 OG SER A 234 15.929 202.516 10.088 1.00 46.09 O
ANISOU 2380 OG SER A 234 6132 5922 5456 -40 -131 -26 O
ATOM 2381 N ALA A 235 15.784 200.249 13.893 1.00 40.03 N
ANISOU 2381 N ALA A 235 5267 5212 4732 -64 -82 -53 N
ATOM 2382 CA ALA A 235 16.188 199.418 14.990 1.00 38.49 C
ANISOU 2382 CA ALA A 235 5049 5042 4534 -74 -64 -61 C
ATOM 2383 C ALA A 235 15.197 198.287 15.232 1.00 37.68 C
ANISOU 2383 C ALA A 235 4922 4933 4462 -62 -84 -60 C
ATOM 2384 O ALA A 235 15.580 197.206 15.554 1.00 37.39 O
ANISOU 2384 O ALA A 235 4874 4916 4415 -63 -83 -63 O
ATOM 2385 CB ALA A 235 16.396 200.243 16.228 1.00 38.43 C
ANISOU 2385 CB ALA A 235 5030 5042 4531 -92 -26 -69 C
ATOM 2386 N ALA A 236 13.922 198.553 15.034 1.00 37.03 N
ANISOU 2386 N ALA A 236 4830 4821 4418 -49 -102 -57 N
ATOM 2387 CA ALA A 236 12.895 197.552 15.206 1.00 36.25 C
ANISOU 2387 CA ALA A 236 4709 4714 4352 -37 -120 -58 C
ATOM 2388 C ALA A 236 12.986 196.473 14.142 1.00 34.96 C
ANISOU 2388 C ALA A 236 4554 4555 4173 -26 -151 -55 C
ATOM 2389 O ALA A 236 12.722 195.346 14.402 1.00 34.32 O
ANISOU 2389 O ALA A 236 4456 4481 4102 -22 -156 -58 O
ATOM 2390 CB ALA A 236 11.524 198.179 15.220 1.00 37.20 C
ANISOU 2390 CB ALA A 236 4816 4800 4518 -27 -132 -56 C
ATOM 2391 N ILE A 237 13.349 196.860 12.939 1.00 34.47 N
ANISOU 2391 N ILE A 237 4520 4489 4088 -23 -169 -48 N
ATOM 2392 CA ILE A 237 13.514 195.926 11.853 1.00 34.56 C
ANISOU 2392 CA ILE A 237 4546 4506 4081 -16 -196 -45 C
ATOM 2393 C ILE A 237 14.610 194.927 12.202 1.00 33.72 C
ANISOU 2393 C ILE A 237 4436 4428 3946 -25 -178 -49 C
ATOM 2394 O ILE A 237 14.457 193.774 11.953 1.00 33.71 O
ANISOU 2394 O ILE A 237 4428 4432 3947 -20 -190 -51 O
ATOM 2395 CB ILE A 237 13.827 196.633 10.532 1.00 35.51 C
ANISOU 2395 CB ILE A 237 4701 4616 4177 -14 -215 -36 C
ATOM 2396 CG1 ILE A 237 12.585 197.253 9.950 1.00 37.29 C
ANISOU 2396 CG1 ILE A 237 4926 4812 4431 0 -244 -29 C
ATOM 2397 CG2 ILE A 237 14.391 195.677 9.515 1.00 35.83 C
ANISOU 2397 CG2 ILE A 237 4760 4667 4187 -14 -232 -35 C
ATOM 2398 CD1 ILE A 237 12.864 198.176 8.809 1.00 38.80 C
ANISOU 2398 CD1 ILE A 237 5152 4991 4599 3 -258 -19 C
ATOM 2399 N ILE A 238 15.695 195.411 12.793 1.00 32.73 N
ANISOU 2399 N ILE A 238 4318 4322 3797 -39 -148 -51 N
ATOM 2400 CA ILE A 238 16.823 194.602 13.221 1.00 32.43 C
ANISOU 2400 CA ILE A 238 4275 4313 3732 -48 -129 -54 C
ATOM 2401 C ILE A 238 16.399 193.562 14.266 1.00 31.77 C
ANISOU 2401 C ILE A 238 4160 4240 3671 -45 -120 -57 C
ATOM 2402 O ILE A 238 16.763 192.424 14.188 1.00 31.43 O
ANISOU 2402 O ILE A 238 4112 4211 3620 -43 -120 -57 O
ATOM 2403 CB ILE A 238 17.949 195.476 13.793 1.00 33.37 C
ANISOU 2403 CB ILE A 238 4402 4450 3826 -64 -98 -57 C
ATOM 2404 CG1 ILE A 238 18.480 196.471 12.769 1.00 35.37 C
ANISOU 2404 CG1 ILE A 238 4689 4694 4054 -67 -102 -54 C
ATOM 2405 CG2 ILE A 238 19.041 194.639 14.398 1.00 33.56 C
ANISOU 2405 CG2 ILE A 238 4416 4506 3827 -73 -78 -58 C
ATOM 2406 CD1 ILE A 238 19.340 195.910 11.698 1.00 36.90 C
ANISOU 2406 CD1 ILE A 238 4907 4895 4217 -68 -111 -52 C
ATOM 2407 N ALA A 239 15.627 193.992 15.245 1.00 31.07 N
ANISOU 2407 N ALA A 239 4051 4142 3612 -46 -110 -61 N
ATOM 2408 CA ALA A 239 15.119 193.114 16.278 1.00 30.05 C
ANISOU 2408 CA ALA A 239 3893 4018 3506 -44 -100 -66 C
ATOM 2409 C ALA A 239 14.138 192.091 15.709 1.00 29.95 C
ANISOU 2409 C ALA A 239 3872 3990 3519 -28 -125 -66 C
ATOM 2410 O ALA A 239 14.118 190.964 16.123 1.00 29.39 O
ANISOU 2410 O ALA A 239 3786 3929 3454 -25 -119 -68 O
ATOM 2411 CB ALA A 239 14.480 193.914 17.364 1.00 29.36 C
ANISOU 2411 CB ALA A 239 3791 3920 3446 -50 -82 -71 C
ATOM 2412 N GLY A 240 13.364 192.523 14.729 1.00 29.77 N
ANISOU 2412 N GLY A 240 3859 3943 3509 -19 -153 -64 N
ATOM 2413 CA GLY A 240 12.398 191.709 14.044 1.00 30.11 C
ANISOU 2413 CA GLY A 240 3896 3971 3575 -6 -181 -66 C
ATOM 2414 C GLY A 240 13.056 190.647 13.213 1.00 29.84 C
ANISOU 2414 C GLY A 240 3874 3951 3514 -5 -190 -64 C
ATOM 2415 O GLY A 240 12.591 189.561 13.159 1.00 30.02 O
ANISOU 2415 O GLY A 240 3883 3973 3551 1 -196 -68 O
ATOM 2416 N LEU A 241 14.150 190.994 12.569 1.00 29.33 N
ANISOU 2416 N LEU A 241 3835 3897 3411 -13 -187 -59 N
ATOM 2417 CA LEU A 241 14.912 190.064 11.776 1.00 29.71 C
ANISOU 2417 CA LEU A 241 3898 3959 3432 -15 -191 -57 C
ATOM 2418 C LEU A 241 15.597 188.998 12.647 1.00 27.78 C
ANISOU 2418 C LEU A 241 3636 3738 3182 -18 -164 -58 C
ATOM 2419 O LEU A 241 15.748 187.897 12.244 1.00 28.02 O
ANISOU 2419 O LEU A 241 3664 3773 3207 -16 -165 -59 O
ATOM 2420 CB LEU A 241 15.893 190.792 10.881 1.00 30.71 C
ANISOU 2420 CB LEU A 241 4058 4089 3522 -23 -193 -52 C
ATOM 2421 CG LEU A 241 15.292 191.499 9.670 1.00 33.43 C
ANISOU 2421 CG LEU A 241 4426 4410 3865 -18 -225 -48 C
ATOM 2422 CD1 LEU A 241 16.319 192.311 8.936 1.00 33.38 C
ANISOU 2422 CD1 LEU A 241 4454 4406 3822 -26 -221 -44 C
ATOM 2423 CD2 LEU A 241 14.543 190.570 8.748 1.00 34.18 C
ANISOU 2423 CD2 LEU A 241 4523 4496 3970 -11 -254 -50 C
ATOM 2424 N PHE A 242 15.969 189.357 13.858 1.00 25.78 N
ANISOU 2424 N PHE A 242 3368 3498 2930 -24 -138 -58 N
ATOM 2425 CA PHE A 242 16.545 188.421 14.778 1.00 24.69 C
ANISOU 2425 CA PHE A 242 3211 3383 2788 -26 -114 -57 C
ATOM 2426 C PHE A 242 15.487 187.369 15.141 1.00 24.53 C
ANISOU 2426 C PHE A 242 3167 3351 2800 -14 -117 -62 C
ATOM 2427 O PHE A 242 15.764 186.216 15.181 1.00 23.95 O
ANISOU 2427 O PHE A 242 3087 3289 2725 -11 -109 -61 O
ATOM 2428 CB PHE A 242 17.114 189.122 16.016 1.00 23.93 C
ANISOU 2428 CB PHE A 242 3106 3304 2684 -36 -88 -57 C
ATOM 2429 CG PHE A 242 17.667 188.196 17.053 1.00 23.92 C
ANISOU 2429 CG PHE A 242 3083 3326 2677 -38 -64 -54 C
ATOM 2430 CD1 PHE A 242 16.851 187.528 17.895 1.00 24.84 C
ANISOU 2430 CD1 PHE A 242 3177 3438 2822 -31 -57 -57 C
ATOM 2431 CD2 PHE A 242 19.010 188.013 17.182 1.00 24.18 C
ANISOU 2431 CD2 PHE A 242 3121 3387 2680 -46 -48 -47 C
ATOM 2432 CE1 PHE A 242 17.355 186.675 18.837 1.00 25.60 C
ANISOU 2432 CE1 PHE A 242 3257 3556 2913 -31 -35 -52 C
ATOM 2433 CE2 PHE A 242 19.525 187.167 18.112 1.00 24.85 C
ANISOU 2433 CE2 PHE A 242 3187 3495 2760 -46 -28 -42 C
ATOM 2434 CZ PHE A 242 18.698 186.497 18.953 1.00 24.88 C
ANISOU 2434 CZ PHE A 242 3169 3494 2790 -38 -21 -44 C
ATOM 2435 N ALA A 243 14.272 187.808 15.377 1.00 24.99 N
ANISOU 2435 N ALA A 243 3215 3389 2892 -9 -129 -69 N
ATOM 2436 CA ALA A 243 13.191 186.925 15.712 1.00 26.00 C
ANISOU 2436 CA ALA A 243 3322 3504 3055 1 -132 -76 C
ATOM 2437 C ALA A 243 12.848 186.018 14.531 1.00 27.84 C
ANISOU 2437 C ALA A 243 3561 3728 3289 8 -154 -78 C
ATOM 2438 O ALA A 243 12.689 184.860 14.688 1.00 28.84 O
ANISOU 2438 O ALA A 243 3674 3858 3425 13 -146 -82 O
ATOM 2439 CB ALA A 243 11.996 187.703 16.184 1.00 26.06 C
ANISOU 2439 CB ALA A 243 3316 3487 3099 5 -139 -82 C
ATOM 2440 N LEU A 244 12.776 186.570 13.347 1.00 28.53 N
ANISOU 2440 N LEU A 244 3670 3805 3365 8 -180 -76 N
ATOM 2441 CA LEU A 244 12.483 185.793 12.175 1.00 30.62 C
ANISOU 2441 CA LEU A 244 3943 4063 3626 11 -202 -79 C
ATOM 2442 C LEU A 244 13.522 184.701 11.912 1.00 29.57 C
ANISOU 2442 C LEU A 244 3818 3950 3468 7 -184 -76 C
ATOM 2443 O LEU A 244 13.173 183.612 11.582 1.00 30.21 O
ANISOU 2443 O LEU A 244 3893 4029 3559 10 -186 -81 O
ATOM 2444 CB LEU A 244 12.355 186.700 10.963 1.00 33.45 C
ANISOU 2444 CB LEU A 244 4328 4409 3972 10 -232 -75 C
ATOM 2445 CG LEU A 244 11.760 186.179 9.658 1.00 39.95 C
ANISOU 2445 CG LEU A 244 5163 5221 4795 12 -264 -78 C
ATOM 2446 CD1 LEU A 244 10.273 185.985 9.850 1.00 42.11 C
ANISOU 2446 CD1 LEU A 244 5412 5476 5112 22 -282 -87 C
ATOM 2447 CD2 LEU A 244 12.039 187.128 8.500 1.00 42.19 C
ANISOU 2447 CD2 LEU A 244 5480 5499 5053 8 -288 -70 C
ATOM 2448 N CYS A 245 14.790 185.029 12.068 1.00 26.90 N
ANISOU 2448 N CYS A 245 3492 3629 3098 -2 -166 -67 N
ATOM 2449 CA CYS A 245 15.871 184.106 11.823 1.00 26.02 C
ANISOU 2449 CA CYS A 245 3388 3535 2963 -7 -148 -63 C
ATOM 2450 C CYS A 245 16.059 183.026 12.887 1.00 25.52 C
ANISOU 2450 C CYS A 245 3298 3486 2911 -2 -119 -62 C
ATOM 2451 O CYS A 245 16.446 181.960 12.571 1.00 26.35 O
ANISOU 2451 O CYS A 245 3403 3598 3012 -2 -108 -60 O
ATOM 2452 CB CYS A 245 17.198 184.840 11.565 1.00 25.95 C
ANISOU 2452 CB CYS A 245 3401 3540 2918 -17 -139 -55 C
ATOM 2453 SG CYS A 245 17.337 185.888 10.131 1.00 29.98 S
ANISOU 2453 SG CYS A 245 3950 4036 3406 -24 -166 -54 S
ATOM 2454 N TRP A 246 15.764 183.324 14.134 1.00 23.78 N
ANISOU 2454 N TRP A 246 3057 3270 2707 1 -106 -62 N
ATOM 2455 CA TRP A 246 15.923 182.389 15.221 1.00 23.51 C
ANISOU 2455 CA TRP A 246 3000 3249 2683 6 -79 -60 C
ATOM 2456 C TRP A 246 14.696 181.562 15.591 1.00 24.72 C
ANISOU 2456 C TRP A 246 3133 3387 2873 16 -79 -70 C
ATOM 2457 O TRP A 246 14.847 180.479 16.062 1.00 24.45 O
ANISOU 2457 O TRP A 246 3084 3360 2844 22 -58 -68 O
ATOM 2458 CB TRP A 246 16.464 183.082 16.470 1.00 22.40 C
ANISOU 2458 CB TRP A 246 2850 3125 2534 0 -60 -54 C
ATOM 2459 CG TRP A 246 17.889 183.339 16.451 1.00 22.32 C
ANISOU 2459 CG TRP A 246 2852 3140 2490 -9 -48 -44 C
ATOM 2460 CD1 TRP A 246 18.476 184.481 16.149 1.00 23.19 C
ANISOU 2460 CD1 TRP A 246 2978 3254 2578 -19 -54 -42 C
ATOM 2461 CD2 TRP A 246 18.930 182.425 16.766 1.00 22.17 C
ANISOU 2461 CD2 TRP A 246 2825 3144 2455 -8 -25 -33 C
ATOM 2462 NE1 TRP A 246 19.810 184.364 16.228 1.00 23.26 N
ANISOU 2462 NE1 TRP A 246 2992 3287 2559 -26 -38 -33 N
ATOM 2463 CE2 TRP A 246 20.123 183.099 16.603 1.00 22.72 C
ANISOU 2463 CE2 TRP A 246 2908 3231 2494 -19 -21 -26 C
ATOM 2464 CE3 TRP A 246 18.968 181.096 17.144 1.00 22.54 C
ANISOU 2464 CE3 TRP A 246 2855 3198 2512 0 -8 -28 C
ATOM 2465 CZ2 TRP A 246 21.347 182.500 16.833 1.00 22.32 C
ANISOU 2465 CZ2 TRP A 246 2853 3205 2424 -21 -1 -15 C
ATOM 2466 CZ3 TRP A 246 20.177 180.513 17.365 1.00 22.68 C
ANISOU 2466 CZ3 TRP A 246 2869 3238 2509 -1 13 -15 C
ATOM 2467 CH2 TRP A 246 21.341 181.207 17.206 1.00 22.31 C
ANISOU 2467 CH2 TRP A 246 2834 3209 2434 -12 15 -8 C
ATOM 2468 N LEU A 247 13.504 182.089 15.359 1.00 25.90 N
ANISOU 2468 N LEU A 247 3280 3514 3048 20 -101 -80 N
ATOM 2469 CA LEU A 247 12.269 181.401 15.698 1.00 26.62 C
ANISOU 2469 CA LEU A 247 3350 3587 3177 30 -101 -92 C
ATOM 2470 C LEU A 247 12.059 179.999 15.149 1.00 26.53 C
ANISOU 2470 C LEU A 247 3334 3573 3172 35 -97 -98 C
ATOM 2471 O LEU A 247 11.635 179.167 15.858 1.00 27.21 O
ANISOU 2471 O LEU A 247 3402 3658 3281 42 -78 -103 O
ATOM 2472 CB LEU A 247 11.051 182.255 15.424 1.00 28.63 C
ANISOU 2472 CB LEU A 247 3602 3816 3458 32 -129 -101 C
ATOM 2473 CG LEU A 247 10.613 183.169 16.541 1.00 31.47 C
ANISOU 2473 CG LEU A 247 3950 4169 3838 31 -120 -103 C
ATOM 2474 CD1 LEU A 247 9.702 184.224 15.975 1.00 32.94 C
ANISOU 2474 CD1 LEU A 247 4141 4333 4044 33 -150 -107 C
ATOM 2475 CD2 LEU A 247 9.921 182.399 17.623 1.00 32.56 C
ANISOU 2475 CD2 LEU A 247 4064 4301 4008 38 -99 -112 C
ATOM 2476 N PRO A 248 12.364 179.756 13.877 1.00 25.47 N
ANISOU 2476 N PRO A 248 3219 3439 3021 30 -112 -97 N
ATOM 2477 CA PRO A 248 12.171 178.410 13.367 1.00 24.77 C
ANISOU 2477 CA PRO A 248 3125 3347 2938 33 -104 -104 C
ATOM 2478 C PRO A 248 12.956 177.348 14.126 1.00 24.46 C
ANISOU 2478 C PRO A 248 3075 3325 2894 36 -66 -96 C
ATOM 2479 O PRO A 248 12.421 176.320 14.328 1.00 25.25 O
ANISOU 2479 O PRO A 248 3160 3418 3015 43 -51 -104 O
ATOM 2480 CB PRO A 248 12.630 178.505 11.934 1.00 25.38 C
ANISOU 2480 CB PRO A 248 3230 3425 2989 23 -124 -101 C
ATOM 2481 CG PRO A 248 12.541 179.919 11.600 1.00 26.58 C
ANISOU 2481 CG PRO A 248 3397 3572 3132 20 -152 -98 C
ATOM 2482 CD PRO A 248 12.802 180.674 12.839 1.00 24.80 C
ANISOU 2482 CD PRO A 248 3160 3354 2909 22 -137 -92 C
ATOM 2483 N LEU A 249 14.182 177.631 14.531 1.00 23.21 N
ANISOU 2483 N LEU A 249 2922 3187 2709 32 -50 -81 N
ATOM 2484 CA LEU A 249 14.991 176.710 15.276 1.00 22.87 C
ANISOU 2484 CA LEU A 249 2868 3162 2660 36 -15 -70 C
ATOM 2485 C LEU A 249 14.424 176.446 16.660 1.00 23.29 C
ANISOU 2485 C LEU A 249 2898 3215 2738 46 4 -72 C
