HEADER SIGNALING PROTEIN 07-OCT-18 6IIU
TITLE CRYSTAL STRUCTURE OF THE HUMAN THROMBOXANE A2 RECEPTOR BOUND TO
TITLE 2 RAMATROBAN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SOLUBLE CYTOCHROME B562,THROMBOXANE A2 RECEPTOR,RUBREDOXIN,
COMPND 3 THROMBOXANE A2 RECEPTOR;
COMPND 4 CHAIN: A;
COMPND 5 SYNONYM: CYTOCHROME B-562,TXA2-R,PROSTANOID TP RECEPTOR,RD,TXA2-R,
COMPND 6 PROSTANOID TP RECEPTOR;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES;
COMPND 9 OTHER_DETAILS: GPCR PROTEIN FOLLOWED A TRADITIONAL FUSION STRATEGY BY
COMPND 10 INTRODUCING A BRIL FUSION PROTEIN AT THE N TERMINUS OF THE RECEPTOR
COMPND 11 AND A RUBREDOXIN FUSION PROTEIN IN THE THIRD INTRACELLULAR LOOP OF
COMPND 12 THE RECEPTOR. THE RESIDUES FROM BRIL WERE NUMBERED WITH 1001-1106 AND
COMPND 13 THE RESIDUES FROM RUBREDOXIN WERE NUMBERED WITH 2001 TO 2054, WITH
COMPND 14 2001 AND 2054 COVALENTLY LINKED TO RESIDUES 228 AND 237 OF THE
COMPND 15 RECEPTOR, RESPECTIVELY.
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI, HOMO SAPIENS, CLOSTRIDIUM
SOURCE 3 PASTEURIANUM;
SOURCE 4 ORGANISM_COMMON: HUMAN;
SOURCE 5 ORGANISM_TAXID: 562, 9606, 1501;
SOURCE 6 GENE: CYBC, TBXA2R;
SOURCE 7 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS GPCR, COMPLEX, ANTAGONIST, SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR H.FAN,Q.ZHAO,B.WU
REVDAT 2 26-DEC-18 6IIU 1 JRNL
REVDAT 1 19-DEC-18 6IIU 0
JRNL AUTH H.FAN,S.CHEN,X.YUAN,S.HAN,H.ZHANG,W.XIA,Y.XU,Q.ZHAO,B.WU
JRNL TITL STRUCTURAL BASIS FOR LIGAND RECOGNITION OF THE HUMAN
JRNL TITL 2 THROMBOXANE A2RECEPTOR.
JRNL REF NAT. CHEM. BIOL. V. 15 27 2019
JRNL REFN ESSN 1552-4469
JRNL PMID 30510189
JRNL DOI 10.1038/S41589-018-0170-9
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.10.2
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) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.53
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.6
REMARK 3 NUMBER OF REFLECTIONS : 27682
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) : 0.199
REMARK 3 R VALUE (WORKING SET) : 0.198
REMARK 3 FREE R VALUE : 0.218
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1411
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.000
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 14
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.59
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 85.52
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2503
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2180
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2382
REMARK 3 BIN R VALUE (WORKING SET) : 0.2170
REMARK 3 BIN FREE R VALUE : 0.2450
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.83
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 121
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.000
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3458
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 96
REMARK 3 SOLVENT ATOMS : 11
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 66.72
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 75.40
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.69370
REMARK 3 B22 (A**2) : 0.72030
REMARK 3 B33 (A**2) : -0.02660
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) : 0.350
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) : 0.191
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.256
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.196
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 : 0.933
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.933
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 3637 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 4967 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 1208 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 69 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 552 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 3637 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : 0 ; 5.000 ; SEMIHARMONIC
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 478 ; 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 : 4258 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.09
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.65
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 18.83
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 19.8658 160.6780 142.3280
REMARK 3 T TENSOR
REMARK 3 T11: -0.0540 T22: -0.2640
REMARK 3 T33: -0.1770 T12: -0.0105
REMARK 3 T13: -0.0365 T23: 0.0064
REMARK 3 L TENSOR
REMARK 3 L11: 0.8061 L22: 4.5865
REMARK 3 L33: 0.9193 L12: 1.4815
REMARK 3 L13: -0.2299 L23: -0.8660
REMARK 3 S TENSOR
REMARK 3 S11: 0.0887 S12: -0.0413 S13: 0.0043
REMARK 3 S21: 0.3724 S22: -0.0915 S23: -0.0857
REMARK 3 S31: -0.0846 S32: 0.0146 S33: 0.0029
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6IIU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 23-OCT-18.
REMARK 100 THE DEPOSITION ID IS D_1300009245.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-DEC-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL41XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 27682
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.6
REMARK 200 DATA REDUNDANCY : 5.800
REMARK 200 R MERGE (I) : 0.15600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.64
REMARK 200 COMPLETENESS FOR SHELL (%) : 89.9
REMARK 200 DATA REDUNDANCY IN SHELL : 5.70
REMARK 200 R MERGE FOR SHELL (I) : 0.64900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 4PXZ, 1M6T, 1IRO
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 67.51
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.79
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MAGNESIUM ACETATE, PEG 500 DME,
REMARK 280 LIPIDIC CUBIC PHASE, TEMPERATURE 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 64.06500
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 64.06500
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 40.58000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 77.54000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 40.58000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 77.54000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 64.06500
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 40.58000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 77.54000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 64.06500
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 40.58000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 77.54000
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: 750 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21430 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 ASP A 991
REMARK 465 TYR A 992
REMARK 465 LYS A 993
REMARK 465 ASP A 994
REMARK 465 ASP A 995
REMARK 465 ASP A 996
REMARK 465 ASP A 997
REMARK 465 GLY A 998
REMARK 465 ALA A 999
REMARK 465 PRO A 1000
REMARK 465 ARG A 53
REMARK 465 GLN A 54
REMARK 465 GLY A 55
REMARK 465 GLY A 56
REMARK 465 SER A 57
REMARK 465 HIS A 58
REMARK 465 GLU A 324
REMARK 465 PHE A 325
REMARK 465 LEU A 326
REMARK 465 GLU A 327
REMARK 465 VAL A 328
REMARK 465 LEU A 329
REMARK 465 PHE A 330
REMARK 465 GLN A 331
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 470 LYS A1051 CG CD CE NZ
REMARK 470 GLU A1057 CG CD OE1 OE2
REMARK 470 LYS A1059 CG CD CE NZ
REMARK 470 GLU A1081 CG CD OE1 OE2
REMARK 470 LYS A1083 CG CD CE NZ
REMARK 470 GLU A1086 CG CD OE1 OE2
REMARK 470 LYS A1095 CG CD CE NZ
REMARK 470 LEU A 19 CG CD1 CD2
REMARK 470 GLU A 20 CG CD OE1 OE2
REMARK 470 ARG A 23 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 24 CG CD1 CD2
REMARK 470 ARG A 136 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 140 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 190 CG CD OE1 OE2
REMARK 470 LYS A2002 CG CD CE NZ
REMARK 470 GLU A2050 CG CD OE1 OE2
REMARK 470 ASN A 272 CG OD1 ND2
REMARK 470 ARG A 313 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 322 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 323 CG CD1 CD2
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 ALA A1020 145.09 -38.58
REMARK 500 ALA A 26 109.29 -54.83
REMARK 500 PRO A 141 108.90 -42.31
REMARK 500 THR A2007 20.43 -76.91
REMARK 500 ASP A2019 71.27 -156.31
REMARK 500 ASN A 272 -72.26 -47.88
REMARK 500 ARG A 322 32.29 -93.67
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 CYS A 11 10.84
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 OLC A 9004
REMARK 610 OLC A 9005
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A9002 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A2006 SG
REMARK 620 2 CYS A2009 SG 111.9
REMARK 620 3 CYS A2039 SG 117.0 96.2
REMARK 620 4 CYS A2042 SG 106.2 114.2 111.5
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 A8X A 9001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 9002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLR A 9003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 9004
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 9005
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 9006
DBREF 6IIU A 1001 1106 UNP P0ABE7 C562_ECOLX 23 128
DBREF 6IIU A 10 228 UNP P21731 TA2R_HUMAN 10 228
DBREF 6IIU A 2001 2054 UNP P00268 RUBR_CLOPA 1 54
DBREF 6IIU A 237 323 UNP P21731 TA2R_HUMAN 237 323
SEQADV 6IIU ASP A 991 UNP P0ABE7 EXPRESSION TAG
SEQADV 6IIU TYR A 992 UNP P0ABE7 EXPRESSION TAG
SEQADV 6IIU LYS A 993 UNP P0ABE7 EXPRESSION TAG
SEQADV 6IIU ASP A 994 UNP P0ABE7 EXPRESSION TAG
SEQADV 6IIU ASP A 995 UNP P0ABE7 EXPRESSION TAG
SEQADV 6IIU ASP A 996 UNP P0ABE7 EXPRESSION TAG
SEQADV 6IIU ASP A 997 UNP P0ABE7 EXPRESSION TAG
SEQADV 6IIU GLY A 998 UNP P0ABE7 EXPRESSION TAG
SEQADV 6IIU ALA A 999 UNP P0ABE7 EXPRESSION TAG
SEQADV 6IIU PRO A 1000 UNP P0ABE7 EXPRESSION TAG
SEQADV 6IIU TRP A 1007 UNP P0ABE7 MET 29 ENGINEERED MUTATION
SEQADV 6IIU ILE A 1102 UNP P0ABE7 HIS 124 ENGINEERED MUTATION
SEQADV 6IIU LEU A 1106 UNP P0ABE7 ARG 128 ENGINEERED MUTATION
SEQADV 6IIU ALA A 247 UNP P21731 LEU 247 ENGINEERED MUTATION
SEQADV 6IIU GLU A 324 UNP P21731 EXPRESSION TAG
SEQADV 6IIU PHE A 325 UNP P21731 EXPRESSION TAG
SEQADV 6IIU LEU A 326 UNP P21731 EXPRESSION TAG
SEQADV 6IIU GLU A 327 UNP P21731 EXPRESSION TAG
SEQADV 6IIU VAL A 328 UNP P21731 EXPRESSION TAG
SEQADV 6IIU LEU A 329 UNP P21731 EXPRESSION TAG
SEQADV 6IIU PHE A 330 UNP P21731 EXPRESSION TAG
SEQADV 6IIU GLN A 331 UNP P21731 EXPRESSION TAG
SEQRES 1 A 484 ASP TYR LYS ASP ASP ASP ASP GLY ALA PRO ALA ASP LEU
SEQRES 2 A 484 GLU ASP ASN TRP GLU THR LEU ASN ASP ASN LEU LYS VAL
SEQRES 3 A 484 ILE GLU LYS ALA ASP ASN ALA ALA GLN VAL LYS ASP ALA
SEQRES 4 A 484 LEU THR LYS MET ARG ALA ALA ALA LEU ASP ALA GLN LYS
SEQRES 5 A 484 ALA THR PRO PRO LYS LEU GLU ASP LYS SER PRO ASP SER
SEQRES 6 A 484 PRO GLU MET LYS ASP PHE ARG HIS GLY PHE ASP ILE LEU
SEQRES 7 A 484 VAL GLY GLN ILE ASP ASP ALA LEU LYS LEU ALA ASN GLU
SEQRES 8 A 484 GLY LYS VAL LYS GLU ALA GLN ALA ALA ALA GLU GLN LEU
SEQRES 9 A 484 LYS THR THR ARG ASN ALA TYR ILE GLN LYS TYR LEU PRO
SEQRES 10 A 484 CYS PHE ARG PRO THR ASN ILE THR LEU GLU GLU ARG ARG
SEQRES 11 A 484 LEU ILE ALA SER PRO TRP PHE ALA ALA SER PHE CYS VAL
SEQRES 12 A 484 VAL GLY LEU ALA SER ASN LEU LEU ALA LEU SER VAL LEU
SEQRES 13 A 484 ALA GLY ALA ARG GLN GLY GLY SER HIS THR ARG SER SER
SEQRES 14 A 484 PHE LEU THR PHE LEU CYS GLY LEU VAL LEU THR ASP PHE
SEQRES 15 A 484 LEU GLY LEU LEU VAL THR GLY THR ILE VAL VAL SER GLN
SEQRES 16 A 484 HIS ALA ALA LEU PHE GLU TRP HIS ALA VAL ASP PRO GLY
SEQRES 17 A 484 CYS ARG LEU CYS ARG PHE MET GLY VAL VAL MET ILE PHE
SEQRES 18 A 484 PHE GLY LEU SER PRO LEU LEU LEU GLY ALA ALA MET ALA
SEQRES 19 A 484 SER GLU ARG TYR LEU GLY ILE THR ARG PRO PHE SER ARG
SEQRES 20 A 484 PRO ALA VAL ALA SER GLN ARG ARG ALA TRP ALA THR VAL
SEQRES 21 A 484 GLY LEU VAL TRP ALA ALA ALA LEU ALA LEU GLY LEU LEU
SEQRES 22 A 484 PRO LEU LEU GLY VAL GLY ARG TYR THR VAL GLN TYR PRO
SEQRES 23 A 484 GLY SER TRP CYS PHE LEU THR LEU GLY ALA GLU SER GLY
SEQRES 24 A 484 ASP VAL ALA PHE GLY LEU LEU PHE SER MET LEU GLY GLY
SEQRES 25 A 484 LEU SER VAL GLY LEU SER PHE LEU LEU ASN THR VAL SER
SEQRES 26 A 484 VAL ALA THR LEU CYS HIS VAL TYR HIS GLY MET LYS LYS
SEQRES 27 A 484 TYR THR CYS THR VAL CYS GLY TYR ILE TYR ASN PRO GLU
SEQRES 28 A 484 ASP GLY ASP PRO ASP ASN GLY VAL ASN PRO GLY THR ASP
SEQRES 29 A 484 PHE LYS ASP ILE PRO ASP ASP TRP VAL CYS PRO LEU CYS
SEQRES 30 A 484 GLY VAL GLY LYS ASP GLN PHE GLU GLU VAL GLU GLU ARG
SEQRES 31 A 484 ASP SER GLU VAL GLU MET MET ALA GLN ALA LEU GLY ILE
SEQRES 32 A 484 MET VAL VAL ALA SER VAL CYS TRP LEU PRO LEU LEU VAL
SEQRES 33 A 484 PHE ILE ALA GLN THR VAL LEU ARG ASN PRO PRO ALA MET
SEQRES 34 A 484 SER PRO ALA GLY GLN LEU SER ARG THR THR GLU LYS GLU
SEQRES 35 A 484 LEU LEU ILE TYR LEU ARG VAL ALA THR TRP ASN GLN ILE
SEQRES 36 A 484 LEU ASP PRO TRP VAL TYR ILE LEU PHE ARG ARG ALA VAL
SEQRES 37 A 484 LEU ARG ARG LEU GLN PRO ARG LEU GLU PHE LEU GLU VAL
SEQRES 38 A 484 LEU PHE GLN
HET A8X A9001 29
HET ZN A9002 1
HET CLR A9003 28
HET OLC A9004 13
HET OLC A9005 19
HET GOL A9006 6
HETNAM A8X 3-[(3R)-3-[(4-FLUOROPHENYL)SULFONYLAMINO]-1,2,3,4-
HETNAM 2 A8X TETRAHYDROCARBAZOL-9-YL]PROPANOIC ACID
HETNAM ZN ZINC ION
HETNAM CLR CHOLESTEROL
HETNAM OLC (2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE
HETNAM GOL GLYCEROL
HETSYN A8X RAMATROBAN
HETSYN OLC 1-OLEOYL-R-GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 A8X C21 H21 F N2 O4 S
FORMUL 3 ZN ZN 2+
FORMUL 4 CLR C27 H46 O
FORMUL 5 OLC 2(C21 H40 O4)
FORMUL 7 GOL C3 H8 O3
FORMUL 8 HOH *11(H2 O)
HELIX 1 AA1 ASP A 1002 ALA A 1020 1 19
HELIX 2 AA2 ASN A 1022 LYS A 1042 1 21
HELIX 3 AA3 PRO A 1045 GLU A 1049 5 5
HELIX 4 AA4 SER A 1055 GLU A 1081 1 27
HELIX 5 AA5 LYS A 1083 GLN A 1093 1 11
HELIX 6 AA6 GLN A 1093 ILE A 1102 1 10
HELIX 7 AA7 GLN A 1103 LEU A 1106 5 4
HELIX 8 AA8 THR A 18 ALA A 26 1 9
HELIX 9 AA9 SER A 27 GLY A 51 1 25
HELIX 10 AB1 SER A 61 ALA A 91 1 31
HELIX 11 AB2 GLU A 94 ASP A 99 1 6
HELIX 12 AB3 CYS A 102 ARG A 136 1 35
HELIX 13 AB4 ALA A 142 LEU A 165 1 24
HELIX 14 AB5 LEU A 166 LEU A 169 5 4
HELIX 15 AB6 GLU A 190 TYR A 226 1 37
HELIX 16 AB7 ASP A 2019 GLY A 2023 5 5
HELIX 17 AB8 ASP A 2029 ILE A 2033 5 5
HELIX 18 AB9 GLY A 2045 ASP A 2047 5 3
HELIX 19 AC1 ARG A 237 ARG A 271 1 35
HELIX 20 AC2 SER A 283 PHE A 311 1 29
HELIX 21 AC3 ARG A 312 ARG A 318 1 7
SHEET 1 AA1 2 TYR A 174 GLN A 177 0
SHEET 2 AA1 2 TRP A 182 LEU A 185 -1 O TRP A 182 N GLN A 177
SHEET 1 AA2 3 ILE A2012 TYR A2013 0
SHEET 2 AA2 3 TYR A2004 CYS A2006 -1 N TYR A2004 O TYR A2013
SHEET 3 AA2 3 PHE A2049 GLU A2051 -1 O GLU A2050 N THR A2005
SSBOND 1 CYS A 11 CYS A 102 1555 1555 2.04
SSBOND 2 CYS A 105 CYS A 183 1555 1555 2.07
LINK SG CYS A2006 ZN ZN A9002 1555 1555 2.23
LINK SG CYS A2009 ZN ZN A9002 1555 1555 2.58
LINK SG CYS A2039 ZN ZN A9002 1555 1555 2.45
LINK SG CYS A2042 ZN ZN A9002 1555 1555 2.27
CISPEP 1 TYR A 178 PRO A 179 0 7.28
SITE 1 AC1 13 ALA A 31 GLY A 77 LEU A 78 THR A 81
SITE 2 AC1 13 VAL A 85 HIS A 89 MET A 112 SER A 181
SITE 3 AC1 13 TRP A 258 LEU A 291 ARG A 295 THR A 298
SITE 4 AC1 13 GLN A 301
SITE 1 AC2 4 CYS A2006 CYS A2009 CYS A2039 CYS A2042
SITE 1 AC3 4 GLN A 146 ARG A 147 TRP A 150 OLC A9004
SITE 1 AC4 5 ARG A 103 ARG A 106 PHE A 107 VAL A 110
SITE 2 AC4 5 CLR A9003
SITE 1 AC5 6 SER A 62 PHE A 66 ALA A 125 SER A 145
SITE 2 AC5 6 SER A 207 HOH A9109
SITE 1 AC6 5 GLU A 94 TRP A 95 HIS A 96 GLN A1103
SITE 2 AC6 5 ASP A2036
CRYST1 81.160 155.080 128.130 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 0.012321 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006448 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007805 0.00000
ATOM 1 N ALA A1001 17.621 188.959 123.319 1.00 87.18 N
ANISOU 1 N ALA A1001 12941 8702 11483 -734 -1808 1409 N
ATOM 2 CA ALA A1001 17.915 187.540 123.578 1.00 85.52 C
ANISOU 2 CA ALA A1001 12720 8634 11139 -738 -1695 1300 C
ATOM 3 C ALA A1001 18.100 187.226 125.077 1.00 86.24 C
ANISOU 3 C ALA A1001 12633 8801 11332 -575 -1469 1159 C
ATOM 4 O ALA A1001 18.131 188.148 125.911 1.00 86.98 O
ANISOU 4 O ALA A1001 12650 8838 11560 -474 -1374 1127 O
ATOM 5 CB ALA A1001 19.154 187.107 122.796 1.00 85.76 C
ANISOU 5 CB ALA A1001 12980 8749 10857 -890 -1613 1220 C
ATOM 6 N ASP A1002 18.220 185.915 125.407 1.00 78.00 N
ANISOU 6 N ASP A1002 11551 7872 10212 -562 -1387 1078 N
ATOM 7 CA ASP A1002 18.441 185.409 126.766 1.00 75.02 C
ANISOU 7 CA ASP A1002 11045 7572 9887 -440 -1194 949 C
ATOM 8 C ASP A1002 19.848 185.781 127.250 1.00 72.31 C
ANISOU 8 C ASP A1002 10776 7291 9409 -455 -1032 825 C
ATOM 9 O ASP A1002 20.759 185.929 126.418 1.00 71.54 O
ANISOU 9 O ASP A1002 10819 7217 9146 -569 -1035 817 O
ATOM 10 CB ASP A1002 18.255 183.874 126.806 1.00 76.89 C
ANISOU 10 CB ASP A1002 11246 7908 10060 -447 -1179 912 C
ATOM 11 CG ASP A1002 16.837 183.381 127.099 1.00 97.74 C
ANISOU 11 CG ASP A1002 13727 10502 12909 -371 -1262 991 C
ATOM 12 OD1 ASP A1002 15.890 184.205 127.039 1.00101.09 O
ANISOU 12 OD1 ASP A1002 14061 10798 13549 -326 -1363 1105 O
ATOM 13 OD2 ASP A1002 16.673 182.163 127.376 1.00106.92 O
ANISOU 13 OD2 ASP A1002 14843 11745 14038 -358 -1223 946 O
ATOM 14 N LEU A1003 20.030 185.924 128.588 1.00 63.77 N
ANISOU 14 N LEU A1003 9611 6221 8399 -354 -890 733 N
ATOM 15 CA LEU A1003 21.326 186.266 129.185 1.00 61.52 C
ANISOU 15 CA LEU A1003 9382 5982 8013 -377 -769 632 C
ATOM 16 C LEU A1003 22.401 185.263 128.825 1.00 63.97 C
ANISOU 16 C LEU A1003 9733 6408 8166 -455 -720 573 C
ATOM 17 O LEU A1003 23.506 185.654 128.467 1.00 63.73 O
ANISOU 17 O LEU A1003 9776 6392 8047 -533 -680 548 O
ATOM 18 CB LEU A1003 21.244 186.367 130.712 1.00 60.80 C
ANISOU 18 CB LEU A1003 9230 5875 7997 -283 -650 550 C
ATOM 19 CG LEU A1003 21.217 187.748 131.321 1.00 65.69 C
ANISOU 19 CG LEU A1003 9890 6378 8692 -249 -602 542 C
ATOM 20 CD1 LEU A1003 21.428 187.659 132.804 1.00 65.30 C
ANISOU 20 CD1 LEU A1003 9852 6322 8639 -206 -473 442 C
ATOM 21 CD2 LEU A1003 22.274 188.653 130.718 1.00 66.89 C
ANISOU 21 CD2 LEU A1003 10148 6522 8747 -343 -633 550 C
ATOM 22 N GLU A1004 22.068 183.968 128.916 1.00 60.88 N
ANISOU 22 N GLU A1004 9284 6086 7761 -434 -711 553 N
ATOM 23 CA GLU A1004 22.954 182.843 128.621 1.00 59.56 C
ANISOU 23 CA GLU A1004 9136 6011 7481 -492 -645 498 C
ATOM 24 C GLU A1004 23.484 182.899 127.194 1.00 61.93 C
ANISOU 24 C GLU A1004 9575 6299 7657 -618 -660 532 C
ATOM 25 O GLU A1004 24.665 182.659 126.966 1.00 59.60 O
ANISOU 25 O GLU A1004 9315 6036 7295 -679 -552 480 O
ATOM 26 CB GLU A1004 22.210 181.556 128.871 1.00 60.43 C
ANISOU 26 CB GLU A1004 9175 6172 7614 -445 -655 491 C
ATOM 27 CG GLU A1004 23.089 180.456 129.415 1.00 72.01 C
ANISOU 27 CG GLU A1004 10597 7723 9040 -439 -551 407 C
ATOM 28 CD GLU A1004 22.292 179.287 129.951 1.00 81.26 C
ANISOU 28 CD GLU A1004 11688 8937 10248 -376 -555 393 C
ATOM 29 OE1 GLU A1004 21.130 179.100 129.520 1.00 62.87 O
ANISOU 29 OE1 GLU A1004 9351 6582 7955 -365 -641 455 O
ATOM 30 OE2 GLU A1004 22.820 178.582 130.837 1.00 74.86 O
ANISOU 30 OE2 GLU A1004 10820 8178 9444 -344 -485 330 O
ATOM 31 N ASP A1005 22.638 183.297 126.250 1.00 60.79 N
ANISOU 31 N ASP A1005 9516 6087 7494 -669 -792 627 N
ATOM 32 CA ASP A1005 23.074 183.452 124.869 1.00 62.25 C
ANISOU 32 CA ASP A1005 9889 6234 7528 -816 -813 666 C
ATOM 33 C ASP A1005 24.082 184.585 124.701 1.00 64.21 C
ANISOU 33 C ASP A1005 10206 6447 7745 -868 -746 650 C
ATOM 34 O ASP A1005 25.093 184.387 124.022 1.00 62.42 O
ANISOU 34 O ASP A1005 10085 6228 7404 -969 -629 611 O
ATOM 35 CB ASP A1005 21.876 183.595 123.936 1.00 66.17 C
ANISOU 35 CB ASP A1005 10478 6653 8012 -878 -1017 792 C
ATOM 36 CG ASP A1005 21.158 182.274 123.777 1.00 83.07 C
ANISOU 36 CG ASP A1005 12600 8830 10134 -882 -1068 804 C
ATOM 37 OD1 ASP A1005 21.700 181.391 123.078 1.00 87.02 O
ANISOU 37 OD1 ASP A1005 13234 9358 10471 -982 -990 760 O
ATOM 38 OD2 ASP A1005 20.092 182.094 124.414 1.00 86.56 O
ANISOU 38 OD2 ASP A1005 12887 9267 10736 -780 -1156 847 O
ATOM 39 N ASN A1006 23.843 185.738 125.374 1.00 61.36 N
ANISOU 39 N ASN A1006 9779 6039 7497 -796 -793 673 N
ATOM 40 CA ASN A1006 24.744 186.904 125.325 1.00 62.07 C
ANISOU 40 CA ASN A1006 9927 6088 7569 -842 -744 662 C
ATOM 41 C ASN A1006 26.063 186.573 126.022 1.00 64.77 C
ANISOU 41 C ASN A1006 10197 6501 7914 -837 -583 562 C
ATOM 42 O ASN A1006 27.132 186.946 125.536 1.00 64.56 O
ANISOU 42 O ASN A1006 10236 6461 7833 -927 -499 545 O
ATOM 43 CB ASN A1006 24.080 188.163 125.924 1.00 63.63 C
ANISOU 43 CB ASN A1006 10080 6200 7896 -763 -828 709 C
ATOM 44 CG ASN A1006 22.841 188.658 125.191 1.00 78.70 C
ANISOU 44 CG ASN A1006 12033 8008 9860 -771 -1007 837 C
ATOM 45 OD1 ASN A1006 21.776 188.855 125.792 1.00 80.94 O
ANISOU 45 OD1 ASN A1006 12200 8240 10312 -662 -1069 879 O
ATOM 46 ND2 ASN A1006 22.945 188.899 123.888 1.00 57.62 N
ANISOU 46 ND2 ASN A1006 9536 5291 7068 -908 -1094 912 N
ATOM 47 N TRP A1007 25.973 185.827 127.130 1.00 61.12 N
ANISOU 47 N TRP A1007 9597 6101 7525 -742 -548 505 N
ATOM 48 CA TRP A1007 27.100 185.319 127.897 1.00 60.85 C
ANISOU 48 CA TRP A1007 9473 6127 7522 -736 -441 432 C
ATOM 49 C TRP A1007 27.991 184.457 126.988 1.00 62.40 C
ANISOU 49 C TRP A1007 9698 6351 7659 -822 -325 410 C
ATOM 50 O TRP A1007 29.191 184.698 126.919 1.00 61.01 O
ANISOU 50 O TRP A1007 9501 6168 7513 -879 -229 388 O
ATOM 51 CB TRP A1007 26.606 184.513 129.105 1.00 59.92 C
ANISOU 51 CB TRP A1007 9239 6058 7469 -633 -451 392 C
ATOM 52 CG TRP A1007 27.715 184.183 130.063 1.00 62.46 C
ANISOU 52 CG TRP A1007 9476 6418 7840 -635 -395 340 C
ATOM 53 CD1 TRP A1007 28.303 185.025 130.974 1.00 65.94 C
ANISOU 53 CD1 TRP A1007 9910 6825 8319 -646 -414 326 C
ATOM 54 CD2 TRP A1007 28.436 182.954 130.131 1.00 62.61 C
ANISOU 54 CD2 TRP A1007 9409 6495 7884 -645 -327 309 C
ATOM 55 NE1 TRP A1007 29.309 184.371 131.643 1.00 65.83 N
ANISOU 55 NE1 TRP A1007 9807 6848 8358 -668 -393 302 N
ATOM 56 CE2 TRP A1007 29.412 183.094 131.147 1.00 67.27 C
ANISOU 56 CE2 TRP A1007 9925 7085 8550 -658 -334 292 C
ATOM 57 CE3 TRP A1007 28.348 181.741 129.435 1.00 64.84 C
ANISOU 57 CE3 TRP A1007 9680 6816 8139 -650 -266 299 C
ATOM 58 CZ2 TRP A1007 30.288 182.064 131.487 1.00 67.36 C
ANISOU 58 CZ2 TRP A1007 9821 7131 8642 -666 -295 279 C
ATOM 59 CZ3 TRP A1007 29.197 180.701 129.795 1.00 67.71 C
ANISOU 59 CZ3 TRP A1007 9936 7214 8575 -647 -195 270 C
ATOM 60 CH2 TRP A1007 30.170 180.874 130.793 1.00 68.64 C
ANISOU 60 CH2 TRP A1007 9953 7328 8800 -652 -214 267 C
ATOM 61 N GLU A1008 27.389 183.501 126.245 1.00 59.64 N
ANISOU 61 N GLU A1008 9407 6017 7235 -841 -326 420 N
ATOM 62 CA GLU A1008 28.097 182.636 125.300 1.00 60.36 C
ANISOU 62 CA GLU A1008 9571 6109 7255 -930 -185 392 C
ATOM 63 C GLU A1008 28.752 183.467 124.197 1.00 65.16 C
ANISOU 63 C GLU A1008 10340 6642 7776 -1060 -114 414 C
ATOM 64 O GLU A1008 29.955 183.309 123.977 1.00 65.15 O
ANISOU 64 O GLU A1008 10319 6625 7810 -1115 62 374 O
ATOM 65 CB GLU A1008 27.174 181.553 124.709 1.00 61.92 C
ANISOU 65 CB GLU A1008 9847 6318 7362 -942 -223 403 C
ATOM 66 CG GLU A1008 26.788 180.443 125.676 1.00 74.10 C
ANISOU 66 CG GLU A1008 11236 7934 8985 -834 -232 366 C
ATOM 67 CD GLU A1008 27.902 179.663 126.353 1.00103.05 C
ANISOU 67 CD GLU A1008 14763 11641 12751 -798 -88 300 C
ATOM 68 OE1 GLU A1008 28.990 179.500 125.752 1.00102.32 O
ANISOU 68 OE1 GLU A1008 14700 11514 12662 -871 74 274 O
ATOM 69 OE2 GLU A1008 27.661 179.176 127.481 1.00 99.77 O
ANISOU 69 OE2 GLU A1008 14209 11277 12421 -702 -134 281 O
ATOM 70 N THR A1009 27.983 184.400 123.566 1.00 62.40 N
ANISOU 70 N THR A1009 10135 6233 7340 -1109 -251 485 N
ATOM 71 CA THR A1009 28.481 185.336 122.547 1.00 64.35 C
ANISOU 71 CA THR A1009 10564 6399 7489 -1242 -214 518 C
ATOM 72 C THR A1009 29.718 186.067 123.091 1.00 70.78 C
ANISOU 72 C THR A1009 11273 7212 8409 -1239 -102 482 C
ATOM 73 O THR A1009 30.732 186.117 122.399 1.00 72.36 O
ANISOU 73 O THR A1009 11547 7370 8576 -1344 70 460 O
ATOM 74 CB THR A1009 27.414 186.392 122.159 1.00 73.85 C
ANISOU 74 CB THR A1009 11880 7535 8644 -1263 -431 619 C
ATOM 75 OG1 THR A1009 26.146 185.789 121.918 1.00 76.53 O
ANISOU 75 OG1 THR A1009 12253 7874 8953 -1244 -588 675 O
ATOM 76 CG2 THR A1009 27.833 187.228 120.957 1.00 72.84 C
ANISOU 76 CG2 THR A1009 11989 7312 8374 -1426 -411 664 C
ATOM 77 N LEU A1010 29.639 186.609 124.332 1.00 67.25 N
ANISOU 77 N LEU A1010 10664 6798 8092 -1130 -188 478 N
ATOM 78 CA LEU A1010 30.758 187.313 124.941 1.00 68.83 C
ANISOU 78 CA LEU A1010 10769 6989 8393 -1140 -126 457 C
ATOM 79 C LEU A1010 32.010 186.444 125.057 1.00 74.81 C
ANISOU 79 C LEU A1010 11403 7772 9248 -1165 52 407 C
ATOM 80 O LEU A1010 33.071 186.864 124.577 1.00 76.15 O
ANISOU 80 O LEU A1010 11583 7894 9456 -1255 179 408 O
ATOM 81 CB LEU A1010 30.391 187.963 126.287 1.00 68.46 C
ANISOU 81 CB LEU A1010 10619 6956 8438 -1039 -253 456 C
ATOM 82 CG LEU A1010 29.640 189.294 126.189 1.00 74.38 C
ANISOU 82 CG LEU A1010 11472 7632 9156 -1034 -375 509 C
ATOM 83 CD1 LEU A1010 28.786 189.533 127.410 1.00 73.76 C
ANISOU 83 CD1 LEU A1010 11321 7552 9152 -914 -468 500 C
ATOM 84 CD2 LEU A1010 30.586 190.456 125.992 1.00 79.26 C
ANISOU 84 CD2 LEU A1010 12144 8192 9778 -1121 -341 522 C
ATOM 85 N ASN A1011 31.880 185.228 125.626 1.00 70.51 N
ANISOU 85 N ASN A1011 10739 7290 8763 -1089 70 373 N
ATOM 86 CA ASN A1011 33.008 184.307 125.783 1.00 71.19 C
ANISOU 86 CA ASN A1011 10679 7385 8986 -1097 228 340 C
ATOM 87 C ASN A1011 33.595 183.840 124.462 1.00 78.74 C
ANISOU 87 C ASN A1011 11741 8280 9895 -1199 454 320 C
ATOM 88 O ASN A1011 34.823 183.814 124.325 1.00 79.21 O
ANISOU 88 O ASN A1011 11704 8293 10100 -1248 625 312 O
ATOM 89 CB ASN A1011 32.633 183.119 126.637 1.00 67.79 C
ANISOU 89 CB ASN A1011 10118 7022 8618 -996 183 314 C
ATOM 90 CG ASN A1011 32.149 183.486 128.008 1.00 83.91 C
ANISOU 90 CG ASN A1011 12082 9104 10697 -912 0 323 C
ATOM 91 OD1 ASN A1011 32.557 184.481 128.625 1.00 76.87 O
ANISOU 91 OD1 ASN A1011 11166 8188 9852 -928 -72 341 O
ATOM 92 ND2 ASN A1011 31.251 182.684 128.503 1.00 67.86 N
ANISOU 92 ND2 ASN A1011 10028 7122 8633 -831 -65 307 N
ATOM 93 N ASP A1012 32.724 183.489 123.489 1.00 76.86 N
ANISOU 93 N ASP A1012 11713 8026 9466 -1244 458 319 N
ATOM 94 CA ASP A1012 33.143 183.033 122.164 1.00 79.03 C
ANISOU 94 CA ASP A1012 12169 8221 9638 -1368 681 293 C
ATOM 95 C ASP A1012 34.109 184.058 121.554 1.00 85.62 C
ANISOU 95 C ASP A1012 13074 8971 10487 -1481 818 305 C
ATOM 96 O ASP A1012 35.207 183.695 121.132 1.00 87.20 O
ANISOU 96 O ASP A1012 13238 9104 10790 -1541 1083 270 O
ATOM 97 CB ASP A1012 31.921 182.780 121.244 1.00 81.29 C
ANISOU 97 CB ASP A1012 12723 8488 9676 -1432 584 314 C
ATOM 98 CG ASP A1012 31.029 181.590 121.611 1.00 95.31 C
ANISOU 98 CG ASP A1012 14453 10327 11432 -1350 498 299 C
ATOM 99 OD1 ASP A1012 31.461 180.741 122.452 1.00 95.64 O
ANISOU 99 OD1 ASP A1012 14280 10422 11637 -1250 565 257 O
ATOM 100 OD2 ASP A1012 29.892 181.508 121.072 1.00 99.91 O
ANISOU 100 OD2 ASP A1012 15213 10901 11849 -1391 345 340 O
ATOM 101 N ASN A1013 33.729 185.343 121.610 1.00 81.70 N
ANISOU 101 N ASN A1013 12649 8470 9924 -1501 647 356 N
ATOM 102 CA ASN A1013 34.511 186.466 121.113 1.00 82.51 C
ANISOU 102 CA ASN A1013 12828 8497 10027 -1607 731 378 C
ATOM 103 C ASN A1013 35.737 186.799 121.980 1.00 87.02 C
ANISOU 103 C ASN A1013 13135 9074 10855 -1572 798 374 C
ATOM 104 O ASN A1013 36.672 187.435 121.484 1.00 88.58 O
ANISOU 104 O ASN A1013 13358 9196 11104 -1672 949 383 O
ATOM 105 CB ASN A1013 33.615 187.673 120.929 1.00 79.79 C
ANISOU 105 CB ASN A1013 12644 8137 9535 -1631 503 441 C
ATOM 106 CG ASN A1013 32.722 187.533 119.737 1.00 92.94 C
ANISOU 106 CG ASN A1013 14609 9747 10956 -1734 456 472 C
ATOM 107 OD1 ASN A1013 33.133 187.792 118.609 1.00 97.08 O
ANISOU 107 OD1 ASN A1013 15367 10177 11341 -1892 598 476 O
ATOM 108 ND2 ASN A1013 31.493 187.096 119.952 1.00 75.74 N
ANISOU 108 ND2 ASN A1013 12443 7615 8721 -1661 254 502 N
ATOM 109 N LEU A1014 35.743 186.378 123.259 1.00 81.54 N
ANISOU 109 N LEU A1014 12202 8457 10322 -1448 678 371 N
ATOM 110 CA LEU A1014 36.895 186.616 124.128 1.00 81.45 C
ANISOU 110 CA LEU A1014 11947 8440 10559 -1434 694 388 C
ATOM 111 C LEU A1014 38.078 185.733 123.707 1.00 84.95 C
ANISOU 111 C LEU A1014 12254 8822 11202 -1474 974 368 C
ATOM 112 O LEU A1014 39.208 186.228 123.621 1.00 85.45 O
ANISOU 112 O LEU A1014 12209 8816 11443 -1543 1093 394 O
ATOM 113 CB LEU A1014 36.542 186.463 125.613 1.00 80.21 C
ANISOU 113 CB LEU A1014 11626 8363 10488 -1319 468 398 C
ATOM 114 CG LEU A1014 36.402 187.784 126.361 1.00 84.92 C
ANISOU 114 CG LEU A1014 12242 8958 11067 -1322 273 432 C
ATOM 115 CD1 LEU A1014 35.221 187.760 127.303 1.00 83.70 C
ANISOU 115 CD1 LEU A1014 12124 8862 10816 -1219 72 422 C
ATOM 116 CD2 LEU A1014 37.667 188.119 127.109 1.00 88.96 C
ANISOU 116 CD2 LEU A1014 12558 9441 11803 -1361 250 467 C
ATOM 117 N LYS A1015 37.793 184.456 123.360 1.00 80.82 N
ANISOU 117 N LYS A1015 11749 8306 10654 -1439 1096 325 N
ATOM 118 CA LYS A1015 38.756 183.475 122.831 1.00 82.12 C
ANISOU 118 CA LYS A1015 11816 8387 10999 -1468 1408 295 C
ATOM 119 C LYS A1015 39.291 183.951 121.462 1.00 87.57 C
ANISOU 119 C LYS A1015 12714 8956 11605 -1617 1690 274 C
ATOM 120 O LYS A1015 40.460 183.730 121.158 1.00 88.52 O
ANISOU 120 O LYS A1015 12702 8973 11959 -1663 1966 270 O
ATOM 121 CB LYS A1015 38.102 182.090 122.679 1.00 83.82 C
ANISOU 121 CB LYS A1015 12079 8631 11139 -1406 1461 245 C
ATOM 122 CG LYS A1015 38.021 181.290 123.975 1.00 96.45 C
ANISOU 122 CG LYS A1015 13421 10311 12915 -1272 1293 262 C
ATOM 123 CD LYS A1015 37.053 180.109 123.879 1.00105.84 C
ANISOU 123 CD LYS A1015 14701 11550 13966 -1211 1278 216 C
ATOM 124 CE LYS A1015 35.628 180.483 124.239 1.00115.26 C
ANISOU 124 CE LYS A1015 16037 12844 14914 -1167 996 224 C
ATOM 125 NZ LYS A1015 34.792 179.289 124.531 1.00119.93 N
ANISOU 125 NZ LYS A1015 16625 13494 15448 -1087 937 197 N
ATOM 126 N VAL A1016 38.430 184.624 120.659 1.00 83.79 N
ANISOU 126 N VAL A1016 12556 8473 10806 -1698 1617 270 N
ATOM 127 CA VAL A1016 38.746 185.196 119.343 1.00 85.40 C
ANISOU 127 CA VAL A1016 13035 8559 10854 -1864 1837 257 C
ATOM 128 C VAL A1016 39.828 186.289 119.493 1.00 92.45 C
ANISOU 128 C VAL A1016 13794 9399 11935 -1919 1900 298 C
ATOM 129 O VAL A1016 40.833 186.231 118.780 1.00 94.59 O
ANISOU 129 O VAL A1016 14074 9546 12319 -2018 2230 277 O
ATOM 130 CB VAL A1016 37.465 185.703 118.611 1.00 87.87 C
ANISOU 130 CB VAL A1016 13711 8883 10794 -1938 1651 274 C
ATOM 131 CG1 VAL A1016 37.798 186.523 117.368 1.00 89.11 C
ANISOU 131 CG1 VAL A1016 14172 8914 10773 -2128 1818 279 C
ATOM 132 CG2 VAL A1016 36.540 184.545 118.256 1.00 87.07 C
ANISOU 132 CG2 VAL A1016 13763 8801 10519 -1924 1635 238 C
ATOM 133 N ILE A1017 39.642 187.250 120.438 1.00 88.47 N
ANISOU 133 N ILE A1017 13164 8973 11476 -1860 1604 353 N
ATOM 134 CA ILE A1017 40.608 188.331 120.708 1.00 89.66 C
ANISOU 134 CA ILE A1017 13185 9079 11803 -1915 1613 400 C
ATOM 135 C ILE A1017 41.916 187.724 121.236 1.00 95.89 C
ANISOU 135 C ILE A1017 13623 9822 12987 -1887 1784 415 C
ATOM 136 O ILE A1017 42.998 188.204 120.892 1.00 97.68 O
ANISOU 136 O ILE A1017 13765 9950 13399 -1978 1980 439 O
ATOM 137 CB ILE A1017 40.046 189.450 121.653 1.00 91.20 C
ANISOU 137 CB ILE A1017 13358 9354 11941 -1863 1256 450 C
ATOM 138 CG1 ILE A1017 38.716 190.019 121.127 1.00 90.96 C
ANISOU 138 CG1 ILE A1017 13635 9345 11579 -1878 1086 453 C
ATOM 139 CG2 ILE A1017 41.073 190.589 121.877 1.00 92.03 C
ANISOU 139 CG2 ILE A1017 13357 9401 12211 -1942 1263 500 C
ATOM 140 CD1 ILE A1017 37.839 190.680 122.162 1.00 96.88 C
ANISOU 140 CD1 ILE A1017 14351 10173 12285 -1777 759 483 C
ATOM 141 N GLU A1018 41.803 186.657 122.047 1.00 92.31 N
ANISOU 141 N GLU A1018 12964 9430 12678 -1767 1710 410 N
ATOM 142 CA GLU A1018 42.924 185.918 122.618 1.00 93.68 C
ANISOU 142 CA GLU A1018 12786 9555 13254 -1726 1825 442 C
ATOM 143 C GLU A1018 43.797 185.310 121.500 1.00101.26 C
ANISOU 143 C GLU A1018 13743 10363 14367 -1801 2279 405 C
ATOM 144 O GLU A1018 44.995 185.590 121.471 1.00103.48 O
ANISOU 144 O GLU A1018 13809 10541 14968 -1854 2447 453 O
ATOM 145 CB GLU A1018 42.394 184.833 123.561 1.00 93.63 C
ANISOU 145 CB GLU A1018 12638 9640 13296 -1590 1649 438 C
ATOM 146 CG GLU A1018 43.286 184.509 124.742 1.00106.13 C
ANISOU 146 CG GLU A1018 13848 11215 15262 -1537 1527 518 C
ATOM 147 CD GLU A1018 42.743 183.390 125.611 1.00133.58 C
ANISOU 147 CD GLU A1018 17222 14771 18761 -1417 1361 513 C
ATOM 148 OE1 GLU A1018 41.551 183.449 125.997 1.00120.00 O
ANISOU 148 OE1 GLU A1018 15673 13163 16757 -1362 1137 481 O
ATOM 149 OE2 GLU A1018 43.512 182.446 125.902 1.00136.21 O
ANISOU 149 OE2 GLU A1018 17295 15043 19417 -1377 1464 547 O
ATOM 150 N LYS A1019 43.193 184.547 120.553 1.00 98.06 N
ANISOU 150 N LYS A1019 13599 9930 13731 -1821 2484 323 N
ATOM 151 CA LYS A1019 43.897 183.918 119.422 1.00100.50 C
ANISOU 151 CA LYS A1019 13987 10073 14126 -1905 2957 265 C
ATOM 152 C LYS A1019 44.381 184.935 118.373 1.00108.10 C
ANISOU 152 C LYS A1019 15171 10919 14985 -2074 3189 257 C
ATOM 153 O LYS A1019 45.437 184.730 117.770 1.00110.54 O
ANISOU 153 O LYS A1019 15403 11064 15533 -2145 3592 241 O
ATOM 154 CB LYS A1019 43.012 182.858 118.727 1.00102.42 C
ANISOU 154 CB LYS A1019 14514 10312 14088 -1904 3074 178 C
ATOM 155 CG LYS A1019 42.496 181.710 119.615 1.00112.28 C
ANISOU 155 CG LYS A1019 15583 11662 15417 -1748 2894 174 C
ATOM 156 CD LYS A1019 43.534 180.636 119.930 1.00119.88 C
ANISOU 156 CD LYS A1019 16209 12524 16817 -1675 3149 180 C
ATOM 157 CE LYS A1019 43.028 179.681 120.981 1.00124.01 C
ANISOU 157 CE LYS A1019 16537 13158 17423 -1523 2899 197 C
ATOM 158 NZ LYS A1019 44.042 178.652 121.330 1.00135.18 N
ANISOU 158 NZ LYS A1019 17605 14462 19295 -1450 3116 222 N
ATOM 159 N ALA A1020 43.600 186.014 118.157 1.00104.61 N
ANISOU 159 N ALA A1020 14999 10545 14202 -2138 2948 270 N
ATOM 160 CA ALA A1020 43.797 187.089 117.167 1.00106.71 C
ANISOU 160 CA ALA A1020 15546 10719 14281 -2308 3087 269 C
ATOM 161 C ALA A1020 45.242 187.572 116.921 1.00112.73 C
ANISOU 161 C ALA A1020 16121 11338 15373 -2394 3401 296 C
ATOM 162 O ALA A1020 46.050 187.654 117.849 1.00112.96 O
ANISOU 162 O ALA A1020 15746 11379 15792 -2320 3328 362 O
ATOM 163 CB ALA A1020 42.931 188.281 117.517 1.00105.96 C
ANISOU 163 CB ALA A1020 15587 10736 13937 -2308 2680 320 C
ATOM 164 N ASP A1021 45.524 187.935 115.651 1.00110.08 N
ANISOU 164 N ASP A1021 16103 10856 14866 -2570 3734 253 N
ATOM 165 CA ASP A1021 46.821 188.410 115.180 1.00112.20 C
ANISOU 165 CA ASP A1021 16265 10960 15407 -2682 4101 267 C
ATOM 166 C ASP A1021 46.805 189.855 114.655 1.00115.86 C
ANISOU 166 C ASP A1021 16979 11396 15647 -2832 4034 300 C
ATOM 167 O ASP A1021 47.871 190.454 114.539 1.00117.87 O
ANISOU 167 O ASP A1021 17079 11544 16164 -2909 4246 335 O
ATOM 168 CB ASP A1021 47.403 187.446 114.131 1.00116.84 C
ANISOU 168 CB ASP A1021 16985 11348 16062 -2767 4670 178 C
ATOM 169 CG ASP A1021 48.090 186.237 114.738 1.00129.06 C
ANISOU 169 CG ASP A1021 18112 12855 18072 -2624 4846 178 C
ATOM 170 OD1 ASP A1021 49.319 186.310 114.972 1.00131.70 O
ANISOU 170 OD1 ASP A1021 18073 13078 18889 -2615 5067 230 O
ATOM 171 OD2 ASP A1021 47.400 185.210 114.972 1.00132.68 O
ANISOU 171 OD2 ASP A1021 18604 13382 18428 -2525 4756 135 O
ATOM 172 N ASN A1022 45.623 190.422 114.346 1.00110.07 N
ANISOU 172 N ASN A1022 16611 10747 14463 -2875 3737 300 N
ATOM 173 CA ASN A1022 45.551 191.804 113.852 1.00110.24 C
ANISOU 173 CA ASN A1022 16880 10736 14270 -3014 3645 340 C
ATOM 174 C ASN A1022 44.458 192.639 114.515 1.00110.37 C
ANISOU 174 C ASN A1022 16954 10911 14072 -2938 3118 400 C
ATOM 175 O ASN A1022 43.531 192.089 115.098 1.00106.80 O
ANISOU 175 O ASN A1022 16464 10583 13533 -2806 2849 396 O
ATOM 176 CB ASN A1022 45.436 191.859 112.321 1.00113.76 C
ANISOU 176 CB ASN A1022 17837 11021 14367 -3233 3963 284 C
ATOM 177 CG ASN A1022 44.211 191.185 111.767 1.00132.78 C
ANISOU 177 CG ASN A1022 20620 13457 16372 -3258 3845 243 C
ATOM 178 OD1 ASN A1022 43.109 191.740 111.778 1.00125.62 O
ANISOU 178 OD1 ASN A1022 19923 12640 15169 -3259 3453 292 O
ATOM 179 ND2 ASN A1022 44.384 189.979 111.252 1.00123.55 N
ANISOU 179 ND2 ASN A1022 19542 12197 15205 -3284 4184 161 N
ATOM 180 N ALA A1023 44.579 193.978 114.408 1.00108.33 N
ANISOU 180 N ALA A1023 16790 10631 13739 -3026 2994 456 N
ATOM 181 CA ALA A1023 43.646 194.966 114.958 1.00106.10 C
ANISOU 181 CA ALA A1023 16578 10457 13280 -2971 2543 517 C
ATOM 182 C ALA A1023 42.221 194.840 114.385 1.00109.22 C
ANISOU 182 C ALA A1023 17344 10881 13274 -2988 2335 515 C
ATOM 183 O ALA A1023 41.256 194.982 115.141 1.00106.51 O
ANISOU 183 O ALA A1023 16936 10655 12877 -2855 1971 547 O
ATOM 184 CB ALA A1023 44.183 196.369 114.731 1.00107.81 C
ANISOU 184 CB ALA A1023 16866 10601 13495 -3093 2535 570 C
ATOM 185 N ALA A1024 42.097 194.557 113.061 1.00107.21 N
ANISOU 185 N ALA A1024 17482 10504 12750 -3162 2570 482 N
ATOM 186 CA ALA A1024 40.824 194.415 112.345 1.00106.15 C
ANISOU 186 CA ALA A1024 17740 10363 12230 -3228 2376 499 C
ATOM 187 C ALA A1024 39.984 193.237 112.827 1.00107.48 C
ANISOU 187 C ALA A1024 17809 10639 12391 -3081 2231 471 C
ATOM 188 O ALA A1024 38.761 193.369 112.912 1.00106.37 O
ANISOU 188 O ALA A1024 17788 10561 12068 -3035 1882 523 O
ATOM 189 CB ALA A1024 41.073 194.303 110.853 1.00109.74 C
ANISOU 189 CB ALA A1024 18650 10637 12408 -3479 2697 467 C
ATOM 190 N GLN A1025 40.632 192.092 113.134 1.00102.78 N
ANISOU 190 N GLN A1025 16984 10052 12016 -3006 2498 397 N
ATOM 191 CA GLN A1025 39.955 190.886 113.611 1.00100.70 C
ANISOU 191 CA GLN A1025 16609 9884 11767 -2868 2397 365 C
ATOM 192 C GLN A1025 39.600 190.965 115.115 1.00101.41 C
ANISOU 192 C GLN A1025 16305 10143 12082 -2641 2063 400 C
ATOM 193 O GLN A1025 38.721 190.224 115.580 1.00 99.77 O
ANISOU 193 O GLN A1025 16046 10030 11831 -2524 1870 395 O
ATOM 194 CB GLN A1025 40.745 189.611 113.251 1.00103.48 C
ANISOU 194 CB GLN A1025 16912 10154 12253 -2888 2824 274 C
ATOM 195 CG GLN A1025 42.041 189.384 114.026 1.00115.01 C
ANISOU 195 CG GLN A1025 17920 11611 14166 -2787 3045 258 C
ATOM 196 CD GLN A1025 42.662 188.047 113.706 1.00135.71 C
ANISOU 196 CD GLN A1025 20477 14140 16946 -2784 3448 177 C
ATOM 197 OE1 GLN A1025 43.692 187.965 113.033 1.00131.51 O
ANISOU 197 OE1 GLN A1025 19978 13446 16544 -2895 3881 137 O
ATOM 198 NE2 GLN A1025 42.055 186.965 114.190 1.00129.49 N
ANISOU 198 NE2 GLN A1025 19592 13440 16168 -2654 3333 151 N
ATOM 199 N VAL A1026 40.294 191.863 115.860 1.00 95.99 N
ANISOU 199 N VAL A1026 15365 9481 11625 -2596 2004 437 N
ATOM 200 CA VAL A1026 40.072 192.158 117.278 1.00 92.91 C
ANISOU 200 CA VAL A1026 14661 9220 11422 -2422 1699 472 C
ATOM 201 C VAL A1026 38.889 193.135 117.337 1.00 95.71 C
ANISOU 201 C VAL A1026 15202 9612 11552 -2409 1351 530 C
ATOM 202 O VAL A1026 38.036 193.014 118.211 1.00 92.87 O
ANISOU 202 O VAL A1026 14729 9352 11207 -2266 1086 545 O
ATOM 203 CB VAL A1026 41.367 192.687 117.971 1.00 97.29 C
ANISOU 203 CB VAL A1026 14904 9757 12305 -2414 1782 494 C
ATOM 204 CG1 VAL A1026 41.074 193.440 119.271 1.00 95.59 C
ANISOU 204 CG1 VAL A1026 14502 9637 12181 -2302 1433 542 C
ATOM 205 CG2 VAL A1026 42.344 191.552 118.240 1.00 97.62 C
ANISOU 205 CG2 VAL A1026 14659 9779 12654 -2369 2039 459 C
ATOM 206 N LYS A1027 38.818 194.061 116.360 1.00 95.46 N
ANISOU 206 N LYS A1027 15469 9483 11320 -2563 1368 567 N
ATOM 207 CA LYS A1027 37.752 195.056 116.201 1.00 95.18 C
ANISOU 207 CA LYS A1027 15636 9441 11088 -2575 1060 640 C
ATOM 208 C LYS A1027 36.390 194.360 115.978 1.00 99.31 C
ANISOU 208 C LYS A1027 16303 10001 11429 -2528 864 658 C
ATOM 209 O LYS A1027 35.433 194.698 116.676 1.00 97.91 O
ANISOU 209 O LYS A1027 16046 9884 11273 -2405 570 704 O
ATOM 210 CB LYS A1027 38.094 196.025 115.049 1.00 99.09 C
ANISOU 210 CB LYS A1027 16445 9801 11404 -2781 1158 679 C
ATOM 211 CG LYS A1027 37.036 197.079 114.728 1.00111.88 C
ANISOU 211 CG LYS A1027 18298 11381 12830 -2817 842 774 C
ATOM 212 CD LYS A1027 37.265 197.649 113.331 1.00125.63 C
ANISOU 212 CD LYS A1027 20435 12972 14325 -3058 963 810 C
ATOM 213 CE LYS A1027 36.389 198.836 113.009 1.00135.66 C
ANISOU 213 CE LYS A1027 21924 14180 15442 -3108 647 923 C
ATOM 214 NZ LYS A1027 36.862 199.557 111.795 1.00141.99 N
ANISOU 214 NZ LYS A1027 23088 14830 16033 -3352 778 959 N
ATOM 215 N ASP A1028 36.312 193.382 115.038 1.00 97.28 N
ANISOU 215 N ASP A1028 16256 9695 11010 -2630 1039 622 N
ATOM 216 CA ASP A1028 35.068 192.653 114.748 1.00 97.05 C
ANISOU 216 CA ASP A1028 16378 9689 10807 -2614 853 646 C
ATOM 217 C ASP A1028 34.567 191.883 115.968 1.00 95.90 C
ANISOU 217 C ASP A1028 15910 9683 10847 -2394 715 621 C
ATOM 218 O ASP A1028 33.371 191.930 116.258 1.00 94.43 O
ANISOU 218 O ASP A1028 15726 9538 10617 -2314 428 678 O
ATOM 219 CB ASP A1028 35.205 191.729 113.522 1.00101.97 C
ANISOU 219 CB ASP A1028 17319 10216 11209 -2790 1094 602 C
ATOM 220 CG ASP A1028 33.903 191.455 112.761 1.00122.92 C
ANISOU 220 CG ASP A1028 20295 12828 13583 -2884 848 672 C
ATOM 221 OD1 ASP A1028 32.810 191.529 113.387 1.00122.87 O
ANISOU 221 OD1 ASP A1028 20157 12900 13628 -2750 512 739 O
ATOM 222 OD2 ASP A1028 33.976 191.136 111.546 1.00134.45 O
ANISOU 222 OD2 ASP A1028 22144 14162 14779 -3100 996 664 O
ATOM 223 N ALA A1029 35.487 191.225 116.707 1.00 89.76 N
ANISOU 223 N ALA A1029 14846 8964 10295 -2302 915 545 N
ATOM 224 CA ALA A1029 35.179 190.497 117.945 1.00 86.31 C
ANISOU 224 CA ALA A1029 14103 8651 10041 -2107 804 519 C
ATOM 225 C ALA A1029 34.664 191.479 119.016 1.00 88.72 C
ANISOU 225 C ALA A1029 14251 9014 10444 -1984 524 568 C
ATOM 226 O ALA A1029 33.695 191.170 119.711 1.00 86.88 O
ANISOU 226 O ALA A1029 13927 8852 10232 -1857 327 580 O
ATOM 227 CB ALA A1029 36.417 189.781 118.447 1.00 86.56 C
ANISOU 227 CB ALA A1029 13875 8701 10314 -2065 1060 453 C
ATOM 228 N LEU A1030 35.277 192.678 119.100 1.00 85.60 N
ANISOU 228 N LEU A1030 13849 8572 10101 -2034 523 595 N
ATOM 229 CA LEU A1030 34.878 193.711 120.050 1.00 84.52 C
ANISOU 229 CA LEU A1030 13610 8460 10044 -1941 295 635 C
ATOM 230 C LEU A1030 33.549 194.358 119.697 1.00 88.02 C
ANISOU 230 C LEU A1030 14236 8864 10343 -1932 54 709 C
ATOM 231 O LEU A1030 32.816 194.745 120.608 1.00 86.62 O
ANISOU 231 O LEU A1030 13948 8716 10247 -1802 -133 729 O
ATOM 232 CB LEU A1030 35.964 194.773 120.221 1.00 85.45 C
ANISOU 232 CB LEU A1030 13677 8528 10261 -2010 366 644 C
ATOM 233 CG LEU A1030 37.155 194.397 121.101 1.00 90.11 C
ANISOU 233 CG LEU A1030 13986 9159 11092 -1974 487 603 C
ATOM 234 CD1 LEU A1030 38.280 195.378 120.895 1.00 92.10 C
ANISOU 234 CD1 LEU A1030 14231 9336 11426 -2092 593 625 C
ATOM 235 CD2 LEU A1030 36.775 194.332 122.580 1.00 90.18 C
ANISOU 235 CD2 LEU A1030 13797 9247 11221 -1826 290 596 C
ATOM 236 N THR A1031 33.226 194.464 118.391 1.00 85.25 N
ANISOU 236 N THR A1031 14171 8430 9792 -2076 58 756 N
ATOM 237 CA THR A1031 31.954 195.031 117.924 1.00 85.00 C
ANISOU 237 CA THR A1031 14316 8337 9643 -2090 -201 856 C
ATOM 238 C THR A1031 30.808 194.089 118.333 1.00 87.97 C
ANISOU 238 C THR A1031 14598 8778 10048 -1966 -349 865 C
ATOM 239 O THR A1031 29.790 194.565 118.842 1.00 88.34 O
ANISOU 239 O THR A1031 14575 8815 10176 -1860 -570 928 O
ATOM 240 CB THR A1031 31.981 195.295 116.401 1.00 90.36 C
ANISOU 240 CB THR A1031 15355 8898 10080 -2309 -173 913 C
ATOM 241 OG1 THR A1031 33.140 196.062 116.062 1.00 91.59 O
ANISOU 241 OG1 THR A1031 15579 8996 10226 -2423 10 892 O
ATOM 242 CG2 THR A1031 30.727 196.016 115.905 1.00 85.80 C
ANISOU 242 CG2 THR A1031 14954 8233 9413 -2341 -486 1048 C
ATOM 243 N LYS A1032 30.996 192.763 118.136 1.00 82.32 N
ANISOU 243 N LYS A1032 13871 8118 9290 -1978 -207 801 N
ATOM 244 CA LYS A1032 30.023 191.718 118.476 1.00 80.80 C
ANISOU 244 CA LYS A1032 13592 7990 9118 -1876 -315 801 C
ATOM 245 C LYS A1032 29.744 191.717 119.975 1.00 81.89 C
ANISOU 245 C LYS A1032 13427 8217 9472 -1672 -387 769 C
ATOM 246 O LYS A1032 28.594 191.570 120.389 1.00 80.80 O
ANISOU 246 O LYS A1032 13218 8092 9388 -1570 -565 813 O
ATOM 247 CB LYS A1032 30.511 190.330 118.019 1.00 82.99 C
ANISOU 247 CB LYS A1032 13918 8298 9316 -1936 -102 723 C
ATOM 248 CG LYS A1032 30.615 190.171 116.501 1.00 94.13 C
ANISOU 248 CG LYS A1032 15694 9601 10471 -2157 -22 748 C
ATOM 249 CD LYS A1032 30.973 188.736 116.103 1.00104.34 C
ANISOU 249 CD LYS A1032 17047 10906 11691 -2206 205 663 C
ATOM 250 CE LYS A1032 31.682 188.643 114.772 1.00111.24 C
ANISOU 250 CE LYS A1032 18264 11654 12347 -2435 446 637 C
ATOM 251 NZ LYS A1032 33.111 189.040 114.875 1.00115.73 N
ANISOU 251 NZ LYS A1032 18737 12198 13038 -2458 748 569 N
ATOM 252 N MET A1033 30.794 191.940 120.775 1.00 77.23 N
ANISOU 252 N MET A1033 12671 7667 9006 -1628 -251 702 N
ATOM 253 CA MET A1033 30.722 192.014 122.232 1.00 75.08 C
ANISOU 253 CA MET A1033 12161 7459 8907 -1472 -303 666 C
ATOM 254 C MET A1033 29.910 193.198 122.702 1.00 78.37 C
ANISOU 254 C MET A1033 12582 7818 9376 -1405 -484 724 C
ATOM 255 O MET A1033 29.150 193.046 123.652 1.00 77.49 O
ANISOU 255 O MET A1033 12345 7734 9363 -1272 -567 715 O
ATOM 256 CB MET A1033 32.116 192.032 122.848 1.00 77.27 C
ANISOU 256 CB MET A1033 12295 7768 9296 -1484 -146 604 C
ATOM 257 CG MET A1033 32.747 190.675 122.860 1.00 81.08 C
ANISOU 257 CG MET A1033 12674 8311 9823 -1483 19 544 C
ATOM 258 SD MET A1033 34.449 190.679 123.429 1.00 86.31 S
ANISOU 258 SD MET A1033 13140 8978 10675 -1516 190 505 S
ATOM 259 CE MET A1033 34.205 190.968 125.176 1.00 81.96 C
ANISOU 259 CE MET A1033 12406 8482 10253 -1386 4 498 C
ATOM 260 N ARG A1034 30.045 194.370 122.032 1.00 75.73 N
ANISOU 260 N ARG A1034 12402 7389 8982 -1498 -529 784 N
ATOM 261 CA ARG A1034 29.288 195.586 122.359 1.00 74.54 C
ANISOU 261 CA ARG A1034 12271 7154 8898 -1441 -688 849 C
ATOM 262 C ARG A1034 27.795 195.376 122.095 1.00 76.39 C
ANISOU 262 C ARG A1034 12524 7347 9153 -1376 -868 933 C
ATOM 263 O ARG A1034 26.982 195.749 122.933 1.00 76.00 O
ANISOU 263 O ARG A1034 12362 7265 9248 -1245 -951 949 O
ATOM 264 CB ARG A1034 29.807 196.792 121.579 1.00 74.27 C