ATOM 2486 O LEU A 249 14.308 175.342 17.048 1.00 23.12 O
ANISOU 2486 O LEU A 249 2862 3193 2729 54 27 -72 O
ATOM 2487 CB LEU A 249 16.458 177.134 15.332 1.00 22.18 C
ANISOU 2487 CB LEU A 249 2792 3097 2538 29 -5 -53 C
ATOM 2488 CG LEU A 249 17.510 176.201 15.933 1.00 23.64 C
ANISOU 2488 CG LEU A 249 2966 3303 2712 32 29 -38 C
ATOM 2489 CD1 LEU A 249 17.509 174.819 15.342 1.00 24.80 C
ANISOU 2489 CD1 LEU A 249 3112 3445 2868 36 46 -39 C
ATOM 2490 CD2 LEU A 249 18.905 176.746 15.905 1.00 23.72 C
ANISOU 2490 CD2 LEU A 249 2987 3335 2691 24 34 -23 C
ATOM 2491 N HIS A 250 14.074 177.501 17.352 1.00 23.62 N
ANISOU 2491 N HIS A 250 2936 3254 2785 44 -6 -74 N
ATOM 2492 CA HIS A 250 13.318 177.391 18.559 1.00 24.63 C
ANISOU 2492 CA HIS A 250 3044 3376 2939 50 8 -80 C
ATOM 2493 C HIS A 250 12.004 176.635 18.445 1.00 26.46 C
ANISOU 2493 C HIS A 250 3262 3582 3208 59 7 -97 C
ATOM 2494 O HIS A 250 11.672 175.904 19.307 1.00 28.36 O
ANISOU 2494 O HIS A 250 3488 3821 3467 67 31 -100 O
ATOM 2495 CB HIS A 250 13.087 178.754 19.152 1.00 24.45 C
ANISOU 2495 CB HIS A 250 3022 3350 2917 44 -3 -81 C
ATOM 2496 CG HIS A 250 14.309 179.380 19.705 1.00 23.74 C
ANISOU 2496 CG HIS A 250 2939 3287 2796 35 8 -66 C
ATOM 2497 ND1 HIS A 250 14.960 178.886 20.796 1.00 24.54 N
ANISOU 2497 ND1 HIS A 250 3029 3408 2887 37 35 -55 N
ATOM 2498 CD2 HIS A 250 14.998 180.461 19.316 1.00 23.49 C
ANISOU 2498 CD2 HIS A 250 2923 3264 2738 25 -5 -60 C
ATOM 2499 CE1 HIS A 250 15.986 179.645 21.067 1.00 24.31 C
ANISOU 2499 CE1 HIS A 250 3007 3402 2829 26 37 -44 C
ATOM 2500 NE2 HIS A 250 16.037 180.598 20.176 1.00 24.25 N
ANISOU 2500 NE2 HIS A 250 3016 3387 2811 19 14 -48 N
ATOM 2501 N ILE A 251 11.270 176.836 17.379 1.00 26.13 N
ANISOU 2501 N ILE A 251 3228 3523 3177 58 -21 -109 N
ATOM 2502 CA ILE A 251 9.996 176.160 17.166 1.00 27.23 C
ANISOU 2502 CA ILE A 251 3355 3640 3353 65 -25 -128 C
ATOM 2503 C ILE A 251 10.196 174.665 16.948 1.00 27.27 C
ANISOU 2503 C ILE A 251 3354 3648 3359 70 0 -130 C
ATOM 2504 O ILE A 251 9.448 173.877 17.439 1.00 27.75 O
ANISOU 2504 O ILE A 251 3398 3697 3448 78 17 -142 O
ATOM 2505 CB ILE A 251 9.149 176.809 16.057 1.00 29.45 C
ANISOU 2505 CB ILE A 251 3643 3903 3644 61 -64 -140 C
ATOM 2506 CG1 ILE A 251 8.627 178.154 16.505 1.00 29.98 C
ANISOU 2506 CG1 ILE A 251 3708 3959 3724 60 -82 -140 C
ATOM 2507 CG2 ILE A 251 7.979 175.949 15.662 1.00 31.34 C
ANISOU 2507 CG2 ILE A 251 3869 4122 3916 67 -69 -159 C
ATOM 2508 CD1 ILE A 251 8.215 179.055 15.384 1.00 31.40 C
ANISOU 2508 CD1 ILE A 251 3901 4128 3901 56 -122 -142 C
ATOM 2509 N ILE A 252 11.246 174.309 16.236 1.00 26.90 N
ANISOU 2509 N ILE A 252 3322 3617 3282 64 5 -118 N
ATOM 2510 CA ILE A 252 11.587 172.933 15.997 1.00 27.95 C
ANISOU 2510 CA ILE A 252 3451 3754 3415 68 32 -117 C
ATOM 2511 C ILE A 252 11.950 172.258 17.312 1.00 28.09 C
ANISOU 2511 C ILE A 252 3452 3782 3438 78 70 -107 C
ATOM 2512 O ILE A 252 11.537 171.179 17.549 1.00 29.12 O
ANISOU 2512 O ILE A 252 3571 3905 3589 86 95 -115 O
ATOM 2513 CB ILE A 252 12.688 172.750 14.959 1.00 28.34 C
ANISOU 2513 CB ILE A 252 3521 3816 3432 58 31 -106 C
ATOM 2514 CG1 ILE A 252 12.196 173.125 13.579 1.00 30.40 C
ANISOU 2514 CG1 ILE A 252 3798 4064 3688 48 -3 -118 C
ATOM 2515 CG2 ILE A 252 13.166 171.329 14.957 1.00 28.41 C
ANISOU 2515 CG2 ILE A 252 3523 3830 3441 62 68 -102 C
ATOM 2516 CD1 ILE A 252 13.300 173.363 12.609 1.00 31.86 C
ANISOU 2516 CD1 ILE A 252 4008 4260 3837 36 -10 -107 C
ATOM 2517 N ASN A 253 12.723 172.911 18.150 1.00 26.37 N
ANISOU 2517 N ASN A 253 3235 3582 3202 77 76 -91 N
ATOM 2518 CA ASN A 253 12.995 172.423 19.483 1.00 26.11 C
ANISOU 2518 CA ASN A 253 3187 3559 3173 86 108 -81 C
ATOM 2519 C ASN A 253 11.747 172.192 20.315 1.00 27.78 C
ANISOU 2519 C ASN A 253 3384 3751 3422 94 117 -98 C
ATOM 2520 O ASN A 253 11.682 171.286 21.052 1.00 29.42 O
ANISOU 2520 O ASN A 253 3579 3958 3640 104 147 -95 O
ATOM 2521 CB ASN A 253 13.963 173.315 20.253 1.00 24.78 C
ANISOU 2521 CB ASN A 253 3023 3415 2979 81 108 -63 C
ATOM 2522 CG ASN A 253 15.341 173.350 19.655 1.00 25.40 C
ANISOU 2522 CG ASN A 253 3113 3515 3023 74 108 -45 C
ATOM 2523 OD1 ASN A 253 15.700 172.533 18.897 1.00 24.18 O
ANISOU 2523 OD1 ASN A 253 2962 3360 2864 76 117 -42 O
ATOM 2524 ND2 ASN A 253 16.083 174.325 20.001 1.00 25.35 N
ANISOU 2524 ND2 ASN A 253 3113 3527 2993 67 100 -34 N
ATOM 2525 N CYS A 254 10.767 173.034 20.173 1.00 27.40 N
ANISOU 2525 N CYS A 254 3335 3684 3392 90 91 -114 N
ATOM 2526 CA CYS A 254 9.514 172.864 20.877 1.00 27.84 C
ANISOU 2526 CA CYS A 254 3376 3717 3487 97 98 -132 C
ATOM 2527 C CYS A 254 8.785 171.587 20.442 1.00 28.79 C
ANISOU 2527 C CYS A 254 3487 3820 3633 105 113 -148 C
ATOM 2528 O CYS A 254 8.269 170.896 21.247 1.00 29.52 O
ANISOU 2528 O CYS A 254 3566 3902 3748 114 139 -156 O
ATOM 2529 CB CYS A 254 8.628 174.113 20.755 1.00 27.55 C
ANISOU 2529 CB CYS A 254 3340 3661 3466 91 67 -144 C
ATOM 2530 SG CYS A 254 9.189 175.578 21.591 1.00 27.77 S
ANISOU 2530 SG CYS A 254 3375 3703 3475 81 60 -131 S
ATOM 2531 N PHE A 255 8.764 171.305 19.150 1.00 28.86 N
ANISOU 2531 N PHE A 255 3503 3826 3636 100 96 -154 N
ATOM 2532 CA PHE A 255 8.167 170.100 18.604 1.00 29.73 C
ANISOU 2532 CA PHE A 255 3607 3924 3767 105 110 -170 C
ATOM 2533 C PHE A 255 8.869 168.841 19.139 1.00 29.45 C
ANISOU 2533 C PHE A 255 3565 3898 3725 113 156 -159 C
ATOM 2534 O PHE A 255 8.235 167.933 19.562 1.00 30.43 O
ANISOU 2534 O PHE A 255 3678 4010 3876 122 182 -171 O
ATOM 2535 CB PHE A 255 8.146 170.122 17.068 1.00 30.63 C
ANISOU 2535 CB PHE A 255 3733 4036 3868 94 83 -177 C
ATOM 2536 CG PHE A 255 6.965 170.821 16.496 1.00 32.41 C
ANISOU 2536 CG PHE A 255 3957 4243 4116 90 45 -197 C
ATOM 2537 CD1 PHE A 255 5.785 170.155 16.317 1.00 34.13 C
ANISOU 2537 CD1 PHE A 255 4160 4440 4369 94 47 -221 C
ATOM 2538 CD2 PHE A 255 7.017 172.153 16.209 1.00 33.46 C
ANISOU 2538 CD2 PHE A 255 4100 4378 4237 84 9 -190 C
ATOM 2539 CE1 PHE A 255 4.686 170.794 15.833 1.00 35.94 C
ANISOU 2539 CE1 PHE A 255 4383 4652 4620 91 11 -238 C
ATOM 2540 CE2 PHE A 255 5.922 172.805 15.723 1.00 35.38 C
ANISOU 2540 CE2 PHE A 255 4339 4602 4502 82 -26 -206 C
ATOM 2541 CZ PHE A 255 4.753 172.119 15.527 1.00 35.98 C
ANISOU 2541 CZ PHE A 255 4398 4659 4613 86 -26 -229 C
ATOM 2542 N THR A 256 10.189 168.849 19.132 1.00 28.32 N
ANISOU 2542 N THR A 256 3433 3780 3549 111 165 -134 N
ATOM 2543 CA THR A 256 11.033 167.785 19.626 1.00 28.81 C
ANISOU 2543 CA THR A 256 3490 3856 3602 120 206 -117 C
ATOM 2544 C THR A 256 10.779 167.510 21.106 1.00 29.88 C
ANISOU 2544 C THR A 256 3611 3989 3753 132 233 -113 C
ATOM 2545 O THR A 256 10.697 166.401 21.510 1.00 31.41 O
ANISOU 2545 O THR A 256 3796 4179 3960 143 269 -113 O
ATOM 2546 CB THR A 256 12.519 168.132 19.421 1.00 28.53 C
ANISOU 2546 CB THR A 256 3466 3847 3528 114 204 -90 C
ATOM 2547 OG1 THR A 256 12.809 168.234 18.042 1.00 30.10 O
ANISOU 2547 OG1 THR A 256 3680 4045 3713 102 184 -93 O
ATOM 2548 CG2 THR A 256 13.403 167.121 20.036 1.00 26.92 C
ANISOU 2548 CG2 THR A 256 3254 3657 3317 124 244 -69 C
ATOM 2549 N PHE A 257 10.627 168.557 21.874 1.00 29.35 N
ANISOU 2549 N PHE A 257 3544 3924 3683 129 217 -111 N
ATOM 2550 CA PHE A 257 10.390 168.479 23.290 1.00 30.23 C
ANISOU 2550 CA PHE A 257 3646 4035 3806 137 240 -108 C
ATOM 2551 C PHE A 257 8.947 168.178 23.702 1.00 32.62 C
ANISOU 2551 C PHE A 257 3938 4306 4151 143 249 -135 C
ATOM 2552 O PHE A 257 8.707 167.260 24.418 1.00 33.45 O
ANISOU 2552 O PHE A 257 4034 4404 4271 154 283 -137 O
ATOM 2553 CB PHE A 257 10.850 169.777 23.931 1.00 28.66 C
ANISOU 2553 CB PHE A 257 3452 3851 3586 128 221 -96 C
ATOM 2554 CG PHE A 257 10.732 169.804 25.407 1.00 28.24 C
ANISOU 2554 CG PHE A 257 3392 3799 3537 133 243 -91 C
ATOM 2555 CD1 PHE A 257 11.508 168.997 26.190 1.00 28.25 C
ANISOU 2555 CD1 PHE A 257 3389 3820 3525 142 275 -70 C
ATOM 2556 CD2 PHE A 257 9.857 170.651 26.010 1.00 29.45 C
ANISOU 2556 CD2 PHE A 257 3543 3936 3709 127 232 -106 C
ATOM 2557 CE1 PHE A 257 11.400 169.018 27.543 1.00 29.32 C
ANISOU 2557 CE1 PHE A 257 3521 3957 3662 145 294 -64 C
ATOM 2558 CE2 PHE A 257 9.746 170.685 27.368 1.00 30.48 C
ANISOU 2558 CE2 PHE A 257 3670 4067 3843 128 254 -102 C
ATOM 2559 CZ PHE A 257 10.517 169.864 28.137 1.00 30.15 C
ANISOU 2559 CZ PHE A 257 3626 4044 3784 137 284 -81 C
ATOM 2560 N PHE A 258 8.010 168.951 23.211 1.00 32.98 N
ANISOU 2560 N PHE A 258 3984 4333 4215 136 218 -156 N
ATOM 2561 CA PHE A 258 6.638 168.849 23.590 1.00 34.39 C
ANISOU 2561 CA PHE A 258 4150 4481 4435 140 222 -182 C
ATOM 2562 C PHE A 258 5.919 167.705 22.888 1.00 37.62 C
ANISOU 2562 C PHE A 258 4551 4872 4870 146 235 -203 C
ATOM 2563 O PHE A 258 5.012 167.181 23.409 1.00 39.17 O
ANISOU 2563 O PHE A 258 4737 5048 5100 152 255 -222 O
ATOM 2564 CB PHE A 258 5.924 170.168 23.346 1.00 33.29 C
ANISOU 2564 CB PHE A 258 4012 4329 4309 130 184 -194 C
ATOM 2565 CG PHE A 258 6.302 171.268 24.284 1.00 32.78 C
ANISOU 2565 CG PHE A 258 3952 4273 4230 124 179 -181 C
ATOM 2566 CD1 PHE A 258 6.173 171.120 25.642 1.00 32.80 C
ANISOU 2566 CD1 PHE A 258 3949 4271 4241 127 208 -179 C
ATOM 2567 CD2 PHE A 258 6.719 172.475 23.814 1.00 32.71 C
ANISOU 2567 CD2 PHE A 258 3953 4275 4200 113 146 -172 C
ATOM 2568 CE1 PHE A 258 6.495 172.131 26.498 1.00 33.10 C
ANISOU 2568 CE1 PHE A 258 3993 4319 4266 118 205 -169 C
ATOM 2569 CE2 PHE A 258 7.042 173.480 24.670 1.00 32.40 C
ANISOU 2569 CE2 PHE A 258 3919 4244 4149 105 145 -162 C
ATOM 2570 CZ PHE A 258 6.933 173.311 26.015 1.00 32.29 C
ANISOU 2570 CZ PHE A 258 3899 4228 4143 107 174 -161 C
ATOM 2571 N CYS A 259 6.357 167.309 21.712 1.00 38.54 N
ANISOU 2571 N CYS A 259 4675 4999 4971 141 226 -200 N
ATOM 2572 CA CYS A 259 5.744 166.211 20.970 1.00 40.44 C
ANISOU 2572 CA CYS A 259 4909 5224 5232 144 240 -221 C
ATOM 2573 C CYS A 259 6.644 165.028 20.709 1.00 40.87 C
ANISOU 2573 C CYS A 259 4966 5292 5269 148 274 -207 C
ATOM 2574 O CYS A 259 7.166 164.880 19.651 1.00 40.44 O
ANISOU 2574 O CYS A 259 4921 5248 5196 140 264 -202 O
ATOM 2575 CB CYS A 259 5.195 166.674 19.628 1.00 42.46 C
ANISOU 2575 CB CYS A 259 5168 5473 5491 132 198 -237 C
ATOM 2576 SG CYS A 259 4.049 165.533 18.833 1.00 49.51 S
ANISOU 2576 SG CYS A 259 6050 6344 6419 132 209 -271 S
ATOM 2577 N PRO A 260 6.777 164.136 21.666 1.00 41.88 N
ANISOU 2577 N PRO A 260 5087 5420 5407 161 318 -201 N
ATOM 2578 CA PRO A 260 7.595 162.950 21.480 1.00 43.24 C
ANISOU 2578 CA PRO A 260 5260 5602 5567 167 356 -186 C
ATOM 2579 C PRO A 260 6.971 161.872 20.603 1.00 46.25 C
ANISOU 2579 C PRO A 260 5637 5967 5969 165 375 -210 C
ATOM 2580 O PRO A 260 7.678 160.951 20.307 1.00 47.16 O
ANISOU 2580 O PRO A 260 5755 6090 6075 167 405 -198 O
ATOM 2581 CB PRO A 260 7.796 162.444 22.892 1.00 43.57 C
ANISOU 2581 CB PRO A 260 5296 5646 5615 182 396 -172 C
ATOM 2582 CG PRO A 260 6.716 163.046 23.667 1.00 43.56 C
ANISOU 2582 CG PRO A 260 5287 5624 5638 184 385 -192 C
ATOM 2583 CD PRO A 260 6.478 164.362 23.072 1.00 41.30 C
ANISOU 2583 CD PRO A 260 5007 5340 5346 170 334 -198 C
ATOM 2584 N ASP A 261 5.696 161.988 20.236 1.00 47.60 N
ANISOU 2584 N ASP A 261 5800 6115 6170 160 358 -243 N
ATOM 2585 CA ASP A 261 5.008 161.084 19.330 1.00 49.78 C
ANISOU 2585 CA ASP A 261 6071 6376 6466 155 369 -270 C
ATOM 2586 C ASP A 261 5.143 161.548 17.895 1.00 49.53 C
ANISOU 2586 C ASP A 261 6051 6353 6415 137 329 -274 C
ATOM 2587 O ASP A 261 4.819 160.846 16.988 1.00 50.59 O
ANISOU 2587 O ASP A 261 6185 6481 6557 128 336 -292 O
ATOM 2588 CB ASP A 261 3.543 160.984 19.681 1.00 54.05 C
ANISOU 2588 CB ASP A 261 6598 6890 7050 158 370 -304 C
ATOM 2589 CG ASP A 261 3.313 160.248 20.946 1.00 62.37 C
ANISOU 2589 CG ASP A 261 7641 7931 8125 175 419 -305 C
ATOM 2590 OD1 ASP A 261 4.096 159.334 21.246 1.00 63.58 O
ANISOU 2590 OD1 ASP A 261 7797 8093 8267 184 461 -287 O
ATOM 2591 OD2 ASP A 261 2.352 160.579 21.651 1.00 66.60 O
ANISOU 2591 OD2 ASP A 261 8167 8446 8690 180 416 -323 O
ATOM 2592 N CYS A 262 5.639 162.752 17.730 1.00 47.97 N
ANISOU 2592 N CYS A 262 5864 6169 6193 131 288 -257 N
ATOM 2593 CA CYS A 262 5.878 163.338 16.437 1.00 47.08 C
ANISOU 2593 CA CYS A 262 5765 6064 6057 114 248 -257 C
ATOM 2594 C CYS A 262 7.262 162.961 15.989 1.00 45.38 C
ANISOU 2594 C CYS A 262 5565 5869 5808 110 265 -232 C
ATOM 2595 O CYS A 262 8.189 162.985 16.750 1.00 44.89 O
ANISOU 2595 O CYS A 262 5504 5821 5730 118 285 -206 O
ATOM 2596 CB CYS A 262 5.854 164.853 16.528 1.00 47.07 C
ANISOU 2596 CB CYS A 262 5771 6068 6045 111 201 -249 C
ATOM 2597 SG CYS A 262 4.321 165.693 16.880 1.00 50.14 S
ANISOU 2597 SG CYS A 262 6145 6434 6471 113 168 -274 S
ATOM 2598 N SER A 263 7.409 162.631 14.731 1.00 44.66 N
ANISOU 2598 N SER A 263 5484 5779 5704 95 258 -239 N
ATOM 2599 CA SER A 263 8.709 162.312 14.205 1.00 43.58 C
ANISOU 2599 CA SER A 263 5363 5658 5537 88 274 -217 C
ATOM 2600 C SER A 263 9.618 163.540 14.301 1.00 40.94 C
ANISOU 2600 C SER A 263 5042 5341 5171 86 242 -192 C
ATOM 2601 O SER A 263 9.213 164.658 14.091 1.00 40.82 O
ANISOU 2601 O SER A 263 5033 5326 5152 81 199 -196 O
ATOM 2602 CB SER A 263 8.604 161.842 12.752 1.00 46.45 C
ANISOU 2602 CB SER A 263 5738 6017 5891 68 268 -232 C
ATOM 2603 OG SER A 263 7.900 160.639 12.649 1.00 50.44 O
ANISOU 2603 OG SER A 263 6233 6509 6424 68 302 -255 O
ATOM 2604 N HIS A 264 10.870 163.309 14.628 1.00 38.61 N
ANISOU 2604 N HIS A 264 4751 5062 4856 90 267 -164 N
ATOM 2605 CA HIS A 264 11.824 164.372 14.729 1.00 36.18 C
ANISOU 2605 CA HIS A 264 4456 4773 4519 87 243 -141 C
ATOM 2606 C HIS A 264 12.011 165.003 13.389 1.00 36.73 C
ANISOU 2606 C HIS A 264 4547 4843 4566 68 208 -146 C
ATOM 2607 O HIS A 264 12.074 164.329 12.396 1.00 38.09 O
ANISOU 2607 O HIS A 264 4728 5010 4734 57 217 -155 O
ATOM 2608 CB HIS A 264 13.165 163.824 15.192 1.00 34.16 C
ANISOU 2608 CB HIS A 264 4199 4534 4247 94 280 -112 C
ATOM 2609 CG HIS A 264 14.101 164.858 15.729 1.00 32.88 C
ANISOU 2609 CG HIS A 264 4042 4392 4060 95 262 -88 C
ATOM 2610 ND1 HIS A 264 14.753 165.762 14.933 1.00 33.83 N
ANISOU 2610 ND1 HIS A 264 4181 4521 4152 81 232 -82 N
ATOM 2611 CD2 HIS A 264 14.500 165.117 16.987 1.00 32.92 C
ANISOU 2611 CD2 HIS A 264 4036 4410 4061 108 272 -70 C
ATOM 2612 CE1 HIS A 264 15.497 166.541 15.677 1.00 33.26 C
ANISOU 2612 CE1 HIS A 264 4107 4466 4062 85 225 -62 C
ATOM 2613 NE2 HIS A 264 15.367 166.164 16.927 1.00 33.22 N
ANISOU 2613 NE2 HIS A 264 4084 4465 4071 101 248 -55 N
ATOM 2614 N ALA A 265 12.132 166.310 13.385 1.00 35.59 N
ANISOU 2614 N ALA A 265 4411 4705 4405 65 169 -140 N
ATOM 2615 CA ALA A 265 12.417 167.065 12.200 1.00 36.25 C
ANISOU 2615 CA ALA A 265 4518 4791 4464 48 134 -141 C
ATOM 2616 C ALA A 265 13.646 166.492 11.499 1.00 36.42 C
ANISOU 2616 C ALA A 265 4555 4821 4462 38 157 -126 C
ATOM 2617 O ALA A 265 14.659 166.228 12.099 1.00 35.98 O
ANISOU 2617 O ALA A 265 4495 4778 4397 45 185 -105 O
ATOM 2618 CB ALA A 265 12.641 168.511 12.545 1.00 35.47 C
ANISOU 2618 CB ALA A 265 4427 4701 4351 49 100 -130 C
ATOM 2619 N PRO A 266 13.558 166.323 10.195 1.00 37.11 N
ANISOU 2619 N PRO A 266 4661 4901 4539 21 145 -138 N
ATOM 2620 CA PRO A 266 14.682 165.743 9.474 1.00 37.36 C
ANISOU 2620 CA PRO A 266 4708 4937 4550 9 170 -127 C
ATOM 2621 C PRO A 266 15.966 166.555 9.525 1.00 37.32 C
ANISOU 2621 C PRO A 266 4717 4947 4516 7 163 -103 C
ATOM 2622 O PRO A 266 15.977 167.730 9.688 1.00 37.28 O
ANISOU 2622 O PRO A 266 4719 4948 4499 8 130 -99 O
ATOM 2623 CB PRO A 266 14.165 165.612 8.047 1.00 38.64 C
ANISOU 2623 CB PRO A 266 4890 5087 4705 -12 150 -147 C
ATOM 2624 CG PRO A 266 12.949 166.409 7.957 1.00 39.44 C
ANISOU 2624 CG PRO A 266 4988 5181 4815 -11 105 -164 C
ATOM 2625 CD PRO A 266 12.528 166.855 9.306 1.00 37.59 C
ANISOU 2625 CD PRO A 266 4731 4950 4601 10 103 -159 C
ATOM 2626 N LEU A 267 17.064 165.869 9.352 1.00 37.36 N
ANISOU 2626 N LEU A 267 4726 4957 4512 3 198 -88 N
ATOM 2627 CA LEU A 267 18.372 166.464 9.383 1.00 37.52 C
ANISOU 2627 CA LEU A 267 4758 4991 4508 0 199 -66 C
ATOM 2628 C LEU A 267 18.534 167.621 8.414 1.00 36.61 C
ANISOU 2628 C LEU A 267 4671 4873 4365 -16 158 -71 C
ATOM 2629 O LEU A 267 19.154 168.592 8.728 1.00 36.00 O
ANISOU 2629 O LEU A 267 4599 4807 4271 -14 143 -59 O
ATOM 2630 CB LEU A 267 19.431 165.391 9.200 1.00 39.04 C
ANISOU 2630 CB LEU A 267 4949 5185 4700 -2 246 -52 C
ATOM 2631 CG LEU A 267 20.889 165.780 9.236 1.00 41.52 C
ANISOU 2631 CG LEU A 267 5270 5512 4992 -5 255 -29 C
ATOM 2632 CD1 LEU A 267 21.170 166.567 10.481 1.00 41.32 C
ANISOU 2632 CD1 LEU A 267 5229 5507 4965 11 243 -13 C
ATOM 2633 CD2 LEU A 267 21.761 164.549 9.201 1.00 42.47 C
ANISOU 2633 CD2 LEU A 267 5383 5631 5122 -4 306 -14 C
ATOM 2634 N TRP A 268 17.939 167.524 7.243 1.00 36.30 N
ANISOU 2634 N TRP A 268 4651 4820 4322 -32 141 -89 N
ATOM 2635 CA TRP A 268 18.021 168.593 6.281 1.00 35.35 C
ANISOU 2635 CA TRP A 268 4560 4697 4175 -47 102 -94 C
ATOM 2636 C TRP A 268 17.341 169.871 6.777 1.00 32.72 C
ANISOU 2636 C TRP A 268 4222 4366 3842 -38 60 -96 C
ATOM 2637 O TRP A 268 17.779 170.937 6.509 1.00 31.44 O
ANISOU 2637 O TRP A 268 4078 4208 3659 -42 36 -90 O
ATOM 2638 CB TRP A 268 17.495 168.158 4.920 1.00 36.80 C
ANISOU 2638 CB TRP A 268 4764 4864 4352 -67 92 -112 C
ATOM 2639 CG TRP A 268 16.036 167.950 4.817 1.00 38.29 C
ANISOU 2639 CG TRP A 268 4943 5045 4562 -66 71 -134 C
ATOM 2640 CD1 TRP A 268 15.388 166.785 4.885 1.00 39.92 C
ANISOU 2640 CD1 TRP A 268 5132 5245 4791 -65 97 -147 C
ATOM 2641 CD2 TRP A 268 15.047 168.941 4.616 1.00 38.52 C
ANISOU 2641 CD2 TRP A 268 4976 5071 4591 -64 22 -144 C
ATOM 2642 NE1 TRP A 268 14.071 166.968 4.751 1.00 40.54 N
ANISOU 2642 NE1 TRP A 268 5202 5316 4884 -64 66 -167 N
ATOM 2643 CE2 TRP A 268 13.827 168.293 4.577 1.00 39.92 C
ANISOU 2643 CE2 TRP A 268 5136 5239 4792 -63 19 -164 C
ATOM 2644 CE3 TRP A 268 15.077 170.319 4.467 1.00 39.06 C
ANISOU 2644 CE3 TRP A 268 5058 5141 4641 -64 -18 -138 C
ATOM 2645 CZ2 TRP A 268 12.652 168.960 4.400 1.00 41.26 C
ANISOU 2645 CZ2 TRP A 268 5302 5403 4971 -61 -25 -178 C
ATOM 2646 CZ3 TRP A 268 13.921 170.974 4.302 1.00 40.72 C
ANISOU 2646 CZ3 TRP A 268 5266 5346 4861 -61 -59 -150 C
ATOM 2647 CH2 TRP A 268 12.718 170.300 4.261 1.00 41.78 C
ANISOU 2647 CH2 TRP A 268 5382 5471 5020 -59 -64 -169 C
ATOM 2648 N LEU A 269 16.274 169.713 7.530 1.00 31.77 N
ANISOU 2648 N LEU A 269 4078 4243 3749 -24 55 -105 N
ATOM 2649 CA LEU A 269 15.538 170.825 8.076 1.00 31.55 C
ANISOU 2649 CA LEU A 269 4043 4216 3728 -15 21 -108 C
ATOM 2650 C LEU A 269 16.294 171.435 9.250 1.00 30.26 C
ANISOU 2650 C LEU A 269 3869 4069 3560 -3 31 -90 C
ATOM 2651 O LEU A 269 16.295 172.613 9.406 1.00 31.01 O
ANISOU 2651 O LEU A 269 3971 4167 3645 -3 5 -86 O
ATOM 2652 CB LEU A 269 14.108 170.432 8.436 1.00 32.13 C
ANISOU 2652 CB LEU A 269 4095 4279 3835 -6 13 -126 C
ATOM 2653 CG LEU A 269 13.161 171.548 8.818 1.00 33.71 C
ANISOU 2653 CG LEU A 269 4288 4473 4046 2 -24 -133 C
ATOM 2654 CD1 LEU A 269 13.075 172.604 7.753 1.00 34.31 C
ANISOU 2654 CD1 LEU A 269 4390 4545 4100 -10 -67 -134 C
ATOM 2655 CD2 LEU A 269 11.798 171.053 9.231 1.00 35.68 C
ANISOU 2655 CD2 LEU A 269 4513 4710 4332 10 -26 -151 C
ATOM 2656 N MET A 270 16.952 170.603 10.034 1.00 28.90 N
ANISOU 2656 N MET A 270 3680 3906 3394 5 70 -77 N
ATOM 2657 CA MET A 270 17.762 171.065 11.128 1.00 28.74 C
ANISOU 2657 CA MET A 270 3648 3904 3366 14 82 -59 C
ATOM 2658 C MET A 270 18.846 171.953 10.547 1.00 29.53 C
ANISOU 2658 C MET A 270 3772 4012 3435 3 69 -48 C
ATOM 2659 O MET A 270 19.040 173.034 11.005 1.00 29.31 O
ANISOU 2659 O MET A 270 3746 3993 3397 4 52 -43 O
ATOM 2660 CB MET A 270 18.400 169.920 11.885 1.00 28.21 C
ANISOU 2660 CB MET A 270 3563 3848 3310 24 126 -45 C
ATOM 2661 CG MET A 270 17.457 169.011 12.622 1.00 29.79 C
ANISOU 2661 CG MET A 270 3739 4040 3541 38 145 -53 C
ATOM 2662 SD MET A 270 16.308 169.764 13.732 1.00 32.60 S
ANISOU 2662 SD MET A 270 4078 4392 3916 50 125 -63 S
ATOM 2663 CE MET A 270 17.312 170.611 14.900 1.00 25.87 C
ANISOU 2663 CE MET A 270 3219 3565 3045 55 128 -40 C
ATOM 2664 N TYR A 271 19.508 171.477 9.502 1.00 29.93 N
ANISOU 2664 N TYR A 271 3842 4058 3471 -10 80 -47 N
ATOM 2665 CA TYR A 271 20.562 172.204 8.832 1.00 30.43 C
ANISOU 2665 CA TYR A 271 3930 4126 3505 -23 72 -40 C
ATOM 2666 C TYR A 271 20.079 173.560 8.319 1.00 29.80 C
ANISOU 2666 C TYR A 271 3870 4039 3411 -30 29 -48 C
ATOM 2667 O TYR A 271 20.750 174.528 8.447 1.00 28.56 O
ANISOU 2667 O TYR A 271 3724 3892 3237 -32 21 -41 O
ATOM 2668 CB TYR A 271 21.119 171.403 7.665 1.00 32.39 C
ANISOU 2668 CB TYR A 271 4198 4364 3744 -38 90 -41 C
ATOM 2669 CG TYR A 271 22.027 170.262 7.992 1.00 34.63 C
ANISOU 2669 CG TYR A 271 4468 4655 4036 -35 136 -28 C
ATOM 2670 CD1 TYR A 271 22.576 170.123 9.234 1.00 35.69 C
ANISOU 2670 CD1 TYR A 271 4576 4807 4178 -19 156 -10 C
ATOM 2671 CD2 TYR A 271 22.341 169.322 7.040 1.00 36.96 C
ANISOU 2671 CD2 TYR A 271 4775 4937 4330 -48 159 -31 C
ATOM 2672 CE1 TYR A 271 23.414 169.096 9.530 1.00 37.47 C
ANISOU 2672 CE1 TYR A 271 4788 5038 4411 -15 197 5 C
ATOM 2673 CE2 TYR A 271 23.187 168.284 7.322 1.00 38.40 C
ANISOU 2673 CE2 TYR A 271 4944 5123 4522 -44 203 -17 C
ATOM 2674 CZ TYR A 271 23.721 168.176 8.575 1.00 39.60 C
ANISOU 2674 CZ TYR A 271 5070 5294 4683 -26 222 2 C
ATOM 2675 OH TYR A 271 24.540 167.146 8.886 1.00 42.64 O
ANISOU 2675 OH TYR A 271 5439 5683 5078 -21 265 19 O
ATOM 2676 N LEU A 272 18.895 173.571 7.738 1.00 29.91 N
ANISOU 2676 N LEU A 272 3890 4038 3436 -32 4 -64 N
ATOM 2677 CA LEU A 272 18.290 174.747 7.196 1.00 30.85 C
ANISOU 2677 CA LEU A 272 4027 4150 3546 -36 -37 -72 C
ATOM 2678 C LEU A 272 17.944 175.753 8.281 1.00 28.71 C
ANISOU 2678 C LEU A 272 3740 3885 3283 -24 -50 -68 C
ATOM 2679 O LEU A 272 18.162 176.910 8.126 1.00 28.70 O
ANISOU 2679 O LEU A 272 3753 3884 3266 -28 -70 -65 O
ATOM 2680 CB LEU A 272 17.080 174.362 6.355 1.00 33.93 C
ANISOU 2680 CB LEU A 272 4421 4522 3947 -41 -59 -89 C
ATOM 2681 CG LEU A 272 16.178 175.428 5.760 1.00 38.23 C
ANISOU 2681 CG LEU A 272 4981 5057 4489 -43 -105 -97 C
ATOM 2682 CD1 LEU A 272 16.967 176.464 5.002 1.00 39.61 C
ANISOU 2682 CD1 LEU A 272 5189 5231 4631 -54 -121 -90 C
ATOM 2683 CD2 LEU A 272 15.097 174.830 4.900 1.00 39.84 C
ANISOU 2683 CD2 LEU A 272 5187 5247 4703 -49 -123 -114 C
ATOM 2684 N ALA A 273 17.401 175.274 9.381 1.00 27.05 N
ANISOU 2684 N ALA A 273 3500 3679 3099 -11 -36 -69 N
ATOM 2685 CA ALA A 273 17.057 176.127 10.487 1.00 25.40 C
ANISOU 2685 CA ALA A 273 3275 3475 2900 -1 -44 -67 C
ATOM 2686 C ALA A 273 18.307 176.711 11.143 1.00 24.45 C
ANISOU 2686 C ALA A 273 3156 3375 2759 -3 -28 -51 C
ATOM 2687 O ALA A 273 18.309 177.827 11.537 1.00 24.33 O
ANISOU 2687 O ALA A 273 3143 3363 2738 -3 -42 -49 O
ATOM 2688 CB ALA A 273 16.233 175.393 11.490 1.00 24.73 C
ANISOU 2688 CB ALA A 273 3161 3389 2848 12 -28 -72 C
ATOM 2689 N ILE A 274 19.361 175.919 11.240 1.00 24.32 N
ANISOU 2689 N ILE A 274 3136 3371 2733 -4 1 -40 N
ATOM 2690 CA ILE A 274 20.621 176.340 11.817 1.00 24.41 C
ANISOU 2690 CA ILE A 274 3147 3403 2725 -6 17 -24 C
ATOM 2691 C ILE A 274 21.271 177.428 10.960 1.00 25.17 C
ANISOU 2691 C ILE A 274 3272 3498 2793 -19 -1 -24 C
ATOM 2692 O ILE A 274 21.661 178.421 11.448 1.00 24.80 O
ANISOU 2692 O ILE A 274 3227 3462 2735 -21 -6 -21 O
ATOM 2693 CB ILE A 274 21.568 175.142 12.032 1.00 24.95 C
ANISOU 2693 CB ILE A 274 3204 3484 2793 -3 53 -11 C
ATOM 2694 CG1 ILE A 274 21.121 174.319 13.218 1.00 25.95 C
ANISOU 2694 CG1 ILE A 274 3300 3617 2943 12 74 -7 C
ATOM 2695 CG2 ILE A 274 22.972 175.592 12.287 1.00 24.40 C
ANISOU 2695 CG2 ILE A 274 3138 3434 2700 -9 65 3 C
ATOM 2696 CD1 ILE A 274 21.429 172.867 13.120 1.00 26.91 C
ANISOU 2696 CD1 ILE A 274 3411 3737 3075 17 106 0 C
ATOM 2697 N VAL A 275 21.317 177.193 9.665 1.00 25.86 N
ANISOU 2697 N VAL A 275 3384 3571 2871 -29 -9 -30 N
ATOM 2698 CA VAL A 275 21.888 178.082 8.703 1.00 26.69 C
ANISOU 2698 CA VAL A 275 3521 3670 2950 -42 -24 -32 C
ATOM 2699 C VAL A 275 21.127 179.406 8.701 1.00 26.85 C
ANISOU 2699 C VAL A 275 3550 3683 2969 -41 -57 -38 C