ANISOU 264 CB ARG A1034 12409 7021 8790 -1570 -695 902 C
ATOM 265 CG ARG A1034 29.342 198.120 122.155 1.00 78.13 C
ANISOU 265 CG ARG A1034 12888 7416 9381 -1502 -813 947 C
ATOM 266 CD ARG A1034 29.580 199.259 121.187 1.00 74.88 C
ANISOU 266 CD ARG A1034 12675 6892 8884 -1635 -862 1025 C
ATOM 267 NE ARG A1034 29.711 200.529 121.896 1.00 76.26 N
ANISOU 267 NE ARG A1034 12826 6990 9158 -1591 -890 1027 N
ATOM 268 CZ ARG A1034 28.695 201.322 122.219 1.00 89.78 C
ANISOU 268 CZ ARG A1034 14534 8597 10983 -1496 -1028 1093 C
ATOM 269 NH1 ARG A1034 27.453 200.991 121.887 1.00 75.92 N
ANISOU 269 NH1 ARG A1034 12766 6799 9280 -1434 -1171 1177 N
ATOM 270 NH2 ARG A1034 28.912 202.452 122.883 1.00 71.68 N
ANISOU 270 NH2 ARG A1034 12242 6224 8770 -1466 -1021 1080 N
ATOM 271 N ALA A1035 27.439 194.753 120.959 1.00 71.71 N
ANISOU 271 N ALA A1035 12075 6742 8428 -1478 -920 988 N
ATOM 272 CA ALA A1035 26.047 194.462 120.635 1.00 71.28 C
ANISOU 272 CA ALA A1035 12033 6644 8408 -1442 -1122 1088 C
ATOM 273 C ALA A1035 25.471 193.475 121.662 1.00 72.18 C
ANISOU 273 C ALA A1035 11928 6847 8650 -1283 -1101 1031 C
ATOM 274 O ALA A1035 24.386 193.732 122.184 1.00 72.06 O
ANISOU 274 O ALA A1035 11798 6782 8798 -1166 -1225 1089 O
ATOM 275 CB ALA A1035 25.932 193.909 119.220 1.00 73.08 C
ANISOU 275 CB ALA A1035 12501 6837 8429 -1619 -1181 1151 C
ATOM 276 N ALA A1036 26.238 192.410 122.015 1.00 65.96 N
ANISOU 276 N ALA A1036 11071 6177 7816 -1275 -929 919 N
ATOM 277 CA ALA A1036 25.845 191.395 123.013 1.00 63.76 C
ANISOU 277 CA ALA A1036 10601 5989 7637 -1140 -892 856 C
ATOM 278 C ALA A1036 25.661 192.012 124.413 1.00 66.84 C
ANISOU 278 C ALA A1036 10830 6370 8195 -996 -878 818 C
ATOM 279 O ALA A1036 24.718 191.645 125.117 1.00 66.24 O
ANISOU 279 O ALA A1036 10635 6297 8236 -877 -923 823 O
ATOM 280 CB ALA A1036 26.868 190.267 123.061 1.00 63.45 C
ANISOU 280 CB ALA A1036 10532 6052 7525 -1176 -710 755 C
ATOM 281 N ALA A1037 26.526 192.979 124.791 1.00 62.89 N
ANISOU 281 N ALA A1037 10349 5844 7704 -1019 -811 782 N
ATOM 282 CA ALA A1037 26.436 193.684 126.070 1.00 62.61 C
ANISOU 282 CA ALA A1037 10227 5773 7790 -917 -791 743 C
ATOM 283 C ALA A1037 25.224 194.608 126.122 1.00 67.18 C
ANISOU 283 C ALA A1037 10812 6222 8492 -841 -903 826 C
ATOM 284 O ALA A1037 24.534 194.632 127.142 1.00 66.68 O
ANISOU 284 O ALA A1037 10652 6127 8558 -719 -880 800 O
ATOM 285 CB ALA A1037 27.703 194.470 126.342 1.00 63.59 C
ANISOU 285 CB ALA A1037 10392 5889 7881 -990 -714 698 C
ATOM 286 N LEU A1038 24.936 195.333 125.014 1.00 64.97 N
ANISOU 286 N LEU A1038 10650 5852 8185 -918 -1018 931 N
ATOM 287 CA LEU A1038 23.778 196.232 124.934 1.00 65.86 C
ANISOU 287 CA LEU A1038 10750 5817 8457 -849 -1147 1038 C
ATOM 288 C LEU A1038 22.505 195.417 124.913 1.00 72.31 C
ANISOU 288 C LEU A1038 11451 6626 9397 -765 -1238 1100 C
ATOM 289 O LEU A1038 21.516 195.820 125.527 1.00 73.42 O
ANISOU 289 O LEU A1038 11477 6666 9754 -639 -1254 1137 O
ATOM 290 CB LEU A1038 23.831 197.159 123.711 1.00 66.93 C
ANISOU 290 CB LEU A1038 11049 5850 8530 -970 -1279 1154 C
ATOM 291 CG LEU A1038 24.920 198.230 123.656 1.00 70.87 C
ANISOU 291 CG LEU A1038 11666 6316 8948 -1053 -1210 1120 C
ATOM 292 CD1 LEU A1038 24.940 198.863 122.295 1.00 72.70 C
ANISOU 292 CD1 LEU A1038 12084 6459 9078 -1196 -1344 1239 C
ATOM 293 CD2 LEU A1038 24.731 199.296 124.738 1.00 71.28 C
ANISOU 293 CD2 LEU A1038 11658 6267 9160 -942 -1160 1091 C
ATOM 294 N ASP A1039 22.544 194.250 124.242 1.00 69.31 N
ANISOU 294 N ASP A1039 11099 6342 8892 -836 -1277 1108 N
ATOM 295 CA ASP A1039 21.438 193.297 124.183 1.00 69.92 C
ANISOU 295 CA ASP A1039 11073 6431 9062 -780 -1371 1164 C
ATOM 296 C ASP A1039 21.148 192.778 125.625 1.00 71.15 C
ANISOU 296 C ASP A1039 11044 6635 9353 -622 -1226 1063 C
ATOM 297 O ASP A1039 20.019 192.917 126.104 1.00 71.39 O
ANISOU 297 O ASP A1039 10943 6576 9605 -507 -1261 1117 O
ATOM 298 CB ASP A1039 21.808 192.141 123.228 1.00 72.53 C
ANISOU 298 CB ASP A1039 11517 6861 9181 -911 -1396 1159 C
ATOM 299 CG ASP A1039 20.659 191.267 122.750 1.00 93.38 C
ANISOU 299 CG ASP A1039 14120 9488 11872 -916 -1559 1256 C
ATOM 300 OD1 ASP A1039 20.103 190.502 123.580 1.00 93.86 O
ANISOU 300 OD1 ASP A1039 14007 9599 12058 -796 -1510 1215 O
ATOM 301 OD2 ASP A1039 20.392 191.257 121.524 1.00105.88 O
ANISOU 301 OD2 ASP A1039 15872 11015 13345 -1061 -1732 1368 O
ATOM 302 N ALA A1040 22.186 192.262 126.328 1.00 64.99 N
ANISOU 302 N ALA A1040 10261 5975 8456 -624 -1062 924 N
ATOM 303 CA ALA A1040 22.083 191.733 127.701 1.00 63.52 C
ANISOU 303 CA ALA A1040 9954 5837 8345 -511 -929 823 C
ATOM 304 C ALA A1040 21.582 192.768 128.722 1.00 68.43 C
ANISOU 304 C ALA A1040 10536 6331 9133 -406 -861 808 C
ATOM 305 O ALA A1040 20.958 192.384 129.705 1.00 66.71 O
ANISOU 305 O ALA A1040 10227 6099 9023 -304 -772 762 O
ATOM 306 CB ALA A1040 23.417 191.153 128.147 1.00 62.68 C
ANISOU 306 CB ALA A1040 9871 5855 8088 -563 -810 706 C
ATOM 307 N GLN A1041 21.831 194.076 128.474 1.00 67.08 N
ANISOU 307 N GLN A1041 10452 6055 8983 -437 -887 845 N
ATOM 308 CA GLN A1041 21.411 195.185 129.340 1.00 67.96 C
ANISOU 308 CA GLN A1041 10560 6014 9247 -351 -805 831 C
ATOM 309 C GLN A1041 19.882 195.315 129.436 1.00 76.21 C
ANISOU 309 C GLN A1041 11473 6921 10564 -227 -830 921 C
ATOM 310 O GLN A1041 19.357 195.669 130.499 1.00 76.72 O
ANISOU 310 O GLN A1041 11493 6878 10778 -122 -680 870 O
ATOM 311 CB GLN A1041 22.026 196.486 128.833 1.00 69.58 C
ANISOU 311 CB GLN A1041 10892 6137 9408 -427 -848 866 C
ATOM 312 CG GLN A1041 21.939 197.661 129.801 1.00 68.54 C
ANISOU 312 CG GLN A1041 10807 5855 9378 -366 -731 819 C
ATOM 313 CD GLN A1041 22.636 198.853 129.231 1.00 80.84 C
ANISOU 313 CD GLN A1041 12496 7348 10873 -455 -784 854 C
ATOM 314 OE1 GLN A1041 22.552 199.149 128.026 1.00 79.14 O
ANISOU 314 OE1 GLN A1041 12312 7109 10647 -518 -931 965 O
ATOM 315 NE2 GLN A1041 23.349 199.560 130.083 1.00 73.95 N
ANISOU 315 NE2 GLN A1041 11723 6432 9941 -480 -676 763 N
ATOM 316 N LYS A1042 19.182 195.004 128.328 1.00 75.63 N
ANISOU 316 N LYS A1042 11342 6835 10558 -250 -1015 1058 N
ATOM 317 CA LYS A1042 17.723 195.041 128.200 1.00 77.84 C
ANISOU 317 CA LYS A1042 11463 6979 11136 -152 -1095 1186 C
ATOM 318 C LYS A1042 17.045 193.842 128.868 1.00 82.32 C
ANISOU 318 C LYS A1042 11882 7607 11788 -68 -1014 1144 C
ATOM 319 O LYS A1042 15.838 193.884 129.109 1.00 83.75 O
ANISOU 319 O LYS A1042 11898 7660 12263 37 -1013 1226 O
ATOM 320 CB LYS A1042 17.326 195.115 126.713 1.00 82.03 C
ANISOU 320 CB LYS A1042 12018 7471 11679 -248 -1372 1365 C
ATOM 321 N ALA A1043 17.813 192.777 129.163 1.00 77.81 N
ANISOU 321 N ALA A1043 11360 7219 10986 -115 -943 1026 N
ATOM 322 CA ALA A1043 17.309 191.548 129.787 1.00 76.51 C
ANISOU 322 CA ALA A1043 11081 7129 10859 -54 -869 977 C
ATOM 323 C ALA A1043 16.785 191.745 131.211 1.00 80.71 C
ANISOU 323 C ALA A1043 11544 7565 11555 73 -642 893 C
ATOM 324 O ALA A1043 17.159 192.701 131.900 1.00 78.27 O
ANISOU 324 O ALA A1043 11325 7168 11245 93 -508 824 O
ATOM 325 CB ALA A1043 18.388 190.468 129.774 1.00 75.10 C
ANISOU 325 CB ALA A1043 10983 7150 10400 -139 -846 874 C
ATOM 326 N THR A1044 15.896 190.828 131.632 1.00 79.93 N
ANISOU 326 N THR A1044 11305 7472 11592 146 -593 899 N
ATOM 327 CA THR A1044 15.358 190.777 132.989 1.00 81.08 C
ANISOU 327 CA THR A1044 11405 7529 11871 251 -348 810 C
ATOM 328 C THR A1044 15.854 189.453 133.607 1.00 82.65 C
ANISOU 328 C THR A1044 11642 7902 11861 219 -280 695 C
ATOM 329 O THR A1044 15.407 188.371 133.198 1.00 81.09 O
ANISOU 329 O THR A1044 11338 7790 11681 216 -372 742 O
ATOM 330 CB THR A1044 13.831 190.983 133.034 1.00 96.15 C
ANISOU 330 CB THR A1044 13106 9252 14175 370 -311 923 C
ATOM 331 OG1 THR A1044 13.511 192.252 132.454 1.00 99.57 O
ANISOU 331 OG1 THR A1044 13513 9519 14800 392 -392 1036 O
ATOM 332 CG2 THR A1044 13.275 190.915 134.466 1.00 96.46 C
ANISOU 332 CG2 THR A1044 13122 9176 14352 472 1 817 C
ATOM 333 N PRO A1045 16.841 189.518 134.527 1.00 78.16 N
ANISOU 333 N PRO A1045 11233 7382 11084 177 -152 556 N
ATOM 334 CA PRO A1045 17.336 188.277 135.134 1.00 76.38 C
ANISOU 334 CA PRO A1045 11040 7304 10678 142 -112 464 C
ATOM 335 C PRO A1045 16.298 187.679 136.082 1.00 80.90 C
ANISOU 335 C PRO A1045 11535 7807 11395 229 57 431 C
ATOM 336 O PRO A1045 15.643 188.438 136.803 1.00 81.54 O
ANISOU 336 O PRO A1045 11632 7710 11639 297 240 409 O
ATOM 337 CB PRO A1045 18.619 188.704 135.847 1.00 77.64 C
ANISOU 337 CB PRO A1045 11389 7494 10616 60 -57 357 C
ATOM 338 CG PRO A1045 18.487 190.153 136.063 1.00 83.65 C
ANISOU 338 CG PRO A1045 12231 8084 11467 80 21 360 C
ATOM 339 CD PRO A1045 17.487 190.714 135.110 1.00 80.27 C
ANISOU 339 CD PRO A1045 11661 7552 11286 153 -50 488 C
ATOM 340 N PRO A1046 16.100 186.333 136.069 1.00 77.19 N
ANISOU 340 N PRO A1046 10986 7458 10883 227 20 428 N
ATOM 341 CA PRO A1046 15.097 185.723 136.959 1.00 77.57 C
ANISOU 341 CA PRO A1046 10962 7439 11073 302 191 398 C
ATOM 342 C PRO A1046 15.237 186.070 138.442 1.00 82.58 C
ANISOU 342 C PRO A1046 11767 7969 11640 304 440 270 C
ATOM 343 O PRO A1046 14.217 186.231 139.108 1.00 84.46 O
ANISOU 343 O PRO A1046 11962 8052 12078 382 646 258 O
ATOM 344 CB PRO A1046 15.252 184.224 136.702 1.00 77.82 C
ANISOU 344 CB PRO A1046 10937 7646 10986 266 86 398 C
ATOM 345 CG PRO A1046 16.585 184.066 136.073 1.00 80.97 C
ANISOU 345 CG PRO A1046 11430 8194 11141 168 -70 381 C
ATOM 346 CD PRO A1046 16.784 185.301 135.264 1.00 77.23 C
ANISOU 346 CD PRO A1046 10977 7653 10715 152 -155 445 C
ATOM 347 N LYS A1047 16.475 186.258 138.947 1.00 77.74 N
ANISOU 347 N LYS A1047 11357 7416 10764 208 426 182 N
ATOM 348 CA LYS A1047 16.685 186.602 140.356 1.00 78.31 C
ANISOU 348 CA LYS A1047 11651 7378 10725 171 629 64 C
ATOM 349 C LYS A1047 16.313 188.069 140.681 1.00 86.62 C
ANISOU 349 C LYS A1047 12797 8211 11904 206 797 48 C
ATOM 350 O LYS A1047 16.470 188.485 141.835 1.00 88.40 O
ANISOU 350 O LYS A1047 13253 8312 12023 159 984 -54 O
ATOM 351 CB LYS A1047 18.102 186.229 140.835 1.00 78.40 C
ANISOU 351 CB LYS A1047 11842 7512 10433 39 520 -2 C
ATOM 352 CG LYS A1047 19.219 187.180 140.432 1.00 81.81 C
ANISOU 352 CG LYS A1047 12366 7960 10757 -39 395 7 C
ATOM 353 CD LYS A1047 20.563 186.487 140.511 1.00 84.63 C
ANISOU 353 CD LYS A1047 12781 8473 10901 -153 228 -11 C
ATOM 354 CE LYS A1047 21.214 186.533 141.871 1.00 86.62 C
ANISOU 354 CE LYS A1047 13279 8666 10966 -264 274 -93 C
ATOM 355 NZ LYS A1047 22.339 185.566 141.974 1.00 85.79 N
ANISOU 355 NZ LYS A1047 13166 8710 10721 -357 98 -84 N
ATOM 356 N LEU A1048 15.782 188.827 139.679 1.00 84.11 N
ANISOU 356 N LEU A1048 12316 7828 11813 281 731 153 N
ATOM 357 CA LEU A1048 15.316 190.218 139.821 1.00 85.86 C
ANISOU 357 CA LEU A1048 12581 7825 12218 336 882 160 C
ATOM 358 C LEU A1048 13.888 190.403 139.231 1.00 93.64 C
ANISOU 358 C LEU A1048 13297 8673 13608 475 928 282 C
ATOM 359 O LEU A1048 13.520 191.516 138.856 1.00 94.02 O
ANISOU 359 O LEU A1048 13300 8561 13863 530 956 344 O
ATOM 360 CB LEU A1048 16.310 191.233 139.183 1.00 84.94 C
ANISOU 360 CB LEU A1048 12561 7732 11981 266 722 183 C
ATOM 361 CG LEU A1048 17.775 191.280 139.661 1.00 86.75 C
ANISOU 361 CG LEU A1048 13026 8065 11868 121 648 93 C
ATOM 362 CD1 LEU A1048 18.543 192.335 138.918 1.00 85.67 C
ANISOU 362 CD1 LEU A1048 12938 7927 11686 70 510 135 C
ATOM 363 CD2 LEU A1048 17.883 191.536 141.144 1.00 89.53 C
ANISOU 363 CD2 LEU A1048 13644 8283 12093 67 874 -37 C
ATOM 364 N GLU A1049 13.090 189.308 139.163 1.00 92.95 N
ANISOU 364 N GLU A1049 13026 8639 13652 527 927 326 N
ATOM 365 CA GLU A1049 11.725 189.291 138.617 1.00 95.39 C
ANISOU 365 CA GLU A1049 13048 8827 14370 644 933 462 C
ATOM 366 C GLU A1049 10.726 190.163 139.389 1.00104.38 C
ANISOU 366 C GLU A1049 14151 9669 15840 753 1266 447 C
ATOM 367 O GLU A1049 9.967 190.921 138.771 1.00105.76 O
ANISOU 367 O GLU A1049 14130 9684 16368 840 1236 577 O
ATOM 368 CB GLU A1049 11.206 187.850 138.494 1.00 96.16 C
ANISOU 368 CB GLU A1049 12987 9053 14498 653 864 498 C
ATOM 369 CG GLU A1049 11.603 187.185 137.183 1.00108.92 C
ANISOU 369 CG GLU A1049 14510 10876 15998 589 505 602 C
ATOM 370 CD GLU A1049 11.146 185.752 136.974 1.00139.47 C
ANISOU 370 CD GLU A1049 18246 14874 19872 582 416 637 C
ATOM 371 OE1 GLU A1049 11.220 184.942 137.928 1.00135.31 O
ANISOU 371 OE1 GLU A1049 17796 14395 19220 573 578 527 O
ATOM 372 OE2 GLU A1049 10.761 185.426 135.827 1.00138.57 O
ANISOU 372 OE2 GLU A1049 17977 14812 19863 568 165 779 O
ATOM 373 N ASP A1050 10.715 190.046 140.732 1.00102.93 N
ANISOU 373 N ASP A1050 14165 9393 15552 740 1589 293 N
ATOM 374 CA ASP A1050 9.825 190.815 141.604 1.00106.23 C
ANISOU 374 CA ASP A1050 14604 9504 16253 830 1983 245 C
ATOM 375 C ASP A1050 10.185 192.313 141.675 1.00112.68 C
ANISOU 375 C ASP A1050 15581 10145 17088 831 2074 217 C
ATOM 376 O ASP A1050 9.322 193.132 141.988 1.00114.57 O
ANISOU 376 O ASP A1050 15754 10104 17674 934 2351 232 O
ATOM 377 CB ASP A1050 9.728 190.191 143.011 1.00108.72 C
ANISOU 377 CB ASP A1050 15138 9762 16407 787 2311 83 C
ATOM 378 CG ASP A1050 10.986 189.537 143.565 1.00119.77 C
ANISOU 378 CG ASP A1050 16843 11370 17292 628 2198 -41 C
ATOM 379 OD1 ASP A1050 12.102 189.916 143.127 1.00118.84 O
ANISOU 379 OD1 ASP A1050 16849 11383 16920 542 1957 -45 O
ATOM 380 OD2 ASP A1050 10.856 188.663 144.455 1.00127.20 O
ANISOU 380 OD2 ASP A1050 17899 12328 18102 584 2352 -129 O
ATOM 381 N LYS A1051 11.447 192.662 141.372 1.00108.87 N
ANISOU 381 N LYS A1051 15296 9814 16256 718 1851 182 N
ATOM 382 CA LYS A1051 11.958 194.029 141.377 1.00110.26 C
ANISOU 382 CA LYS A1051 15645 9856 16393 694 1890 155 C
ATOM 383 C LYS A1051 11.403 194.824 140.187 1.00117.39 C
ANISOU 383 C LYS A1051 16282 10671 17651 793 1724 333 C
ATOM 384 O LYS A1051 11.414 194.320 139.060 1.00115.80 O
ANISOU 384 O LYS A1051 15874 10642 17482 790 1398 467 O
ATOM 385 CB LYS A1051 13.496 194.012 141.355 1.00110.37 C
ANISOU 385 CB LYS A1051 15914 10078 15944 532 1669 83 C
ATOM 386 N SER A1052 10.913 196.062 140.447 1.00117.74 N
ANISOU 386 N SER A1052 16349 10429 17957 870 1952 336 N
ATOM 387 CA SER A1052 10.362 196.981 139.437 1.00119.88 C
ANISOU 387 CA SER A1052 16390 10563 18597 964 1814 511 C
ATOM 388 C SER A1052 11.439 197.368 138.408 1.00123.97 C
ANISOU 388 C SER A1052 16986 11269 18848 859 1438 570 C
ATOM 389 O SER A1052 12.615 197.388 138.779 1.00122.66 O
ANISOU 389 O SER A1052 17100 11238 18269 733 1409 443 O
ATOM 390 CB SER A1052 9.816 198.246 140.100 1.00126.45 C
ANISOU 390 CB SER A1052 17292 11039 19713 1054 2177 469 C
ATOM 391 OG SER A1052 10.802 199.244 140.319 1.00134.79 O
ANISOU 391 OG SER A1052 18660 12062 20494 963 2192 374 O
ATOM 392 N PRO A1053 11.085 197.745 137.149 1.00121.30 N
ANISOU 392 N PRO A1053 16424 10920 18743 898 1156 764 N
ATOM 393 CA PRO A1053 12.131 198.116 136.171 1.00119.87 C
ANISOU 393 CA PRO A1053 16351 10906 18289 782 830 812 C
ATOM 394 C PRO A1053 13.093 199.229 136.597 1.00124.88 C
ANISOU 394 C PRO A1053 17277 11475 18699 712 928 700 C
ATOM 395 O PRO A1053 14.227 199.257 136.116 1.00123.17 O
ANISOU 395 O PRO A1053 17204 11444 18152 586 716 681 O
ATOM 396 CB PRO A1053 11.330 198.524 134.927 1.00122.88 C
ANISOU 396 CB PRO A1053 16468 11190 19030 843 575 1046 C
ATOM 397 CG PRO A1053 9.935 198.768 135.415 1.00129.81 C
ANISOU 397 CG PRO A1053 17114 11783 20424 1008 820 1111 C
ATOM 398 CD PRO A1053 9.745 197.797 136.530 1.00124.66 C
ANISOU 398 CD PRO A1053 16498 11181 19687 1027 1096 961 C
ATOM 399 N ASP A1054 12.649 200.123 137.511 1.00123.63 N
ANISOU 399 N ASP A1054 17211 11039 18722 786 1264 624 N
ATOM 400 CA ASP A1054 13.406 201.280 138.002 1.00123.72 C
ANISOU 400 CA ASP A1054 17514 10934 18560 722 1390 519 C
ATOM 401 C ASP A1054 13.915 201.136 139.463 1.00125.44 C
ANISOU 401 C ASP A1054 18057 11119 18485 643 1689 300 C
ATOM 402 O ASP A1054 14.304 202.132 140.080 1.00126.16 O
ANISOU 402 O ASP A1054 18409 11041 18483 597 1866 203 O
ATOM 403 CB ASP A1054 12.565 202.560 137.818 1.00128.91 C
ANISOU 403 CB ASP A1054 18070 11264 19644 847 1525 612 C
ATOM 404 CG ASP A1054 12.022 202.761 136.409 1.00143.35 C
ANISOU 404 CG ASP A1054 19600 13092 21774 907 1199 850 C
ATOM 405 OD1 ASP A1054 11.185 201.934 135.967 1.00143.76 O
ANISOU 405 OD1 ASP A1054 19370 13185 22066 976 1091 971 O
ATOM 406 OD2 ASP A1054 12.396 203.773 135.765 1.00151.00 O
ANISOU 406 OD2 ASP A1054 20627 13999 22748 876 1048 924 O
ATOM 407 N SER A1055 13.950 199.893 139.990 1.00118.92 N
ANISOU 407 N SER A1055 17238 10453 17494 608 1722 228 N
ATOM 408 CA SER A1055 14.424 199.573 141.346 1.00117.94 C
ANISOU 408 CA SER A1055 17432 10314 17067 508 1956 39 C
ATOM 409 C SER A1055 15.976 199.688 141.490 1.00118.72 C
ANISOU 409 C SER A1055 17815 10589 16704 316 1757 -39 C
ATOM 410 O SER A1055 16.657 199.701 140.458 1.00116.73 O
ANISOU 410 O SER A1055 17461 10524 16368 272 1440 52 O
ATOM 411 CB SER A1055 13.954 198.175 141.743 1.00119.74 C
ANISOU 411 CB SER A1055 17551 10660 17284 530 2010 14 C
ATOM 412 OG SER A1055 14.457 197.197 140.851 1.00123.90 O
ANISOU 412 OG SER A1055 17907 11492 17675 489 1653 99 O
ATOM 413 N PRO A1056 16.561 199.760 142.730 1.00114.13 N
ANISOU 413 N PRO A1056 17595 9944 15827 186 1930 -198 N
ATOM 414 CA PRO A1056 18.035 199.849 142.852 1.00111.60 C
ANISOU 414 CA PRO A1056 17510 9781 15113 -6 1704 -245 C
ATOM 415 C PRO A1056 18.776 198.663 142.234 1.00109.19 C
ANISOU 415 C PRO A1056 17041 9806 14639 -64 1379 -186 C
ATOM 416 O PRO A1056 19.776 198.859 141.541 1.00107.39 O
ANISOU 416 O PRO A1056 16796 9728 14278 -147 1119 -135 O
ATOM 417 CB PRO A1056 18.269 199.907 144.370 1.00114.89 C
ANISOU 417 CB PRO A1056 18329 10046 15277 -135 1949 -408 C
ATOM 418 CG PRO A1056 16.984 200.340 144.944 1.00122.16 C
ANISOU 418 CG PRO A1056 19273 10667 16473 -7 2357 -458 C
ATOM 419 CD PRO A1056 15.927 199.766 144.065 1.00117.47 C
ANISOU 419 CD PRO A1056 18243 10133 16257 188 2329 -332 C
ATOM 420 N GLU A1057 18.266 197.441 142.473 1.00102.35 N
ANISOU 420 N GLU A1057 16053 9037 13798 -18 1416 -194 N
ATOM 421 CA GLU A1057 18.806 196.187 141.955 1.00 98.69 C
ANISOU 421 CA GLU A1057 15429 8860 13207 -56 1156 -145 C
ATOM 422 C GLU A1057 18.854 196.157 140.406 1.00 97.72 C
ANISOU 422 C GLU A1057 15018 8886 13224 6 900 -3 C
ATOM 423 O GLU A1057 19.826 195.643 139.844 1.00 95.42 O
ANISOU 423 O GLU A1057 14686 8807 12762 -79 663 28 O
ATOM 424 CB GLU A1057 18.017 194.998 142.524 1.00 99.95 C
ANISOU 424 CB GLU A1057 15516 9047 13415 0 1289 -179 C
ATOM 425 N MET A1058 17.830 196.742 139.733 1.00 92.72 N
ANISOU 425 N MET A1058 14201 8120 12907 141 953 88 N
ATOM 426 CA MET A1058 17.742 196.851 138.268 1.00 90.67 C
ANISOU 426 CA MET A1058 13715 7952 12784 182 710 236 C
ATOM 427 C MET A1058 18.677 197.927 137.729 1.00 93.16 C
ANISOU 427 C MET A1058 14148 8262 12985 96 576 260 C
ATOM 428 O MET A1058 19.213 197.771 136.630 1.00 91.39 O
ANISOU 428 O MET A1058 13836 8193 12696 48 338 344 O
ATOM 429 CB MET A1058 16.305 197.132 137.800 1.00 94.22 C
ANISOU 429 CB MET A1058 13932 8232 13635 341 782 348 C
ATOM 430 CG MET A1058 15.386 195.923 137.846 1.00 97.22 C
ANISOU 430 CG MET A1058 14107 8669 14162 420 813 380 C
ATOM 431 SD MET A1058 15.960 194.418 137.017 1.00 98.48 S
ANISOU 431 SD MET A1058 14157 9157 14103 343 519 424 S
ATOM 432 CE MET A1058 16.077 194.975 135.317 1.00 94.87 C
ANISOU 432 CE MET A1058 13575 8741 13730 324 211 598 C
ATOM 433 N LYS A1059 18.859 199.027 138.493 1.00 90.22 N
ANISOU 433 N LYS A1059 13994 7699 12586 68 745 183 N
ATOM 434 CA LYS A1059 19.762 200.122 138.128 1.00 89.31 C
ANISOU 434 CA LYS A1059 14020 7556 12357 -25 641 193 C
ATOM 435 C LYS A1059 21.204 199.598 138.151 1.00 87.99 C
ANISOU 435 C LYS A1059 13956 7609 11866 -188 461 151 C
ATOM 436 O LYS A1059 21.922 199.798 137.174 1.00 86.70 O
ANISOU 436 O LYS A1059 13739 7559 11642 -249 262 222 O
ATOM 437 CB LYS A1059 19.580 201.339 139.057 1.00 94.08 C
ANISOU 437 CB LYS A1059 14861 7888 12997 -26 887 108 C
ATOM 438 N ASP A1060 21.595 198.867 139.226 1.00 81.81 N
ANISOU 438 N ASP A1060 13308 6880 10898 -261 528 48 N
ATOM 439 CA ASP A1060 22.921 198.237 139.354 1.00 79.99 C
ANISOU 439 CA ASP A1060 13141 6842 10411 -411 352 24 C
ATOM 440 C ASP A1060 23.145 197.170 138.248 1.00 79.02 C
ANISOU 440 C ASP A1060 12766 6953 10306 -388 162 108 C
ATOM 441 O ASP A1060 24.270 197.027 137.743 1.00 77.28 O
ANISOU 441 O ASP A1060 12528 6870 9962 -491 -5 135 O
ATOM 442 CB ASP A1060 23.127 197.623 140.761 1.00 82.54 C
ANISOU 442 CB ASP A1060 13659 7143 10557 -492 448 -85 C
ATOM 443 CG ASP A1060 23.523 198.595 141.874 1.00101.61 C
ANISOU 443 CG ASP A1060 16418 9367 12821 -614 558 -176 C
ATOM 444 OD1 ASP A1060 23.871 199.776 141.557 1.00104.15 O
ANISOU 444 OD1 ASP A1060 16824 9591 13155 -650 537 -158 O
ATOM 445 OD2 ASP A1060 23.531 198.172 143.054 1.00108.38 O
ANISOU 445 OD2 ASP A1060 17485 10168 13528 -693 652 -262 O
ATOM 446 N PHE A1061 22.058 196.457 137.850 1.00 72.34 N
ANISOU 446 N PHE A1061 11729 6130 9628 -259 199 152 N
ATOM 447 CA PHE A1061 22.104 195.467 136.787 1.00 69.55 C
ANISOU 447 CA PHE A1061 11170 5965 9290 -241 39 230 C
ATOM 448 C PHE A1061 22.468 196.140 135.465 1.00 71.62 C
ANISOU 448 C PHE A1061 11379 6253 9580 -271 -112 327 C
ATOM 449 O PHE A1061 23.485 195.781 134.873 1.00 69.93 O
ANISOU 449 O PHE A1061 11150 6186 9233 -364 -240 343 O
ATOM 450 CB PHE A1061 20.780 194.682 136.671 1.00 71.37 C
ANISOU 450 CB PHE A1061 11227 6186 9706 -110 101 267 C
ATOM 451 CG PHE A1061 20.798 193.652 135.559 1.00 71.33 C
ANISOU 451 CG PHE A1061 11047 6359 9696 -110 -70 347 C
ATOM 452 CD1 PHE A1061 21.556 192.490 135.676 1.00 72.86 C
ANISOU 452 CD1 PHE A1061 11228 6732 9724 -175 -131 306 C
ATOM 453 CD2 PHE A1061 20.106 193.872 134.374 1.00 73.46 C
ANISOU 453 CD2 PHE A1061 11187 6603 10123 -61 -179 469 C
ATOM 454 CE1 PHE A1061 21.611 191.561 134.629 1.00 73.43 C
ANISOU 454 CE1 PHE A1061 11171 6949 9780 -185 -262 370 C
ATOM 455 CE2 PHE A1061 20.164 192.944 133.325 1.00 75.71 C
ANISOU 455 CE2 PHE A1061 11366 7035 10364 -91 -337 538 C
ATOM 456 CZ PHE A1061 20.903 191.787 133.463 1.00 72.50 C
ANISOU 456 CZ PHE A1061 10960 6801 9786 -149 -359 480 C
ATOM 457 N ARG A1062 21.666 197.136 135.030 1.00 68.95 N
ANISOU 457 N ARG A1062 11020 5755 9424 -198 -86 393 N
ATOM 458 CA ARG A1062 21.890 197.885 133.788 1.00 68.95 C
ANISOU 458 CA ARG A1062 10999 5745 9454 -233 -234 496 C
ATOM 459 C ARG A1062 23.206 198.658 133.818 1.00 72.29 C
ANISOU 459 C ARG A1062 11582 6186 9700 -365 -273 458 C
ATOM 460 O ARG A1062 23.843 198.817 132.774 1.00 71.32 O
ANISOU 460 O ARG A1062 11450 6140 9509 -442 -406 521 O
ATOM 461 CB ARG A1062 20.711 198.822 133.469 1.00 71.16 C
ANISOU 461 CB ARG A1062 11220 5818 10000 -124 -203 585 C
ATOM 462 CG ARG A1062 19.401 198.102 133.153 1.00 82.45 C
ANISOU 462 CG ARG A1062 12446 7223 11657 -6 -217 667 C
ATOM 463 CD ARG A1062 18.402 199.010 132.450 1.00 92.81 C
ANISOU 463 CD ARG A1062 13659 8346 13259 74 -279 810 C
ATOM 464 NE ARG A1062 17.793 200.005 133.340 1.00 99.53 N
ANISOU 464 NE ARG A1062 14546 8953 14319 171 -62 773 N
ATOM 465 CZ ARG A1062 16.666 199.820 134.023 1.00112.45 C
ANISOU 465 CZ ARG A1062 16063 10446 16219 302 120 768 C
ATOM 466 NH1 ARG A1062 16.015 198.662 133.947 1.00 96.95 N
ANISOU 466 NH1 ARG A1062 13928 8571 14339 350 90 802 N
ATOM 467 NH2 ARG A1062 16.188 200.785 134.798 1.00 99.02 N
ANISOU 467 NH2 ARG A1062 14419 8498 14705 381 354 726 N
ATOM 468 N HIS A1063 23.632 199.102 135.010 1.00 70.48 N
ANISOU 468 N HIS A1063 11513 5878 9388 -406 -158 357 N
ATOM 469 CA HIS A1063 24.887 199.830 135.153 1.00 71.60 C
ANISOU 469 CA HIS A1063 11807 6023 9374 -545 -207 326 C
ATOM 470 C HIS A1063 26.100 198.962 134.846 1.00 73.57 C
ANISOU 470 C HIS A1063 12005 6476 9472 -658 -329 324 C
ATOM 471 O HIS A1063 27.064 199.459 134.251 1.00 73.94 O
ANISOU 471 O HIS A1063 12082 6558 9454 -761 -416 356 O
ATOM 472 CB HIS A1063 25.030 200.498 136.523 1.00 74.41 C
ANISOU 472 CB HIS A1063 12381 6226 9664 -586 -73 225 C
ATOM 473 CG HIS A1063 26.185 201.449 136.566 1.00 79.56 C
ANISOU 473 CG HIS A1063 13190 6847 10191 -730 -145 216 C
ATOM 474 ND1 HIS A1063 26.287 202.515 135.665 1.00 82.44 N
ANISOU 474 ND1 HIS A1063 13562 7144 10617 -740 -199 285 N
ATOM 475 CD2 HIS A1063 27.280 201.441 137.359 1.00 82.05 C
ANISOU 475 CD2 HIS A1063 13648 7192 10336 -879 -194 160 C
ATOM 476 CE1 HIS A1063 27.422 203.126 135.961 1.00 82.57 C
ANISOU 476 CE1 HIS A1063 13722 7151 10499 -888 -257 260 C
ATOM 477 NE2 HIS A1063 28.054 202.523 136.976 1.00 82.82 N
ANISOU 477 NE2 HIS A1063 13835 7237 10397 -979 -266 190 N
ATOM 478 N GLY A1064 26.031 197.684 135.236 1.00 66.88 N
ANISOU 478 N GLY A1064 11074 5747 8592 -635 -322 291 N
ATOM 479 CA GLY A1064 27.073 196.701 134.967 1.00 64.32 C
ANISOU 479 CA GLY A1064 10666 5601 8173 -719 -416 295 C
ATOM 480 C GLY A1064 27.435 196.619 133.497 1.00 65.14 C
ANISOU 480 C GLY A1064 10668 5791 8289 -746 -498 374 C
ATOM 481 O GLY A1064 28.613 196.514 133.144 1.00 65.22 O
ANISOU 481 O GLY A1064 10663 5881 8238 -853 -550 385 O
ATOM 482 N PHE A1065 26.430 196.728 132.632 1.00 60.19 N
ANISOU 482 N PHE A1065 9988 5130 7753 -663 -508 438 N
ATOM 483 CA PHE A1065 26.634 196.702 131.191 1.00 60.11 C
ANISOU 483 CA PHE A1065 9940 5174 7726 -708 -590 519 C
ATOM 484 C PHE A1065 27.180 198.023 130.668 1.00 67.01 C
ANISOU 484 C PHE A1065 10922 5960 8579 -789 -624 558 C
ATOM 485 O PHE A1065 27.868 198.002 129.651 1.00 66.59 O
ANISOU 485 O PHE A1065 10878 5963 8459 -882 -666 599 O
ATOM 486 CB PHE A1065 25.377 196.235 130.446 1.00 61.48 C
ANISOU 486 CB PHE A1065 10031 5337 7990 -620 -636 592 C
ATOM 487 CG PHE A1065 24.995 194.843 130.893 1.00 61.08 C
ANISOU 487 CG PHE A1065 9874 5389 7945 -560 -604 553 C
ATOM 488 CD1 PHE A1065 25.662 193.727 130.394 1.00 62.52 C
ANISOU 488 CD1 PHE A1065 10007 5717 8030 -619 -623 542 C
ATOM 489 CD2 PHE A1065 24.039 194.653 131.881 1.00 62.81 C
ANISOU 489 CD2 PHE A1065 10052 5547 8267 -450 -530 518 C
ATOM 490 CE1 PHE A1065 25.362 192.451 130.862 1.00 62.69 C
ANISOU 490 CE1 PHE A1065 9937 5828 8055 -567 -593 503 C
ATOM 491 CE2 PHE A1065 23.743 193.373 132.355 1.00 65.04 C
ANISOU 491 CE2 PHE A1065 10246 5922 8543 -404 -496 478 C
ATOM 492 CZ PHE A1065 24.387 192.277 131.825 1.00 62.15 C
ANISOU 492 CZ PHE A1065 9830 5708 8078 -461 -541 474 C
ATOM 493 N ASP A1066 26.966 199.158 131.389 1.00 65.16 N
ANISOU 493 N ASP A1066 10788 5580 8391 -769 -584 536 N
ATOM 494 CA ASP A1066 27.560 200.443 130.990 1.00 65.70 C
ANISOU 494 CA ASP A1066 10970 5559 8432 -854 -615 568 C
ATOM 495 C ASP A1066 29.058 200.332 131.247 1.00 69.58 C
ANISOU 495 C ASP A1066 11487 6138 8812 -992 -623 525 C
ATOM 496 O ASP A1066 29.853 200.757 130.413 1.00 68.36 O
ANISOU 496 O ASP A1066 11357 6003 8615 -1093 -659 567 O
ATOM 497 CB ASP A1066 26.953 201.632 131.760 1.00 69.03 C
ANISOU 497 CB ASP A1066 11503 5787 8937 -798 -552 548 C
ATOM 498 CG ASP A1066 25.478 201.898 131.485 1.00 85.87 C
ANISOU 498 CG ASP A1066 13579 7794 11253 -657 -538 612 C
ATOM 499 OD1 ASP A1066 25.083 201.920 130.286 1.00 87.93 O
ANISOU 499 OD1 ASP A1066 13785 8061 11565 -653 -647 719 O
ATOM 500 OD2 ASP A1066 24.731 202.160 132.458 1.00 92.95 O
ANISOU 500 OD2 ASP A1066 14501 8564 12253 -563 -417 563 O
ATOM 501 N ILE A1067 29.436 199.656 132.361 1.00 67.52 N
ANISOU 501 N ILE A1067 11209 5931 8517 -1002 -595 452 N
ATOM 502 CA ILE A1067 30.834 199.392 132.730 1.00 68.03 C
ANISOU 502 CA ILE A1067 11257 6071 8522 -1131 -631 430 C
ATOM 503 C ILE A1067 31.488 198.454 131.690 1.00 71.52 C
ANISOU 503 C ILE A1067 11554 6652 8966 -1171 -640 469 C
ATOM 504 O ILE A1067 32.596 198.729 131.231 1.00 71.22 O
ANISOU 504 O ILE A1067 11500 6634 8926 -1285 -652 496 O
ATOM 505 CB ILE A1067 30.962 198.915 134.209 1.00 71.17 C
ANISOU 505 CB ILE A1067 11695 6464 8884 -1142 -630 361 C
ATOM 506 CG1 ILE A1067 30.582 200.083 135.163 1.00 73.97 C
ANISOU 506 CG1 ILE A1067 12258 6642 9207 -1151 -591 316 C
ATOM 507 CG2 ILE A1067 32.376 198.391 134.524 1.00 69.43 C
ANISOU 507 CG2 ILE A1067 11406 6327 8646 -1274 -709 369 C
ATOM 508 CD1 ILE A1067 30.096 199.637 136.548 1.00 88.21 C
ANISOU 508 CD1 ILE A1067 14160 8396 10961 -1125 -538 239 C
ATOM 509 N LEU A1068 30.767 197.397 131.276 1.00 67.99 N
ANISOU 509 N LEU A1068 11014 6285 8534 -1082 -618 473 N
ATOM 510 CA LEU A1068 31.217 196.446 130.258 1.00 67.21 C
ANISOU 510 CA LEU A1068 10814 6297 8427 -1115 -596 499 C
ATOM 511 C LEU A1068 31.379 197.132 128.892 1.00 69.82 C
ANISOU 511 C LEU A1068 11216 6589 8723 -1184 -592 561 C
ATOM 512 O LEU A1068 32.428 197.002 128.274 1.00 69.47 O
ANISOU 512 O LEU A1068 11148 6581 8668 -1287 -545 573 O
ATOM 513 CB LEU A1068 30.208 195.305 130.170 1.00 66.92 C
ANISOU 513 CB LEU A1068 10704 6324 8398 -1007 -585 491 C
ATOM 514 CG LEU A1068 30.724 193.900 130.425 1.00 71.80 C
ANISOU 514 CG LEU A1068 11197 7060 9025 -1007 -553 458 C
ATOM 515 CD1 LEU A1068 31.165 193.716 131.867 1.00 71.73 C
ANISOU 515 CD1 LEU A1068 11164 7053 9038 -1012 -577 410 C
ATOM 516 CD2 LEU A1068 29.647 192.887 130.113 1.00 74.10 C
ANISOU 516 CD2 LEU A1068 11438 7402 9313 -913 -546 460 C
ATOM 517 N VAL A1069 30.366 197.899 128.449 1.00 66.33 N
ANISOU 517 N VAL A1069 10866 6056 8280 -1135 -638 607 N
ATOM 518 CA VAL A1069 30.394 198.644 127.180 1.00 66.71 C
ANISOU 518 CA VAL A1069 11021 6045 8283 -1211 -667 680 C
ATOM 519 C VAL A1069 31.515 199.690 127.222 1.00 73.47 C
ANISOU 519 C VAL A1069 11945 6848 9123 -1326 -646 679 C
ATOM 520 O VAL A1069 32.209 199.854 126.227 1.00 75.09 O
ANISOU 520 O VAL A1069 12201 7057 9273 -1438 -611 713 O
ATOM 521 CB VAL A1069 29.011 199.235 126.781 1.00 69.76 C
ANISOU 521 CB VAL A1069 11469 6324 8712 -1132 -758 752 C
ATOM 522 CG1 VAL A1069 29.121 200.253 125.643 1.00 70.55 C
ANISOU 522 CG1 VAL A1069 11711 6332 8763 -1229 -816 838 C
ATOM 523 CG2 VAL A1069 28.023 198.128 126.418 1.00 68.43 C
ANISOU 523 CG2 VAL A1069 11231 6211 8558 -1059 -796 779 C
ATOM 524 N GLY A1070 31.731 200.315 128.381 1.00 69.52 N
ANISOU 524 N GLY A1070 11457 6296 8662 -1314 -657 637 N
ATOM 525 CA GLY A1070 32.808 201.280 128.572 1.00 69.52 C
ANISOU 525 CA GLY A1070 11518 6243 8655 -1432 -657 637 C
ATOM 526 C GLY A1070 34.170 200.618 128.450 1.00 72.43 C
ANISOU 526 C GLY A1070 11775 6705 9042 -1539 -607 627 C
ATOM 527 O GLY A1070 35.111 201.230 127.945 1.00 73.25 O
ANISOU 527 O GLY A1070 11904 6779 9148 -1659 -580 657 O
ATOM 528 N GLN A1071 34.276 199.348 128.894 1.00 66.60 N
ANISOU 528 N GLN A1071 10900 6068 8338 -1494 -584 592 N
ATOM 529 CA GLN A1071 35.506 198.565 128.817 1.00 66.32 C
ANISOU 529 CA GLN A1071 10718 6106 8373 -1575 -528 592 C
ATOM 530 C GLN A1071 35.715 198.063 127.386 1.00 72.23 C
ANISOU 530 C GLN A1071 11456 6890 9100 -1617 -409 618 C
ATOM 531 O GLN A1071 36.863 197.957 126.944 1.00 73.32 O
ANISOU 531 O GLN A1071 11522 7029 9306 -1721 -316 634 O
ATOM 532 CB GLN A1071 35.486 197.403 129.823 1.00 66.34 C
ANISOU 532 CB GLN A1071 10592 6186 8428 -1511 -555 554 C
ATOM 533 CG GLN A1071 35.891 197.817 131.239 1.00 75.46 C
ANISOU 533 CG GLN A1071 11767 7295 9608 -1550 -664 538 C
ATOM 534 CD GLN A1071 35.577 196.797 132.314 1.00 85.01 C
ANISOU 534 CD GLN A1071 12916 8556 10827 -1487 -712 502 C
ATOM 535 OE1 GLN A1071 35.426 195.609 132.070 1.00 74.64 O
ANISOU 535 OE1 GLN A1071 11483 7331 9547 -1425 -665 494 O
ATOM 536 NE2 GLN A1071 35.501 197.242 133.548 1.00 86.05 N
ANISOU 536 NE2 GLN A1071 13152 8622 10919 -1515 -805 478 N
ATOM 537 N ILE A1072 34.602 197.771 126.663 1.00 68.30 N
ANISOU 537 N ILE A1072 11040 6402 8511 -1547 -408 626 N
ATOM 538 CA ILE A1072 34.601 197.326 125.263 1.00 68.72 C
ANISOU 538 CA ILE A1072 11158 6464 8488 -1605 -311 651 C
ATOM 539 C ILE A1072 35.054 198.491 124.398 1.00 75.95 C
ANISOU 539 C ILE A1072 12221 7289 9348 -1728 -285 697 C
ATOM 540 O ILE A1072 35.962 198.315 123.596 1.00 76.56 O
ANISOU 540 O ILE A1072 12308 7360 9422 -1841 -141 701 O
ATOM 541 CB ILE A1072 33.235 196.709 124.811 1.00 70.31 C
ANISOU 541 CB ILE A1072 11424 6685 8606 -1517 -370 664 C
ATOM 542 CG1 ILE A1072 33.041 195.302 125.407 1.00 68.55 C
ANISOU 542 CG1 ILE A1072 11052 6563 8432 -1426 -344 615 C
ATOM 543 CG2 ILE A1072 33.107 196.653 123.287 1.00 71.34 C
ANISOU 543 CG2 ILE A1072 11720 6779 8607 -1618 -321 710 C
ATOM 544 CD1 ILE A1072 31.586 194.938 125.650 1.00 71.40 C
ANISOU 544 CD1 ILE A1072 11422 6934 8771 -1302 -450 624 C
ATOM 545 N ASP A1073 34.466 199.684 124.610 1.00 75.04 N
ANISOU 545 N ASP A1073 12216 7090 9205 -1709 -405 730 N
ATOM 546 CA ASP A1073 34.807 200.937 123.926 1.00 76.86 C
ANISOU 546 CA ASP A1073 12598 7221 9386 -1820 -410 780 C
ATOM 547 C ASP A1073 36.254 201.354 124.195 1.00 84.93 C
ANISOU 547 C ASP A1073 13549 8234 10488 -1932 -324 766 C
ATOM 548 O ASP A1073 36.887 201.917 123.308 1.00 87.83 O
ANISOU 548 O ASP A1073 14011 8546 10816 -2060 -243 799 O
ATOM 549 CB ASP A1073 33.832 202.062 124.316 1.00 78.51 C
ANISOU 549 CB ASP A1073 12906 7331 9593 -1750 -556 814 C
ATOM 550 CG ASP A1073 32.405 201.859 123.822 1.00 86.53 C
ANISOU 550 CG ASP A1073 13988 8316 10572 -1660 -657 864 C
ATOM 551 OD1 ASP A1073 32.185 200.946 122.997 1.00 86.49 O
ANISOU 551 OD1 ASP A1073 14004 8362 10495 -1684 -632 881 O
ATOM 552 OD2 ASP A1073 31.504 202.597 124.284 1.00 91.66 O
ANISOU 552 OD2 ASP A1073 14668 8879 11281 -1570 -758 891 O
ATOM 553 N ASP A1074 36.786 201.057 125.391 1.00 81.78 N
ANISOU 553 N ASP A1074 12990 7879 10206 -1899 -349 727 N
ATOM 554 CA ASP A1074 38.177 201.341 125.731 1.00 83.11 C
ANISOU 554 CA ASP A1074 13052 8033 10493 -2011 -303 734 C
ATOM 555 C ASP A1074 39.123 200.428 124.953 1.00 88.87 C
ANISOU 555 C ASP A1074 13660 8805 11303 -2083 -116 736 C
ATOM 556 O ASP A1074 40.163 200.881 124.506 1.00 91.17 O
ANISOU 556 O ASP A1074 13928 9045 11666 -2209 -14 764 O
ATOM 557 CB ASP A1074 38.410 201.268 127.246 1.00 85.08 C
ANISOU 557 CB ASP A1074 13193 8300 10834 -1975 -424 709 C
ATOM 558 CG ASP A1074 38.210 202.600 127.958 1.00103.98 C
ANISOU 558 CG ASP A1074 15726 10595 13186 -1998 -548 713 C
ATOM 559 OD1 ASP A1074 37.213 203.301 127.650 1.00105.56 O
ANISOU 559 OD1 ASP A1074 16089 10733 13286 -1942 -578 717 O
ATOM 560 OD2 ASP A1074 39.058 202.951 128.811 1.00114.09 O
ANISOU 560 OD2 ASP A1074 16959 11847 14545 -2080 -621 720 O
ATOM 561 N ALA A1075 38.732 199.176 124.725 1.00 85.48 N
ANISOU 561 N ALA A1075 13167 8449 10862 -2008 -49 706 N
ATOM 562 CA ALA A1075 39.507 198.216 123.937 1.00 85.98 C
ANISOU 562 CA ALA A1075 13138 8531 10998 -2065 167 697 C
ATOM 563 C ALA A1075 39.310 198.454 122.416 1.00 90.78 C
ANISOU 563 C ALA A1075 13972 9079 11442 -2160 310 710 C
ATOM 564 O ALA A1075 40.200 198.121 121.630 1.00 91.24 O
ANISOU 564 O ALA A1075 14011 9099 11556 -2262 538 706 O
ATOM 565 CB ALA A1075 39.107 196.797 124.311 1.00 85.22 C
ANISOU 565 CB ALA A1075 12919 8524 10937 -1954 180 657 C
ATOM 566 N LEU A1076 38.138 199.016 122.015 1.00 86.88 N
ANISOU 566 N LEU A1076 13697 8559 10756 -2133 177 731 N
ATOM 567 CA LEU A1076 37.781 199.338 120.626 1.00 87.65 C
ANISOU 567 CA LEU A1076 14056 8584 10662 -2238 240 764 C
ATOM 568 C LEU A1076 38.593 200.524 120.150 1.00 92.01 C
ANISOU 568 C LEU A1076 14709 9041 11211 -2381 305 800 C
ATOM 569 O LEU A1076 39.029 200.532 119.001 1.00 92.49 O
ANISOU 569 O LEU A1076 14929 9036 11178 -2521 484 809 O
ATOM 570 CB LEU A1076 36.281 199.645 120.463 1.00 87.14 C
ANISOU 570 CB LEU A1076 14158 8504 10449 -2166 25 805 C
ATOM 571 CG LEU A1076 35.396 198.544 119.877 1.00 91.63 C
ANISOU 571 CG LEU A1076 14804 9110 10904 -2133 19 802 C
ATOM 572 CD1 LEU A1076 33.953 199.004 119.811 1.00 91.70 C
ANISOU 572 CD1 LEU A1076 14925 9084 10835 -2060 -225 868 C
ATOM 573 CD2 LEU A1076 35.850 198.125 118.478 1.00 95.62 C
ANISOU 573 CD2 LEU A1076 15516 9558 11256 -2301 214 803 C
ATOM 574 N LYS A1077 38.789 201.524 121.038 1.00 88.70 N
ANISOU 574 N LYS A1077 14219 8601 10881 -2358 169 818 N
ATOM 575 CA LYS A1077 39.614 202.713 120.809 1.00 90.06 C
ANISOU 575 CA LYS A1077 14453 8685 11080 -2488 206 853 C
ATOM 576 C LYS A1077 41.060 202.237 120.575 1.00 98.08 C
ANISOU 576 C LYS A1077 15309 9697 12261 -2593 453 837 C
ATOM 577 O LYS A1077 41.681 202.671 119.607 1.00 99.73 O
ANISOU 577 O LYS A1077 15640 9824 12429 -2739 625 857 O
ATOM 578 CB LYS A1077 39.516 203.684 122.003 1.00 90.66 C
ANISOU 578 CB LYS A1077 14470 8745 11233 -2431 8 864 C
ATOM 579 CG LYS A1077 40.385 204.929 121.894 1.00 97.99 C
ANISOU 579 CG LYS A1077 15451 9580 12199 -2566 23 901 C
ATOM 580 CD LYS A1077 41.639 204.822 122.770 1.00106.32 C
ANISOU 580 CD LYS A1077 16264 10657 13477 -2612 55 894 C
ATOM 581 CE LYS A1077 42.865 205.352 122.068 1.00116.13 C
ANISOU 581 CE LYS A1077 17495 11824 14805 -2786 223 931 C
ATOM 582 NZ LYS A1077 44.111 204.953 122.767 1.00125.86 N
ANISOU 582 NZ LYS A1077 18439 13074 16309 -2833 269 944 N
ATOM 583 N LEU A1078 41.551 201.293 121.416 1.00 95.80 N
ANISOU 583 N LEU A1078 14749 9483 12169 -2520 481 807 N
ATOM 584 CA LEU A1078 42.879 200.675 121.325 1.00 97.65 C
ANISOU 584 CA LEU A1078 14762 9703 12637 -2591 706 804 C
ATOM 585 C LEU A1078 43.077 199.905 120.023 1.00104.47 C
ANISOU 585 C LEU A1078 15729 10529 13436 -2662 1007 776 C
ATOM 586 O LEU A1078 44.183 199.912 119.488 1.00106.02 O
ANISOU 586 O LEU A1078 15852 10649 13783 -2777 1260 784 O
ATOM 587 CB LEU A1078 43.140 199.736 122.520 1.00 96.94 C
ANISOU 587 CB LEU A1078 14379 9695 12760 -2483 622 792 C
ATOM 588 CG LEU A1078 43.358 200.393 123.887 1.00101.64 C
ANISOU 588 CG LEU A1078 14853 10300 13465 -2464 368 824 C
ATOM 589 CD1 LEU A1078 43.220 199.394 124.983 1.00100.26 C
ANISOU 589 CD1 LEU A1078 14485 10205 13402 -2353 249 809 C
ATOM 590 CD2 LEU A1078 44.715 201.095 123.980 1.00107.22 C
ANISOU 590 CD2 LEU A1078 15422 10926 14392 -2607 417 884 C
ATOM 591 N ALA A1079 42.022 199.231 119.520 1.00102.05 N
ANISOU 591 N ALA A1079 15596 10259 12918 -2603 991 744 N
ATOM 592 CA ALA A1079 42.096 198.466 118.270 1.00103.90 C
ANISOU 592 CA ALA A1079 15996 10441 13039 -2689 1268 710 C
ATOM 593 C ALA A1079 42.043 199.395 117.049 1.00110.89 C
ANISOU 593 C ALA A1079 17221 11213 13698 -2859 1351 739 C
ATOM 594 O ALA A1079 42.766 199.161 116.084 1.00112.57 O
ANISOU 594 O ALA A1079 17538 11332 13901 -2998 1666 718 O
ATOM 595 CB ALA A1079 40.989 197.425 118.209 1.00103.23 C
ANISOU 595 CB ALA A1079 15988 10429 12804 -2586 1187 676 C
ATOM 596 N ASN A1080 41.216 200.464 117.109 1.00107.85 N
ANISOU 596 N ASN A1080 17011 10820 13147 -2853 1082 789 N
ATOM 597 CA ASN A1080 41.089 201.470 116.045 1.00109.74 C
ANISOU 597 CA ASN A1080 17580 10944 13170 -3015 1096 836 C
ATOM 598 C ASN A1080 42.311 202.406 115.963 1.00115.80 C
ANISOU 598 C ASN A1080 18296 11631 14073 -3142 1249 856 C
ATOM 599 O ASN A1080 42.517 203.062 114.935 1.00116.82 O
ANISOU 599 O ASN A1080 18695 11647 14044 -3312 1369 883 O
ATOM 600 CB ASN A1080 39.776 202.252 116.162 1.00110.36 C
ANISOU 600 CB ASN A1080 17831 11023 13077 -2954 752 898 C
ATOM 601 CG ASN A1080 38.565 201.486 115.676 1.00137.80 C
ANISOU 601 CG ASN A1080 21474 14522 16363 -2913 639 907 C
ATOM 602 OD1 ASN A1080 37.627 201.213 116.436 1.00129.75 O
ANISOU 602 OD1 ASN A1080 20337 13579 15383 -2749 417 913 O
ATOM 603 ND2 ASN A1080 38.545 201.134 114.392 1.00132.99 N
ANISOU 603 ND2 ASN A1080 21160 13832 15540 -3074 792 911 N
ATOM 604 N GLU A1081 43.126 202.443 117.044 1.00111.96 N
ANISOU 604 N GLU A1081 17469 11193 13880 -3074 1237 851 N
ATOM 605 CA GLU A1081 44.385 203.184 117.132 1.00112.70 C
ANISOU 605 CA GLU A1081 17434 11215 14174 -3187 1371 878 C
ATOM 606 C GLU A1081 45.551 202.229 116.768 1.00117.96 C
ANISOU 606 C GLU A1081 17908 11840 15071 -3247 1745 844 C
ATOM 607 O GLU A1081 46.717 202.554 116.998 1.00119.25 O
ANISOU 607 O GLU A1081 17857 11949 15503 -3319 1876 873 O
ATOM 608 CB GLU A1081 44.570 203.818 118.526 1.00112.78 C
ANISOU 608 CB GLU A1081 17205 11276 14369 -3102 1107 909 C
ATOM 609 N GLY A1082 45.202 201.062 116.211 1.00113.83 N
ANISOU 609 N GLY A1082 17461 11330 14460 -3220 1914 790 N
ATOM 610 CA GLY A1082 46.122 200.041 115.718 1.00114.96 C
ANISOU 610 CA GLY A1082 17477 11409 14793 -3269 2311 746 C
ATOM 611 C GLY A1082 46.885 199.196 116.715 1.00118.75 C
ANISOU 611 C GLY A1082 17508 11940 15674 -3155 2351 747 C
ATOM 612 O GLY A1082 47.497 198.206 116.307 1.00119.98 O
ANISOU 612 O GLY A1082 17552 12036 15999 -3169 2682 709 O
ATOM 613 N LYS A1083 46.875 199.562 118.016 1.00114.05 N
ANISOU 613 N LYS A1083 16663 11434 15236 -3052 2024 794 N
ATOM 614 CA LYS A1083 47.581 198.806 119.065 1.00113.77 C
ANISOU 614 CA LYS A1083 16209 11438 15579 -2959 1990 818 C
ATOM 615 C LYS A1083 46.917 197.432 119.350 1.00115.56 C
ANISOU 615 C LYS A1083 16376 11756 15776 -2811 1967 765 C
ATOM 616 O LYS A1083 45.837 197.382 119.944 1.00113.17 O
ANISOU 616 O LYS A1083 16160 11561 15277 -2700 1675 750 O
ATOM 617 CB LYS A1083 47.752 199.656 120.337 1.00115.33 C
ANISOU 617 CB LYS A1083 16232 11684 15905 -2934 1634 887 C
ATOM 618 N VAL A1084 47.573 196.328 118.907 1.00112.91 N
ANISOU 618 N VAL A1084 15891 11359 15652 -2813 2300 736 N
ATOM 619 CA VAL A1084 47.087 194.935 119.009 1.00111.50 C
ANISOU 619 CA VAL A1084 15661 11237 15468 -2692 2351 682 C
ATOM 620 C VAL A1084 47.149 194.367 120.442 1.00113.37 C
ANISOU 620 C VAL A1084 15554 11572 15950 -2549 2076 723 C
ATOM 621 O VAL A1084 46.114 193.936 120.953 1.00110.88 O
ANISOU 621 O VAL A1084 15313 11371 15444 -2433 1843 693 O
ATOM 622 CB VAL A1084 47.786 193.992 117.980 1.00117.54 C
ANISOU 622 CB VAL A1084 16418 11870 16371 -2754 2843 631 C
ATOM 623 CG1 VAL A1084 47.417 192.527 118.202 1.00116.41 C
ANISOU 623 CG1 VAL A1084 16180 11775 16276 -2626 2895 582 C
ATOM 624 CG2 VAL A1084 47.456 194.405 116.551 1.00118.62 C
ANISOU 624 CG2 VAL A1084 16999 11913 16159 -2907 3088 577 C
ATOM 625 N LYS A1085 48.343 194.322 121.063 1.00111.31 N
ANISOU 625 N LYS A1085 14923 11254 16116 -2567 2102 799 N
ATOM 626 CA LYS A1085 48.522 193.766 122.416 1.00110.53 C
ANISOU 626 CA LYS A1085 14506 11222 16268 -2463 1828 858 C
ATOM 627 C LYS A1085 47.811 194.602 123.511 1.00111.54 C
ANISOU 627 C LYS A1085 14723 11456 16202 -2431 1378 885 C
ATOM 628 O LYS A1085 47.414 194.056 124.542 1.00109.13 O
ANISOU 628 O LYS A1085 14315 11234 15917 -2332 1129 896 O
ATOM 629 CB LYS A1085 50.025 193.548 122.726 1.00115.62 C
ANISOU 629 CB LYS A1085 14732 11749 17449 -2516 1952 958 C
ATOM 630 CG LYS A1085 50.355 192.685 123.958 1.00125.29 C
ANISOU 630 CG LYS A1085 15606 13005 18992 -2425 1720 1035 C
ATOM 631 CD LYS A1085 50.046 191.201 123.780 1.00133.93 C
ANISOU 631 CD LYS A1085 16632 14114 20143 -2305 1897 978 C
ATOM 632 CE LYS A1085 50.690 190.352 124.852 1.00145.98 C
ANISOU 632 CE LYS A1085 17758 15621 22086 -2244 1724 1082 C
ATOM 633 NZ LYS A1085 50.275 188.925 124.758 1.00153.06 N
ANISOU 633 NZ LYS A1085 18610 16540 23005 -2117 1860 1024 N
ATOM 634 N GLU A1086 47.629 195.911 123.260 1.00108.06 N
ANISOU 634 N GLU A1086 14497 10999 15563 -2518 1296 890 N
ATOM 635 CA GLU A1086 46.948 196.833 124.172 1.00106.20 C
ANISOU 635 CA GLU A1086 14390 10829 15131 -2499 928 905 C
ATOM 636 C GLU A1086 45.438 196.536 124.236 1.00105.85 C
ANISOU 636 C GLU A1086 14591 10889 14739 -2375 799 828 C
ATOM 637 O GLU A1086 44.866 196.551 125.327 1.00103.30 O
ANISOU 637 O GLU A1086 14259 10633 14357 -2298 525 830 O
ATOM 638 CB GLU A1086 47.220 198.299 123.776 1.00108.50 C
ANISOU 638 CB GLU A1086 14841 11052 15333 -2628 915 933 C
ATOM 639 N ALA A1087 44.811 196.246 123.070 1.00101.47 N
ANISOU 639 N ALA A1087 14258 10331 13964 -2370 1002 767 N
ATOM 640 CA ALA A1087 43.390 195.899 122.956 1.00 98.98 C
ANISOU 640 CA ALA A1087 14162 10097 13350 -2267 895 710 C
ATOM 641 C ALA A1087 43.124 194.483 123.491 1.00101.69 C
ANISOU 641 C ALA A1087 14342 10515 13779 -2143 886 680 C
ATOM 642 O ALA A1087 42.041 194.227 124.011 1.00 99.26 O
ANISOU 642 O ALA A1087 14114 10288 13311 -2037 698 653 O
ATOM 643 CB ALA A1087 42.926 196.024 121.513 1.00100.18 C
ANISOU 643 CB ALA A1087 14610 10199 13254 -2337 1086 677 C
ATOM 644 N GLN A1088 44.121 193.580 123.398 1.00 99.43 N
ANISOU 644 N GLN A1088 13815 10188 13774 -2156 1092 691 N
ATOM 645 CA GLN A1088 44.032 192.218 123.923 1.00 98.93 C
ANISOU 645 CA GLN A1088 13571 10179 13840 -2046 1092 673 C
ATOM 646 C GLN A1088 44.126 192.238 125.452 1.00103.68 C
ANISOU 646 C GLN A1088 13977 10836 14583 -1989 778 725 C
ATOM 647 O GLN A1088 43.611 191.333 126.119 1.00103.07 O
ANISOU 647 O GLN A1088 13834 10829 14501 -1885 667 707 O
ATOM 648 CB GLN A1088 45.151 191.343 123.347 1.00102.35 C
ANISOU 648 CB GLN A1088 13795 10519 14575 -2082 1426 680 C
ATOM 649 CG GLN A1088 44.910 190.899 121.909 1.00120.54 C
ANISOU 649 CG GLN A1088 16332 12764 16704 -2128 1768 606 C
ATOM 650 CD GLN A1088 46.030 190.060 121.340 1.00140.81 C
ANISOU 650 CD GLN A1088 18705 15208 19588 -2164 2153 602 C
ATOM 651 OE1 GLN A1088 46.904 189.548 122.053 1.00136.87 O
ANISOU 651 OE1 GLN A1088 17849 14678 19478 -2123 2154 661 O
ATOM 652 NE2 GLN A1088 46.005 189.871 120.032 1.00134.27 N
ANISOU 652 NE2 GLN A1088 18121 14290 18606 -2249 2495 536 N
ATOM 653 N ALA A1089 44.811 193.262 126.001 1.00101.12 N
ANISOU 653 N ALA A1089 13577 10465 14377 -2075 635 793 N
ATOM 654 CA ALA A1089 45.003 193.454 127.438 1.00100.28 C
ANISOU 654 CA ALA A1089 13341 10382 14380 -2070 321 852 C
ATOM 655 C ALA A1089 43.703 193.933 128.069 1.00100.97 C
ANISOU 655 C ALA A1089 13675 10543 14146 -2002 89 802 C
ATOM 656 O ALA A1089 43.257 193.348 129.057 1.00 99.54 O
ANISOU 656 O ALA A1089 13458 10416 13947 -1929 -86 796 O
ATOM 657 CB ALA A1089 46.119 194.462 127.688 1.00102.80 C
ANISOU 657 CB ALA A1089 13545 10611 14903 -2209 252 941 C
ATOM 658 N ALA A1090 43.079 194.965 127.464 1.00 96.77 N
ANISOU 658 N ALA A1090 13395 9998 13374 -2026 106 769 N
ATOM 659 CA ALA A1090 41.817 195.559 127.900 1.00 95.56 C
ANISOU 659 CA ALA A1090 13475 9883 12950 -1959 -68 726 C
ATOM 660 C ALA A1090 40.637 194.602 127.730 1.00100.13 C
ANISOU 660 C ALA A1090 14127 10541 13376 -1826 -40 665 C
ATOM 661 O ALA A1090 39.681 194.678 128.508 1.00 99.43 O
ANISOU 661 O ALA A1090 14130 10488 13161 -1746 -199 637 O
ATOM 662 CB ALA A1090 41.559 196.850 127.148 1.00 96.56 C