ATOM 2700 O VAL A 275 21.712 180.423 8.657 1.00 27.41 O
ANISOU 2700 O VAL A 275 3635 3758 3021 -46 -62 -35 O
ATOM 2701 CB VAL A 275 21.979 177.378 7.329 1.00 29.19 C
ANISOU 2701 CB VAL A 275 3861 3971 3258 -53 -24 -37 C
ATOM 2702 CG1 VAL A 275 21.764 178.318 6.191 1.00 31.21 C
ANISOU 2702 CG1 VAL A 275 4152 4212 3494 -64 -54 -45 C
ATOM 2703 CG2 VAL A 275 23.277 176.615 7.187 1.00 29.18 C
ANISOU 2703 CG2 VAL A 275 3863 3978 3248 -60 10 -27 C
ATOM 2704 N LEU A 276 19.815 179.351 8.813 1.00 26.78 N
ANISOU 2704 N LEU A 276 3530 3662 2982 -33 -76 -47 N
ATOM 2705 CA LEU A 276 19.000 180.534 8.866 1.00 27.23 C
ANISOU 2705 CA LEU A 276 3591 3710 3044 -30 -104 -52 C
ATOM 2706 C LEU A 276 19.294 181.359 10.126 1.00 26.27 C
ANISOU 2706 C LEU A 276 3453 3603 2924 -26 -95 -46 C
ATOM 2707 O LEU A 276 19.335 182.545 10.070 1.00 26.47 O
ANISOU 2707 O LEU A 276 3491 3626 2940 -29 -108 -46 O
ATOM 2708 CB LEU A 276 17.515 180.209 8.738 1.00 28.27 C
ANISOU 2708 CB LEU A 276 3711 3825 3203 -23 -125 -63 C
ATOM 2709 CG LEU A 276 16.491 181.329 8.850 1.00 30.22 C
ANISOU 2709 CG LEU A 276 3957 4061 3465 -18 -155 -68 C
ATOM 2710 CD1 LEU A 276 16.481 182.309 7.708 1.00 30.07 C
ANISOU 2710 CD1 LEU A 276 3970 4030 3425 -25 -184 -68 C
ATOM 2711 CD2 LEU A 276 15.095 180.853 9.175 1.00 31.47 C
ANISOU 2711 CD2 LEU A 276 4091 4206 3658 -8 -166 -78 C
ATOM 2712 N ALA A 277 19.511 180.690 11.239 1.00 24.95 N
ANISOU 2712 N ALA A 277 3260 3451 2769 -20 -70 -41 N
ATOM 2713 CA ALA A 277 19.861 181.343 12.463 1.00 24.46 C
ANISOU 2713 CA ALA A 277 3183 3406 2706 -18 -58 -35 C
ATOM 2714 C ALA A 277 21.192 182.047 12.274 1.00 24.20 C
ANISOU 2714 C ALA A 277 3167 3387 2642 -29 -50 -28 C
ATOM 2715 O ALA A 277 21.309 183.173 12.599 1.00 24.34 O
ANISOU 2715 O ALA A 277 3189 3408 2652 -33 -55 -29 O
ATOM 2716 CB ALA A 277 19.912 180.362 13.613 1.00 23.73 C
ANISOU 2716 CB ALA A 277 3061 3328 2629 -9 -32 -30 C
ATOM 2717 N HIS A 278 22.170 181.374 11.703 1.00 24.34 N
ANISOU 2717 N HIS A 278 3194 3411 2644 -34 -35 -22 N
ATOM 2718 CA HIS A 278 23.470 181.951 11.453 1.00 24.53 C
ANISOU 2718 CA HIS A 278 3234 3447 2641 -44 -26 -17 C
ATOM 2719 C HIS A 278 23.429 183.130 10.501 1.00 26.10 C
ANISOU 2719 C HIS A 278 3464 3630 2822 -53 -47 -24 C
ATOM 2720 O HIS A 278 24.161 184.053 10.661 1.00 25.81 O
ANISOU 2720 O HIS A 278 3436 3602 2768 -60 -43 -23 O
ATOM 2721 CB HIS A 278 24.429 180.903 10.974 1.00 23.86 C
ANISOU 2721 CB HIS A 278 3151 3367 2548 -48 -5 -10 C
ATOM 2722 CG HIS A 278 24.735 179.882 12.001 1.00 24.25 C
ANISOU 2722 CG HIS A 278 3169 3435 2610 -39 20 1 C
ATOM 2723 ND1 HIS A 278 25.212 178.644 11.692 1.00 25.11 N
ANISOU 2723 ND1 HIS A 278 3273 3545 2724 -37 41 8 N
ATOM 2724 CD2 HIS A 278 24.606 179.909 13.343 1.00 24.21 C
ANISOU 2724 CD2 HIS A 278 3137 3448 2614 -31 29 7 C
ATOM 2725 CE1 HIS A 278 25.369 177.953 12.795 1.00 25.25 C
ANISOU 2725 CE1 HIS A 278 3261 3579 2752 -27 61 19 C
ATOM 2726 NE2 HIS A 278 25.002 178.695 13.810 1.00 24.42 N
ANISOU 2726 NE2 HIS A 278 3143 3486 2650 -23 53 18 N
ATOM 2727 N THR A 279 22.524 183.060 9.535 1.00 27.38 N
ANISOU 2727 N THR A 279 3642 3769 2990 -52 -70 -31 N
ATOM 2728 CA THR A 279 22.284 184.085 8.529 1.00 29.30 C
ANISOU 2728 CA THR A 279 3917 3996 3220 -58 -94 -37 C
ATOM 2729 C THR A 279 21.898 185.393 9.151 1.00 28.98 C
ANISOU 2729 C THR A 279 3873 3955 3182 -56 -104 -38 C
ATOM 2730 O THR A 279 22.167 186.412 8.633 1.00 29.75 O
ANISOU 2730 O THR A 279 3995 4046 3264 -62 -112 -40 O
ATOM 2731 CB THR A 279 21.236 183.668 7.483 1.00 32.34 C
ANISOU 2731 CB THR A 279 4316 4359 3615 -56 -120 -43 C
ATOM 2732 OG1 THR A 279 21.771 182.639 6.685 1.00 34.10 O
ANISOU 2732 OG1 THR A 279 4550 4579 3827 -64 -109 -43 O
ATOM 2733 CG2 THR A 279 20.911 184.775 6.606 1.00 33.50 C
ANISOU 2733 CG2 THR A 279 4492 4489 3748 -60 -146 -46 C
ATOM 2734 N ASN A 280 21.360 185.366 10.351 1.00 27.87 N
ANISOU 2734 N ASN A 280 3703 3823 3064 -48 -98 -38 N
ATOM 2735 CA ASN A 280 21.067 186.587 11.072 1.00 27.56 C
ANISOU 2735 CA ASN A 280 3659 3784 3028 -49 -101 -40 C
ATOM 2736 C ASN A 280 22.328 187.466 11.291 1.00 27.15 C
ANISOU 2736 C ASN A 280 3619 3749 2949 -60 -83 -37 C
ATOM 2737 O ASN A 280 22.256 188.663 11.225 1.00 27.68 O
ANISOU 2737 O ASN A 280 3698 3809 3009 -64 -89 -40 O
ATOM 2738 CB ASN A 280 20.358 186.344 12.398 1.00 27.31 C
ANISOU 2738 CB ASN A 280 3593 3759 3023 -41 -92 -40 C
ATOM 2739 CG ASN A 280 19.982 187.631 13.080 1.00 30.02 C
ANISOU 2739 CG ASN A 280 3934 4100 3373 -44 -94 -43 C
ATOM 2740 OD1 ASN A 280 19.129 188.318 12.619 1.00 33.97 O
ANISOU 2740 OD1 ASN A 280 4444 4579 3884 -41 -114 -47 O
ATOM 2741 ND2 ASN A 280 20.642 187.966 14.136 1.00 27.47 N
ANISOU 2741 ND2 ASN A 280 3598 3798 3042 -50 -72 -41 N
ATOM 2742 N SER A 281 23.490 186.864 11.490 1.00 26.08 N
ANISOU 2742 N SER A 281 3478 3633 2798 -65 -61 -32 N
ATOM 2743 CA SER A 281 24.755 187.542 11.603 1.00 26.41 C
ANISOU 2743 CA SER A 281 3529 3690 2814 -77 -44 -31 C
ATOM 2744 C SER A 281 25.271 188.274 10.339 1.00 27.29 C
ANISOU 2744 C SER A 281 3679 3786 2902 -85 -52 -36 C
ATOM 2745 O SER A 281 26.222 188.967 10.416 1.00 27.50 O
ANISOU 2745 O SER A 281 3716 3824 2911 -95 -38 -37 O
ATOM 2746 CB SER A 281 25.810 186.576 12.122 1.00 26.88 C
ANISOU 2746 CB SER A 281 3571 3775 2868 -78 -21 -23 C
ATOM 2747 OG SER A 281 25.450 186.054 13.361 1.00 28.21 O
ANISOU 2747 OG SER A 281 3707 3959 3053 -72 -12 -19 O
ATOM 2748 N VAL A 282 24.600 188.092 9.225 1.00 28.01 N
ANISOU 2748 N VAL A 282 3792 3854 2997 -82 -73 -38 N
ATOM 2749 CA VAL A 282 24.949 188.756 7.983 1.00 29.40 C
ANISOU 2749 CA VAL A 282 4007 4012 3151 -90 -82 -41 C
ATOM 2750 C VAL A 282 24.072 189.978 7.719 1.00 32.59 C
ANISOU 2750 C VAL A 282 4426 4398 3558 -86 -103 -44 C
ATOM 2751 O VAL A 282 24.508 190.928 7.121 1.00 33.89 O
ANISOU 2751 O VAL A 282 4619 4553 3703 -93 -103 -47 O
ATOM 2752 CB VAL A 282 24.812 187.801 6.775 1.00 28.61 C
ANISOU 2752 CB VAL A 282 3927 3897 3048 -91 -94 -41 C
ATOM 2753 CG1 VAL A 282 25.076 188.527 5.485 1.00 29.41 C
ANISOU 2753 CG1 VAL A 282 4071 3978 3125 -99 -105 -45 C
ATOM 2754 CG2 VAL A 282 25.704 186.598 6.919 1.00 27.63 C
ANISOU 2754 CG2 VAL A 282 3790 3787 2922 -94 -70 -37 C
ATOM 2755 N VAL A 283 22.845 189.939 8.210 1.00 33.45 N
ANISOU 2755 N VAL A 283 4515 4501 3694 -76 -119 -44 N
ATOM 2756 CA VAL A 283 21.879 190.965 7.910 1.00 35.79 C
ANISOU 2756 CA VAL A 283 4822 4777 3998 -70 -141 -45 C
ATOM 2757 C VAL A 283 22.010 192.361 8.457 1.00 38.19 C
ANISOU 2757 C VAL A 283 5129 5082 4301 -74 -131 -46 C
ATOM 2758 O VAL A 283 21.707 193.267 7.755 1.00 39.95 O
ANISOU 2758 O VAL A 283 5376 5286 4518 -73 -144 -46 O
ATOM 2759 CB VAL A 283 20.421 190.493 8.007 1.00 36.45 C
ANISOU 2759 CB VAL A 283 4887 4848 4114 -58 -165 -44 C
ATOM 2760 CG1 VAL A 283 20.162 189.308 7.130 1.00 37.83 C
ANISOU 2760 CG1 VAL A 283 5068 5017 4289 -56 -179 -45 C
ATOM 2761 CG2 VAL A 283 20.009 190.222 9.412 1.00 35.76 C
ANISOU 2761 CG2 VAL A 283 4761 4773 4052 -53 -151 -45 C
ATOM 2762 N ASN A 284 22.468 192.554 9.669 1.00 38.53 N
ANISOU 2762 N ASN A 284 5149 5145 4346 -79 -106 -48 N
ATOM 2763 CA ASN A 284 22.575 193.919 10.203 1.00 40.14 C
ANISOU 2763 CA ASN A 284 5356 5349 4547 -85 -93 -52 C
ATOM 2764 C ASN A 284 23.307 194.983 9.353 1.00 41.25 C
ANISOU 2764 C ASN A 284 5533 5480 4661 -93 -88 -54 C
ATOM 2765 O ASN A 284 22.745 196.006 9.094 1.00 41.75 O
ANISOU 2765 O ASN A 284 5609 5524 4728 -90 -96 -54 O
ATOM 2766 CB ASN A 284 22.976 193.936 11.685 1.00 40.88 C
ANISOU 2766 CB ASN A 284 5419 5468 4645 -92 -67 -54 C
ATOM 2767 CG ASN A 284 22.007 193.154 12.556 1.00 44.13 C
ANISOU 2767 CG ASN A 284 5798 5883 5088 -83 -72 -52 C
ATOM 2768 OD1 ASN A 284 20.945 192.759 12.121 1.00 44.36 O
ANISOU 2768 OD1 ASN A 284 5825 5892 5137 -71 -95 -50 O
ATOM 2769 ND2 ASN A 284 22.373 192.939 13.784 1.00 44.46 N
ANISOU 2769 ND2 ASN A 284 5814 5947 5130 -89 -51 -53 N
ATOM 2770 N PRO A 285 24.505 194.704 8.843 1.00 41.16 N
ANISOU 2770 N PRO A 285 5539 5479 4623 -102 -76 -56 N
ATOM 2771 CA PRO A 285 25.196 195.683 8.014 1.00 42.13 C
ANISOU 2771 CA PRO A 285 5698 5589 4720 -109 -69 -60 C
ATOM 2772 C PRO A 285 24.408 196.170 6.792 1.00 43.68 C
ANISOU 2772 C PRO A 285 5927 5755 4916 -101 -96 -56 C
ATOM 2773 O PRO A 285 24.564 197.300 6.433 1.00 43.75 O
ANISOU 2773 O PRO A 285 5959 5751 4912 -104 -91 -58 O
ATOM 2774 CB PRO A 285 26.460 194.958 7.599 1.00 42.50 C
ANISOU 2774 CB PRO A 285 5755 5649 4744 -119 -54 -63 C
ATOM 2775 CG PRO A 285 26.670 193.983 8.676 1.00 42.46 C
ANISOU 2775 CG PRO A 285 5712 5671 4752 -118 -43 -60 C
ATOM 2776 CD PRO A 285 25.317 193.516 9.051 1.00 40.55 C
ANISOU 2776 CD PRO A 285 5448 5421 4538 -105 -64 -55 C
ATOM 2777 N PHE A 286 23.589 195.327 6.193 1.00 44.16 N
ANISOU 2777 N PHE A 286 5987 5804 4987 -92 -124 -51 N
ATOM 2778 CA PHE A 286 22.767 195.699 5.070 1.00 46.10 C
ANISOU 2778 CA PHE A 286 6260 6024 5233 -84 -154 -45 C
ATOM 2779 C PHE A 286 21.660 196.617 5.519 1.00 47.16 C
ANISOU 2779 C PHE A 286 6381 6145 5391 -74 -165 -41 C
ATOM 2780 O PHE A 286 21.379 197.573 4.865 1.00 48.56 O
ANISOU 2780 O PHE A 286 6584 6303 5563 -70 -175 -37 O
ATOM 2781 CB PHE A 286 22.242 194.468 4.342 1.00 46.58 C
ANISOU 2781 CB PHE A 286 6321 6079 5298 -80 -179 -42 C
ATOM 2782 CG PHE A 286 23.316 193.682 3.701 1.00 47.16 C
ANISOU 2782 CG PHE A 286 6413 6158 5346 -91 -167 -46 C
ATOM 2783 CD1 PHE A 286 24.045 192.775 4.419 1.00 47.04 C
ANISOU 2783 CD1 PHE A 286 6375 6165 5334 -96 -144 -48 C
ATOM 2784 CD2 PHE A 286 23.649 193.907 2.389 1.00 49.20 C
ANISOU 2784 CD2 PHE A 286 6715 6399 5579 -97 -177 -45 C
ATOM 2785 CE1 PHE A 286 25.083 192.091 3.847 1.00 47.98 C
ANISOU 2785 CE1 PHE A 286 6509 6288 5432 -107 -130 -51 C
ATOM 2786 CE2 PHE A 286 24.681 193.218 1.803 1.00 50.06 C
ANISOU 2786 CE2 PHE A 286 6843 6512 5667 -109 -162 -50 C
ATOM 2787 CZ PHE A 286 25.400 192.317 2.538 1.00 48.87 C
ANISOU 2787 CZ PHE A 286 6665 6381 5521 -114 -137 -52 C
ATOM 2788 N ILE A 287 21.067 196.357 6.670 1.00 46.45 N
ANISOU 2788 N ILE A 287 6253 6065 5330 -69 -160 -42 N
ATOM 2789 CA ILE A 287 20.019 197.212 7.157 1.00 47.49 C
ANISOU 2789 CA ILE A 287 6371 6183 5489 -61 -167 -39 C
ATOM 2790 C ILE A 287 20.509 198.612 7.487 1.00 48.04 C
ANISOU 2790 C ILE A 287 6454 6251 5550 -68 -142 -42 C
ATOM 2791 O ILE A 287 19.804 199.564 7.303 1.00 48.68 O
ANISOU 2791 O ILE A 287 6541 6310 5643 -61 -150 -37 O
ATOM 2792 CB ILE A 287 19.324 196.644 8.379 1.00 47.31 C
ANISOU 2792 CB ILE A 287 6307 6171 5500 -57 -163 -41 C
ATOM 2793 CG1 ILE A 287 18.747 195.279 8.075 1.00 47.87 C
ANISOU 2793 CG1 ILE A 287 6364 6242 5582 -49 -186 -40 C
ATOM 2794 CG2 ILE A 287 18.227 197.577 8.799 1.00 47.87 C
ANISOU 2794 CG2 ILE A 287 6366 6223 5601 -49 -169 -38 C
ATOM 2795 CD1 ILE A 287 17.591 195.307 7.134 1.00 49.96 C
ANISOU 2795 CD1 ILE A 287 6637 6482 5861 -37 -223 -34 C
ATOM 2796 N TYR A 288 21.732 198.722 7.966 1.00 47.70 N
ANISOU 2796 N TYR A 288 6412 6228 5485 -82 -110 -50 N
ATOM 2797 CA TYR A 288 22.304 200.006 8.290 1.00 48.23 C
ANISOU 2797 CA TYR A 288 6491 6295 5541 -92 -82 -55 C
ATOM 2798 C TYR A 288 22.612 200.764 7.018 1.00 49.94 C
ANISOU 2798 C TYR A 288 6750 6490 5734 -91 -88 -53 C
ATOM 2799 O TYR A 288 22.402 201.926 6.960 1.00 50.95 O
ANISOU 2799 O TYR A 288 6892 6603 5865 -90 -79 -52 O
ATOM 2800 CB TYR A 288 23.566 199.867 9.122 1.00 46.89 C
ANISOU 2800 CB TYR A 288 6309 6155 5352 -108 -49 -66 C
ATOM 2801 CG TYR A 288 23.388 199.160 10.412 1.00 46.20 C
ANISOU 2801 CG TYR A 288 6181 6090 5283 -111 -40 -67 C
ATOM 2802 CD1 TYR A 288 22.349 199.451 11.238 1.00 47.01 C
ANISOU 2802 CD1 TYR A 288 6260 6187 5416 -106 -42 -66 C
ATOM 2803 CD2 TYR A 288 24.269 198.199 10.798 1.00 45.97 C
ANISOU 2803 CD2 TYR A 288 6138 6088 5241 -118 -30 -70 C
ATOM 2804 CE1 TYR A 288 22.194 198.799 12.434 1.00 47.09 C
ANISOU 2804 CE1 TYR A 288 6234 6216 5441 -110 -32 -68 C
ATOM 2805 CE2 TYR A 288 24.128 197.536 11.970 1.00 46.10 C
ANISOU 2805 CE2 TYR A 288 6119 6125 5272 -119 -22 -70 C
ATOM 2806 CZ TYR A 288 23.096 197.842 12.794 1.00 47.01 C
ANISOU 2806 CZ TYR A 288 6213 6234 5415 -116 -23 -69 C
ATOM 2807 OH TYR A 288 22.987 197.175 13.959 1.00 47.22 O
ANISOU 2807 OH TYR A 288 6207 6281 5454 -118 -14 -70 O
ATOM 2808 N ALA A 289 23.093 200.072 6.004 1.00 50.20 N
ANISOU 2808 N ALA A 289 6807 6521 5745 -91 -102 -52 N
ATOM 2809 CA ALA A 289 23.435 200.675 4.743 1.00 52.36 C
ANISOU 2809 CA ALA A 289 7126 6775 5994 -91 -108 -50 C
ATOM 2810 C ALA A 289 22.235 201.207 3.997 1.00 55.08 C
ANISOU 2810 C ALA A 289 7485 7091 6351 -76 -139 -37 C
ATOM 2811 O ALA A 289 22.287 202.265 3.430 1.00 55.96 O
ANISOU 2811 O ALA A 289 7626 7184 6452 -74 -135 -34 O
ATOM 2812 CB ALA A 289 24.172 199.693 3.877 1.00 52.42 C
ANISOU 2812 CB ALA A 289 7153 6785 5977 -97 -114 -52 C
ATOM 2813 N TYR A 290 21.157 200.453 4.009 1.00 56.04 N
ANISOU 2813 N TYR A 290 7586 7210 6498 -65 -170 -30 N
ATOM 2814 CA TYR A 290 19.951 200.838 3.338 1.00 58.54 C
ANISOU 2814 CA TYR A 290 7911 7503 6830 -49 -204 -17 C
ATOM 2815 C TYR A 290 19.131 201.866 4.086 1.00 58.48 C
ANISOU 2815 C TYR A 290 7883 7484 6853 -41 -197 -12 C
ATOM 2816 O TYR A 290 18.501 202.684 3.460 1.00 59.86 O
ANISOU 2816 O TYR A 290 8075 7635 7033 -30 -213 -1 O
ATOM 2817 CB TYR A 290 19.105 199.609 3.035 1.00 59.92 C
ANISOU 2817 CB TYR A 290 8068 7679 7020 -42 -239 -13 C
ATOM 2818 CG TYR A 290 19.511 198.926 1.768 1.00 63.35 C
ANISOU 2818 CG TYR A 290 8537 8110 7425 -46 -258 -12 C
ATOM 2819 CD1 TYR A 290 18.992 199.319 0.552 1.00 66.44 C
ANISOU 2819 CD1 TYR A 290 8959 8480 7804 -39 -289 -1 C
ATOM 2820 CD2 TYR A 290 20.438 197.911 1.773 1.00 64.51 C
ANISOU 2820 CD2 TYR A 290 8683 8274 7553 -59 -243 -21 C
ATOM 2821 CE1 TYR A 290 19.377 198.713 -0.622 1.00 68.54 C
ANISOU 2821 CE1 TYR A 290 9259 8743 8040 -47 -304 -1 C
ATOM 2822 CE2 TYR A 290 20.835 197.303 0.608 1.00 66.73 C
ANISOU 2822 CE2 TYR A 290 8996 8550 7807 -66 -256 -21 C
ATOM 2823 CZ TYR A 290 20.297 197.707 -0.586 1.00 69.54 C
ANISOU 2823 CZ TYR A 290 9386 8884 8151 -60 -286 -12 C
ATOM 2824 OH TYR A 290 20.684 197.104 -1.747 1.00 73.07 O
ANISOU 2824 OH TYR A 290 9867 9326 8569 -70 -298 -13 O
ATOM 2825 N ARG A 291 19.262 201.909 5.406 1.00 56.31 N
ANISOU 2825 N ARG A 291 7575 7225 6596 -48 -169 -20 N
ATOM 2826 CA ARG A 291 18.384 202.704 6.230 1.00 55.66 C
ANISOU 2826 CA ARG A 291 7468 7131 6547 -42 -162 -17 C
ATOM 2827 C ARG A 291 19.014 203.872 6.957 1.00 54.70 C
ANISOU 2827 C ARG A 291 7349 7012 6421 -53 -119 -25 C
ATOM 2828 O ARG A 291 18.327 204.701 7.458 1.00 55.13 O
ANISOU 2828 O ARG A 291 7392 7053 6503 -49 -110 -21 O
ATOM 2829 CB ARG A 291 17.672 201.826 7.220 1.00 55.63 C
ANISOU 2829 CB ARG A 291 7422 7138 6576 -39 -167 -20 C
ATOM 2830 CG ARG A 291 16.587 200.998 6.619 1.00 57.70 C
ANISOU 2830 CG ARG A 291 7675 7390 6858 -25 -210 -12 C
ATOM 2831 CD ARG A 291 15.550 200.787 7.658 1.00 60.69 C
ANISOU 2831 CD ARG A 291 8013 7766 7280 -19 -210 -13 C
ATOM 2832 NE ARG A 291 14.237 200.840 7.082 1.00 64.19 N
ANISOU 2832 NE ARG A 291 8450 8186 7752 -2 -247 -2 N
ATOM 2833 CZ ARG A 291 13.329 201.752 7.376 1.00 66.69 C
ANISOU 2833 CZ ARG A 291 8755 8481 8102 7 -248 5 C
ATOM 2834 NH1 ARG A 291 12.155 201.693 6.802 1.00 66.31 N
ANISOU 2834 NH1 ARG A 291 8700 8413 8080 23 -284 16 N
ATOM 2835 NH2 ARG A 291 13.584 202.710 8.249 1.00 66.56 N
ANISOU 2835 NH2 ARG A 291 8733 8462 8095 -1 -211 1 N
ATOM 2836 N ILE A 292 20.321 203.917 7.024 1.00 53.65 N
ANISOU 2836 N ILE A 292 7231 6897 6256 -69 -92 -36 N
ATOM 2837 CA ILE A 292 20.990 204.962 7.765 1.00 53.52 C
ANISOU 2837 CA ILE A 292 7215 6886 6233 -83 -49 -46 C
ATOM 2838 C ILE A 292 22.070 205.603 6.931 1.00 54.76 C
ANISOU 2838 C ILE A 292 7414 7039 6354 -90 -32 -51 C
ATOM 2839 O ILE A 292 23.064 204.998 6.669 1.00 53.84 O
ANISOU 2839 O ILE A 292 7307 6939 6210 -99 -27 -58 O
ATOM 2840 CB ILE A 292 21.610 204.444 9.081 1.00 52.63 C
ANISOU 2840 CB ILE A 292 7070 6805 6120 -99 -22 -59 C
ATOM 2841 CG1 ILE A 292 20.565 203.791 9.980 1.00 52.55 C
ANISOU 2841 CG1 ILE A 292 7021 6799 6147 -93 -35 -56 C
ATOM 2842 CG2 ILE A 292 22.265 205.577 9.846 1.00 53.03 C
ANISOU 2842 CG2 ILE A 292 7122 6864 6164 -116 22 -71 C
ATOM 2843 CD1 ILE A 292 21.095 202.863 11.038 1.00 51.49 C
ANISOU 2843 CD1 ILE A 292 6858 6697 6010 -104 -21 -64 C
ATOM 2844 N ARG A 293 21.843 206.847 6.530 1.00 56.45 N
ANISOU 2844 N ARG A 293 7651 7230 6570 -86 -22 -46 N
ATOM 2845 CA ARG A 293 22.752 207.654 5.713 1.00 58.37 C
ANISOU 2845 CA ARG A 293 7936 7463 6780 -91 -2 -51 C
ATOM 2846 C ARG A 293 24.197 207.741 6.167 1.00 56.97 C
ANISOU 2846 C ARG A 293 7762 7309 6575 -113 37 -71 C
ATOM 2847 O ARG A 293 25.109 207.534 5.413 1.00 57.59 O
ANISOU 2847 O ARG A 293 7869 7390 6624 -118 40 -76 O
ATOM 2848 CB ARG A 293 22.246 209.079 5.695 1.00 63.20 C
ANISOU 2848 CB ARG A 293 8559 8049 7406 -85 15 -45 C
ATOM 2849 CG ARG A 293 21.113 209.334 4.742 1.00 71.46 C
ANISOU 2849 CG ARG A 293 9621 9064 8467 -62 -22 -23 C
ATOM 2850 CD ARG A 293 21.336 210.607 3.954 1.00 78.86 C
ANISOU 2850 CD ARG A 293 10599 9975 9389 -58 -5 -18 C
ATOM 2851 NE ARG A 293 20.114 210.973 3.260 1.00 85.36 N
ANISOU 2851 NE ARG A 293 11429 10769 10234 -35 -38 6 N
ATOM 2852 CZ ARG A 293 19.060 211.491 3.863 1.00 90.17 C
ANISOU 2852 CZ ARG A 293 12011 11365 10883 -25 -38 16 C
ATOM 2853 NH1 ARG A 293 19.086 211.711 5.173 1.00 90.15 N
ANISOU 2853 NH1 ARG A 293 11975 11375 10903 -38 -4 3 N
ATOM 2854 NH2 ARG A 293 17.989 211.795 3.155 1.00 92.04 N
ANISOU 2854 NH2 ARG A 293 12254 11576 11139 -3 -71 38 N
ATOM 2855 N GLU A 294 24.401 208.097 7.416 1.00 54.99 N
ANISOU 2855 N GLU A 294 7483 7076 6335 -126 69 -82 N
ATOM 2856 CA GLU A 294 25.739 208.214 7.906 1.00 53.62 C
ANISOU 2856 CA GLU A 294 7310 6928 6136 -148 105 -101 C
ATOM 2857 C GLU A 294 26.551 206.945 7.815 1.00 51.89 C
ANISOU 2857 C GLU A 294 7083 6733 5898 -153 94 -105 C
ATOM 2858 O GLU A 294 27.729 207.025 7.637 1.00 52.20 O
ANISOU 2858 O GLU A 294 7138 6784 5911 -166 115 -118 O
ATOM 2859 CB GLU A 294 25.713 208.735 9.316 1.00 55.55 C
ANISOU 2859 CB GLU A 294 7522 7189 6396 -162 138 -111 C
ATOM 2860 CG GLU A 294 27.034 209.268 9.777 1.00 61.18 C
ANISOU 2860 CG GLU A 294 8239 7924 7083 -186 180 -132 C
ATOM 2861 CD GLU A 294 27.316 210.637 9.263 1.00 67.99 C
ANISOU 2861 CD GLU A 294 9135 8763 7935 -189 210 -139 C
ATOM 2862 OE1 GLU A 294 26.371 211.345 8.926 1.00 71.46 O
ANISOU 2862 OE1 GLU A 294 9585 9173 8394 -176 205 -127 O
ATOM 2863 OE2 GLU A 294 28.483 210.987 9.199 1.00 68.71 O
ANISOU 2863 OE2 GLU A 294 9240 8866 8000 -205 239 -156 O
ATOM 2864 N PHE A 295 25.928 205.781 7.967 1.00 49.84 N
ANISOU 2864 N PHE A 295 6800 6481 5654 -144 62 -96 N
ATOM 2865 CA PHE A 295 26.638 204.514 7.875 1.00 48.80 C
ANISOU 2865 CA PHE A 295 6661 6371 5509 -148 53 -98 C
ATOM 2866 C PHE A 295 26.989 204.268 6.431 1.00 49.68 C
ANISOU 2866 C PHE A 295 6813 6465 5599 -142 36 -94 C
ATOM 2867 O PHE A 295 28.092 203.965 6.101 1.00 50.04 O
ANISOU 2867 O PHE A 295 6873 6520 5621 -153 49 -103 O
ATOM 2868 CB PHE A 295 25.808 203.336 8.400 1.00 47.25 C
ANISOU 2868 CB PHE A 295 6430 6185 5337 -138 26 -89 C
ATOM 2869 CG PHE A 295 26.056 203.015 9.839 1.00 46.27 C
ANISOU 2869 CG PHE A 295 6267 6092 5222 -150 46 -96 C
ATOM 2870 CD1 PHE A 295 27.239 202.465 10.238 1.00 46.10 C
ANISOU 2870 CD1 PHE A 295 6235 6100 5180 -163 63 -104 C
ATOM 2871 CD2 PHE A 295 25.111 203.290 10.789 1.00 46.55 C
ANISOU 2871 CD2 PHE A 295 6275 6126 5285 -148 47 -93 C
ATOM 2872 CE1 PHE A 295 27.477 202.189 11.546 1.00 46.15 C
ANISOU 2872 CE1 PHE A 295 6206 6136 5193 -174 79 -109 C
ATOM 2873 CE2 PHE A 295 25.340 203.003 12.113 1.00 46.53 C
ANISOU 2873 CE2 PHE A 295 6239 6152 5289 -160 65 -100 C
ATOM 2874 CZ PHE A 295 26.529 202.452 12.488 1.00 45.85 C
ANISOU 2874 CZ PHE A 295 6143 6097 5179 -172 80 -107 C
ATOM 2875 N ARG A 296 25.997 204.399 5.584 1.00 50.26 N
ANISOU 2875 N ARG A 296 6905 6511 5682 -126 6 -81 N
ATOM 2876 CA ARG A 296 26.119 204.219 4.160 1.00 51.93 C
ANISOU 2876 CA ARG A 296 7158 6702 5873 -121 -14 -75 C
ATOM 2877 C ARG A 296 27.266 205.037 3.563 1.00 53.55 C
ANISOU 2877 C ARG A 296 7401 6898 6046 -132 16 -86 C
ATOM 2878 O ARG A 296 28.089 204.498 2.867 1.00 54.08 O
ANISOU 2878 O ARG A 296 7490 6966 6091 -139 17 -92 O
ATOM 2879 CB ARG A 296 24.792 204.588 3.541 1.00 53.87 C
ANISOU 2879 CB ARG A 296 7414 6920 6135 -102 -47 -59 C
ATOM 2880 CG ARG A 296 24.708 204.457 2.054 1.00 58.30 C
ANISOU 2880 CG ARG A 296 8018 7459 6676 -95 -73 -50 C
ATOM 2881 CD ARG A 296 23.261 204.356 1.636 1.00 61.35 C
ANISOU 2881 CD ARG A 296 8399 7827 7084 -77 -115 -32 C
ATOM 2882 NE ARG A 296 22.563 205.621 1.635 1.00 63.74 N
ANISOU 2882 NE ARG A 296 8708 8108 7401 -66 -113 -23 N
ATOM 2883 CZ ARG A 296 21.557 205.923 2.432 1.00 66.15 C
ANISOU 2883 CZ ARG A 296 8980 8411 7741 -56 -118 -16 C
ATOM 2884 NH1 ARG A 296 20.982 207.093 2.338 1.00 66.80 N
ANISOU 2884 NH1 ARG A 296 9072 8472 7837 -47 -113 -7 N
ATOM 2885 NH2 ARG A 296 21.123 205.065 3.326 1.00 65.30 N
ANISOU 2885 NH2 ARG A 296 8831 8322 7659 -57 -125 -19 N
ATOM 2886 N GLN A 297 27.325 206.324 3.891 1.00 53.90 N
ANISOU 2886 N GLN A 297 7453 6935 6093 -135 43 -92 N
ATOM 2887 CA GLN A 297 28.350 207.241 3.404 1.00 55.21 C
ANISOU 2887 CA GLN A 297 7655 7091 6231 -145 76 -104 C
ATOM 2888 C GLN A 297 29.718 206.850 3.887 1.00 54.50 C
ANISOU 2888 C GLN A 297 7555 7028 6125 -165 105 -123 C
ATOM 2889 O GLN A 297 30.675 206.970 3.182 1.00 55.51 O
ANISOU 2889 O GLN A 297 7714 7149 6227 -173 121 -133 O
ATOM 2890 CB GLN A 297 28.032 208.686 3.800 1.00 58.19 C
ANISOU 2890 CB GLN A 297 8036 7455 6618 -145 102 -106 C
ATOM 2891 CG GLN A 297 26.740 209.227 3.212 1.00 64.37 C
ANISOU 2891 CG GLN A 297 8833 8207 7418 -124 75 -86 C
ATOM 2892 CD GLN A 297 26.416 210.650 3.642 1.00 72.60 C
ANISOU 2892 CD GLN A 297 9877 9234 8473 -123 106 -87 C
ATOM 2893 OE1 GLN A 297 26.885 211.118 4.663 1.00 74.88 O
ANISOU 2893 OE1 GLN A 297 10144 9539 8766 -138 143 -102 O
ATOM 2894 NE2 GLN A 297 25.616 211.343 2.848 1.00 74.00 N
ANISOU 2894 NE2 GLN A 297 10079 9380 8656 -106 90 -70 N
ATOM 2895 N THR A 298 29.811 206.357 5.100 1.00 52.76 N
ANISOU 2895 N THR A 298 7290 6838 5918 -172 113 -128 N
ATOM 2896 CA THR A 298 31.075 205.918 5.652 1.00 52.01 C
ANISOU 2896 CA THR A 298 7179 6772 5809 -190 138 -143 C
ATOM 2897 C THR A 298 31.496 204.589 5.092 1.00 51.79 C
ANISOU 2897 C THR A 298 7153 6750 5773 -189 118 -139 C
ATOM 2898 O THR A 298 32.650 204.313 4.976 1.00 52.00 O
ANISOU 2898 O THR A 298 7186 6789 5783 -201 137 -150 O
ATOM 2899 CB THR A 298 31.003 205.797 7.178 1.00 51.62 C
ANISOU 2899 CB THR A 298 7082 6756 5776 -198 150 -147 C
ATOM 2900 OG1 THR A 298 30.256 206.880 7.699 1.00 52.30 O
ANISOU 2900 OG1 THR A 298 7162 6831 5877 -197 162 -147 O
ATOM 2901 CG2 THR A 298 32.354 205.799 7.774 1.00 51.69 C
ANISOU 2901 CG2 THR A 298 7078 6793 5768 -218 183 -165 C
ATOM 2902 N PHE A 299 30.541 203.742 4.784 1.00 51.43 N
ANISOU 2902 N PHE A 299 7101 6698 5742 -174 81 -123 N
ATOM 2903 CA PHE A 299 30.870 202.456 4.214 1.00 51.96 C
ANISOU 2903 CA PHE A 299 7170 6768 5803 -174 65 -119 C
ATOM 2904 C PHE A 299 31.521 202.726 2.831 1.00 54.38 C
ANISOU 2904 C PHE A 299 7530 7050 6084 -178 69 -124 C
ATOM 2905 O PHE A 299 32.467 202.083 2.445 1.00 54.11 O
ANISOU 2905 O PHE A 299 7504 7019 6035 -187 79 -130 O
ATOM 2906 CB PHE A 299 29.626 201.554 4.045 1.00 50.50 C
ANISOU 2906 CB PHE A 299 6972 6578 5639 -158 25 -102 C
ATOM 2907 CG PHE A 299 29.038 200.987 5.324 1.00 48.88 C
ANISOU 2907 CG PHE A 299 6716 6396 5459 -154 19 -98 C
ATOM 2908 CD1 PHE A 299 29.703 201.011 6.517 1.00 48.43 C
ANISOU 2908 CD1 PHE A 299 6628 6370 5404 -165 46 -106 C
ATOM 2909 CD2 PHE A 299 27.799 200.404 5.296 1.00 48.82 C
ANISOU 2909 CD2 PHE A 299 6695 6382 5473 -140 -13 -85 C
ATOM 2910 CE1 PHE A 299 29.132 200.480 7.647 1.00 47.97 C
ANISOU 2910 CE1 PHE A 299 6528 6332 5368 -162 40 -101 C
ATOM 2911 CE2 PHE A 299 27.221 199.866 6.418 1.00 48.29 C
ANISOU 2911 CE2 PHE A 299 6585 6334 5431 -136 -17 -82 C
ATOM 2912 CZ PHE A 299 27.887 199.909 7.598 1.00 47.49 C