ANISOU 662 CB ALA A1090 13819 9953 12916 -2023 -38 726 C
ATOM 663 N ALA A1091 40.709 193.696 126.730 1.00 96.78 N
ANISOU 663 N ALA A1091 13672 10131 12969 -1813 175 642 N
ATOM 664 CA ALA A1091 39.677 192.700 126.476 1.00 95.34 C
ANISOU 664 CA ALA A1091 13555 10015 12653 -1707 206 591 C
ATOM 665 C ALA A1091 39.715 191.599 127.519 1.00 99.37 C
ANISOU 665 C ALA A1091 13878 10585 13292 -1623 122 587 C
ATOM 666 O ALA A1091 38.655 191.099 127.881 1.00 97.71 O
ANISOU 666 O ALA A1091 13734 10436 12954 -1524 37 550 O
ATOM 667 CB ALA A1091 39.838 192.108 125.090 1.00 96.91 C
ANISOU 667 CB ALA A1091 13817 10188 12818 -1749 467 568 C
ATOM 668 N GLU A1092 40.922 191.227 128.014 1.00 97.65 N
ANISOU 668 N GLU A1092 13423 10337 13342 -1668 132 634 N
ATOM 669 CA GLU A1092 41.102 190.177 129.030 1.00 97.16 C
ANISOU 669 CA GLU A1092 13174 10313 13430 -1609 27 652 C
ATOM 670 C GLU A1092 40.566 190.607 130.406 1.00 98.08 C
ANISOU 670 C GLU A1092 13364 10455 13448 -1588 -253 657 C
ATOM 671 O GLU A1092 40.255 189.749 131.233 1.00 96.91 O
ANISOU 671 O GLU A1092 13157 10350 13315 -1524 -356 652 O
ATOM 672 CB GLU A1092 42.569 189.704 129.100 1.00100.70 C
ANISOU 672 CB GLU A1092 13331 10694 14235 -1673 104 726 C
ATOM 673 CG GLU A1092 42.779 188.344 129.767 1.00114.19 C
ANISOU 673 CG GLU A1092 14833 12426 16130 -1605 62 748 C
ATOM 674 CD GLU A1092 42.409 187.071 129.017 1.00139.98 C
ANISOU 674 CD GLU A1092 18080 15721 19387 -1515 286 689 C
ATOM 675 OE1 GLU A1092 41.661 187.142 128.014 1.00135.84 O
ANISOU 675 OE1 GLU A1092 17762 15219 18631 -1495 442 615 O
ATOM 676 OE2 GLU A1092 42.858 185.986 129.457 1.00136.01 O
ANISOU 676 OE2 GLU A1092 17364 15206 19108 -1473 287 723 O
ATOM 677 N GLN A1093 40.417 191.932 130.626 1.00 93.29 N
ANISOU 677 N GLN A1093 12912 9809 12725 -1646 -358 663 N
ATOM 678 CA GLN A1093 39.838 192.509 131.846 1.00 91.68 C
ANISOU 678 CA GLN A1093 12844 9598 12391 -1642 -577 653 C
ATOM 679 C GLN A1093 38.334 192.162 131.951 1.00 92.33 C
ANISOU 679 C GLN A1093 13081 9738 12263 -1512 -575 579 C
ATOM 680 O GLN A1093 37.808 192.019 133.058 1.00 91.89 O
ANISOU 680 O GLN A1093 13089 9686 12137 -1479 -706 559 O
ATOM 681 CB GLN A1093 40.050 194.028 131.881 1.00 93.35 C
ANISOU 681 CB GLN A1093 13197 9733 12538 -1737 -643 671 C
ATOM 682 CG GLN A1093 41.433 194.434 132.380 1.00103.25 C
ANISOU 682 CG GLN A1093 14312 10919 13999 -1881 -750 757 C
ATOM 683 CD GLN A1093 41.693 195.901 132.167 1.00123.43 C
ANISOU 683 CD GLN A1093 17003 13398 16497 -1982 -779 774 C
ATOM 684 OE1 GLN A1093 41.018 196.772 132.726 1.00119.75 O
ANISOU 684 OE1 GLN A1093 16755 12894 15851 -1986 -887 741 O
ATOM 685 NE2 GLN A1093 42.694 196.209 131.360 1.00118.29 N
ANISOU 685 NE2 GLN A1093 16229 12706 16009 -2069 -666 825 N
ATOM 686 N LEU A1094 37.667 191.979 130.789 1.00 86.14 N
ANISOU 686 N LEU A1094 12358 8985 11388 -1451 -424 546 N
ATOM 687 CA LEU A1094 36.253 191.618 130.682 1.00 83.26 C
ANISOU 687 CA LEU A1094 12106 8664 10864 -1336 -419 496 C
ATOM 688 C LEU A1094 35.962 190.221 131.209 1.00 83.78 C
ANISOU 688 C LEU A1094 12066 8801 10967 -1256 -427 474 C
ATOM 689 O LEU A1094 34.810 189.927 131.518 1.00 81.59 O
ANISOU 689 O LEU A1094 11865 8552 10583 -1164 -461 438 O
ATOM 690 CB LEU A1094 35.742 191.769 129.247 1.00 83.04 C
ANISOU 690 CB LEU A1094 12177 8635 10739 -1329 -294 492 C
ATOM 691 CG LEU A1094 35.533 193.189 128.784 1.00 88.46 C
ANISOU 691 CG LEU A1094 13022 9249 11340 -1380 -319 512 C
ATOM 692 CD1 LEU A1094 36.017 193.362 127.371 1.00 89.75 C
ANISOU 692 CD1 LEU A1094 13233 9384 11483 -1466 -176 534 C
ATOM 693 CD2 LEU A1094 34.079 193.591 128.902 1.00 90.54 C
ANISOU 693 CD2 LEU A1094 13424 9495 11482 -1289 -399 500 C
ATOM 694 N LYS A1095 36.996 189.365 131.330 1.00 79.99 N
ANISOU 694 N LYS A1095 11398 8334 10661 -1289 -395 502 N
ATOM 695 CA LYS A1095 36.844 188.018 131.876 1.00 78.75 C
ANISOU 695 CA LYS A1095 11128 8231 10561 -1222 -414 491 C
ATOM 696 C LYS A1095 36.519 188.112 133.370 1.00 81.09 C
ANISOU 696 C LYS A1095 11479 8522 10810 -1214 -605 489 C
ATOM 697 O LYS A1095 35.788 187.273 133.892 1.00 80.56 O
ANISOU 697 O LYS A1095 11421 8500 10688 -1138 -632 458 O
ATOM 698 CB LYS A1095 38.099 187.174 131.629 1.00 82.66 C
ANISOU 698 CB LYS A1095 11394 8711 11300 -1263 -331 537 C
ATOM 699 N THR A1096 37.020 189.159 134.040 1.00 76.97 N
ANISOU 699 N THR A1096 11023 7934 10289 -1307 -729 519 N
ATOM 700 CA THR A1096 36.753 189.402 135.457 1.00 76.32 C
ANISOU 700 CA THR A1096 11060 7815 10124 -1338 -901 513 C
ATOM 701 C THR A1096 35.412 190.134 135.642 1.00 76.92 C
ANISOU 701 C THR A1096 11361 7868 9996 -1271 -872 444 C
ATOM 702 O THR A1096 34.627 189.733 136.505 1.00 77.37 O
ANISOU 702 O THR A1096 11509 7926 9962 -1222 -905 404 O
ATOM 703 CB THR A1096 37.953 190.101 136.125 1.00 86.13 C
ANISOU 703 CB THR A1096 12282 8977 11468 -1491 -1060 586 C
ATOM 704 OG1 THR A1096 39.124 189.314 135.890 1.00 87.21 O
ANISOU 704 OG1 THR A1096 12160 9121 11854 -1533 -1071 664 O
ATOM 705 CG2 THR A1096 37.759 190.316 137.638 1.00 83.16 C
ANISOU 705 CG2 THR A1096 12083 8539 10975 -1562 -1251 584 C
ATOM 706 N THR A1097 35.142 191.182 134.836 1.00 69.99 N
ANISOU 706 N THR A1097 10568 6958 9069 -1269 -800 435 N
ATOM 707 CA THR A1097 33.892 191.941 134.944 1.00 68.58 C
ANISOU 707 CA THR A1097 10571 6732 8754 -1199 -765 386 C
ATOM 708 C THR A1097 32.657 191.152 134.470 1.00 71.23 C
ANISOU 708 C THR A1097 10883 7127 9053 -1062 -677 354 C
ATOM 709 O THR A1097 31.579 191.376 135.019 1.00 70.78 O
ANISOU 709 O THR A1097 10934 7029 8930 -991 -662 316 O
ATOM 710 CB THR A1097 33.982 193.321 134.298 1.00 70.99 C
ANISOU 710 CB THR A1097 10972 6965 9034 -1243 -742 402 C
ATOM 711 OG1 THR A1097 34.446 193.213 132.953 1.00 62.38 O
ANISOU 711 OG1 THR A1097 9783 5918 8001 -1258 -661 437 O
ATOM 712 CG2 THR A1097 34.844 194.279 135.106 1.00 71.60 C
ANISOU 712 CG2 THR A1097 11138 6955 9112 -1375 -848 422 C
ATOM 713 N ARG A1098 32.812 190.188 133.524 1.00 67.34 N
ANISOU 713 N ARG A1098 10256 6718 8613 -1032 -611 370 N
ATOM 714 CA ARG A1098 31.711 189.325 133.074 1.00 65.28 C
ANISOU 714 CA ARG A1098 9974 6513 8317 -924 -553 348 C
ATOM 715 C ARG A1098 31.211 188.484 134.244 1.00 65.44 C
ANISOU 715 C ARG A1098 9985 6557 8324 -869 -589 313 C
ATOM 716 O ARG A1098 30.035 188.159 134.287 1.00 64.68 O
ANISOU 716 O ARG A1098 9919 6467 8191 -777 -558 290 O
ATOM 717 CB ARG A1098 32.125 188.425 131.894 1.00 67.31 C
ANISOU 717 CB ARG A1098 10127 6836 8613 -932 -467 366 C
ATOM 718 CG ARG A1098 32.920 187.179 132.291 1.00 84.53 C
ANISOU 718 CG ARG A1098 12156 9070 10893 -942 -457 365 C
ATOM 719 CD ARG A1098 33.456 186.374 131.121 1.00 95.34 C
ANISOU 719 CD ARG A1098 13438 10470 12316 -961 -326 374 C
ATOM 720 NE ARG A1098 34.531 185.476 131.548 1.00 99.21 N
ANISOU 720 NE ARG A1098 13754 10973 12967 -985 -310 391 N
ATOM 721 CZ ARG A1098 34.352 184.222 131.941 1.00114.31 C
ANISOU 721 CZ ARG A1098 15580 12931 14920 -927 -311 377 C
ATOM 722 NH1 ARG A1098 33.140 183.688 131.948 1.00108.25 N
ANISOU 722 NH1 ARG A1098 14886 12210 14035 -845 -317 340 N
ATOM 723 NH2 ARG A1098 35.386 183.488 132.327 1.00103.28 N
ANISOU 723 NH2 ARG A1098 14012 11525 13705 -952 -311 410 N
ATOM 724 N ASN A1099 32.105 188.142 135.193 1.00 60.59 N
ANISOU 724 N ASN A1099 9332 5941 7748 -936 -666 320 N
ATOM 725 CA ASN A1099 31.748 187.384 136.388 1.00 59.88 C
ANISOU 725 CA ASN A1099 9270 5858 7625 -913 -717 293 C
ATOM 726 C ASN A1099 30.976 188.241 137.374 1.00 62.75 C
ANISOU 726 C ASN A1099 9833 6127 7883 -911 -724 250 C
ATOM 727 O ASN A1099 30.032 187.757 138.010 1.00 63.99 O
ANISOU 727 O ASN A1099 10048 6277 7988 -846 -683 208 O
ATOM 728 CB ASN A1099 32.974 186.759 137.056 1.00 61.54 C
ANISOU 728 CB ASN A1099 9385 6078 7921 -1003 -828 335 C
ATOM 729 CG ASN A1099 33.634 185.660 136.267 1.00 75.55 C
ANISOU 729 CG ASN A1099 10949 7925 9833 -983 -781 369 C
ATOM 730 OD1 ASN A1099 34.850 185.488 136.315 1.00 75.54 O
ANISOU 730 OD1 ASN A1099 10818 7910 9976 -1060 -836 427 O
ATOM 731 ND2 ASN A1099 32.862 184.883 135.537 1.00 64.31 N
ANISOU 731 ND2 ASN A1099 9485 6565 8387 -884 -672 338 N
ATOM 732 N ALA A1100 31.356 189.512 137.489 1.00 56.70 N
ANISOU 732 N ALA A1100 9178 5275 7089 -985 -752 257 N
ATOM 733 CA ALA A1100 30.683 190.433 138.378 1.00 56.34 C
ANISOU 733 CA ALA A1100 9348 5110 6947 -993 -726 209 C
ATOM 734 C ALA A1100 29.305 190.830 137.868 1.00 59.59 C
ANISOU 734 C ALA A1100 9788 5485 7367 -863 -593 181 C
ATOM 735 O ALA A1100 28.370 190.920 138.657 1.00 59.46 O
ANISOU 735 O ALA A1100 9892 5390 7313 -814 -513 131 O
ATOM 736 CB ALA A1100 31.531 191.675 138.543 1.00 58.51 C
ANISOU 736 CB ALA A1100 9734 5298 7200 -1116 -796 230 C
ATOM 737 N TYR A1101 29.177 191.065 136.550 1.00 55.64 N
ANISOU 737 N TYR A1101 9184 5025 6930 -816 -569 221 N
ATOM 738 CA TYR A1101 27.972 191.609 135.943 1.00 54.96 C
ANISOU 738 CA TYR A1101 9114 4884 6886 -713 -492 228 C
ATOM 739 C TYR A1101 27.094 190.619 135.166 1.00 57.56 C
ANISOU 739 C TYR A1101 9309 5293 7270 -613 -466 252 C
ATOM 740 O TYR A1101 25.935 190.941 134.892 1.00 57.25 O
ANISOU 740 O TYR A1101 9269 5190 7295 -524 -423 269 O
ATOM 741 CB TYR A1101 28.349 192.817 135.049 1.00 55.69 C
ANISOU 741 CB TYR A1101 9243 4924 6993 -759 -515 272 C
ATOM 742 CG TYR A1101 29.172 193.855 135.787 1.00 58.92 C
ANISOU 742 CG TYR A1101 9793 5243 7351 -867 -548 253 C
ATOM 743 CD1 TYR A1101 28.731 194.396 136.996 1.00 61.69 C
ANISOU 743 CD1 TYR A1101 10314 5469 7655 -870 -500 197 C
ATOM 744 CD2 TYR A1101 30.376 194.318 135.267 1.00 59.62 C
ANISOU 744 CD2 TYR A1101 9861 5352 7438 -977 -614 292 C
ATOM 745 CE1 TYR A1101 29.472 195.361 137.668 1.00 61.54 C
ANISOU 745 CE1 TYR A1101 10462 5353 7568 -989 -541 180 C
ATOM 746 CE2 TYR A1101 31.143 195.258 135.948 1.00 60.71 C
ANISOU 746 CE2 TYR A1101 10129 5404 7536 -1091 -666 285 C
ATOM 747 CZ TYR A1101 30.687 195.775 137.150 1.00 67.57 C
ANISOU 747 CZ TYR A1101 11186 6151 8335 -1101 -642 229 C
ATOM 748 OH TYR A1101 31.421 196.718 137.822 1.00 66.43 O
ANISOU 748 OH TYR A1101 11206 5907 8128 -1233 -703 222 O
ATOM 749 N ILE A1102 27.614 189.467 134.762 1.00 53.24 N
ANISOU 749 N ILE A1102 8648 4866 6715 -629 -496 262 N
ATOM 750 CA ILE A1102 26.761 188.549 133.998 1.00 52.17 C
ANISOU 750 CA ILE A1102 8416 4794 6611 -552 -479 285 C
ATOM 751 C ILE A1102 26.565 187.257 134.704 1.00 56.60 C
ANISOU 751 C ILE A1102 8916 5424 7167 -516 -464 249 C
ATOM 752 O ILE A1102 25.411 186.876 134.931 1.00 56.54 O
ANISOU 752 O ILE A1102 8889 5402 7194 -430 -427 243 O
ATOM 753 CB ILE A1102 27.212 188.333 132.540 1.00 54.73 C
ANISOU 753 CB ILE A1102 8692 5178 6926 -597 -499 333 C
ATOM 754 CG1 ILE A1102 27.521 189.667 131.862 1.00 55.84 C
ANISOU 754 CG1 ILE A1102 8915 5244 7058 -653 -519 372 C
ATOM 755 CG2 ILE A1102 26.165 187.529 131.752 1.00 54.45 C
ANISOU 755 CG2 ILE A1102 8607 5178 6903 -537 -506 365 C
ATOM 756 CD1 ILE A1102 28.617 189.566 130.917 1.00 68.40 C
ANISOU 756 CD1 ILE A1102 10493 6878 8617 -749 -506 392 C
ATOM 757 N GLN A1103 27.684 186.588 135.066 1.00 54.39 N
ANISOU 757 N GLN A1103 8594 5205 6865 -581 -496 236 N
ATOM 758 CA GLN A1103 27.709 185.263 135.689 1.00 54.05 C
ANISOU 758 CA GLN A1103 8486 5228 6821 -562 -502 214 C
ATOM 759 C GLN A1103 26.659 185.092 136.795 1.00 59.91 C
ANISOU 759 C GLN A1103 9301 5923 7537 -502 -463 172 C
ATOM 760 O GLN A1103 25.858 184.163 136.698 1.00 61.28 O
ANISOU 760 O GLN A1103 9411 6142 7730 -432 -429 166 O
ATOM 761 CB GLN A1103 29.134 184.898 136.160 1.00 55.45 C
ANISOU 761 CB GLN A1103 8618 5432 7017 -654 -569 225 C
ATOM 762 CG GLN A1103 29.248 183.926 137.363 1.00 63.41 C
ANISOU 762 CG GLN A1103 9626 6455 8010 -664 -619 207 C
ATOM 763 CD GLN A1103 29.241 182.474 136.970 1.00 77.66 C
ANISOU 763 CD GLN A1103 11293 8348 9865 -618 -599 214 C
ATOM 764 OE1 GLN A1103 29.077 182.109 135.807 1.00 74.05 O
ANISOU 764 OE1 GLN A1103 10758 7941 9438 -578 -535 223 O
ATOM 765 NE2 GLN A1103 29.453 181.608 137.937 1.00 74.08 N
ANISOU 765 NE2 GLN A1103 10830 7906 9413 -636 -659 213 N
ATOM 766 N LYS A1104 26.614 185.984 137.795 1.00 56.64 N
ANISOU 766 N LYS A1104 9035 5408 7080 -536 -449 141 N
ATOM 767 CA LYS A1104 25.682 185.824 138.926 1.00 56.41 C
ANISOU 767 CA LYS A1104 9110 5306 7016 -498 -369 89 C
ATOM 768 C LYS A1104 24.213 185.911 138.561 1.00 59.89 C
ANISOU 768 C LYS A1104 9506 5704 7546 -377 -257 89 C
ATOM 769 O LYS A1104 23.387 185.560 139.386 1.00 60.27 O
ANISOU 769 O LYS A1104 9604 5699 7597 -334 -161 49 O
ATOM 770 CB LYS A1104 25.985 186.794 140.083 1.00 59.45 C
ANISOU 770 CB LYS A1104 9713 5563 7312 -585 -356 48 C
ATOM 771 CG LYS A1104 26.399 188.199 139.682 1.00 70.38 C
ANISOU 771 CG LYS A1104 11167 6871 8704 -626 -368 63 C
ATOM 772 CD LYS A1104 26.602 189.100 140.904 1.00 81.56 C
ANISOU 772 CD LYS A1104 12838 8140 10011 -723 -343 13 C
ATOM 773 CE LYS A1104 25.335 189.827 141.304 1.00 97.10 C
ANISOU 773 CE LYS A1104 14929 9957 12008 -642 -149 -40 C
ATOM 774 NZ LYS A1104 25.557 190.781 142.426 1.00110.63 N
ANISOU 774 NZ LYS A1104 16935 11503 13598 -751 -96 -99 N
ATOM 775 N TYR A1105 23.887 186.377 137.359 1.00 56.52 N
ANISOU 775 N TYR A1105 8991 5284 7201 -332 -275 142 N
ATOM 776 CA TYR A1105 22.502 186.566 136.907 1.00 56.72 C
ANISOU 776 CA TYR A1105 8948 5249 7355 -227 -212 175 C
ATOM 777 C TYR A1105 22.009 185.453 136.008 1.00 61.23 C
ANISOU 777 C TYR A1105 9370 5921 7971 -185 -267 223 C
ATOM 778 O TYR A1105 20.859 185.490 135.547 1.00 62.02 O
ANISOU 778 O TYR A1105 9391 5976 8200 -111 -256 274 O
ATOM 779 CB TYR A1105 22.354 187.924 136.205 1.00 57.59 C
ANISOU 779 CB TYR A1105 9083 5264 7534 -220 -225 222 C
ATOM 780 CG TYR A1105 22.647 189.102 137.098 1.00 58.32 C
ANISOU 780 CG TYR A1105 9340 5226 7593 -256 -152 173 C
ATOM 781 CD1 TYR A1105 21.749 189.492 138.090 1.00 61.48 C
ANISOU 781 CD1 TYR A1105 9822 5480 8056 -200 7 125 C
ATOM 782 CD2 TYR A1105 23.806 189.850 136.936 1.00 58.47 C
ANISOU 782 CD2 TYR A1105 9443 5251 7523 -355 -224 173 C
ATOM 783 CE1 TYR A1105 21.994 190.609 138.888 1.00 63.47 C
ANISOU 783 CE1 TYR A1105 10265 5589 8260 -246 93 72 C
ATOM 784 CE2 TYR A1105 24.075 190.954 137.744 1.00 60.17 C
ANISOU 784 CE2 TYR A1105 9832 5336 7694 -404 -168 129 C
ATOM 785 CZ TYR A1105 23.163 191.335 138.716 1.00 70.98 C
ANISOU 785 CZ TYR A1105 11310 6555 9103 -352 -9 76 C
ATOM 786 OH TYR A1105 23.407 192.449 139.494 1.00 77.26 O
ANISOU 786 OH TYR A1105 12316 7200 9840 -413 65 25 O
ATOM 787 N LEU A1106 22.871 184.451 135.784 1.00 56.89 N
ANISOU 787 N LEU A1106 8784 5496 7336 -237 -326 214 N
ATOM 788 CA LEU A1106 22.579 183.307 134.947 1.00 56.26 C
ANISOU 788 CA LEU A1106 8599 5510 7267 -219 -369 247 C
ATOM 789 C LEU A1106 21.497 182.406 135.574 1.00 60.59 C
ANISOU 789 C LEU A1106 9092 6058 7870 -145 -315 231 C
ATOM 790 O LEU A1106 21.399 182.363 136.800 1.00 60.08 O
ANISOU 790 O LEU A1106 9088 5951 7789 -134 -237 175 O
ATOM 791 CB LEU A1106 23.866 182.543 134.598 1.00 55.70 C
ANISOU 791 CB LEU A1106 8507 5542 7114 -291 -408 234 C
ATOM 792 CG LEU A1106 24.809 183.199 133.562 1.00 59.34 C
ANISOU 792 CG LEU A1106 8992 6008 7547 -365 -442 265 C
ATOM 793 CD1 LEU A1106 26.042 182.358 133.365 1.00 58.31 C
ANISOU 793 CD1 LEU A1106 8813 5952 7390 -425 -435 250 C
ATOM 794 CD2 LEU A1106 24.133 183.376 132.215 1.00 60.45 C
ANISOU 794 CD2 LEU A1106 9136 6136 7696 -366 -478 327 C
ATOM 795 N PRO A 10 20.648 181.728 134.751 1.00 57.71 N
ANISOU 795 N PRO A 10 8634 5724 7568 -109 -357 285 N
ATOM 796 CA PRO A 10 19.521 180.947 135.316 1.00 58.39 C
ANISOU 796 CA PRO A 10 8650 5796 7739 -40 -302 282 C
ATOM 797 C PRO A 10 19.822 179.953 136.481 1.00 64.79 C
ANISOU 797 C PRO A 10 9488 6655 8474 -43 -236 207 C
ATOM 798 O PRO A 10 18.901 179.702 137.250 1.00 65.24 O
ANISOU 798 O PRO A 10 9527 6660 8601 11 -145 190 O
ATOM 799 CB PRO A 10 18.924 180.243 134.098 1.00 59.40 C
ANISOU 799 CB PRO A 10 8692 5970 7908 -42 -405 360 C
ATOM 800 CG PRO A 10 19.795 180.589 132.926 1.00 61.84 C
ANISOU 800 CG PRO A 10 9058 6315 8124 -123 -494 391 C
ATOM 801 CD PRO A 10 20.599 181.752 133.273 1.00 57.59 C
ANISOU 801 CD PRO A 10 8596 5735 7550 -147 -459 359 C
ATOM 802 N CYS A 11 21.071 179.447 136.657 1.00 63.17 N
ANISOU 802 N CYS A 11 9324 6529 8148 -108 -275 171 N
ATOM 803 CA CYS A 11 21.555 178.594 137.784 1.00 63.86 C
ANISOU 803 CA CYS A 11 9454 6648 8160 -133 -253 118 C
ATOM 804 C CYS A 11 21.258 179.162 139.125 1.00 60.86 C
ANISOU 804 C CYS A 11 9200 6168 7755 -137 -165 68 C
ATOM 805 O CYS A 11 21.186 178.409 140.100 1.00 57.77 O
ANISOU 805 O CYS A 11 8864 5776 7309 -153 -131 31 O
ATOM 806 CB CYS A 11 23.071 178.482 137.724 1.00 67.05 C
ANISOU 806 CB CYS A 11 9873 7108 8496 -211 -330 114 C
ATOM 807 SG CYS A 11 23.696 177.537 136.362 1.00 72.89 S
ANISOU 807 SG CYS A 11 10500 7947 9247 -226 -377 148 S
ATOM 808 N PHE A 12 21.519 180.482 139.218 1.00 54.25 N
ANISOU 808 N PHE A 12 8450 5248 6915 -160 -147 63 N
ATOM 809 CA PHE A 12 21.636 181.184 140.468 1.00 53.97 C
ANISOU 809 CA PHE A 12 8595 5101 6809 -207 -72 8 C
ATOM 810 C PHE A 12 20.391 181.879 140.884 1.00 59.55 C
ANISOU 810 C PHE A 12 9349 5670 7607 -139 98 -15 C
ATOM 811 O PHE A 12 19.917 182.815 140.221 1.00 61.00 O
ANISOU 811 O PHE A 12 9477 5791 7908 -85 127 20 O
ATOM 812 CB PHE A 12 22.846 182.153 140.440 1.00 55.17 C
ANISOU 812 CB PHE A 12 8838 5234 6891 -296 -158 12 C
ATOM 813 CG PHE A 12 24.131 181.541 139.936 1.00 55.04 C
ANISOU 813 CG PHE A 12 8735 5333 6844 -358 -306 48 C
ATOM 814 CD1 PHE A 12 24.886 180.704 140.747 1.00 58.45 C
ANISOU 814 CD1 PHE A 12 9204 5797 7208 -429 -384 42 C
ATOM 815 CD2 PHE A 12 24.561 181.764 138.639 1.00 56.79 C
ANISOU 815 CD2 PHE A 12 8841 5614 7121 -350 -357 94 C
ATOM 816 CE1 PHE A 12 26.055 180.102 140.268 1.00 58.88 C
ANISOU 816 CE1 PHE A 12 9141 5935 7294 -474 -500 85 C
ATOM 817 CE2 PHE A 12 25.735 181.168 138.161 1.00 59.61 C
ANISOU 817 CE2 PHE A 12 9111 6055 7484 -402 -443 122 C
ATOM 818 CZ PHE A 12 26.474 180.342 138.981 1.00 57.61 C
ANISOU 818 CZ PHE A 12 8858 5827 7206 -456 -508 120 C
ATOM 819 N ARG A 13 19.867 181.414 142.013 1.00 55.52 N
ANISOU 819 N ARG A 13 8946 5096 7054 -146 221 -70 N
ATOM 820 CA ARG A 13 18.703 182.007 142.638 1.00 56.55 C
ANISOU 820 CA ARG A 13 9143 5062 7282 -89 443 -107 C
ATOM 821 C ARG A 13 19.226 182.986 143.710 1.00 63.50 C
ANISOU 821 C ARG A 13 10305 5803 8018 -186 526 -178 C
ATOM 822 O ARG A 13 20.414 182.902 144.053 1.00 61.47 O
ANISOU 822 O ARG A 13 10172 5599 7585 -303 378 -187 O
ATOM 823 CB ARG A 13 17.820 180.924 143.260 1.00 52.12 C
ANISOU 823 CB ARG A 13 8560 4492 6749 -55 563 -133 C
ATOM 824 CG ARG A 13 17.114 180.008 142.266 1.00 49.32 C
ANISOU 824 CG ARG A 13 7943 4242 6554 37 500 -61 C
ATOM 825 CD ARG A 13 16.318 178.939 142.989 1.00 58.96 C
ANISOU 825 CD ARG A 13 9158 5451 7795 57 622 -89 C
ATOM 826 NE ARG A 13 17.184 177.996 143.710 1.00 55.96 N
ANISOU 826 NE ARG A 13 8914 5152 7197 -39 542 -131 N
ATOM 827 CZ ARG A 13 17.418 178.022 145.016 1.00 67.28 C
ANISOU 827 CZ ARG A 13 10599 6494 8470 -128 640 -203 C
ATOM 828 NH1 ARG A 13 16.817 178.916 145.789 1.00 56.70 N
ANISOU 828 NH1 ARG A 13 9421 4971 7150 -131 868 -260 N
ATOM 829 NH2 ARG A 13 18.248 177.150 145.561 1.00 61.70 N
ANISOU 829 NH2 ARG A 13 9997 5860 7586 -222 515 -214 N
ATOM 830 N PRO A 14 18.424 183.957 144.211 1.00 64.32 N
ANISOU 830 N PRO A 14 10517 5716 8205 -150 750 -220 N
ATOM 831 CA PRO A 14 18.962 184.841 145.252 1.00 67.04 C
ANISOU 831 CA PRO A 14 11180 5916 8376 -267 832 -296 C
ATOM 832 C PRO A 14 19.106 184.097 146.594 1.00 77.59 C
ANISOU 832 C PRO A 14 12771 7207 9503 -382 897 -367 C
ATOM 833 O PRO A 14 18.283 183.240 146.917 1.00 76.43 O
ANISOU 833 O PRO A 14 12577 7056 9409 -333 1024 -384 O
ATOM 834 CB PRO A 14 17.953 185.986 145.312 1.00 69.84 C
ANISOU 834 CB PRO A 14 11557 6063 8914 -179 1088 -320 C
ATOM 835 CG PRO A 14 16.684 185.415 144.809 1.00 73.69 C
ANISOU 835 CG PRO A 14 11778 6556 9666 -29 1195 -273 C
ATOM 836 CD PRO A 14 17.006 184.256 143.918 1.00 66.89 C
ANISOU 836 CD PRO A 14 10689 5928 8798 -11 947 -198 C
ATOM 837 N THR A 15 20.190 184.399 147.338 1.00 79.59 N
ANISOU 837 N THR A 15 13296 7426 9517 -551 782 -396 N
ATOM 838 CA THR A 15 20.517 183.854 148.660 1.00 82.42 C
ANISOU 838 CA THR A 15 13966 7718 9631 -710 787 -449 C
ATOM 839 C THR A 15 20.952 184.981 149.605 1.00 92.42 C
ANISOU 839 C THR A 15 15625 8788 10700 -870 852 -513 C
ATOM 840 O THR A 15 21.402 186.051 149.154 1.00 91.66 O
ANISOU 840 O THR A 15 15527 8663 10636 -876 796 -498 O
ATOM 841 CB THR A 15 21.630 182.797 148.582 1.00 93.94 C
ANISOU 841 CB THR A 15 15350 9357 10987 -795 470 -381 C
ATOM 842 OG1 THR A 15 22.615 183.187 147.617 1.00 89.25 O
ANISOU 842 OG1 THR A 15 14572 8881 10457 -791 241 -308 O
ATOM 843 CG2 THR A 15 21.097 181.387 148.302 1.00 95.94 C
ANISOU 843 CG2 THR A 15 15383 9740 11331 -699 468 -354 C
ATOM 844 N ASN A 16 20.817 184.725 150.923 1.00 93.07 N
ANISOU 844 N ASN A 16 16072 8727 10564 -1014 969 -585 N
ATOM 845 CA ASN A 16 21.227 185.643 151.983 1.00 95.91 C
ANISOU 845 CA ASN A 16 16888 8876 10676 -1211 1029 -653 C
ATOM 846 C ASN A 16 22.397 185.003 152.767 1.00 99.09 C
ANISOU 846 C ASN A 16 17527 9318 10802 -1444 709 -609 C
ATOM 847 O ASN A 16 22.468 185.089 154.005 1.00103.03 O
ANISOU 847 O ASN A 16 18478 9638 11031 -1645 771 -668 O
ATOM 848 CB ASN A 16 20.031 186.052 152.882 1.00103.47 C
ANISOU 848 CB ASN A 16 18138 9574 11602 -1210 1472 -777 C
ATOM 849 CG ASN A 16 20.202 187.376 153.601 1.00140.80 C
ANISOU 849 CG ASN A 16 23281 14053 16163 -1350 1627 -859 C
ATOM 850 OD1 ASN A 16 20.549 188.404 153.001 1.00140.54 O
ANISOU 850 OD1 ASN A 16 23168 14011 16218 -1313 1568 -838 O
ATOM 851 ND2 ASN A 16 19.908 187.392 154.901 1.00135.38 N
ANISOU 851 ND2 ASN A 16 23071 13142 15227 -1520 1852 -961 N
ATOM 852 N ILE A 17 23.311 184.343 152.019 1.00 89.13 N
ANISOU 852 N ILE A 17 15962 8279 9625 -1422 367 -496 N
ATOM 853 CA ILE A 17 24.541 183.762 152.554 1.00 87.06 C
ANISOU 853 CA ILE A 17 15823 8064 9192 -1621 12 -416 C
ATOM 854 C ILE A 17 25.640 184.832 152.469 1.00 88.35 C
ANISOU 854 C ILE A 17 16082 8187 9301 -1753 -202 -370 C
ATOM 855 O ILE A 17 25.730 185.566 151.475 1.00 86.91 O
ANISOU 855 O ILE A 17 15660 8067 9294 -1631 -185 -354 O
ATOM 856 CB ILE A 17 24.948 182.414 151.893 1.00 87.61 C
ANISOU 856 CB ILE A 17 15522 8359 9408 -1534 -213 -318 C
ATOM 857 CG1 ILE A 17 26.166 181.781 152.605 1.00 88.21 C
ANISOU 857 CG1 ILE A 17 15738 8442 9337 -1750 -575 -222 C
ATOM 858 CG2 ILE A 17 25.192 182.557 150.380 1.00 87.06 C
ANISOU 858 CG2 ILE A 17 15004 8469 9608 -1351 -280 -259 C
ATOM 859 CD1 ILE A 17 26.018 180.339 152.982 1.00 92.96 C
ANISOU 859 CD1 ILE A 17 16304 9104 9910 -1757 -644 -191 C
ATOM 860 N THR A 18 26.441 184.934 153.527 1.00 84.12 N
ANISOU 860 N THR A 18 15913 7532 8516 -2015 -409 -343 N
ATOM 861 CA THR A 18 27.538 185.886 153.612 1.00 84.26 C
ANISOU 861 CA THR A 18 16063 7489 8461 -2184 -649 -287 C
ATOM 862 C THR A 18 28.845 185.171 153.311 1.00 86.43 C
ANISOU 862 C THR A 18 16087 7914 8838 -2257 -1074 -129 C
ATOM 863 O THR A 18 28.880 183.942 153.325 1.00 85.08 O
ANISOU 863 O THR A 18 15757 7847 8723 -2221 -1176 -76 O
ATOM 864 CB THR A 18 27.544 186.570 154.992 1.00 96.13 C
ANISOU 864 CB THR A 18 18174 8727 9623 -2451 -600 -356 C
ATOM 865 OG1 THR A 18 27.471 185.576 156.025 1.00 98.26 O
ANISOU 865 OG1 THR A 18 18712 8935 9686 -2603 -667 -350 O
ATOM 866 CG2 THR A 18 26.416 187.584 155.146 1.00 93.78 C
ANISOU 866 CG2 THR A 18 18095 8251 9284 -2372 -155 -510 C
ATOM 867 N LEU A 19 29.921 185.936 153.039 1.00 83.61 N
ANISOU 867 N LEU A 19 15684 7556 8530 -2357 -1311 -49 N
ATOM 868 CA LEU A 19 31.250 185.386 152.783 1.00 83.03 C
ANISOU 868 CA LEU A 19 15362 7587 8599 -2440 -1706 115 C
ATOM 869 C LEU A 19 31.751 184.622 154.031 1.00 87.66 C
ANISOU 869 C LEU A 19 16237 8075 8994 -2687 -1984 193 C
ATOM 870 O LEU A 19 32.318 183.532 153.888 1.00 87.01 O
ANISOU 870 O LEU A 19 15899 8099 9062 -2674 -2211 308 O
ATOM 871 CB LEU A 19 32.225 186.503 152.384 1.00 83.74 C
ANISOU 871 CB LEU A 19 15410 7648 8759 -2532 -1876 178 C
ATOM 872 N GLU A 20 31.465 185.155 155.244 1.00 85.04 N
ANISOU 872 N GLU A 20 16456 7527 8328 -2909 -1945 127 N
ATOM 873 CA GLU A 20 31.838 184.540 156.527 1.00 86.68 C
ANISOU 873 CA GLU A 20 17045 7602 8288 -3184 -2201 193 C
ATOM 874 C GLU A 20 31.156 183.198 156.746 1.00 88.39 C
ANISOU 874 C GLU A 20 17198 7888 8500 -3088 -2101 172 C
ATOM 875 O GLU A 20 31.848 182.251 157.113 1.00 89.33 O
ANISOU 875 O GLU A 20 17260 8033 8649 -3199 -2431 308 O
ATOM 876 CB GLU A 20 31.598 185.490 157.719 1.00 90.87 C
ANISOU 876 CB GLU A 20 18237 7863 8427 -3450 -2120 103 C
ATOM 877 N GLU A 21 29.816 183.098 156.500 1.00 82.28 N
ANISOU 877 N GLU A 21 16407 7137 7719 -2880 -1660 17 N
ATOM 878 CA GLU A 21 29.033 181.847 156.637 1.00 80.48 C
ANISOU 878 CA GLU A 21 16099 6978 7503 -2768 -1520 -15 C
ATOM 879 C GLU A 21 29.610 180.755 155.729 1.00 81.37 C
ANISOU 879 C GLU A 21 15673 7316 7926 -2612 -1741 111 C
ATOM 880 O GLU A 21 29.641 179.591 156.117 1.00 80.72 O
ANISOU 880 O GLU A 21 15577 7264 7828 -2646 -1869 169 O
ATOM 881 CB GLU A 21 27.551 182.066 156.272 1.00 80.69 C
ANISOU 881 CB GLU A 21 16084 7005 7570 -2539 -1016 -183 C
ATOM 882 CG GLU A 21 26.683 182.582 157.405 1.00 94.67 C
ANISOU 882 CG GLU A 21 18410 8528 9032 -2681 -708 -322 C
ATOM 883 CD GLU A 21 25.445 183.385 157.029 1.00122.25 C
ANISOU 883 CD GLU A 21 21882 11955 12612 -2485 -218 -475 C
ATOM 884 OE1 GLU A 21 25.319 183.814 155.858 1.00103.45 O
ANISOU 884 OE1 GLU A 21 19090 9708 10509 -2259 -149 -469 O
ATOM 885 OE2 GLU A 21 24.620 183.635 157.938 1.00128.22 O
ANISOU 885 OE2 GLU A 21 23058 12502 13159 -2574 99 -597 O
ATOM 886 N ARG A 22 30.078 181.156 154.525 1.00 75.66 N
ANISOU 886 N ARG A 22 14532 6734 7480 -2451 -1775 153 N
ATOM 887 CA ARG A 22 30.685 180.292 153.519 1.00 73.15 C
ANISOU 887 CA ARG A 22 13707 6610 7477 -2299 -1934 260 C
ATOM 888 C ARG A 22 32.006 179.716 153.996 1.00 78.85 C
ANISOU 888 C ARG A 22 14396 7307 8256 -2490 -2376 439 C
ATOM 889 O ARG A 22 32.236 178.529 153.802 1.00 78.66 O
ANISOU 889 O ARG A 22 14119 7375 8392 -2422 -2491 517 O
ATOM 890 CB ARG A 22 30.881 181.044 152.197 1.00 68.36 C
ANISOU 890 CB ARG A 22 12750 6116 7106 -2125 -1838 252 C
ATOM 891 CG ARG A 22 29.631 181.116 151.365 1.00 70.30 C
ANISOU 891 CG ARG A 22 12839 6447 7426 -1876 -1463 128 C
ATOM 892 CD ARG A 22 29.845 181.946 150.125 1.00 76.37 C
ANISOU 892 CD ARG A 22 13330 7300 8388 -1742 -1396 128 C
ATOM 893 NE ARG A 22 28.661 181.891 149.274 1.00 82.96 N
ANISOU 893 NE ARG A 22 13987 8216 9318 -1512 -1091 39 N
ATOM 894 CZ ARG A 22 28.684 181.924 147.950 1.00 96.54 C
ANISOU 894 CZ ARG A 22 15365 10068 11247 -1348 -1039 58 C
ATOM 895 NH1 ARG A 22 29.836 182.035 147.300 1.00 78.59 N
ANISOU 895 NH1 ARG A 22 12883 7860 9117 -1376 -1226 148 N
ATOM 896 NH2 ARG A 22 27.554 181.839 147.261 1.00 91.90 N
ANISOU 896 NH2 ARG A 22 14650 9535 10735 -1166 -799 -7 N
ATOM 897 N ARG A 23 32.871 180.546 154.607 1.00 77.33 N
ANISOU 897 N ARG A 23 14449 6977 7955 -2730 -2632 513 N
ATOM 898 CA ARG A 23 34.179 180.132 155.113 1.00 79.43 C
ANISOU 898 CA ARG A 23 14692 7186 8302 -2943 -3099 710 C
ATOM 899 C ARG A 23 34.011 179.109 156.236 1.00 86.12 C
ANISOU 899 C ARG A 23 15824 7943 8956 -3102 -3259 757 C
ATOM 900 O ARG A 23 34.822 178.186 156.346 1.00 86.68 O
ANISOU 900 O ARG A 23 15698 8032 9207 -3160 -3584 924 O
ATOM 901 CB ARG A 23 34.990 181.354 155.586 1.00 82.01 C
ANISOU 901 CB ARG A 23 15279 7364 8517 -3188 -3324 769 C
ATOM 902 N LEU A 24 32.925 179.247 157.029 1.00 83.97 N
ANISOU 902 N LEU A 24 16000 7566 8338 -3161 -3003 610 N
ATOM 903 CA LEU A 24 32.586 178.350 158.133 1.00 85.98 C
ANISOU 903 CA LEU A 24 16599 7718 8351 -3320 -3085 624 C
ATOM 904 C LEU A 24 32.098 176.984 157.657 1.00 87.71 C
ANISOU 904 C LEU A 24 16481 8094 8752 -3101 -2976 623 C
ATOM 905 O LEU A 24 32.548 175.976 158.213 1.00 89.25 O
ANISOU 905 O LEU A 24 16705 8257 8949 -3218 -3261 749 O
ATOM 906 CB LEU A 24 31.559 178.989 159.083 1.00 87.84 C
ANISOU 906 CB LEU A 24 17429 7773 8172 -3451 -2782 452 C
ATOM 907 N ILE A 25 31.179 176.944 156.648 1.00 80.01 N
ANISOU 907 N ILE A 25 15200 7272 7928 -2797 -2584 490 N
ATOM 908 CA ILE A 25 30.608 175.704 156.094 1.00 76.94 C
ANISOU 908 CA ILE A 25 14492 7034 7708 -2579 -2446 473 C
ATOM 909 C ILE A 25 31.640 174.950 155.253 1.00 78.69 C
ANISOU 909 C ILE A 25 14213 7391 8296 -2478 -2705 627 C
ATOM 910 O ILE A 25 31.634 173.709 155.266 1.00 77.86 O
ANISOU 910 O ILE A 25 13955 7339 8289 -2426 -2783 686 O
ATOM 911 CB ILE A 25 29.289 175.934 155.276 1.00 77.99 C
ANISOU 911 CB ILE A 25 14476 7267 7889 -2312 -1973 299 C
ATOM 912 CG1 ILE A 25 28.217 176.689 156.076 1.00 79.08 C
ANISOU 912 CG1 ILE A 25 15074 7247 7725 -2389 -1659 144 C
ATOM 913 CG2 ILE A 25 28.705 174.593 154.733 1.00 77.31 C
ANISOU 913 CG2 ILE A 25 14078 7329 7968 -2110 -1860 291 C
ATOM 914 CD1 ILE A 25 27.159 177.383 155.178 1.00 78.03 C
ANISOU 914 CD1 ILE A 25 14769 7174 7706 -2151 -1253 5 C
ATOM 915 N ALA A 26 32.463 175.685 154.462 1.00 73.87 N
ANISOU 915 N ALA A 26 13336 6829 7903 -2434 -2793 682 N
ATOM 916 CA ALA A 26 33.466 175.091 153.563 1.00 72.93 C
ANISOU 916 CA ALA A 26 12727 6817 8167 -2329 -2974 817 C
ATOM 917 C ALA A 26 34.427 174.146 154.284 1.00 80.31 C
ANISOU 917 C ALA A 26 13639 7674 9202 -2493 -3380 1009 C
ATOM 918 O ALA A 26 35.238 174.589 155.109 1.00 83.76 O
ANISOU 918 O ALA A 26 14294 7967 9563 -2744 -3714 1130 O
ATOM 919 CB ALA A 26 34.238 176.166 152.818 1.00 73.30 C
ANISOU 919 CB ALA A 26 12583 6882 8386 -2317 -3015 851 C
ATOM 920 N SER A 27 34.281 172.836 154.008 1.00 75.14 N
ANISOU 920 N SER A 27 12745 7099 8707 -2363 -3360 1040 N
ATOM 921 CA SER A 27 35.096 171.767 154.588 1.00 76.85 C
ANISOU 921 CA SER A 27 12888 7244 9068 -2480 -3723 1226 C
ATOM 922 C SER A 27 35.403 170.688 153.518 1.00 76.35 C
ANISOU 922 C SER A 27 12308 7305 9399 -2248 -3652 1275 C
ATOM 923 O SER A 27 34.787 169.613 153.514 1.00 71.99 O
ANISOU 923 O SER A 27 11718 6804 8831 -2146 -3540 1236 O
ATOM 924 CB SER A 27 34.435 171.181 155.842 1.00 83.06 C
ANISOU 924 CB SER A 27 14115 7928 9516 -2642 -3791 1210 C
ATOM 925 OG SER A 27 33.068 170.864 155.624 1.00 91.46 O
ANISOU 925 OG SER A 27 15256 9082 10412 -2475 -3392 1023 O
ATOM 926 N PRO A 28 36.344 170.989 152.580 1.00 72.35 N
ANISOU 926 N PRO A 28 11410 6835 9244 -2166 -3688 1352 N
ATOM 927 CA PRO A 28 36.653 170.021 151.507 1.00 71.38 C
ANISOU 927 CA PRO A 28 10820 6807 9495 -1950 -3569 1383 C
ATOM 928 C PRO A 28 37.247 168.690 151.975 1.00 78.69 C
ANISOU 928 C PRO A 28 11602 7659 10639 -1990 -3831 1549 C
ATOM 929 O PRO A 28 36.987 167.658 151.358 1.00 76.96 O
ANISOU 929 O PRO A 28 11155 7513 10572 -1814 -3659 1516 O
ATOM 930 CB PRO A 28 37.609 170.803 150.598 1.00 72.68 C
ANISOU 930 CB PRO A 28 10676 6981 9958 -1910 -3563 1437 C
ATOM 931 CG PRO A 28 38.232 171.806 151.494 1.00 77.76 C
ANISOU 931 CG PRO A 28 11564 7495 10486 -2159 -3870 1533 C
ATOM 932 CD PRO A 28 37.145 172.218 152.427 1.00 72.92 C
ANISOU 932 CD PRO A 28 11460 6856 9390 -2267 -3808 1405 C
ATOM 933 N TRP A 29 38.029 168.710 153.062 1.00 80.34 N
ANISOU 933 N TRP A 29 11956 7710 10859 -2232 -4257 1732 N
ATOM 934 CA TRP A 29 38.661 167.511 153.604 1.00 83.20 C
ANISOU 934 CA TRP A 29 12194 7972 11447 -2299 -4569 1924 C
ATOM 935 C TRP A 29 37.683 166.572 154.265 1.00 88.36 C
ANISOU 935 C TRP A 29 13121 8636 11818 -2305 -4517 1856 C
ATOM 936 O TRP A 29 37.856 165.370 154.130 1.00 88.58 O
ANISOU 936 O TRP A 29 12925 8658 12075 -2218 -4562 1933 O
ATOM 937 CB TRP A 29 39.827 167.860 154.527 1.00 85.54 C
ANISOU 937 CB TRP A 29 12562 8081 11858 -2577 -5083 2165 C
ATOM 938 CG TRP A 29 41.010 168.330 153.741 1.00 87.80 C
ANISOU 938 CG TRP A 29 12413 8342 12603 -2534 -5157 2289 C
ATOM 939 CD1 TRP A 29 41.397 169.620 153.538 1.00 90.99 C
ANISOU 939 CD1 TRP A 29 12852 8738 12983 -2612 -5170 2277 C
ATOM 940 CD2 TRP A 29 41.852 167.521 152.905 1.00 88.46 C
ANISOU 940 CD2 TRP A 29 11950 8417 13246 -2370 -5135 2410 C
ATOM 941 NE1 TRP A 29 42.477 169.662 152.686 1.00 91.25 N
ANISOU 941 NE1 TRP A 29 12392 8751 13528 -2524 -5186 2398 N
ATOM 942 CE2 TRP A 29 42.772 168.387 152.276 1.00 93.06 C
ANISOU 942 CE2 TRP A 29 12256 8973 14129 -2372 -5148 2478 C
ATOM 943 CE3 TRP A 29 41.943 166.135 152.657 1.00 90.13 C
ANISOU 943 CE3 TRP A 29 11883 8618 13745 -2229 -5099 2472 C
ATOM 944 CZ2 TRP A 29 43.774 167.917 151.417 1.00 93.52 C
ANISOU 944 CZ2 TRP A 29 11771 8988 14774 -2239 -5104 2604 C
ATOM 945 CZ3 TRP A 29 42.933 165.672 151.803 1.00 92.50 C
ANISOU 945 CZ3 TRP A 29 11651 8871 14624 -2093 -5055 2593 C
ATOM 946 CH2 TRP A 29 43.834 166.556 151.194 1.00 93.94 C
ANISOU 946 CH2 TRP A 29 11566 9021 15105 -2099 -5047 2657 C
ATOM 947 N PHE A 30 36.650 167.105 154.944 1.00 85.93 N
ANISOU 947 N PHE A 30 13286 8332 11031 -2401 -4394 1708 N
ATOM 948 CA PHE A 30 35.601 166.328 155.605 1.00 86.19 C
ANISOU 948 CA PHE A 30 13619 8368 10760 -2417 -4292 1621 C
ATOM 949 C PHE A 30 34.797 165.580 154.541 1.00 87.02 C
ANISOU 949 C PHE A 30 13443 8641 10978 -2123 -3896 1477 C
ATOM 950 O PHE A 30 34.560 164.372 154.675 1.00 87.36 O
ANISOU 950 O PHE A 30 13424 8689 11078 -2069 -3910 1508 O
ATOM 951 CB PHE A 30 34.678 167.248 156.440 1.00 89.34 C
ANISOU 951 CB PHE A 30 14568 8720 10658 -2573 -4168 1476 C
ATOM 952 CG PHE A 30 33.496 166.551 157.081 1.00 92.22 C
ANISOU 952 CG PHE A 30 15251 9083 10705 -2582 -3986 1362 C
ATOM 953 CD1 PHE A 30 33.609 165.969 158.342 1.00 98.89 C
ANISOU 953 CD1 PHE A 30 16457 9776 11343 -2825 -4278 1469 C
ATOM 954 CD2 PHE A 30 32.274 166.456 156.414 1.00 93.38 C
ANISOU 954 CD2 PHE A 30 15336 9370 10774 -2359 -3532 1159 C
ATOM 955 CE1 PHE A 30 32.525 165.300 158.923 1.00100.21 C
ANISOU 955 CE1 PHE A 30 16917 9934 11224 -2838 -4087 1364 C
ATOM 956 CE2 PHE A 30 31.193 165.774 156.988 1.00 96.41 C
ANISOU 956 CE2 PHE A 30 15980 9746 10906 -2366 -3355 1064 C
ATOM 957 CZ PHE A 30 31.325 165.205 158.240 1.00 97.20 C
ANISOU 957 CZ PHE A 30 16439 9697 10796 -2603 -3616 1160 C
ATOM 958 N ALA A 31 34.392 166.310 153.488 1.00 80.10 N
ANISOU 958 N ALA A 31 12413 7892 10130 -1948 -3564 1329 N
ATOM 959 CA ALA A 31 33.610 165.812 152.362 1.00 76.62 C
ANISOU 959 CA ALA A 31 11731 7606 9776 -1688 -3192 1189 C
ATOM 960 C ALA A 31 34.352 164.720 151.592 1.00 79.56 C
ANISOU 960 C ALA A 31 11674 8000 10557 -1553 -3234 1293 C
ATOM 961 O ALA A 31 33.776 163.647 151.381 1.00 78.74 O
ANISOU 961 O ALA A 31 11507 7946 10465 -1442 -3104 1249 O
ATOM 962 CB ALA A 31 33.220 166.962 151.440 1.00 75.45 C
ANISOU 962 CB ALA A 31 11523 7554 9590 -1575 -2909 1051 C
ATOM 963 N ALA A 32 35.642 164.964 151.236 1.00 75.27 N
ANISOU 963 N ALA A 32 10846 7397 10358 -1575 -3416 1435 N
ATOM 964 CA ALA A 32 36.492 164.010 150.516 1.00 74.37 C
ANISOU 964 CA ALA A 32 10305 7261 10689 -1453 -3436 1545 C
ATOM 965 C ALA A 32 36.644 162.699 151.279 1.00 77.48 C
ANISOU 965 C ALA A 32 10705 7566 11168 -1505 -3663 1672 C
ATOM 966 O ALA A 32 36.382 161.635 150.721 1.00 76.70 O
ANISOU 966 O ALA A 32 10420 7510 11214 -1349 -3492 1638 O
ATOM 967 CB ALA A 32 37.852 164.622 150.232 1.00 76.71 C
ANISOU 967 CB ALA A 32 10333 7474 11339 -1505 -3612 1693 C
ATOM 968 N SER A 33 36.988 162.782 152.569 1.00 74.80 N
ANISOU 968 N SER A 33 10621 7095 10703 -1737 -4044 1810 N
ATOM 969 CA SER A 33 37.153 161.640 153.469 1.00 75.61 C
ANISOU 969 CA SER A 33 10797 7088 10845 -1835 -4327 1954 C
ATOM 970 C SER A 33 35.877 160.787 153.479 1.00 80.40 C
ANISOU 970 C SER A 33 11570 7789 11190 -1730 -4066 1797 C
ATOM 971 O SER A 33 35.918 159.555 153.339 1.00 79.29 O
ANISOU 971 O SER A 33 11256 7632 11241 -1641 -4069 1850 O
ATOM 972 CB SER A 33 37.455 162.147 154.877 1.00 78.20 C
ANISOU 972 CB SER A 33 11513 7269 10931 -2141 -4742 2084 C
ATOM 973 OG SER A 33 38.703 162.813 154.903 1.00 80.86 O
ANISOU 973 OG SER A 33 11672 7501 11550 -2255 -5037 2260 O
ATOM 974 N PHE A 34 34.744 161.477 153.598 1.00 78.14 N
ANISOU 974 N PHE A 34 11602 7595 10494 -1736 -3823 1606 N
ATOM 975 CA PHE A 34 33.422 160.896 153.624 1.00 77.63 C
ANISOU 975 CA PHE A 34 11715 7618 10161 -1651 -3549 1446 C
ATOM 976 C PHE A 34 33.034 160.178 152.292 1.00 78.70 C
ANISOU 976 C PHE A 34 11505 7887 10510 -1384 -3216 1344 C
ATOM 977 O PHE A 34 32.323 159.175 152.347 1.00 78.11 O
ANISOU 977 O PHE A 34 11466 7844 10366 -1319 -3109 1296 O
ATOM 978 CB PHE A 34 32.409 161.967 154.036 1.00 79.94 C
ANISOU 978 CB PHE A 34 12393 7947 10035 -1725 -3364 1283 C
ATOM 979 CG PHE A 34 31.103 161.354 154.430 1.00 82.56 C
ANISOU 979 CG PHE A 34 12966 8316 10085 -1701 -3151 1158 C
ATOM 980 CD1 PHE A 34 30.967 160.693 155.642 1.00 88.88 C
ANISOU 980 CD1 PHE A 34 14073 9003 10694 -1878 -3353 1230 C
ATOM 981 CD2 PHE A 34 30.027 161.362 153.554 1.00 84.60 C
ANISOU 981 CD2 PHE A 34 13133 8716 10297 -1507 -2762 981 C
ATOM 982 CE1 PHE A 34 29.772 160.060 155.974 1.00 90.00 C
ANISOU 982 CE1 PHE A 34 14416 9176 10604 -1851 -3135 1117 C
ATOM 983 CE2 PHE A 34 28.827 160.736 153.891 1.00 87.57 C
ANISOU 983 CE2 PHE A 34 13690 9119 10462 -1482 -2566 880 C
ATOM 984 CZ PHE A 34 28.709 160.087 155.095 1.00 87.22 C
ANISOU 984 CZ PHE A 34 13940 8966 10235 -1649 -2738 943 C
ATOM 985 N CYS A 35 33.530 160.665 151.124 1.00 72.68 N
ANISOU 985 N CYS A 35 10432 7187 9998 -1249 -3064 1318 N
ATOM 986 CA CYS A 35 33.317 160.058 149.807 1.00 70.30 C
ANISOU 986 CA CYS A 35 9833 6982 9896 -1028 -2764 1233 C
ATOM 987 C CYS A 35 34.171 158.830 149.692 1.00 74.08 C
ANISOU 987 C CYS A 35 10034 7371 10740 -981 -2892 1374 C
ATOM 988 O CYS A 35 33.707 157.799 149.196 1.00 71.90 O
ANISOU 988 O CYS A 35 9664 7137 10519 -854 -2714 1317 O
ATOM 989 CB CYS A 35 33.641 161.039 148.689 1.00 70.36 C
ANISOU 989 CB CYS A 35 9655 7055 10024 -938 -2574 1169 C
ATOM 990 SG CYS A 35 32.547 162.471 148.631 1.00 73.06 S
ANISOU 990 SG CYS A 35 10283 7497 9980 -959 -2382 997 S
ATOM 991 N VAL A 36 35.433 158.944 150.146 1.00 72.86 N
ANISOU 991 N VAL A 36 9744 7080 10859 -1087 -3207 1568 N
ATOM 992 CA VAL A 36 36.402 157.853 150.138 1.00 74.29 C
ANISOU 992 CA VAL A 36 9629 7134 11463 -1056 -3372 1741 C
ATOM 993 C VAL A 36 35.836 156.645 150.907 1.00 79.47 C
ANISOU 993 C VAL A 36 10449 7756 11989 -1088 -3478 1770 C
ATOM 994 O VAL A 36 35.888 155.528 150.391 1.00 79.46 O
ANISOU 994 O VAL A 36 10236 7736 12218 -955 -3359 1779 O
ATOM 995 CB VAL A 36 37.791 158.332 150.628 1.00 80.03 C
ANISOU 995 CB VAL A 36 10203 7705 12501 -1197 -3742 1967 C
ATOM 996 CG1 VAL A 36 38.748 157.159 150.858 1.00 81.78 C
ANISOU 996 CG1 VAL A 36 10134 7759 13178 -1188 -3972 2181 C
ATOM 997 CG2 VAL A 36 38.391 159.334 149.640 1.00 79.19 C
ANISOU 997 CG2 VAL A 36 9864 7631 12594 -1130 -3574 1934 C
ATOM 998 N VAL A 37 35.209 156.896 152.082 1.00 75.80 N
ANISOU 998 N VAL A 37 10388 7280 11131 -1263 -3657 1764 N
ATOM 999 CA VAL A 37 34.561 155.878 152.924 1.00 75.05 C
ANISOU 999 CA VAL A 37 10525 7153 10839 -1326 -3752 1779 C
ATOM 1000 C VAL A 37 33.426 155.188 152.138 1.00 76.03 C
ANISOU 1000 C VAL A 37 10624 7416 10850 -1138 -3358 1589 C
ATOM 1001 O VAL A 37 33.294 153.964 152.198 1.00 76.11 O
ANISOU 1001 O VAL A 37 10570 7391 10956 -1085 -3365 1625 O
ATOM 1002 CB VAL A 37 34.088 156.502 154.273 1.00 78.96 C
ANISOU 1002 CB VAL A 37 11507 7599 10894 -1570 -3959 1784 C
ATOM 1003 CG1 VAL A 37 32.931 155.730 154.902 1.00 78.00 C
ANISOU 1003 CG1 VAL A 37 11693 7502 10443 -1602 -3866 1696 C
ATOM 1004 CG2 VAL A 37 35.247 156.616 155.250 1.00 81.49 C
ANISOU 1004 CG2 VAL A 37 11878 7733 11351 -1794 -4455 2030 C
ATOM 1005 N GLY A 38 32.648 155.982 151.401 1.00 69.11 N
ANISOU 1005 N GLY A 38 9791 6681 9785 -1047 -3040 1402 N
ATOM 1006 CA GLY A 38 31.537 155.491 150.594 1.00 65.86 C
ANISOU 1006 CA GLY A 38 9362 6400 9262 -887 -2687 1229 C
ATOM 1007 C GLY A 38 31.977 154.646 149.415 1.00 66.50 C
ANISOU 1007 C GLY A 38 9091 6487 9689 -710 -2523 1232 C
ATOM 1008 O GLY A 38 31.355 153.629 149.116 1.00 64.85 O
ANISOU 1008 O GLY A 38 8869 6311 9461 -624 -2377 1174 O
ATOM 1009 N LEU A 39 33.052 155.072 148.741 1.00 62.57 N
ANISOU 1009 N LEU A 39 8321 5946 9509 -663 -2529 1297 N
ATOM 1010 CA LEU A 39 33.648 154.396 147.590 1.00 60.95 C
ANISOU 1010 CA LEU A 39 7783 5709 9667 -508 -2340 1303 C
ATOM 1011 C LEU A 39 34.318 153.105 148.044 1.00 63.96 C
ANISOU 1011 C LEU A 39 8014 5943 10344 -507 -2523 1459 C
ATOM 1012 O LEU A 39 34.095 152.076 147.419 1.00 64.04 O
ANISOU 1012 O LEU A 39 7918 5949 10465 -388 -2330 1410 O
ATOM 1013 CB LEU A 39 34.655 155.314 146.857 1.00 61.24 C
ANISOU 1013 CB LEU A 39 7587 5716 9967 -482 -2290 1338 C
ATOM 1014 CG LEU A 39 34.148 156.661 146.358 1.00 63.54 C
ANISOU 1014 CG LEU A 39 8001 6133 10010 -485 -2126 1203 C
ATOM 1015 CD1 LEU A 39 35.290 157.515 145.893 1.00 64.93 C
ANISOU 1015 CD1 LEU A 39 7961 6249 10460 -496 -2153 1277 C
ATOM 1016 CD2 LEU A 39 33.116 156.512 145.258 1.00 61.98 C
ANISOU 1016 CD2 LEU A 39 7843 6062 9646 -358 -1769 1017 C
ATOM 1017 N ALA A 40 35.093 153.149 149.149 1.00 60.68 N
ANISOU 1017 N ALA A 40 7614 5398 10044 -651 -2910 1651 N
ATOM 1018 CA ALA A 40 35.741 151.983 149.756 1.00 62.17 C
ANISOU 1018 CA ALA A 40 7681 5425 10516 -679 -3160 1835 C
ATOM 1019 C ALA A 40 34.692 150.926 150.146 1.00 67.42 C
ANISOU 1019 C ALA A 40 8560 6131 10924 -667 -3105 1764 C
ATOM 1020 O ALA A 40 34.909 149.744 149.890 1.00 68.74 O
ANISOU 1020 O ALA A 40 8555 6219 11342 -575 -3060 1812 O
ATOM 1021 CB ALA A 40 36.546 152.403 150.980 1.00 64.89 C
ANISOU 1021 CB ALA A 40 8104 5636 10915 -885 -3630 2049 C
ATOM 1022 N SER A 41 33.541 151.351 150.715 1.00 63.85 N
ANISOU 1022 N SER A 41 8474 5794 9990 -754 -3077 1643 N
ATOM 1023 CA SER A 41 32.434 150.465 151.095 1.00 63.61 C
ANISOU 1023 CA SER A 41 8667 5812 9688 -755 -2997 1562 C
ATOM 1024 C SER A 41 31.845 149.759 149.870 1.00 68.77 C
ANISOU 1024 C SER A 41 9169 6555 10406 -562 -2625 1414 C
ATOM 1025 O SER A 41 31.610 148.542 149.892 1.00 69.05 O
ANISOU 1025 O SER A 41 9179 6548 10508 -514 -2599 1430 O
ATOM 1026 CB SER A 41 31.341 151.251 151.806 1.00 64.76 C
ANISOU 1026 CB SER A 41 9202 6053 9350 -875 -2969 1448 C
ATOM 1027 OG SER A 41 31.813 151.686 153.069 1.00 70.91 O
ANISOU 1027 OG SER A 41 10202 6721 10020 -1087 -3326 1586 O
ATOM 1028 N ASN A 42 31.636 150.521 148.794 1.00 64.10 N
ANISOU 1028 N ASN A 42 8488 6072 9795 -464 -2350 1280 N
ATOM 1029 CA ASN A 42 31.093 149.967 147.565 1.00 62.16 C
ANISOU 1029 CA ASN A 42 8137 5899 9581 -311 -2010 1142 C
ATOM 1030 C ASN A 42 32.120 149.066 146.845 1.00 67.99 C
ANISOU 1030 C ASN A 42 8562 6507 10763 -201 -1944 1221 C
ATOM 1031 O ASN A 42 31.729 148.018 146.324 1.00 66.58 O
ANISOU 1031 O ASN A 42 8353 6319 10623 -115 -1770 1163 O
ATOM 1032 CB ASN A 42 30.522 151.073 146.700 1.00 56.54 C
ANISOU 1032 CB ASN A 42 7467 5326 8689 -267 -1770 989 C
ATOM 1033 CG ASN A 42 29.163 151.513 147.205 1.00 67.29 C
ANISOU 1033 CG ASN A 42 9119 6806 9642 -328 -1730 881 C
ATOM 1034 OD1 ASN A 42 28.166 150.778 147.143 1.00 59.68 O
ANISOU 1034 OD1 ASN A 42 8258 5894 8523 -300 -1612 805 O
ATOM 1035 ND2 ASN A 42 29.090 152.713 147.736 1.00 59.08 N
ANISOU 1035 ND2 ASN A 42 8218 5796 8436 -418 -1819 877 N
ATOM 1036 N LEU A 43 33.436 149.410 146.909 1.00 66.41 N
ANISOU 1036 N LEU A 43 8133 6183 10917 -215 -2094 1366 N
ATOM 1037 CA LEU A 43 34.478 148.556 146.333 1.00 68.44 C
ANISOU 1037 CA LEU A 43 8069 6278 11658 -113 -2024 1460 C
ATOM 1038 C LEU A 43 34.567 147.237 147.107 1.00 71.70 C
ANISOU 1038 C LEU A 43 8475 6568 12199 -128 -2218 1583 C
ATOM 1039 O LEU A 43 34.715 146.185 146.488 1.00 71.20 O
ANISOU 1039 O LEU A 43 8263 6420 12370 -15 -2032 1570 O
ATOM 1040 CB LEU A 43 35.848 149.250 146.252 1.00 71.19 C
ANISOU 1040 CB LEU A 43 8145 6507 12396 -127 -2140 1602 C
ATOM 1041 CG LEU A 43 36.009 150.319 145.139 1.00 76.24 C
ANISOU 1041 CG LEU A 43 8704 7223 13041 -71 -1859 1483 C
ATOM 1042 CD1 LEU A 43 37.346 151.058 145.270 1.00 78.20 C
ANISOU 1042 CD1 LEU A 43 8701 7352 13659 -115 -2026 1643 C
ATOM 1043 CD2 LEU A 43 35.817 149.727 143.714 1.00 77.20 C
ANISOU 1043 CD2 LEU A 43 8729 7341 13262 78 -1419 1338 C
ATOM 1044 N LEU A 44 34.389 147.295 148.444 1.00 67.74 N
ANISOU 1044 N LEU A 44 8178 6054 11507 -280 -2574 1689 N
ATOM 1045 CA LEU A 44 34.373 146.124 149.318 1.00 68.71 C
ANISOU 1045 CA LEU A 44 8358 6065 11685 -328 -2802 1813 C
ATOM 1046 C LEU A 44 33.186 145.210 148.962 1.00 72.25 C
ANISOU 1046 C LEU A 44 8964 6605 11882 -254 -2550 1654 C
ATOM 1047 O LEU A 44 33.388 144.007 148.818 1.00 72.18 O
ANISOU 1047 O LEU A 44 8838 6485 12103 -185 -2526 1708 O
ATOM 1048 CB LEU A 44 34.337 146.546 150.805 1.00 69.19 C
ANISOU 1048 CB LEU A 44 8683 6098 11509 -541 -3220 1941 C
ATOM 1049 CG LEU A 44 34.266 145.459 151.890 1.00 74.97 C
ANISOU 1049 CG LEU A 44 9555 6712 12217 -640 -3509 2081 C
ATOM 1050 CD1 LEU A 44 35.402 144.461 151.781 1.00 76.93 C
ANISOU 1050 CD1 LEU A 44 9460 6748 13024 -569 -3652 2280 C
ATOM 1051 CD2 LEU A 44 34.288 146.084 153.275 1.00 79.76 C
ANISOU 1051 CD2 LEU A 44 10475 7283 12549 -880 -3900 2194 C
ATOM 1052 N ALA A 45 31.971 145.778 148.772 1.00 66.94 N
ANISOU 1052 N ALA A 45 8536 6122 10776 -267 -2359 1465 N
ATOM 1053 CA ALA A 45 30.805 144.968 148.423 1.00 65.24 C
ANISOU 1053 CA ALA A 45 8462 5993 10333 -212 -2138 1325 C
ATOM 1054 C ALA A 45 31.043 144.250 147.092 1.00 71.82 C
ANISOU 1054 C ALA A 45 9075 6787 11425 -51 -1830 1253 C
ATOM 1055 O ALA A 45 30.881 143.033 147.026 1.00 71.30 O
ANISOU 1055 O ALA A 45 8997 6654 11442 -3 -1778 1259 O
ATOM 1056 CB ALA A 45 29.554 145.822 148.360 1.00 63.42 C
ANISOU 1056 CB ALA A 45 8479 5949 9669 -252 -1995 1159 C
ATOM 1057 N LEU A 46 31.525 144.985 146.066 1.00 70.50 N
ANISOU 1057 N LEU A 46 8747 6638 11401 22 -1631 1194 N
ATOM 1058 CA LEU A 46 31.844 144.429 144.743 1.00 71.05 C
ANISOU 1058 CA LEU A 46 8642 6646 11706 154 -1304 1117 C
ATOM 1059 C LEU A 46 32.879 143.312 144.838 1.00 77.45 C
ANISOU 1059 C LEU A 46 9215 7236 12975 218 -1352 1260 C
ATOM 1060 O LEU A 46 32.738 142.294 144.160 1.00 77.52 O
ANISOU 1060 O LEU A 46 9194 7178 13081 303 -1125 1198 O
ATOM 1061 CB LEU A 46 32.329 145.528 143.783 1.00 70.72 C
ANISOU 1061 CB LEU A 46 8487 6639 11745 192 -1114 1054 C
ATOM 1062 CG LEU A 46 31.254 146.458 143.239 1.00 72.14 C