ANISOU 2912 CZ PHE A 299 6455 6260 5330 -147 10 -89 C
ATOM 2913 N ARG A 300 31.003 203.699 2.101 1.00 56.61 N
ANISOU 2913 N ARG A 300 7847 7304 6360 -171 63 -120 N
ATOM 2914 CA ARG A 300 31.519 204.032 0.766 1.00 59.69 C
ANISOU 2914 CA ARG A 300 8291 7666 6724 -174 67 -124 C
ATOM 2915 C ARG A 300 32.954 204.501 0.775 1.00 61.40 C
ANISOU 2915 C ARG A 300 8522 7886 6920 -192 109 -144 C
ATOM 2916 O ARG A 300 33.736 204.083 -0.035 1.00 61.89 O
ANISOU 2916 O ARG A 300 8611 7938 6964 -200 115 -150 O
ATOM 2917 CB ARG A 300 30.659 205.079 0.105 1.00 62.50 C
ANISOU 2917 CB ARG A 300 8678 7992 7078 -162 54 -114 C
ATOM 2918 CG ARG A 300 29.334 204.578 -0.388 1.00 67.11 C
ANISOU 2918 CG ARG A 300 9260 8563 7674 -145 8 -94 C
ATOM 2919 CD ARG A 300 28.650 205.673 -1.153 1.00 72.60 C
ANISOU 2919 CD ARG A 300 9992 9228 8364 -133 -2 -83 C
ATOM 2920 NE ARG A 300 27.226 205.479 -1.129 1.00 76.75 N
ANISOU 2920 NE ARG A 300 10500 9749 8914 -116 -42 -65 N
ATOM 2921 CZ ARG A 300 26.592 204.644 -1.922 1.00 80.25 C
ANISOU 2921 CZ ARG A 300 10952 10184 9355 -109 -81 -53 C
ATOM 2922 NH1 ARG A 300 27.259 203.942 -2.817 1.00 80.11 N
ANISOU 2922 NH1 ARG A 300 10964 10162 9312 -119 -84 -58 N
ATOM 2923 NH2 ARG A 300 25.292 204.523 -1.822 1.00 81.42 N
ANISOU 2923 NH2 ARG A 300 11079 10328 9527 -93 -116 -37 N
ATOM 2924 N LYS A 301 33.274 205.364 1.723 1.00 62.16 N
ANISOU 2924 N LYS A 301 8599 7997 7021 -198 138 -155 N
ATOM 2925 CA LYS A 301 34.602 205.899 1.906 1.00 63.88 C
ANISOU 2925 CA LYS A 301 8825 8223 7223 -216 180 -176 C
ATOM 2926 C LYS A 301 35.556 204.846 2.355 1.00 64.66 C
ANISOU 2926 C LYS A 301 8896 8350 7321 -227 188 -183 C
ATOM 2927 O LYS A 301 36.700 204.890 2.023 1.00 65.83 O
ANISOU 2927 O LYS A 301 9061 8497 7454 -240 214 -198 O
ATOM 2928 CB LYS A 301 34.593 206.990 2.963 1.00 66.02 C
ANISOU 2928 CB LYS A 301 9076 8509 7502 -221 208 -186 C
ATOM 2929 CG LYS A 301 33.578 208.064 2.727 1.00 71.17 C
ANISOU 2929 CG LYS A 301 9746 9135 8159 -209 203 -177 C
ATOM 2930 CD LYS A 301 33.991 209.374 3.365 1.00 75.98 C
ANISOU 2930 CD LYS A 301 10355 9748 8767 -220 246 -194 C
ATOM 2931 CE LYS A 301 33.042 210.488 2.948 1.00 79.97 C
ANISOU 2931 CE LYS A 301 10885 10221 9278 -207 245 -183 C
ATOM 2932 NZ LYS A 301 33.472 211.258 1.747 1.00 82.68 N
ANISOU 2932 NZ LYS A 301 11284 10531 9598 -206 260 -188 N
ATOM 2933 N ILE A 302 35.115 203.915 3.159 1.00 64.27 N
ANISOU 2933 N ILE A 302 8804 8326 7291 -222 170 -173 N
ATOM 2934 CA ILE A 302 36.019 202.882 3.596 1.00 65.17 C
ANISOU 2934 CA ILE A 302 8890 8466 7405 -232 178 -177 C
ATOM 2935 C ILE A 302 36.318 201.989 2.418 1.00 67.43 C
ANISOU 2935 C ILE A 302 9205 8732 7683 -231 166 -172 C
ATOM 2936 O ILE A 302 37.424 201.565 2.230 1.00 68.11 O
ANISOU 2936 O ILE A 302 9294 8824 7761 -243 185 -182 O
ATOM 2937 CB ILE A 302 35.445 202.029 4.746 1.00 63.93 C
ANISOU 2937 CB ILE A 302 8681 8339 7270 -226 161 -165 C
ATOM 2938 CG1 ILE A 302 35.299 202.828 6.031 1.00 64.29 C
ANISOU 2938 CG1 ILE A 302 8695 8408 7323 -231 177 -171 C
ATOM 2939 CG2 ILE A 302 36.341 200.858 5.016 1.00 64.09 C
ANISOU 2939 CG2 ILE A 302 8676 8383 7291 -232 166 -165 C
ATOM 2940 CD1 ILE A 302 34.449 202.149 7.072 1.00 64.10 C
ANISOU 2940 CD1 ILE A 302 8627 8407 7321 -223 158 -158 C
ATOM 2941 N ILE A 303 35.298 201.681 1.656 1.00 68.65 N
ANISOU 2941 N ILE A 303 9379 8864 7840 -218 134 -158 N
ATOM 2942 CA ILE A 303 35.431 200.812 0.513 1.00 71.24 C
ANISOU 2942 CA ILE A 303 9735 9172 8159 -219 120 -154 C
ATOM 2943 C ILE A 303 36.274 201.497 -0.569 1.00 74.42 C
ANISOU 2943 C ILE A 303 10192 9547 8537 -230 142 -167 C
ATOM 2944 O ILE A 303 37.160 200.887 -1.123 1.00 75.18 O
ANISOU 2944 O ILE A 303 10302 9637 8624 -241 155 -174 O
ATOM 2945 CB ILE A 303 34.052 200.371 -0.014 1.00 71.51 C
ANISOU 2945 CB ILE A 303 9776 9191 8201 -204 79 -136 C
ATOM 2946 CG1 ILE A 303 33.408 199.376 0.927 1.00 71.45 C
ANISOU 2946 CG1 ILE A 303 9719 9210 8219 -196 61 -125 C
ATOM 2947 CG2 ILE A 303 34.164 199.693 -1.351 1.00 72.76 C
ANISOU 2947 CG2 ILE A 303 9975 9325 8346 -208 66 -133 C
ATOM 2948 CD1 ILE A 303 31.919 199.317 0.764 1.00 72.49 C
ANISOU 2948 CD1 ILE A 303 9848 9331 8365 -180 23 -110 C
ATOM 2949 N ARG A 304 36.019 202.768 -0.840 1.00 76.43 N
ANISOU 2949 N ARG A 304 10474 9783 8782 -227 149 -171 N
ATOM 2950 CA ARG A 304 36.778 203.506 -1.849 1.00 79.72 C
ANISOU 2950 CA ARG A 304 10944 10172 9174 -236 172 -184 C
ATOM 2951 C ARG A 304 38.256 203.574 -1.527 1.00 81.44 C
ANISOU 2951 C ARG A 304 11156 10402 9386 -254 214 -206 C
ATOM 2952 O ARG A 304 39.070 203.033 -2.245 1.00 82.61 O
ANISOU 2952 O ARG A 304 11326 10537 9524 -265 225 -213 O
ATOM 2953 CB ARG A 304 36.201 204.899 -2.063 1.00 82.14 C
ANISOU 2953 CB ARG A 304 11278 10458 9473 -228 175 -184 C
ATOM 2954 CG ARG A 304 34.944 204.875 -2.911 1.00 86.71 C
ANISOU 2954 CG ARG A 304 11882 11012 10051 -213 135 -164 C
ATOM 2955 CD ARG A 304 34.245 206.209 -3.006 1.00 91.49 C
ANISOU 2955 CD ARG A 304 12508 11600 10655 -201 136 -158 C
ATOM 2956 NE ARG A 304 32.866 206.038 -3.452 1.00 95.86 N
ANISOU 2956 NE ARG A 304 13065 12141 11215 -184 91 -135 N
ATOM 2957 CZ ARG A 304 31.995 207.030 -3.597 1.00 99.54 C
ANISOU 2957 CZ ARG A 304 13545 12590 11686 -170 81 -124 C
ATOM 2958 NH1 ARG A 304 30.758 206.779 -4.002 1.00 99.28 N
ANISOU 2958 NH1 ARG A 304 13513 12548 11662 -154 38 -103 N
ATOM 2959 NH2 ARG A 304 32.359 208.275 -3.331 1.00100.36 N
ANISOU 2959 NH2 ARG A 304 13661 12687 11786 -171 116 -134 N
ATOM 2960 N SER A 305 38.594 204.218 -0.432 1.00 81.59 N
ANISOU 2960 N SER A 305 11143 10445 9412 -259 236 -216 N
ATOM 2961 CA SER A 305 39.965 204.325 0.009 1.00 83.26 C
ANISOU 2961 CA SER A 305 11342 10673 9619 -276 274 -237 C
ATOM 2962 C SER A 305 40.667 202.987 0.096 1.00 83.87 C
ANISOU 2962 C SER A 305 11395 10767 9704 -282 272 -235 C
ATOM 2963 O SER A 305 40.112 202.015 0.587 1.00 83.37 O
ANISOU 2963 O SER A 305 11298 10723 9657 -274 248 -219 O
ATOM 2964 CB SER A 305 39.998 205.007 1.365 1.00 84.43 C
ANISOU 2964 CB SER A 305 11449 10854 9777 -279 290 -244 C
ATOM 2965 OG SER A 305 39.128 206.120 1.370 1.00 86.84 O
ANISOU 2965 OG SER A 305 11770 11144 10080 -271 288 -241 O
TER 2966 SER A 305
HETATM 2967 C1 QGW A1201 21.663 171.518 16.707 0.90 32.86 C
ANISOU 2967 C1 QGW A1201 4095 4532 3858 54 166 34 C
HETATM 2968 C10 QGW A1201 17.916 177.221 19.695 0.90 31.45 C
ANISOU 2968 C10 QGW A1201 3916 4334 3701 37 63 -19 C
HETATM 2969 C11 QGW A1201 23.756 172.525 16.074 0.90 33.53 C
ANISOU 2969 C11 QGW A1201 4199 4642 3899 37 160 52 C
HETATM 2970 C12 QGW A1201 24.082 171.347 15.440 0.90 35.32 C
ANISOU 2970 C12 QGW A1201 4425 4860 4134 39 184 57 C
HETATM 2971 C13 QGW A1201 23.248 170.248 15.422 0.90 35.75 C
ANISOU 2971 C13 QGW A1201 4471 4899 4214 48 201 51 C
HETATM 2972 C14 QGW A1201 21.996 170.314 16.074 0.90 34.38 C
ANISOU 2972 C14 QGW A1201 4288 4717 4058 56 192 38 C
HETATM 2973 C15 QGW A1201 24.157 168.069 15.339 0.90 37.16 C
ANISOU 2973 C15 QGW A1201 4631 5078 4411 60 264 74 C
HETATM 2974 C16 QGW A1201 23.910 166.868 14.409 0.90 37.38 C
ANISOU 2974 C16 QGW A1201 4664 5083 4455 57 289 67 C
HETATM 2975 C17 QGW A1201 25.384 171.229 14.726 0.90 36.28 C
ANISOU 2975 C17 QGW A1201 4557 4988 4240 30 197 69 C
HETATM 2976 C18 QGW A1201 25.328 171.871 13.400 0.90 36.60 C
ANISOU 2976 C18 QGW A1201 4628 5011 4268 13 175 53 C
HETATM 2977 C19 QGW A1201 24.624 171.014 12.383 0.90 37.55 C
ANISOU 2977 C19 QGW A1201 4759 5105 4401 9 181 40 C
HETATM 2978 C2 QGW A1201 22.543 172.604 16.695 0.90 32.54 C
ANISOU 2978 C2 QGW A1201 4064 4508 3792 44 151 41 C
HETATM 2979 C3 QGW A1201 22.214 173.840 17.354 0.90 31.81 C
ANISOU 2979 C3 QGW A1201 3972 4422 3692 40 129 35 C
HETATM 2980 C4 QGW A1201 20.915 173.784 18.020 0.90 31.15 C
ANISOU 2980 C4 QGW A1201 3878 4326 3632 48 125 23 C
HETATM 2981 C5 QGW A1201 20.175 172.677 17.905 0.90 30.55 C
ANISOU 2981 C5 QGW A1201 3794 4234 3581 58 139 17 C
HETATM 2982 C6 QGW A1201 18.859 172.407 18.472 0.90 28.94 C
ANISOU 2982 C6 QGW A1201 3578 4013 3404 66 139 3 C
HETATM 2983 C7 QGW A1201 20.505 175.057 18.607 0.90 31.48 C
ANISOU 2983 C7 QGW A1201 3922 4370 3670 42 104 16 C
HETATM 2984 C8 QGW A1201 19.218 176.626 19.282 0.90 31.61 C
ANISOU 2984 C8 QGW A1201 3939 4373 3698 36 76 -3 C
HETATM 2985 C9 QGW A1201 20.368 177.349 19.330 0.90 31.80 C
ANISOU 2985 C9 QGW A1201 3970 4419 3693 27 75 8 C
HETATM 2986 N1 QGW A1201 19.292 175.385 18.874 0.90 31.27 N
ANISOU 2986 N1 QGW A1201 3892 4325 3663 45 92 1 N
HETATM 2987 O1 QGW A1201 20.481 171.557 17.321 0.90 31.48 O
ANISOU 2987 O1 QGW A1201 3911 4347 3703 61 160 21 O
HETATM 2988 O2 QGW A1201 22.983 174.782 17.338 0.90 31.67 O
ANISOU 2988 O2 QGW A1201 3963 4418 3652 30 119 40 O
HETATM 2989 O3 QGW A1201 23.729 169.186 14.744 0.90 36.87 O
ANISOU 2989 O3 QGW A1201 4615 5034 4361 47 228 57 O
HETATM 2990 O4 QGW A1201 24.664 168.010 16.446 0.90 36.58 O
ANISOU 2990 O4 QGW A1201 4538 5025 4335 71 275 94 O
HETATM 2991 S1 QGW A1201 21.593 176.381 18.796 0.90 32.22 S
ANISOU 2991 S1 QGW A1201 4025 4487 3732 29 93 24 S
HETATM 2992 NA NA A1202 23.312 188.615 16.412 1.00 47.04 NA1+
HETATM 2993 C1 CLR A1203 8.180 169.031 13.267 1.00 43.20 C
HETATM 2994 C2 CLR A1203 8.227 167.509 13.262 1.00 43.17 C
HETATM 2995 C3 CLR A1203 6.857 166.888 12.990 1.00 42.89 C
HETATM 2996 C4 CLR A1203 6.325 167.348 11.632 1.00 42.97 C
HETATM 2997 C5 CLR A1203 6.357 168.860 11.552 1.00 43.32 C
HETATM 2998 C6 CLR A1203 5.260 169.492 11.076 1.00 43.27 C
HETATM 2999 C7 CLR A1203 5.178 171.000 10.934 1.00 43.44 C
HETATM 3000 C8 CLR A1203 6.547 171.687 10.984 1.00 43.79 C
HETATM 3001 C9 CLR A1203 7.398 171.108 12.154 1.00 43.47 C
HETATM 3002 C10 CLR A1203 7.638 169.600 11.950 1.00 43.52 C
HETATM 3003 C11 CLR A1203 8.732 171.861 12.423 1.00 43.28 C
HETATM 3004 C12 CLR A1203 8.524 173.391 12.422 1.00 43.54 C
HETATM 3005 C13 CLR A1203 7.754 173.922 11.190 1.00 44.24 C
HETATM 3006 C14 CLR A1203 6.384 173.216 11.135 1.00 44.37 C
HETATM 3007 C15 CLR A1203 5.575 173.996 10.105 1.00 44.94 C
HETATM 3008 C16 CLR A1203 6.043 175.438 10.352 1.00 44.87 C
HETATM 3009 C17 CLR A1203 7.287 175.390 11.261 1.00 44.59 C
HETATM 3010 C18 CLR A1203 8.576 173.684 9.901 1.00 44.17 C
HETATM 3011 C19 CLR A1203 8.607 169.328 10.793 1.00 43.62 C
HETATM 3012 C20 CLR A1203 8.284 176.527 10.953 1.00 44.75 C
HETATM 3013 C21 CLR A1203 9.565 176.446 11.784 1.00 45.05 C
HETATM 3014 C22 CLR A1203 7.634 177.866 11.276 1.00 44.87 C
HETATM 3015 C23 CLR A1203 8.416 179.080 10.789 1.00 45.11 C
HETATM 3016 C24 CLR A1203 7.663 180.335 11.219 1.00 45.63 C
HETATM 3017 C25 CLR A1203 8.485 181.605 11.014 1.00 45.88 C
HETATM 3018 C26 CLR A1203 7.624 182.668 10.341 1.00 46.12 C
HETATM 3019 C27 CLR A1203 9.021 182.110 12.345 1.00 45.43 C
HETATM 3020 O1 CLR A1203 7.005 165.469 12.980 1.00 42.54 O
HETATM 3021 C1 CLR A1204 -1.155 169.109 21.833 1.00 37.27 C
HETATM 3022 C2 CLR A1204 -1.521 167.652 22.090 1.00 37.23 C
HETATM 3023 C3 CLR A1204 -1.285 167.267 23.552 1.00 37.45 C
HETATM 3024 C4 CLR A1204 -2.130 168.131 24.486 1.00 37.05 C
HETATM 3025 C5 CLR A1204 -1.900 169.593 24.177 1.00 37.36 C
HETATM 3026 C6 CLR A1204 -1.719 170.421 25.224 1.00 37.75 C
HETATM 3027 C7 CLR A1204 -1.400 171.898 25.090 1.00 37.99 C
HETATM 3028 C8 CLR A1204 -1.709 172.465 23.701 1.00 38.12 C
HETATM 3029 C9 CLR A1204 -1.305 171.478 22.574 1.00 37.76 C
HETATM 3030 C10 CLR A1204 -1.946 170.081 22.729 1.00 37.53 C
HETATM 3031 C11 CLR A1204 -1.519 172.057 21.141 1.00 37.62 C
HETATM 3032 C12 CLR A1204 -0.810 173.427 21.041 1.00 37.99 C
HETATM 3033 C13 CLR A1204 -1.257 174.432 22.128 1.00 38.39 C
HETATM 3034 C14 CLR A1204 -0.961 173.805 23.509 1.00 38.58 C
HETATM 3035 C15 CLR A1204 -1.166 174.929 24.525 1.00 38.83 C
HETATM 3036 C16 CLR A1204 -0.620 176.132 23.750 1.00 39.04 C
HETATM 3037 C17 CLR A1204 -0.426 175.723 22.266 1.00 39.10 C
HETATM 3038 C18 CLR A1204 -2.748 174.769 21.958 1.00 38.25 C
HETATM 3039 C19 CLR A1204 -3.427 170.065 22.316 1.00 37.13 C
HETATM 3040 C20 CLR A1204 -0.646 176.896 21.295 1.00 39.78 C
HETATM 3041 C21 CLR A1204 -0.511 176.561 19.809 1.00 39.57 C
HETATM 3042 C22 CLR A1204 0.341 178.018 21.625 1.00 41.02 C
HETATM 3043 C23 CLR A1204 0.010 179.344 20.943 1.00 41.97 C
HETATM 3044 C24 CLR A1204 0.889 180.440 21.528 1.00 42.98 C
HETATM 3045 C25 CLR A1204 0.669 181.761 20.795 1.00 44.11 C
HETATM 3046 C26 CLR A1204 1.273 182.921 21.576 1.00 44.51 C
HETATM 3047 C27 CLR A1204 1.199 181.718 19.359 1.00 44.15 C
HETATM 3048 O1 CLR A1204 -1.669 165.904 23.705 1.00 37.96 O
HETATM 3049 C1 CLR A1205 2.980 171.644 21.311 1.00 35.43 C
HETATM 3050 C2 CLR A1205 2.796 170.129 21.290 1.00 35.03 C
HETATM 3051 C3 CLR A1205 1.852 169.663 20.188 1.00 34.97 C
HETATM 3052 C4 CLR A1205 2.336 170.153 18.816 1.00 35.36 C
HETATM 3053 C5 CLR A1205 2.590 171.655 18.864 1.00 35.87 C
HETATM 3054 C6 CLR A1205 2.044 172.430 17.898 1.00 36.30 C
HETATM 3055 C7 CLR A1205 2.224 173.940 17.832 1.00 36.70 C
HETATM 3056 C8 CLR A1205 3.398 174.427 18.683 1.00 37.01 C
HETATM 3057 C9 CLR A1205 3.400 173.748 20.087 1.00 36.60 C
HETATM 3058 C10 CLR A1205 3.482 172.210 19.977 1.00 35.91 C
HETATM 3059 C11 CLR A1205 4.482 174.293 21.079 1.00 36.82 C
HETATM 3060 C12 CLR A1205 4.529 175.834 21.064 1.00 37.36 C
HETATM 3061 C13 CLR A1205 4.610 176.447 19.644 1.00 38.14 C
HETATM 3062 C14 CLR A1205 3.403 175.963 18.811 1.00 37.61 C
HETATM 3063 C15 CLR A1205 3.405 176.819 17.554 1.00 37.75 C
HETATM 3064 C16 CLR A1205 3.878 178.172 18.094 1.00 38.30 C
HETATM 3065 C17 CLR A1205 4.385 177.973 19.541 1.00 39.14 C
HETATM 3066 C18 CLR A1205 5.962 176.051 19.014 1.00 37.98 C
HETATM 3067 C19 CLR A1205 4.909 171.711 19.690 1.00 35.44 C
HETATM 3068 C20 CLR A1205 5.521 178.941 19.966 1.00 40.55 C
HETATM 3069 C21 CLR A1205 5.918 178.832 21.443 1.00 40.22 C
HETATM 3070 C22 CLR A1205 5.166 180.394 19.620 1.00 41.92 C
HETATM 3071 C23 CLR A1205 6.203 181.448 20.029 1.00 43.17 C
HETATM 3072 C24 CLR A1205 6.292 182.575 19.000 1.00 44.22 C
HETATM 3073 C25 CLR A1205 5.573 183.891 19.308 1.00 44.98 C
HETATM 3074 C26 CLR A1205 4.854 184.401 18.068 1.00 45.01 C
HETATM 3075 C27 CLR A1205 4.658 183.937 20.531 1.00 45.44 C
HETATM 3076 O1 CLR A1205 1.876 168.238 20.216 1.00 34.62 O
HETATM 3077 C1 OLB A1206 2.167 171.008 25.256 1.00 54.27 C
HETATM 3078 C2 OLB A1206 2.703 172.256 25.888 1.00 53.57 C
HETATM 3079 C3 OLB A1206 2.794 173.408 24.933 1.00 53.12 C
HETATM 3080 C4 OLB A1206 3.177 174.709 25.612 1.00 53.02 C
HETATM 3081 C5 OLB A1206 3.164 175.900 24.688 1.00 53.23 C
HETATM 3082 O19 OLB A1206 1.639 170.962 24.184 1.00 54.80 O
HETATM 3083 O20 OLB A1206 2.384 169.929 25.999 1.00 54.77 O
HETATM 3084 C21 OLB A1206 2.459 168.681 25.275 1.00 55.30 C
HETATM 3085 C22 OLB A1206 2.021 167.549 26.174 1.00 55.73 C
HETATM 3086 O23 OLB A1206 0.753 167.879 26.735 1.00 56.16 O
HETATM 3087 C24 OLB A1206 1.937 166.218 25.459 1.00 55.85 C
HETATM 3088 O25 OLB A1206 1.337 165.221 26.280 1.00 56.05 O
HETATM 3089 C6 OLB A1206 3.461 177.219 25.357 1.00 53.29 C
HETATM 3090 C7 OLB A1206 3.467 178.406 24.402 1.00 53.36 C
HETATM 3091 C8 OLB A1206 3.673 179.731 25.069 1.00 53.36 C
HETATM 3092 C1 OLA A1207 34.584 200.573 17.765 1.00 57.07 C
HETATM 3093 O1 OLA A1207 33.743 200.587 16.838 1.00 57.43 O
HETATM 3094 O2 OLA A1207 34.563 201.403 18.708 1.00 57.33 O
HETATM 3095 C2 OLA A1207 35.663 199.512 17.721 1.00 56.18 C
HETATM 3096 C3 OLA A1207 35.237 198.288 18.522 1.00 55.35 C
HETATM 3097 C4 OLA A1207 35.763 196.997 17.906 1.00 54.41 C
HETATM 3098 C5 OLA A1207 35.714 195.859 18.917 1.00 53.69 C
HETATM 3099 C6 OLA A1207 34.881 194.690 18.417 1.00 53.05 C
HETATM 3100 C7 OLA A1207 35.736 193.498 18.012 1.00 52.68 C
HETATM 3101 C8 OLA A1207 35.161 192.200 18.572 1.00 52.42 C
HETATM 3102 C9 OLA A1207 35.423 191.030 17.647 1.00 52.19 C
HETATM 3103 C1 OLA A1208 -2.977 165.015 13.138 1.00 62.27 C
HETATM 3104 O1 OLA A1208 -3.657 163.958 13.074 1.00 62.51 O
HETATM 3105 O2 OLA A1208 -1.918 165.099 13.805 1.00 62.35 O
HETATM 3106 C2 OLA A1208 -3.460 166.224 12.358 1.00 61.50 C
HETATM 3107 C3 OLA A1208 -2.902 167.536 12.904 1.00 60.78 C
HETATM 3108 C4 OLA A1208 -3.524 168.717 12.164 1.00 60.29 C
HETATM 3109 C5 OLA A1208 -2.656 169.966 12.266 1.00 59.98 C
HETATM 3110 C6 OLA A1208 -3.117 171.037 11.284 1.00 59.65 C
HETATM 3111 C7 OLA A1208 -3.222 172.392 11.970 1.00 59.51 C
HETATM 3112 C8 OLA A1208 -2.517 173.490 11.194 1.00 59.69 C
HETATM 3113 C9 OLA A1208 -3.384 173.968 10.056 1.00 59.93 C
HETATM 3114 C10 OLA A1208 -3.275 175.231 9.650 1.00 60.07 C
HETATM 3115 C12 OLA A1209 33.604 188.834 29.354 1.00 51.00 C
HETATM 3116 C13 OLA A1209 33.569 189.786 28.164 1.00 51.12 C
HETATM 3117 C14 OLA A1209 33.765 191.234 28.606 1.00 51.17 C
HETATM 3118 C15 OLA A1209 33.378 192.206 27.495 1.00 51.26 C
HETATM 3119 C16 OLA A1209 33.869 193.616 27.800 1.00 51.26 C
HETATM 3120 C17 OLA A1209 33.372 194.616 26.762 1.00 51.27 C
HETATM 3121 C18 OLA A1209 33.824 196.026 27.093 1.00 51.31 C
HETATM 3122 C1 OLA A1210 8.623 165.496 8.362 1.00 71.68 C
HETATM 3123 O1 OLA A1210 8.259 164.718 7.446 1.00 71.75 O
HETATM 3124 O2 OLA A1210 8.658 165.158 9.571 1.00 71.76 O
HETATM 3125 C2 OLA A1210 9.070 166.898 8.002 1.00 71.18 C
HETATM 3126 C3 OLA A1210 8.299 167.435 6.803 1.00 70.73 C
HETATM 3127 C4 OLA A1210 8.954 168.697 6.254 1.00 70.26 C
HETATM 3128 C5 OLA A1210 8.102 169.930 6.529 1.00 69.95 C
HETATM 3129 C6 OLA A1210 8.825 171.189 6.073 1.00 69.65 C
HETATM 3130 C7 OLA A1210 7.915 172.414 6.127 1.00 69.59 C
HETATM 3131 C8 OLA A1210 8.725 173.710 6.098 1.00 69.55 C
HETATM 3132 C9 OLA A1210 9.590 173.774 4.857 1.00 69.52 C
HETATM 3133 C10 OLA A1210 10.434 174.783 4.659 1.00 69.33 C
HETATM 3134 C11 OLA A1210 11.279 174.811 3.407 1.00 69.24 C
HETATM 3135 C12 OLA A1210 11.425 176.243 2.906 1.00 69.16 C
HETATM 3136 C13 OLA A1210 11.734 176.255 1.411 1.00 69.27 C
HETATM 3137 C13 OLA A1211 24.002 183.147 2.113 1.00 45.81 C
HETATM 3138 C14 OLA A1211 23.815 184.425 2.922 1.00 45.56 C
HETATM 3139 C15 OLA A1211 22.520 185.153 2.581 1.00 45.55 C
HETATM 3140 C16 OLA A1211 22.539 186.529 3.242 1.00 45.99 C
HETATM 3141 C17 OLA A1211 21.222 187.298 3.125 1.00 46.26 C
HETATM 3142 C18 OLA A1211 21.431 188.741 3.554 1.00 46.40 C
HETATM 3143 C1 OLA A1212 33.625 170.948 1.871 1.00 78.58 C
HETATM 3144 O1 OLA A1212 32.393 171.153 1.932 1.00 78.85 O
HETATM 3145 O2 OLA A1212 34.192 170.028 2.503 1.00 78.47 O
HETATM 3146 C2 OLA A1212 34.459 171.856 0.993 1.00 78.33 C
HETATM 3147 C3 OLA A1212 34.295 173.305 1.443 1.00 78.04 C
HETATM 3148 C4 OLA A1212 35.209 174.236 0.653 1.00 77.87 C
HETATM 3149 C5 OLA A1212 34.666 175.661 0.628 1.00 77.78 C
HETATM 3150 C13 OLA A1213 38.373 198.376 14.781 1.00 54.89 C
HETATM 3151 C14 OLA A1213 37.972 197.254 13.825 1.00 55.10 C
HETATM 3152 C15 OLA A1213 37.600 195.983 14.586 1.00 55.16 C
HETATM 3153 C16 OLA A1213 37.617 194.758 13.686 1.00 55.10 C
HETATM 3154 C17 OLA A1213 37.565 193.484 14.523 1.00 55.16 C
HETATM 3155 C12 OLA A1214 19.661 195.256 29.607 1.00 47.27 C
HETATM 3156 C13 OLA A1214 19.485 196.447 28.674 1.00 47.22 C
HETATM 3157 C14 OLA A1214 19.123 197.729 29.425 1.00 47.17 C
HETATM 3158 C15 OLA A1214 20.217 198.778 29.256 1.00 47.17 C
HETATM 3159 C16 OLA A1214 19.678 200.205 29.325 1.00 47.12 C
HETATM 3160 C17 OLA A1214 19.820 200.906 27.976 1.00 47.04 C
HETATM 3161 C18 OLA A1214 20.685 202.144 28.055 1.00 46.95 C
HETATM 3162 C1 OLA A1215 -0.229 165.485 17.716 1.00 51.79 C
HETATM 3163 O1 OLA A1215 0.114 165.211 16.554 1.00 52.34 O
HETATM 3164 O2 OLA A1215 -0.552 164.598 18.533 1.00 52.40 O
HETATM 3165 C2 OLA A1215 -0.231 166.935 18.136 1.00 50.45 C
HETATM 3166 C3 OLA A1215 -0.744 167.823 17.002 1.00 49.25 C
HETATM 3167 C4 OLA A1215 -1.096 169.208 17.539 1.00 48.23 C
HETATM 3168 C5 OLA A1215 -1.679 170.097 16.455 1.00 47.37 C
HETATM 3169 C6 OLA A1215 -1.218 171.537 16.629 1.00 46.65 C
HETATM 3170 C7 OLA A1215 -2.295 172.429 17.225 1.00 46.06 C
HETATM 3171 C8 OLA A1215 -1.948 173.898 17.001 1.00 45.56 C
HETATM 3172 C9 OLA A1215 -2.004 174.227 15.525 1.00 44.62 C
HETATM 3173 C10 OLA A1215 -1.783 175.451 15.029 1.00 43.80 C
HETATM 3174 C11 OLA A1215 -1.439 176.643 15.885 1.00 43.33 C
HETATM 3175 C12 OLA A1215 -0.870 177.756 15.015 1.00 43.27 C
HETATM 3176 C13 OLA A1215 -0.121 178.779 15.863 1.00 43.26 C
HETATM 3177 C1 OLA A1216 21.335 169.695 3.069 1.00 65.08 C
HETATM 3178 O1 OLA A1216 20.581 169.822 2.080 1.00 65.56 O
HETATM 3179 O2 OLA A1216 21.690 168.577 3.512 1.00 65.03 O
HETATM 3180 C2 OLA A1216 21.870 170.934 3.748 1.00 64.55 C
HETATM 3181 C3 OLA A1216 21.007 172.172 3.511 1.00 64.00 C
HETATM 3182 C4 OLA A1216 21.684 173.386 4.145 1.00 63.45 C
HETATM 3183 C5 OLA A1216 21.134 174.705 3.616 1.00 62.97 C
HETATM 3184 C6 OLA A1216 21.560 174.954 2.174 1.00 62.59 C
HETATM 3185 C7 OLA A1216 20.457 175.621 1.359 1.00 62.33 C
HETATM 3186 C8 OLA A1216 20.070 176.985 1.918 1.00 62.25 C
HETATM 3187 C9 OLA A1216 21.058 178.036 1.467 1.00 62.10 C
HETATM 3188 C1 OLA A1217 1.623 162.720 14.904 1.00 61.38 C
HETATM 3189 O1 OLA A1217 2.020 161.575 14.582 1.00 61.81 O
HETATM 3190 O2 OLA A1217 1.374 163.028 16.091 1.00 61.61 O
HETATM 3191 C2 OLA A1217 1.445 163.780 13.832 1.00 60.54 C
HETATM 3192 C3 OLA A1217 2.641 164.732 13.842 1.00 59.68 C
HETATM 3193 C4 OLA A1217 2.424 166.012 13.034 1.00 58.62 C
HETATM 3194 C5 OLA A1217 1.890 167.183 13.860 1.00 57.64 C
HETATM 3195 C6 OLA A1217 2.169 168.491 13.123 1.00 56.95 C
HETATM 3196 C7 OLA A1217 1.597 169.731 13.805 1.00 56.58 C
HETATM 3197 C8 OLA A1217 2.092 171.005 13.120 1.00 56.50 C
HETATM 3198 C9 OLA A1217 1.055 172.106 13.246 1.00 56.53 C
HETATM 3199 C10 OLA A1217 1.329 173.420 13.254 1.00 56.35 C
HETATM 3200 C11 OLA A1217 2.730 173.985 13.136 1.00 56.15 C
HETATM 3201 C12 OLA A1217 2.703 175.463 12.760 1.00 55.68 C
HETATM 3202 C13 OLA A1217 3.678 176.265 13.617 1.00 55.27 C
HETATM 3203 C14 OLA A1217 3.742 177.716 13.147 1.00 55.04 C
HETATM 3204 C15 OLA A1217 4.305 178.635 14.225 1.00 54.78 C
HETATM 3205 C1 OLA A1218 7.049 172.920 33.673 1.00 52.43 C
HETATM 3206 O1 OLA A1218 7.685 171.843 33.717 1.00 52.87 O
HETATM 3207 O2 OLA A1218 5.804 172.940 33.722 1.00 52.80 O
HETATM 3208 C2 OLA A1218 7.815 174.221 33.570 1.00 51.74 C
HETATM 3209 C3 OLA A1218 6.949 175.398 33.106 1.00 51.16 C
HETATM 3210 C4 OLA A1218 7.864 176.539 32.660 1.00 50.81 C
HETATM 3211 C5 OLA A1218 7.123 177.767 32.147 1.00 50.51 C
HETATM 3212 C6 OLA A1218 7.805 179.059 32.585 1.00 50.00 C
HETATM 3213 C7 OLA A1218 8.901 179.491 31.616 1.00 49.49 C
HETATM 3214 C8 OLA A1218 9.044 181.009 31.593 1.00 49.09 C
HETATM 3215 C12 OLA A1219 10.029 194.196 17.230 1.00 43.08 C
HETATM 3216 C13 OLA A1219 10.490 193.106 18.200 1.00 43.15 C
HETATM 3217 C14 OLA A1219 10.234 191.697 17.668 1.00 43.12 C
HETATM 3218 C15 OLA A1219 9.016 191.098 18.351 1.00 43.45 C
HETATM 3219 C16 OLA A1219 8.888 189.595 18.093 1.00 43.86 C
HETATM 3220 C17 OLA A1219 7.942 188.946 19.111 1.00 43.85 C
HETATM 3221 C18 OLA A1219 8.194 187.458 19.264 1.00 43.81 C
HETATM 3222 C11 OLA A1220 10.420 192.389 10.515 1.00 60.66 C
HETATM 3223 C12 OLA A1220 9.775 191.015 10.690 1.00 60.89 C
HETATM 3224 C13 OLA A1220 9.227 190.799 12.103 1.00 60.90 C
HETATM 3225 C14 OLA A1220 8.534 189.443 12.220 1.00 60.90 C
HETATM 3226 C15 OLA A1220 8.299 189.042 13.675 1.00 60.80 C
HETATM 3227 C10 OLC A1221 34.097 188.001 24.269 1.00 55.22 C
HETATM 3228 C9 OLC A1221 33.352 189.092 24.107 1.00 55.55 C
HETATM 3229 C8 OLC A1221 33.990 190.444 23.858 1.00 55.91 C
HETATM 3230 C24 OLC A1221 33.708 203.264 24.325 1.00 65.85 C
HETATM 3231 C7 OLC A1221 33.037 191.384 23.124 1.00 56.25 C
HETATM 3232 C6 OLC A1221 33.557 192.816 23.104 1.00 56.80 C
HETATM 3233 C5 OLC A1221 32.469 193.813 22.709 1.00 57.51 C
HETATM 3234 C4 OLC A1221 33.069 195.121 22.200 1.00 58.45 C
HETATM 3235 C3 OLC A1221 32.097 196.299 22.272 1.00 59.61 C
HETATM 3236 C2 OLC A1221 32.675 197.363 23.196 1.00 61.06 C
HETATM 3237 C21 OLC A1221 32.659 201.258 23.209 1.00 64.52 C
HETATM 3238 C1 OLC A1221 32.219 198.772 22.886 1.00 62.60 C