ANISOU 1062 CG LEU A 46 8873 7016 11523 167 -963 886 C
ATOM 1063 CD1 LEU A 46 31.862 147.753 142.702 1.00 71.91 C
ANISOU 1063 CD1 LEU A 46 8745 7010 11566 166 -897 874 C
ATOM 1064 CD2 LEU A 46 30.371 145.752 142.202 1.00 72.24 C
ANISOU 1064 CD2 LEU A 46 8993 7075 11381 224 -670 734 C
ATOM 1065 N SER A 47 33.878 143.483 145.717 1.00 75.84 N
ANISOU 1065 N SER A 47 8856 6908 13052 166 -1664 1459 N
ATOM 1066 CA SER A 47 34.923 142.496 145.957 1.00 78.66 C
ANISOU 1066 CA SER A 47 8954 7030 13903 215 -1776 1639 C
ATOM 1067 C SER A 47 34.341 141.203 146.571 1.00 83.96 C
ANISOU 1067 C SER A 47 9759 7657 14485 203 -1882 1670 C
ATOM 1068 O SER A 47 34.592 140.123 146.039 1.00 84.62 O
ANISOU 1068 O SER A 47 9706 7603 14842 309 -1700 1672 O
ATOM 1069 CB SER A 47 36.025 143.090 146.830 1.00 83.94 C
ANISOU 1069 CB SER A 47 9453 7585 14855 128 -2153 1864 C
ATOM 1070 OG SER A 47 37.011 142.124 147.156 1.00 97.66 O
ANISOU 1070 OG SER A 47 10924 9079 17103 166 -2314 2070 O
ATOM 1071 N VAL A 48 33.530 141.312 147.647 1.00 80.62 N
ANISOU 1071 N VAL A 48 9622 7341 13669 70 -2141 1683 N
ATOM 1072 CA VAL A 48 32.908 140.148 148.295 1.00 81.21 C
ANISOU 1072 CA VAL A 48 9859 7383 13614 37 -2247 1710 C
ATOM 1073 C VAL A 48 31.780 139.544 147.391 1.00 85.20 C
ANISOU 1073 C VAL A 48 10502 8002 13868 119 -1881 1494 C
ATOM 1074 O VAL A 48 31.428 138.380 147.548 1.00 85.14 O
ANISOU 1074 O VAL A 48 10554 7933 13861 137 -1870 1502 O
ATOM 1075 CB VAL A 48 32.477 140.419 149.776 1.00 85.35 C
ANISOU 1075 CB VAL A 48 10664 7951 13816 -150 -2630 1804 C
ATOM 1076 CG1 VAL A 48 31.559 141.617 149.911 1.00 83.35 C
ANISOU 1076 CG1 VAL A 48 10672 7908 13088 -234 -2567 1657 C
ATOM 1077 CG2 VAL A 48 31.847 139.197 150.420 1.00 85.59 C
ANISOU 1077 CG2 VAL A 48 10865 7935 13720 -190 -2725 1835 C
ATOM 1078 N LEU A 49 31.269 140.314 146.418 1.00 82.03 N
ANISOU 1078 N LEU A 49 10146 7748 13273 160 -1597 1317 N
ATOM 1079 CA LEU A 49 30.259 139.845 145.464 1.00 80.58 C
ANISOU 1079 CA LEU A 49 10090 7660 12868 218 -1276 1128 C
ATOM 1080 C LEU A 49 30.948 139.050 144.350 1.00 88.38 C
ANISOU 1080 C LEU A 49 10878 8489 14214 347 -992 1102 C
ATOM 1081 O LEU A 49 30.352 138.129 143.794 1.00 87.66 O
ANISOU 1081 O LEU A 49 10880 8385 14044 387 -792 1005 O
ATOM 1082 CB LEU A 49 29.470 141.041 144.893 1.00 78.00 C
ANISOU 1082 CB LEU A 49 9897 7533 12206 192 -1126 973 C
ATOM 1083 CG LEU A 49 28.166 140.810 144.113 1.00 80.46 C
ANISOU 1083 CG LEU A 49 10394 7976 12199 201 -885 795 C
ATOM 1084 CD1 LEU A 49 27.395 139.607 144.605 1.00 81.11 C
ANISOU 1084 CD1 LEU A 49 10614 8044 12158 175 -934 796 C
ATOM 1085 CD2 LEU A 49 27.274 142.023 144.193 1.00 79.89 C
ANISOU 1085 CD2 LEU A 49 10477 8093 11783 135 -894 709 C
ATOM 1086 N ALA A 50 32.213 139.395 144.049 1.00 88.72 N
ANISOU 1086 N ALA A 50 10653 8393 14663 405 -965 1192 N
ATOM 1087 CA ALA A 50 33.025 138.725 143.034 1.00 90.99 C
ANISOU 1087 CA ALA A 50 10730 8488 15353 528 -661 1179 C
ATOM 1088 C ALA A 50 33.400 137.316 143.488 1.00 99.23 C
ANISOU 1088 C ALA A 50 11672 9331 16701 576 -738 1297 C
ATOM 1089 O ALA A 50 33.434 136.401 142.665 1.00100.32 O
ANISOU 1089 O ALA A 50 11784 9346 16985 662 -434 1220 O
ATOM 1090 CB ALA A 50 34.270 139.543 142.725 1.00 93.09 C
ANISOU 1090 CB ALA A 50 10720 8653 15996 566 -627 1261 C
ATOM 1091 N GLY A 51 33.624 137.152 144.793 1.00 97.69 N
ANISOU 1091 N GLY A 51 11453 9096 16568 505 -1143 1480 N
ATOM 1092 CA GLY A 51 33.938 135.870 145.415 1.00 99.65 C
ANISOU 1092 CA GLY A 51 11622 9155 17084 528 -1297 1624 C
ATOM 1093 C GLY A 51 32.716 135.125 145.924 1.00103.11 C
ANISOU 1093 C GLY A 51 12360 9698 17117 462 -1372 1557 C
ATOM 1094 O GLY A 51 32.825 134.324 146.857 1.00104.49 O
ANISOU 1094 O GLY A 51 12542 9763 17396 425 -1634 1704 O
ATOM 1095 N ALA A 52 31.542 135.374 145.309 1.00 97.49 N
ANISOU 1095 N ALA A 52 11894 9189 15958 442 -1148 1346 N
ATOM 1096 CA ALA A 52 30.273 134.736 145.669 1.00130.74 C
ANISOU 1096 CA ALA A 52 16385 13514 19776 377 -1172 1264 C
ATOM 1097 C ALA A 52 29.467 134.387 144.422 1.00159.03 C
ANISOU 1097 C ALA A 52 20089 17165 23168 428 -791 1055 C
ATOM 1098 O ALA A 52 29.968 133.695 143.538 1.00122.94 O
ANISOU 1098 O ALA A 52 15409 12438 18865 524 -531 1019 O
ATOM 1099 CB ALA A 52 29.463 135.651 146.575 1.00129.79 C
ANISOU 1099 CB ALA A 52 16485 13595 19236 242 -1404 1255 C
ATOM 1100 N THR A 59 25.376 132.304 141.505 1.00104.17 N
ANISOU 1100 N THR A 59 13922 10475 15183 343 10 472 N
ATOM 1101 CA THR A 59 26.323 132.851 140.531 1.00104.58 C
ANISOU 1101 CA THR A 59 13846 10438 15450 412 229 433 C
ATOM 1102 C THR A 59 25.533 133.675 139.499 1.00103.99 C
ANISOU 1102 C THR A 59 13934 10516 15060 351 388 286 C
ATOM 1103 O THR A 59 25.710 134.895 139.420 1.00103.26 O
ANISOU 1103 O THR A 59 13783 10526 14924 343 353 283 O
ATOM 1104 CB THR A 59 27.181 131.716 139.885 1.00120.26 C
ANISOU 1104 CB THR A 59 15750 12159 17785 503 477 431 C
ATOM 1105 OG1 THR A 59 27.476 130.683 140.835 1.00121.39 O
ANISOU 1105 OG1 THR A 59 15810 12173 18141 535 305 560 O
ATOM 1106 CG2 THR A 59 28.477 132.237 139.259 1.00121.33 C
ANISOU 1106 CG2 THR A 59 15674 12150 18274 589 670 447 C
ATOM 1107 N ARG A 60 24.628 132.997 138.749 1.00 97.06 N
ANISOU 1107 N ARG A 60 13269 9647 13961 295 533 177 N
ATOM 1108 CA ARG A 60 23.749 133.552 137.708 1.00 93.68 C
ANISOU 1108 CA ARG A 60 13032 9336 13226 211 655 52 C
ATOM 1109 C ARG A 60 22.378 134.033 138.282 1.00 90.41 C
ANISOU 1109 C ARG A 60 12720 9146 12487 118 435 54 C
ATOM 1110 O ARG A 60 21.379 134.106 137.550 1.00 89.98 O
ANISOU 1110 O ARG A 60 12838 9169 12181 31 485 -26 O
ATOM 1111 CB ARG A 60 23.558 132.511 136.570 1.00 94.36 C
ANISOU 1111 CB ARG A 60 13312 9276 13266 178 919 -53 C
ATOM 1112 CG ARG A 60 24.709 132.461 135.558 1.00102.05 C
ANISOU 1112 CG ARG A 60 14251 10047 14477 238 1238 -107 C
ATOM 1113 CD ARG A 60 25.502 131.168 135.591 1.00110.61 C
ANISOU 1113 CD ARG A 60 15274 10876 15877 321 1409 -86 C
ATOM 1114 NE ARG A 60 24.705 130.034 135.116 1.00121.84 N
ANISOU 1114 NE ARG A 60 16950 12234 17111 247 1506 -165 N
ATOM 1115 CZ ARG A 60 25.187 128.826 134.837 1.00128.77 C
ANISOU 1115 CZ ARG A 60 17861 12874 18193 294 1715 -185 C
ATOM 1116 NH1 ARG A 60 26.484 128.572 134.969 1.00118.78 N
ANISOU 1116 NH1 ARG A 60 16367 11399 17366 425 1862 -124 N
ATOM 1117 NH2 ARG A 60 24.378 127.866 134.415 1.00104.82 N
ANISOU 1117 NH2 ARG A 60 15085 9796 14947 207 1781 -259 N
ATOM 1118 N SER A 61 22.345 134.370 139.592 1.00 80.94 N
ANISOU 1118 N SER A 61 11419 8029 11308 128 197 152 N
ATOM 1119 CA SER A 61 21.146 134.835 140.296 1.00 76.15 C
ANISOU 1119 CA SER A 61 10890 7601 10444 51 22 160 C
ATOM 1120 C SER A 61 20.700 136.230 139.845 1.00 72.61 C
ANISOU 1120 C SER A 61 10452 7300 9837 16 26 114 C
ATOM 1121 O SER A 61 21.535 137.100 139.598 1.00 72.80 O
ANISOU 1121 O SER A 61 10375 7317 9970 60 58 121 O
ATOM 1122 CB SER A 61 21.365 134.798 141.805 1.00 79.02 C
ANISOU 1122 CB SER A 61 11183 7973 10869 56 -200 273 C
ATOM 1123 OG SER A 61 20.462 135.643 142.500 1.00 86.56 O
ANISOU 1123 OG SER A 61 12195 9087 11608 -11 -324 277 O
ATOM 1124 N SER A 62 19.376 136.428 139.765 1.00 63.17 N
ANISOU 1124 N SER A 62 9367 6228 8408 -65 -14 78 N
ATOM 1125 CA SER A 62 18.723 137.674 139.410 1.00 60.72 C
ANISOU 1125 CA SER A 62 9068 6051 7952 -105 -33 48 C
ATOM 1126 C SER A 62 18.876 138.695 140.537 1.00 63.51 C
ANISOU 1126 C SER A 62 9328 6486 8317 -85 -168 106 C
ATOM 1127 O SER A 62 19.081 139.874 140.266 1.00 63.94 O
ANISOU 1127 O SER A 62 9334 6598 8362 -73 -162 95 O
ATOM 1128 CB SER A 62 17.244 137.433 139.152 1.00 63.30 C
ANISOU 1128 CB SER A 62 9505 6456 8089 -196 -61 23 C
ATOM 1129 OG SER A 62 17.068 136.515 138.087 1.00 76.61 O
ANISOU 1129 OG SER A 62 11314 8059 9734 -242 46 -29 O
ATOM 1130 N PHE A 63 18.796 138.236 141.793 1.00 57.41 N
ANISOU 1130 N PHE A 63 8557 5703 7552 -93 -287 168 N
ATOM 1131 CA PHE A 63 18.905 139.063 142.982 1.00 55.52 C
ANISOU 1131 CA PHE A 63 8293 5513 7290 -104 -419 224 C
ATOM 1132 C PHE A 63 20.290 139.696 143.059 1.00 59.31 C
ANISOU 1132 C PHE A 63 8658 5938 7940 -48 -460 268 C
ATOM 1133 O PHE A 63 20.405 140.894 143.360 1.00 56.51 O
ANISOU 1133 O PHE A 63 8279 5648 7544 -57 -509 276 O
ATOM 1134 CB PHE A 63 18.620 138.220 144.245 1.00 57.06 C
ANISOU 1134 CB PHE A 63 8562 5669 7450 -147 -531 284 C
ATOM 1135 CG PHE A 63 18.595 139.037 145.514 1.00 57.64 C
ANISOU 1135 CG PHE A 63 8680 5778 7443 -194 -654 333 C
ATOM 1136 CD1 PHE A 63 17.493 139.820 145.834 1.00 59.35 C
ANISOU 1136 CD1 PHE A 63 8964 6093 7492 -246 -616 295 C
ATOM 1137 CD2 PHE A 63 19.706 139.091 146.345 1.00 59.52 C
ANISOU 1137 CD2 PHE A 63 8895 5932 7787 -193 -804 423 C
ATOM 1138 CE1 PHE A 63 17.473 140.582 147.001 1.00 59.77 C
ANISOU 1138 CE1 PHE A 63 9099 6155 7455 -302 -693 328 C
ATOM 1139 CE2 PHE A 63 19.694 139.876 147.495 1.00 62.17 C
ANISOU 1139 CE2 PHE A 63 9322 6284 8014 -264 -923 466 C
ATOM 1140 CZ PHE A 63 18.575 140.611 147.817 1.00 59.53 C
ANISOU 1140 CZ PHE A 63 9090 6043 7484 -319 -849 409 C
ATOM 1141 N LEU A 64 21.346 138.885 142.808 1.00 57.16 N
ANISOU 1141 N LEU A 64 8306 5532 7881 9 -435 303 N
ATOM 1142 CA LEU A 64 22.707 139.415 142.847 1.00 57.71 C
ANISOU 1142 CA LEU A 64 8229 5526 8171 63 -471 362 C
ATOM 1143 C LEU A 64 22.978 140.346 141.683 1.00 62.66 C
ANISOU 1143 C LEU A 64 8806 6190 8811 93 -319 291 C
ATOM 1144 O LEU A 64 23.813 141.243 141.806 1.00 63.21 O
ANISOU 1144 O LEU A 64 8772 6254 8992 115 -363 330 O
ATOM 1145 CB LEU A 64 23.772 138.329 142.956 1.00 59.00 C
ANISOU 1145 CB LEU A 64 8286 5512 8618 121 -480 436 C
ATOM 1146 CG LEU A 64 23.722 137.476 144.212 1.00 63.88 C
ANISOU 1146 CG LEU A 64 8948 6071 9253 85 -676 536 C
ATOM 1147 CD1 LEU A 64 24.584 136.262 144.050 1.00 66.04 C
ANISOU 1147 CD1 LEU A 64 9118 6156 9817 152 -642 595 C
ATOM 1148 CD2 LEU A 64 24.069 138.269 145.459 1.00 63.18 C
ANISOU 1148 CD2 LEU A 64 8860 6002 9143 27 -921 638 C
ATOM 1149 N THR A 65 22.236 140.168 140.567 1.00 58.48 N
ANISOU 1149 N THR A 65 8371 5698 8153 76 -156 194 N
ATOM 1150 CA THR A 65 22.358 141.033 139.400 1.00 57.11 C
ANISOU 1150 CA THR A 65 8199 5555 7946 78 -17 125 C
ATOM 1151 C THR A 65 21.874 142.429 139.779 1.00 56.74 C
ANISOU 1151 C THR A 65 8153 5647 7760 47 -119 130 C
ATOM 1152 O THR A 65 22.601 143.392 139.558 1.00 56.81 O
ANISOU 1152 O THR A 65 8082 5659 7847 71 -104 137 O
ATOM 1153 CB THR A 65 21.631 140.436 138.196 1.00 64.25 C
ANISOU 1153 CB THR A 65 9248 6445 8720 35 139 37 C
ATOM 1154 OG1 THR A 65 22.213 139.168 137.880 1.00 65.18 O
ANISOU 1154 OG1 THR A 65 9371 6405 8989 69 263 29 O
ATOM 1155 CG2 THR A 65 21.664 141.369 136.979 1.00 60.78 C
ANISOU 1155 CG2 THR A 65 8858 6034 8201 7 260 -27 C
ATOM 1156 N PHE A 66 20.679 142.522 140.395 1.00 50.38 N
ANISOU 1156 N PHE A 66 7429 4941 6773 -6 -210 128 N
ATOM 1157 CA PHE A 66 20.105 143.785 140.864 1.00 49.08 C
ANISOU 1157 CA PHE A 66 7272 4887 6490 -34 -284 131 C
ATOM 1158 C PHE A 66 20.991 144.435 141.931 1.00 56.56 C
ANISOU 1158 C PHE A 66 8155 5815 7520 -20 -406 198 C
ATOM 1159 O PHE A 66 21.281 145.636 141.845 1.00 56.34 O
ANISOU 1159 O PHE A 66 8092 5830 7486 -17 -418 195 O
ATOM 1160 CB PHE A 66 18.664 143.590 141.353 1.00 49.12 C
ANISOU 1160 CB PHE A 66 7363 4965 6335 -89 -318 121 C
ATOM 1161 CG PHE A 66 17.719 143.272 140.223 1.00 49.78 C
ANISOU 1161 CG PHE A 66 7502 5075 6335 -125 -238 72 C
ATOM 1162 CD1 PHE A 66 17.552 144.156 139.161 1.00 53.09 C
ANISOU 1162 CD1 PHE A 66 7922 5532 6716 -137 -189 39 C
ATOM 1163 CD2 PHE A 66 16.979 142.101 140.226 1.00 49.88 C
ANISOU 1163 CD2 PHE A 66 7581 5068 6302 -162 -233 68 C
ATOM 1164 CE1 PHE A 66 16.694 143.847 138.110 1.00 53.36 C
ANISOU 1164 CE1 PHE A 66 8034 5576 6665 -197 -156 11 C
ATOM 1165 CE2 PHE A 66 16.122 141.798 139.180 1.00 51.99 C
ANISOU 1165 CE2 PHE A 66 7914 5348 6492 -218 -192 36 C
ATOM 1166 CZ PHE A 66 15.989 142.664 138.128 1.00 50.89 C
ANISOU 1166 CZ PHE A 66 7786 5238 6312 -241 -163 12 C
ATOM 1167 N LEU A 67 21.482 143.615 142.874 1.00 54.89 N
ANISOU 1167 N LEU A 67 7937 5526 7392 -22 -511 266 N
ATOM 1168 CA LEU A 67 22.403 144.008 143.936 1.00 55.68 C
ANISOU 1168 CA LEU A 67 7999 5576 7583 -36 -675 355 C
ATOM 1169 C LEU A 67 23.710 144.578 143.355 1.00 59.19 C
ANISOU 1169 C LEU A 67 8289 5962 8239 17 -656 383 C
ATOM 1170 O LEU A 67 24.171 145.609 143.836 1.00 59.01 O
ANISOU 1170 O LEU A 67 8244 5956 8223 -7 -756 422 O
ATOM 1171 CB LEU A 67 22.661 142.799 144.851 1.00 56.66 C
ANISOU 1171 CB LEU A 67 8150 5602 7775 -56 -799 435 C
ATOM 1172 CG LEU A 67 23.420 142.962 146.178 1.00 62.77 C
ANISOU 1172 CG LEU A 67 8943 6304 8603 -112 -1033 554 C
ATOM 1173 CD1 LEU A 67 23.065 144.234 146.913 1.00 62.54 C
ANISOU 1173 CD1 LEU A 67 9030 6349 8385 -188 -1104 546 C
ATOM 1174 CD2 LEU A 67 23.080 141.813 147.086 1.00 67.61 C
ANISOU 1174 CD2 LEU A 67 9665 6855 9168 -164 -1139 609 C
ATOM 1175 N CYS A 68 24.251 143.959 142.285 1.00 56.46 N
ANISOU 1175 N CYS A 68 7854 5542 8057 80 -505 356 N
ATOM 1176 CA CYS A 68 25.455 144.424 141.582 1.00 57.96 C
ANISOU 1176 CA CYS A 68 7892 5657 8472 132 -423 371 C
ATOM 1177 C CYS A 68 25.183 145.779 140.868 1.00 60.22 C
ANISOU 1177 C CYS A 68 8206 6048 8628 118 -340 301 C
ATOM 1178 O CYS A 68 26.045 146.672 140.856 1.00 59.93 O
ANISOU 1178 O CYS A 68 8066 5992 8712 129 -366 337 O
ATOM 1179 CB CYS A 68 25.953 143.362 140.608 1.00 59.95 C
ANISOU 1179 CB CYS A 68 8085 5783 8910 192 -226 341 C
ATOM 1180 SG CYS A 68 27.510 143.788 139.788 1.00 65.99 S
ANISOU 1180 SG CYS A 68 8645 6413 10014 259 -73 366 S
ATOM 1181 N GLY A 69 23.967 145.923 140.329 1.00 54.35 N
ANISOU 1181 N GLY A 69 7594 5405 7650 87 -264 217 N
ATOM 1182 CA GLY A 69 23.503 147.166 139.730 1.00 53.02 C
ANISOU 1182 CA GLY A 69 7468 5335 7344 65 -218 163 C
ATOM 1183 C GLY A 69 23.482 148.299 140.749 1.00 55.16 C
ANISOU 1183 C GLY A 69 7734 5668 7557 38 -369 206 C
ATOM 1184 O GLY A 69 23.953 149.401 140.462 1.00 53.37 O
ANISOU 1184 O GLY A 69 7462 5460 7355 41 -359 204 O
ATOM 1185 N LEU A 70 22.977 148.003 141.970 1.00 52.25 N
ANISOU 1185 N LEU A 70 7433 5314 7106 2 -499 244 N
ATOM 1186 CA LEU A 70 22.824 148.921 143.111 1.00 52.28 C
ANISOU 1186 CA LEU A 70 7499 5353 7013 -48 -631 278 C
ATOM 1187 C LEU A 70 24.159 149.391 143.637 1.00 58.46 C
ANISOU 1187 C LEU A 70 8199 6065 7947 -57 -760 359 C
ATOM 1188 O LEU A 70 24.314 150.578 143.886 1.00 58.52 O
ANISOU 1188 O LEU A 70 8225 6103 7905 -85 -803 361 O
ATOM 1189 CB LEU A 70 22.013 148.250 144.237 1.00 52.47 C
ANISOU 1189 CB LEU A 70 7650 5375 6912 -101 -707 296 C
ATOM 1190 CG LEU A 70 21.717 149.072 145.493 1.00 56.87 C
ANISOU 1190 CG LEU A 70 8338 5943 7328 -177 -804 317 C
ATOM 1191 CD1 LEU A 70 20.720 150.155 145.223 1.00 55.75 C
ANISOU 1191 CD1 LEU A 70 8243 5884 7057 -179 -693 246 C
ATOM 1192 CD2 LEU A 70 21.175 148.193 146.569 1.00 61.29 C
ANISOU 1192 CD2 LEU A 70 9034 6467 7788 -239 -866 344 C
ATOM 1193 N VAL A 71 25.135 148.479 143.762 1.00 55.92 N
ANISOU 1193 N VAL A 71 7776 5636 7834 -35 -825 433 N
ATOM 1194 CA VAL A 71 26.472 148.807 144.250 1.00 55.65 C
ANISOU 1194 CA VAL A 71 7625 5510 8009 -48 -977 540 C
ATOM 1195 C VAL A 71 27.240 149.665 143.239 1.00 58.08 C
ANISOU 1195 C VAL A 71 7792 5814 8460 -2 -864 519 C
ATOM 1196 O VAL A 71 27.896 150.624 143.648 1.00 58.36 O
ANISOU 1196 O VAL A 71 7792 5839 8545 -41 -982 574 O
ATOM 1197 CB VAL A 71 27.245 147.551 144.712 1.00 60.45 C
ANISOU 1197 CB VAL A 71 8140 5983 8846 -35 -1088 646 C
ATOM 1198 CG1 VAL A 71 28.622 147.928 145.227 1.00 62.34 C
ANISOU 1198 CG1 VAL A 71 8231 6111 9343 -59 -1281 783 C
ATOM 1199 CG2 VAL A 71 26.474 146.817 145.813 1.00 59.59 C
ANISOU 1199 CG2 VAL A 71 8205 5876 8561 -103 -1219 672 C
ATOM 1200 N LEU A 72 27.143 149.342 141.933 1.00 54.41 N
ANISOU 1200 N LEU A 72 7275 5351 8047 64 -635 440 N
ATOM 1201 CA LEU A 72 27.785 150.111 140.857 1.00 54.67 C
ANISOU 1201 CA LEU A 72 7212 5374 8187 96 -485 405 C
ATOM 1202 C LEU A 72 27.180 151.505 140.747 1.00 54.12 C
ANISOU 1202 C LEU A 72 7239 5422 7903 57 -491 352 C
ATOM 1203 O LEU A 72 27.919 152.458 140.522 1.00 53.27 O
ANISOU 1203 O LEU A 72 7053 5301 7886 53 -491 372 O
ATOM 1204 CB LEU A 72 27.659 149.402 139.501 1.00 55.63 C
ANISOU 1204 CB LEU A 72 7337 5459 8343 144 -226 320 C
ATOM 1205 CG LEU A 72 28.584 148.231 139.241 1.00 62.32 C
ANISOU 1205 CG LEU A 72 8048 6146 9484 201 -126 361 C
ATOM 1206 CD1 LEU A 72 28.102 147.440 138.043 1.00 62.64 C
ANISOU 1206 CD1 LEU A 72 8191 6158 9453 218 128 255 C
ATOM 1207 CD2 LEU A 72 30.039 148.689 139.074 1.00 64.00 C
ANISOU 1207 CD2 LEU A 72 8048 6243 10026 232 -95 434 C
ATOM 1208 N THR A 73 25.844 151.622 140.928 1.00 48.72 N
ANISOU 1208 N THR A 73 6711 4839 6960 30 -494 292 N
ATOM 1209 CA THR A 73 25.140 152.897 140.932 1.00 47.89 C
ANISOU 1209 CA THR A 73 6693 4829 6673 -1 -500 250 C
ATOM 1210 C THR A 73 25.575 153.747 142.134 1.00 53.75 C
ANISOU 1210 C THR A 73 7458 5562 7405 -52 -676 313 C
ATOM 1211 O THR A 73 25.915 154.918 141.937 1.00 54.16 O
ANISOU 1211 O THR A 73 7494 5632 7453 -65 -679 309 O
ATOM 1212 CB THR A 73 23.635 152.688 140.843 1.00 55.72 C
ANISOU 1212 CB THR A 73 7809 5901 7462 -13 -452 189 C
ATOM 1213 OG1 THR A 73 23.368 151.925 139.668 1.00 53.24 O
ANISOU 1213 OG1 THR A 73 7493 5579 7156 12 -315 141 O
ATOM 1214 CG2 THR A 73 22.861 154.013 140.789 1.00 53.41 C
ANISOU 1214 CG2 THR A 73 7581 5683 7028 -34 -442 154 C
ATOM 1215 N ASP A 74 25.615 153.163 143.356 1.00 50.93 N
ANISOU 1215 N ASP A 74 7157 5161 7035 -96 -830 375 N
ATOM 1216 CA ASP A 74 26.053 153.875 144.568 1.00 52.35 C
ANISOU 1216 CA ASP A 74 7410 5304 7175 -179 -1021 443 C
ATOM 1217 C ASP A 74 27.494 154.347 144.450 1.00 58.84 C
ANISOU 1217 C ASP A 74 8080 6054 8222 -186 -1117 526 C
ATOM 1218 O ASP A 74 27.753 155.521 144.709 1.00 60.42 O
ANISOU 1218 O ASP A 74 8321 6264 8372 -235 -1180 536 O
ATOM 1219 CB ASP A 74 25.889 153.014 145.817 1.00 55.79 C
ANISOU 1219 CB ASP A 74 7962 5685 7551 -246 -1174 504 C
ATOM 1220 CG ASP A 74 24.465 152.618 146.146 1.00 68.57 C
ANISOU 1220 CG ASP A 74 9745 7361 8947 -259 -1083 432 C
ATOM 1221 OD1 ASP A 74 23.525 153.162 145.504 1.00 69.46 O
ANISOU 1221 OD1 ASP A 74 9877 7558 8959 -221 -920 342 O
ATOM 1222 OD2 ASP A 74 24.285 151.763 147.027 1.00 70.56 O
ANISOU 1222 OD2 ASP A 74 10100 7565 9145 -313 -1179 474 O
ATOM 1223 N PHE A 75 28.415 153.459 144.004 1.00 54.87 N
ANISOU 1223 N PHE A 75 7394 5467 7988 -135 -1109 586 N
ATOM 1224 CA PHE A 75 29.827 153.788 143.796 1.00 55.24 C
ANISOU 1224 CA PHE A 75 7243 5421 8325 -130 -1174 678 C
ATOM 1225 C PHE A 75 29.947 154.974 142.853 1.00 59.82 C
ANISOU 1225 C PHE A 75 7785 6057 8887 -108 -1027 611 C
ATOM 1226 O PHE A 75 30.511 155.988 143.235 1.00 60.36 O
ANISOU 1226 O PHE A 75 7843 6113 8980 -166 -1148 660 O
ATOM 1227 CB PHE A 75 30.615 152.581 143.242 1.00 57.26 C
ANISOU 1227 CB PHE A 75 7293 5565 8897 -53 -1094 727 C
ATOM 1228 CG PHE A 75 32.065 152.882 142.933 1.00 60.01 C
ANISOU 1228 CG PHE A 75 7397 5797 9607 -36 -1115 825 C
ATOM 1229 CD1 PHE A 75 33.040 152.788 143.922 1.00 64.83 C
ANISOU 1229 CD1 PHE A 75 7896 6291 10446 -97 -1396 993 C
ATOM 1230 CD2 PHE A 75 32.458 153.263 141.653 1.00 61.71 C
ANISOU 1230 CD2 PHE A 75 7498 6006 9944 27 -860 759 C
ATOM 1231 CE1 PHE A 75 34.375 153.100 143.642 1.00 66.74 C
ANISOU 1231 CE1 PHE A 75 7879 6413 11066 -85 -1423 1100 C
ATOM 1232 CE2 PHE A 75 33.793 153.586 141.377 1.00 65.41 C
ANISOU 1232 CE2 PHE A 75 7728 6356 10769 39 -853 850 C
ATOM 1233 CZ PHE A 75 34.743 153.482 142.368 1.00 65.14 C
ANISOU 1233 CZ PHE A 75 7546 6207 10997 -10 -1133 1024 C
ATOM 1234 N LEU A 76 29.395 154.859 141.638 1.00 57.07 N
ANISOU 1234 N LEU A 76 7441 5765 8480 -41 -782 503 N
ATOM 1235 CA LEU A 76 29.457 155.912 140.625 1.00 56.91 C
ANISOU 1235 CA LEU A 76 7408 5789 8427 -28 -633 439 C
ATOM 1236 C LEU A 76 28.826 157.208 141.038 1.00 58.81 C
ANISOU 1236 C LEU A 76 7787 6116 8443 -80 -707 408 C
ATOM 1237 O LEU A 76 29.373 158.258 140.727 1.00 58.85 O
ANISOU 1237 O LEU A 76 7747 6118 8495 -98 -701 417 O
ATOM 1238 CB LEU A 76 28.892 155.448 139.307 1.00 56.77 C
ANISOU 1238 CB LEU A 76 7426 5800 8346 22 -390 339 C
ATOM 1239 CG LEU A 76 29.971 155.135 138.328 1.00 63.83 C
ANISOU 1239 CG LEU A 76 8169 6589 9496 62 -213 346 C
ATOM 1240 CD1 LEU A 76 29.871 153.690 137.863 1.00 64.88 C
ANISOU 1240 CD1 LEU A 76 8290 6651 9709 108 -72 319 C
ATOM 1241 CD2 LEU A 76 29.981 156.164 137.200 1.00 66.01 C
ANISOU 1241 CD2 LEU A 76 8485 6896 9699 48 -55 280 C
ATOM 1242 N GLY A 77 27.704 157.123 141.745 1.00 54.23 N
ANISOU 1242 N GLY A 77 7368 5597 7639 -106 -762 375 N
ATOM 1243 CA GLY A 77 26.988 158.280 142.262 1.00 52.94 C
ANISOU 1243 CA GLY A 77 7351 5491 7271 -152 -806 342 C
ATOM 1244 C GLY A 77 27.890 159.109 143.138 1.00 57.82 C
ANISOU 1244 C GLY A 77 7978 6054 7938 -228 -984 418 C
ATOM 1245 O GLY A 77 28.130 160.284 142.847 1.00 56.62 O
ANISOU 1245 O GLY A 77 7828 5917 7770 -246 -968 405 O
ATOM 1246 N LEU A 78 28.469 158.454 144.165 1.00 55.63 N
ANISOU 1246 N LEU A 78 7702 5699 7736 -284 -1170 511 N
ATOM 1247 CA LEU A 78 29.399 159.083 145.107 1.00 57.07 C
ANISOU 1247 CA LEU A 78 7909 5804 7972 -388 -1398 612 C
ATOM 1248 C LEU A 78 30.610 159.708 144.414 1.00 60.27 C
ANISOU 1248 C LEU A 78 8112 6168 8618 -375 -1403 665 C
ATOM 1249 O LEU A 78 30.995 160.806 144.769 1.00 59.84 O
ANISOU 1249 O LEU A 78 8111 6097 8529 -449 -1505 693 O
ATOM 1250 CB LEU A 78 29.839 158.098 146.223 1.00 58.25 C
ANISOU 1250 CB LEU A 78 8089 5859 8185 -460 -1626 725 C
ATOM 1251 CG LEU A 78 28.788 157.771 147.275 1.00 61.55 C
ANISOU 1251 CG LEU A 78 8773 6287 8325 -530 -1671 692 C
ATOM 1252 CD1 LEU A 78 29.039 156.428 147.887 1.00 62.11 C
ANISOU 1252 CD1 LEU A 78 8830 6284 8485 -553 -1813 780 C
ATOM 1253 CD2 LEU A 78 28.671 158.880 148.312 1.00 63.59 C
ANISOU 1253 CD2 LEU A 78 9280 6512 8370 -668 -1798 699 C
ATOM 1254 N LEU A 79 31.169 159.034 143.406 1.00 57.09 N
ANISOU 1254 N LEU A 79 7495 5740 8456 -285 -1268 671 N
ATOM 1255 CA LEU A 79 32.326 159.504 142.656 1.00 57.70 C
ANISOU 1255 CA LEU A 79 7364 5761 8800 -266 -1218 718 C
ATOM 1256 C LEU A 79 32.035 160.748 141.818 1.00 61.29 C
ANISOU 1256 C LEU A 79 7870 6291 9126 -256 -1065 627 C
ATOM 1257 O LEU A 79 32.773 161.724 141.927 1.00 63.30 O
ANISOU 1257 O LEU A 79 8078 6514 9459 -311 -1151 678 O
ATOM 1258 CB LEU A 79 32.882 158.363 141.793 1.00 58.58 C
ANISOU 1258 CB LEU A 79 7268 5804 9184 -173 -1051 728 C
ATOM 1259 CG LEU A 79 34.148 158.638 140.981 1.00 64.11 C
ANISOU 1259 CG LEU A 79 7725 6410 10224 -146 -946 781 C
ATOM 1260 CD1 LEU A 79 35.325 158.971 141.885 1.00 65.21 C
ANISOU 1260 CD1 LEU A 79 7717 6440 10621 -225 -1224 949 C
ATOM 1261 CD2 LEU A 79 34.468 157.446 140.082 1.00 65.76 C
ANISOU 1261 CD2 LEU A 79 7785 6539 10661 -51 -705 758 C
ATOM 1262 N VAL A 80 30.955 160.740 141.023 1.00 55.19 N
ANISOU 1262 N VAL A 80 7200 5610 8160 -199 -867 507 N
ATOM 1263 CA VAL A 80 30.594 161.866 140.152 1.00 53.73 C
ANISOU 1263 CA VAL A 80 7073 5489 7854 -192 -732 430 C
ATOM 1264 C VAL A 80 30.148 163.104 140.959 1.00 57.33 C
ANISOU 1264 C VAL A 80 7686 5981 8116 -259 -858 424 C
ATOM 1265 O VAL A 80 30.801 164.146 140.860 1.00 57.33 O
ANISOU 1265 O VAL A 80 7655 5958 8168 -300 -895 450 O
ATOM 1266 CB VAL A 80 29.566 161.445 139.070 1.00 56.30 C
ANISOU 1266 CB VAL A 80 7470 5881 8043 -131 -527 328 C
ATOM 1267 CG1 VAL A 80 29.145 162.636 138.209 1.00 55.47 C
ANISOU 1267 CG1 VAL A 80 7439 5828 7810 -138 -427 268 C
ATOM 1268 CG2 VAL A 80 30.118 160.309 138.202 1.00 56.23 C
ANISOU 1268 CG2 VAL A 80 7339 5809 8217 -81 -370 324 C
ATOM 1269 N THR A 81 29.056 162.978 141.753 1.00 52.45 N
ANISOU 1269 N THR A 81 7240 5403 7285 -274 -903 387 N
ATOM 1270 CA THR A 81 28.501 164.032 142.602 1.00 51.28 C
ANISOU 1270 CA THR A 81 7275 5263 6944 -338 -978 367 C
ATOM 1271 C THR A 81 29.452 164.426 143.748 1.00 58.87 C
ANISOU 1271 C THR A 81 8280 6140 7946 -450 -1205 460 C
ATOM 1272 O THR A 81 29.501 165.592 144.117 1.00 60.37 O
ANISOU 1272 O THR A 81 8584 6314 8042 -515 -1255 455 O
ATOM 1273 CB THR A 81 27.120 163.639 143.157 1.00 54.98 C
ANISOU 1273 CB THR A 81 7904 5769 7216 -326 -926 306 C
ATOM 1274 OG1 THR A 81 27.238 162.471 143.961 1.00 61.34 O
ANISOU 1274 OG1 THR A 81 8729 6539 8040 -351 -1025 351 O
ATOM 1275 CG2 THR A 81 26.090 163.394 142.083 1.00 47.45 C
ANISOU 1275 CG2 THR A 81 6919 4889 6221 -238 -745 232 C
ATOM 1276 N GLY A 82 30.174 163.459 144.310 1.00 56.68 N
ANISOU 1276 N GLY A 82 7927 5799 7811 -482 -1354 552 N
ATOM 1277 CA GLY A 82 31.116 163.691 145.399 1.00 57.62 C
ANISOU 1277 CA GLY A 82 8083 5819 7989 -610 -1621 669 C
ATOM 1278 C GLY A 82 32.251 164.606 144.997 1.00 63.19 C
ANISOU 1278 C GLY A 82 8649 6484 8878 -644 -1683 732 C
ATOM 1279 O GLY A 82 32.604 165.509 145.760 1.00 64.32 O
ANISOU 1279 O GLY A 82 8921 6574 8943 -766 -1855 779 O
ATOM 1280 N THR A 83 32.808 164.403 143.785 1.00 59.64 N
ANISOU 1280 N THR A 83 7954 6046 8660 -549 -1528 729 N
ATOM 1281 CA THR A 83 33.911 165.227 143.265 1.00 60.77 C
ANISOU 1281 CA THR A 83 7935 6144 9012 -574 -1542 786 C
ATOM 1282 C THR A 83 33.458 166.650 142.933 1.00 62.29 C
ANISOU 1282 C THR A 83 8267 6395 9007 -594 -1457 703 C
ATOM 1283 O THR A 83 34.287 167.555 142.957 1.00 64.28 O
ANISOU 1283 O THR A 83 8470 6599 9356 -664 -1548 762 O
ATOM 1284 CB THR A 83 34.649 164.552 142.100 1.00 76.20 C
ANISOU 1284 CB THR A 83 9610 8066 11276 -477 -1360 802 C
ATOM 1285 OG1 THR A 83 33.700 164.194 141.104 1.00 85.12 O
ANISOU 1285 OG1 THR A 83 10793 9283 12265 -375 -1094 671 O
ATOM 1286 CG2 THR A 83 35.413 163.298 142.533 1.00 73.64 C
ANISOU 1286 CG2 THR A 83 9101 7640 11240 -470 -1481 922 C
ATOM 1287 N ILE A 84 32.158 166.862 142.659 1.00 53.77 N
ANISOU 1287 N ILE A 84 7352 5405 7674 -537 -1296 580 N
ATOM 1288 CA ILE A 84 31.636 168.206 142.402 1.00 51.36 C
ANISOU 1288 CA ILE A 84 7181 5138 7195 -551 -1221 509 C
ATOM 1289 C ILE A 84 31.457 168.908 143.742 1.00 55.33 C
ANISOU 1289 C ILE A 84 7913 5591 7518 -669 -1396 527 C
ATOM 1290 O ILE A 84 31.854 170.063 143.888 1.00 57.95 O
ANISOU 1290 O ILE A 84 8308 5889 7822 -740 -1456 541 O
ATOM 1291 CB ILE A 84 30.352 168.207 141.534 1.00 51.96 C
ANISOU 1291 CB ILE A 84 7319 5304 7121 -451 -1000 394 C
ATOM 1292 CG1 ILE A 84 30.650 167.594 140.137 1.00 50.94 C
ANISOU 1292 CG1 ILE A 84 7012 5200 7144 -370 -830 378 C
ATOM 1293 CG2 ILE A 84 29.746 169.636 141.433 1.00 51.77 C
ANISOU 1293 CG2 ILE A 84 7439 5297 6935 -467 -948 337 C
ATOM 1294 CD1 ILE A 84 29.465 167.363 139.256 1.00 53.09 C
ANISOU 1294 CD1 ILE A 84 7345 5544 7285 -296 -660 292 C
ATOM 1295 N VAL A 85 30.907 168.196 144.723 1.00 49.03 N
ANISOU 1295 N VAL A 85 7258 4775 6595 -703 -1472 528 N
ATOM 1296 CA VAL A 85 30.708 168.673 146.083 1.00 49.29 C
ANISOU 1296 CA VAL A 85 7564 4735 6428 -838 -1623 541 C
ATOM 1297 C VAL A 85 32.060 169.101 146.710 1.00 59.11 C
ANISOU 1297 C VAL A 85 8794 5879 7788 -985 -1898 672 C
ATOM 1298 O VAL A 85 32.182 170.230 147.173 1.00 60.29 O
ANISOU 1298 O VAL A 85 9118 5977 7814 -1089 -1968 669 O
ATOM 1299 CB VAL A 85 29.947 167.607 146.910 1.00 51.65 C
ANISOU 1299 CB VAL A 85 8003 5026 6595 -849 -1636 526 C
ATOM 1300 CG1 VAL A 85 30.116 167.828 148.405 1.00 52.96 C
ANISOU 1300 CG1 VAL A 85 8458 5080 6586 -1032 -1845 576 C
ATOM 1301 CG2 VAL A 85 28.469 167.594 146.532 1.00 49.61 C
ANISOU 1301 CG2 VAL A 85 7821 4841 6186 -744 -1379 397 C
ATOM 1302 N VAL A 86 33.080 168.227 146.649 1.00 58.98 N
ANISOU 1302 N VAL A 86 8553 5822 8034 -991 -2048 792 N
ATOM 1303 CA VAL A 86 34.430 168.470 147.181 1.00 60.96 C
ANISOU 1303 CA VAL A 86 8726 5962 8473 -1129 -2340 950 C
ATOM 1304 C VAL A 86 35.083 169.664 146.480 1.00 65.58 C
ANISOU 1304 C VAL A 86 9201 6549 9167 -1136 -2298 954 C
ATOM 1305 O VAL A 86 35.660 170.518 147.169 1.00 67.52 O
ANISOU 1305 O VAL A 86 9573 6713 9368 -1290 -2508 1024 O
ATOM 1306 CB VAL A 86 35.308 167.188 147.140 1.00 65.22 C
ANISOU 1306 CB VAL A 86 8995 6447 9340 -1104 -2475 1085 C
ATOM 1307 CG1 VAL A 86 36.752 167.477 147.540 1.00 66.94 C
ANISOU 1307 CG1 VAL A 86 9064 6538 9833 -1237 -2778 1271 C
ATOM 1308 CG2 VAL A 86 34.713 166.097 148.025 1.00 64.84 C
ANISOU 1308 CG2 VAL A 86 9103 6378 9154 -1133 -2568 1097 C
ATOM 1309 N SER A 87 34.951 169.756 145.128 1.00 59.17 N
ANISOU 1309 N SER A 87 8192 5820 8469 -986 -2030 878 N
ATOM 1310 CA SER A 87 35.521 170.888 144.384 1.00 58.93 C
ANISOU 1310 CA SER A 87 8069 5792 8531 -992 -1962 874 C
ATOM 1311 C SER A 87 34.910 172.218 144.841 1.00 61.01 C
ANISOU 1311 C SER A 87 8623 6058 8501 -1069 -1969 801 C
ATOM 1312 O SER A 87 35.650 173.172 145.052 1.00 61.45 O
ANISOU 1312 O SER A 87 8698 6051 8600 -1178 -2101 861 O
ATOM 1313 CB SER A 87 35.335 170.714 142.879 1.00 61.02 C
ANISOU 1313 CB SER A 87 8150 6136 8898 -837 -1658 791 C
ATOM 1314 OG SER A 87 36.091 169.608 142.418 1.00 71.48 O
ANISOU 1314 OG SER A 87 9201 7424 10535 -779 -1625 863 O
ATOM 1315 N GLN A 88 33.569 172.253 145.032 1.00 55.33 N
ANISOU 1315 N GLN A 88 8123 5393 7507 -1017 -1822 679 N
ATOM 1316 CA GLN A 88 32.845 173.438 145.470 1.00 54.92 C
ANISOU 1316 CA GLN A 88 8348 5324 7195 -1071 -1775 597 C
ATOM 1317 C GLN A 88 33.192 173.877 146.867 1.00 62.50 C
ANISOU 1317 C GLN A 88 9570 6166 8010 -1265 -2018 656 C
ATOM 1318 O GLN A 88 33.208 175.078 147.103 1.00 64.26 O
ANISOU 1318 O GLN A 88 9968 6339 8110 -1346 -2029 630 O
ATOM 1319 CB GLN A 88 31.331 173.285 145.315 1.00 54.46 C
ANISOU 1319 CB GLN A 88 8417 5330 6945 -960 -1543 467 C
ATOM 1320 CG GLN A 88 30.835 173.210 143.864 1.00 58.62 C
ANISOU 1320 CG GLN A 88 8758 5960 7557 -799 -1312 402 C
ATOM 1321 CD GLN A 88 31.228 174.376 142.982 1.00 69.19 C
ANISOU 1321 CD GLN A 88 10036 7305 8950 -791 -1248 393 C
ATOM 1322 OE1 GLN A 88 31.323 174.241 141.757 1.00 67.61 O
ANISOU 1322 OE1 GLN A 88 9662 7162 8866 -705 -1121 381 O
ATOM 1323 NE2 GLN A 88 31.430 175.551 143.562 1.00 50.26 N
ANISOU 1323 NE2 GLN A 88 7807 4837 6452 -890 -1323 394 N
ATOM 1324 N HIS A 89 33.491 172.934 147.789 1.00 59.43 N
ANISOU 1324 N HIS A 89 9234 5720 7629 -1354 -2224 742 N
ATOM 1325 CA HIS A 89 33.901 173.252 149.163 1.00 61.19 C
ANISOU 1325 CA HIS A 89 9743 5809 7699 -1578 -2501 819 C
ATOM 1326 C HIS A 89 35.310 173.840 149.114 1.00 68.91 C
ANISOU 1326 C HIS A 89 10579 6716 8890 -1696 -2752 961 C
ATOM 1327 O HIS A 89 35.550 174.888 149.715 1.00 70.70 O
ANISOU 1327 O HIS A 89 11043 6854 8967 -1855 -2876 974 O
ATOM 1328 CB HIS A 89 33.856 172.013 150.065 1.00 62.16 C
ANISOU 1328 CB HIS A 89 9952 5884 7783 -1646 -2669 888 C
ATOM 1329 CG HIS A 89 32.489 171.680 150.576 1.00 64.56 C
ANISOU 1329 CG HIS A 89 10526 6204 7799 -1614 -2474 759 C
ATOM 1330 ND1 HIS A 89 32.084 172.054 151.843 1.00 67.79 N
ANISOU 1330 ND1 HIS A 89 11365 6497 7897 -1795 -2545 732 N
ATOM 1331 CD2 HIS A 89 31.491 170.978 149.992 1.00 63.74 C
ANISOU 1331 CD2 HIS A 89 10322 6205 7691 -1436 -2215 658 C
ATOM 1332 CE1 HIS A 89 30.856 171.575 151.982 1.00 65.66 C
ANISOU 1332 CE1 HIS A 89 11219 6263 7466 -1709 -2302 615 C
ATOM 1333 NE2 HIS A 89 30.452 170.938 150.888 1.00 63.65 N
ANISOU 1333 NE2 HIS A 89 10645 6145 7394 -1493 -2112 572 N
ATOM 1334 N ALA A 90 36.209 173.216 148.310 1.00 65.77 N
ANISOU 1334 N ALA A 90 9787 6348 8856 -1612 -2788 1058 N
ATOM 1335 CA ALA A 90 37.591 173.660 148.080 1.00 66.44 C
ANISOU 1335 CA ALA A 90 9644 6364 9236 -1696 -2986 1203 C
ATOM 1336 C ALA A 90 37.663 175.033 147.400 1.00 69.34 C
ANISOU 1336 C ALA A 90 10016 6758 9571 -1684 -2844 1136 C
ATOM 1337 O ALA A 90 38.674 175.724 147.527 1.00 71.23 O
ANISOU 1337 O ALA A 90 10185 6918 9961 -1808 -3038 1247 O
ATOM 1338 CB ALA A 90 38.350 172.621 147.263 1.00 66.94 C
ANISOU 1338 CB ALA A 90 9279 6445 9712 -1575 -2956 1295 C
ATOM 1339 N ALA A 91 36.596 175.437 146.694 1.00 63.85 N
ANISOU 1339 N ALA A 91 9404 6164 8691 -1543 -2526 967 N
ATOM 1340 CA ALA A 91 36.535 176.734 146.014 1.00 62.84 C
ANISOU 1340 CA ALA A 91 9302 6060 8516 -1522 -2379 897 C
ATOM 1341 C ALA A 91 35.702 177.757 146.793 1.00 68.65 C
ANISOU 1341 C ALA A 91 10435 6748 8900 -1609 -2356 801 C
ATOM 1342 O ALA A 91 35.410 178.842 146.273 1.00 69.05 O
ANISOU 1342 O ALA A 91 10545 6815 8876 -1575 -2205 725 O
ATOM 1343 CB ALA A 91 35.983 176.564 144.613 1.00 61.20 C
ANISOU 1343 CB ALA A 91 8902 5973 8379 -1318 -2057 796 C
ATOM 1344 N LEU A 92 35.321 177.420 148.039 1.00 65.71 N
ANISOU 1344 N LEU A 92 10350 6301 8315 -1728 -2492 806 N
ATOM 1345 CA LEU A 92 34.507 178.277 148.912 1.00 66.00 C
ANISOU 1345 CA LEU A 92 10807 6257 8010 -1827 -2438 709 C
ATOM 1346 C LEU A 92 33.161 178.673 148.272 1.00 71.10 C
ANISOU 1346 C LEU A 92 11504 6979 8533 -1648 -2074 541 C
ATOM 1347 O LEU A 92 32.671 179.788 148.460 1.00 71.11 O
ANISOU 1347 O LEU A 92 11729 6920 8368 -1679 -1961 461 O
ATOM 1348 CB LEU A 92 35.279 179.511 149.422 1.00 66.91 C
ANISOU 1348 CB LEU A 92 11111 6252 8059 -2027 -2634 766 C
ATOM 1349 CG LEU A 92 36.681 179.309 149.994 1.00 72.20 C
ANISOU 1349 CG LEU A 92 11712 6829 8892 -2226 -3036 959 C
ATOM 1350 CD1 LEU A 92 37.284 180.631 150.383 1.00 72.01 C
ANISOU 1350 CD1 LEU A 92 11889 6690 8781 -2418 -3196 998 C
ATOM 1351 CD2 LEU A 92 36.679 178.329 151.192 1.00 74.99 C
ANISOU 1351 CD2 LEU A 92 12265 7101 9128 -2366 -3267 1033 C
ATOM 1352 N PHE A 93 32.581 177.729 147.510 1.00 67.41 N
ANISOU 1352 N PHE A 93 10817 6629 8168 -1465 -1904 501 N
ATOM 1353 CA PHE A 93 31.284 177.786 146.849 1.00 66.78 C
ANISOU 1353 CA PHE A 93 10725 6624 8025 -1290 -1600 374 C
ATOM 1354 C PHE A 93 31.197 178.848 145.743 1.00 73.92 C
ANISOU 1354 C PHE A 93 11517 7568 8999 -1201 -1452 333 C
ATOM 1355 O PHE A 93 30.084 179.187 145.324 1.00 74.77 O
ANISOU 1355 O PHE A 93 11664 7701 9044 -1087 -1232 241 O
ATOM 1356 CB PHE A 93 30.139 177.916 147.883 1.00 69.15 C
ANISOU 1356 CB PHE A 93 11366 6843 8066 -1329 -1480 280 C
ATOM 1357 CG PHE A 93 30.246 176.924 149.025 1.00 72.33 C
ANISOU 1357 CG PHE A 93 11928 7189 8364 -1446 -1634 324 C
ATOM 1358 CD1 PHE A 93 30.172 175.551 148.789 1.00 74.69 C
ANISOU 1358 CD1 PHE A 93 12030 7572 8775 -1360 -1653 358 C
ATOM 1359 CD2 PHE A 93 30.431 177.359 150.331 1.00 75.64 C
ANISOU 1359 CD2 PHE A 93 12720 7458 8561 -1656 -1768 335 C
ATOM 1360 CE1 PHE A 93 30.273 174.637 149.847 1.00 76.88 C
ANISOU 1360 CE1 PHE A 93 12464 7789 8956 -1475 -1810 407 C
ATOM 1361 CE2 PHE A 93 30.534 176.445 151.382 1.00 79.65 C
ANISOU 1361 CE2 PHE A 93 13408 7902 8955 -1785 -1931 386 C
ATOM 1362 CZ PHE A 93 30.451 175.093 151.137 1.00 77.21 C
ANISOU 1362 CZ PHE A 93 12883 7682 8771 -1690 -1955 424 C
ATOM 1363 N GLU A 94 32.360 179.313 145.219 1.00 70.83 N
ANISOU 1363 N GLU A 94 10966 7178 8767 -1251 -1573 412 N
ATOM 1364 CA GLU A 94 32.425 180.261 144.097 1.00 69.33 C
ANISOU 1364 CA GLU A 94 10664 7025 8655 -1181 -1448 387 C
ATOM 1365 C GLU A 94 32.413 179.429 142.801 1.00 71.87 C
ANISOU 1365 C GLU A 94 10692 7463 9155 -1034 -1324 391 C
ATOM 1366 O GLU A 94 33.479 179.037 142.324 1.00 71.23 O
ANISOU 1366 O GLU A 94 10393 7397 9274 -1052 -1398 470 O
ATOM 1367 CB GLU A 94 33.697 181.144 144.169 1.00 71.47 C
ANISOU 1367 CB GLU A 94 10916 7229 9012 -1321 -1624 471 C
ATOM 1368 CG GLU A 94 33.678 182.238 145.231 1.00 78.81 C
ANISOU 1368 CG GLU A 94 12173 8031 9740 -1476 -1720 455 C
ATOM 1369 CD GLU A 94 32.722 183.415 145.094 1.00 84.71 C
ANISOU 1369 CD GLU A 94 13120 8737 10328 -1430 -1522 346 C
ATOM 1370 OE1 GLU A 94 32.201 183.682 143.985 1.00 70.80 O
ANISOU 1370 OE1 GLU A 94 11217 7048 8636 -1285 -1338 301 O
ATOM 1371 OE2 GLU A 94 32.497 184.080 146.127 1.00 77.40 O
ANISOU 1371 OE2 GLU A 94 12513 7690 9207 -1551 -1556 311 O
ATOM 1372 N TRP A 95 31.203 179.141 142.255 1.00 68.04 N
ANISOU 1372 N TRP A 95 10207 7040 8605 -900 -1132 310 N
ATOM 1373 CA TRP A 95 30.992 178.319 141.056 1.00 68.00 C
ANISOU 1373 CA TRP A 95 9993 7131 8713 -777 -1007 301 C
ATOM 1374 C TRP A 95 31.882 178.684 139.864 1.00 72.58 C
ANISOU 1374 C TRP A 95 10399 7733 9446 -774 -969 338 C
ATOM 1375 O TRP A 95 32.384 177.769 139.206 1.00 73.01 O
ANISOU 1375 O TRP A 95 10270 7826 9643 -736 -929 367 O
ATOM 1376 CB TRP A 95 29.514 178.286 140.629 1.00 66.38 C
ANISOU 1376 CB TRP A 95 9848 6965 8409 -663 -839 223 C
ATOM 1377 CG TRP A 95 28.730 177.211 141.310 1.00 67.86 C
ANISOU 1377 CG TRP A 95 10079 7170 8536 -626 -823 197 C
ATOM 1378 CD1 TRP A 95 28.173 177.271 142.551 1.00 71.65 C
ANISOU 1378 CD1 TRP A 95 10756 7585 8884 -672 -842 166 C
ATOM 1379 CD2 TRP A 95 28.503 175.876 140.833 1.00 67.10 C
ANISOU 1379 CD2 TRP A 95 9842 7147 8504 -553 -783 200 C
ATOM 1380 NE1 TRP A 95 27.595 176.058 142.872 1.00 70.60 N
ANISOU 1380 NE1 TRP A 95 10604 7487 8734 -629 -817 154 N
ATOM 1381 CE2 TRP A 95 27.782 175.186 141.836 1.00 70.47 C
ANISOU 1381 CE2 TRP A 95 10376 7559 8840 -552 -790 176 C
ATOM 1382 CE3 TRP A 95 28.838 175.195 139.656 1.00 68.22 C
ANISOU 1382 CE3 TRP A 95 9805 7354 8763 -497 -726 217 C
ATOM 1383 CZ2 TRP A 95 27.393 173.856 141.702 1.00 68.81 C
ANISOU 1383 CZ2 TRP A 95 10079 7404 8660 -493 -761 173 C
ATOM 1384 CZ3 TRP A 95 28.459 173.864 139.532 1.00 69.39 C
ANISOU 1384 CZ3 TRP A 95 9882 7549 8935 -441 -692 210 C
ATOM 1385 CH2 TRP A 95 27.732 173.216 140.542 1.00 69.47 C
ANISOU 1385 CH2 TRP A 95 9982 7552 8862 -435 -718 191 C
ATOM 1386 N HIS A 96 32.097 179.998 139.595 1.00 67.68 N
ANISOU 1386 N HIS A 96 9845 7073 8798 -818 -962 336 N
ATOM 1387 CA HIS A 96 32.935 180.468 138.476 1.00 67.23 C
ANISOU 1387 CA HIS A 96 9653 7023 8871 -832 -908 369 C
ATOM 1388 C HIS A 96 34.391 179.954 138.547 1.00 72.86 C
ANISOU 1388 C HIS A 96 10173 7708 9805 -902 -1004 459 C
ATOM 1389 O HIS A 96 35.034 179.815 137.501 1.00 73.56 O
ANISOU 1389 O HIS A 96 10100 7804 10044 -887 -896 480 O
ATOM 1390 CB HIS A 96 32.887 182.005 138.330 1.00 67.61 C
ANISOU 1390 CB HIS A 96 9828 7020 8839 -878 -904 354 C
ATOM 1391 CG HIS A 96 33.551 182.730 139.458 1.00 72.02 C
ANISOU 1391 CG HIS A 96 10496 7493 9374 -1007 -1074 393 C
ATOM 1392 ND1 HIS A 96 32.920 182.905 140.678 1.00 73.92 N
ANISOU 1392 ND1 HIS A 96 10954 7680 9452 -1045 -1141 359 N
ATOM 1393 CD2 HIS A 96 34.795 183.258 139.531 1.00 74.95 C
ANISOU 1393 CD2 HIS A 96 10797 7813 9866 -1119 -1189 468 C
ATOM 1394 CE1 HIS A 96 33.796 183.533 141.443 1.00 74.80 C
ANISOU 1394 CE1 HIS A 96 11149 7709 9565 -1190 -1309 413 C
ATOM 1395 NE2 HIS A 96 34.935 183.772 140.796 1.00 75.77 N
ANISOU 1395 NE2 HIS A 96 11089 7834 9868 -1238 -1358 486 N
ATOM 1396 N ALA A 97 34.899 179.674 139.778 1.00 69.14 N
ANISOU 1396 N ALA A 97 9724 7184 9361 -989 -1202 518 N
ATOM 1397 CA ALA A 97 36.252 179.168 140.020 1.00 70.02 C
ANISOU 1397 CA ALA A 97 9636 7244 9723 -1064 -1343 632 C
ATOM 1398 C ALA A 97 36.379 177.740 139.493 1.00 75.73 C
ANISOU 1398 C ALA A 97 10153 8006 10614 -971 -1244 644 C
ATOM 1399 O ALA A 97 37.416 177.391 138.927 1.00 78.07 O
ANISOU 1399 O ALA A 97 10217 8268 11180 -976 -1203 712 O
ATOM 1400 CB ALA A 97 36.566 179.200 141.504 1.00 71.57 C
ANISOU 1400 CB ALA A 97 9960 7365 9868 -1194 -1612 699 C
ATOM 1401 N VAL A 98 35.319 176.925 139.670 1.00 69.78 N
ANISOU 1401 N VAL A 98 9486 7310 9716 -888 -1185 578 N
ATOM 1402 CA VAL A 98 35.254 175.539 139.208 1.00 68.53 C
ANISOU 1402 CA VAL A 98 9177 7187 9673 -797 -1083 574 C
ATOM 1403 C VAL A 98 34.872 175.535 137.710 1.00 73.46 C
ANISOU 1403 C VAL A 98 9761 7864 10285 -709 -824 501 C
ATOM 1404 O VAL A 98 35.672 175.095 136.880 1.00 73.99 O
ANISOU 1404 O VAL A 98 9650 7904 10559 -694 -702 528 O
ATOM 1405 CB VAL A 98 34.283 174.710 140.083 1.00 70.20 C
ANISOU 1405 CB VAL A 98 9519 7431 9724 -765 -1144 540 C
ATOM 1406 CG1 VAL A 98 34.339 173.227 139.727 1.00 69.03 C
ANISOU 1406 CG1 VAL A 98 9212 7303 9712 -686 -1069 550 C
ATOM 1407 CG2 VAL A 98 34.560 174.931 141.570 1.00 70.80 C
ANISOU 1407 CG2 VAL A 98 9725 7437 9737 -886 -1398 603 C
ATOM 1408 N ASP A 99 33.676 176.064 137.369 1.00 69.76 N
ANISOU 1408 N ASP A 99 9467 7451 9588 -664 -740 417 N
ATOM 1409 CA ASP A 99 33.201 176.160 135.989 1.00 69.60 C
ANISOU 1409 CA ASP A 99 9461 7468 9514 -609 -543 361 C
ATOM 1410 C ASP A 99 32.428 177.471 135.772 1.00 72.60 C
ANISOU 1410 C ASP A 99 10008 7857 9718 -617 -537 322 C
ATOM 1411 O ASP A 99 31.335 177.615 136.324 1.00 71.27 O
ANISOU 1411 O ASP A 99 9967 7709 9403 -582 -575 285 O
ATOM 1412 CB ASP A 99 32.340 174.925 135.606 1.00 71.03 C
ANISOU 1412 CB ASP A 99 9648 7702 9638 -527 -448 314 C
ATOM 1413 CG ASP A 99 31.659 174.971 134.231 1.00 80.57 C
ANISOU 1413 CG ASP A 99 10928 8939 10744 -496 -287 263 C
ATOM 1414 OD1 ASP A 99 30.413 175.163 134.184 1.00 80.33 O
ANISOU 1414 OD1 ASP A 99 11021 8948 10553 -460 -302 228 O
ATOM 1415 OD2 ASP A 99 32.362 174.780 133.210 1.00 84.79 O
ANISOU 1415 OD2 ASP A 99 11403 9443 11369 -516 -144 264 O
ATOM 1416 N PRO A 100 32.941 178.441 134.973 1.00 69.74 N
ANISOU 1416 N PRO A 100 9648 7467 9384 -660 -475 332 N
ATOM 1417 CA PRO A 100 32.154 179.667 134.728 1.00 68.55 C
ANISOU 1417 CA PRO A 100 9653 7313 9081 -662 -474 303 C
ATOM 1418 C PRO A 100 30.970 179.310 133.834 1.00 68.84 C
ANISOU 1418 C PRO A 100 9759 7393 9006 -594 -378 262 C
ATOM 1419 O PRO A 100 31.086 178.439 132.972 1.00 70.02 O
ANISOU 1419 O PRO A 100 9856 7562 9186 -581 -275 254 O
ATOM 1420 CB PRO A 100 33.159 180.633 134.067 1.00 71.19 C
ANISOU 1420 CB PRO A 100 9956 7600 9492 -737 -436 335 C
ATOM 1421 CG PRO A 100 34.517 179.970 134.222 1.00 76.94 C
ANISOU 1421 CG PRO A 100 10494 8298 10444 -780 -437 389 C
ATOM 1422 CD PRO A 100 34.218 178.488 134.236 1.00 72.30 C
ANISOU 1422 CD PRO A 100 9832 7747 9891 -711 -388 372 C
ATOM 1423 N GLY A 101 29.824 179.894 134.131 1.00 62.72 N
ANISOU 1423 N GLY A 101 9099 6616 8117 -556 -417 242 N
ATOM 1424 CA GLY A 101 28.584 179.614 133.427 1.00 62.25 C
ANISOU 1424 CA GLY A 101 9092 6583 7979 -499 -375 226 C
ATOM 1425 C GLY A 101 27.654 178.667 134.156 1.00 67.92 C
ANISOU 1425 C GLY A 101 9799 7333 8674 -432 -396 204 C
ATOM 1426 O GLY A 101 27.736 178.503 135.378 1.00 68.52 O
ANISOU 1426 O GLY A 101 9880 7400 8756 -428 -448 193 O
ATOM 1427 N CYS A 102 26.803 177.989 133.395 1.00 65.09 N
ANISOU 1427 N CYS A 102 9443 7005 8282 -395 -362 203 N
ATOM 1428 CA CYS A 102 25.773 177.142 133.959 1.00 65.19 C
ANISOU 1428 CA CYS A 102 9444 7045 8281 -332 -375 188 C
ATOM 1429 C CYS A 102 25.830 175.624 133.636 1.00 63.64 C
ANISOU 1429 C CYS A 102 9189 6899 8093 -321 -339 177 C
ATOM 1430 O CYS A 102 25.040 174.877 134.220 1.00 61.95 O
ANISOU 1430 O CYS A 102 8960 6707 7871 -274 -353 165 O
ATOM 1431 CB CYS A 102 24.423 177.727 133.571 1.00 67.55 C
ANISOU 1431 CB CYS A 102 9790 7314 8561 -294 -392 210 C
ATOM 1432 SG CYS A 102 23.765 178.857 134.807 1.00 73.20 S
ANISOU 1432 SG CYS A 102 10556 7955 9301 -252 -396 197 S
ATOM 1433 N ARG A 103 26.756 175.181 132.756 1.00 57.71 N
ANISOU 1433 N ARG A 103 8411 6152 7365 -365 -273 179 N
ATOM 1434 CA ARG A 103 26.897 173.804 132.282 1.00 56.31 C
ANISOU 1434 CA ARG A 103 8198 5997 7199 -361 -206 164 C
ATOM 1435 C ARG A 103 27.111 172.783 133.398 1.00 60.13 C
ANISOU 1435 C ARG A 103 8594 6503 7749 -321 -234 153 C
ATOM 1436 O ARG A 103 26.396 171.780 133.430 1.00 59.99 O
ANISOU 1436 O ARG A 103 8578 6514 7702 -287 -230 140 O
ATOM 1437 CB ARG A 103 27.995 173.683 131.206 1.00 56.47 C
ANISOU 1437 CB ARG A 103 8217 5982 7255 -423 -82 160 C
ATOM 1438 CG ARG A 103 27.670 174.409 129.889 1.00 75.62 C
ANISOU 1438 CG ARG A 103 10781 8378 9572 -486 -45 170 C
ATOM 1439 CD ARG A 103 28.725 174.216 128.799 1.00 96.33 C
ANISOU 1439 CD ARG A 103 13440 10946 12214 -562 125 154 C
ATOM 1440 NE ARG A 103 28.903 172.805 128.430 1.00111.82 N
ANISOU 1440 NE ARG A 103 15395 12896 14195 -561 246 121 N
ATOM 1441 CZ ARG A 103 29.397 172.379 127.269 1.00124.70 C
ANISOU 1441 CZ ARG A 103 17128 14461 15792 -635 429 94 C
ATOM 1442 NH1 ARG A 103 29.756 173.249 126.332 1.00111.53 N
ANISOU 1442 NH1 ARG A 103 15582 12736 14056 -724 507 99 N
ATOM 1443 NH2 ARG A 103 29.523 171.078 127.032 1.00107.56 N
ANISOU 1443 NH2 ARG A 103 14957 12265 13645 -628 549 59 N
ATOM 1444 N LEU A 104 28.091 173.016 134.296 1.00 55.53 N
ANISOU 1444 N LEU A 104 7944 5900 7256 -337 -280 169 N
ATOM 1445 CA LEU A 104 28.391 172.089 135.390 1.00 54.37 C
ANISOU 1445 CA LEU A 104 7729 5756 7173 -320 -341 178 C
ATOM 1446 C LEU A 104 27.227 171.921 136.332 1.00 57.82 C
ANISOU 1446 C LEU A 104 8241 6216 7514 -284 -403 160 C
ATOM 1447 O LEU A 104 26.952 170.792 136.745 1.00 57.98 O
ANISOU 1447 O LEU A 104 8236 6255 7539 -257 -409 154 O
ATOM 1448 CB LEU A 104 29.661 172.476 136.150 1.00 55.03 C
ANISOU 1448 CB LEU A 104 7740 5794 7376 -371 -423 223 C
ATOM 1449 CG LEU A 104 30.154 171.482 137.199 1.00 60.14 C
ANISOU 1449 CG LEU A 104 8313 6424 8114 -375 -519 259 C
ATOM 1450 CD1 LEU A 104 30.499 170.116 136.580 1.00 59.94 C
ANISOU 1450 CD1 LEU A 104 8169 6396 8209 -336 -422 261 C
ATOM 1451 CD2 LEU A 104 31.331 172.037 137.933 1.00 65.31 C
ANISOU 1451 CD2 LEU A 104 8913 7019 8884 -449 -650 325 C
ATOM 1452 N CYS A 105 26.522 173.023 136.638 1.00 54.04 N
ANISOU 1452 N CYS A 105 7854 5722 6959 -283 -426 150 N
ATOM 1453 CA CYS A 105 25.335 172.988 137.465 1.00 54.08 C
ANISOU 1453 CA CYS A 105 7931 5722 6894 -248 -434 128 C
ATOM 1454 C CYS A 105 24.266 172.075 136.893 1.00 54.26 C
ANISOU 1454 C CYS A 105 7927 5784 6903 -195 -386 118 C
ATOM 1455 O CYS A 105 23.708 171.266 137.626 1.00 53.34 O
ANISOU 1455 O CYS A 105 7817 5678 6771 -172 -387 106 O
ATOM 1456 CB CYS A 105 24.775 174.380 137.700 1.00 56.60 C
ANISOU 1456 CB CYS A 105 8340 5992 7174 -247 -424 119 C
ATOM 1457 SG CYS A 105 23.331 174.378 138.791 1.00 62.11 S
ANISOU 1457 SG CYS A 105 9124 6647 7827 -203 -373 87 S
ATOM 1458 N ARG A 106 23.964 172.212 135.590 1.00 50.64 N
ANISOU 1458 N ARG A 106 7459 5340 6442 -193 -354 131 N
ATOM 1459 CA ARG A 106 22.951 171.388 134.922 1.00 49.30 C
ANISOU 1459 CA ARG A 106 7282 5197 6254 -169 -340 137 C
ATOM 1460 C ARG A 106 23.369 169.961 134.829 1.00 50.96 C
ANISOU 1460 C ARG A 106 7452 5438 6471 -171 -314 122 C
ATOM 1461 O ARG A 106 22.526 169.086 135.002 1.00 51.88 O
ANISOU 1461 O ARG A 106 7562 5575 6575 -146 -317 119 O
ATOM 1462 CB ARG A 106 22.543 171.948 133.566 1.00 47.03 C
ANISOU 1462 CB ARG A 106 7034 4895 5939 -198 -347 168 C
ATOM 1463 CG ARG A 106 21.536 173.071 133.693 1.00 50.72 C
ANISOU 1463 CG ARG A 106 7517 5320 6433 -171 -387 199 C
ATOM 1464 CD ARG A 106 21.046 173.557 132.352 1.00 60.60 C
ANISOU 1464 CD ARG A 106 8813 6545 7666 -212 -438 253 C
ATOM 1465 NE ARG A 106 22.156 174.145 131.616 1.00 76.02 N
ANISOU 1465 NE ARG A 106 10826 8490 9569 -275 -414 248 N
ATOM 1466 CZ ARG A 106 22.380 175.448 131.508 1.00 84.87 C
ANISOU 1466 CZ ARG A 106 11979 9569 10700 -289 -431 267 C
ATOM 1467 NH1 ARG A 106 21.511 176.324 132.007 1.00 61.78 N
ANISOU 1467 NH1 ARG A 106 9036 6598 7841 -240 -471 295 N
ATOM 1468 NH2 ARG A 106 23.454 175.888 130.867 1.00 69.22 N
ANISOU 1468 NH2 ARG A 106 10047 7577 8677 -352 -392 260 N
ATOM 1469 N PHE A 107 24.675 169.704 134.630 1.00 45.64 N
ANISOU 1469 N PHE A 107 6740 4757 5844 -199 -281 118 N
ATOM 1470 CA PHE A 107 25.197 168.337 134.595 1.00 44.60 C
ANISOU 1470 CA PHE A 107 6555 4632 5761 -194 -240 108 C
ATOM 1471 C PHE A 107 24.965 167.716 136.004 1.00 51.78 C
ANISOU 1471 C PHE A 107 7438 5551 6684 -164 -307 109 C
ATOM 1472 O PHE A 107 24.401 166.629 136.106 1.00 51.25 O
ANISOU 1472 O PHE A 107 7368 5503 6602 -141 -297 99 O
ATOM 1473 CB PHE A 107 26.686 168.320 134.169 1.00 45.33 C
ANISOU 1473 CB PHE A 107 6580 4683 5959 -224 -173 116 C
ATOM 1474 CG PHE A 107 27.405 167.020 134.468 1.00 44.91 C
ANISOU 1474 CG PHE A 107 6434 4609 6022 -206 -137 120 C
ATOM 1475 CD1 PHE A 107 27.254 165.913 133.632 1.00 46.97 C
ANISOU 1475 CD1 PHE A 107 6715 4857 6276 -202 -26 93 C
ATOM 1476 CD2 PHE A 107 28.174 166.882 135.616 1.00 45.14 C
ANISOU 1476 CD2 PHE A 107 6370 4614 6165 -203 -229 158 C
ATOM 1477 CE1 PHE A 107 27.884 164.701 133.927 1.00 48.04 C
ANISOU 1477 CE1 PHE A 107 6758 4956 6540 -177 17 99 C
ATOM 1478 CE2 PHE A 107 28.789 165.665 135.925 1.00 49.19 C
ANISOU 1478 CE2 PHE A 107 6785 5093 6814 -184 -218 179 C
ATOM 1479 CZ PHE A 107 28.647 164.581 135.075 1.00 47.73 C
ANISOU 1479 CZ PHE A 107 6599 4894 6642 -162 -83 147 C
ATOM 1480 N MET A 108 25.341 168.458 137.067 1.00 51.19 N
ANISOU 1480 N MET A 108 7377 5454 6618 -180 -378 122 N
ATOM 1481 CA MET A 108 25.180 168.103 138.481 1.00 52.57 C
ANISOU 1481 CA MET A 108 7588 5616 6772 -185 -451 126 C
ATOM 1482 C MET A 108 23.723 167.715 138.765 1.00 54.56 C
ANISOU 1482 C MET A 108 7895 5888 6947 -147 -415 99 C
ATOM 1483 O MET A 108 23.498 166.637 139.291 1.00 55.47 O
ANISOU 1483 O MET A 108 8007 6012 7057 -138 -426 97 O
ATOM 1484 CB MET A 108 25.716 169.253 139.395 1.00 56.67 C
ANISOU 1484 CB MET A 108 8173 6087 7270 -237 -528 140 C
ATOM 1485 CG MET A 108 25.629 169.032 140.923 1.00 63.12 C
ANISOU 1485 CG MET A 108 9095 6864 8023 -281 -611 145 C
ATOM 1486 SD MET A 108 26.551 167.618 141.572 1.00 71.13 S
ANISOU 1486 SD MET A 108 10042 7861 9122 -314 -727 200 S
ATOM 1487 CE MET A 108 26.315 167.832 143.333 1.00 67.87 C
ANISOU 1487 CE MET A 108 9842 7379 8566 -406 -836 206 C
ATOM 1488 N GLY A 109 22.762 168.532 138.334 1.00 48.54 N
ANISOU 1488 N GLY A 109 7164 5125 6153 -125 -373 89 N
ATOM 1489 CA GLY A 109 21.338 168.283 138.535 1.00 46.93 C
ANISOU 1489 CA GLY A 109 6978 4922 5932 -88 -331 80 C
ATOM 1490 C GLY A 109 20.849 166.989 137.917 1.00 49.17 C
ANISOU 1490 C GLY A 109 7210 5247 6225 -71 -322 85 C
ATOM 1491 O GLY A 109 20.242 166.173 138.608 1.00 48.38 O
ANISOU 1491 O GLY A 109 7117 5149 6115 -57 -308 76 O
ATOM 1492 N VAL A 110 21.145 166.769 136.621 1.00 46.22 N
ANISOU 1492 N VAL A 110 6810 4895 5857 -85 -321 97 N
ATOM 1493 CA VAL A 110 20.795 165.544 135.866 1.00 45.86 C
ANISOU 1493 CA VAL A 110 6753 4873 5799 -91 -309 98 C
ATOM 1494 C VAL A 110 21.286 164.297 136.614 1.00 50.31 C
ANISOU 1494 C VAL A 110 7293 5445 6377 -81 -302 81 C
ATOM 1495 O VAL A 110 20.521 163.352 136.892 1.00 50.11 O
ANISOU 1495 O VAL A 110 7268 5433 6340 -69 -301 79 O
ATOM 1496 CB VAL A 110 21.366 165.611 134.415 1.00 49.19 C
ANISOU 1496 CB VAL A 110 7206 5288 6198 -135 -283 102 C
ATOM 1497 CG1 VAL A 110 21.213 164.285 133.682 1.00 48.40 C
ANISOU 1497 CG1 VAL A 110 7135 5191 6065 -160 -250 92 C
ATOM 1498 CG2 VAL A 110 20.708 166.739 133.621 1.00 49.14 C
ANISOU 1498 CG2 VAL A 110 7239 5265 6167 -159 -322 135 C
ATOM 1499 N VAL A 111 22.559 164.354 136.997 1.00 47.42 N
ANISOU 1499 N VAL A 111 6902 5061 6055 -90 -310 81 N
ATOM 1500 CA VAL A 111 23.314 163.292 137.665 1.00 46.76 C
ANISOU 1500 CA VAL A 111 6777 4962 6026 -88 -329 88 C
ATOM 1501 C VAL A 111 22.839 163.099 139.125 1.00 51.35 C
ANISOU 1501 C VAL A 111 7406 5538 6568 -90 -391 92 C
ATOM 1502 O VAL A 111 22.868 161.975 139.610 1.00 53.91 O
ANISOU 1502 O VAL A 111 7723 5857 6906 -87 -411 99 O
ATOM 1503 CB VAL A 111 24.818 163.603 137.459 1.00 50.09 C
ANISOU 1503 CB VAL A 111 7132 5347 6554 -106 -329 109 C
ATOM 1504 CG1 VAL A 111 25.565 163.984 138.715 1.00 49.81 C
ANISOU 1504 CG1 VAL A 111 7085 5279 6563 -133 -439 145 C
ATOM 1505 CG2 VAL A 111 25.509 162.525 136.670 1.00 49.85 C
ANISOU 1505 CG2 VAL A 111 7037 5287 6618 -97 -246 106 C
ATOM 1506 N MET A 112 22.292 164.142 139.766 1.00 46.57 N
ANISOU 1506 N MET A 112 6870 4921 5906 -99 -400 84 N
ATOM 1507 CA MET A 112 21.720 164.058 141.111 1.00 46.49 C
ANISOU 1507 CA MET A 112 6953 4882 5830 -118 -412 76 C
ATOM 1508 C MET A 112 20.400 163.259 141.068 1.00 51.28 C
ANISOU 1508 C MET A 112 7557 5510 6419 -86 -346 60 C
ATOM 1509 O MET A 112 20.133 162.452 141.971 1.00 50.44 O
ANISOU 1509 O MET A 112 7503 5387 6275 -103 -351 57 O
ATOM 1510 CB MET A 112 21.439 165.468 141.675 1.00 49.09 C
ANISOU 1510 CB MET A 112 7373 5168 6110 -138 -390 60 C
ATOM 1511 CG MET A 112 22.659 166.162 142.223 1.00 53.87 C
ANISOU 1511 CG MET A 112 8029 5734 6706 -199 -481 81 C
ATOM 1512 SD MET A 112 23.432 165.273 143.584 1.00 59.72 S
ANISOU 1512 SD MET A 112 8855 6427 7411 -278 -612 117 S
ATOM 1513 CE MET A 112 22.460 165.854 144.933 1.00 57.58 C
ANISOU 1513 CE MET A 112 8817 6081 6979 -334 -545 73 C
ATOM 1514 N ILE A 113 19.553 163.534 140.037 1.00 48.23 N
ANISOU 1514 N ILE A 113 7116 5147 6062 -54 -299 60 N
ATOM 1515 CA ILE A 113 18.257 162.869 139.828 1.00 47.39 C
ANISOU 1515 CA ILE A 113 6981 5053 5974 -33 -258 64 C
ATOM 1516 C ILE A 113 18.541 161.405 139.458 1.00 52.64 C
ANISOU 1516 C ILE A 113 7620 5749 6632 -40 -284 67 C
ATOM 1517 O ILE A 113 17.988 160.502 140.075 1.00 51.32 O
ANISOU 1517 O ILE A 113 7468 5579 6453 -41 -270 63 O
ATOM 1518 CB ILE A 113 17.405 163.606 138.738 1.00 49.15 C
ANISOU 1518 CB ILE A 113 7148 5276 6250 -17 -253 92 C
ATOM 1519 CG1 ILE A 113 17.093 165.098 139.118 1.00 48.52 C
ANISOU 1519 CG1 ILE A 113 7083 5145 6207 0 -213 93 C
ATOM 1520 CG2 ILE A 113 16.133 162.834 138.358 1.00 48.71 C
ANISOU 1520 CG2 ILE A 113 7039 5226 6242 -12 -253 120 C
ATOM 1521 CD1 ILE A 113 16.212 165.357 140.302 1.00 49.85 C
ANISOU 1521 CD1 ILE A 113 7285 5252 6404 18 -113 75 C
ATOM 1522 N PHE A 114 19.432 161.189 138.463 1.00 49.57 N
ANISOU 1522 N PHE A 114 7205 5374 6256 -48 -303 69 N
ATOM 1523 CA PHE A 114 19.832 159.871 137.999 1.00 48.11 C
ANISOU 1523 CA PHE A 114 7007 5195 6080 -53 -296 64 C
ATOM 1524 C PHE A 114 20.254 158.963 139.173 1.00 54.57 C
ANISOU 1524 C PHE A 114 7829 5994 6909 -50 -323 67 C
ATOM 1525 O PHE A 114 19.667 157.894 139.351 1.00 53.76 O
ANISOU 1525 O PHE A 114 7737 5896 6794 -50 -316 65 O
ATOM 1526 CB PHE A 114 20.947 159.998 136.960 1.00 49.01 C
ANISOU 1526 CB PHE A 114 7104 5293 6224 -65 -265 59 C
ATOM 1527 CG PHE A 114 21.460 158.663 136.506 1.00 50.84 C
ANISOU 1527 CG PHE A 114 7330 5501 6488 -68 -218 47 C
ATOM 1528 CD1 PHE A 114 20.795 157.943 135.518 1.00 53.18 C
ANISOU 1528 CD1 PHE A 114 7682 5796 6729 -95 -180 34 C
ATOM 1529 CD2 PHE A 114 22.573 158.088 137.106 1.00 53.50 C
ANISOU 1529 CD2 PHE A 114 7608 5799 6921 -49 -220 59 C
ATOM 1530 CE1 PHE A 114 21.238 156.686 135.137 1.00 53.71 C
ANISOU 1530 CE1 PHE A 114 7765 5822 6820 -100 -114 15 C
ATOM 1531 CE2 PHE A 114 23.004 156.814 136.730 1.00 55.87 C
ANISOU 1531 CE2 PHE A 114 7891 6055 7282 -41 -158 50 C
ATOM 1532 CZ PHE A 114 22.332 156.125 135.751 1.00 53.38 C
ANISOU 1532 CZ PHE A 114 7649 5738 6895 -64 -89 20 C
ATOM 1533 N PHE A 115 21.237 159.416 139.990 1.00 52.34 N
ANISOU 1533 N PHE A 115 7552 5684 6651 -62 -374 82 N
ATOM 1534 CA PHE A 115 21.775 158.673 141.143 1.00 51.59 C
ANISOU 1534 CA PHE A 115 7480 5553 6569 -82 -446 107 C
ATOM 1535 C PHE A 115 20.890 158.761 142.413 1.00 57.47 C
ANISOU 1535 C PHE A 115 8339 6285 7214 -112 -456 99 C
ATOM 1536 O PHE A 115 21.230 158.205 143.459 1.00 59.20 O
ANISOU 1536 O PHE A 115 8622 6463 7408 -152 -528 124 O
ATOM 1537 CB PHE A 115 23.223 159.104 141.428 1.00 52.89 C
ANISOU 1537 CB PHE A 115 7602 5674 6819 -104 -529 147 C
ATOM 1538 CG PHE A 115 24.216 158.787 140.325 1.00 53.50 C
ANISOU 1538 CG PHE A 115 7559 5734 7033 -76 -482 158 C
ATOM 1539 CD1 PHE A 115 24.511 157.467 139.986 1.00 54.30 C
ANISOU 1539 CD1 PHE A 115 7603 5805 7223 -51 -448 166 C
ATOM 1540 CD2 PHE A 115 24.891 159.809 139.656 1.00 54.87 C
ANISOU 1540 CD2 PHE A 115 7688 5903 7257 -79 -453 157 C
ATOM 1541 CE1 PHE A 115 25.445 157.174 138.987 1.00 55.46 C
ANISOU 1541 CE1 PHE A 115 7652 5907 7512 -28 -357 167 C
ATOM 1542 CE2 PHE A 115 25.837 159.516 138.663 1.00 57.71 C
ANISOU 1542 CE2 PHE A 115 7949 6225 7752 -61 -369 162 C
ATOM 1543 CZ PHE A 115 26.097 158.198 138.326 1.00 56.52 C
ANISOU 1543 CZ PHE A 115 7747 6034 7694 -35 -308 163 C
ATOM 1544 N GLY A 116 19.766 159.444 142.303 1.00 53.69 N
ANISOU 1544 N GLY A 116 7887 5821 6690 -100 -376 71 N
ATOM 1545 CA GLY A 116 18.806 159.567 143.386 1.00 54.55 C
ANISOU 1545 CA GLY A 116 8102 5898 6729 -124 -320 54 C
ATOM 1546 C GLY A 116 17.679 158.582 143.159 1.00 60.62 C
ANISOU 1546 C GLY A 116 8833 6687 7512 -103 -258 48 C
ATOM 1547 O GLY A 116 17.299 157.815 144.050 1.00 60.84 O
ANISOU 1547 O GLY A 116 8935 6689 7493 -132 -239 45 O
ATOM 1548 N LEU A 117 17.193 158.551 141.932 1.00 57.32 N
ANISOU 1548 N LEU A 117 8313 6311 7154 -67 -240 53 N
ATOM 1549 CA LEU A 117 16.131 157.667 141.553 1.00 58.00 C
ANISOU 1549 CA LEU A 117 8356 6413 7268 -61 -209 61 C
ATOM 1550 C LEU A 117 16.604 156.220 141.306 1.00 61.53 C
ANISOU 1550 C LEU A 117 8800 6876 7702 -70 -255 65 C
ATOM 1551 O LEU A 117 15.908 155.289 141.719 1.00 62.19 O
ANISOU 1551 O LEU A 117 8902 6953 7775 -84 -234 67 O
ATOM 1552 CB LEU A 117 15.409 158.256 140.343 1.00 58.96 C
ANISOU 1552 CB LEU A 117 8395 6554 7455 -45 -208 82 C
ATOM 1553 CG LEU A 117 13.904 158.032 140.310 1.00 66.51 C
ANISOU 1553 CG LEU A 117 9291 7493 8485 -44 -168 110 C
ATOM 1554 CD1 LEU A 117 13.194 158.826 141.416 1.00 68.26 C
ANISOU 1554 CD1 LEU A 117 9525 7656 8753 -28 -53 100 C
ATOM 1555 CD2 LEU A 117 13.349 158.412 138.963 1.00 71.38 C
ANISOU 1555 CD2 LEU A 117 9832 8119 9167 -53 -233 157 C
ATOM 1556 N SER A 118 17.782 156.024 140.662 1.00 55.55 N
ANISOU 1556 N SER A 118 8021 6124 6961 -64 -298 66 N
ATOM 1557 CA SER A 118 18.301 154.685 140.348 1.00 53.61 C
ANISOU 1557 CA SER A 118 7767 5868 6735 -64 -312 67 C
ATOM 1558 C SER A 118 18.415 153.728 141.543 1.00 57.78 C
ANISOU 1558 C SER A 118 8340 6366 7248 -79 -347 81 C
ATOM 1559 O SER A 118 17.936 152.602 141.399 1.00 55.25 O
ANISOU 1559 O SER A 118 8027 6044 6923 -84 -333 79 O
ATOM 1560 CB SER A 118 19.634 154.746 139.619 1.00 53.38 C
ANISOU 1560 CB SER A 118 7697 5817 6767 -51 -313 67 C
ATOM 1561 OG SER A 118 19.494 155.218 138.296 1.00 59.05 O
ANISOU 1561 OG SER A 118 8409 6550 7476 -57 -268 52 O
ATOM 1562 N PRO A 119 19.037 154.099 142.708 1.00 55.52 N
ANISOU 1562 N PRO A 119 8107 6045 6943 -101 -406 100 N
ATOM 1563 CA PRO A 119 19.124 153.126 143.820 1.00 55.22 C
ANISOU 1563 CA PRO A 119 8143 5965 6874 -136 -462 125 C
ATOM 1564 C PRO A 119 17.733 152.729 144.333 1.00 57.98 C
ANISOU 1564 C PRO A 119 8562 6322 7147 -159 -387 104 C
ATOM 1565 O PRO A 119 17.500 151.561 144.642 1.00 58.84 O
ANISOU 1565 O PRO A 119 8698 6414 7244 -174 -398 115 O
ATOM 1566 CB PRO A 119 19.949 153.865 144.891 1.00 57.61 C
ANISOU 1566 CB PRO A 119 8525 6218 7146 -185 -559 157 C
ATOM 1567 CG PRO A 119 20.578 155.022 144.199 1.00 61.46 C
ANISOU 1567 CG PRO A 119 8941 6725 7688 -160 -557 151 C
ATOM 1568 CD PRO A 119 19.646 155.392 143.088 1.00 56.43 C
ANISOU 1568 CD PRO A 119 8244 6147 7050 -114 -441 106 C
ATOM 1569 N LEU A 120 16.793 153.695 144.347 1.00 52.18 N
ANISOU 1569 N LEU A 120 7837 5603 6387 -157 -299 79 N
ATOM 1570 CA LEU A 120 15.415 153.494 144.778 1.00 51.38 C
ANISOU 1570 CA LEU A 120 7766 5492 6265 -173 -195 64 C
ATOM 1571 C LEU A 120 14.650 152.543 143.840 1.00 56.54 C
ANISOU 1571 C LEU A 120 8324 6182 6977 -154 -182 72 C
ATOM 1572 O LEU A 120 14.045 151.558 144.291 1.00 56.58 O
ANISOU 1572 O LEU A 120 8362 6172 6965 -180 -157 77 O
ATOM 1573 CB LEU A 120 14.715 154.841 144.904 1.00 50.88 C
ANISOU 1573 CB LEU A 120 7701 5413 6220 -163 -94 45 C
ATOM 1574 CG LEU A 120 15.179 155.711 146.051 1.00 54.56 C
ANISOU 1574 CG LEU A 120 8318 5816 6595 -208 -72 28 C
ATOM 1575 CD1 LEU A 120 14.558 157.090 145.953 1.00 55.56 C
ANISOU 1575 CD1 LEU A 120 8423 5917 6769 -183 44 5 C
ATOM 1576 CD2 LEU A 120 14.842 155.087 147.368 1.00 54.75 C
ANISOU 1576 CD2 LEU A 120 8512 5774 6517 -281 -20 19 C
ATOM 1577 N LEU A 121 14.748 152.795 142.537 1.00 52.15 N
ANISOU 1577 N LEU A 121 7675 5665 6475 -125 -209 76 N
ATOM 1578 CA LEU A 121 14.125 151.929 141.548 1.00 51.35 C
ANISOU 1578 CA LEU A 121 7522 5583 6403 -133 -222 88 C
ATOM 1579 C LEU A 121 14.739 150.522 141.581 1.00 55.79 C
ANISOU 1579 C LEU A 121 8127 6131 6939 -143 -257 85 C
ATOM 1580 O LEU A 121 13.991 149.551 141.473 1.00 57.07 O
ANISOU 1580 O LEU A 121 8294 6289 7099 -169 -249 93 O
ATOM 1581 CB LEU A 121 14.216 152.558 140.160 1.00 50.31 C
ANISOU 1581 CB LEU A 121 7340 5476 6300 -127 -254 95 C
ATOM 1582 CG LEU A 121 13.319 153.766 139.960 1.00 54.09 C
ANISOU 1582 CG LEU A 121 7755 5957 6840 -121 -237 119 C
ATOM 1583 CD1 LEU A 121 13.701 154.529 138.720 1.00 53.43 C
ANISOU 1583 CD1 LEU A 121 7655 5887 6758 -124 -288 129 C
ATOM 1584 CD2 LEU A 121 11.857 153.358 139.902 1.00 56.80 C
ANISOU 1584 CD2 LEU A 121 8036 6287 7259 -147 -228 159 C
ATOM 1585 N LEU A 122 16.078 150.413 141.804 1.00 49.92 N
ANISOU 1585 N LEU A 122 7404 5365 6197 -125 -297 82 N
ATOM 1586 CA LEU A 122 16.779 149.130 141.890 1.00 49.20 C
ANISOU 1586 CA LEU A 122 7332 5234 6126 -124 -327 91 C
ATOM 1587 C LEU A 122 16.390 148.350 143.150 1.00 55.42 C
ANISOU 1587 C LEU A 122 8193 5994 6871 -156 -349 109 C
ATOM 1588 O LEU A 122 16.351 147.116 143.117 1.00 52.55 O
ANISOU 1588 O LEU A 122 7848 5603 6517 -164 -359 116 O
ATOM 1589 CB LEU A 122 18.309 149.272 141.757 1.00 48.67 C
ANISOU 1589 CB LEU A 122 7229 5129 6136 -93 -365 103 C
ATOM 1590 CG LEU A 122 18.856 149.571 140.336 1.00 51.49 C
ANISOU 1590 CG LEU A 122 7535 5486 6543 -69 -307 78 C
ATOM 1591 CD1 LEU A 122 20.287 150.053 140.399 1.00 51.59 C
ANISOU 1591 CD1 LEU A 122 7485 5457 6659 -40 -328 98 C
ATOM 1592 CD2 LEU A 122 18.765 148.372 139.432 1.00 50.68 C
ANISOU 1592 CD2 LEU A 122 7456 5348 6452 -75 -248 57 C
ATOM 1593 N GLY A 123 16.074 149.083 144.230 1.00 54.28 N
ANISOU 1593 N GLY A 123 8112 5843 6669 -184 -341 112 N
ATOM 1594 CA GLY A 123 15.587 148.497 145.473 1.00 54.62 C
ANISOU 1594 CA GLY A 123 8267 5846 6639 -238 -335 124 C
ATOM 1595 C GLY A 123 14.216 147.864 145.284 1.00 58.86 C
ANISOU 1595 C GLY A 123 8787 6400 7176 -253 -247 112 C
ATOM 1596 O GLY A 123 13.950 146.784 145.809 1.00 60.23 O
ANISOU 1596 O GLY A 123 9023 6545 7319 -288 -252 125 O
ATOM 1597 N ALA A 124 13.342 148.522 144.506 1.00 54.94 N
ANISOU 1597 N ALA A 124 8199 5943 6732 -233 -183 100 N
ATOM 1598 CA ALA A 124 12.007 148.035 144.159 1.00 54.67 C
ANISOU 1598 CA ALA A 124 8108 5918 6745 -253 -125 109 C
ATOM 1599 C ALA A 124 12.142 146.820 143.230 1.00 58.58 C
ANISOU 1599 C ALA A 124 8583 6425 7249 -260 -191 117 C
ATOM 1600 O ALA A 124 11.346 145.877 143.339 1.00 58.57 O
ANISOU 1600 O ALA A 124 8590 6411 7253 -297 -174 130 O
ATOM 1601 CB ALA A 124 11.204 149.134 143.472 1.00 55.12 C
ANISOU 1601 CB ALA A 124 8055 5998 6891 -233 -84 119 C
ATOM 1602 N ALA A 125 13.155 146.835 142.326 1.00 53.60 N
ANISOU 1602 N ALA A 125 7939 5804 6621 -230 -247 107 N
ATOM 1603 CA ALA A 125 13.408 145.717 141.420 1.00 53.16 C
ANISOU 1603 CA ALA A 125 7901 5732 6566 -242 -274 102 C
ATOM 1604 C ALA A 125 13.771 144.449 142.250 1.00 58.42 C
ANISOU 1604 C ALA A 125 8632 6350 7213 -250 -288 108 C
ATOM 1605 O ALA A 125 13.271 143.360 141.945 1.00 58.06 O
ANISOU 1605 O ALA A 125 8615 6285 7159 -282 -287 110 O
ATOM 1606 CB ALA A 125 14.529 146.067 140.449 1.00 53.29 C
ANISOU 1606 CB ALA A 125 7909 5741 6598 -210 -281 81 C
ATOM 1607 N MET A 126 14.591 144.620 143.325 1.00 55.28 N
ANISOU 1607 N MET A 126 8270 5924 6809 -234 -319 121 N
ATOM 1608 CA MET A 126 15.017 143.569 144.253 1.00 57.07 C
ANISOU 1608 CA MET A 126 8568 6092 7024 -251 -366 148 C
ATOM 1609 C MET A 126 13.842 142.978 145.028 1.00 61.45 C
ANISOU 1609 C MET A 126 9191 6642 7514 -310 -329 155 C
ATOM 1610 O MET A 126 13.773 141.761 145.177 1.00 63.21 O
ANISOU 1610 O MET A 126 9458 6827 7734 -331 -348 168 O
ATOM 1611 CB MET A 126 16.059 144.101 145.233 1.00 60.82 C
ANISOU 1611 CB MET A 126 9080 6529 7500 -249 -446 181 C
ATOM 1612 CG MET A 126 17.457 144.049 144.693 1.00 66.54 C
ANISOU 1612 CG MET A 126 9729 7212 8342 -195 -502 200 C
ATOM 1613 SD MET A 126 18.684 144.963 145.673 1.00 73.14 S
ANISOU 1613 SD MET A 126 10575 8005 9209 -206 -630 257 S
ATOM 1614 CE MET A 126 18.591 144.086 147.163 1.00 70.68 C
ANISOU 1614 CE MET A 126 10415 7621 8818 -287 -740 316 C
ATOM 1615 N ALA A 127 12.927 143.832 145.530 1.00 56.07 N
ANISOU 1615 N ALA A 127 8519 5987 6798 -337 -257 146 N
ATOM 1616 CA ALA A 127 11.720 143.404 146.235 1.00 55.31 C
ANISOU 1616 CA ALA A 127 8472 5874 6671 -395 -175 150 C
ATOM 1617 C ALA A 127 10.806 142.573 145.298 1.00 59.94 C
ANISOU 1617 C ALA A 127 8980 6481 7313 -409 -161 155 C
ATOM 1618 O ALA A 127 10.230 141.572 145.739 1.00 62.12 O
ANISOU 1618 O ALA A 127 9305 6727 7569 -457 -140 168 O
ATOM 1619 CB ALA A 127 10.980 144.613 146.774 1.00 55.72 C
ANISOU 1619 CB ALA A 127 8520 5928 6723 -407 -61 135 C
ATOM 1620 N SER A 128 10.730 142.967 144.001 1.00 54.53 N
ANISOU 1620 N SER A 128 8197 5837 6686 -382 -188 150 N
ATOM 1621 CA SER A 128 9.960 142.312 142.927 1.00 53.61 C
ANISOU 1621 CA SER A 128 8032 5729 6607 -418 -215 164 C
ATOM 1622 C SER A 128 10.514 140.930 142.597 1.00 57.74 C
ANISOU 1622 C SER A 128 8634 6215 7090 -431 -260 155 C
ATOM 1623 O SER A 128 9.736 139.985 142.454 1.00 57.64 O
ANISOU 1623 O SER A 128 8640 6184 7077 -488 -265 170 O
ATOM 1624 CB SER A 128 9.909 143.185 141.673 1.00 53.38 C
ANISOU 1624 CB SER A 128 7929 5735 6618 -407 -254 167 C
ATOM 1625 OG SER A 128 9.358 144.460 141.968 1.00 55.04 O
ANISOU 1625 OG SER A 128 8054 5967 6894 -390 -210 183 O
ATOM 1626 N GLU A 129 11.854 140.807 142.496 1.00 54.93 N
ANISOU 1626 N GLU A 129 8317 5833 6723 -381 -284 135 N
ATOM 1627 CA GLU A 129 12.539 139.536 142.237 1.00 55.29 C
ANISOU 1627 CA GLU A 129 8426 5814 6769 -376 -300 127 C
ATOM 1628 C GLU A 129 12.237 138.557 143.386 1.00 60.74 C
ANISOU 1628 C GLU A 129 9180 6465 7433 -409 -311 153 C
ATOM 1629 O GLU A 129 11.894 137.412 143.110 1.00 61.21 O
ANISOU 1629 O GLU A 129 9287 6487 7484 -445 -312 154 O
ATOM 1630 CB GLU A 129 14.052 139.747 142.046 1.00 56.38 C
ANISOU 1630 CB GLU A 129 8551 5911 6961 -306 -306 116 C
ATOM 1631 CG GLU A 129 14.849 138.475 141.764 1.00 68.39 C
ANISOU 1631 CG GLU A 129 10115 7335 8534 -286 -294 112 C
ATOM 1632 CD GLU A 129 15.236 137.602 142.950 1.00 90.88 C
ANISOU 1632 CD GLU A 129 12997 10120 11415 -281 -351 157 C
ATOM 1633 OE1 GLU A 129 15.265 138.132 144.084 1.00 83.89 O
ANISOU 1633 OE1 GLU A 129 12117 9256 10501 -290 -412 193 O
ATOM 1634 OE2 GLU A 129 15.525 136.397 142.749 1.00 82.35 O
ANISOU 1634 OE2 GLU A 129 11955 8953 10380 -276 -338 160 O
ATOM 1635 N ARG A 130 12.337 139.025 144.659 1.00 57.89 N
ANISOU 1635 N ARG A 130 8848 6104 7045 -411 -319 174 N
ATOM 1636 CA ARG A 130 12.040 138.246 145.868 1.00 58.49 C
ANISOU 1636 CA ARG A 130 9023 6134 7068 -463 -327 203 C
ATOM 1637 C ARG A 130 10.601 137.758 145.868 1.00 63.37 C
ANISOU 1637 C ARG A 130 9641 6769 7670 -529 -259 203 C
ATOM 1638 O ARG A 130 10.374 136.569 146.064 1.00 64.54 O
ANISOU 1638 O ARG A 130 9852 6873 7800 -568 -272 217 O
ATOM 1639 CB ARG A 130 12.295 139.068 147.156 1.00 58.21 C
ANISOU 1639 CB ARG A 130 9062 6087 6970 -484 -333 219 C
ATOM 1640 CG ARG A 130 13.751 139.228 147.609 1.00 61.87 C
ANISOU 1640 CG ARG A 130 9560 6499 7447 -455 -450 253 C
ATOM 1641 CD ARG A 130 14.723 138.213 147.063 1.00 68.62 C
ANISOU 1641 CD ARG A 130 10376 7294 8404 -407 -529 278 C
ATOM 1642 NE ARG A 130 14.626 136.906 147.697 1.00 80.41 N
ANISOU 1642 NE ARG A 130 11962 8713 9875 -452 -576 316 N
ATOM 1643 CZ ARG A 130 14.824 135.755 147.063 1.00 89.09 C
ANISOU 1643 CZ ARG A 130 13035 9762 11051 -424 -575 317 C
ATOM 1644 NH1 ARG A 130 15.101 135.743 145.761 1.00 63.39 N
ANISOU 1644 NH1 ARG A 130 9685 6518 7881 -362 -515 275 N
ATOM 1645 NH2 ARG A 130 14.735 134.605 147.721 1.00 72.15 N
ANISOU 1645 NH2 ARG A 130 10982 7543 8887 -467 -625 358 N
ATOM 1646 N TYR A 131 9.639 138.673 145.634 1.00 59.02 N
ANISOU 1646 N TYR A 131 9004 6268 7150 -541 -189 196 N
ATOM 1647 CA TYR A 131 8.225 138.372 145.595 1.00 59.47 C
ANISOU 1647 CA TYR A 131 9013 6331 7251 -602 -125 213 C
ATOM 1648 C TYR A 131 7.923 137.303 144.543 1.00 65.99 C
ANISOU 1648 C TYR A 131 9826 7150 8097 -636 -190 222 C
ATOM 1649 O TYR A 131 7.374 136.270 144.901 1.00 66.78 O
ANISOU 1649 O TYR A 131 9974 7215 8184 -693 -178 239 O
ATOM 1650 CB TYR A 131 7.392 139.653 145.399 1.00 61.29 C
ANISOU 1650 CB TYR A 131 9117 6599 7570 -593 -54 220 C
ATOM 1651 CG TYR A 131 5.908 139.383 145.273 1.00 65.77 C
ANISOU 1651 CG TYR A 131 9586 7156 8248 -655 4 259 C
ATOM 1652 CD1 TYR A 131 5.121 139.167 146.400 1.00 68.53 C
ANISOU 1652 CD1 TYR A 131 9965 7458 8617 -702 141 268 C
ATOM 1653 CD2 TYR A 131 5.299 139.284 144.020 1.00 67.42 C
ANISOU 1653 CD2 TYR A 131 9685 7385 8546 -683 -85 296 C
ATOM 1654 CE1 TYR A 131 3.762 138.876 146.289 1.00 70.08 C
ANISOU 1654 CE1 TYR A 131 10042 7629 8956 -760 204 315 C
ATOM 1655 CE2 TYR A 131 3.942 138.980 143.898 1.00 69.60 C
ANISOU 1655 CE2 TYR A 131 9850 7638 8957 -752 -65 355 C
ATOM 1656 CZ TYR A 131 3.177 138.778 145.038 1.00 76.21 C
ANISOU 1656 CZ TYR A 131 10677 8429 9849 -783 87 365 C
ATOM 1657 OH TYR A 131 1.832 138.520 144.944 1.00 76.71 O
ANISOU 1657 OH TYR A 131 10599 8457 10090 -848 123 432 O
ATOM 1658 N LEU A 132 8.324 137.506 143.270 1.00 63.04 N
ANISOU 1658 N LEU A 132 9419 6797 7737 -613 -252 208 N
ATOM 1659 CA LEU A 132 8.078 136.518 142.211 1.00 62.34 C
ANISOU 1659 CA LEU A 132 9371 6681 7636 -668 -308 210 C
ATOM 1660 C LEU A 132 8.795 135.220 142.492 1.00 66.93 C
ANISOU 1660 C LEU A 132 10070 7194 8168 -662 -312 193 C
ATOM 1661 O LEU A 132 8.200 134.164 142.319 1.00 67.71 O
ANISOU 1661 O LEU A 132 10220 7257 8252 -731 -328 205 O
ATOM 1662 CB LEU A 132 8.438 137.046 140.812 1.00 61.93 C
ANISOU 1662 CB LEU A 132 9314 6640 7575 -665 -355 193 C
ATOM 1663 CG LEU A 132 7.694 138.307 140.345 1.00 66.56 C
ANISOU 1663 CG LEU A 132 9784 7280 8225 -680 -384 226 C
ATOM 1664 CD1 LEU A 132 8.466 139.037 139.260 1.00 66.29 C
ANISOU 1664 CD1 LEU A 132 9776 7254 8155 -656 -413 199 C
ATOM 1665 CD2 LEU A 132 6.283 138.005 139.925 1.00 68.28 C
ANISOU 1665 CD2 LEU A 132 9942 7491 8508 -782 -447 290 C
ATOM 1666 N GLY A 133 10.032 135.309 142.981 1.00 63.20 N
ANISOU 1666 N GLY A 133 9628 6694 7689 -587 -308 176 N
ATOM 1667 CA GLY A 133 10.872 134.161 143.314 1.00 62.95 C
ANISOU 1667 CA GLY A 133 9683 6579 7658 -565 -323 177 C
ATOM 1668 C GLY A 133 10.354 133.279 144.430 1.00 68.49 C
ANISOU 1668 C GLY A 133 10451 7245 8326 -616 -331 211 C
ATOM 1669 O GLY A 133 10.464 132.057 144.339 1.00 69.68 O
ANISOU 1669 O GLY A 133 10675 7324 8476 -636 -345 215 O
ATOM 1670 N ILE A 134 9.806 133.885 145.498 1.00 65.78 N
ANISOU 1670 N ILE A 134 10103 6939 7952 -644 -305 232 N
ATOM 1671 CA ILE A 134 9.265 133.186 146.679 1.00 66.54 C
ANISOU 1671 CA ILE A 134 10291 6994 7995 -710 -287 262 C
ATOM 1672 C ILE A 134 7.812 132.734 146.463 1.00 73.72 C
ANISOU 1672 C ILE A 134 11172 7921 8918 -793 -229 270 C
ATOM 1673 O ILE A 134 7.445 131.624 146.873 1.00 73.23 O
ANISOU 1673 O ILE A 134 11190 7806 8827 -851 -230 289 O
ATOM 1674 CB ILE A 134 9.438 134.061 147.955 1.00 68.80 C
ANISOU 1674 CB ILE A 134 10635 7282 8224 -720 -262 275 C
ATOM 1675 CG1 ILE A 134 10.929 134.188 148.336 1.00 68.63 C
ANISOU 1675 CG1 ILE A 134 10663 7213 8199 -666 -372 296 C
ATOM 1676 CG2 ILE A 134 8.594 133.573 149.134 1.00 68.94 C
ANISOU 1676 CG2 ILE A 134 10770 7257 8167 -816 -192 296 C
ATOM 1677 CD1 ILE A 134 11.278 135.406 149.151 1.00 73.14 C
ANISOU 1677 CD1 ILE A 134 11274 7797 8717 -670 -373 301 C
ATOM 1678 N THR A 135 6.983 133.595 145.837 1.00 71.90 N
ANISOU 1678 N THR A 135 10816 7752 8749 -803 -189 267 N
ATOM 1679 CA THR A 135 5.578 133.266 145.634 1.00 72.75 C
ANISOU 1679 CA THR A 135 10856 7864 8920 -886 -152 297 C
ATOM 1680 C THR A 135 5.394 132.270 144.503 1.00 80.27 C
ANISOU 1680 C THR A 135 11829 8796 9876 -933 -240 303 C
ATOM 1681 O THR A 135 4.651 131.317 144.682 1.00 82.24 O
ANISOU 1681 O THR A 135 12110 9009 10129 -1012 -237 328 O
ATOM 1682 CB THR A 135 4.706 134.506 145.494 1.00 76.08 C
ANISOU 1682 CB THR A 135 11121 8332 9452 -886 -89 316 C
ATOM 1683 OG1 THR A 135 5.060 135.205 144.299 1.00 73.55 O
ANISOU 1683 OG1 THR A 135 10730 8056 9162 -845 -172 308 O
ATOM 1684 CG2 THR A 135 4.771 135.417 146.725 1.00 74.07 C
ANISOU 1684 CG2 THR A 135 10888 8072 9184 -859 41 302 C
ATOM 1685 N ARG A 136 6.045 132.466 143.353 1.00 78.48 N
ANISOU 1685 N ARG A 136 11605 8579 9635 -901 -308 277 N
ATOM 1686 CA ARG A 136 5.915 131.505 142.254 1.00 79.91 C
ANISOU 1686 CA ARG A 136 11862 8715 9785 -967 -376 273 C
ATOM 1687 C ARG A 136 6.872 130.315 142.503 1.00 88.43 C
ANISOU 1687 C ARG A 136 13085 9712 10803 -937 -365 241 C
ATOM 1688 O ARG A 136 7.810 130.472 143.289 1.00 86.39 O
ANISOU 1688 O ARG A 136 12841 9441 10542 -854 -339 230 O
ATOM 1689 CB ARG A 136 6.151 132.175 140.895 1.00 78.50 C
ANISOU 1689 CB ARG A 136 11675 8554 9597 -971 -433 257 C
ATOM 1690 N PRO A 137 6.653 129.098 141.922 1.00 91.43 N
ANISOU 1690 N PRO A 137 13573 10021 11146 -1009 -392 235 N
ATOM 1691 CA PRO A 137 7.583 127.979 142.211 1.00 93.05 C
ANISOU 1691 CA PRO A 137 13900 10128 11328 -968 -368 211 C
ATOM 1692 C PRO A 137 9.058 128.289 141.912 1.00 99.63 C
ANISOU 1692 C PRO A 137 14746 10918 12191 -852 -332 169 C
ATOM 1693 O PRO A 137 9.374 129.255 141.197 1.00 99.39 O
ANISOU 1693 O PRO A 137 14669 10929 12166 -821 -320 143 O
ATOM 1694 CB PRO A 137 7.032 126.815 141.366 1.00 95.05 C
ANISOU 1694 CB PRO A 137 14275 10307 11534 -1076 -392 203 C
ATOM 1695 CG PRO A 137 5.611 127.174 141.123 1.00 99.22 C
ANISOU 1695 CG PRO A 137 14725 10902 12073 -1189 -454 252 C
ATOM 1696 CD PRO A 137 5.585 128.664 140.992 1.00 93.96 C
ANISOU 1696 CD PRO A 137 13920 10329 11452 -1139 -458 260 C
ATOM 1697 N PHE A 138 9.959 127.489 142.496 1.00 97.32 N
ANISOU 1697 N PHE A 138 14504 10533 11939 -791 -318 174 N
ATOM 1698 CA PHE A 138 11.390 127.685 142.320 1.00 97.56 C
ANISOU 1698 CA PHE A 138 14514 10497 12058 -679 -282 155 C
ATOM 1699 C PHE A 138 11.873 127.414 140.892 1.00102.11 C
ANISOU 1699 C PHE A 138 15164 10990 12642 -674 -192 89 C
ATOM 1700 O PHE A 138 11.308 126.584 140.171 1.00101.59 O
ANISOU 1700 O PHE A 138 15223 10867 12507 -762 -167 61 O
ATOM 1701 CB PHE A 138 12.200 126.876 143.354 1.00100.07 C
ANISOU 1701 CB PHE A 138 14849 10714 12459 -623 -317 203 C
ATOM 1702 CG PHE A 138 13.627 127.348 143.538 1.00102.03 C
ANISOU 1702 CG PHE A 138 15013 10907 12848 -506 -322 222 C
ATOM 1703 CD1 PHE A 138 13.903 128.590 144.109 1.00104.73 C
ANISOU 1703 CD1 PHE A 138 15262 11338 13192 -473 -377 247 C
ATOM 1704 CD2 PHE A 138 14.697 126.551 143.142 1.00105.19 C
ANISOU 1704 CD2 PHE A 138 15418 11150 13399 -433 -266 219 C
ATOM 1705 CE1 PHE A 138 15.224 129.033 144.263 1.00105.94 C
ANISOU 1705 CE1 PHE A 138 15325 11434 13492 -378 -402 278 C
ATOM 1706 CE2 PHE A 138 16.018 126.990 143.307 1.00108.49 C
ANISOU 1706 CE2 PHE A 138 15722 11503 13998 -327 -275 254 C
ATOM 1707 CZ PHE A 138 16.272 128.229 143.864 1.00105.94 C
ANISOU 1707 CZ PHE A 138 15304 11280 13670 -305 -357 287 C
ATOM 1708 N SER A 139 12.894 128.184 140.485 1.00 99.31 N
ANISOU 1708 N SER A 139 14747 10623 12363 -587 -137 65 N
ATOM 1709 CA SER A 139 13.606 128.072 139.217 1.00 99.96 C
ANISOU 1709 CA SER A 139 14904 10604 12470 -570 -7 -3 C
ATOM 1710 C SER A 139 15.082 128.328 139.516 1.00102.94 C
ANISOU 1710 C SER A 139 15170 10904 13038 -432 52 9 C
ATOM 1711 O SER A 139 15.426 129.367 140.101 1.00101.55 O
ANISOU 1711 O SER A 139 14861 10817 12908 -377 -15 46 O
ATOM 1712 CB SER A 139 13.076 129.062 138.181 1.00103.68 C
ANISOU 1712 CB SER A 139 15407 11160 12825 -639 -2 -41 C
ATOM 1713 OG SER A 139 13.554 128.718 136.888 1.00114.75 O
ANISOU 1713 OG SER A 139 16964 12440 14197 -670 138 -114 O
ATOM 1714 N ARG A 140 15.940 127.337 139.183 1.00 99.66 N
ANISOU 1714 N ARG A 140 14802 10308 12755 -380 173 -11 N
ATOM 1715 CA ARG A 140 17.393 127.401 139.384 1.00 99.05 C
ANISOU 1715 CA ARG A 140 14595 10113 12928 -248 240 16 C
ATOM 1716 C ARG A 140 17.989 128.597 138.597 1.00 99.33 C
ANISOU 1716 C ARG A 140 14568 10182 12989 -212 336 -28 C
ATOM 1717 O ARG A 140 17.694 128.725 137.398 1.00 98.55 O
ANISOU 1717 O ARG A 140 14608 10070 12765 -279 464 -112 O
ATOM 1718 CB ARG A 140 18.063 126.076 138.966 1.00 99.88 C
ANISOU 1718 CB ARG A 140 14770 9991 13191 -207 399 -7 C
ATOM 1719 N PRO A 141 18.756 129.509 139.265 1.00 92.77 N
ANISOU 1719 N PRO A 141 13554 9398 12297 -127 259 33 N
ATOM 1720 CA PRO A 141 19.336 130.661 138.552 1.00 90.97 C
ANISOU 1720 CA PRO A 141 13262 9202 12100 -95 348 -5 C
ATOM 1721 C PRO A 141 19.910 130.292 137.182 1.00 91.13 C
ANISOU 1721 C PRO A 141 13386 9064 12175 -91 612 -96 C
ATOM 1722 O PRO A 141 20.891 129.551 137.063 1.00 93.45 O
ANISOU 1722 O PRO A 141 13633 9167 12707 -11 758 -92 O
ATOM 1723 CB PRO A 141 20.397 131.202 139.528 1.00 93.11 C
ANISOU 1723 CB PRO A 141 13322 9459 12597 5 243 90 C
ATOM 1724 CG PRO A 141 20.510 130.171 140.620 1.00 98.87 C
ANISOU 1724 CG PRO A 141 14023 10109 13435 26 116 178 C
ATOM 1725 CD PRO A 141 19.168 129.520 140.680 1.00 94.12 C
ANISOU 1725 CD PRO A 141 13590 9578 12594 -75 77 144 C
ATOM 1726 N ALA A 142 19.203 130.747 136.144 1.00 80.47 N
ANISOU 1726 N ALA A 142 12199 7777 10598 -193 674 -175 N
ATOM 1727 CA ALA A 142 19.507 130.493 134.755 1.00 77.18 C
ANISOU 1727 CA ALA A 142 11966 7219 10141 -240 923 -275 C
ATOM 1728 C ALA A 142 20.238 131.694 134.140 1.00 75.36 C
ANISOU 1728 C ALA A 142 11675 7000 9958 -208 1031 -303 C
ATOM 1729 O ALA A 142 20.190 132.805 134.673 1.00 73.61 O
ANISOU 1729 O ALA A 142 11298 6931 9738 -176 879 -251 O
ATOM 1730 CB ALA A 142 18.217 130.192 134.005 1.00 77.16 C
ANISOU 1730 CB ALA A 142 12220 7260 9835 -407 884 -327 C
ATOM 1731 N VAL A 143 20.935 131.454 133.023 1.00 68.65 N
ANISOU 1731 N VAL A 143 10963 5972 9150 -221 1314 -389 N
ATOM 1732 CA VAL A 143 21.678 132.457 132.261 1.00 66.41 C
ANISOU 1732 CA VAL A 143 10664 5660 8907 -207 1474 -430 C
ATOM 1733 C VAL A 143 20.693 133.492 131.681 1.00 64.83 C
ANISOU 1733 C VAL A 143 10606 5633 8394 -340 1339 -451 C
ATOM 1734 O VAL A 143 21.022 134.676 131.595 1.00 63.18 O
ANISOU 1734 O VAL A 143 10297 5507 8202 -316 1316 -438 O
ATOM 1735 CB VAL A 143 22.585 131.771 131.191 1.00 72.44 C
ANISOU 1735 CB VAL A 143 11580 6153 9792 -203 1860 -526 C
ATOM 1736 CG1 VAL A 143 21.780 130.978 130.161 1.00 72.78 C
ANISOU 1736 CG1 VAL A 143 12007 6100 9545 -372 1975 -624 C
ATOM 1737 CG2 VAL A 143 23.517 132.765 130.516 1.00 73.35 C
ANISOU 1737 CG2 VAL A 143 11648 6216 10007 -174 2058 -561 C
ATOM 1738 N ALA A 144 19.472 133.026 131.333 1.00 59.24 N
ANISOU 1738 N ALA A 144 10115 4971 7425 -483 1229 -469 N
ATOM 1739 CA ALA A 144 18.361 133.802 130.787 1.00 57.57 C
ANISOU 1739 CA ALA A 144 10039 4897 6937 -628 1059 -464 C
ATOM 1740 C ALA A 144 17.794 134.758 131.834 1.00 60.28 C
ANISOU 1740 C ALA A 144 10136 5463 7305 -573 791 -371 C
ATOM 1741 O ALA A 144 17.505 135.919 131.521 1.00 60.03 O
ANISOU 1741 O ALA A 144 10087 5536 7185 -610 707 -356 O
ATOM 1742 CB ALA A 144 17.270 132.872 130.282 1.00 58.23 C
ANISOU 1742 CB ALA A 144 10381 4943 6802 -790 992 -483 C
ATOM 1743 N SER A 145 17.661 134.275 133.078 1.00 55.85 N
ANISOU 1743 N SER A 145 9403 4955 6864 -489 673 -311 N
ATOM 1744 CA SER A 145 17.149 135.078 134.178 1.00 54.24 C
ANISOU 1744 CA SER A 145 8997 4931 6681 -442 458 -232 C
ATOM 1745 C SER A 145 18.142 136.208 134.543 1.00 56.24 C
ANISOU 1745 C SER A 145 9064 5223 7080 -333 478 -211 C
ATOM 1746 O SER A 145 17.703 137.321 134.855 1.00 54.85 O
ANISOU 1746 O SER A 145 8803 5186 6851 -337 350 -177 O
ATOM 1747 CB SER A 145 16.781 134.193 135.374 1.00 57.84 C
ANISOU 1747 CB SER A 145 9372 5404 7200 -406 351 -179 C
ATOM 1748 OG SER A 145 17.902 133.692 136.089 1.00 70.78 O
ANISOU 1748 OG SER A 145 10885 6950 9059 -284 409 -153 O
ATOM 1749 N GLN A 146 19.470 135.924 134.454 1.00 52.00 N
ANISOU 1749 N GLN A 146 8463 4548 6746 -240 648 -229 N
ATOM 1750 CA GLN A 146 20.544 136.870 134.735 1.00 51.72 C
ANISOU 1750 CA GLN A 146 8246 4519 6888 -143 677 -202 C
ATOM 1751 C GLN A 146 20.563 137.943 133.617 1.00 56.85 C
ANISOU 1751 C GLN A 146 8988 5196 7415 -203 763 -256 C
ATOM 1752 O GLN A 146 20.696 139.146 133.894 1.00 55.78 O
ANISOU 1752 O GLN A 146 8735 5165 7293 -175 677 -224 O
ATOM 1753 CB GLN A 146 21.876 136.124 134.839 1.00 54.30 C
ANISOU 1753 CB GLN A 146 8470 4657 7505 -39 843 -194 C
ATOM 1754 CG GLN A 146 23.093 137.010 135.104 1.00 74.06 C
ANISOU 1754 CG GLN A 146 10759 7138 10244 57 869 -150 C
ATOM 1755 CD GLN A 146 24.401 136.255 134.965 1.00102.52 C
ANISOU 1755 CD GLN A 146 14252 10519 14182 151 1073 -139 C
ATOM 1756 OE1 GLN A 146 25.308 136.390 135.792 1.00100.52 O
ANISOU 1756 OE1 GLN A 146 13766 10223 14206 244 993 -46 O
ATOM 1757 NE2 GLN A 146 24.546 135.457 133.906 1.00 98.26 N
ANISOU 1757 NE2 GLN A 146 13880 9814 13640 123 1346 -229 N
ATOM 1758 N ARG A 147 20.362 137.490 132.372 1.00 52.76 N
ANISOU 1758 N ARG A 147 8712 4578 6758 -304 922 -334 N
ATOM 1759 CA ARG A 147 20.267 138.294 131.159 1.00 51.94 C
ANISOU 1759 CA ARG A 147 8779 4469 6488 -404 1006 -387 C
ATOM 1760 C ARG A 147 19.072 139.248 131.310 1.00 54.59 C
ANISOU 1760 C ARG A 147 9107 4993 6640 -476 751 -337 C
ATOM 1761 O ARG A 147 19.253 140.463 131.214 1.00 54.31 O
ANISOU 1761 O ARG A 147 8999 5035 6601 -463 711 -321 O
ATOM 1762 CB ARG A 147 20.082 137.340 129.972 1.00 53.26 C
ANISOU 1762 CB ARG A 147 9262 4474 6502 -530 1189 -471 C
ATOM 1763 CG ARG A 147 20.379 137.902 128.610 1.00 60.65 C
ANISOU 1763 CG ARG A 147 10435 5321 7290 -641 1364 -542 C
ATOM 1764 CD ARG A 147 20.019 136.875 127.550 1.00 57.51 C
ANISOU 1764 CD ARG A 147 10402 4756 6693 -798 1511 -621 C
ATOM 1765 NE ARG A 147 20.893 135.731 127.700 1.00 59.70 N
ANISOU 1765 NE ARG A 147 10661 4845 7175 -707 1771 -671 N
ATOM 1766 CZ ARG A 147 20.500 134.471 127.702 1.00 74.53 C
ANISOU 1766 CZ ARG A 147 12681 6627 9010 -751 1805 -696 C
ATOM 1767 NH1 ARG A 147 19.226 134.161 127.473 1.00 61.51 N
ANISOU 1767 NH1 ARG A 147 11226 5047 7097 -905 1595 -680 N
ATOM 1768 NH2 ARG A 147 21.377 133.504 127.900 1.00 68.41 N
ANISOU 1768 NH2 ARG A 147 11851 5670 8471 -646 2048 -732 N
ATOM 1769 N ARG A 148 17.880 138.703 131.651 1.00 50.75 N
ANISOU 1769 N ARG A 148 8664 4576 6043 -540 580 -303 N
ATOM 1770 CA ARG A 148 16.647 139.460 131.904 1.00 49.98 C
ANISOU 1770 CA ARG A 148 8521 4634 5833 -600 347 -240 C
ATOM 1771 C ARG A 148 16.828 140.504 133.013 1.00 52.10 C
ANISOU 1771 C ARG A 148 8539 5032 6226 -485 246 -186 C
ATOM 1772 O ARG A 148 16.363 141.627 132.862 1.00 50.67 O
ANISOU 1772 O ARG A 148 8321 4941 5990 -512 148 -157 O
ATOM 1773 CB ARG A 148 15.485 138.499 132.224 1.00 53.23 C
ANISOU 1773 CB ARG A 148 8987 5067 6171 -673 220 -209 C
ATOM 1774 CG ARG A 148 14.111 139.157 132.391 1.00 64.30 C
ANISOU 1774 CG ARG A 148 10332 6598 7501 -745 -1 -135 C
ATOM 1775 CD ARG A 148 13.022 138.104 132.436 1.00 82.44 C
ANISOU 1775 CD ARG A 148 12707 8881 9734 -843 -100 -105 C
ATOM 1776 NE ARG A 148 11.879 138.560 133.227 1.00104.66 N
ANISOU 1776 NE ARG A 148 15350 11815 12599 -843 -271 -23 N
ATOM 1777 CZ ARG A 148 11.252 137.822 134.140 1.00122.94 C
ANISOU 1777 CZ ARG A 148 17592 14156 14965 -833 -321 10 C
ATOM 1778 NH1 ARG A 148 11.643 136.574 134.379 1.00111.53 N
ANISOU 1778 NH1 ARG A 148 16230 12631 13517 -823 -241 -27 N
ATOM 1779 NH2 ARG A 148 10.222 138.323 134.814 1.00106.02 N
ANISOU 1779 NH2 ARG A 148 15293 12103 12887 -835 -434 81 N
ATOM 1780 N ALA A 149 17.528 140.149 134.101 1.00 49.91 N
ANISOU 1780 N ALA A 149 8106 4745 6112 -368 264 -167 N
ATOM 1781 CA ALA A 149 17.795 141.052 135.229 1.00 48.75 C
ANISOU 1781 CA ALA A 149 7764 4694 6067 -278 167 -116 C
ATOM 1782 C ALA A 149 18.726 142.198 134.822 1.00 53.29 C
ANISOU 1782 C ALA A 149 8279 5268 6701 -237 233 -129 C
ATOM 1783 O ALA A 149 18.454 143.343 135.176 1.00 53.57 O
ANISOU 1783 O ALA A 149 8235 5405 6716 -226 137 -99 O
ATOM 1784 CB ALA A 149 18.363 140.276 136.406 1.00 49.45 C
ANISOU 1784 CB ALA A 149 7749 4740 6300 -196 148 -81 C
ATOM 1785 N TRP A 150 19.759 141.920 134.007 1.00 49.70 N
ANISOU 1785 N TRP A 150 7876 4688 6320 -223 418 -177 N
ATOM 1786 CA TRP A 150 20.655 142.968 133.514 1.00 49.40 C
ANISOU 1786 CA TRP A 150 7791 4633 6345 -196 508 -192 C
ATOM 1787 C TRP A 150 19.947 143.921 132.527 1.00 52.54 C
ANISOU 1787 C TRP A 150 8322 5093 6547 -297 477 -212 C
ATOM 1788 O TRP A 150 20.192 145.123 132.559 1.00 51.13 O
ANISOU 1788 O TRP A 150 8066 4978 6384 -276 438 -194 O
ATOM 1789 CB TRP A 150 21.927 142.375 132.896 1.00 49.75 C
ANISOU 1789 CB TRP A 150 7850 4502 6549 -158 753 -237 C
ATOM 1790 CG TRP A 150 23.086 142.227 133.841 1.00 51.13 C
ANISOU 1790 CG TRP A 150 7797 4619 7011 -35 761 -183 C
ATOM 1791 CD1 TRP A 150 23.707 141.065 134.193 1.00 54.83 C
ANISOU 1791 CD1 TRP A 150 8201 4956 7676 27 837 -167 C
ATOM 1792 CD2 TRP A 150 23.739 143.274 134.585 1.00 50.55 C
ANISOU 1792 CD2 TRP A 150 7529 4608 7071 28 655 -121 C
ATOM 1793 NE1 TRP A 150 24.702 141.317 135.110 1.00 54.58 N
ANISOU 1793 NE1 TRP A 150 7937 4898 7905 121 765 -85 N
ATOM 1794 CE2 TRP A 150 24.714 142.657 135.404 1.00 55.34 C
ANISOU 1794 CE2 TRP A 150 7959 5115 7951 116 643 -56 C
ATOM 1795 CE3 TRP A 150 23.550 144.665 134.689 1.00 51.01 C
ANISOU 1795 CE3 TRP A 150 7551 4788 7042 12 550 -105 C
ATOM 1796 CZ2 TRP A 150 25.529 143.388 136.283 1.00 54.86 C
ANISOU 1796 CZ2 TRP A 150 7701 5072 8072 172 514 28 C
ATOM 1797 CZ3 TRP A 150 24.349 145.393 135.569 1.00 52.53 C
ANISOU 1797 CZ3 TRP A 150 7558 5001 7400 73 449 -37 C
ATOM 1798 CH2 TRP A 150 25.338 144.759 136.340 1.00 54.29 C
ANISOU 1798 CH2 TRP A 150 7619 5122 7885 145 425 31 C
ATOM 1799 N ALA A 151 19.064 143.390 131.670 1.00 50.18 N
ANISOU 1799 N ALA A 151 8229 4768 6070 -416 471 -238 N
ATOM 1800 CA ALA A 151 18.275 144.182 130.728 1.00 49.82 C
ANISOU 1800 CA ALA A 151 8328 4763 5838 -537 390 -232 C
ATOM 1801 C ALA A 151 17.387 145.154 131.539 1.00 54.04 C
ANISOU 1801 C ALA A 151 8700 5451 6380 -510 173 -157 C
ATOM 1802 O ALA A 151 17.345 146.356 131.233 1.00 55.25 O
ANISOU 1802 O ALA A 151 8832 5654 6507 -523 124 -138 O
ATOM 1803 CB ALA A 151 17.434 143.261 129.853 1.00 51.19 C
ANISOU 1803 CB ALA A 151 8749 4868 5835 -684 375 -251 C
ATOM 1804 N THR A 152 16.785 144.658 132.636 1.00 48.47 N
ANISOU 1804 N THR A 152 7877 4806 5732 -463 72 -119 N
ATOM 1805 CA THR A 152 15.946 145.443 133.553 1.00 47.78 C
ANISOU 1805 CA THR A 152 7641 4837 5678 -431 -81 -58 C
ATOM 1806 C THR A 152 16.735 146.581 134.230 1.00 53.01 C
ANISOU 1806 C THR A 152 8160 5545 6435 -334 -68 -51 C
ATOM 1807 O THR A 152 16.188 147.665 134.375 1.00 54.11 O
ANISOU 1807 O THR A 152 8239 5755 6567 -336 -151 -17 O
ATOM 1808 CB THR A 152 15.257 144.524 134.596 1.00 51.37 C
ANISOU 1808 CB THR A 152 8035 5316 6168 -411 -140 -31 C
ATOM 1809 OG1 THR A 152 14.629 143.435 133.915 1.00 52.09 O
ANISOU 1809 OG1 THR A 152 8267 5351 6173 -507 -147 -40 O
ATOM 1810 CG2 THR A 152 14.216 145.262 135.447 1.00 42.87 C
ANISOU 1810 CG2 THR A 152 6836 4333 5122 -399 -253 26 C
ATOM 1811 N VAL A 153 17.994 146.331 134.670 1.00 48.77 N
ANISOU 1811 N VAL A 153 7563 4959 6009 -255 26 -73 N
ATOM 1812 CA VAL A 153 18.874 147.340 135.294 1.00 47.05 C
ANISOU 1812 CA VAL A 153 7218 4766 5891 -179 22 -57 C
ATOM 1813 C VAL A 153 19.146 148.471 134.268 1.00 51.55 C
ANISOU 1813 C VAL A 153 7829 5341 6416 -212 65 -74 C
ATOM 1814 O VAL A 153 19.199 149.633 134.646 1.00 50.15 O
ANISOU 1814 O VAL A 153 7575 5224 6254 -186 4 -51 O
ATOM 1815 CB VAL A 153 20.192 146.711 135.835 1.00 50.35 C
ANISOU 1815 CB VAL A 153 7554 5102 6475 -105 91 -55 C
ATOM 1816 CG1 VAL A 153 21.170 147.781 136.322 1.00 49.54 C
ANISOU 1816 CG1 VAL A 153 7328 5010 6484 -51 70 -27 C
ATOM 1817 CG2 VAL A 153 19.904 145.703 136.954 1.00 49.66 C
ANISOU 1817 CG2 VAL A 153 7435 5011 6423 -83 15 -22 C
ATOM 1818 N GLY A 154 19.307 148.100 132.996 1.00 49.59 N
ANISOU 1818 N GLY A 154 7728 5017 6096 -280 173 -117 N
ATOM 1819 CA GLY A 154 19.523 149.026 131.893 1.00 49.83 C
ANISOU 1819 CA GLY A 154 7854 5031 6050 -339 222 -135 C
ATOM 1820 C GLY A 154 18.297 149.887 131.635 1.00 53.82 C
ANISOU 1820 C GLY A 154 8390 5618 6443 -405 58 -89 C
ATOM 1821 O GLY A 154 18.437 151.083 131.380 1.00 53.01 O
ANISOU 1821 O GLY A 154 8260 5546 6335 -405 30 -73 O
ATOM 1822 N LEU A 155 17.080 149.287 131.728 1.00 50.49 N
ANISOU 1822 N LEU A 155 8005 5220 5957 -460 -57 -57 N
ATOM 1823 CA LEU A 155 15.807 149.995 131.545 1.00 49.17 C
ANISOU 1823 CA LEU A 155 7826 5111 5745 -520 -227 11 C
ATOM 1824 C LEU A 155 15.610 150.949 132.706 1.00 50.59 C
ANISOU 1824 C LEU A 155 7811 5373 6037 -421 -283 45 C
ATOM 1825 O LEU A 155 15.204 152.090 132.484 1.00 50.27 O
ANISOU 1825 O LEU A 155 7736 5361 6004 -434 -357 85 O
ATOM 1826 CB LEU A 155 14.621 149.037 131.449 1.00 49.37 C
ANISOU 1826 CB LEU A 155 7904 5128 5726 -599 -329 47 C
ATOM 1827 CG LEU A 155 14.524 148.171 130.199 1.00 55.61 C
ANISOU 1827 CG LEU A 155 8939 5825 6366 -740 -313 25 C
ATOM 1828 CD1 LEU A 155 13.434 147.199 130.347 1.00 56.54 C
ANISOU 1828 CD1 LEU A 155 9075 5940 6469 -805 -422 65 C
ATOM 1829 CD2 LEU A 155 14.214 148.990 128.980 1.00 58.12 C
ANISOU 1829 CD2 LEU A 155 9409 6109 6566 -869 -404 62 C
ATOM 1830 N VAL A 156 15.974 150.519 133.929 1.00 45.29 N
ANISOU 1830 N VAL A 156 7035 4724 5450 -332 -243 30 N
ATOM 1831 CA VAL A 156 15.917 151.385 135.110 1.00 44.62 C
ANISOU 1831 CA VAL A 156 6817 4695 5444 -255 -272 51 C
ATOM 1832 C VAL A 156 16.858 152.601 134.935 1.00 50.89 C
ANISOU 1832 C VAL A 156 7585 5493 6259 -222 -239 39 C
ATOM 1833 O VAL A 156 16.411 153.736 135.122 1.00 53.01 O
ANISOU 1833 O VAL A 156 7802 5794 6545 -211 -288 67 O
ATOM 1834 CB VAL A 156 16.194 150.620 136.400 1.00 47.35 C
ANISOU 1834 CB VAL A 156 7112 5041 5839 -199 -249 42 C
ATOM 1835 CG1 VAL A 156 16.643 151.559 137.521 1.00 47.01 C
ANISOU 1835 CG1 VAL A 156 6993 5023 5845 -141 -258 49 C
ATOM 1836 CG2 VAL A 156 14.980 149.811 136.809 1.00 46.96 C
ANISOU 1836 CG2 VAL A 156 7063 5001 5779 -230 -289 65 C
ATOM 1837 N TRP A 157 18.121 152.370 134.526 1.00 46.78 N
ANISOU 1837 N TRP A 157 7095 4924 5754 -209 -147 1 N
ATOM 1838 CA TRP A 157 19.087 153.444 134.285 1.00 47.38 C
ANISOU 1838 CA TRP A 157 7143 4994 5866 -187 -105 -8 C
ATOM 1839 C TRP A 157 18.600 154.437 133.205 1.00 51.36 C
ANISOU 1839 C TRP A 157 7721 5506 6287 -252 -138 6 C
ATOM 1840 O TRP A 157 18.730 155.634 133.398 1.00 49.92 O
ANISOU 1840 O TRP A 157 7487 5353 6130 -229 -170 23 O
ATOM 1841 CB TRP A 157 20.472 152.879 133.924 1.00 46.25 C
ANISOU 1841 CB TRP A 157 7003 4773 5797 -167 27 -43 C
ATOM 1842 CG TRP A 157 21.256 152.343 135.087 1.00 46.68 C
ANISOU 1842 CG TRP A 157 6943 4808 5986 -96 20 -28 C
ATOM 1843 CD1 TRP A 157 21.150 152.713 136.396 1.00 48.79 C
ANISOU 1843 CD1 TRP A 157 7131 5120 6287 -60 -88 8 C
ATOM 1844 CD2 TRP A 157 22.296 151.355 135.030 1.00 47.15 C
ANISOU 1844 CD2 TRP A 157 6968 4775 6174 -65 122 -39 C
ATOM 1845 NE1 TRP A 157 22.062 152.021 137.160 1.00 48.63 N
ANISOU 1845 NE1 TRP A 157 7039 5047 6393 -21 -97 31 N
ATOM 1846 CE2 TRP A 157 22.801 151.202 136.344 1.00 51.07 C
ANISOU 1846 CE2 TRP A 157 7347 5270 6789 -13 30 9 C
ATOM 1847 CE3 TRP A 157 22.841 150.566 133.994 1.00 49.18 C
ANISOU 1847 CE3 TRP A 157 7294 4930 6464 -84 293 -82 C
ATOM 1848 CZ2 TRP A 157 23.815 150.278 136.656 1.00 51.43 C
ANISOU 1848 CZ2 TRP A 157 7308 5218 7014 30 71 32 C
ATOM 1849 CZ3 TRP A 157 23.867 149.674 134.293 1.00 51.40 C
ANISOU 1849 CZ3 TRP A 157 7484 5109 6936 -28 380 -74 C
ATOM 1850 CH2 TRP A 157 24.342 149.530 135.607 1.00 52.06 C
ANISOU 1850 CH2 TRP A 157 7418 5196 7167 32 255 -9 C
ATOM 1851 N ALA A 158 18.009 153.925 132.107 1.00 49.55 N
ANISOU 1851 N ALA A 158 7630 5241 5956 -344 -147 6 N
ATOM 1852 CA ALA A 158 17.467 154.702 130.990 1.00 49.87 C
ANISOU 1852 CA ALA A 158 7779 5269 5902 -438 -217 38 C
ATOM 1853 C ALA A 158 16.281 155.549 131.456 1.00 55.93 C
ANISOU 1853 C ALA A 158 8441 6092 6719 -424 -370 110 C
ATOM 1854 O ALA A 158 16.166 156.702 131.045 1.00 57.87 O
ANISOU 1854 O ALA A 158 8687 6339 6962 -442 -424 144 O
ATOM 1855 CB ALA A 158 17.041 153.775 129.851 1.00 50.95 C
ANISOU 1855 CB ALA A 158 8115 5338 5905 -564 -221 32 C
ATOM 1856 N ALA A 159 15.433 154.999 132.340 1.00 50.83 N
ANISOU 1856 N ALA A 159 7700 5477 6136 -389 -420 135 N
ATOM 1857 CA ALA A 159 14.272 155.695 132.874 1.00 50.04 C
ANISOU 1857 CA ALA A 159 7479 5403 6129 -367 -519 202 C
ATOM 1858 C ALA A 159 14.740 156.816 133.819 1.00 54.74 C
ANISOU 1858 C ALA A 159 7971 6027 6799 -273 -466 186 C
ATOM 1859 O ALA A 159 14.184 157.921 133.788 1.00 54.80 O
ANISOU 1859 O ALA A 159 7919 6031 6870 -263 -518 233 O
ATOM 1860 CB ALA A 159 13.355 154.711 133.609 1.00 49.99 C
ANISOU 1860 CB ALA A 159 7409 5408 6178 -359 -540 221 C
ATOM 1861 N ALA A 160 15.761 156.528 134.655 1.00 50.92 N
ANISOU 1861 N ALA A 160 7473 5557 6317 -212 -376 129 N
ATOM 1862 CA ALA A 160 16.310 157.508 135.601 1.00 49.87 C