HETATM 3239 C22 OLC A1221 32.781 202.068 24.501 1.00 65.29 C
HETATM 3240 O19 OLC A1221 31.289 198.992 22.129 1.00 62.82 O
HETATM 3241 O25 OLC A1221 33.487 204.206 25.388 1.00 66.27 O
HETATM 3242 O23 OLC A1221 31.492 202.544 24.903 1.00 65.57 O
HETATM 3243 O20 OLC A1221 32.918 199.887 23.519 1.00 63.76 O
HETATM 3244 O HOH A1301 24.500 162.775 2.028 1.00 59.23 O
HETATM 3245 O HOH A1302 14.335 206.914 17.622 1.00 48.49 O
HETATM 3246 O HOH A1303 25.129 166.068 11.144 1.00 46.37 O
HETATM 3247 O HOH A1304 23.483 164.639 33.353 1.00 50.87 O
HETATM 3248 O HOH A1305 19.533 167.898 16.157 1.00 31.52 O
HETATM 3249 O HOH A1306 18.888 169.871 23.011 1.00 45.15 O
HETATM 3250 O HOH A1307 22.885 207.825 21.440 1.00 51.63 O
HETATM 3251 O HOH A1308 16.306 196.709 19.074 1.00 33.62 O
HETATM 3252 O HOH A1309 13.086 162.238 11.176 1.00 56.29 O
HETATM 3253 O HOH A1310 18.984 191.289 13.081 1.00 33.26 O
HETATM 3254 O HOH A1311 11.412 167.907 15.831 1.00 25.25 O
HETATM 3255 O HOH A1312 2.297 166.413 22.077 1.00 46.26 O
HETATM 3256 O HOH A1313 23.418 184.586 14.196 1.00 26.99 O
HETATM 3257 O HOH A1314 20.751 163.388 18.919 1.00 53.61 O
HETATM 3258 O HOH A1315 18.123 166.884 23.845 1.00 38.40 O
HETATM 3259 O HOH A1316 10.290 160.528 20.642 1.00 50.17 O
HETATM 3260 O HOH A1317 25.103 195.726 14.692 1.00 35.62 O
HETATM 3261 O HOH A1318 0.142 162.574 20.137 1.00 75.39 O
HETATM 3262 O HOH A1319 25.298 193.095 13.699 1.00 29.72 O
HETATM 3263 O HOH A1320 25.582 174.601 18.787 1.00 28.95 O
HETATM 3264 O HOH A1321 26.031 191.722 21.530 1.00 28.40 O
HETATM 3265 O HOH A1322 26.268 161.378 22.193 1.00 33.46 O
HETATM 3266 O HOH A1323 26.077 191.812 25.564 1.00 37.56 O
HETATM 3267 O HOH A1324 20.915 182.512 24.348 1.00 23.01 O
HETATM 3268 O HOH A1325 -3.044 253.004 24.311 1.00 60.80 O
HETATM 3269 O HOH A1326 25.006 177.047 15.991 1.00 29.47 O
HETATM 3270 O HOH A1327 32.799 155.981 25.229 1.00 59.16 O
HETATM 3271 O HOH A1328 27.241 191.248 6.883 1.00 45.39 O
HETATM 3272 O HOH A1329 28.799 177.227 19.556 1.00 24.54 O
HETATM 3273 O HOH A1330 16.136 165.125 21.177 1.00 57.40 O
HETATM 3274 O HOH A1331 20.830 191.154 15.239 1.00 46.19 O
HETATM 3275 O HOH A1332 15.098 176.392 22.017 1.00 23.00 O
HETATM 3276 O HOH A1333 16.132 179.184 12.612 1.00 27.15 O
HETATM 3277 O HOH A1334 27.549 176.746 17.033 1.00 24.92 O
HETATM 3278 O HOH A1335 15.170 169.967 17.911 1.00 33.27 O
HETATM 3279 O HOH A1336 19.472 181.588 22.291 1.00 29.83 O
HETATM 3280 O HOH A1337 9.687 164.806 18.424 1.00 52.21 O
HETATM 3281 O HOH A1338 22.196 186.277 15.750 1.00 35.09 O
HETATM 3282 O HOH A1339 23.920 190.933 11.681 1.00 36.41 O
HETATM 3283 O HOH A1340 25.671 162.791 26.897 1.00 42.68 O
HETATM 3284 O HOH A1341 28.003 174.330 17.738 1.00 35.23 O
HETATM 3285 O HOH A1342 27.644 159.042 22.442 1.00 26.27 O
HETATM 3286 O HOH A1343 17.533 165.975 29.010 1.00 61.67 O
HETATM 3287 O HOH A1344 18.028 197.183 17.007 1.00 41.32 O
HETATM 3288 O HOH A1345 21.050 166.083 4.753 1.00 58.55 O
HETATM 3289 O HOH A1346 5.346 238.148 30.970 1.00 85.75 O
HETATM 3290 O HOH A1347 18.095 182.641 20.281 1.00 25.05 O
HETATM 3291 O HOH A1348 7.692 169.273 30.487 1.00 50.81 O
HETATM 3292 O HOH A1349 25.710 194.191 24.888 1.00 34.41 O
HETATM 3293 O HOH A1350 5.123 162.160 12.949 1.00 64.79 O
HETATM 3294 O HOH A1351 35.890 161.088 16.342 1.00 53.34 O
HETATM 3295 O HOH A1352 25.801 161.038 24.880 1.00 28.15 O
HETATM 3296 O HOH A1353 4.185 243.398 27.548 1.00 60.64 O
HETATM 3297 O HOH A1354 24.974 186.628 17.514 1.00 54.54 O
HETATM 3298 O HOH A1355 26.262 166.545 34.796 1.00 69.50 O
HETATM 3299 O HOH A1356 16.812 162.866 9.151 1.00 44.62 O
HETATM 3300 O HOH A1357 33.806 165.878 30.348 1.00 59.46 O
HETATM 3301 O HOH A1358 27.477 160.684 14.318 1.00 56.36 O
HETATM 3302 O HOH A1359 21.726 166.976 17.640 1.00 30.37 O
HETATM 3303 O HOH A1360 -5.789 255.982 26.444 1.00 42.29 O
HETATM 3304 O HOH A1361 17.436 165.018 12.544 1.00 47.90 O
HETATM 3305 O HOH A1362 29.873 161.766 29.376 1.00 55.75 O
HETATM 3306 O HOH A1363 25.390 209.389 23.023 1.00 54.14 O
HETATM 3307 O HOH A1364 28.970 170.289 35.205 1.00 62.24 O
HETATM 3308 O HOH A1365 21.056 207.410 17.950 1.00 60.26 O
HETATM 3309 O HOH A1366 19.993 167.244 33.424 1.00 68.88 O
HETATM 3310 O HOH A1367 17.683 163.894 19.375 1.00 51.40 O
HETATM 3311 O HOH A1368 17.160 166.161 26.192 1.00 37.92 O
HETATM 3312 O HOH A1369 17.551 164.595 6.029 1.00 42.87 O
HETATM 3313 O HOH A1370 9.012 166.483 16.718 1.00 35.55 O
HETATM 3314 O HOH A1371 3.468 163.603 21.894 1.00 40.69 O
HETATM 3315 O HOH A1372 15.067 167.442 28.656 1.00 31.88 O
HETATM 3316 O HOH A1373 11.410 168.952 32.264 1.00 40.14 O
HETATM 3317 O HOH A1374 -7.923 253.279 18.423 1.00 62.96 O
HETATM 3318 O HOH A1375 21.721 156.936 27.329 1.00 56.60 O
HETATM 3319 O HOH A1376 24.410 165.048 6.023 1.00 66.08 O
HETATM 3320 O HOH A1377 5.894 241.417 28.520 1.00 60.43 O
HETATM 3321 O HOH A1378 20.122 165.964 2.203 1.00 67.01 O
HETATM 3322 O HOH A1379 18.894 208.151 7.617 1.00 45.81 O
HETATM 3323 O HOH A1380 26.904 162.654 12.536 1.00 64.03 O
HETATM 3324 O HOH A1381 17.719 167.602 32.325 1.00 47.86 O
HETATM 3325 O HOH A1382 37.572 155.711 15.580 1.00 61.72 O
HETATM 3326 O HOH A1383 7.619 167.369 27.830 1.00 61.24 O
HETATM 3327 O HOH A1384 38.054 158.715 19.333 1.00 66.15 O
HETATM 3328 O HOH A1385 13.552 166.058 23.766 1.00 48.21 O
HETATM 3329 O HOH A1386 16.314 162.622 12.178 1.00 65.83 O
HETATM 3330 O HOH A1387 31.486 163.326 31.269 1.00 56.04 O
HETATM 3331 O HOH A1388 24.397 163.573 12.343 1.00 54.04 O
HETATM 3332 O HOH A1389 21.681 164.628 17.135 1.00 44.98 O
CONECT 410 2992
CONECT 551 1204
CONECT 567 1113
CONECT 587 1248
CONECT 697 2992
CONECT 1113 567
CONECT 1204 551
CONECT 1248 587
CONECT 2576 2597
CONECT 2597 2576
CONECT 2967 2972 2978 2987
CONECT 2968 2984
CONECT 2969 2970 2978
CONECT 2970 2969 2971 2975
CONECT 2971 2970 2972 2989
CONECT 2972 2967 2971
CONECT 2973 2974 2989 2990
CONECT 2974 2973
CONECT 2975 2970 2976
CONECT 2976 2975 2977
CONECT 2977 2976
CONECT 2978 2967 2969 2979
CONECT 2979 2978 2980 2988
CONECT 2980 2979 2981 2983
CONECT 2981 2980 2982 2987
CONECT 2982 2981
CONECT 2983 2980 2986 2991
CONECT 2984 2968 2985 2986
CONECT 2985 2984 2991
CONECT 2986 2983 2984
CONECT 2987 2967 2981
CONECT 2988 2979
CONECT 2989 2971 2973
CONECT 2990 2973
CONECT 2991 2983 2985
CONECT 2992 410 697 3281 3297
CONECT 2993 2994 3002
CONECT 2994 2993 2995
CONECT 2995 2994 2996 3020
CONECT 2996 2995 2997
CONECT 2997 2996 2998 3002
CONECT 2998 2997 2999
CONECT 2999 2998 3000
CONECT 3000 2999 3001 3006
CONECT 3001 3000 3002 3003
CONECT 3002 2993 2997 3001 3011
CONECT 3003 3001 3004
CONECT 3004 3003 3005
CONECT 3005 3004 3006 3009 3010
CONECT 3006 3000 3005 3007
CONECT 3007 3006 3008
CONECT 3008 3007 3009
CONECT 3009 3005 3008 3012
CONECT 3010 3005
CONECT 3011 3002
CONECT 3012 3009 3013 3014
CONECT 3013 3012
CONECT 3014 3012 3015
CONECT 3015 3014 3016
CONECT 3016 3015 3017
CONECT 3017 3016 3018 3019
CONECT 3018 3017
CONECT 3019 3017
CONECT 3020 2995
CONECT 3021 3022 3030
CONECT 3022 3021 3023
CONECT 3023 3022 3024 3048
CONECT 3024 3023 3025
CONECT 3025 3024 3026 3030
CONECT 3026 3025 3027
CONECT 3027 3026 3028
CONECT 3028 3027 3029 3034
CONECT 3029 3028 3030 3031
CONECT 3030 3021 3025 3029 3039
CONECT 3031 3029 3032
CONECT 3032 3031 3033
CONECT 3033 3032 3034 3037 3038
CONECT 3034 3028 3033 3035
CONECT 3035 3034 3036
CONECT 3036 3035 3037
CONECT 3037 3033 3036 3040
CONECT 3038 3033
CONECT 3039 3030
CONECT 3040 3037 3041 3042
CONECT 3041 3040
CONECT 3042 3040 3043
CONECT 3043 3042 3044
CONECT 3044 3043 3045
CONECT 3045 3044 3046 3047
CONECT 3046 3045
CONECT 3047 3045
CONECT 3048 3023
CONECT 3049 3050 3058
CONECT 3050 3049 3051
CONECT 3051 3050 3052 3076
CONECT 3052 3051 3053
CONECT 3053 3052 3054 3058
CONECT 3054 3053 3055
CONECT 3055 3054 3056
CONECT 3056 3055 3057 3062
CONECT 3057 3056 3058 3059
CONECT 3058 3049 3053 3057 3067
CONECT 3059 3057 3060
CONECT 3060 3059 3061
CONECT 3061 3060 3062 3065 3066
CONECT 3062 3056 3061 3063
CONECT 3063 3062 3064
CONECT 3064 3063 3065
CONECT 3065 3061 3064 3068
CONECT 3066 3061
CONECT 3067 3058
CONECT 3068 3065 3069 3070
CONECT 3069 3068
CONECT 3070 3068 3071
CONECT 3071 3070 3072
CONECT 3072 3071 3073
CONECT 3073 3072 3074 3075
CONECT 3074 3073
CONECT 3075 3073
CONECT 3076 3051
CONECT 3077 3078 3082 3083
CONECT 3078 3077 3079
CONECT 3079 3078 3080
CONECT 3080 3079 3081
CONECT 3081 3080 3089
CONECT 3082 3077
CONECT 3083 3077 3084
CONECT 3084 3083 3085
CONECT 3085 3084 3086 3087
CONECT 3086 3085
CONECT 3087 3085 3088
CONECT 3088 3087
CONECT 3089 3081 3090
CONECT 3090 3089 3091
CONECT 3091 3090
CONECT 3092 3093 3094 3095
CONECT 3093 3092
CONECT 3094 3092
CONECT 3095 3092 3096
CONECT 3096 3095 3097
CONECT 3097 3096 3098
CONECT 3098 3097 3099
CONECT 3099 3098 3100
CONECT 3100 3099 3101
CONECT 3101 3100 3102
CONECT 3102 3101
CONECT 3103 3104 3105 3106
CONECT 3104 3103
CONECT 3105 3103
CONECT 3106 3103 3107
CONECT 3107 3106 3108
CONECT 3108 3107 3109
CONECT 3109 3108 3110
CONECT 3110 3109 3111
CONECT 3111 3110 3112
CONECT 3112 3111 3113
CONECT 3113 3112 3114
CONECT 3114 3113
CONECT 3115 3116
CONECT 3116 3115 3117
CONECT 3117 3116 3118
CONECT 3118 3117 3119
CONECT 3119 3118 3120
CONECT 3120 3119 3121
CONECT 3121 3120
CONECT 3122 3123 3124 3125
CONECT 3123 3122
CONECT 3124 3122
CONECT 3125 3122 3126
CONECT 3126 3125 3127
CONECT 3127 3126 3128
CONECT 3128 3127 3129
CONECT 3129 3128 3130
CONECT 3130 3129 3131
CONECT 3131 3130 3132
CONECT 3132 3131 3133
CONECT 3133 3132 3134
CONECT 3134 3133 3135
CONECT 3135 3134 3136
CONECT 3136 3135
CONECT 3137 3138
CONECT 3138 3137 3139
CONECT 3139 3138 3140
CONECT 3140 3139 3141
CONECT 3141 3140 3142
CONECT 3142 3141
CONECT 3143 3144 3145 3146
CONECT 3144 3143
CONECT 3145 3143
CONECT 3146 3143 3147
CONECT 3147 3146 3148
CONECT 3148 3147 3149
CONECT 3149 3148
CONECT 3150 3151
CONECT 3151 3150 3152
CONECT 3152 3151 3153
CONECT 3153 3152 3154
CONECT 3154 3153
CONECT 3155 3156
CONECT 3156 3155 3157
CONECT 3157 3156 3158
CONECT 3158 3157 3159
CONECT 3159 3158 3160
CONECT 3160 3159 3161
CONECT 3161 3160
CONECT 3162 3163 3164 3165
CONECT 3163 3162
CONECT 3164 3162
CONECT 3165 3162 3166
CONECT 3166 3165 3167
CONECT 3167 3166 3168
CONECT 3168 3167 3169
CONECT 3169 3168 3170
CONECT 3170 3169 3171
CONECT 3171 3170 3172
CONECT 3172 3171 3173
CONECT 3173 3172 3174
CONECT 3174 3173 3175
CONECT 3175 3174 3176
CONECT 3176 3175
CONECT 3177 3178 3179 3180
CONECT 3178 3177
CONECT 3179 3177
CONECT 3180 3177 3181
CONECT 3181 3180 3182
CONECT 3182 3181 3183
CONECT 3183 3182 3184
CONECT 3184 3183 3185
CONECT 3185 3184 3186
CONECT 3186 3185 3187
CONECT 3187 3186
CONECT 3188 3189 3190 3191
CONECT 3189 3188
CONECT 3190 3188
CONECT 3191 3188 3192
CONECT 3192 3191 3193
CONECT 3193 3192 3194
CONECT 3194 3193 3195
CONECT 3195 3194 3196
CONECT 3196 3195 3197
CONECT 3197 3196 3198
CONECT 3198 3197 3199
CONECT 3199 3198 3200
CONECT 3200 3199 3201
CONECT 3201 3200 3202
CONECT 3202 3201 3203
CONECT 3203 3202 3204
CONECT 3204 3203
CONECT 3205 3206 3207 3208
CONECT 3206 3205
CONECT 3207 3205
CONECT 3208 3205 3209
CONECT 3209 3208 3210
CONECT 3210 3209 3211
CONECT 3211 3210 3212
CONECT 3212 3211 3213
CONECT 3213 3212 3214
CONECT 3214 3213
CONECT 3215 3216
CONECT 3216 3215 3217
CONECT 3217 3216 3218
CONECT 3218 3217 3219
CONECT 3219 3218 3220
CONECT 3220 3219 3221
CONECT 3221 3220
CONECT 3222 3223
CONECT 3223 3222 3224
CONECT 3224 3223 3225
CONECT 3225 3224 3226
CONECT 3226 3225
CONECT 3227 3228
CONECT 3228 3227 3229
CONECT 3229 3228 3231
CONECT 3230 3239 3241
CONECT 3231 3229 3232
CONECT 3232 3231 3233
CONECT 3233 3232 3234
CONECT 3234 3233 3235
CONECT 3235 3234 3236
CONECT 3236 3235 3238
CONECT 3237 3239 3243
CONECT 3238 3236 3240 3243
CONECT 3239 3230 3237 3242
CONECT 3240 3238
CONECT 3241 3230
CONECT 3242 3239
CONECT 3243 3237 3238
CONECT 3281 2992
CONECT 3297 2992
MASTER 522 0 21 19 2 0 25 6 3304 1 289 34
END