ANISOU 1862 CA ALA A 160 7279 5438 6231 -147 -342 115 C
ATOM 1863 C ALA A 160 17.018 158.652 134.829 1.00 53.59 C
ANISOU 1863 C ALA A 160 7775 5900 6685 -159 -341 114 C
ATOM 1864 O ALA A 160 16.853 159.812 135.182 1.00 50.68 O
ANISOU 1864 O ALA A 160 7365 5534 6355 -133 -355 131 O
ATOM 1865 CB ALA A 160 17.256 156.830 136.578 1.00 49.52 C
ANISOU 1865 CB ALA A 160 7228 5393 6195 -109 -293 78 C
ATOM 1866 N LEU A 161 17.738 158.321 133.737 1.00 52.38 N
ANISOU 1866 N LEU A 161 7706 5723 6472 -207 -308 94 N
ATOM 1867 CA LEU A 161 18.387 159.308 132.881 1.00 53.05 C
ANISOU 1867 CA LEU A 161 7840 5789 6528 -237 -290 93 C
ATOM 1868 C LEU A 161 17.322 160.201 132.185 1.00 55.82 C
ANISOU 1868 C LEU A 161 8217 6133 6858 -286 -398 154 C
ATOM 1869 O LEU A 161 17.398 161.419 132.326 1.00 55.99 O
ANISOU 1869 O LEU A 161 8197 6157 6918 -261 -418 173 O
ATOM 1870 CB LEU A 161 19.313 158.620 131.855 1.00 54.19 C
ANISOU 1870 CB LEU A 161 8095 5882 6612 -291 -188 51 C
ATOM 1871 CG LEU A 161 20.020 159.561 130.834 1.00 60.40 C
ANISOU 1871 CG LEU A 161 8965 6632 7353 -342 -135 44 C
ATOM 1872 CD1 LEU A 161 21.024 160.523 131.519 1.00 59.85 C
ANISOU 1872 CD1 LEU A 161 8784 6576 7380 -275 -94 34 C
ATOM 1873 CD2 LEU A 161 20.707 158.761 129.766 1.00 63.63 C
ANISOU 1873 CD2 LEU A 161 9522 6964 7690 -415 1 -2 C
ATOM 1874 N ALA A 162 16.300 159.595 131.518 1.00 50.84 N
ANISOU 1874 N ALA A 162 7644 5484 6188 -358 -483 198 N
ATOM 1875 CA ALA A 162 15.199 160.311 130.849 1.00 50.89 C
ANISOU 1875 CA ALA A 162 7658 5465 6213 -419 -631 287 C
ATOM 1876 C ALA A 162 14.528 161.323 131.776 1.00 55.48 C
ANISOU 1876 C ALA A 162 8074 6058 6947 -333 -660 329 C
ATOM 1877 O ALA A 162 14.249 162.463 131.381 1.00 55.58 O
ANISOU 1877 O ALA A 162 8070 6042 7006 -344 -731 385 O
ATOM 1878 CB ALA A 162 14.166 159.329 130.325 1.00 51.98 C
ANISOU 1878 CB ALA A 162 7846 5578 6325 -505 -738 339 C
ATOM 1879 N LEU A 163 14.304 160.909 133.019 1.00 52.06 N
ANISOU 1879 N LEU A 163 7539 5651 6588 -253 -590 299 N
ATOM 1880 CA LEU A 163 13.712 161.734 134.050 1.00 52.51 C
ANISOU 1880 CA LEU A 163 7474 5698 6780 -176 -558 316 C
ATOM 1881 C LEU A 163 14.580 162.951 134.381 1.00 55.27 C
ANISOU 1881 C LEU A 163 7832 6047 7122 -132 -501 282 C
ATOM 1882 O LEU A 163 14.030 164.054 134.477 1.00 57.71 O
ANISOU 1882 O LEU A 163 8081 6316 7529 -105 -516 324 O
ATOM 1883 CB LEU A 163 13.470 160.883 135.301 1.00 53.30 C
ANISOU 1883 CB LEU A 163 7526 5815 6911 -127 -473 278 C
ATOM 1884 CG LEU A 163 12.027 160.718 135.774 1.00 60.47 C
ANISOU 1884 CG LEU A 163 8320 6687 7968 -112 -477 335 C
ATOM 1885 CD1 LEU A 163 11.435 162.080 136.245 1.00 61.54 C
ANISOU 1885 CD1 LEU A 163 8362 6765 8257 -56 -429 368 C
ATOM 1886 CD2 LEU A 163 11.155 159.951 134.736 1.00 62.81 C
ANISOU 1886 CD2 LEU A 163 8607 6970 8289 -194 -615 413 C
ATOM 1887 N GLY A 164 15.908 162.750 134.499 1.00 46.61 N
ANISOU 1887 N GLY A 164 6800 4978 5930 -129 -441 216 N
ATOM 1888 CA GLY A 164 16.884 163.795 134.780 1.00 45.04 C
ANISOU 1888 CA GLY A 164 6615 4777 5722 -105 -401 187 C
ATOM 1889 C GLY A 164 17.013 164.832 133.669 1.00 49.43 C
ANISOU 1889 C GLY A 164 7210 5309 6260 -146 -452 223 C
ATOM 1890 O GLY A 164 17.459 165.949 133.907 1.00 49.39 O
ANISOU 1890 O GLY A 164 7201 5290 6275 -125 -434 217 O
ATOM 1891 N LEU A 165 16.636 164.467 132.445 1.00 44.77 N
ANISOU 1891 N LEU A 165 6686 4706 5621 -220 -523 263 N
ATOM 1892 CA LEU A 165 16.708 165.305 131.262 1.00 44.08 C
ANISOU 1892 CA LEU A 165 6680 4583 5487 -290 -590 307 C
ATOM 1893 C LEU A 165 15.467 166.173 131.131 1.00 52.94 C
ANISOU 1893 C LEU A 165 7733 5661 6723 -286 -710 401 C
ATOM 1894 O LEU A 165 15.487 167.099 130.323 1.00 54.62 O
ANISOU 1894 O LEU A 165 7999 5834 6920 -333 -781 450 O
ATOM 1895 CB LEU A 165 16.866 164.431 129.995 1.00 43.56 C
ANISOU 1895 CB LEU A 165 6767 4496 5286 -402 -616 309 C
ATOM 1896 CG LEU A 165 18.176 163.612 129.808 1.00 45.28 C
ANISOU 1896 CG LEU A 165 7068 4721 5416 -418 -467 221 C
ATOM 1897 CD1 LEU A 165 18.134 162.842 128.490 1.00 44.99 C
ANISOU 1897 CD1 LEU A 165 7225 4631 5236 -546 -471 223 C
ATOM 1898 CD2 LEU A 165 19.444 164.513 129.829 1.00 42.11 C
ANISOU 1898 CD2 LEU A 165 6666 4314 5020 -397 -369 182 C
ATOM 1899 N LEU A 166 14.386 165.905 131.915 1.00 50.11 N
ANISOU 1899 N LEU A 166 7247 5293 6500 -232 -724 435 N
ATOM 1900 CA LEU A 166 13.167 166.729 131.829 1.00 50.45 C
ANISOU 1900 CA LEU A 166 7181 5268 6721 -216 -819 538 C
ATOM 1901 C LEU A 166 13.441 168.248 131.944 1.00 54.13 C
ANISOU 1901 C LEU A 166 7627 5692 7248 -174 -798 549 C
ATOM 1902 O LEU A 166 12.928 168.937 131.074 1.00 55.39 O
ANISOU 1902 O LEU A 166 7786 5792 7468 -222 -935 648 O
ATOM 1903 CB LEU A 166 12.064 166.288 132.799 1.00 50.84 C
ANISOU 1903 CB LEU A 166 7079 5297 6942 -150 -772 559 C
ATOM 1904 CG LEU A 166 11.311 165.009 132.428 1.00 56.81 C
ANISOU 1904 CG LEU A 166 7819 6060 7706 -210 -862 606 C
ATOM 1905 CD1 LEU A 166 10.404 164.594 133.529 1.00 58.19 C
ANISOU 1905 CD1 LEU A 166 7848 6215 8047 -139 -769 608 C
ATOM 1906 CD2 LEU A 166 10.503 165.171 131.151 1.00 60.16 C
ANISOU 1906 CD2 LEU A 166 8246 6422 8189 -311 -1085 743 C
ATOM 1907 N PRO A 167 14.283 168.817 132.867 1.00 48.50 N
ANISOU 1907 N PRO A 167 6923 4998 6506 -108 -659 463 N
ATOM 1908 CA PRO A 167 14.491 170.289 132.858 1.00 48.16 C
ANISOU 1908 CA PRO A 167 6879 4903 6515 -83 -652 480 C
ATOM 1909 C PRO A 167 15.141 170.825 131.592 1.00 55.67 C
ANISOU 1909 C PRO A 167 7945 5853 7356 -167 -747 510 C
ATOM 1910 O PRO A 167 14.897 171.976 131.223 1.00 59.37 O
ANISOU 1910 O PRO A 167 8405 6258 7894 -169 -805 569 O
ATOM 1911 CB PRO A 167 15.352 170.541 134.092 1.00 48.68 C
ANISOU 1911 CB PRO A 167 6970 4991 6534 -27 -502 378 C
ATOM 1912 CG PRO A 167 15.017 169.388 135.008 1.00 52.93 C
ANISOU 1912 CG PRO A 167 7474 5561 7077 2 -430 335 C
ATOM 1913 CD PRO A 167 14.947 168.220 134.042 1.00 48.61 C
ANISOU 1913 CD PRO A 167 6948 5062 6459 -61 -523 362 C
ATOM 1914 N LEU A 168 15.897 169.979 130.879 1.00 50.98 N
ANISOU 1914 N LEU A 168 7464 5309 6595 -244 -755 475 N
ATOM 1915 CA LEU A 168 16.541 170.347 129.615 1.00 50.08 C
ANISOU 1915 CA LEU A 168 7498 5179 6351 -346 -810 494 C
ATOM 1916 C LEU A 168 15.510 170.429 128.520 1.00 55.33 C
ANISOU 1916 C LEU A 168 8211 5781 7032 -438 -1000 615 C
ATOM 1917 O LEU A 168 15.699 171.131 127.546 1.00 54.81 O
ANISOU 1917 O LEU A 168 8265 5667 6892 -526 -1083 665 O
ATOM 1918 CB LEU A 168 17.630 169.332 129.264 1.00 49.45 C
ANISOU 1918 CB LEU A 168 7529 5146 6116 -397 -710 411 C
ATOM 1919 CG LEU A 168 18.983 169.501 129.937 1.00 52.77 C
ANISOU 1919 CG LEU A 168 7928 5603 6521 -348 -561 320 C
ATOM 1920 CD1 LEU A 168 18.896 169.278 131.439 1.00 51.28 C
ANISOU 1920 CD1 LEU A 168 7610 5449 6426 -244 -507 280 C
ATOM 1921 CD2 LEU A 168 19.970 168.519 129.354 1.00 56.74 C
ANISOU 1921 CD2 LEU A 168 8523 6116 6919 -405 -459 262 C
ATOM 1922 N LEU A 169 14.408 169.712 128.695 1.00 56.30 N
ANISOU 1922 N LEU A 169 8243 5892 7257 -429 -1081 672 N
ATOM 1923 CA LEU A 169 13.262 169.694 127.801 1.00 59.04 C
ANISOU 1923 CA LEU A 169 8598 6166 7669 -521 -1303 814 C
ATOM 1924 C LEU A 169 12.240 170.750 128.228 1.00 66.15 C
ANISOU 1924 C LEU A 169 9305 6987 8840 -442 -1380 919 C
ATOM 1925 O LEU A 169 11.280 170.982 127.502 1.00 68.69 O
ANISOU 1925 O LEU A 169 9599 7224 9276 -513 -1595 1067 O
ATOM 1926 CB LEU A 169 12.617 168.303 127.792 1.00 59.62 C
ANISOU 1926 CB LEU A 169 8659 6260 7735 -559 -1349 826 C
ATOM 1927 CG LEU A 169 13.472 167.160 127.271 1.00 65.06 C
ANISOU 1927 CG LEU A 169 9545 6997 8178 -646 -1274 734 C
ATOM 1928 CD1 LEU A 169 12.784 165.857 127.528 1.00 65.90 C
ANISOU 1928 CD1 LEU A 169 9606 7123 8309 -655 -1297 738 C
ATOM 1929 CD2 LEU A 169 13.745 167.300 125.775 1.00 69.01 C
ANISOU 1929 CD2 LEU A 169 10304 7437 8482 -824 -1394 782 C
ATOM 1930 N GLY A 170 12.462 171.383 129.381 1.00 62.34 N
ANISOU 1930 N GLY A 170 8705 6514 8469 -307 -1208 850 N
ATOM 1931 CA GLY A 170 11.599 172.441 129.885 1.00 63.63 C
ANISOU 1931 CA GLY A 170 8694 6580 8902 -218 -1213 927 C
ATOM 1932 C GLY A 170 10.554 172.063 130.915 1.00 68.24 C
ANISOU 1932 C GLY A 170 9078 7128 9725 -118 -1121 940 C
ATOM 1933 O GLY A 170 9.535 172.755 131.046 1.00 70.67 O
ANISOU 1933 O GLY A 170 9216 7319 10316 -66 -1158 1046 O
ATOM 1934 N VAL A 171 10.779 170.975 131.645 1.00 61.49 N
ANISOU 1934 N VAL A 171 8233 6354 8778 -93 -993 840 N
ATOM 1935 CA VAL A 171 9.893 170.579 132.726 1.00 61.27 C
ANISOU 1935 CA VAL A 171 8046 6290 8944 -7 -862 831 C
ATOM 1936 C VAL A 171 10.805 170.606 133.939 1.00 62.69 C
ANISOU 1936 C VAL A 171 8304 6523 8994 59 -633 676 C
ATOM 1937 O VAL A 171 11.592 169.684 134.142 1.00 62.54 O
ANISOU 1937 O VAL A 171 8387 6602 8775 32 -593 587 O
ATOM 1938 CB VAL A 171 9.198 169.205 132.511 1.00 65.78 C
ANISOU 1938 CB VAL A 171 8570 6891 9532 -58 -945 874 C
ATOM 1939 CG1 VAL A 171 8.393 168.778 133.748 1.00 65.61 C
ANISOU 1939 CG1 VAL A 171 8395 6830 9703 31 -768 850 C
ATOM 1940 CG2 VAL A 171 8.314 169.225 131.269 1.00 67.08 C
ANISOU 1940 CG2 VAL A 171 8687 6989 9811 -157 -1220 1046 C
ATOM 1941 N GLY A 172 10.734 171.689 134.696 1.00 56.68 N
ANISOU 1941 N GLY A 172 7508 5682 8345 135 -497 651 N
ATOM 1942 CA GLY A 172 11.571 171.867 135.870 1.00 54.36 C
ANISOU 1942 CA GLY A 172 7321 5412 7920 173 -305 517 C
ATOM 1943 C GLY A 172 12.801 172.675 135.531 1.00 55.56 C
ANISOU 1943 C GLY A 172 7604 5600 7906 141 -341 475 C
ATOM 1944 O GLY A 172 12.934 173.173 134.405 1.00 56.28 O
ANISOU 1944 O GLY A 172 7704 5688 7992 98 -487 545 O
ATOM 1945 N ARG A 173 13.705 172.819 136.507 1.00 49.18 N
ANISOU 1945 N ARG A 173 6908 4817 6963 149 -218 368 N
ATOM 1946 CA ARG A 173 14.929 173.603 136.339 1.00 48.04 C
ANISOU 1946 CA ARG A 173 6875 4697 6679 116 -240 327 C
ATOM 1947 C ARG A 173 15.900 173.303 137.433 1.00 52.02 C
ANISOU 1947 C ARG A 173 7492 5240 7034 99 -153 228 C
ATOM 1948 O ARG A 173 15.508 173.128 138.582 1.00 53.76 O
ANISOU 1948 O ARG A 173 7743 5412 7272 124 -27 182 O
ATOM 1949 CB ARG A 173 14.668 175.139 136.238 1.00 45.68 C
ANISOU 1949 CB ARG A 173 6568 4289 6499 148 -216 362 C
ATOM 1950 CG ARG A 173 13.888 175.719 137.378 1.00 54.67 C
ANISOU 1950 CG ARG A 173 7689 5303 7782 216 -32 334 C
ATOM 1951 CD ARG A 173 13.460 177.141 137.111 1.00 80.01 C
ANISOU 1951 CD ARG A 173 10856 8383 11160 257 -12 389 C
ATOM 1952 NE ARG A 173 12.354 177.514 137.996 1.00 93.68 N
ANISOU 1952 NE ARG A 173 12518 9964 13114 335 187 387 N
ATOM 1953 CZ ARG A 173 12.468 178.327 139.040 1.00106.54 C
ANISOU 1953 CZ ARG A 173 14262 11482 14737 356 389 306 C
ATOM 1954 NH1 ARG A 173 13.635 178.902 139.321 1.00 88.24 N
ANISOU 1954 NH1 ARG A 173 12126 9196 12206 301 380 233 N
ATOM 1955 NH2 ARG A 173 11.413 178.591 139.800 1.00 94.38 N
ANISOU 1955 NH2 ARG A 173 12663 9782 13414 425 611 300 N
ATOM 1956 N TYR A 174 17.170 173.230 137.067 1.00 47.11 N
ANISOU 1956 N TYR A 174 6937 4689 6272 47 -221 202 N
ATOM 1957 CA TYR A 174 18.255 172.970 137.980 1.00 45.56 C
ANISOU 1957 CA TYR A 174 6833 4522 5956 13 -192 136 C
ATOM 1958 C TYR A 174 18.890 174.278 138.405 1.00 50.80 C
ANISOU 1958 C TYR A 174 7585 5125 6590 -7 -169 113 C
ATOM 1959 O TYR A 174 19.256 175.109 137.570 1.00 51.63 O
ANISOU 1959 O TYR A 174 7684 5226 6708 -20 -218 142 O
ATOM 1960 CB TYR A 174 19.281 172.054 137.343 1.00 45.04 C
ANISOU 1960 CB TYR A 174 6756 4548 5808 -30 -270 134 C
ATOM 1961 CG TYR A 174 18.762 170.667 137.054 1.00 46.02 C
ANISOU 1961 CG TYR A 174 6824 4722 5937 -21 -285 144 C
ATOM 1962 CD1 TYR A 174 18.212 169.882 138.067 1.00 48.30 C
ANISOU 1962 CD1 TYR A 174 7116 5006 6232 0 -231 119 C
ATOM 1963 CD2 TYR A 174 18.865 170.112 135.778 1.00 46.09 C
ANISOU 1963 CD2 TYR A 174 6808 4776 5929 -49 -343 174 C
ATOM 1964 CE1 TYR A 174 17.740 168.597 137.812 1.00 46.52 C
ANISOU 1964 CE1 TYR A 174 6842 4822 6010 4 -247 130 C
ATOM 1965 CE2 TYR A 174 18.414 168.817 135.515 1.00 46.97 C
ANISOU 1965 CE2 TYR A 174 6892 4924 6032 -53 -357 180 C
ATOM 1966 CZ TYR A 174 17.870 168.057 136.543 1.00 52.31 C
ANISOU 1966 CZ TYR A 174 7546 5601 6729 -22 -315 160 C
ATOM 1967 OH TYR A 174 17.424 166.778 136.326 1.00 52.49 O
ANISOU 1967 OH TYR A 174 7544 5656 6745 -29 -329 166 O
ATOM 1968 N THR A 175 18.988 174.469 139.717 1.00 47.06 N
ANISOU 1968 N THR A 175 7221 4595 6066 -23 -92 61 N
ATOM 1969 CA THR A 175 19.614 175.640 140.306 1.00 46.70 C
ANISOU 1969 CA THR A 175 7300 4478 5966 -64 -71 33 C
ATOM 1970 C THR A 175 20.541 175.186 141.407 1.00 49.50 C
ANISOU 1970 C THR A 175 7782 4836 6189 -143 -108 -5 C
ATOM 1971 O THR A 175 20.330 174.119 141.988 1.00 47.50 O
ANISOU 1971 O THR A 175 7542 4606 5901 -150 -98 -18 O
ATOM 1972 CB THR A 175 18.570 176.631 140.873 1.00 46.49 C
ANISOU 1972 CB THR A 175 7329 4314 6019 -21 81 13 C
ATOM 1973 OG1 THR A 175 17.724 175.947 141.789 1.00 48.12 O
ANISOU 1973 OG1 THR A 175 7571 4474 6239 -2 208 -20 O
ATOM 1974 CG2 THR A 175 17.745 177.301 139.801 1.00 38.37 C
ANISOU 1974 CG2 THR A 175 6168 3255 5157 49 79 76 C
ATOM 1975 N VAL A 176 21.550 176.021 141.703 1.00 47.72 N
ANISOU 1975 N VAL A 176 7656 4578 5898 -213 -167 -10 N
ATOM 1976 CA VAL A 176 22.522 175.895 142.802 1.00 47.69 C
ANISOU 1976 CA VAL A 176 7801 4543 5775 -320 -246 -24 C
ATOM 1977 C VAL A 176 21.729 175.982 144.123 1.00 54.15 C
ANISOU 1977 C VAL A 176 8822 5248 6506 -350 -117 -81 C
ATOM 1978 O VAL A 176 20.751 176.727 144.221 1.00 55.17 O
ANISOU 1978 O VAL A 176 8996 5288 6679 -300 47 -114 O
ATOM 1979 CB VAL A 176 23.599 176.998 142.707 1.00 50.29 C
ANISOU 1979 CB VAL A 176 8185 4841 6080 -392 -335 -7 C
ATOM 1980 CG1 VAL A 176 24.601 176.885 143.834 1.00 49.93 C
ANISOU 1980 CG1 VAL A 176 8294 4749 5927 -524 -460 2 C
ATOM 1981 CG2 VAL A 176 24.306 176.947 141.354 1.00 49.51 C
ANISOU 1981 CG2 VAL A 176 7898 4837 6077 -364 -411 42 C
ATOM 1982 N GLN A 177 22.103 175.162 145.093 1.00 50.96 N
ANISOU 1982 N GLN A 177 8534 4834 5994 -430 -177 -86 N
ATOM 1983 CA GLN A 177 21.396 175.035 146.352 1.00 51.83 C
ANISOU 1983 CA GLN A 177 8866 4834 5992 -480 -47 -141 C
ATOM 1984 C GLN A 177 22.338 175.324 147.495 1.00 56.14 C
ANISOU 1984 C GLN A 177 9680 5293 6357 -648 -163 -143 C
ATOM 1985 O GLN A 177 23.519 175.023 147.395 1.00 54.39 O
ANISOU 1985 O GLN A 177 9408 5127 6130 -715 -385 -80 O
ATOM 1986 CB GLN A 177 20.862 173.579 146.518 1.00 52.73 C
ANISOU 1986 CB GLN A 177 8909 5010 6117 -448 -34 -135 C
ATOM 1987 CG GLN A 177 19.985 173.011 145.397 1.00 51.91 C
ANISOU 1987 CG GLN A 177 8544 4999 6180 -308 31 -117 C
ATOM 1988 CD GLN A 177 18.664 173.715 145.195 1.00 61.78 C
ANISOU 1988 CD GLN A 177 9756 6170 7546 -221 239 -144 C
ATOM 1989 OE1 GLN A 177 17.922 174.026 146.133 1.00 50.53 O
ANISOU 1989 OE1 GLN A 177 8490 4619 6091 -239 426 -196 O
ATOM 1990 NE2 GLN A 177 18.326 173.930 143.941 1.00 56.41 N
ANISOU 1990 NE2 GLN A 177 8865 5551 7016 -130 214 -101 N
ATOM 1991 N TYR A 178 21.807 175.839 148.605 1.00 55.21 N
ANISOU 1991 N TYR A 178 9856 5023 6100 -727 -12 -208 N
ATOM 1992 CA TYR A 178 22.603 176.117 149.800 1.00 57.68 C
ANISOU 1992 CA TYR A 178 10495 5222 6198 -923 -131 -209 C
ATOM 1993 C TYR A 178 23.296 174.795 150.259 1.00 62.19 C
ANISOU 1993 C TYR A 178 11071 5852 6705 -1010 -355 -143 C
ATOM 1994 O TYR A 178 22.644 173.752 150.233 1.00 61.12 O
ANISOU 1994 O TYR A 178 10851 5768 6605 -943 -282 -151 O
ATOM 1995 CB TYR A 178 21.708 176.742 150.892 1.00 60.74 C
ANISOU 1995 CB TYR A 178 11231 5415 6434 -994 132 -307 C
ATOM 1996 CG TYR A 178 22.318 176.764 152.273 1.00 65.47 C
ANISOU 1996 CG TYR A 178 12244 5876 6757 -1228 27 -314 C
ATOM 1997 CD1 TYR A 178 23.012 177.882 152.733 1.00 68.83 C
ANISOU 1997 CD1 TYR A 178 12926 6184 7045 -1374 -51 -320 C
ATOM 1998 CD2 TYR A 178 22.176 175.679 153.137 1.00 66.79 C
ANISOU 1998 CD2 TYR A 178 12578 6013 6785 -1321 2 -311 C
ATOM 1999 CE1 TYR A 178 23.582 177.903 154.003 1.00 71.98 C
ANISOU 1999 CE1 TYR A 178 13744 6439 7168 -1620 -178 -316 C
ATOM 2000 CE2 TYR A 178 22.755 175.683 154.401 1.00 69.76 C
ANISOU 2000 CE2 TYR A 178 13372 6247 6886 -1563 -127 -304 C
ATOM 2001 CZ TYR A 178 23.454 176.800 154.833 1.00 78.96 C
ANISOU 2001 CZ TYR A 178 14799 7294 7910 -1719 -223 -305 C
ATOM 2002 OH TYR A 178 24.006 176.812 156.088 1.00 81.16 O
ANISOU 2002 OH TYR A 178 15526 7415 7898 -1987 -375 -288 O
ATOM 2003 N PRO A 179 24.608 174.792 150.601 1.00 60.35 N
ANISOU 2003 N PRO A 179 10906 5611 6414 -1152 -640 -64 N
ATOM 2004 CA PRO A 179 25.526 175.953 150.751 1.00 61.49 C
ANISOU 2004 CA PRO A 179 11172 5685 6507 -1268 -776 -37 C
ATOM 2005 C PRO A 179 26.138 176.517 149.456 1.00 64.85 C
ANISOU 2005 C PRO A 179 11286 6218 7136 -1166 -843 6 C
ATOM 2006 O PRO A 179 26.799 177.556 149.491 1.00 67.26 O
ANISOU 2006 O PRO A 179 11678 6465 7414 -1253 -932 25 O
ATOM 2007 CB PRO A 179 26.597 175.414 151.703 1.00 64.22 C
ANISOU 2007 CB PRO A 179 11690 5973 6738 -1472 -1086 56 C
ATOM 2008 CG PRO A 179 26.676 173.933 151.332 1.00 67.20 C
ANISOU 2008 CG PRO A 179 11807 6474 7253 -1384 -1174 116 C
ATOM 2009 CD PRO A 179 25.256 173.532 151.028 1.00 61.54 C
ANISOU 2009 CD PRO A 179 11041 5797 6546 -1230 -867 17 C
ATOM 2010 N GLY A 180 25.908 175.848 148.338 1.00 57.15 N
ANISOU 2010 N GLY A 180 9983 5385 6348 -1000 -796 22 N
ATOM 2011 CA GLY A 180 26.438 176.266 147.049 1.00 55.36 C
ANISOU 2011 CA GLY A 180 9484 5252 6298 -912 -833 59 C
ATOM 2012 C GLY A 180 27.358 175.205 146.491 1.00 58.54 C
ANISOU 2012 C GLY A 180 9635 5756 6851 -892 -1001 145 C
ATOM 2013 O GLY A 180 28.156 175.480 145.590 1.00 59.74 O
ANISOU 2013 O GLY A 180 9591 5960 7147 -866 -1065 192 O
ATOM 2014 N SER A 181 27.234 173.981 147.031 1.00 51.56 N
ANISOU 2014 N SER A 181 8761 4885 5944 -905 -1052 164 N
ATOM 2015 CA SER A 181 28.031 172.815 146.678 1.00 51.17 C
ANISOU 2015 CA SER A 181 8492 4903 6048 -886 -1196 245 C
ATOM 2016 C SER A 181 27.291 171.858 145.751 1.00 55.10 C
ANISOU 2016 C SER A 181 8789 5507 6640 -730 -1047 212 C
ATOM 2017 O SER A 181 27.886 170.878 145.299 1.00 54.65 O
ANISOU 2017 O SER A 181 8539 5500 6725 -696 -1119 267 O
ATOM 2018 CB SER A 181 28.414 172.055 147.943 1.00 55.57 C
ANISOU 2018 CB SER A 181 9216 5385 6515 -1022 -1382 303 C
ATOM 2019 OG SER A 181 27.232 171.746 148.665 1.00 63.61 O
ANISOU 2019 OG SER A 181 10440 6371 7357 -1019 -1236 225 O
ATOM 2020 N TRP A 182 25.993 172.096 145.508 1.00 50.80 N
ANISOU 2020 N TRP A 182 8292 4980 6030 -643 -843 130 N
ATOM 2021 CA TRP A 182 25.188 171.182 144.712 1.00 49.34 C
ANISOU 2021 CA TRP A 182 7948 4882 5916 -518 -725 106 C
ATOM 2022 C TRP A 182 24.041 171.837 144.000 1.00 55.35 C
ANISOU 2022 C TRP A 182 8681 5660 6689 -422 -544 50 C
ATOM 2023 O TRP A 182 23.501 172.849 144.459 1.00 55.45 O
ANISOU 2023 O TRP A 182 8838 5596 6633 -440 -456 10 O
ATOM 2024 CB TRP A 182 24.668 170.014 145.600 1.00 47.57 C
ANISOU 2024 CB TRP A 182 7813 4643 5617 -539 -726 99 C
ATOM 2025 CG TRP A 182 23.746 170.435 146.708 1.00 48.61 C
ANISOU 2025 CG TRP A 182 8201 4680 5587 -592 -615 39 C
ATOM 2026 CD1 TRP A 182 24.038 171.265 147.753 1.00 52.62 C
ANISOU 2026 CD1 TRP A 182 8967 5074 5952 -721 -655 29 C
ATOM 2027 CD2 TRP A 182 22.370 170.083 146.846 1.00 48.10 C
ANISOU 2027 CD2 TRP A 182 8169 4609 5499 -525 -421 -19 C
ATOM 2028 NE1 TRP A 182 22.926 171.454 148.531 1.00 52.61 N
ANISOU 2028 NE1 TRP A 182 9174 4987 5830 -735 -465 -45 N
ATOM 2029 CE2 TRP A 182 21.884 170.739 148.002 1.00 53.42 C
ANISOU 2029 CE2 TRP A 182 9123 5153 6022 -611 -316 -72 C
ATOM 2030 CE3 TRP A 182 21.500 169.248 146.124 1.00 48.55 C
ANISOU 2030 CE3 TRP A 182 8052 4742 5651 -413 -325 -29 C
ATOM 2031 CZ2 TRP A 182 20.565 170.580 148.459 1.00 53.14 C
ANISOU 2031 CZ2 TRP A 182 9175 5058 5958 -576 -89 -134 C
ATOM 2032 CZ3 TRP A 182 20.204 169.080 146.586 1.00 50.80 C
ANISOU 2032 CZ3 TRP A 182 8410 4980 5912 -383 -141 -77 C
ATOM 2033 CH2 TRP A 182 19.744 169.750 147.737 1.00 52.90 C
ANISOU 2033 CH2 TRP A 182 8931 5111 6056 -457 -10 -130 C
ATOM 2034 N CYS A 183 23.657 171.228 142.882 1.00 53.51 N
ANISOU 2034 N CYS A 183 8269 5511 6552 -328 -492 55 N
ATOM 2035 CA CYS A 183 22.518 171.635 142.073 1.00 54.57 C
ANISOU 2035 CA CYS A 183 8346 5661 6728 -242 -365 31 C
ATOM 2036 C CYS A 183 21.446 170.549 142.171 1.00 53.17 C
ANISOU 2036 C CYS A 183 8133 5508 6561 -191 -294 17 C
ATOM 2037 O CYS A 183 21.756 169.381 142.422 1.00 51.90 O
ANISOU 2037 O CYS A 183 7949 5383 6388 -205 -348 29 O
ATOM 2038 CB CYS A 183 22.926 171.902 140.627 1.00 56.35 C
ANISOU 2038 CB CYS A 183 8432 5944 7036 -207 -385 58 C
ATOM 2039 SG CYS A 183 24.035 173.324 140.422 1.00 62.48 S
ANISOU 2039 SG CYS A 183 9241 6682 7815 -265 -442 75 S
ATOM 2040 N PHE A 184 20.188 170.945 142.015 1.00 47.26 N
ANISOU 2040 N PHE A 184 7374 4727 5855 -133 -175 1 N
ATOM 2041 CA PHE A 184 19.053 170.040 142.114 1.00 47.34 C
ANISOU 2041 CA PHE A 184 7337 4746 5904 -88 -98 -4 C
ATOM 2042 C PHE A 184 17.821 170.719 141.516 1.00 53.13 C
ANISOU 2042 C PHE A 184 7987 5440 6761 -19 -5 11 C
ATOM 2043 O PHE A 184 17.905 171.889 141.116 1.00 52.72 O
ANISOU 2043 O PHE A 184 7934 5350 6747 -8 -1 21 O
ATOM 2044 CB PHE A 184 18.807 169.710 143.603 1.00 49.71 C
ANISOU 2044 CB PHE A 184 7802 4975 6111 -137 -26 -45 C
ATOM 2045 CG PHE A 184 18.026 168.461 143.926 1.00 50.67 C
ANISOU 2045 CG PHE A 184 7897 5114 6241 -120 26 -49 C
ATOM 2046 CD1 PHE A 184 18.386 167.228 143.373 1.00 52.14 C
ANISOU 2046 CD1 PHE A 184 7979 5394 6439 -110 -78 -20 C
ATOM 2047 CD2 PHE A 184 16.979 168.496 144.849 1.00 52.35 C
ANISOU 2047 CD2 PHE A 184 8205 5234 6450 -121 196 -85 C
ATOM 2048 CE1 PHE A 184 17.675 166.063 143.695 1.00 51.91 C
ANISOU 2048 CE1 PHE A 184 7935 5377 6413 -101 -35 -22 C
ATOM 2049 CE2 PHE A 184 16.274 167.329 145.175 1.00 54.26 C
ANISOU 2049 CE2 PHE A 184 8425 5488 6702 -113 248 -87 C
ATOM 2050 CZ PHE A 184 16.629 166.124 144.597 1.00 51.23 C
ANISOU 2050 CZ PHE A 184 7933 5209 6322 -104 119 -53 C
ATOM 2051 N LEU A 185 16.675 169.975 141.443 1.00 49.94 N
ANISOU 2051 N LEU A 185 7500 5036 6441 24 57 26 N
ATOM 2052 CA LEU A 185 15.383 170.517 141.008 1.00 49.39 C
ANISOU 2052 CA LEU A 185 7321 4902 6541 87 135 63 C
ATOM 2053 C LEU A 185 15.042 171.711 141.898 1.00 54.05 C
ANISOU 2053 C LEU A 185 8011 5360 7167 98 295 25 C
ATOM 2054 O LEU A 185 15.454 171.754 143.062 1.00 55.03 O
ANISOU 2054 O LEU A 185 8312 5435 7163 46 373 -38 O
ATOM 2055 CB LEU A 185 14.247 169.462 141.035 1.00 49.10 C
ANISOU 2055 CB LEU A 185 7183 4869 6602 116 180 88 C
ATOM 2056 CG LEU A 185 14.133 168.486 142.214 1.00 52.31 C
ANISOU 2056 CG LEU A 185 7684 5266 6925 88 271 37 C
ATOM 2057 CD1 LEU A 185 13.424 169.108 143.411 1.00 52.24 C
ANISOU 2057 CD1 LEU A 185 7774 5117 6957 94 492 -9 C
ATOM 2058 CD2 LEU A 185 13.353 167.244 141.795 1.00 54.65 C
ANISOU 2058 CD2 LEU A 185 7857 5612 7294 103 239 76 C
ATOM 2059 N THR A 186 14.384 172.716 141.336 1.00 51.07 N
ANISOU 2059 N THR A 186 7542 4910 6952 151 332 67 N
ATOM 2060 CA THR A 186 14.070 173.930 142.074 1.00 51.60 C
ANISOU 2060 CA THR A 186 7700 4830 7076 168 503 30 C
ATOM 2061 C THR A 186 12.753 173.774 142.827 1.00 58.60 C
ANISOU 2061 C THR A 186 8553 5590 8125 215 730 18 C
ATOM 2062 O THR A 186 11.713 173.543 142.214 1.00 59.54 O
ANISOU 2062 O THR A 186 8466 5687 8469 279 732 93 O
ATOM 2063 CB THR A 186 14.112 175.113 141.106 1.00 55.68 C
ANISOU 2063 CB THR A 186 8136 5317 7702 202 430 87 C
ATOM 2064 OG1 THR A 186 15.379 175.098 140.466 1.00 60.79 O
ANISOU 2064 OG1 THR A 186 8828 6080 8188 146 250 89 O
ATOM 2065 CG2 THR A 186 13.932 176.428 141.784 1.00 45.40 C
ANISOU 2065 CG2 THR A 186 6935 3855 6458 220 603 48 C
ATOM 2066 N LEU A 187 12.788 173.920 144.153 1.00 57.21 N
ANISOU 2066 N LEU A 187 8584 5311 7841 172 924 -70 N
ATOM 2067 CA LEU A 187 11.589 173.818 144.987 1.00 59.05 C
ANISOU 2067 CA LEU A 187 8821 5394 8221 206 1202 -98 C
ATOM 2068 C LEU A 187 10.758 175.102 144.891 1.00 69.29 C
ANISOU 2068 C LEU A 187 10037 6513 9779 286 1388 -78 C
ATOM 2069 O LEU A 187 10.711 175.894 145.829 1.00 71.28 O
ANISOU 2069 O LEU A 187 10487 6604 9992 263 1621 -157 O
ATOM 2070 CB LEU A 187 11.980 173.474 146.438 1.00 59.12 C
ANISOU 2070 CB LEU A 187 9138 5341 7985 104 1349 -203 C
ATOM 2071 CG LEU A 187 12.688 172.119 146.646 1.00 60.89 C
ANISOU 2071 CG LEU A 187 9430 5710 7994 29 1177 -209 C
ATOM 2072 CD1 LEU A 187 13.133 171.958 148.080 1.00 61.49 C
ANISOU 2072 CD1 LEU A 187 9847 5699 7818 -95 1287 -296 C
ATOM 2073 CD2 LEU A 187 11.803 170.977 146.241 1.00 60.10 C
ANISOU 2073 CD2 LEU A 187 9120 5670 8045 83 1175 -159 C
ATOM 2074 N GLY A 188 10.179 175.323 143.711 1.00 68.84 N
ANISOU 2074 N GLY A 188 9705 6476 9976 367 1266 34 N
ATOM 2075 CA GLY A 188 9.368 176.492 143.376 1.00 70.77 C
ANISOU 2075 CA GLY A 188 9806 6555 10529 454 1381 92 C
ATOM 2076 C GLY A 188 7.896 176.151 143.288 1.00 78.74 C
ANISOU 2076 C GLY A 188 10557 7452 11909 537 1515 173 C
ATOM 2077 O GLY A 188 7.510 174.991 143.470 1.00 78.41 O
ANISOU 2077 O GLY A 188 10456 7472 11864 521 1516 180 O
ATOM 2078 N ALA A 189 7.061 177.157 143.034 1.00 79.20 N
ANISOU 2078 N ALA A 189 10449 7331 12313 624 1631 244 N
ATOM 2079 CA ALA A 189 5.611 176.962 142.943 1.00 81.78 C
ANISOU 2079 CA ALA A 189 10485 7515 13074 709 1762 345 C
ATOM 2080 C ALA A 189 5.118 177.008 141.490 1.00 85.63 C
ANISOU 2080 C ALA A 189 10665 8046 13825 746 1439 535 C
ATOM 2081 O ALA A 189 3.915 176.832 141.241 1.00 87.20 O
ANISOU 2081 O ALA A 189 10578 8127 14426 807 1472 658 O
ATOM 2082 CB ALA A 189 4.879 177.984 143.807 1.00 85.39 C
ANISOU 2082 CB ALA A 189 10951 7690 13803 782 2167 301 C
ATOM 2083 N GLU A 190 6.057 177.208 140.534 1.00 79.52 N
ANISOU 2083 N GLU A 190 9961 7431 12823 693 1120 565 N
ATOM 2084 CA GLU A 190 5.784 177.188 139.097 1.00 78.96 C
ANISOU 2084 CA GLU A 190 9688 7417 12897 683 773 736 C
ATOM 2085 C GLU A 190 5.353 175.764 138.696 1.00 81.80 C
ANISOU 2085 C GLU A 190 9930 7893 13257 638 611 800 C
ATOM 2086 O GLU A 190 5.825 174.779 139.286 1.00 80.10 O
ANISOU 2086 O GLU A 190 9860 7798 12778 592 674 690 O
ATOM 2087 CB GLU A 190 7.032 177.597 138.298 1.00 78.59 C
ANISOU 2087 CB GLU A 190 9812 7515 12533 614 525 719 C
ATOM 2088 N SER A 191 4.426 175.676 137.719 1.00 77.80 N
ANISOU 2088 N SER A 191 9166 7333 13061 643 393 986 N
ATOM 2089 CA SER A 191 3.850 174.459 137.150 1.00 76.35 C
ANISOU 2089 CA SER A 191 8846 7225 12937 588 194 1086 C
ATOM 2090 C SER A 191 4.899 173.343 136.977 1.00 74.11 C
ANISOU 2090 C SER A 191 8787 7174 12196 490 63 983 C
ATOM 2091 O SER A 191 4.708 172.245 137.488 1.00 74.26 O
ANISOU 2091 O SER A 191 8810 7250 12154 473 141 935 O
ATOM 2092 CB SER A 191 3.198 174.790 135.808 1.00 82.86 C
ANISOU 2092 CB SER A 191 9470 7989 14024 556 -146 1307 C
ATOM 2093 OG SER A 191 1.870 174.303 135.722 1.00 98.83 O
ANISOU 2093 OG SER A 191 11207 9903 16440 570 -192 1458 O
ATOM 2094 N GLY A 192 6.007 173.669 136.315 1.00 66.26 N
ANISOU 2094 N GLY A 192 7976 6294 10906 432 -104 947 N
ATOM 2095 CA GLY A 192 7.126 172.776 136.036 1.00 63.24 C
ANISOU 2095 CA GLY A 192 7798 6105 10124 345 -217 857 C
ATOM 2096 C GLY A 192 7.888 172.310 137.259 1.00 66.69 C
ANISOU 2096 C GLY A 192 8406 6612 10322 357 10 682 C
ATOM 2097 O GLY A 192 8.314 171.148 137.301 1.00 67.25 O
ANISOU 2097 O GLY A 192 8554 6805 10193 306 -36 632 O
ATOM 2098 N ASP A 193 8.059 173.206 138.266 1.00 61.20 N
ANISOU 2098 N ASP A 193 7787 5824 9644 414 249 595 N
ATOM 2099 CA ASP A 193 8.716 172.912 139.549 1.00 59.01 C
ANISOU 2099 CA ASP A 193 7705 5572 9145 405 460 441 C
ATOM 2100 C ASP A 193 7.850 171.952 140.359 1.00 61.30 C
ANISOU 2100 C ASP A 193 7933 5821 9538 420 628 423 C
ATOM 2101 O ASP A 193 8.370 171.022 140.966 1.00 59.91 O
ANISOU 2101 O ASP A 193 7897 5732 9135 374 666 336 O
ATOM 2102 CB ASP A 193 8.961 174.198 140.357 1.00 61.63 C
ANISOU 2102 CB ASP A 193 8155 5776 9486 440 669 367 C
ATOM 2103 CG ASP A 193 9.823 175.235 139.668 1.00 79.12 C
ANISOU 2103 CG ASP A 193 10441 8017 11603 423 530 379 C
ATOM 2104 OD1 ASP A 193 10.747 174.838 138.908 1.00 78.44 O
ANISOU 2104 OD1 ASP A 193 10417 8083 11304 361 317 382 O
ATOM 2105 OD2 ASP A 193 9.592 176.448 139.902 1.00 91.06 O
ANISOU 2105 OD2 ASP A 193 11956 9388 13256 470 654 380 O
ATOM 2106 N VAL A 194 6.524 172.162 140.336 1.00 58.89 N
ANISOU 2106 N VAL A 194 7406 5371 9599 482 723 516 N
ATOM 2107 CA VAL A 194 5.557 171.311 141.029 1.00 59.07 C
ANISOU 2107 CA VAL A 194 7331 5330 9783 499 900 516 C
ATOM 2108 C VAL A 194 5.538 169.922 140.362 1.00 63.96 C
ANISOU 2108 C VAL A 194 7894 6103 10307 437 665 569 C
ATOM 2109 O VAL A 194 5.748 168.922 141.047 1.00 63.87 O
ANISOU 2109 O VAL A 194 7992 6157 10119 401 745 489 O
ATOM 2110 CB VAL A 194 4.150 171.967 141.113 1.00 64.19 C
ANISOU 2110 CB VAL A 194 7718 5759 10912 586 1073 619 C
ATOM 2111 CG1 VAL A 194 3.142 171.037 141.782 1.00 64.99 C
ANISOU 2111 CG1 VAL A 194 7699 5792 11204 596 1263 628 C
ATOM 2112 CG2 VAL A 194 4.203 173.308 141.836 1.00 64.63 C
ANISOU 2112 CG2 VAL A 194 7864 5644 11048 646 1351 547 C
ATOM 2113 N ALA A 195 5.344 169.871 139.030 1.00 59.98 N
ANISOU 2113 N ALA A 195 7253 5645 9889 409 368 702 N
ATOM 2114 CA ALA A 195 5.295 168.628 138.259 1.00 58.54 C
ANISOU 2114 CA ALA A 195 7043 5585 9613 334 134 759 C
ATOM 2115 C ALA A 195 6.574 167.766 138.386 1.00 59.69 C
ANISOU 2115 C ALA A 195 7429 5903 9347 273 89 634 C
ATOM 2116 O ALA A 195 6.485 166.557 138.596 1.00 58.67 O
ANISOU 2116 O ALA A 195 7321 5839 9132 237 87 609 O
ATOM 2117 CB ALA A 195 5.020 168.947 136.799 1.00 59.75 C
ANISOU 2117 CB ALA A 195 7092 5739 9873 288 -179 913 C
ATOM 2118 N PHE A 196 7.750 168.391 138.275 1.00 54.95 N
ANISOU 2118 N PHE A 196 6994 5362 8523 262 58 564 N
ATOM 2119 CA PHE A 196 9.010 167.678 138.363 1.00 52.70 C
ANISOU 2119 CA PHE A 196 6900 5214 7908 210 12 465 C
ATOM 2120 C PHE A 196 9.323 167.287 139.790 1.00 56.47 C
ANISOU 2120 C PHE A 196 7501 5686 8269 222 222 349 C
ATOM 2121 O PHE A 196 9.816 166.190 140.003 1.00 56.00 O
ANISOU 2121 O PHE A 196 7522 5714 8041 182 190 304 O
ATOM 2122 CB PHE A 196 10.151 168.509 137.758 1.00 53.95 C
ANISOU 2122 CB PHE A 196 7172 5422 7906 189 -87 441 C
ATOM 2123 CG PHE A 196 11.450 167.755 137.580 1.00 54.83 C
ANISOU 2123 CG PHE A 196 7432 5660 7741 134 -159 369 C
ATOM 2124 CD1 PHE A 196 11.474 166.510 136.950 1.00 56.38 C
ANISOU 2124 CD1 PHE A 196 7630 5934 7859 83 -271 388 C
ATOM 2125 CD2 PHE A 196 12.656 168.308 137.999 1.00 57.55 C
ANISOU 2125 CD2 PHE A 196 7908 6031 7926 129 -115 290 C
ATOM 2126 CE1 PHE A 196 12.673 165.824 136.766 1.00 56.03 C
ANISOU 2126 CE1 PHE A 196 7704 5979 7604 42 -309 326 C
ATOM 2127 CE2 PHE A 196 13.859 167.619 137.812 1.00 59.53 C
ANISOU 2127 CE2 PHE A 196 8257 6378 7984 84 -178 241 C
ATOM 2128 CZ PHE A 196 13.857 166.382 137.186 1.00 55.94 C
ANISOU 2128 CZ PHE A 196 7790 5988 7476 47 -262 258 C
ATOM 2129 N GLY A 197 9.052 168.178 140.748 1.00 53.44 N
ANISOU 2129 N GLY A 197 7151 5184 7968 265 434 305 N
ATOM 2130 CA GLY A 197 9.256 167.914 142.168 1.00 53.46 C
ANISOU 2130 CA GLY A 197 7320 5147 7846 250 645 199 C
ATOM 2131 C GLY A 197 8.408 166.749 142.655 1.00 58.79 C
ANISOU 2131 C GLY A 197 7937 5810 8590 242 735 205 C
ATOM 2132 O GLY A 197 8.895 165.897 143.394 1.00 57.85 O
ANISOU 2132 O GLY A 197 7970 5741 8271 193 765 137 O
ATOM 2133 N LEU A 198 7.136 166.690 142.221 1.00 57.37 N
ANISOU 2133 N LEU A 198 7529 5556 8711 283 759 300 N
ATOM 2134 CA LEU A 198 6.221 165.619 142.588 1.00 57.97 C
ANISOU 2134 CA LEU A 198 7516 5611 8899 273 841 323 C
ATOM 2135 C LEU A 198 6.565 164.368 141.822 1.00 64.00 C
ANISOU 2135 C LEU A 198 8271 6526 9520 218 598 354 C
ATOM 2136 O LEU A 198 6.477 163.288 142.382 1.00 63.19 O
ANISOU 2136 O LEU A 198 8228 6455 9327 184 650 317 O
ATOM 2137 CB LEU A 198 4.754 166.005 142.350 1.00 59.36 C
ANISOU 2137 CB LEU A 198 7421 5642 9492 331 933 433 C
ATOM 2138 CG LEU A 198 4.153 167.041 143.291 1.00 64.82 C
ANISOU 2138 CG LEU A 198 8102 6136 10389 392 1267 396 C
ATOM 2139 CD1 LEU A 198 2.763 167.401 142.853 1.00 67.26 C
ANISOU 2139 CD1 LEU A 198 8086 6297 11171 456 1315 536 C
ATOM 2140 CD2 LEU A 198 4.150 166.570 144.741 1.00 64.65 C
ANISOU 2140 CD2 LEU A 198 8288 6053 10223 360 1569 270 C
ATOM 2141 N LEU A 199 6.991 164.495 140.549 1.00 61.65 N
ANISOU 2141 N LEU A 199 7929 6311 9185 200 344 418 N
ATOM 2142 CA LEU A 199 7.386 163.321 139.760 1.00 60.38 C
ANISOU 2142 CA LEU A 199 7798 6274 8869 137 137 436 C
ATOM 2143 C LEU A 199 8.541 162.594 140.430 1.00 61.31 C
ANISOU 2143 C LEU A 199 8118 6479 8698 108 171 325 C
ATOM 2144 O LEU A 199 8.495 161.375 140.571 1.00 61.22 O
ANISOU 2144 O LEU A 199 8130 6515 8615 73 147 314 O
ATOM 2145 CB LEU A 199 7.746 163.711 138.324 1.00 60.38 C
ANISOU 2145 CB LEU A 199 7779 6322 8840 104 -102 507 C
ATOM 2146 CG LEU A 199 7.947 162.599 137.311 1.00 65.51 C
ANISOU 2146 CG LEU A 199 8467 7060 9365 24 -301 541 C
ATOM 2147 CD1 LEU A 199 6.946 161.464 137.481 1.00 66.52 C
ANISOU 2147 CD1 LEU A 199 8496 7170 9607 -2 -304 589 C
ATOM 2148 CD2 LEU A 199 7.842 163.155 135.923 1.00 71.13 C
ANISOU 2148 CD2 LEU A 199 9151 7762 10113 -26 -514 639 C
ATOM 2149 N PHE A 200 9.533 163.346 140.907 1.00 56.06 N
ANISOU 2149 N PHE A 200 7591 5820 7891 118 224 252 N
ATOM 2150 CA PHE A 200 10.674 162.779 141.603 1.00 54.36 C
ANISOU 2150 CA PHE A 200 7554 5664 7437 84 229 168 C
ATOM 2151 C PHE A 200 10.288 162.111 142.940 1.00 60.62 C
ANISOU 2151 C PHE A 200 8434 6406 8192 65 394 118 C
ATOM 2152 O PHE A 200 10.688 160.970 143.184 1.00 59.69 O
ANISOU 2152 O PHE A 200 8386 6345 7949 28 342 98 O
ATOM 2153 CB PHE A 200 11.758 163.846 141.792 1.00 54.46 C
ANISOU 2153 CB PHE A 200 7681 5674 7339 84 225 122 C
ATOM 2154 CG PHE A 200 13.008 163.353 142.482 1.00 54.13 C
ANISOU 2154 CG PHE A 200 7802 5676 7087 38 190 62 C
ATOM 2155 CD1 PHE A 200 13.964 162.622 141.786 1.00 53.92 C
ANISOU 2155 CD1 PHE A 200 7774 5741 6972 17 40 70 C
ATOM 2156 CD2 PHE A 200 13.241 163.643 143.826 1.00 55.97 C
ANISOU 2156 CD2 PHE A 200 8201 5839 7225 6 305 6 C
ATOM 2157 CE1 PHE A 200 15.126 162.188 142.421 1.00 54.46 C
ANISOU 2157 CE1 PHE A 200 7956 5830 6905 -21 -8 36 C
ATOM 2158 CE2 PHE A 200 14.414 163.217 144.457 1.00 57.43 C
ANISOU 2158 CE2 PHE A 200 8534 6051 7237 -53 224 -24 C
ATOM 2159 CZ PHE A 200 15.348 162.497 143.748 1.00 54.31 C
ANISOU 2159 CZ PHE A 200 8088 5747 6801 -59 60 -1 C
ATOM 2160 N SER A 201 9.514 162.820 143.788 1.00 59.70 N
ANISOU 2160 N SER A 201 8328 6169 8187 87 605 99 N
ATOM 2161 CA SER A 201 9.092 162.337 145.099 1.00 60.93 C
ANISOU 2161 CA SER A 201 8608 6246 8298 54 806 45 C
ATOM 2162 C SER A 201 8.058 161.195 145.033 1.00 67.07 C
ANISOU 2162 C SER A 201 9259 7023 9202 51 839 88 C
ATOM 2163 O SER A 201 8.147 160.265 145.841 1.00 65.46 O
ANISOU 2163 O SER A 201 9184 6822 8867 -1 894 48 O
ATOM 2164 CB SER A 201 8.610 163.491 145.964 1.00 64.95 C
ANISOU 2164 CB SER A 201 9191 6599 8887 70 1061 2 C
ATOM 2165 OG SER A 201 7.537 164.151 145.319 1.00 77.83 O
ANISOU 2165 OG SER A 201 10587 8157 10829 144 1129 72 O
ATOM 2166 N MET A 202 7.109 161.244 144.067 1.00 66.82 N
ANISOU 2166 N MET A 202 8985 6984 9420 92 781 180 N
ATOM 2167 CA MET A 202 6.122 160.178 143.870 1.00 69.10 C
ANISOU 2167 CA MET A 202 9132 7272 9849 77 773 239 C
ATOM 2168 C MET A 202 6.834 158.916 143.387 1.00 68.48 C
ANISOU 2168 C MET A 202 9122 7328 9570 27 566 235 C
ATOM 2169 O MET A 202 6.563 157.847 143.924 1.00 67.70 O
ANISOU 2169 O MET A 202 9064 7233 9425 -9 615 219 O
ATOM 2170 CB MET A 202 4.982 160.556 142.894 1.00 74.30 C
ANISOU 2170 CB MET A 202 9513 7878 10839 113 706 363 C
ATOM 2171 CG MET A 202 4.049 161.677 143.379 1.00 82.74 C
ANISOU 2171 CG MET A 202 10456 8779 12201 175 944 387 C
ATOM 2172 SD MET A 202 3.587 161.570 145.124 1.00 91.86 S
ANISOU 2172 SD MET A 202 11762 9795 13346 168 1352 281 S
ATOM 2173 CE MET A 202 2.723 163.166 145.348 1.00 90.69 C
ANISOU 2173 CE MET A 202 11464 9434 13561 255 1619 310 C
ATOM 2174 N LEU A 203 7.776 159.038 142.420 1.00 62.09 N
ANISOU 2174 N LEU A 203 8337 6613 8641 23 360 243 N
ATOM 2175 CA LEU A 203 8.539 157.886 141.921 1.00 59.88 C
ANISOU 2175 CA LEU A 203 8129 6436 8188 -20 198 232 C
ATOM 2176 C LEU A 203 9.341 157.186 143.012 1.00 62.01 C
ANISOU 2176 C LEU A 203 8578 6722 8260 -46 258 155 C
ATOM 2177 O LEU A 203 9.262 155.963 143.109 1.00 60.63 O
ANISOU 2177 O LEU A 203 8426 6575 8035 -79 225 156 O
ATOM 2178 CB LEU A 203 9.427 158.221 140.716 1.00 58.71 C
ANISOU 2178 CB LEU A 203 7990 6358 7960 -24 20 247 C
ATOM 2179 CG LEU A 203 8.767 158.074 139.352 1.00 63.80 C
ANISOU 2179 CG LEU A 203 8518 7012 8711 -54 -137 338 C
ATOM 2180 CD1 LEU A 203 9.572 158.795 138.279 1.00 64.02 C
ANISOU 2180 CD1 LEU A 203 8583 7072 8668 -64 -261 348 C
ATOM 2181 CD2 LEU A 203 8.559 156.601 138.983 1.00 64.75 C
ANISOU 2181 CD2 LEU A 203 8659 7171 8771 -111 -220 351 C
ATOM 2182 N GLY A 204 10.053 157.962 143.842 1.00 58.22 N
ANISOU 2182 N GLY A 204 8231 6210 7679 -43 333 99 N
ATOM 2183 CA GLY A 204 10.831 157.441 144.965 1.00 57.93 C
ANISOU 2183 CA GLY A 204 8389 6165 7458 -90 358 45 C
ATOM 2184 C GLY A 204 9.947 156.870 146.065 1.00 64.18 C
ANISOU 2184 C GLY A 204 9252 6880 8255 -127 530 26 C
ATOM 2185 O GLY A 204 10.228 155.789 146.581 1.00 64.19 O
ANISOU 2185 O GLY A 204 9354 6896 8141 -174 495 15 O
ATOM 2186 N GLY A 205 8.869 157.592 146.406 1.00 61.54 N
ANISOU 2186 N GLY A 205 8860 6449 8072 -105 729 26 N
ATOM 2187 CA GLY A 205 7.891 157.177 147.401 1.00 62.11 C
ANISOU 2187 CA GLY A 205 8987 6422 8191 -139 951 6 C
ATOM 2188 C GLY A 205 7.276 155.843 147.040 1.00 67.32 C
ANISOU 2188 C GLY A 205 9533 7127 8918 -153 892 52 C
ATOM 2189 O GLY A 205 7.345 154.897 147.827 1.00 67.41 O
ANISOU 2189 O GLY A 205 9685 7126 8802 -213 932 26 O
ATOM 2190 N LEU A 206 6.729 155.740 145.815 1.00 65.05 N
ANISOU 2190 N LEU A 206 9012 6891 8813 -111 770 126 N
ATOM 2191 CA LEU A 206 6.119 154.517 145.280 1.00 66.03 C
ANISOU 2191 CA LEU A 206 9023 7056 9009 -135 680 180 C
ATOM 2192 C LEU A 206 7.092 153.349 145.245 1.00 71.09 C
ANISOU 2192 C LEU A 206 9800 7784 9427 -176 527 154 C
ATOM 2193 O LEU A 206 6.665 152.220 145.467 1.00 71.75 O
ANISOU 2193 O LEU A 206 9889 7868 9504 -216 534 166 O
ATOM 2194 CB LEU A 206 5.538 154.753 143.878 1.00 66.33 C
ANISOU 2194 CB LEU A 206 8835 7124 9245 -110 524 274 C
ATOM 2195 CG LEU A 206 4.028 155.021 143.741 1.00 73.28 C
ANISOU 2195 CG LEU A 206 9484 7907 10452 -96 622 360 C
ATOM 2196 CD1 LEU A 206 3.523 156.088 144.715 1.00 74.85 C
ANISOU 2196 CD1 LEU A 206 9675 7974 10792 -52 907 327 C
ATOM 2197 CD2 LEU A 206 3.696 155.462 142.326 1.00 77.18 C
ANISOU 2197 CD2 LEU A 206 9796 8421 11108 -88 407 464 C
ATOM 2198 N SER A 207 8.395 153.610 144.984 1.00 66.65 N
ANISOU 2198 N SER A 207 9335 7283 8707 -166 398 123 N
ATOM 2199 CA SER A 207 9.430 152.569 144.956 1.00 64.82 C
ANISOU 2199 CA SER A 207 9211 7110 8308 -193 263 105 C
ATOM 2200 C SER A 207 9.600 151.946 146.338 1.00 67.78 C
ANISOU 2200 C SER A 207 9766 7433 8553 -247 347 70 C
ATOM 2201 O SER A 207 9.683 150.722 146.449 1.00 68.29 O
ANISOU 2201 O SER A 207 9872 7513 8561 -280 290 79 O
ATOM 2202 CB SER A 207 10.759 153.136 144.467 1.00 66.49 C
ANISOU 2202 CB SER A 207 9460 7368 8433 -169 140 89 C
ATOM 2203 OG SER A 207 10.742 153.255 143.055 1.00 75.03 O
ANISOU 2203 OG SER A 207 10420 8502 9587 -145 35 122 O
ATOM 2204 N VAL A 208 9.635 152.787 147.380 1.00 62.86 N
ANISOU 2204 N VAL A 208 9275 6736 7873 -269 480 33 N
ATOM 2205 CA VAL A 208 9.767 152.364 148.771 1.00 63.80 C
ANISOU 2205 CA VAL A 208 9625 6781 7836 -350 565 1 C
ATOM 2206 C VAL A 208 8.456 151.671 149.262 1.00 69.50 C
ANISOU 2206 C VAL A 208 10332 7441 8632 -383 747 3 C
ATOM 2207 O VAL A 208 8.526 150.639 149.931 1.00 69.35 O
ANISOU 2207 O VAL A 208 10448 7403 8500 -449 736 2 O
ATOM 2208 CB VAL A 208 10.255 153.523 149.690 1.00 67.95 C
ANISOU 2208 CB VAL A 208 10345 7229 8246 -389 647 -43 C
ATOM 2209 CG1 VAL A 208 10.477 153.041 151.125 1.00 68.95 C
ANISOU 2209 CG1 VAL A 208 10767 7262 8168 -507 702 -68 C
ATOM 2210 CG2 VAL A 208 11.536 154.150 149.143 1.00 66.30 C
ANISOU 2210 CG2 VAL A 208 10120 7081 7990 -360 454 -33 C
ATOM 2211 N GLY A 209 7.301 152.213 148.867 1.00 66.91 N
ANISOU 2211 N GLY A 209 9825 7079 8520 -339 896 20 N
ATOM 2212 CA GLY A 209 5.985 151.673 149.199 1.00 68.22 C
ANISOU 2212 CA GLY A 209 9916 7175 8828 -362 1082 36 C
ATOM 2213 C GLY A 209 5.749 150.309 148.587 1.00 72.97 C
ANISOU 2213 C GLY A 209 10415 7849 9460 -375 936 85 C
ATOM 2214 O GLY A 209 5.272 149.390 149.263 1.00 74.72 O
ANISOU 2214 O GLY A 209 10712 8028 9651 -435 1028 82 O
ATOM 2215 N LEU A 210 6.120 150.160 147.310 1.00 67.71 N
ANISOU 2215 N LEU A 210 9607 7284 8836 -331 713 126 N
ATOM 2216 CA LEU A 210 6.041 148.892 146.599 1.00 67.44 C
ANISOU 2216 CA LEU A 210 9509 7311 8803 -352 560 165 C
ATOM 2217 C LEU A 210 6.962 147.887 147.277 1.00 69.72 C
ANISOU 2217 C LEU A 210 10004 7614 8874 -397 495 130 C
ATOM 2218 O LEU A 210 6.558 146.748 147.463 1.00 69.87 O
ANISOU 2218 O LEU A 210 10043 7624 8883 -442 495 146 O
ATOM 2219 CB LEU A 210 6.438 149.076 145.117 1.00 67.20 C
ANISOU 2219 CB LEU A 210 9354 7363 8816 -314 355 201 C
ATOM 2220 CG LEU A 210 6.370 147.854 144.186 1.00 72.09 C
ANISOU 2220 CG LEU A 210 9935 8031 9426 -348 196 237 C
ATOM 2221 CD1 LEU A 210 4.914 147.435 143.893 1.00 73.32 C
ANISOU 2221 CD1 LEU A 210 9932 8149 9776 -388 221 308 C
ATOM 2222 CD2 LEU A 210 7.127 148.118 142.903 1.00 73.37 C
ANISOU 2222 CD2 LEU A 210 10075 8253 9548 -327 26 245 C
ATOM 2223 N SER A 211 8.187 148.309 147.661 1.00 65.29 N
ANISOU 2223 N SER A 211 9587 7062 8159 -391 428 96 N
ATOM 2224 CA SER A 211 9.161 147.453 148.334 1.00 65.09 C
ANISOU 2224 CA SER A 211 9743 7029 7960 -436 332 86 C
ATOM 2225 C SER A 211 8.601 146.930 149.649 1.00 73.89 C
ANISOU 2225 C SER A 211 11031 8056 8988 -521 474 73 C
ATOM 2226 O SER A 211 8.802 145.760 149.964 1.00 74.49 O
ANISOU 2226 O SER A 211 11195 8124 8985 -567 404 89 O
ATOM 2227 CB SER A 211 10.462 148.201 148.582 1.00 67.57 C
ANISOU 2227 CB SER A 211 10157 7346 8170 -426 233 72 C
ATOM 2228 OG SER A 211 11.274 148.192 147.425 1.00 77.20 O
ANISOU 2228 OG SER A 211 11259 8638 9437 -365 78 87 O
ATOM 2229 N PHE A 212 7.864 147.783 150.396 1.00 72.97 N
ANISOU 2229 N PHE A 212 10971 7860 8892 -547 693 43 N
ATOM 2230 CA PHE A 212 7.227 147.416 151.652 1.00 74.31 C
ANISOU 2230 CA PHE A 212 11332 7923 8980 -642 888 20 C
ATOM 2231 C PHE A 212 6.155 146.333 151.451 1.00 76.58 C
ANISOU 2231 C PHE A 212 11500 8209 9386 -657 956 50 C
ATOM 2232 O PHE A 212 6.230 145.291 152.095 1.00 77.19 O
ANISOU 2232 O PHE A 212 11729 8258 9341 -731 932 55 O
ATOM 2233 CB PHE A 212 6.677 148.647 152.381 1.00 78.16 C
ANISOU 2233 CB PHE A 212 11909 8303 9485 -662 1151 -28 C
ATOM 2234 CG PHE A 212 6.303 148.308 153.798 1.00 83.25 C
ANISOU 2234 CG PHE A 212 12845 8815 9973 -788 1357 -65 C
ATOM 2235 CD1 PHE A 212 7.257 148.324 154.807 1.00 88.64 C
ANISOU 2235 CD1 PHE A 212 13865 9437 10376 -896 1281 -86 C
ATOM 2236 CD2 PHE A 212 5.010 147.896 154.115 1.00 88.37 C
ANISOU 2236 CD2 PHE A 212 13441 9385 10751 -816 1613 -69 C
ATOM 2237 CE1 PHE A 212 6.921 147.953 156.117 1.00 92.31 C
ANISOU 2237 CE1 PHE A 212 14651 9764 10658 -1041 1460 -117 C
ATOM 2238 CE2 PHE A 212 4.677 147.515 155.419 1.00 93.58 C
ANISOU 2238 CE2 PHE A 212 14401 9909 11246 -948 1824 -108 C
ATOM 2239 CZ PHE A 212 5.633 147.550 156.413 1.00 92.55 C
ANISOU 2239 CZ PHE A 212 14643 9718 10803 -1066 1748 -135 C
ATOM 2240 N LEU A 213 5.191 146.570 150.545 1.00 71.97 N
ANISOU 2240 N LEU A 213 10647 7651 9047 -595 1010 81 N
ATOM 2241 CA LEU A 213 4.109 145.645 150.196 1.00 72.10 C
ANISOU 2241 CA LEU A 213 10509 7665 9220 -614 1047 127 C
ATOM 2242 C LEU A 213 4.612 144.267 149.793 1.00 73.56 C
ANISOU 2242 C LEU A 213 10731 7918 9301 -638 834 151 C
ATOM 2243 O LEU A 213 4.182 143.262 150.372 1.00 73.73 O
ANISOU 2243 O LEU A 213 10836 7897 9280 -707 895 157 O
ATOM 2244 CB LEU A 213 3.294 146.220 149.038 1.00 72.59 C
ANISOU 2244 CB LEU A 213 10264 7754 9561 -547 1026 184 C
ATOM 2245 CG LEU A 213 1.962 146.844 149.385 1.00 80.40 C
ANISOU 2245 CG LEU A 213 11107 8633 10808 -544 1294 205 C
ATOM 2246 CD1 LEU A 213 2.140 148.238 149.977 1.00 81.39 C
ANISOU 2246 CD1 LEU A 213 11310 8685 10929 -510 1479 151 C
ATOM 2247 CD2 LEU A 213 1.099 146.940 148.146 1.00 84.69 C
ANISOU 2247 CD2 LEU A 213 11329 9201 11647 -506 1185 301 C
ATOM 2248 N LEU A 214 5.513 144.216 148.794 1.00 67.24 N
ANISOU 2248 N LEU A 214 9874 7209 8466 -585 606 162 N
ATOM 2249 CA LEU A 214 6.054 142.956 148.279 1.00 65.24 C
ANISOU 2249 CA LEU A 214 9648 7002 8138 -598 425 180 C
ATOM 2250 C LEU A 214 6.894 142.193 149.308 1.00 69.84 C
ANISOU 2250 C LEU A 214 10465 7545 8526 -648 387 162 C
ATOM 2251 O LEU A 214 6.848 140.964 149.343 1.00 71.27 O
ANISOU 2251 O LEU A 214 10691 7716 8671 -686 330 181 O
ATOM 2252 CB LEU A 214 6.852 143.171 146.983 1.00 63.18 C
ANISOU 2252 CB LEU A 214 9294 6819 7893 -534 241 187 C
ATOM 2253 CG LEU A 214 6.180 143.931 145.835 1.00 66.72 C
ANISOU 2253 CG LEU A 214 9541 7303 8507 -500 217 218 C
ATOM 2254 CD1 LEU A 214 7.185 144.263 144.772 1.00 66.42 C
ANISOU 2254 CD1 LEU A 214 9488 7322 8425 -453 66 209 C
ATOM 2255 CD2 LEU A 214 5.012 143.176 145.230 1.00 66.33 C
ANISOU 2255 CD2 LEU A 214 9368 7246 8590 -550 195 274 C
ATOM 2256 N ASN A 215 7.654 142.912 150.135 1.00 64.77 N
ANISOU 2256 N ASN A 215 9977 6868 7763 -658 402 137 N
ATOM 2257 CA ASN A 215 8.524 142.297 151.125 1.00 64.31 C
ANISOU 2257 CA ASN A 215 10153 6757 7526 -724 318 143 C
ATOM 2258 C ASN A 215 7.774 141.692 152.274 1.00 69.26 C
ANISOU 2258 C ASN A 215 10957 7295 8064 -830 463 140 C
ATOM 2259 O ASN A 215 8.197 140.657 152.770 1.00 69.48 O
ANISOU 2259 O ASN A 215 11129 7287 7985 -888 360 167 O
ATOM 2260 CB ASN A 215 9.580 143.283 151.614 1.00 64.96 C
ANISOU 2260 CB ASN A 215 10358 6819 7505 -726 252 132 C
ATOM 2261 CG ASN A 215 10.736 143.466 150.664 1.00 71.35 C
ANISOU 2261 CG ASN A 215 11046 7696 8369 -641 56 150 C
ATOM 2262 OD1 ASN A 215 11.012 142.646 149.781 1.00 67.92 O
ANISOU 2262 OD1 ASN A 215 10495 7304 8008 -593 -48 169 O
ATOM 2263 ND2 ASN A 215 11.466 144.522 150.858 1.00 59.73 N
ANISOU 2263 ND2 ASN A 215 9618 6219 6858 -632 17 141 N
ATOM 2264 N THR A 216 6.664 142.323 152.707 1.00 66.71 N
ANISOU 2264 N THR A 216 10627 6919 7799 -859 715 110 N
ATOM 2265 CA THR A 216 5.846 141.806 153.807 1.00 67.79 C
ANISOU 2265 CA THR A 216 10941 6952 7863 -970 913 99 C
ATOM 2266 C THR A 216 5.212 140.483 153.355 1.00 70.73 C
ANISOU 2266 C THR A 216 11198 7352 8325 -979 878 136 C
ATOM 2267 O THR A 216 5.359 139.474 154.058 1.00 71.54 O
ANISOU 2267 O THR A 216 11488 7402 8292 -1066 849 151 O
ATOM 2268 CB THR A 216 4.891 142.877 154.356 1.00 81.34 C
ANISOU 2268 CB THR A 216 12673 8582 9652 -992 1230 54 C
ATOM 2269 OG1 THR A 216 4.214 143.506 153.275 1.00 85.24 O
ANISOU 2269 OG1 THR A 216 12843 9134 10411 -885 1274 68 O
ATOM 2270 CG2 THR A 216 5.629 143.966 155.145 1.00 81.03 C
ANISOU 2270 CG2 THR A 216 12872 8478 9437 -1032 1267 11 C
ATOM 2271 N VAL A 217 4.652 140.449 152.118 1.00 64.22 N
ANISOU 2271 N VAL A 217 10084 6607 7711 -899 834 161 N
ATOM 2272 CA VAL A 217 4.081 139.232 151.526 1.00 62.58 C
ANISOU 2272 CA VAL A 217 9763 6425 7590 -915 769 201 C
ATOM 2273 C VAL A 217 5.146 138.121 151.400 1.00 65.69 C
ANISOU 2273 C VAL A 217 10275 6844 7841 -921 541 216 C
ATOM 2274 O VAL A 217 4.858 136.977 151.743 1.00 66.98 O
ANISOU 2274 O VAL A 217 10520 6970 7961 -986 538 236 O
ATOM 2275 CB VAL A 217 3.324 139.488 150.197 1.00 64.98 C
ANISOU 2275 CB VAL A 217 9767 6791 8132 -855 733 236 C
ATOM 2276 CG1 VAL A 217 2.668 138.210 149.679 1.00 64.64 C
ANISOU 2276 CG1 VAL A 217 9645 6756 8161 -902 665 282 C
ATOM 2277 CG2 VAL A 217 2.274 140.583 150.364 1.00 65.74 C
ANISOU 2277 CG2 VAL A 217 9720 6837 8421 -843 957 240 C
ATOM 2278 N SER A 218 6.375 138.462 150.966 1.00 59.91 N
ANISOU 2278 N SER A 218 9551 6158 7054 -855 366 211 N
ATOM 2279 CA SER A 218 7.490 137.507 150.824 1.00 58.35 C
ANISOU 2279 CA SER A 218 9434 5960 6776 -844 165 233 C
ATOM 2280 C SER A 218 7.965 136.932 152.171 1.00 63.82 C
ANISOU 2280 C SER A 218 10386 6561 7300 -934 135 253 C
ATOM 2281 O SER A 218 8.212 135.723 152.268 1.00 61.79 O
ANISOU 2281 O SER A 218 10197 6271 7012 -962 36 286 O
ATOM 2282 CB SER A 218 8.665 138.158 150.111 1.00 57.31 C
ANISOU 2282 CB SER A 218 9232 5877 6666 -754 25 227 C
ATOM 2283 OG SER A 218 8.221 138.645 148.862 1.00 63.82 O
ANISOU 2283 OG SER A 218 9855 6773 7620 -692 40 214 O
ATOM 2284 N VAL A 219 8.129 137.803 153.196 1.00 61.86 N
ANISOU 2284 N VAL A 219 10306 6261 6937 -989 209 238 N
ATOM 2285 CA VAL A 219 8.556 137.351 154.520 1.00 63.09 C
ANISOU 2285 CA VAL A 219 10757 6311 6902 -1108 165 266 C
ATOM 2286 C VAL A 219 7.494 136.408 155.080 1.00 67.98 C
ANISOU 2286 C VAL A 219 11473 6873 7484 -1202 310 267 C
ATOM 2287 O VAL A 219 7.843 135.314 155.511 1.00 69.23 O
ANISOU 2287 O VAL A 219 11763 6980 7562 -1260 187 313 O
ATOM 2288 CB VAL A 219 8.883 138.504 155.490 1.00 67.83 C
ANISOU 2288 CB VAL A 219 11564 6850 7359 -1177 225 245 C
ATOM 2289 CG1 VAL A 219 9.129 137.970 156.902 1.00 69.48 C
ANISOU 2289 CG1 VAL A 219 12132 6927 7339 -1343 191 278 C
ATOM 2290 CG2 VAL A 219 10.089 139.300 155.002 1.00 66.76 C
ANISOU 2290 CG2 VAL A 219 11348 6761 7257 -1097 38 259 C
ATOM 2291 N ALA A 220 6.204 136.809 155.015 1.00 63.72 N
ANISOU 2291 N ALA A 220 10842 6336 7034 -1212 569 227 N
ATOM 2292 CA ALA A 220 5.079 136.014 155.492 1.00 64.44 C
ANISOU 2292 CA ALA A 220 10983 6366 7133 -1301 748 228 C
ATOM 2293 C ALA A 220 5.011 134.653 154.770 1.00 69.82 C
ANISOU 2293 C ALA A 220 11548 7089 7889 -1278 600 270 C
ATOM 2294 O ALA A 220 4.766 133.635 155.429 1.00 71.57 O
ANISOU 2294 O ALA A 220 11929 7243 8021 -1373 617 293 O
ATOM 2295 CB ALA A 220 3.779 136.787 155.334 1.00 65.60 C
ANISOU 2295 CB ALA A 220 10961 6508 7456 -1285 1033 194 C
ATOM 2296 N THR A 221 5.309 134.620 153.448 1.00 64.11 N
ANISOU 2296 N THR A 221 10587 6465 7308 -1164 453 278 N
ATOM 2297 CA THR A 221 5.334 133.376 152.671 1.00 62.82 C
ANISOU 2297 CA THR A 221 10340 6327 7202 -1145 317 308 C
ATOM 2298 C THR A 221 6.491 132.473 153.130 1.00 68.39 C
ANISOU 2298 C THR A 221 11227 6979 7781 -1163 125 342 C
ATOM 2299 O THR A 221 6.292 131.266 153.259 1.00 68.36 O
ANISOU 2299 O THR A 221 11286 6931 7756 -1212 85 370 O
ATOM 2300 CB THR A 221 5.340 133.670 151.166 1.00 60.43 C
ANISOU 2300 CB THR A 221 9789 6118 7054 -1044 236 301 C
ATOM 2301 OG1 THR A 221 4.216 134.492 150.860 1.00 56.52 O
ANISOU 2301 OG1 THR A 221 9127 5651 6699 -1043 390 293 O
ATOM 2302 CG2 THR A 221 5.278 132.403 150.307 1.00 58.14 C
ANISOU 2302 CG2 THR A 221 9446 5836 6809 -1044 119 322 C
ATOM 2303 N LEU A 222 7.681 133.054 153.385 1.00 65.78 N
ANISOU 2303 N LEU A 222 10968 6638 7387 -1127 -1 352 N
ATOM 2304 CA LEU A 222 8.862 132.314 153.830 1.00 66.86 C
ANISOU 2304 CA LEU A 222 11244 6705 7456 -1140 -210 409 C
ATOM 2305 C LEU A 222 8.661 131.724 155.198 1.00 75.18 C
ANISOU 2305 C LEU A 222 12576 7649 8339 -1284 -197 446 C
ATOM 2306 O LEU A 222 9.059 130.580 155.432 1.00 74.94 O
ANISOU 2306 O LEU A 222 12634 7551 8288 -1316 -333 502 O
ATOM 2307 CB LEU A 222 10.124 133.187 153.841 1.00 66.75 C
ANISOU 2307 CB LEU A 222 11224 6693 7444 -1083 -353 426 C
ATOM 2308 CG LEU A 222 10.984 133.203 152.583 1.00 70.68 C
ANISOU 2308 CG LEU A 222 11507 7243 8105 -946 -467 426 C
ATOM 2309 CD1 LEU A 222 12.236 133.995 152.826 1.00 70.59 C
ANISOU 2309 CD1 LEU A 222 11510 7210 8101 -914 -609 460 C
ATOM 2310 CD2 LEU A 222 11.356 131.787 152.118 1.00 72.19 C
ANISOU 2310 CD2 LEU A 222 11669 7382 8377 -917 -569 463 C
ATOM 2311 N CYS A 223 8.048 132.498 156.105 1.00 75.05 N
ANISOU 2311 N CYS A 223 12716 7599 8200 -1379 -24 415 N
ATOM 2312 CA CYS A 223 7.785 132.040 157.461 1.00 78.32 C
ANISOU 2312 CA CYS A 223 13450 7892 8416 -1545 23 442 C
ATOM 2313 C CYS A 223 6.852 130.837 157.488 1.00 83.21 C
ANISOU 2313 C CYS A 223 14077 8485 9054 -1600 120 448 C
ATOM 2314 O CYS A 223 7.207 129.823 158.082 1.00 83.40 O
ANISOU 2314 O CYS A 223 14286 8424 8979 -1680 -13 509 O
ATOM 2315 CB CYS A 223 7.274 133.180 158.331 1.00 80.50 C
ANISOU 2315 CB CYS A 223 13908 8120 8559 -1638 243 390 C
ATOM 2316 SG CYS A 223 8.505 134.466 158.637 1.00 84.71 S
ANISOU 2316 SG CYS A 223 14542 8642 9003 -1629 85 400 S
ATOM 2317 N HIS A 224 5.708 130.936 156.779 1.00 80.24 N
ANISOU 2317 N HIS A 224 13482 8179 8828 -1554 320 400 N
ATOM 2318 CA HIS A 224 4.678 129.910 156.648 1.00 81.18 C
ANISOU 2318 CA HIS A 224 13554 8284 9008 -1604 426 406 C
ATOM 2319 C HIS A 224 5.181 128.637 155.967 1.00 85.14 C
ANISOU 2319 C HIS A 224 13991 8797 9563 -1557 208 451 C
ATOM 2320 O HIS A 224 4.750 127.539 156.327 1.00 86.43 O
ANISOU 2320 O HIS A 224 14258 8899 9684 -1641 221 479 O
ATOM 2321 CB HIS A 224 3.459 130.475 155.891 1.00 81.91 C
ANISOU 2321 CB HIS A 224 13375 8446 9301 -1556 637 366 C
ATOM 2322 CG HIS A 224 2.427 129.445 155.540 1.00 86.16 C
ANISOU 2322 CG HIS A 224 13809 8980 9949 -1599 704 386 C
ATOM 2323 ND1 HIS A 224 2.404 128.843 154.292 1.00 87.20 N
ANISOU 2323 ND1 HIS A 224 13730 9184 10217 -1526 556 404 N
ATOM 2324 CD2 HIS A 224 1.441 128.912 156.297 1.00 89.54 C
ANISOU 2324 CD2 HIS A 224 14336 9326 10358 -1720 903 392 C
ATOM 2325 CE1 HIS A 224 1.399 127.981 154.326 1.00 87.28 C
ANISOU 2325 CE1 HIS A 224 13711 9161 10292 -1606 645 426 C
ATOM 2326 NE2 HIS A 224 0.788 127.991 155.509 1.00 89.14 N
ANISOU 2326 NE2 HIS A 224 14112 9308 10451 -1718 859 422 N
ATOM 2327 N VAL A 225 6.083 128.792 154.998 1.00 80.27 N
ANISOU 2327 N VAL A 225 13214 8243 9043 -1429 32 454 N
ATOM 2328 CA VAL A 225 6.628 127.736 154.149 1.00 80.04 C
ANISOU 2328 CA VAL A 225 13099 8214 9098 -1363 -136 481 C
ATOM 2329 C VAL A 225 7.875 127.027 154.758 1.00 86.39 C
ANISOU 2329 C VAL A 225 14073 8918 9834 -1374 -352 551 C
ATOM 2330 O VAL A 225 8.018 125.823 154.545 1.00 88.16 O
ANISOU 2330 O VAL A 225 14316 9087 10094 -1376 -438 585 O
ATOM 2331 CB VAL A 225 6.866 128.354 152.730 1.00 82.39 C
ANISOU 2331 CB VAL A 225 13144 8614 9547 -1231 -164 442 C
ATOM 2332 CG1 VAL A 225 8.181 127.952 152.081 1.00 81.47 C
ANISOU 2332 CG1 VAL A 225 12984 8476 9495 -1132 -347 462 C
ATOM 2333 CG2 VAL A 225 5.680 128.116 151.805 1.00 81.77 C
ANISOU 2333 CG2 VAL A 225 12902 8592 9575 -1240 -63 417 C
ATOM 2334 N TYR A 226 8.744 127.738 155.510 1.00 83.61 N
ANISOU 2334 N TYR A 226 13843 8527 9398 -1391 -450 582 N
ATOM 2335 CA TYR A 226 9.959 127.154 156.116 1.00 84.97 C
ANISOU 2335 CA TYR A 226 14156 8586 9543 -1411 -695 677 C
ATOM 2336 C TYR A 226 9.727 126.627 157.556 1.00 91.43 C
ANISOU 2336 C TYR A 226 15301 9282 10154 -1591 -725 737 C
ATOM 2337 O TYR A 226 10.649 126.589 158.384 1.00 93.63 O
ANISOU 2337 O TYR A 226 15761 9457 10356 -1657 -934 826 O
ATOM 2338 CB TYR A 226 11.158 128.142 156.049 1.00 86.22 C
ANISOU 2338 CB TYR A 226 14255 8753 9751 -1340 -841 703 C
ATOM 2339 CG TYR A 226 11.859 128.235 154.702 1.00 86.96 C
ANISOU 2339 CG TYR A 226 14071 8905 10066 -1169 -890 682 C
ATOM 2340 CD1 TYR A 226 11.208 127.879 153.523 1.00 88.16 C
ANISOU 2340 CD1 TYR A 226 14047 9132 10319 -1094 -759 612 C
ATOM 2341 CD2 TYR A 226 13.170 128.701 154.607 1.00 87.11 C
ANISOU 2341 CD2 TYR A 226 14017 8890 10190 -1099 -1064 736 C
ATOM 2342 CE1 TYR A 226 11.840 127.977 152.285 1.00 87.83 C
ANISOU 2342 CE1 TYR A 226 13801 9124 10447 -960 -779 585 C
ATOM 2343 CE2 TYR A 226 13.815 128.798 153.372 1.00 86.63 C
ANISOU 2343 CE2 TYR A 226 13717 8865 10334 -950 -1067 711 C
ATOM 2344 CZ TYR A 226 13.139 128.450 152.213 1.00 91.41 C
ANISOU 2344 CZ TYR A 226 14186 9540 11004 -884 -912 628 C
ATOM 2345 OH TYR A 226 13.754 128.518 150.987 1.00 88.92 O
ANISOU 2345 OH TYR A 226 13685 9241 10860 -759 -892 595 O
ATOM 2346 N HIS A 227 8.489 126.214 157.842 1.00 86.06 N
ANISOU 2346 N HIS A 227 14702 8604 9394 -1682 -522 696 N
ATOM 2347 CA HIS A 227 8.089 125.662 159.127 1.00 86.57 C
ANISOU 2347 CA HIS A 227 15089 8550 9254 -1865 -494 738 C
ATOM 2348 C HIS A 227 6.935 124.672 158.911 1.00 83.56 C
ANISOU 2348 C HIS A 227 14673 8174 8903 -1905 -330 711 C
ATOM 2349 O HIS A 227 6.216 124.782 157.918 1.00 81.48 O
ANISOU 2349 O HIS A 227 14155 8013 8790 -1817 -192 648 O
ATOM 2350 CB HIS A 227 7.726 126.788 160.125 1.00 89.65 C
ANISOU 2350 CB HIS A 227 15705 8910 9447 -1990 -333 702 C
ATOM 2351 CG HIS A 227 6.263 127.114 160.209 1.00 94.82 C
ANISOU 2351 CG HIS A 227 16341 9598 10089 -2042 25 613 C
ATOM 2352 ND1 HIS A 227 5.477 126.639 161.243 1.00 99.23 N
ANISOU 2352 ND1 HIS A 227 17179 10049 10476 -2220 196 614 N
ATOM 2353 CD2 HIS A 227 5.486 127.842 159.374 1.00 96.60 C
ANISOU 2353 CD2 HIS A 227 16289 9935 10479 -1941 232 534 C
ATOM 2354 CE1 HIS A 227 4.254 127.092 161.008 1.00 99.08 C
ANISOU 2354 CE1 HIS A 227 17021 10076 10550 -2213 520 535 C
ATOM 2355 NE2 HIS A 227 4.212 127.828 159.898 1.00 97.83 N
ANISOU 2355 NE2 HIS A 227 16522 10048 10600 -2047 536 492 N
ATOM 2356 N GLY A 228 6.782 123.718 159.824 1.00 76.86 N
ANISOU 2356 N GLY A 228 14086 7206 7912 -2048 -365 768 N
ATOM 2357 CA GLY A 228 5.697 122.752 159.757 1.00 75.24 C
ANISOU 2357 CA GLY A 228 13877 6989 7723 -2108 -212 752 C
ATOM 2358 C GLY A 228 5.992 121.486 158.981 1.00 73.94 C
ANISOU 2358 C GLY A 228 13586 6812 7695 -2031 -374 792 C
ATOM 2359 O GLY A 228 7.124 121.004 158.985 1.00 73.51 O
ANISOU 2359 O GLY A 228 13566 6691 7675 -1983 -627 866 O
ATOM 2360 N MET A2001 4.959 120.929 158.332 1.00 66.86 N
ANISOU 2360 N MET A2001 12547 5964 6892 -2027 -225 750 N
ATOM 2361 CA MET A2001 5.045 119.671 157.576 1.00 65.14 C
ANISOU 2361 CA MET A2001 12242 5723 6786 -1978 -336 774 C
ATOM 2362 C MET A2001 5.565 119.903 156.161 1.00 68.71 C
ANISOU 2362 C MET A2001 12420 6261 7427 -1804 -411 736 C
ATOM 2363 O MET A2001 5.610 121.043 155.709 1.00 67.00 O
ANISOU 2363 O MET A2001 12057 6141 7260 -1729 -355 688 O
ATOM 2364 CB MET A2001 3.695 118.922 157.576 1.00 66.80 C
ANISOU 2364 CB MET A2001 12457 5928 6997 -2082 -159 755 C
ATOM 2365 CG MET A2001 3.175 118.605 158.964 1.00 70.72 C
ANISOU 2365 CG MET A2001 13249 6320 7303 -2266 -56 790 C
ATOM 2366 SD MET A2001 1.435 118.082 159.035 1.00 75.09 S
ANISOU 2366 SD MET A2001 13766 6875 7892 -2396 232 759 S
ATOM 2367 CE MET A2001 1.540 116.377 158.429 1.00 71.74 C
ANISOU 2367 CE MET A2001 13332 6395 7531 -2392 57 806 C
ATOM 2368 N LYS A2002 5.973 118.825 155.464 1.00 66.57 N
ANISOU 2368 N LYS A2002 12100 5940 7254 -1746 -524 755 N
ATOM 2369 CA LYS A2002 6.522 118.908 154.107 1.00 64.67 C
ANISOU 2369 CA LYS A2002 11651 5746 7174 -1599 -572 714 C
ATOM 2370 C LYS A2002 5.487 119.437 153.114 1.00 67.34 C
ANISOU 2370 C LYS A2002 11806 6210 7570 -1592 -422 638 C
ATOM 2371 O LYS A2002 4.446 118.822 152.899 1.00 69.72 O
ANISOU 2371 O LYS A2002 12103 6515 7874 -1675 -343 630 O
ATOM 2372 CB LYS A2002 7.120 117.561 153.667 1.00 67.11 C
ANISOU 2372 CB LYS A2002 11994 5936 7567 -1559 -686 748 C
ATOM 2373 N LYS A2003 5.753 120.604 152.573 1.00 60.70 N
ANISOU 2373 N LYS A2003 10818 5462 6781 -1506 -399 597 N
ATOM 2374 CA LYS A2003 4.881 121.277 151.616 1.00 59.10 C
ANISOU 2374 CA LYS A2003 10433 5372 6650 -1496 -295 543 C
ATOM 2375 C LYS A2003 5.274 121.000 150.168 1.00 60.32 C
ANISOU 2375 C LYS A2003 10484 5537 6899 -1415 -357 507 C
ATOM 2376 O LYS A2003 6.392 120.564 149.871 1.00 58.54 O
ANISOU 2376 O LYS A2003 10293 5240 6708 -1332 -446 510 O
ATOM 2377 CB LYS A2003 4.801 122.788 151.905 1.00 60.09 C
ANISOU 2377 CB LYS A2003 10477 5585 6771 -1465 -216 520 C
ATOM 2378 CG LYS A2003 4.053 123.086 153.203 1.00 68.52 C
ANISOU 2378 CG LYS A2003 11659 6632 7744 -1576 -80 537 C
ATOM 2379 CD LYS A2003 4.516 124.380 153.857 1.00 71.11 C
ANISOU 2379 CD LYS A2003 12025 6984 8011 -1548 -47 524 C
ATOM 2380 CE LYS A2003 3.925 124.551 155.222 1.00 72.02 C
ANISOU 2380 CE LYS A2003 12330 7038 7997 -1677 102 535 C
ATOM 2381 NZ LYS A2003 4.463 123.556 156.189 1.00 75.45 N
ANISOU 2381 NZ LYS A2003 13030 7354 8286 -1764 -7 592 N
ATOM 2382 N TYR A2004 4.309 121.191 149.284 1.00 56.98 N
ANISOU 2382 N TYR A2004 9944 5181 6524 -1454 -304 481 N
ATOM 2383 CA TYR A2004 4.429 120.959 147.857 1.00 56.38 C
ANISOU 2383 CA TYR A2004 9814 5107 6500 -1425 -350 445 C
ATOM 2384 C TYR A2004 3.734 122.069 147.134 1.00 59.45 C
ANISOU 2384 C TYR A2004 10041 5604 6943 -1433 -319 429 C
ATOM 2385 O TYR A2004 2.696 122.528 147.592 1.00 59.04 O
ANISOU 2385 O TYR A2004 9906 5602 6925 -1500 -251 456 O
ATOM 2386 CB TYR A2004 3.788 119.610 147.496 1.00 58.23 C
ANISOU 2386 CB TYR A2004 10136 5266 6721 -1526 -370 456 C
ATOM 2387 CG TYR A2004 4.698 118.428 147.738 1.00 60.07 C
ANISOU 2387 CG TYR A2004 10523 5368 6932 -1492 -418 463 C
ATOM 2388 CD1 TYR A2004 4.871 117.907 149.018 1.00 62.31 C
ANISOU 2388 CD1 TYR A2004 10915 5589 7172 -1516 -431 514 C
ATOM 2389 CD2 TYR A2004 5.392 117.831 146.690 1.00 61.30 C
ANISOU 2389 CD2 TYR A2004 10732 5442 7119 -1443 -442 423 C
ATOM 2390 CE1 TYR A2004 5.722 116.832 149.253 1.00 64.23 C
ANISOU 2390 CE1 TYR A2004 11283 5695 7426 -1482 -497 539 C
ATOM 2391 CE2 TYR A2004 6.226 116.735 146.908 1.00 63.43 C
ANISOU 2391 CE2 TYR A2004 11122 5567 7413 -1401 -469 436 C
ATOM 2392 CZ TYR A2004 6.378 116.231 148.192 1.00 73.59 C
ANISOU 2392 CZ TYR A2004 12485 6797 8680 -1417 -511 501 C
ATOM 2393 OH TYR A2004 7.174 115.134 148.421 1.00 77.18 O
ANISOU 2393 OH TYR A2004 13046 7093 9186 -1378 -558 531 O
ATOM 2394 N THR A2005 4.284 122.506 146.010 1.00 56.94 N
ANISOU 2394 N THR A2005 9679 5307 6648 -1370 -360 390 N
ATOM 2395 CA THR A2005 3.679 123.586 145.231 1.00 57.19 C
ANISOU 2395 CA THR A2005 9566 5432 6733 -1383 -361 386 C
ATOM 2396 C THR A2005 3.279 123.097 143.854 1.00 63.02 C
ANISOU 2396 C THR A2005 10336 6142 7466 -1461 -433 376 C
ATOM 2397 O THR A2005 3.966 122.253 143.273 1.00 63.75 O
ANISOU 2397 O THR A2005 10568 6148 7505 -1451 -452 339 O
ATOM 2398 CB THR A2005 4.615 124.806 145.178 1.00 68.87 C
ANISOU 2398 CB THR A2005 10978 6965 8222 -1260 -349 355 C
ATOM 2399 OG1 THR A2005 4.848 125.274 146.500 1.00 75.16 O
ANISOU 2399 OG1 THR A2005 11777 7776 9003 -1222 -297 371 O
ATOM 2400 CG2 THR A2005 4.028 125.965 144.415 1.00 70.95 C
ANISOU 2400 CG2 THR A2005 11096 7316 8544 -1269 -357 357 C
ATOM 2401 N CYS A2006 2.157 123.627 143.343 1.00 59.51 N
ANISOU 2401 N CYS A2006 9771 5753 7088 -1549 -472 418 N
ATOM 2402 CA CYS A2006 1.692 123.385 141.992 1.00 60.01 C
ANISOU 2402 CA CYS A2006 9874 5791 7137 -1654 -580 427 C
ATOM 2403 C CYS A2006 2.594 124.274 141.101 1.00 67.64 C
ANISOU 2403 C CYS A2006 10854 6782 8064 -1572 -593 375 C
ATOM 2404 O CYS A2006 2.606 125.498 141.242 1.00 66.77 O
ANISOU 2404 O CYS A2006 10601 6755 8016 -1505 -576 384 O
ATOM 2405 CB CYS A2006 0.217 123.761 141.860 1.00 59.83 C
ANISOU 2405 CB CYS A2006 9684 5809 7240 -1775 -644 516 C
ATOM 2406 SG CYS A2006 -0.428 123.680 140.167 1.00 63.59 S
ANISOU 2406 SG CYS A2006 10210 6250 7701 -1938 -842 559 S
ATOM 2407 N THR A2007 3.368 123.650 140.213 1.00 67.47 N
ANISOU 2407 N THR A2007 11015 6675 7944 -1577 -600 315 N
ATOM 2408 CA THR A2007 4.287 124.348 139.311 1.00 67.35 C
ANISOU 2408 CA THR A2007 11049 6657 7884 -1513 -581 258 C
ATOM 2409 C THR A2007 3.558 125.006 138.135 1.00 74.50 C
ANISOU 2409 C THR A2007 11950 7589 8766 -1634 -699 290 C
ATOM 2410 O THR A2007 4.192 125.289 137.127 1.00 76.42 O
ANISOU 2410 O THR A2007 12317 7792 8927 -1639 -692 240 O
ATOM 2411 CB THR A2007 5.429 123.412 138.846 1.00 76.12 C
ANISOU 2411 CB THR A2007 12364 7635 8923 -1469 -494 178 C
ATOM 2412 OG1 THR A2007 4.886 122.332 138.088 1.00 81.06 O
ANISOU 2412 OG1 THR A2007 13179 8159 9462 -1620 -538 173 O
ATOM 2413 CG2 THR A2007 6.279 122.883 139.994 1.00 72.92 C
ANISOU 2413 CG2 THR A2007 11938 7191 8577 -1339 -411 168 C
ATOM 2414 N VAL A2008 2.238 125.251 138.255 1.00 71.54 N
ANISOU 2414 N VAL A2008 11436 7266 8479 -1739 -808 384 N
ATOM 2415 CA VAL A2008 1.399 125.847 137.204 1.00 71.81 C
ANISOU 2415 CA VAL A2008 11440 7313 8532 -1876 -973 452 C
ATOM 2416 C VAL A2008 0.735 127.129 137.739 1.00 76.75 C
ANISOU 2416 C VAL A2008 11780 8045 9339 -1823 -991 528 C
ATOM 2417 O VAL A2008 0.723 128.155 137.034 1.00 77.50 O
ANISOU 2417 O VAL A2008 11822 8172 9453 -1828 -1066 551 O
ATOM 2418 CB VAL A2008 0.351 124.840 136.623 1.00 76.62 C
ANISOU 2418 CB VAL A2008 12150 7843 9117 -2087 -1125 521 C
ATOM 2419 CG1 VAL A2008 -0.485 125.474 135.512 1.00 77.35 C
ANISOU 2419 CG1 VAL A2008 12222 7931 9238 -2249 -1344 616 C
ATOM 2420 CG2 VAL A2008 1.007 123.550 136.128 1.00 76.72 C
ANISOU 2420 CG2 VAL A2008 12470 7732 8948 -2140 -1079 437 C
ATOM 2421 N CYS A2009 0.181 127.071 138.974 1.00 72.21 N
ANISOU 2421 N CYS A2009 11035 7505 8895 -1779 -906 565 N
ATOM 2422 CA CYS A2009 -0.488 128.225 139.582 1.00 71.58 C
ANISOU 2422 CA CYS A2009 10692 7497 9008 -1728 -870 628 C
ATOM 2423 C CYS A2009 0.171 128.701 140.890 1.00 73.74 C
ANISOU 2423 C CYS A2009 10912 7819 9287 -1566 -675 568 C
ATOM 2424 O CYS A2009 -0.199 129.749 141.414 1.00 73.52 O
ANISOU 2424 O CYS A2009 10705 7838 9394 -1510 -605 598 O
ATOM 2425 CB CYS A2009 -1.982 127.958 139.765 1.00 73.24 C
ANISOU 2425 CB CYS A2009 10731 7683 9413 -1855 -936 747 C
ATOM 2426 SG CYS A2009 -2.397 126.982 141.235 1.00 77.53 S
ANISOU 2426 SG CYS A2009 11255 8201 10002 -1851 -763 743 S
ATOM 2427 N GLY A2010 1.107 127.920 141.420 1.00 68.81 N
ANISOU 2427 N GLY A2010 10451 7167 8528 -1505 -595 493 N
ATOM 2428 CA GLY A2010 1.775 128.258 142.669 1.00 66.66 C
ANISOU 2428 CA GLY A2010 10170 6919 8237 -1383 -454 451 C
ATOM 2429 C GLY A2010 1.047 127.837 143.936 1.00 68.53 C
ANISOU 2429 C GLY A2010 10372 7138 8530 -1418 -347 483 C
ATOM 2430 O GLY A2010 1.564 128.101 145.028 1.00 68.56 O
ANISOU 2430 O GLY A2010 10414 7146 8490 -1346 -239 454 O
ATOM 2431 N TYR A2011 -0.149 127.174 143.825 1.00 62.88 N
ANISOU 2431 N TYR A2011 9599 6388 7903 -1544 -378 549 N
ATOM 2432 CA TYR A2011 -0.925 126.692 144.988 1.00 61.58 C
ANISOU 2432 CA TYR A2011 9408 6190 7801 -1596 -253 582 C
ATOM 2433 C TYR A2011 -0.031 125.831 145.857 1.00 64.86 C
ANISOU 2433 C TYR A2011 10030 6564 8049 -1559 -199 528 C
ATOM 2434 O TYR A2011 0.690 124.970 145.340 1.00 64.45 O
ANISOU 2434 O TYR A2011 10126 6475 7887 -1554 -289 496 O
ATOM 2435 CB TYR A2011 -2.179 125.886 144.566 1.00 62.47 C
ANISOU 2435 CB TYR A2011 9449 6258 8029 -1746 -325 663 C
ATOM 2436 CG TYR A2011 -2.824 125.082 145.682 1.00 62.03 C
ANISOU 2436 CG TYR A2011 9415 6149 8004 -1812 -193 686 C
ATOM 2437 CD1 TYR A2011 -3.744 125.668 146.549 1.00 64.17 C
ANISOU 2437 CD1 TYR A2011 9525 6410 8448 -1826 -14 727 C
ATOM 2438 CD2 TYR A2011 -2.509 123.739 145.876 1.00 62.20 C
ANISOU 2438 CD2 TYR A2011 9633 6115 7886 -1863 -225 664 C
ATOM 2439 CE1 TYR A2011 -4.327 124.941 147.590 1.00 63.74 C
ANISOU 2439 CE1 TYR A2011 9516 6293 8408 -1898 138 743 C
ATOM 2440 CE2 TYR A2011 -3.070 123.007 146.925 1.00 63.77 C
ANISOU 2440 CE2 TYR A2011 9875 6260 8095 -1930 -102 686 C
ATOM 2441 CZ TYR A2011 -3.982 123.612 147.776 1.00 71.84 C
ANISOU 2441 CZ TYR A2011 10747 7275 9273 -1953 83 724 C
ATOM 2442 OH TYR A2011 -4.575 122.885 148.779 1.00 75.88 O
ANISOU 2442 OH TYR A2011 11319 7720 9791 -2036 228 743 O
ATOM 2443 N ILE A2012 -0.054 126.071 147.167 1.00 61.29 N
ANISOU 2443 N ILE A2012 9603 6100 7582 -1539 -49 521 N
ATOM 2444 CA ILE A2012 0.781 125.281 148.047 1.00 60.34 C
ANISOU 2444 CA ILE A2012 9691 5928 7308 -1522 -33 492 C
ATOM 2445 C ILE A2012 -0.089 124.280 148.759 1.00 64.43 C
ANISOU 2445 C ILE A2012 10267 6381 7831 -1637 40 530 C
ATOM 2446 O ILE A2012 -1.094 124.650 149.378 1.00 65.62 O
ANISOU 2446 O ILE A2012 10326 6524 8082 -1696 189 559 O
ATOM 2447 CB ILE A2012 1.751 126.080 148.983 1.00 63.06 C
ANISOU 2447 CB ILE A2012 10118 6281 7561 -1433 24 458 C
ATOM 2448 CG1 ILE A2012 1.268 126.154 150.427 1.00 66.21 C
ANISOU 2448 CG1 ILE A2012 10607 6633 7915 -1497 187 469 C
ATOM 2449 CG2 ILE A2012 2.112 127.476 148.474 1.00 59.87 C
ANISOU 2449 CG2 ILE A2012 9587 5952 7211 -1342 21 434 C
ATOM 2450 CD1 ILE A2012 1.971 125.214 151.315 1.00 83.07 C
ANISOU 2450 CD1 ILE A2012 12973 8691 9898 -1526 145 475 C
ATOM 2451 N TYR A2013 0.253 122.989 148.612 1.00 58.96 N
ANISOU 2451 N TYR A2013 9720 5629 7052 -1673 -49 530 N
ATOM 2452 CA TYR A2013 -0.450 121.964 149.339 1.00 57.24 C
ANISOU 2452 CA TYR A2013 9588 5342 6818 -1784 12 564 C
ATOM 2453 C TYR A2013 0.147 121.985 150.748 1.00 61.81 C
ANISOU 2453 C TYR A2013 10342 5876 7267 -1769 97 553 C
ATOM 2454 O TYR A2013 1.341 121.732 150.920 1.00 60.51 O
ANISOU 2454 O TYR A2013 10313 5682 6996 -1700 1 536 O
ATOM 2455 CB TYR A2013 -0.335 120.568 148.709 1.00 56.24 C
ANISOU 2455 CB TYR A2013 9571 5153 6644 -1837 -112 571 C
ATOM 2456 CG TYR A2013 -0.988 119.560 149.627 1.00 54.75 C
ANISOU 2456 CG TYR A2013 9485 4890 6427 -1950 -39 608 C
ATOM 2457 CD1 TYR A2013 -2.377 119.474 149.714 1.00 57.37 C
ANISOU 2457 CD1 TYR A2013 9691 5220 6888 -2068 47 658 C
ATOM 2458 CD2 TYR A2013 -0.234 118.830 150.541 1.00 53.39 C
ANISOU 2458 CD2 TYR A2013 9526 4642 6118 -1943 -44 604 C
ATOM 2459 CE1 TYR A2013 -2.993 118.646 150.646 1.00 56.91 C
ANISOU 2459 CE1 TYR A2013 9727 5089 6808 -2177 148 690 C
ATOM 2460 CE2 TYR A2013 -0.840 118.021 151.495 1.00 54.94 C
ANISOU 2460 CE2 TYR A2013 9838 4767 6271 -2057 38 639 C
ATOM 2461 CZ TYR A2013 -2.220 117.931 151.541 1.00 60.82 C
ANISOU 2461 CZ TYR A2013 10465 5515 7131 -2174 148 675 C
ATOM 2462 OH TYR A2013 -2.830 117.124 152.456 1.00 64.49 O
ANISOU 2462 OH TYR A2013 11044 5900 7557 -2293 248 709 O
ATOM 2463 N ASN A2014 -0.681 122.316 151.741 1.00 59.79 N
ANISOU 2463 N ASN A2014 10085 5599 7033 -1843 279 570 N
ATOM 2464 CA ASN A2014 -0.260 122.362 153.123 1.00 60.20 C
ANISOU 2464 CA ASN A2014 10350 5590 6934 -1872 371 564 C
ATOM 2465 C ASN A2014 -0.906 121.200 153.844 1.00 64.36 C
ANISOU 2465 C ASN A2014 11018 6026 7410 -2005 441 598 C
ATOM 2466 O ASN A2014 -2.134 121.147 153.918 1.00 65.79 O
ANISOU 2466 O ASN A2014 11088 6194 7713 -2092 597 619 O
ATOM 2467 CB ASN A2014 -0.613 123.721 153.758 1.00 66.20 C
ANISOU 2467 CB ASN A2014 11058 6370 7726 -1863 566 541 C
ATOM 2468 CG ASN A2014 0.059 123.989 155.084 1.00 96.72 C
ANISOU 2468 CG ASN A2014 15190 10169 11392 -1896 628 527 C
ATOM 2469 OD1 ASN A2014 0.586 123.092 155.756 1.00 89.77 O
ANISOU 2469 OD1 ASN A2014 14543 9210 10353 -1955 546 551 O
ATOM 2470 ND2 ASN A2014 0.008 125.234 155.515 1.00 91.44 N
ANISOU 2470 ND2 ASN A2014 14508 9513 10723 -1874 771 495 N
ATOM 2471 N PRO A2015 -0.097 120.216 154.318 1.00 59.76 N
ANISOU 2471 N PRO A2015 10662 5370 6675 -2023 317 614 N
ATOM 2472 CA PRO A2015 -0.674 119.031 155.005 1.00 59.94 C
ANISOU 2472 CA PRO A2015 10844 5298 6634 -2157 370 651 C
ATOM 2473 C PRO A2015 -1.514 119.370 156.225 1.00 67.27 C
ANISOU 2473 C PRO A2015 11875 6171 7514 -2279 624 655 C
ATOM 2474 O PRO A2015 -2.501 118.687 156.470 1.00 67.37 O
ANISOU 2474 O PRO A2015 11892 6134 7573 -2394 744 680 O
ATOM 2475 CB PRO A2015 0.550 118.197 155.372 1.00 61.01 C
ANISOU 2475 CB PRO A2015 11205 5356 6621 -2134 178 675 C
ATOM 2476 CG PRO A2015 1.623 118.670 154.438 1.00 63.95 C
ANISOU 2476 CG PRO A2015 11463 5786 7048 -1978 15 650 C
ATOM 2477 CD PRO A2015 1.376 120.122 154.238 1.00 59.41 C
ANISOU 2477 CD PRO A2015 10722 5311 6539 -1922 121 611 C
ATOM 2478 N GLU A2016 -1.151 120.463 156.953 1.00 67.15 N
ANISOU 2478 N GLU A2016 11945 6155 7414 -2260 723 626 N
ATOM 2479 CA GLU A2016 -1.864 121.020 158.116 1.00 69.18 C
ANISOU 2479 CA GLU A2016 12332 6342 7613 -2372 1013 611 C
ATOM 2480 C GLU A2016 -3.359 121.233 157.782 1.00 73.14 C
ANISOU 2480 C GLU A2016 12573 6855 8360 -2415 1259 612 C
ATOM 2481 O GLU A2016 -4.208 120.916 158.606 1.00 71.93 O
ANISOU 2481 O GLU A2016 12521 6607 8201 -2547 1497 620 O
ATOM 2482 CB GLU A2016 -1.231 122.370 158.529 1.00 70.60 C
ANISOU 2482 CB GLU A2016 12576 6540 7710 -2315 1061 569 C
ATOM 2483 CG GLU A2016 -2.005 123.079 159.634 1.00 90.57 C
ANISOU 2483 CG GLU A2016 15248 8979 10186 -2431 1406 537 C
ATOM 2484 CD GLU A2016 -1.689 124.529 159.940 1.00126.45 C
ANISOU 2484 CD GLU A2016 19814 13534 14697 -2383 1524 486 C
ATOM 2485 OE1 GLU A2016 -1.464 125.313 158.988 1.00135.26 O
ANISOU 2485 OE1 GLU A2016 20661 14760 15972 -2239 1438 469 O
ATOM 2486 OE2 GLU A2016 -1.716 124.891 161.140 1.00121.80 O
ANISOU 2486 OE2 GLU A2016 19530 12830 13918 -2504 1717 460 O
ATOM 2487 N ASP A2017 -3.658 121.749 156.557 1.00 70.41 N
ANISOU 2487 N ASP A2017 11895 6613 8244 -2311 1189 614 N
ATOM 2488 CA ASP A2017 -5.008 122.051 156.080 1.00 72.05 C
ANISOU 2488 CA ASP A2017 11803 6830 8744 -2340 1359 642 C
ATOM 2489 C ASP A2017 -5.684 120.974 155.262 1.00 78.59 C
ANISOU 2489 C ASP A2017 12482 7664 9713 -2396 1236 700 C
ATOM 2490 O ASP A2017 -6.910 120.862 155.342 1.00 81.11 O
ANISOU 2490 O ASP A2017 12637 7935 10244 -2484 1414 744 O
ATOM 2491 CB ASP A2017 -5.012 123.354 155.277 1.00 73.35 C
ANISOU 2491 CB ASP A2017 11702 7083 9086 -2217 1345 628 C
ATOM 2492 CG ASP A2017 -4.517 124.555 156.061 1.00 86.64 C
ANISOU 2492 CG ASP A2017 13506 8750 10662 -2170 1502 570 C
ATOM 2493 OD1 ASP A2017 -4.912 124.692 157.245 1.00 88.81 O
ANISOU 2493 OD1 ASP A2017 13962 8918 10862 -2265 1777 548 O
ATOM 2494 OD2 ASP A2017 -3.729 125.358 155.490 1.00 89.97 O
ANISOU 2494 OD2 ASP A2017 13867 9256 11063 -2050 1356 544 O
ATOM 2495 N GLY A2018 -4.911 120.234 154.457 1.00 73.78 N
ANISOU 2495 N GLY A2018 11922 7102 9010 -2350 946 704 N
ATOM 2496 CA GLY A2018 -5.427 119.225 153.537 1.00 73.18 C
ANISOU 2496 CA GLY A2018 11740 7028 9037 -2407 794 752 C
ATOM 2497 C GLY A2018 -6.127 119.910 152.375 1.00 77.29 C
ANISOU 2497 C GLY A2018 11934 7616 9817 -2379 733 789 C
ATOM 2498 O GLY A2018 -5.687 120.971 151.912 1.00 76.53 O
ANISOU 2498 O GLY A2018 11735 7591 9754 -2270 690 763 O
ATOM 2499 N ASP A2019 -7.225 119.320 151.910 1.00 74.98 N
ANISOU 2499 N ASP A2019 11482 7293 9714 -2490 713 861 N
ATOM 2500 CA ASP A2019 -8.123 119.830 150.858 1.00 75.15 C
ANISOU 2500 CA ASP A2019 11183 7348 10024 -2512 629 935 C
ATOM 2501 C ASP A2019 -9.431 119.106 151.186 1.00 78.16 C
ANISOU 2501 C ASP A2019 11449 7643 10607 -2668 746 1019 C
ATOM 2502 O ASP A2019 -9.735 118.106 150.539 1.00 76.38 O
ANISOU 2502 O ASP A2019 11230 7397 10393 -2766 562 1069 O
ATOM 2503 CB ASP A2019 -7.577 119.474 149.452 1.00 76.37 C
ANISOU 2503 CB ASP A2019 11356 7555 10106 -2495 306 938 C
ATOM 2504 CG ASP A2019 -8.368 120.005 148.266 1.00 87.57 C
ANISOU 2504 CG ASP A2019 12496 9001 11776 -2536 152 1024 C
ATOM 2505 OD1 ASP A2019 -9.278 120.840 148.479 1.00 91.00 O
ANISOU 2505 OD1 ASP A2019 12665 9422 12488 -2547 287 1088 O
ATOM 2506 OD2 ASP A2019 -8.070 119.591 147.120 1.00 89.39 O
ANISOU 2506 OD2 ASP A2019 12786 9249 11931 -2566 -102 1031 O
ATOM 2507 N PRO A2020 -10.114 119.494 152.307 1.00 76.91 N
ANISOU 2507 N PRO A2020 11237 7415 10571 -2702 1075 1025 N
ATOM 2508 CA PRO A2020 -11.254 118.686 152.800 1.00 79.57 C
ANISOU 2508 CA PRO A2020 11505 7651 11077 -2855 1231 1095 C
ATOM 2509 C PRO A2020 -12.480 118.648 151.916 1.00 88.68 C
ANISOU 2509 C PRO A2020 12298 8782 12614 -2944 1131 1225 C
ATOM 2510 O PRO A2020 -13.188 117.643 151.914 1.00 89.46 O
ANISOU 2510 O PRO A2020 12374 8817 12799 -3083 1105 1292 O
ATOM 2511 CB PRO A2020 -11.565 119.279 154.178 1.00 82.24 C
ANISOU 2511 CB PRO A2020 11897 7907 11445 -2860 1641 1055 C
ATOM 2512 CG PRO A2020 -10.414 120.186 154.500 1.00 84.22 C
ANISOU 2512 CG PRO A2020 12334 8216 11449 -2724 1655 954 C
ATOM 2513 CD PRO A2020 -9.840 120.632 153.210 1.00 77.33 C
ANISOU 2513 CD PRO A2020 11329 7459 10593 -2615 1340 960 C
ATOM 2514 N ASP A2021 -12.716 119.717 151.138 1.00 88.60 N
ANISOU 2514 N ASP A2021 12010 8818 12835 -2874 1045 1272 N
ATOM 2515 CA ASP A2021 -13.844 119.768 150.207 1.00 90.78 C
ANISOU 2515 CA ASP A2021 11929 9064 13498 -2965 885 1422 C
ATOM 2516 C ASP A2021 -13.686 118.700 149.108 1.00 93.40 C
ANISOU 2516 C ASP A2021 12368 9424 13694 -3067 498 1463 C
ATOM 2517 O ASP A2021 -14.672 118.332 148.462 1.00 95.36 O
ANISOU 2517 O ASP A2021 12399 9622 14212 -3204 339 1599 O
ATOM 2518 CB ASP A2021 -14.000 121.182 149.614 1.00 92.82 C
ANISOU 2518 CB ASP A2021 11902 9358 14006 -2864 849 1466 C
ATOM 2519 CG ASP A2021 -14.345 122.257 150.636 1.00105.87 C
ANISOU 2519 CG ASP A2021 13416 10951 15858 -2781 1257 1438 C
ATOM 2520 OD1 ASP A2021 -15.054 121.938 151.628 1.00107.42 O
ANISOU 2520 OD1 ASP A2021 13584 11039 16191 -2852 1580 1449 O
ATOM 2521 OD2 ASP A2021 -13.934 123.423 150.431 1.00112.86 O
ANISOU 2521 OD2 ASP A2021 14227 11884 16769 -2653 1269 1406 O
ATOM 2522 N ASN A2022 -12.453 118.158 148.961 1.00 85.87 N
ANISOU 2522 N ASN A2022 11764 8531 12333 -3010 363 1350 N
ATOM 2523 CA ASN A2022 -12.121 117.144 147.973 1.00 84.19 C
ANISOU 2523 CA ASN A2022 11721 8325 11942 -3093 45 1358 C
ATOM 2524 C ASN A2022 -11.574 115.843 148.597 1.00 85.95 C
ANISOU 2524 C ASN A2022 12276 8508 11872 -3130 87 1284 C
ATOM 2525 O ASN A2022 -10.852 115.088 147.939 1.00 85.44 O
ANISOU 2525 O ASN A2022 12441 8449 11571 -3139 -120 1239 O
ATOM 2526 CB ASN A2022 -11.197 117.727 146.912 1.00 82.06 C
ANISOU 2526 CB ASN A2022 11524 8137 11518 -2998 -186 1310 C
ATOM 2527 CG ASN A2022 -11.754 118.985 146.274 1.00114.68 C
ANISOU 2527 CG ASN A2022 15338 12297 15937 -2974 -254 1396 C
ATOM 2528 OD1 ASN A2022 -12.857 119.001 145.705 1.00115.12 O
ANISOU 2528 OD1 ASN A2022 15142 12304 16292 -3103 -389 1539 O
ATOM 2529 ND2 ASN A2022 -11.015 120.078 146.378 1.00105.25 N
ANISOU 2529 ND2 ASN A2022 14139 11172 14680 -2813 -171 1322 N
ATOM 2530 N GLY A2023 -11.975 115.573 149.837 1.00 81.06 N
ANISOU 2530 N GLY A2023 11682 7829 11286 -3164 363 1280 N
ATOM 2531 CA GLY A2023 -11.655 114.336 150.546 1.00 80.30 C
ANISOU 2531 CA GLY A2023 11878 7673 10958 -3225 417 1236 C
ATOM 2532 C GLY A2023 -10.359 114.233 151.326 1.00 79.90 C
ANISOU 2532 C GLY A2023 12150 7637 10572 -3110 492 1120 C
ATOM 2533 O GLY A2023 -10.122 113.215 151.995 1.00 80.98 O
ANISOU 2533 O GLY A2023 12526 7708 10534 -3167 538 1099 O
ATOM 2534 N VAL A2024 -9.514 115.256 151.247 1.00 70.58 N
ANISOU 2534 N VAL A2024 10977 6531 9309 -2956 486 1055 N
ATOM 2535 CA VAL A2024 -8.229 115.259 151.933 1.00 67.89 C
ANISOU 2535 CA VAL A2024 10916 6198 8680 -2848 517 963 C
ATOM 2536 C VAL A2024 -8.366 115.979 153.274 1.00 72.20 C
ANISOU 2536 C VAL A2024 11501 6716 9217 -2834 816 938 C
ATOM 2537 O VAL A2024 -8.415 117.205 153.340 1.00 71.53 O
ANISOU 2537 O VAL A2024 11272 6675 9231 -2754 927 921 O
ATOM 2538 CB VAL A2024 -7.082 115.809 151.047 1.00 69.90 C
ANISOU 2538 CB VAL A2024 11199 6534 8826 -2701 321 906 C
ATOM 2539 CG1 VAL A2024 -5.747 115.714 151.766 1.00 68.56 C
ANISOU 2539 CG1 VAL A2024 11296 6352 8400 -2600 324 834 C
ATOM 2540 CG2 VAL A2024 -7.020 115.079 149.706 1.00 69.58 C
ANISOU 2540 CG2 VAL A2024 11164 6494 8780 -2743 64 923 C
ATOM 2541 N ASN A2025 -8.457 115.202 154.346 1.00 70.49 N
ANISOU 2541 N ASN A2025 11501 6409 8871 -2926 954 936 N
ATOM 2542 CA ASN A2025 -8.574 115.720 155.699 1.00 71.04 C
ANISOU 2542 CA ASN A2025 11699 6420 8874 -2954 1251 907 C
ATOM 2543 C ASN A2025 -7.249 116.308 156.146 1.00 73.14 C
ANISOU 2543 C ASN A2025 12185 6716 8889 -2838 1197 838 C
ATOM 2544 O ASN A2025 -6.209 115.863 155.660 1.00 70.20 O
ANISOU 2544 O ASN A2025 11931 6375 8366 -2763 943 820 O
ATOM 2545 CB ASN A2025 -8.987 114.601 156.648 1.00 76.26 C
ANISOU 2545 CB ASN A2025 12579 6964 9432 -3108 1380 931 C
ATOM 2546 CG ASN A2025 -10.461 114.550 156.967 1.00106.61 C
ANISOU 2546 CG ASN A2025 16229 10736 13542 -3241 1651 987 C
ATOM 2547 OD1 ASN A2025 -11.304 115.198 156.325 1.00105.20 O
ANISOU 2547 OD1 ASN A2025 15701 10588 13682 -3226 1701 1032 O
ATOM 2548 ND2 ASN A2025 -10.801 113.758 157.967 1.00 98.04 N
ANISOU 2548 ND2 ASN A2025 15364 9538 12349 -3379 1828 996 N
ATOM 2549 N PRO A2026 -7.247 117.308 157.063 1.00 71.82 N
ANISOU 2549 N PRO A2026 12080 6523 8686 -2828 1439 801 N
ATOM 2550 CA PRO A2026 -5.972 117.856 157.540 1.00 70.35 C
ANISOU 2550 CA PRO A2026 12122 6352 8254 -2743 1364 747 C
ATOM 2551 C PRO A2026 -5.132 116.785 158.236 1.00 73.59 C
ANISOU 2551 C PRO A2026 12891 6687 8384 -2801 1225 756 C
ATOM 2552 O PRO A2026 -5.644 115.929 158.965 1.00 74.69 O
ANISOU 2552 O PRO A2026 13198 6726 8453 -2942 1333 784 O
ATOM 2553 CB PRO A2026 -6.407 118.957 158.511 1.00 73.43 C
ANISOU 2553 CB PRO A2026 12553 6689 8657 -2778 1700 712 C
ATOM 2554 CG PRO A2026 -7.794 119.289 158.124 1.00 79.17 C
ANISOU 2554 CG PRO A2026 12942 7412 9728 -2809 1909 745 C
ATOM 2555 CD PRO A2026 -8.379 117.975 157.735 1.00 75.50 C
ANISOU 2555 CD PRO A2026 12426 6924 9338 -2903 1805 807 C
ATOM 2556 N GLY A2027 -3.845 116.834 157.958 1.00 69.11 N
ANISOU 2556 N GLY A2027 12416 6158 7684 -2690 977 742 N
ATOM 2557 CA GLY A2027 -2.862 115.909 158.490 1.00 69.51 C
ANISOU 2557 CA GLY A2027 12762 6131 7516 -2714 787 768 C
ATOM 2558 C GLY A2027 -2.296 115.005 157.422 1.00 74.24 C
ANISOU 2558 C GLY A2027 13282 6755 8171 -2633 520 786 C
ATOM 2559 O GLY A2027 -1.242 114.401 157.630 1.00 76.03 O
ANISOU 2559 O GLY A2027 13691 6923 8276 -2599 326 810 O
ATOM 2560 N THR A2028 -2.992 114.906 156.272 1.00 68.72 N
ANISOU 2560 N THR A2028 12321 6125 7665 -2609 509 781 N
ATOM 2561 CA THR A2028 -2.601 114.043 155.163 1.00 66.96 C
ANISOU 2561 CA THR A2028 12047 5908 7487 -2556 293 786 C
ATOM 2562 C THR A2028 -1.312 114.519 154.501 1.00 67.46 C
ANISOU 2562 C THR A2028 12082 6017 7533 -2390 118 753 C
ATOM 2563 O THR A2028 -1.251 115.604 153.922 1.00 64.74 O
ANISOU 2563 O THR A2028 11558 5768 7271 -2303 134 720 O
ATOM 2564 CB THR A2028 -3.758 113.847 154.157 1.00 72.30 C
ANISOU 2564 CB THR A2028 12490 6628 8353 -2613 315 800 C
ATOM 2565 OG1 THR A2028 -4.928 113.438 154.859 1.00 73.85 O
ANISOU 2565 OG1 THR A2028 12694 6768 8596 -2767 495 839 O
ATOM 2566 CG2 THR A2028 -3.441 112.797 153.081 1.00 68.73 C
ANISOU 2566 CG2 THR A2028 12062 6148 7905 -2603 113 802 C
ATOM 2567 N ASP A2029 -0.282 113.673 154.565 1.00 63.49 N
ANISOU 2567 N ASP A2029 11746 5431 6944 -2347 -44 769 N
ATOM 2568 CA ASP A2029 0.963 113.985 153.891 1.00 61.24 C
ANISOU 2568 CA ASP A2029 11420 5164 6684 -2191 -192 744 C
ATOM 2569 C ASP A2029 0.725 113.864 152.399 1.00 61.55 C
ANISOU 2569 C ASP A2029 11295 5253 6839 -2148 -236 705 C
ATOM 2570 O ASP A2029 -0.076 113.039 151.961 1.00 60.83 O
ANISOU 2570 O ASP A2029 11202 5133 6779 -2243 -231 715 O
ATOM 2571 CB ASP A2029 2.125 113.113 154.406 1.00 63.60 C
ANISOU 2571 CB ASP A2029 11919 5334 6914 -2155 -344 788 C
ATOM 2572 CG ASP A2029 2.819 113.752 155.610 1.00 79.38 C
ANISOU 2572 CG ASP A2029 14052 7304 8805 -2154 -374 826 C
ATOM 2573 OD1 ASP A2029 3.302 114.947 155.479 1.00 77.01 O
ANISOU 2573 OD1 ASP A2029 13649 7085 8527 -2064 -371 797 O
ATOM 2574 OD2 ASP A2029 2.856 113.097 156.695 1.00 84.41 O
ANISOU 2574 OD2 ASP A2029 14917 7833 9323 -2259 -406 888 O
ATOM 2575 N PHE A2030 1.344 114.743 151.629 1.00 57.22 N
ANISOU 2575 N PHE A2030 10622 4775 6345 -2026 -276 664 N
ATOM 2576 CA PHE A2030 1.197 114.784 150.177 1.00 56.22 C
ANISOU 2576 CA PHE A2030 10374 4688 6298 -1997 -320 624 C
ATOM 2577 C PHE A2030 1.374 113.410 149.517 1.00 64.62 C
ANISOU 2577 C PHE A2030 11560 5640 7353 -2028 -396 619 C
ATOM 2578 O PHE A2030 0.631 113.099 148.589 1.00 67.20 O
ANISOU 2578 O PHE A2030 11846 5976 7711 -2108 -412 608 O
ATOM 2579 CB PHE A2030 2.119 115.839 149.576 1.00 55.78 C
ANISOU 2579 CB PHE A2030 10220 4696 6277 -1855 -351 581 C
ATOM 2580 CG PHE A2030 1.977 116.046 148.088 1.00 56.31 C
ANISOU 2580 CG PHE A2030 10194 4802 6400 -1841 -388 538 C
ATOM 2581 CD1 PHE A2030 1.000 116.891 147.578 1.00 58.80 C
ANISOU 2581 CD1 PHE A2030 10346 5218 6777 -1896 -362 543 C
ATOM 2582 CD2 PHE A2030 2.835 115.412 147.198 1.00 57.64 C
ANISOU 2582 CD2 PHE A2030 10449 4885 6565 -1782 -443 498 C
ATOM 2583 CE1 PHE A2030 0.869 117.081 146.202 1.00 58.91 C
ANISOU 2583 CE1 PHE A2030 10309 5254 6821 -1910 -428 517 C
ATOM 2584 CE2 PHE A2030 2.715 115.618 145.829 1.00 59.68 C
ANISOU 2584 CE2 PHE A2030 10677 5161 6837 -1796 -466 455 C
ATOM 2585 CZ PHE A2030 1.726 116.445 145.339 1.00 57.58 C
ANISOU 2585 CZ PHE A2030 10272 5002 6604 -1869 -477 469 C
ATOM 2586 N LYS A2031 2.279 112.563 150.048 1.00 61.43 N
ANISOU 2586 N LYS A2031 11313 5116 6912 -1985 -448 638 N
ATOM 2587 CA LYS A2031 2.533 111.212 149.547 1.00 61.95 C
ANISOU 2587 CA LYS A2031 11512 5045 6980 -2005 -499 634 C
ATOM 2588 C LYS A2031 1.331 110.287 149.727 1.00 69.76 C
ANISOU 2588 C LYS A2031 12571 6004 7932 -2174 -478 665 C
ATOM 2589 O LYS A2031 1.206 109.300 148.994 1.00 72.86 O
ANISOU 2589 O LYS A2031 13051 6308 8324 -2225 -509 648 O
ATOM 2590 CB LYS A2031 3.796 110.603 150.189 1.00 64.43 C
ANISOU 2590 CB LYS A2031 11948 5223 7310 -1910 -566 669 C
ATOM 2591 CG LYS A2031 3.702 110.363 151.697 1.00 77.03 C
ANISOU 2591 CG LYS A2031 13656 6781 8830 -1976 -592 747 C
ATOM 2592 CD LYS A2031 4.885 109.587 152.241 1.00 87.17 C
ANISOU 2592 CD LYS A2031 15067 7900 10155 -1907 -706 808 C
ATOM 2593 CE LYS A2031 4.926 109.591 153.755 1.00 99.05 C
ANISOU 2593 CE LYS A2031 16706 9368 11559 -1981 -765 895 C
ATOM 2594 NZ LYS A2031 3.866 108.734 154.357 1.00109.06 N
ANISOU 2594 NZ LYS A2031 18119 10600 12718 -2150 -717 925 N
ATOM 2595 N ASP A2032 0.460 110.583 150.712 1.00 64.97 N
ANISOU 2595 N ASP A2032 11937 5453 7295 -2270 -409 708 N
ATOM 2596 CA ASP A2032 -0.723 109.767 151.002 1.00 64.14 C
ANISOU 2596 CA ASP A2032 11877 5316 7176 -2438 -366 748 C
ATOM 2597 C ASP A2032 -1.975 110.258 150.279 1.00 67.50 C
ANISOU 2597 C ASP A2032 12118 5837 7693 -2533 -326 749 C
ATOM 2598 O ASP A2032 -3.046 109.681 150.452 1.00 66.61 O
ANISOU 2598 O ASP A2032 11999 5699 7609 -2680 -292 791 O
ATOM 2599 CB ASP A2032 -0.941 109.636 152.507 1.00 66.01 C
ANISOU 2599 CB ASP A2032 12224 5519 7337 -2505 -290 799 C
ATOM 2600 CG ASP A2032 0.212 108.943 153.203 1.00 84.78 C
ANISOU 2600 CG ASP A2032 14805 7773 9636 -2445 -385 828 C
ATOM 2601 OD1 ASP A2032 0.813 108.022 152.592 1.00 89.14 O
ANISOU 2601 OD1 ASP A2032 15432 8224 10215 -2400 -480 821 O
ATOM 2602 OD2 ASP A2032 0.498 109.293 154.366 1.00 91.20 O
ANISOU 2602 OD2 ASP A2032 15712 8571 10369 -2453 -367 864 O
ATOM 2603 N ILE A2033 -1.847 111.329 149.468 1.00 64.56 N
ANISOU 2603 N ILE A2033 11585 5561 7382 -2457 -344 715 N
ATOM 2604 CA ILE A2033 -2.964 111.843 148.676 1.00 64.91 C
ANISOU 2604 CA ILE A2033 11441 5682 7540 -2547 -352 736 C
ATOM 2605 C ILE A2033 -3.063 110.894 147.464 1.00 72.14 C
ANISOU 2605 C ILE A2033 12453 6524 8432 -2626 -481 724 C
ATOM 2606 O ILE A2033 -2.044 110.679 146.806 1.00 71.73 O
ANISOU 2606 O ILE A2033 12519 6424 8311 -2536 -535 666 O
ATOM 2607 CB ILE A2033 -2.730 113.312 148.221 1.00 66.46 C
ANISOU 2607 CB ILE A2033 11458 5994 7801 -2443 -345 711 C
ATOM 2608 CG1 ILE A2033 -2.641 114.289 149.395 1.00 65.87 C
ANISOU 2608 CG1 ILE A2033 11315 5977 7736 -2377 -206 714 C
ATOM 2609 CG2 ILE A2033 -3.812 113.758 147.251 1.00 67.89 C
ANISOU 2609 CG2 ILE A2033 11450 6229 8115 -2543 -404 751 C
ATOM 2610 CD1 ILE A2033 -2.152 115.588 148.979 1.00 69.99 C
ANISOU 2610 CD1 ILE A2033 11710 6591 8294 -2257 -211 680 C
ATOM 2611 N PRO A2034 -4.233 110.314 147.122 1.00 71.78 N
ANISOU 2611 N PRO A2034 12374 6453 8446 -2799 -525 779 N
ATOM 2612 CA PRO A2034 -4.263 109.426 145.944 1.00 72.83 C
ANISOU 2612 CA PRO A2034 12649 6500 8523 -2893 -658 764 C
ATOM 2613 C PRO A2034 -3.943 110.134 144.636 1.00 78.03 C
ANISOU 2613 C PRO A2034 13279 7195 9172 -2863 -753 725 C
ATOM 2614 O PRO A2034 -4.104 111.348 144.526 1.00 77.31 O
ANISOU 2614 O PRO A2034 12994 7214 9166 -2813 -746 739 O
ATOM 2615 CB PRO A2034 -5.670 108.829 145.948 1.00 76.00 C
ANISOU 2615 CB PRO A2034 12986 6876 9013 -3100 -701 850 C
ATOM 2616 CG PRO A2034 -6.454 109.641 146.877 1.00 80.61 C
ANISOU 2616 CG PRO A2034 13334 7547 9747 -3104 -581 910 C
ATOM 2617 CD PRO A2034 -5.549 110.401 147.788 1.00 74.54 C
ANISOU 2617 CD PRO A2034 12569 6829 8923 -2927 -448 860 C
ATOM 2618 N ASP A2035 -3.430 109.356 143.675 1.00 76.13 N
ANISOU 2618 N ASP A2035 13261 6847 8819 -2896 -822 671 N
ATOM 2619 CA ASP A2035 -3.062 109.675 142.284 1.00 76.48 C
ANISOU 2619 CA ASP A2035 13395 6867 8795 -2913 -905 620 C
ATOM 2620 C ASP A2035 -4.083 110.546 141.513 1.00 75.52 C
ANISOU 2620 C ASP A2035 13107 6832 8756 -3043 -1043 691 C
ATOM 2621 O ASP A2035 -3.687 111.243 140.587 1.00 74.79 O
ANISOU 2621 O ASP A2035 13040 6759 8618 -3020 -1094 655 O
ATOM 2622 CB ASP A2035 -2.988 108.323 141.507 1.00 81.89 C
ANISOU 2622 CB ASP A2035 14379 7382 9354 -3040 -955 584 C
ATOM 2623 CG ASP A2035 -1.611 107.735 141.258 1.00103.92 C
ANISOU 2623 CG ASP A2035 17398 10039 12049 -2907 -846 477 C
ATOM 2624 OD1 ASP A2035 -0.712 107.923 142.123 1.00105.88 O
ANISOU 2624 OD1 ASP A2035 17583 10302 12345 -2718 -738 455 O
ATOM 2625 OD2 ASP A2035 -1.442 107.037 140.225 1.00112.01 O
ANISOU 2625 OD2 ASP A2035 18675 10923 12962 -3002 -866 423 O
ATOM 2626 N ASP A2036 -5.393 110.384 141.803 1.00 70.81 N
ANISOU 2626 N ASP A2036 12361 6257 8285 -3199 -1114 799 N
ATOM 2627 CA ASP A2036 -6.516 111.018 141.115 1.00 71.30 C
ANISOU 2627 CA ASP A2036 12242 6367 8482 -3352 -1280 903 C
ATOM 2628 C ASP A2036 -6.990 112.316 141.753 1.00 74.99 C
ANISOU 2628 C ASP A2036 12368 6967 9160 -3265 -1214 965 C
ATOM 2629 O ASP A2036 -8.079 112.802 141.439 1.00 75.61 O
ANISOU 2629 O ASP A2036 12230 7072 9427 -3387 -1333 1079 O
ATOM 2630 CB ASP A2036 -7.687 110.024 140.937 1.00 75.51 C
ANISOU 2630 CB ASP A2036 12800 6817 9072 -3592 -1414 1001 C
ATOM 2631 CG ASP A2036 -8.124 109.237 142.161 1.00 87.36 C
ANISOU 2631 CG ASP A2036 14251 8297 10646 -3606 -1286 1033 C
ATOM 2632 OD1 ASP A2036 -7.724 109.611 143.289 1.00 87.00 O
ANISOU 2632 OD1 ASP A2036 14109 8312 10633 -3443 -1093 1000 O
ATOM 2633 OD2 ASP A2036 -8.913 108.274 141.996 1.00 97.61 O
ANISOU 2633 OD2 ASP A2036 15615 9510 11963 -3797 -1385 1098 O
ATOM 2634 N TRP A2037 -6.165 112.888 142.638 1.00 70.79 N
ANISOU 2634 N TRP A2037 11789 6499 8608 -3061 -1029 896 N
ATOM 2635 CA TRP A2037 -6.420 114.187 143.248 1.00 69.63 C
ANISOU 2635 CA TRP A2037 11367 6463 8626 -2960 -931 928 C
ATOM 2636 C TRP A2037 -5.776 115.201 142.328 1.00 72.67 C
ANISOU 2636 C TRP A2037 11742 6903 8966 -2876 -1007 887 C
ATOM 2637 O TRP A2037 -4.773 114.899 141.665 1.00 71.83 O
ANISOU 2637 O TRP A2037 11863 6753 8675 -2829 -1037 799 O
ATOM 2638 CB TRP A2037 -5.805 114.263 144.649 1.00 66.87 C
ANISOU 2638 CB TRP A2037 11031 6138 8236 -2809 -714 874 C
ATOM 2639 CG TRP A2037 -5.885 115.598 145.339 1.00 66.42 C
ANISOU 2639 CG TRP A2037 10756 6178 8304 -2697 -579 882 C
ATOM 2640 CD1 TRP A2037 -6.855 116.017 146.201 1.00 70.09 C
ANISOU 2640 CD1 TRP A2037 11016 6660 8955 -2734 -440 948 C
ATOM 2641 CD2 TRP A2037 -4.879 116.624 145.337 1.00 64.29 C
ANISOU 2641 CD2 TRP A2037 10478 5976 7972 -2527 -536 813 C
ATOM 2642 NE1 TRP A2037 -6.542 117.265 146.697 1.00 68.46 N
ANISOU 2642 NE1 TRP A2037 10688 6525 8798 -2601 -312 921 N
ATOM 2643 CE2 TRP A2037 -5.324 117.651 146.198 1.00 68.03 C
ANISOU 2643 CE2 TRP A2037 10751 6509 8586 -2474 -382 840 C
ATOM 2644 CE3 TRP A2037 -3.639 116.771 144.695 1.00 64.04 C
ANISOU 2644 CE3 TRP A2037 10591 5950 7792 -2417 -595 731 C
ATOM 2645 CZ2 TRP A2037 -4.576 118.808 146.432 1.00 66.11 C
ANISOU 2645 CZ2 TRP A2037 10462 6336 8319 -2324 -311 789 C
ATOM 2646 CZ3 TRP A2037 -2.899 117.918 144.927 1.00 64.19 C
ANISOU 2646 CZ3 TRP A2037 10539 6044 7807 -2265 -527 687 C
ATOM 2647 CH2 TRP A2037 -3.378 118.932 145.767 1.00 64.89 C
ANISOU 2647 CH2 TRP A2037 10437 6198 8019 -2223 -401 717 C
ATOM 2648 N VAL A2038 -6.389 116.385 142.264 1.00 69.37 N
ANISOU 2648 N VAL A2038 11059 6564 8735 -2865 -1025 955 N
ATOM 2649 CA VAL A2038 -5.962 117.531 141.449 1.00 68.31 C
ANISOU 2649 CA VAL A2038 10868 6489 8596 -2796 -1101 938 C
ATOM 2650 C VAL A2038 -5.813 118.780 142.299 1.00 70.65 C
ANISOU 2650 C VAL A2038 10947 6882 9016 -2633 -936 929 C
ATOM 2651 O VAL A2038 -6.400 118.867 143.383 1.00 68.53 O
ANISOU 2651 O VAL A2038 10526 6624 8889 -2621 -785 967 O
ATOM 2652 CB VAL A2038 -6.929 117.801 140.266 1.00 73.30 C
ANISOU 2652 CB VAL A2038 11408 7099 9345 -2979 -1351 1054 C
ATOM 2653 CG1 VAL A2038 -6.773 116.751 139.170 1.00 74.11 C
ANISOU 2653 CG1 VAL A2038 11816 7096 9247 -3142 -1529 1036 C
ATOM 2654 CG2 VAL A2038 -8.382 117.913 140.740 1.00 74.34 C
ANISOU 2654 CG2 VAL A2038 11234 7227 9786 -3087 -1372 1202 C
ATOM 2655 N CYS A2039 -5.081 119.776 141.768 1.00 69.39 N
ANISOU 2655 N CYS A2039 10782 6779 8805 -2525 -958 881 N
ATOM 2656 CA CYS A2039 -4.887 121.071 142.415 1.00 68.80 C
ANISOU 2656 CA CYS A2039 10518 6789 8834 -2377 -822 869 C
ATOM 2657 C CYS A2039 -6.246 121.770 142.581 1.00 72.43 C
ANISOU 2657 C CYS A2039 10666 7262 9594 -2449 -827 995 C
ATOM 2658 O CYS A2039 -6.988 121.905 141.606 1.00 71.68 O
ANISOU 2658 O CYS A2039 10474 7144 9618 -2576 -1029 1092 O
ATOM 2659 CB CYS A2039 -3.910 121.931 141.627 1.00 68.62 C
ANISOU 2659 CB CYS A2039 10553 6812 8705 -2275 -875 806 C
ATOM 2660 SG CYS A2039 -3.917 123.677 142.116 1.00 72.61 S
ANISOU 2660 SG CYS A2039 10799 7414 9375 -2135 -766 819 S
ATOM 2661 N PRO A2040 -6.605 122.198 143.808 1.00 70.15 N
ANISOU 2661 N PRO A2040 10223 6989 9441 -2382 -604 1002 N
ATOM 2662 CA PRO A2040 -7.920 122.840 143.993 1.00 72.80 C
ANISOU 2662 CA PRO A2040 10237 7308 10115 -2442 -563 1124 C
ATOM 2663 C PRO A2040 -8.066 124.223 143.356 1.00 80.41 C
ANISOU 2663 C PRO A2040 10992 8315 11245 -2385 -635 1172 C
ATOM 2664 O PRO A2040 -9.192 124.710 143.247 1.00 82.50 O
ANISOU 2664 O PRO A2040 10969 8545 11835 -2448 -655 1299 O
ATOM 2665 CB PRO A2040 -8.109 122.874 145.512 1.00 74.27 C
ANISOU 2665 CB PRO A2040 10388 7476 10356 -2386 -252 1092 C
ATOM 2666 CG PRO A2040 -6.789 122.655 146.084 1.00 75.72 C
ANISOU 2666 CG PRO A2040 10846 7691 10234 -2271 -167 960 C
ATOM 2667 CD PRO A2040 -5.871 122.067 145.079 1.00 69.96 C
ANISOU 2667 CD PRO A2040 10328 6974 9279 -2268 -380 909 C
ATOM 2668 N LEU A2041 -6.948 124.835 142.911 1.00 77.00 N
ANISOU 2668 N LEU A2041 10693 7946 10618 -2272 -680 1083 N
ATOM 2669 CA LEU A2041 -6.930 126.160 142.286 1.00 77.79 C
ANISOU 2669 CA LEU A2041 10633 8087 10835 -2213 -754 1118 C
ATOM 2670 C LEU A2041 -6.992 126.107 140.751 1.00 82.29 C
ANISOU 2670 C LEU A2041 11260 8643 11363 -2331 -1071 1181 C
ATOM 2671 O LEU A2041 -7.783 126.853 140.167 1.00 83.47 O
ANISOU 2671 O LEU A2041 11186 8775 11755 -2392 -1213 1307 O
ATOM 2672 CB LEU A2041 -5.684 126.955 142.724 1.00 76.24 C
ANISOU 2672 CB LEU A2041 10545 7962 10462 -2031 -611 991 C
ATOM 2673 CG LEU A2041 -5.876 128.329 143.396 1.00 81.88 C
ANISOU 2673 CG LEU A2041 11048 8703 11361 -1915 -426 997 C
ATOM 2674 CD1 LEU A2041 -4.520 129.004 143.628 1.00 80.09 C
ANISOU 2674 CD1 LEU A2041 10972 8542 10915 -1762 -349 875 C
ATOM 2675 CD2 LEU A2041 -6.757 129.277 142.559 1.00 85.34 C
ANISOU 2675 CD2 LEU A2041 11211 9128 12087 -1957 -567 1124 C
ATOM 2676 N CYS A2042 -6.147 125.258 140.098 1.00 76.80 N
ANISOU 2676 N CYS A2042 10876 7936 10369 -2370 -1177 1099 N
ATOM 2677 CA CYS A2042 -6.099 125.162 138.630 1.00 75.65 C
ANISOU 2677 CA CYS A2042 10871 7755 10116 -2503 -1452 1138 C
ATOM 2678 C CYS A2042 -6.526 123.788 138.059 1.00 78.39 C
ANISOU 2678 C CYS A2042 11407 8012 10365 -2702 -1617 1175 C
ATOM 2679 O CYS A2042 -6.769 123.694 136.855 1.00 78.29 O
ANISOU 2679 O CYS A2042 11510 7946 10290 -2864 -1869 1237 O
ATOM 2680 CB CYS A2042 -4.736 125.592 138.100 1.00 73.79 C
ANISOU 2680 CB CYS A2042 10853 7557 9626 -2394 -1426 1011 C
ATOM 2681 SG CYS A2042 -3.434 124.356 138.301 1.00 76.36 S
ANISOU 2681 SG CYS A2042 11536 7845 9632 -2341 -1301 850 S
ATOM 2682 N GLY A2043 -6.608 122.757 138.906 1.00 73.73 N
ANISOU 2682 N GLY A2043 10872 7397 9746 -2703 -1483 1140 N
ATOM 2683 CA GLY A2043 -7.072 121.429 138.510 1.00 73.61 C
ANISOU 2683 CA GLY A2043 11022 7291 9655 -2890 -1617 1176 C
ATOM 2684 C GLY A2043 -6.110 120.477 137.830 1.00 76.12 C
ANISOU 2684 C GLY A2043 11730 7547 9644 -2927 -1650 1061 C
ATOM 2685 O GLY A2043 -6.544 119.465 137.285 1.00 76.73 O
ANISOU 2685 O GLY A2043 11973 7533 9648 -3110 -1795 1098 O
ATOM 2686 N VAL A2044 -4.810 120.763 137.844 1.00 71.83 N
ANISOU 2686 N VAL A2044 11339 7035 8917 -2762 -1511 924 N
ATOM 2687 CA VAL A2044 -3.818 119.843 137.267 1.00 71.34 C
ANISOU 2687 CA VAL A2044 11633 6889 8584 -2775 -1485 807 C
ATOM 2688 C VAL A2044 -3.502 118.748 138.306 1.00 75.74 C
ANISOU 2688 C VAL A2044 12266 7413 9099 -2708 -1318 748 C
ATOM 2689 O VAL A2044 -3.646 118.985 139.509 1.00 74.70 O
ANISOU 2689 O VAL A2044 11945 7344 9092 -2600 -1182 761 O
ATOM 2690 CB VAL A2044 -2.543 120.563 136.747 1.00 73.48 C
ANISOU 2690 CB VAL A2044 12029 7180 8709 -2639 -1405 697 C
ATOM 2691 CG1 VAL A2044 -2.894 121.587 135.677 1.00 73.91 C
ANISOU 2691 CG1 VAL A2044 12046 7253 8782 -2731 -1588 762 C
ATOM 2692 CG2 VAL A2044 -1.744 121.207 137.879 1.00 70.99 C
ANISOU 2692 CG2 VAL A2044 11562 6957 8455 -2398 -1193 632 C
ATOM 2693 N GLY A2045 -3.062 117.584 137.842 1.00 73.32 N
ANISOU 2693 N GLY A2045 12253 6992 8613 -2777 -1322 684 N
ATOM 2694 CA GLY A2045 -2.752 116.447 138.708 1.00 73.01 C
ANISOU 2694 CA GLY A2045 12313 6895 8530 -2731 -1192 637 C
ATOM 2695 C GLY A2045 -1.533 116.606 139.594 1.00 75.63 C
ANISOU 2695 C GLY A2045 12644 7254 8837 -2502 -993 546 C
ATOM 2696 O GLY A2045 -0.786 117.575 139.449 1.00 73.39 O
ANISOU 2696 O GLY A2045 12309 7028 8549 -2371 -941 500 O
ATOM 2697 N LYS A2046 -1.322 115.632 140.518 1.00 73.91 N
ANISOU 2697 N LYS A2046 12490 6984 8608 -2465 -899 530 N
ATOM 2698 CA LYS A2046 -0.200 115.571 141.478 1.00 73.48 C
ANISOU 2698 CA LYS A2046 12454 6926 8541 -2277 -751 471 C
ATOM 2699 C LYS A2046 1.167 115.590 140.795 1.00 81.21 C
ANISOU 2699 C LYS A2046 13584 7834 9436 -2161 -691 374 C
ATOM 2700 O LYS A2046 2.141 116.043 141.397 1.00 80.19 O
ANISOU 2700 O LYS A2046 13396 7731 9341 -1992 -603 342 O
ATOM 2701 CB LYS A2046 -0.282 114.300 142.336 1.00 75.50 C
ANISOU 2701 CB LYS A2046 12815 7094 8777 -2307 -709 483 C
ATOM 2702 CG LYS A2046 -1.230 114.363 143.513 1.00 72.27 C
ANISOU 2702 CG LYS A2046 12250 6749 8460 -2352 -679 561 C
ATOM 2703 CD LYS A2046 -1.095 113.079 144.364 1.00 74.23 C
ANISOU 2703 CD LYS A2046 12646 6897 8662 -2371 -632 566 C
ATOM 2704 CE LYS A2046 -0.032 113.200 145.428 1.00 66.98 C
ANISOU 2704 CE LYS A2046 11752 5973 7726 -2213 -545 543 C
ATOM 2705 NZ LYS A2046 0.564 111.899 145.798 1.00 67.95 N
ANISOU 2705 NZ LYS A2046 12071 5955 7792 -2201 -538 532 N
ATOM 2706 N ASP A2047 1.243 115.047 139.557 1.00 81.84 N
ANISOU 2706 N ASP A2047 13876 7807 9412 -2265 -730 331 N
ATOM 2707 CA ASP A2047 2.447 114.978 138.719 1.00 82.34 C
ANISOU 2707 CA ASP A2047 14118 7768 9400 -2186 -635 231 C
ATOM 2708 C ASP A2047 3.106 116.363 138.543 1.00 82.62 C
ANISOU 2708 C ASP A2047 14012 7903 9476 -2054 -597 206 C
ATOM 2709 O ASP A2047 4.330 116.450 138.498 1.00 83.10 O
ANISOU 2709 O ASP A2047 14112 7906 9556 -1907 -471 139 O
ATOM 2710 CB ASP A2047 2.145 114.289 137.351 1.00 86.54 C
ANISOU 2710 CB ASP A2047 14934 8164 9784 -2375 -684 194 C
ATOM 2711 CG ASP A2047 1.003 114.895 136.524 1.00102.38 C
ANISOU 2711 CG ASP A2047 16920 10237 11744 -2571 -878 263 C
ATOM 2712 OD1 ASP A2047 -0.167 114.759 136.939 1.00104.40 O
ANISOU 2712 OD1 ASP A2047 17045 10553 12070 -2687 -1011 363 O
ATOM 2713 OD2 ASP A2047 1.279 115.436 135.424 1.00107.53 O
ANISOU 2713 OD2 ASP A2047 17700 10860 12298 -2624 -899 224 O
ATOM 2714 N GLN A2048 2.299 117.437 138.529 1.00 75.88 N
ANISOU 2714 N GLN A2048 12973 7191 8667 -2100 -700 270 N
ATOM 2715 CA GLN A2048 2.751 118.828 138.382 1.00 73.59 C
ANISOU 2715 CA GLN A2048 12538 7004 8418 -1991 -682 257 C
ATOM 2716 C GLN A2048 3.201 119.486 139.714 1.00 74.23 C
ANISOU 2716 C GLN A2048 12409 7183 8610 -1814 -604 272 C
ATOM 2717 O GLN A2048 3.540 120.678 139.733 1.00 72.91 O
ANISOU 2717 O GLN A2048 12111 7107 8486 -1722 -588 267 O
ATOM 2718 CB GLN A2048 1.651 119.682 137.703 1.00 75.34 C
ANISOU 2718 CB GLN A2048 12662 7309 8654 -2128 -840 330 C
ATOM 2719 CG GLN A2048 1.276 119.265 136.276 1.00100.02 C
ANISOU 2719 CG GLN A2048 16029 10333 11641 -2327 -956 325 C
ATOM 2720 CD GLN A2048 2.440 119.347 135.318 1.00131.77 C
ANISOU 2720 CD GLN A2048 20276 14260 15531 -2282 -846 215 C
ATOM 2721 OE1 GLN A2048 2.903 120.435 134.937 1.00127.87 O
ANISOU 2721 OE1 GLN A2048 19721 13824 15039 -2213 -827 195 O
ATOM 2722 NE2 GLN A2048 2.954 118.187 134.930 1.00129.89 N
ANISOU 2722 NE2 GLN A2048 20306 13860 15186 -2321 -749 140 N
ATOM 2723 N PHE A2049 3.200 118.724 140.822 1.00 68.72 N
ANISOU 2723 N PHE A2049 11706 6458 7946 -1783 -564 294 N
ATOM 2724 CA PHE A2049 3.587 119.248 142.125 1.00 66.35 C
ANISOU 2724 CA PHE A2049 11268 6226 7715 -1655 -509 315 C
ATOM 2725 C PHE A2049 5.033 118.983 142.491 1.00 73.54 C
ANISOU 2725 C PHE A2049 12243 7057 8642 -1505 -438 273 C
ATOM 2726 O PHE A2049 5.518 117.862 142.329 1.00 74.37 O
ANISOU 2726 O PHE A2049 12497 7027 8734 -1504 -410 249 O
ATOM 2727 CB PHE A2049 2.654 118.756 143.215 1.00 67.20 C
ANISOU 2727 CB PHE A2049 11330 6352 7850 -1728 -514 380 C
ATOM 2728 CG PHE A2049 1.378 119.544 143.351 1.00 67.55 C
ANISOU 2728 CG PHE A2049 11197 6501 7968 -1814 -541 442 C
ATOM 2729 CD1 PHE A2049 0.364 119.425 142.409 1.00 70.19 C
ANISOU 2729 CD1 PHE A2049 11511 6833 8324 -1960 -640 480 C
ATOM 2730 CD2 PHE A2049 1.164 120.360 144.453 1.00 68.56 C
ANISOU 2730 CD2 PHE A2049 11185 6707 8159 -1760 -467 471 C
ATOM 2731 CE1 PHE A2049 -0.828 120.130 142.552 1.00 71.39 C
ANISOU 2731 CE1 PHE A2049 11460 7059 8605 -2035 -670 558 C
ATOM 2732 CE2 PHE A2049 -0.029 121.070 144.594 1.00 71.63 C
ANISOU 2732 CE2 PHE A2049 11392 7164 8661 -1831 -455 530 C
ATOM 2733 CZ PHE A2049 -1.018 120.947 143.645 1.00 70.50 C
ANISOU 2733 CZ PHE A2049 11186 7017 8583 -1960 -559 579 C
ATOM 2734 N GLU A2050 5.717 120.033 143.000 1.00 71.49 N
ANISOU 2734 N GLU A2050 11862 6869 8433 -1381 -414 272 N
ATOM 2735 CA GLU A2050 7.122 120.003 143.413 1.00 71.45 C
ANISOU 2735 CA GLU A2050 11865 6795 8488 -1236 -376 257 C
ATOM 2736 C GLU A2050 7.232 120.150 144.917 1.00 76.01 C
ANISOU 2736 C GLU A2050 12393 7403 9085 -1200 -406 318 C
ATOM 2737 O GLU A2050 6.392 120.807 145.522 1.00 74.64 O
ANISOU 2737 O GLU A2050 12144 7334 8881 -1252 -411 347 O
ATOM 2738 CB GLU A2050 7.903 121.144 142.735 1.00 72.02 C
ANISOU 2738 CB GLU A2050 11855 6913 8596 -1140 -342 215 C
ATOM 2739 N GLU A2051 8.274 119.557 145.520 1.00 74.25 N
ANISOU 2739 N GLU A2051 12219 7070 8922 -1120 -423 343 N
ATOM 2740 CA GLU A2051 8.518 119.674 146.954 1.00 74.36 C
ANISOU 2740 CA GLU A2051 12234 7087 8934 -1106 -483 411 C
ATOM 2741 C GLU A2051 9.052 121.057 147.252 1.00 79.42 C
ANISOU 2741 C GLU A2051 12763 7816 9595 -1030 -496 414 C
ATOM 2742 O GLU A2051 9.853 121.581 146.478 1.00 80.32 O
ANISOU 2742 O GLU A2051 12803 7927 9786 -938 -475 379 O
ATOM 2743 CB GLU A2051 9.521 118.621 147.419 1.00 76.74 C
ANISOU 2743 CB GLU A2051 12616 7222 9318 -1052 -537 458 C
ATOM 2744 CG GLU A2051 9.391 118.294 148.892 1.00 88.71 C
ANISOU 2744 CG GLU A2051 14217 8711 10779 -1111 -624 543 C
ATOM 2745 CD GLU A2051 10.603 117.624 149.502 1.00107.53 C
ANISOU 2745 CD GLU A2051 16643 10934 13280 -1041 -733 621 C
ATOM 2746 OE1 GLU A2051 11.285 118.279 150.324 1.00 98.73 O
ANISOU 2746 OE1 GLU A2051 15502 9821 12191 -1007 -831 682 O
ATOM 2747 OE2 GLU A2051 10.866 116.445 149.167 1.00 98.89 O
ANISOU 2747 OE2 GLU A2051 15609 9699 12264 -1027 -728 628 O
ATOM 2748 N VAL A2052 8.587 121.661 148.350 1.00 75.74 N
ANISOU 2748 N VAL A2052 12300 7420 9057 -1080 -512 452 N
ATOM 2749 CA VAL A2052 9.033 122.977 148.810 1.00 74.39 C
ANISOU 2749 CA VAL A2052 12058 7323 8884 -1029 -526 459 C
ATOM 2750 C VAL A2052 10.278 122.712 149.647 1.00 79.81 C
ANISOU 2750 C VAL A2052 12803 7902 9620 -976 -644 527 C
ATOM 2751 O VAL A2052 10.182 122.121 150.736 1.00 80.80 O
ANISOU 2751 O VAL A2052 13059 7960 9679 -1049 -708 590 O
ATOM 2752 CB VAL A2052 7.922 123.702 149.610 1.00 77.95 C
ANISOU 2752 CB VAL A2052 12517 7865 9234 -1121 -459 464 C
ATOM 2753 CG1 VAL A2052 8.460 124.921 150.343 1.00 77.23 C
ANISOU 2753 CG1 VAL A2052 12416 7814 9114 -1087 -476 477 C
ATOM 2754 CG2 VAL A2052 6.766 124.093 148.705 1.00 77.41 C
ANISOU 2754 CG2 VAL A2052 12338 7891 9183 -1161 -369 420 C
ATOM 2755 N GLU A2053 11.451 123.074 149.098 1.00 76.45 N
ANISOU 2755 N GLU A2053 12282 7441 9325 -860 -679 524 N
ATOM 2756 CA GLU A2053 12.733 122.855 149.768 1.00 77.48 C
ANISOU 2756 CA GLU A2053 12422 7451 9566 -804 -817 610 C
ATOM 2757 C GLU A2053 13.245 124.116 150.451 1.00 80.82 C
ANISOU 2757 C GLU A2053 12813 7930 9967 -794 -895 645 C
ATOM 2758 O GLU A2053 13.273 125.173 149.829 1.00 80.19 O
ANISOU 2758 O GLU A2053 12624 7950 9897 -744 -827 588 O
ATOM 2759 CB GLU A2053 13.765 122.260 148.799 1.00 79.58 C
ANISOU 2759 CB GLU A2053 12597 7595 10043 -687 -797 603 C
ATOM 2760 CG GLU A2053 14.010 120.777 149.048 1.00 96.42 C
ANISOU 2760 CG GLU A2053 14817 9563 12257 -696 -843 657 C
ATOM 2761 CD GLU A2053 14.315 119.889 147.852 1.00130.20 C
ANISOU 2761 CD GLU A2053 19067 13726 16675 -624 -717 600 C
ATOM 2762 OE1 GLU A2053 14.582 120.422 146.749 1.00132.54 O
ANISOU 2762 OE1 GLU A2053 19279 14054 17025 -559 -594 520 O
ATOM 2763 OE2 GLU A2053 14.293 118.648 148.028 1.00126.32 O
ANISOU 2763 OE2 GLU A2053 18662 13101 16232 -642 -733 633 O
ATOM 2764 N GLU A2054 13.600 124.011 151.745 1.00 77.97 N
ANISOU 2764 N GLU A2054 12574 7498 9555 -860 -1046 743 N
ATOM 2765 CA GLU A2054 14.125 125.114 152.553 1.00 77.47 C
ANISOU 2765 CA GLU A2054 12535 7457 9442 -884 -1151 790 C
ATOM 2766 C GLU A2054 15.575 125.419 152.164 1.00 81.48 C
ANISOU 2766 C GLU A2054 12885 7894 10180 -766 -1265 844 C
ATOM 2767 O GLU A2054 16.456 124.570 152.334 1.00 82.37 O
ANISOU 2767 O GLU A2054 12974 7855 10467 -729 -1397 938 O
ATOM 2768 CB GLU A2054 14.045 124.794 154.056 1.00 80.38 C
ANISOU 2768 CB GLU A2054 13139 7744 9659 -1026 -1294 886 C
ATOM 2769 CG GLU A2054 12.642 124.731 154.643 1.00 94.63 C
ANISOU 2769 CG GLU A2054 15114 9610 11232 -1160 -1151 835 C
ATOM 2770 CD GLU A2054 12.531 124.339 156.110 1.00123.56 C
ANISOU 2770 CD GLU A2054 19059 13171 14718 -1322 -1263 922 C
ATOM 2771 OE1 GLU A2054 13.507 124.535 156.873 1.00110.62 O
ANISOU 2771 OE1 GLU A2054 17517 11435 13077 -1362 -1480 1027 O
ATOM 2772 OE2 GLU A2054 11.442 123.856 156.500 1.00123.99 O
ANISOU 2772 OE2 GLU A2054 19248 13233 14631 -1425 -1135 892 O
ATOM 2773 N ARG A 237 15.820 126.633 151.637 1.00 77.10 N
ANISOU 2773 N ARG A 237 12208 7438 9649 -706 -1207 791 N
ATOM 2774 CA ARG A 237 17.153 127.084 151.226 1.00 76.40 C
ANISOU 2774 CA ARG A 237 11950 7293 9786 -598 -1286 835 C
ATOM 2775 C ARG A 237 17.563 128.295 152.052 1.00 77.37 C
ANISOU 2775 C ARG A 237 12110 7453 9836 -649 -1415 885 C
ATOM 2776 O ARG A 237 16.832 129.288 152.096 1.00 75.65 O
ANISOU 2776 O ARG A 237 11935 7366 9444 -689 -1312 808 O
ATOM 2777 CB ARG A 237 17.196 127.415 149.720 1.00 76.00 C
ANISOU 2777 CB ARG A 237 11730 7307 9842 -483 -1092 725 C
ATOM 2778 CG ARG A 237 16.840 126.253 148.812 1.00 88.41 C
ANISOU 2778 CG ARG A 237 13295 8820 11475 -447 -959 669 C
ATOM 2779 CD ARG A 237 16.445 126.705 147.418 1.00100.25 C
ANISOU 2779 CD ARG A 237 14724 10412 12955 -401 -763 545 C
ATOM 2780 NE ARG A 237 15.787 125.619 146.689 1.00111.85 N
ANISOU 2780 NE ARG A 237 16265 11843 14388 -424 -648 485 N
ATOM 2781 CZ ARG A 237 14.469 125.477 146.585 1.00129.25 C
ANISOU 2781 CZ ARG A 237 18561 14145 16405 -517 -594 434 C
ATOM 2782 NH1 ARG A 237 13.652 126.370 147.134 1.00119.05 N
ANISOU 2782 NH1 ARG A 237 17283 12986 14963 -582 -613 429 N
ATOM 2783 NH2 ARG A 237 13.956 124.447 145.922 1.00113.78 N
ANISOU 2783 NH2 ARG A 237 16675 12134 14423 -549 -514 391 N
ATOM 2784 N ASP A 238 18.728 128.203 152.721 1.00 74.45 N
ANISOU 2784 N ASP A 238 11727 6950 9612 -655 -1648 1024 N
ATOM 2785 CA ASP A 238 19.312 129.277 153.541 1.00 73.98 C
ANISOU 2785 CA ASP A 238 11719 6889 9501 -722 -1823 1097 C
ATOM 2786 C ASP A 238 19.596 130.516 152.706 1.00 73.21 C
ANISOU 2786 C ASP A 238 11450 6901 9466 -633 -1711 1019 C
ATOM 2787 O ASP A 238 19.429 131.636 153.190 1.00 72.72 O
ANISOU 2787 O ASP A 238 11476 6913 9241 -701 -1731 1001 O
ATOM 2788 CB ASP A 238 20.602 128.806 154.236 1.00 78.48 C
ANISOU 2788 CB ASP A 238 12263 7270 10287 -741 -2129 1285 C
ATOM 2789 CG ASP A 238 20.400 127.968 155.494 1.00 93.49 C
ANISOU 2789 CG ASP A 238 14420 9057 12047 -894 -2330 1399 C
ATOM 2790 OD1 ASP A 238 19.250 127.505 155.729 1.00 93.18 O
ANISOU 2790 OD1 ASP A 238 14560 9074 11770 -968 -2192 1321 O
ATOM 2791 OD2 ASP A 238 21.394 127.767 156.242 1.00101.06 O
ANISOU 2791 OD2 ASP A 238 15398 9858 13141 -951 -2635 1575 O
ATOM 2792 N SER A 239 19.988 130.307 151.439 1.00 66.49 N
ANISOU 2792 N SER A 239 10380 6048 8836 -489 -1574 966 N
ATOM 2793 CA SER A 239 20.273 131.359 150.476 1.00 64.22 C
ANISOU 2793 CA SER A 239 9930 5851 8621 -400 -1444 886 C
ATOM 2794 C SER A 239 19.055 132.280 150.257 1.00 66.94 C
ANISOU 2794 C SER A 239 10357 6375 8701 -443 -1278 759 C
ATOM 2795 O SER A 239 19.230 133.496 150.135 1.00 65.62 O
ANISOU 2795 O SER A 239 10143 6285 8504 -433 -1261 730 O
ATOM 2796 CB SER A 239 20.748 130.754 149.159 1.00 66.90 C
ANISOU 2796 CB SER A 239 10088 6132 9201 -266 -1283 839 C
ATOM 2797 OG SER A 239 19.714 130.039 148.501 1.00 77.24 O
ANISOU 2797 OG SER A 239 11469 7492 10387 -269 -1100 733 O
ATOM 2798 N GLU A 240 17.829 131.704 150.262 1.00 63.14 N
ANISOU 2798 N GLU A 240 9993 5946 8051 -496 -1166 695 N
ATOM 2799 CA GLU A 240 16.581 132.452 150.078 1.00 61.85 C
ANISOU 2799 CA GLU A 240 9883 5928 7691 -538 -1009 594 C
ATOM 2800 C GLU A 240 16.337 133.373 151.256 1.00 65.59 C
ANISOU 2800 C GLU A 240 10503 6428 7989 -640 -1071 618 C
ATOM 2801 O GLU A 240 15.819 134.474 151.072 1.00 64.84 O
ANISOU 2801 O GLU A 240 10392 6433 7810 -643 -964 552 O
ATOM 2802 CB GLU A 240 15.367 131.508 149.894 1.00 63.16 C
ANISOU 2802 CB GLU A 240 10122 6116 7761 -583 -894 545 C
ATOM 2803 CG GLU A 240 15.455 130.537 148.726 1.00 76.99 C
ANISOU 2803 CG GLU A 240 11783 7828 9641 -510 -816 509 C
ATOM 2804 CD GLU A 240 15.780 131.108 147.359 1.00 99.15 C
ANISOU 2804 CD GLU A 240 14448 10682 12543 -421 -708 438 C
ATOM 2805 OE1 GLU A 240 15.002 131.960 146.871 1.00 72.33 O
ANISOU 2805 OE1 GLU A 240 11028 7403 9051 -437 -618 373 O
ATOM 2806 OE2 GLU A 240 16.793 130.672 146.759 1.00 98.42 O
ANISOU 2806 OE2 GLU A 240 14272 10493 12631 -339 -701 450 O
ATOM 2807 N VAL A 241 16.697 132.900 152.472 1.00 62.76 N
ANISOU 2807 N VAL A 241 10309 5963 7574 -735 -1243 717 N
ATOM 2808 CA VAL A 241 16.571 133.624 153.738 1.00 62.46 C
ANISOU 2808 CA VAL A 241 10487 5907 7339 -868 -1319 752 C
ATOM 2809 C VAL A 241 17.592 134.754 153.718 1.00 66.15 C
ANISOU 2809 C VAL A 241 10878 6375 7880 -839 -1432 786 C
ATOM 2810 O VAL A 241 17.249 135.884 154.066 1.00 64.36 O
ANISOU 2810 O VAL A 241 10740 6205 7509 -891 -1366 739 O
ATOM 2811 CB VAL A 241 16.763 132.690 154.977 1.00 67.15 C
ANISOU 2811 CB VAL A 241 11309 6361 7845 -998 -1505 864 C
ATOM 2812 CG1 VAL A 241 16.655 133.467 156.296 1.00 67.40 C
ANISOU 2812 CG1 VAL A 241 11626 6350 7634 -1167 -1579 897 C
ATOM 2813 CG2 VAL A 241 15.767 131.539 154.955 1.00 66.87 C
ANISOU 2813 CG2 VAL A 241 11340 6321 7746 -1026 -1386 830 C
ATOM 2814 N GLU A 242 18.840 134.436 153.295 1.00 64.83 N
ANISOU 2814 N GLU A 242 10539 6133 7961 -754 -1586 868 N
ATOM 2815 CA GLU A 242 19.958 135.374 153.191 1.00 65.97 C
ANISOU 2815 CA GLU A 242 10567 6260 8240 -719 -1712 921 C
ATOM 2816 C GLU A 242 19.575 136.548 152.280 1.00 68.49 C
ANISOU 2816 C GLU A 242 10769 6722 8533 -643 -1510 798 C
ATOM 2817 O GLU A 242 19.766 137.696 152.672 1.00 69.42 O
ANISOU 2817 O GLU A 242 10945 6868 8565 -691 -1552 798 O
ATOM 2818 CB GLU A 242 21.231 134.654 152.692 1.00 68.66 C
ANISOU 2818 CB GLU A 242 10686 6482 8919 -616 -1843 1021 C
ATOM 2819 CG GLU A 242 22.502 135.483 152.846 1.00 83.75 C
ANISOU 2819 CG GLU A 242 12485 8332 11005 -610 -2035 1122 C
ATOM 2820 CD GLU A 242 23.798 134.834 152.393 1.00110.89 C
ANISOU 2820 CD GLU A 242 15670 11626 14837 -507 -2149 1237 C
ATOM 2821 OE1 GLU A 242 24.327 135.241 151.334 1.00106.86 O
ANISOU 2821 OE1 GLU A 242 14931 11140 14532 -384 -2016 1191 O
ATOM 2822 OE2 GLU A 242 24.317 133.961 153.127 1.00110.99 O
ANISOU 2822 OE2 GLU A 242 15715 11487 14970 -557 -2374 1382 O
ATOM 2823 N MET A 243 18.970 136.251 151.108 1.00 62.80 N
ANISOU 2823 N MET A 243 9914 6081 7864 -543 -1302 697 N
ATOM 2824 CA MET A 243 18.513 137.227 150.120 1.00 60.48 C
ANISOU 2824 CA MET A 243 9513 5913 7553 -477 -1122 589 C
ATOM 2825 C MET A 243 17.322 138.027 150.636 1.00 63.20 C
ANISOU 2825 C MET A 243 9999 6344 7669 -556 -1011 523 C
ATOM 2826 O MET A 243 17.245 139.227 150.378 1.00 62.29 O
ANISOU 2826 O MET A 243 9845 6299 7524 -539 -948 478 O
ATOM 2827 CB MET A 243 18.150 136.536 148.808 1.00 61.96 C
ANISOU 2827 CB MET A 243 9573 6133 7835 -387 -965 518 C
ATOM 2828 CG MET A 243 19.337 136.004 148.052 1.00 67.25 C
ANISOU 2828 CG MET A 243 10086 6710 8755 -291 -992 555 C
ATOM 2829 SD MET A 243 18.802 135.225 146.502 1.00 72.97 S
ANISOU 2829 SD MET A 243 10747 7453 9525 -223 -777 453 S
ATOM 2830 CE MET A 243 20.375 134.891 145.769 1.00 71.68 C
ANISOU 2830 CE MET A 243 10411 7152 9671 -113 -762 492 C
ATOM 2831 N MET A 244 16.387 137.375 151.351 1.00 59.37 N
ANISOU 2831 N MET A 244 9674 5842 7042 -642 -967 518 N
ATOM 2832 CA MET A 244 15.239 138.079 151.913 1.00 59.22 C
ANISOU 2832 CA MET A 244 9785 5873 6842 -719 -823 459 C
ATOM 2833 C MET A 244 15.731 139.092 152.977 1.00 63.43 C
ANISOU 2833 C MET A 244 10485 6360 7254 -808 -909 491 C
ATOM 2834 O MET A 244 15.304 140.247 152.964 1.00 63.75 O
ANISOU 2834 O MET A 244 10535 6454 7233 -810 -789 432 O
ATOM 2835 CB MET A 244 14.197 137.091 152.472 1.00 62.35 C
ANISOU 2835 CB MET A 244 10318 6240 7134 -800 -742 453 C
ATOM 2836 CG MET A 244 12.859 137.722 152.823 1.00 66.53 C
ANISOU 2836 CG MET A 244 10922 6811 7544 -858 -526 383 C
ATOM 2837 SD MET A 244 12.030 138.434 151.383 1.00 70.76 S
ANISOU 2837 SD MET A 244 11200 7475 8213 -747 -356 303 S
ATOM 2838 CE MET A 244 12.135 140.195 151.770 1.00 66.65 C
ANISOU 2838 CE MET A 244 10716 6973 7636 -753 -287 269 C
ATOM 2839 N ALA A 245 16.690 138.681 153.827 1.00 58.91 N
ANISOU 2839 N ALA A 245 10039 5678 6666 -882 -1136 595 N
ATOM 2840 CA ALA A 245 17.315 139.537 154.839 1.00 59.32 C
ANISOU 2840 CA ALA A 245 10280 5661 6597 -994 -1278 649 C
ATOM 2841 C ALA A 245 17.991 140.785 154.180 1.00 62.47 C
ANISOU 2841 C ALA A 245 10515 6120 7103 -914 -1293 629 C
ATOM 2842 O ALA A 245 17.857 141.913 154.681 1.00 61.23 O
ANISOU 2842 O ALA A 245 10493 5965 6809 -982 -1255 599 O
ATOM 2843 CB ALA A 245 18.349 138.734 155.621 1.00 61.18 C
ANISOU 2843 CB ALA A 245 10624 5758 6863 -1079 -1576 794 C
ATOM 2844 N GLN A 246 18.713 140.559 153.068 1.00 57.74 N
ANISOU 2844 N GLN A 246 9641 5553 6743 -776 -1332 644 N
ATOM 2845 CA GLN A 246 19.411 141.603 152.332 1.00 57.72 C
ANISOU 2845 CA GLN A 246 9467 5600 6865 -694 -1338 630 C
ATOM 2846 C GLN A 246 18.413 142.545 151.661 1.00 58.92 C
ANISOU 2846 C GLN A 246 9570 5873 6944 -644 -1097 506 C
ATOM 2847 O GLN A 246 18.591 143.749 151.768 1.00 58.01 O
ANISOU 2847 O GLN A 246 9482 5780 6779 -661 -1087 486 O
ATOM 2848 CB GLN A 246 20.396 141.003 151.315 1.00 59.67 C
ANISOU 2848 CB GLN A 246 9455 5826 7393 -569 -1395 672 C
ATOM 2849 CG GLN A 246 21.592 140.300 151.960 1.00 69.76 C
ANISOU 2849 CG GLN A 246 10726 6959 8822 -608 -1661 822 C
ATOM 2850 CD GLN A 246 22.391 139.466 150.988 1.00 84.60 C
ANISOU 2850 CD GLN A 246 12353 8784 11006 -478 -1655 857 C
ATOM 2851 OE1 GLN A 246 21.973 139.176 149.855 1.00 82.86 O
ANISOU 2851 OE1 GLN A 246 12013 8629 10843 -375 -1445 761 O
ATOM 2852 NE2 GLN A 246 23.539 138.998 151.438 1.00 71.53 N
ANISOU 2852 NE2 GLN A 246 10629 6988 9559 -492 -1885 1002 N
ATOM 2853 N ALA A 247 17.332 142.012 151.044 1.00 54.29 N
ANISOU 2853 N ALA A 247 8926 5351 6350 -597 -918 434 N
ATOM 2854 CA ALA A 247 16.274 142.835 150.445 1.00 53.27 C
ANISOU 2854 CA ALA A 247 8741 5319 6182 -560 -713 341 C
ATOM 2855 C ALA A 247 15.583 143.716 151.489 1.00 60.74 C
ANISOU 2855 C ALA A 247 9882 6244 6954 -657 -623 311 C
ATOM 2856 O ALA A 247 15.235 144.851 151.175 1.00 62.82 O
ANISOU 2856 O ALA A 247 10099 6554 7216 -628 -515 260 O
ATOM 2857 CB ALA A 247 15.258 141.968 149.727 1.00 53.07 C
ANISOU 2857 CB ALA A 247 8636 5339 6191 -524 -587 299 C
ATOM 2858 N LEU A 248 15.422 143.217 152.729 1.00 59.29 N
ANISOU 2858 N LEU A 248 9933 5971 6622 -779 -658 344 N
ATOM 2859 CA LEU A 248 14.835 143.956 153.854 1.00 60.23 C
ANISOU 2859 CA LEU A 248 10302 6031 6549 -898 -546 312 C
ATOM 2860 C LEU A 248 15.755 145.089 154.301 1.00 64.55 C
ANISOU 2860 C LEU A 248 10952 6540 7036 -946 -664 335 C
ATOM 2861 O LEU A 248 15.279 146.199 154.548 1.00 64.36 O
ANISOU 2861 O LEU A 248 11011 6511 6931 -972 -511 274 O
ATOM 2862 CB LEU A 248 14.554 143.025 155.056 1.00 61.55 C
ANISOU 2862 CB LEU A 248 10742 6094 6552 -1040 -571 349 C
ATOM 2863 CG LEU A 248 13.396 142.041 154.932 1.00 65.53 C
ANISOU 2863 CG LEU A 248 11217 6614 7068 -1034 -406 317 C
ATOM 2864 CD1 LEU A 248 13.382 141.038 156.130 1.00 66.25 C
ANISOU 2864 CD1 LEU A 248 11596 6587 6989 -1186 -479 371 C
ATOM 2865 CD2 LEU A 248 12.058 142.765 154.783 1.00 66.54 C
ANISOU 2865 CD2 LEU A 248 11299 6776 7208 -1014 -103 226 C
ATOM 2866 N GLY A 249 17.052 144.779 154.428 1.00 61.57 N
ANISOU 2866 N GLY A 249 10563 6118 6713 -964 -934 431 N
ATOM 2867 CA GLY A 249 18.101 145.719 154.807 1.00 61.92 C
ANISOU 2867 CA GLY A 249 10678 6114 6733 -1020 -1109 482 C
ATOM 2868 C GLY A 249 18.125 146.915 153.877 1.00 66.12 C
ANISOU 2868 C GLY A 249 11021 6738 7362 -911 -999 417 C
ATOM 2869 O GLY A 249 18.115 148.060 154.340 1.00 68.67 O
ANISOU 2869 O GLY A 249 11487 7034 7571 -976 -961 388 O
ATOM 2870 N ILE A 250 18.062 146.651 152.559 1.00 59.13 N
ANISOU 2870 N ILE A 250 9845 5953 6670 -757 -929 387 N
ATOM 2871 CA ILE A 250 18.026 147.669 151.526 1.00 57.38 C
ANISOU 2871 CA ILE A 250 9439 5820 6545 -654 -827 330 C
ATOM 2872 C ILE A 250 16.728 148.492 151.622 1.00 61.99 C
ANISOU 2872 C ILE A 250 10088 6433 7031 -660 -583 239 C
ATOM 2873 O ILE A 250 16.779 149.716 151.535 1.00 62.22 O
ANISOU 2873 O ILE A 250 10120 6474 7047 -651 -530 206 O
ATOM 2874 CB ILE A 250 18.308 147.062 150.129 1.00 58.98 C
ANISOU 2874 CB ILE A 250 9368 6092 6949 -520 -821 328 C
ATOM 2875 CG1 ILE A 250 19.830 146.983 149.919 1.00 60.39 C
ANISOU 2875 CG1 ILE A 250 9439 6226 7280 -496 -1018 411 C
ATOM 2876 CG2 ILE A 250 17.688 147.908 149.004 1.00 56.85 C
ANISOU 2876 CG2 ILE A 250 8950 5918 6732 -431 -657 252 C
ATOM 2877 CD1 ILE A 250 20.378 145.661 149.710 1.00 70.19 C
ANISOU 2877 CD1 ILE A 250 10595 7417 8659 -464 -1112 472 C
ATOM 2878 N MET A 251 15.598 147.845 151.877 1.00 59.67 N
ANISOU 2878 N MET A 251 9850 6133 6687 -681 -435 205 N
ATOM 2879 CA MET A 251 14.328 148.556 152.018 1.00 60.28 C
ANISOU 2879 CA MET A 251 9963 6212 6728 -684 -185 132 C
ATOM 2880 C MET A 251 14.304 149.440 153.275 1.00 65.16 C
ANISOU 2880 C MET A 251 10869 6724 7163 -807 -116 110 C
ATOM 2881 O MET A 251 13.765 150.547 153.224 1.00 66.47 O
ANISOU 2881 O MET A 251 11035 6881 7338 -788 59 53 O
ATOM 2882 CB MET A 251 13.163 147.571 152.004 1.00 63.17 C
ANISOU 2882 CB MET A 251 10301 6583 7119 -684 -47 116 C
ATOM 2883 CG MET A 251 11.830 148.245 152.119 1.00 68.19 C
ANISOU 2883 CG MET A 251 10930 7198 7782 -682 221 57 C
ATOM 2884 SD MET A 251 10.622 147.184 152.907 1.00 74.98 S
ANISOU 2884 SD MET A 251 11903 7990 8595 -762 395 48 S
ATOM 2885 CE MET A 251 11.355 146.966 154.546 1.00 73.27 C
ANISOU 2885 CE MET A 251 12096 7642 8101 -937 319 65 C
ATOM 2886 N VAL A 252 14.908 148.972 154.386 1.00 60.23 N
ANISOU 2886 N VAL A 252 10505 6005 6374 -942 -259 159 N
ATOM 2887 CA VAL A 252 14.965 149.744 155.637 1.00 59.94 C
ANISOU 2887 CA VAL A 252 10814 5843 6118 -1098 -215 141 C
ATOM 2888 C VAL A 252 15.854 150.962 155.425 1.00 62.33 C
ANISOU 2888 C VAL A 252 11098 6153 6432 -1089 -325 149 C
ATOM 2889 O VAL A 252 15.437 152.071 155.756 1.00 62.40 O
ANISOU 2889 O VAL A 252 11237 6112 6362 -1123 -149 84 O
ATOM 2890 CB VAL A 252 15.356 148.866 156.870 1.00 64.40 C
ANISOU 2890 CB VAL A 252 11698 6289 6482 -1275 -369 206 C
ATOM 2891 CG1 VAL A 252 15.680 149.710 158.107 1.00 65.82 C
ANISOU 2891 CG1 VAL A 252 12279 6325 6404 -1468 -389 203 C
ATOM 2892 CG2 VAL A 252 14.257 147.854 157.188 1.00 63.94 C
ANISOU 2892 CG2 VAL A 252 11699 6209 6387 -1300 -185 177 C
ATOM 2893 N VAL A 253 17.029 150.765 154.793 1.00 58.40 N
ANISOU 2893 N VAL A 253 10414 5712 6063 -1030 -587 225 N
ATOM 2894 CA VAL A 253 17.988 151.830 154.488 1.00 58.58 C
ANISOU 2894 CA VAL A 253 10376 5748 6133 -1015 -715 247 C
ATOM 2895 C VAL A 253 17.332 152.946 153.617 1.00 60.68 C
ANISOU 2895 C VAL A 253 10475 6089 6491 -896 -490 158 C
ATOM 2896 O VAL A 253 17.438 154.121 153.976 1.00 60.30 O
ANISOU 2896 O VAL A 253 10559 5992 6358 -947 -441 127 O
ATOM 2897 CB VAL A 253 19.331 151.282 153.906 1.00 62.60 C
ANISOU 2897 CB VAL A 253 10674 6290 6821 -962 -1000 351 C
ATOM 2898 CG1 VAL A 253 20.245 152.418 153.444 1.00 61.95 C
ANISOU 2898 CG1 VAL A 253 10488 6227 6822 -934 -1098 369 C
ATOM 2899 CG2 VAL A 253 20.066 150.423 154.942 1.00 63.74 C
ANISOU 2899 CG2 VAL A 253 11008 6323 6886 -1103 -1261 462 C
ATOM 2900 N ALA A 254 16.598 152.578 152.546 1.00 55.95 N
ANISOU 2900 N ALA A 254 9616 5591 6052 -757 -359 123 N
ATOM 2901 CA ALA A 254 15.895 153.550 151.693 1.00 54.79 C
ANISOU 2901 CA ALA A 254 9303 5503 6011 -653 -175 61 C
ATOM 2902 C ALA A 254 14.747 154.248 152.446 1.00 62.89 C
ANISOU 2902 C ALA A 254 10501 6444 6949 -704 91 -9 C
ATOM 2903 O ALA A 254 14.544 155.439 152.260 1.00 64.69 O
ANISOU 2903 O ALA A 254 10717 6658 7206 -675 199 -48 O
ATOM 2904 CB ALA A 254 15.383 152.877 150.434 1.00 53.80 C
ANISOU 2904 CB ALA A 254 8900 5482 6059 -528 -138 60 C
ATOM 2905 N SER A 255 14.043 153.540 153.339 1.00 61.21 N
ANISOU 2905 N SER A 255 10466 6156 6634 -786 211 -25 N
ATOM 2906 CA SER A 255 12.967 154.137 154.140 1.00 63.07 C
ANISOU 2906 CA SER A 255 10886 6279 6799 -844 511 -96 C
ATOM 2907 C SER A 255 13.494 155.249 155.056 1.00 69.80 C
ANISOU 2907 C SER A 255 12042 7014 7463 -963 528 -125 C
ATOM 2908 O SER A 255 12.933 156.333 155.098 1.00 69.11 O
ANISOU 2908 O SER A 255 11983 6867 7408 -943 751 -187 O
ATOM 2909 CB SER A 255 12.270 153.080 154.993 1.00 66.91 C
ANISOU 2909 CB SER A 255 11544 6691 7186 -935 627 -103 C
ATOM 2910 OG SER A 255 11.727 152.052 154.185 1.00 78.20 O
ANISOU 2910 OG SER A 255 12711 8218 8785 -839 619 -77 O
ATOM 2911 N VAL A 256 14.557 154.954 155.807 1.00 69.14 N
ANISOU 2911 N VAL A 256 12194 6883 7194 -1097 285 -72 N
ATOM 2912 CA VAL A 256 15.172 155.852 156.780 1.00 70.21 C
ANISOU 2912 CA VAL A 256 12675 6892 7110 -1255 239 -82 C
ATOM 2913 C VAL A 256 15.912 157.004 156.094 1.00 74.58 C
ANISOU 2913 C VAL A 256 13084 7499 7755 -1186 135 -76 C
ATOM 2914 O VAL A 256 15.752 158.145 156.507 1.00 76.69 O
ANISOU 2914 O VAL A 256 13532 7673 7932 -1239 285 -135 O
ATOM 2915 CB VAL A 256 16.058 155.028 157.771 1.00 74.76 C
ANISOU 2915 CB VAL A 256 13539 7390 7477 -1439 -44 3 C
ATOM 2916 CG1 VAL A 256 17.046 155.903 158.546 1.00 76.01 C
ANISOU 2916 CG1 VAL A 256 14010 7435 7435 -1611 -224 34 C
ATOM 2917 CG2 VAL A 256 15.192 154.220 158.732 1.00 75.75 C
ANISOU 2917 CG2 VAL A 256 13930 7411 7440 -1555 130 -25 C
ATOM 2918 N CYS A 257 16.679 156.719 155.031 1.00 69.28 N
ANISOU 2918 N CYS A 257 12094 6963 7264 -1068 -91 -11 N
ATOM 2919 CA CYS A 257 17.488 157.722 154.347 1.00 67.74 C
ANISOU 2919 CA CYS A 257 11758 6820 7160 -1011 -209 5 C
ATOM 2920 C CYS A 257 16.767 158.507 153.259 1.00 69.87 C
ANISOU 2920 C CYS A 257 11767 7167 7612 -849 -8 -54 C
ATOM 2921 O CYS A 257 17.012 159.708 153.149 1.00 71.62 O
ANISOU 2921 O CYS A 257 12020 7364 7829 -848 23 -79 O
ATOM 2922 CB CYS A 257 18.767 157.095 153.804 1.00 67.28 C
ANISOU 2922 CB CYS A 257 11513 6838 7214 -983 -530 108 C
ATOM 2923 SG CYS A 257 19.768 156.255 155.060 1.00 73.01 S
ANISOU 2923 SG CYS A 257 12516 7450 7775 -1182 -840 217 S
ATOM 2924 N TRP A 258 15.943 157.865 152.420 1.00 62.94 N
ANISOU 2924 N TRP A 258 10638 6377 6898 -723 98 -64 N
ATOM 2925 CA TRP A 258 15.335 158.599 151.308 1.00 61.51 C
ANISOU 2925 CA TRP A 258 10205 6264 6903 -584 227 -93 C
ATOM 2926 C TRP A 258 13.960 159.238 151.606 1.00 65.39 C
ANISOU 2926 C TRP A 258 10735 6670 7441 -564 543 -159 C
ATOM 2927 O TRP A 258 13.681 160.310 151.065 1.00 63.42 O
ANISOU 2927 O TRP A 258 10380 6416 7302 -494 636 -179 O
ATOM 2928 CB TRP A 258 15.270 157.729 150.039 1.00 59.00 C
ANISOU 2928 CB TRP A 258 9584 6076 6755 -469 139 -55 C
ATOM 2929 CG TRP A 258 16.549 157.779 149.249 1.00 59.78 C
ANISOU 2929 CG TRP A 258 9556 6252 6906 -435 -84 -8 C
ATOM 2930 CD1 TRP A 258 17.549 156.849 149.242 1.00 62.55 C
ANISOU 2930 CD1 TRP A 258 9888 6625 7252 -460 -283 48 C
ATOM 2931 CD2 TRP A 258 16.999 158.861 148.411 1.00 59.26 C
ANISOU 2931 CD2 TRP A 258 9370 6225 6920 -378 -114 -9 C
ATOM 2932 NE1 TRP A 258 18.599 157.287 148.462 1.00 61.44 N
ANISOU 2932 NE1 TRP A 258 9614 6530 7199 -419 -414 80 N
ATOM 2933 CE2 TRP A 258 18.279 158.511 147.925 1.00 62.20 C
ANISOU 2933 CE2 TRP A 258 9655 6644 7333 -372 -314 43 C
ATOM 2934 CE3 TRP A 258 16.443 160.098 148.029 1.00 61.02 C
ANISOU 2934 CE3 TRP A 258 9548 6436 7199 -330 17 -43 C
ATOM 2935 CZ2 TRP A 258 19.016 159.351 147.088 1.00 60.93 C
ANISOU 2935 CZ2 TRP A 258 9378 6521 7251 -331 -375 54 C
ATOM 2936 CZ3 TRP A 258 17.166 160.924 147.176 1.00 62.16 C
ANISOU 2936 CZ3 TRP A 258 9584 6627 7408 -289 -68 -28 C
ATOM 2937 CH2 TRP A 258 18.446 160.559 146.736 1.00 62.29 C
ANISOU 2937 CH2 TRP A 258 9532 6692 7445 -294 -256 16 C
ATOM 2938 N LEU A 259 13.105 158.590 152.425 1.00 63.09 N
ANISOU 2938 N LEU A 259 10580 6299 7091 -621 716 -186 N
ATOM 2939 CA LEU A 259 11.751 159.089 152.700 1.00 63.51 C
ANISOU 2939 CA LEU A 259 10635 6250 7246 -595 1052 -241 C
ATOM 2940 C LEU A 259 11.696 160.492 153.317 1.00 68.28 C
ANISOU 2940 C LEU A 259 11441 6717 7787 -640 1239 -303 C
ATOM 2941 O LEU A 259 10.904 161.295 152.810 1.00 68.29 O
ANISOU 2941 O LEU A 259 11268 6685 7993 -541 1427 -320 O
ATOM 2942 CB LEU A 259 10.909 158.110 153.523 1.00 64.37 C
ANISOU 2942 CB LEU A 259 10872 6284 7302 -663 1223 -260 C
ATOM 2943 CG LEU A 259 10.366 156.901 152.778 1.00 68.32 C
ANISOU 2943 CG LEU A 259 11110 6891 7958 -587 1163 -211 C
ATOM 2944 CD1 LEU A 259 9.667 155.961 153.735 1.00 70.28 C
ANISOU 2944 CD1 LEU A 259 11529 7051 8124 -677 1330 -231 C
ATOM 2945 CD2 LEU A 259 9.373 157.313 151.666 1.00 69.83 C
ANISOU 2945 CD2 LEU A 259 10954 7123 8453 -446 1266 -191 C
ATOM 2946 N PRO A 260 12.500 160.862 154.355 1.00 64.96 N
ANISOU 2946 N PRO A 260 11380 6201 7102 -791 1186 -329 N
ATOM 2947 CA PRO A 260 12.407 162.241 154.869 1.00 65.13 C
ANISOU 2947 CA PRO A 260 11607 6078 7062 -837 1383 -395 C
ATOM 2948 C PRO A 260 12.599 163.298 153.780 1.00 67.59 C
ANISOU 2948 C PRO A 260 11657 6461 7562 -705 1328 -380 C
ATOM 2949 O PRO A 260 11.820 164.250 153.749 1.00 69.48 O
ANISOU 2949 O PRO A 260 11874 6597 7928 -651 1593 -428 O
ATOM 2950 CB PRO A 260 13.484 162.296 155.957 1.00 67.71 C
ANISOU 2950 CB PRO A 260 12347 6321 7059 -1038 1214 -395 C
ATOM 2951 CG PRO A 260 13.691 160.883 156.368 1.00 71.93 C
ANISOU 2951 CG PRO A 260 12952 6894 7484 -1114 1058 -347 C
ATOM 2952 CD PRO A 260 13.510 160.085 155.111 1.00 66.13 C
ANISOU 2952 CD PRO A 260 11777 6346 7003 -939 937 -290 C
ATOM 2953 N LEU A 261 13.578 163.098 152.853 1.00 61.35 N
ANISOU 2953 N LEU A 261 10661 5834 6815 -649 1007 -312 N
ATOM 2954 CA LEU A 261 13.872 163.995 151.720 1.00 59.66 C
ANISOU 2954 CA LEU A 261 10205 5700 6763 -536 923 -288 C
ATOM 2955 C LEU A 261 12.734 164.047 150.693 1.00 62.45 C
ANISOU 2955 C LEU A 261 10228 6097 7401 -382 1057 -272 C
ATOM 2956 O LEU A 261 12.356 165.131 150.243 1.00 62.68 O
ANISOU 2956 O LEU A 261 10159 6084 7573 -311 1167 -281 O
ATOM 2957 CB LEU A 261 15.188 163.596 151.014 1.00 58.01 C
ANISOU 2957 CB LEU A 261 9876 5637 6531 -529 579 -220 C
ATOM 2958 CG LEU A 261 15.573 164.394 149.733 1.00 60.64 C
ANISOU 2958 CG LEU A 261 9959 6063 7019 -422 479 -191 C
ATOM 2959 CD1 LEU A 261 15.774 165.887 150.036 1.00 60.96 C
ANISOU 2959 CD1 LEU A 261 10141 6007 7014 -454 557 -228 C
ATOM 2960 CD2 LEU A 261 16.818 163.844 149.102 1.00 59.05 C
ANISOU 2960 CD2 LEU A 261 9644 5980 6813 -421 197 -129 C
ATOM 2961 N LEU A 262 12.216 162.877 150.316 1.00 58.17 N
ANISOU 2961 N LEU A 262 9523 5633 6947 -341 1026 -237 N
ATOM 2962 CA LEU A 262 11.144 162.729 149.338 1.00 57.58 C
ANISOU 2962 CA LEU A 262 9140 5598 7139 -222 1096 -198 C
ATOM 2963 C LEU A 262 9.870 163.390 149.824 1.00 65.16 C
ANISOU 2963 C LEU A 262 10097 6400 8263 -194 1428 -231 C
ATOM 2964 O LEU A 262 9.222 164.087 149.047 1.00 66.40 O
ANISOU 2964 O LEU A 262 10026 6540 8664 -97 1483 -196 O
ATOM 2965 CB LEU A 262 10.910 161.256 148.997 1.00 56.29 C
ANISOU 2965 CB LEU A 262 8858 5531 6999 -216 990 -157 C
ATOM 2966 CG LEU A 262 12.072 160.503 148.343 1.00 58.61 C
ANISOU 2966 CG LEU A 262 9105 5967 7196 -222 694 -118 C
ATOM 2967 CD1 LEU A 262 11.794 159.025 148.332 1.00 58.57 C
ANISOU 2967 CD1 LEU A 262 9058 6014 7184 -236 641 -94 C
ATOM 2968 CD2 LEU A 262 12.337 160.984 146.925 1.00 57.98 C
ANISOU 2968 CD2 LEU A 262 8801 5981 7246 -138 554 -75 C
ATOM 2969 N VAL A 263 9.543 163.229 151.117 1.00 62.70 N
ANISOU 2969 N VAL A 263 10049 5951 7823 -286 1655 -296 N
ATOM 2970 CA VAL A 263 8.373 163.865 151.730 1.00 63.93 C
ANISOU 2970 CA VAL A 263 10240 5916 8136 -271 2037 -342 C
ATOM 2971 C VAL A 263 8.588 165.392 151.736 1.00 67.82 C
ANISOU 2971 C VAL A 263 10800 6310 8659 -247 2137 -378 C
ATOM 2972 O VAL A 263 7.700 166.128 151.305 1.00 67.89 O
ANISOU 2972 O VAL A 263 10601 6232 8961 -145 2317 -359 O
ATOM 2973 CB VAL A 263 8.062 163.284 153.143 1.00 68.57 C
ANISOU 2973 CB VAL A 263 11154 6366 8534 -401 2276 -414 C
ATOM 2974 CG1 VAL A 263 6.915 164.035 153.820 1.00 70.79 C
ANISOU 2974 CG1 VAL A 263 11506 6413 8976 -393 2730 -477 C
ATOM 2975 CG2 VAL A 263 7.741 161.798 153.065 1.00 67.21 C
ANISOU 2975 CG2 VAL A 263 10879 6284 8375 -411 2193 -371 C
ATOM 2976 N PHE A 264 9.792 165.848 152.163 1.00 63.96 N
ANISOU 2976 N PHE A 264 10583 5831 7889 -343 1991 -415 N
ATOM 2977 CA PHE A 264 10.162 167.261 152.226 1.00 64.25 C
ANISOU 2977 CA PHE A 264 10731 5777 7903 -345 2053 -452 C
ATOM 2978 C PHE A 264 10.042 167.927 150.862 1.00 67.81 C
ANISOU 2978 C PHE A 264 10829 6316 8619 -198 1931 -383 C
ATOM 2979 O PHE A 264 9.459 168.999 150.786 1.00 70.46 O
ANISOU 2979 O PHE A 264 11116 6524 9133 -137 2135 -399 O
ATOM 2980 CB PHE A 264 11.574 167.450 152.816 1.00 65.97 C
ANISOU 2980 CB PHE A 264 11272 6016 7779 -489 1836 -476 C
ATOM 2981 CG PHE A 264 12.025 168.892 152.952 1.00 68.38 C
ANISOU 2981 CG PHE A 264 11727 6223 8031 -514 1885 -516 C
ATOM 2982 CD1 PHE A 264 11.624 169.668 154.040 1.00 73.21 C
ANISOU 2982 CD1 PHE A 264 12670 6605 8542 -604 2209 -609 C
ATOM 2983 CD2 PHE A 264 12.856 169.472 151.998 1.00 68.93 C
ANISOU 2983 CD2 PHE A 264 11628 6416 8146 -458 1625 -464 C
ATOM 2984 CE1 PHE A 264 12.040 170.997 154.166 1.00 74.91 C
ANISOU 2984 CE1 PHE A 264 13042 6719 8704 -633 2257 -648 C
ATOM 2985 CE2 PHE A 264 13.262 170.810 152.117 1.00 72.84 C
ANISOU 2985 CE2 PHE A 264 12263 6818 8596 -485 1669 -499 C
ATOM 2986 CZ PHE A 264 12.855 171.562 153.204 1.00 73.06 C
ANISOU 2986 CZ PHE A 264 12618 6620 8523 -571 1976 -590 C
ATOM 2987 N ILE A 265 10.560 167.299 149.790 1.00 60.79 N
ANISOU 2987 N ILE A 265 9711 5625 7759 -149 1615 -306 N
ATOM 2988 CA ILE A 265 10.461 167.856 148.440 1.00 58.58 C
ANISOU 2988 CA ILE A 265 9133 5426 7698 -35 1478 -234 C
ATOM 2989 C ILE A 265 8.988 168.122 148.136 1.00 62.91 C
ANISOU 2989 C ILE A 265 9444 5869 8591 65 1697 -196 C
ATOM 2990 O ILE A 265 8.636 169.279 147.919 1.00 63.08 O
ANISOU 2990 O ILE A 265 9397 5787 8785 125 1809 -188 O
ATOM 2991 CB ILE A 265 11.175 166.963 147.366 1.00 58.77 C
ANISOU 2991 CB ILE A 265 8992 5658 7681 -20 1146 -167 C
ATOM 2992 CG1 ILE A 265 12.707 167.057 147.515 1.00 58.11 C
ANISOU 2992 CG1 ILE A 265 9083 5651 7347 -98 935 -186 C
ATOM 2993 CG2 ILE A 265 10.748 167.319 145.920 1.00 56.52 C
ANISOU 2993 CG2 ILE A 265 8406 5435 7634 81 1030 -82 C
ATOM 2994 CD1 ILE A 265 13.441 165.868 147.019 1.00 63.59 C
ANISOU 2994 CD1 ILE A 265 9703 6496 7961 -114 695 -146 C
ATOM 2995 N ALA A 266 8.125 167.075 148.201 1.00 59.01 N
ANISOU 2995 N ALA A 266 8828 5379 8212 78 1766 -168 N
ATOM 2996 CA ALA A 266 6.682 167.182 147.933 1.00 60.68 C
ANISOU 2996 CA ALA A 266 8777 5481 8797 165 1958 -109 C
ATOM 2997 C ALA A 266 5.952 168.228 148.809 1.00 69.39 C
ANISOU 2997 C ALA A 266 9970 6341 10055 185 2352 -168 C
ATOM 2998 O ALA A 266 5.155 168.995 148.274 1.00 72.33 O
ANISOU 2998 O ALA A 266 10101 6614 10768 283 2441 -103 O
ATOM 2999 CB ALA A 266 6.010 165.818 148.034 1.00 61.27 C
ANISOU 2999 CB ALA A 266 8755 5595 8928 148 1970 -79 C
ATOM 3000 N GLN A 267 6.268 168.301 150.123 1.00 66.16 N
ANISOU 3000 N GLN A 267 9923 5821 9394 85 2579 -285 N
ATOM 3001 CA GLN A 267 5.699 169.271 151.068 1.00 67.85 C
ANISOU 3001 CA GLN A 267 10310 5779 9690 77 2995 -367 C
ATOM 3002 C GLN A 267 6.086 170.717 150.713 1.00 72.01 C
ANISOU 3002 C GLN A 267 10847 6244 10271 125 2985 -373 C
ATOM 3003 O GLN A 267 5.238 171.613 150.822 1.00 73.88 O
ANISOU 3003 O GLN A 267 10989 6279 10802 201 3283 -375 O
ATOM 3004 CB GLN A 267 6.164 168.966 152.501 1.00 70.07 C
ANISOU 3004 CB GLN A 267 11059 5969 9597 -84 3174 -491 C
ATOM 3005 CG GLN A 267 5.423 167.829 153.195 1.00 84.77 C
ANISOU 3005 CG GLN A 267 12967 7780 11462 -136 3368 -510 C
ATOM 3006 CD GLN A 267 5.864 167.617 154.635 1.00103.18 C
ANISOU 3006 CD GLN A 267 15810 9992 13402 -319 3546 -628 C
ATOM 3007 OE1 GLN A 267 7.056 167.687 154.984 1.00 95.90 O
ANISOU 3007 OE1 GLN A 267 15186 9137 12115 -437 3318 -660 O
ATOM 3008 NE2 GLN A 267 4.907 167.298 155.499 1.00 96.23 N
ANISOU 3008 NE2 GLN A 267 15045 8923 12594 -362 3947 -684 N
ATOM 3009 N THR A 268 7.366 170.947 150.315 1.00 66.15 N
ANISOU 3009 N THR A 268 10212 5658 9262 80 2658 -372 N
ATOM 3010 CA THR A 268 7.882 172.282 149.949 1.00 66.13 C
ANISOU 3010 CA THR A 268 10238 5618 9271 109 2607 -376 C
ATOM 3011 C THR A 268 7.181 172.802 148.694 1.00 71.33 C
ANISOU 3011 C THR A 268 10489 6286 10327 259 2528 -258 C
ATOM 3012 O THR A 268 6.732 173.950 148.656 1.00 73.44 O
ANISOU 3012 O THR A 268 10706 6389 10810 324 2712 -256 O
ATOM 3013 CB THR A 268 9.414 172.253 149.715 1.00 69.19 C
ANISOU 3013 CB THR A 268 10786 6184 9319 24 2252 -382 C
ATOM 3014 OG1 THR A 268 10.051 171.568 150.784 1.00 75.02 O
ANISOU 3014 OG1 THR A 268 11862 6926 9717 -122 2247 -454 O
ATOM 3015 CG2 THR A 268 10.020 173.636 149.606 1.00 64.89 C
ANISOU 3015 CG2 THR A 268 10347 5575 8732 21 2236 -406 C
ATOM 3016 N VAL A 269 7.102 171.943 147.673 1.00 65.56 N
ANISOU 3016 N VAL A 269 9490 5736 9684 299 2244 -156 N
ATOM 3017 CA VAL A 269 6.534 172.209 146.365 1.00 64.75 C
ANISOU 3017 CA VAL A 269 9027 5672 9904 402 2072 -22 C
ATOM 3018 C VAL A 269 5.014 172.457 146.429 1.00 71.44 C
ANISOU 3018 C VAL A 269 9618 6318 11206 497 2341 43 C
ATOM 3019 O VAL A 269 4.507 173.208 145.597 1.00 71.67 O
ANISOU 3019 O VAL A 269 9400 6283 11547 582 2277 147 O
ATOM 3020 CB VAL A 269 6.976 171.043 145.444 1.00 66.98 C
ANISOU 3020 CB VAL A 269 9192 6189 10069 375 1715 47 C
ATOM 3021 CG1 VAL A 269 5.827 170.340 144.711 1.00 67.15 C
ANISOU 3021 CG1 VAL A 269 8887 6215 10411 431 1650 171 C
ATOM 3022 CG2 VAL A 269 8.086 171.485 144.504 1.00 65.37 C
ANISOU 3022 CG2 VAL A 269 9011 6130 9697 359 1410 72 C
ATOM 3023 N LEU A 270 4.308 171.879 147.440 1.00 69.82 N
ANISOU 3023 N LEU A 270 9479 5996 11053 476 2650 -15 N
ATOM 3024 CA LEU A 270 2.849 171.994 147.623 1.00 72.05 C
ANISOU 3024 CA LEU A 270 9509 6068 11798 560 2954 44 C
ATOM 3025 C LEU A 270 2.366 173.031 148.671 1.00 81.98 C
ANISOU 3025 C LEU A 270 10918 7033 13197 585 3440 -51 C
ATOM 3026 O LEU A 270 1.151 173.204 148.803 1.00 84.21 O
ANISOU 3026 O LEU A 270 10960 7112 13922 666 3725 4 O
ATOM 3027 CB LEU A 270 2.235 170.621 147.948 1.00 71.46 C
ANISOU 3027 CB LEU A 270 9369 6032 11752 523 3011 56 C
ATOM 3028 CG LEU A 270 2.192 169.586 146.820 1.00 73.37 C
ANISOU 3028 CG LEU A 270 9360 6486 12030 523 2609 182 C
ATOM 3029 CD1 LEU A 270 1.821 168.221 147.353 1.00 71.71 C
ANISOU 3029 CD1 LEU A 270 9182 6319 11747 464 2682 159 C
ATOM 3030 CD2 LEU A 270 1.243 170.006 145.701 1.00 77.40 C
ANISOU 3030 CD2 LEU A 270 9453 6934 13022 619 2474 362 C
ATOM 3031 N ARG A 271 3.288 173.710 149.395 1.00 80.91 N
ANISOU 3031 N ARG A 271 11172 6858 12710 509 3540 -187 N
ATOM 3032 CA ARG A 271 2.977 174.707 150.442 1.00 85.12 C
ANISOU 3032 CA ARG A 271 11943 7104 13293 501 4009 -301 C
ATOM 3033 C ARG A 271 1.975 175.807 150.007 1.00 97.51 C
ANISOU 3033 C ARG A 271 13199 8444 15405 651 4226 -218 C
ATOM 3034 O ARG A 271 2.172 176.413 148.942 1.00 96.66 O
ANISOU 3034 O ARG A 271 12870 8413 15442 725 3935 -111 O
ATOM 3035 CB ARG A 271 4.265 175.328 151.006 1.00 81.40 C
ANISOU 3035 CB ARG A 271 11921 6660 12347 383 3954 -426 C
ATOM 3036 CG ARG A 271 4.777 174.580 152.227 1.00 85.54 C
ANISOU 3036 CG ARG A 271 12884 7184 12434 213 4071 -557 C
ATOM 3037 CD ARG A 271 6.231 174.852 152.547 1.00 93.79 C
ANISOU 3037 CD ARG A 271 14313 8335 12990 73 3833 -631 C
ATOM 3038 NE ARG A 271 6.464 176.230 152.988 1.00106.28 N
ANISOU 3038 NE ARG A 271 16137 9719 14526 49 4042 -709 N
ATOM 3039 CZ ARG A 271 7.557 176.639 153.629 1.00116.08 C
ANISOU 3039 CZ ARG A 271 17802 10952 15350 -106 3961 -797 C
ATOM 3040 NH1 ARG A 271 8.525 175.777 153.926 1.00 98.08 N
ANISOU 3040 NH1 ARG A 271 15736 8845 12685 -246 3670 -807 N
ATOM 3041 NH2 ARG A 271 7.687 177.915 153.986 1.00 95.21 N
ANISOU 3041 NH2 ARG A 271 15373 8116 12689 -127 4162 -865 N
ATOM 3042 N ASN A 272 0.886 176.024 150.838 1.00100.57 N
ANISOU 3042 N ASN A 272 13568 8536 16110 691 4748 -261 N
ATOM 3043 CA ASN A 272 -0.225 176.989 150.637 1.00104.38 C
ANISOU 3043 CA ASN A 272 13738 8733 17188 839 5057 -184 C
ATOM 3044 C ASN A 272 0.337 178.334 150.274 1.00110.91 C
ANISOU 3044 C ASN A 272 14634 9505 18003 880 4982 -189 C
ATOM 3045 O ASN A 272 0.326 178.623 149.078 1.00110.87 O
ANISOU 3045 O ASN A 272 14296 9606 18225 966 4619 -32 O
ATOM 3046 CB ASN A 272 -1.203 177.037 151.819 1.00108.68 C
ANISOU 3046 CB ASN A 272 14385 8949 17960 841 5700 -282 C
ATOM 3047 N PRO A 273 0.975 179.120 151.185 1.00108.75 N
ANISOU 3047 N PRO A 273 14815 9099 17405 796 5237 -358 N
ATOM 3048 CA PRO A 273 1.705 180.308 150.702 1.00106.99 C
ANISOU 3048 CA PRO A 273 14663 8885 17104 818 5059 -352 C
ATOM 3049 C PRO A 273 3.039 179.748 150.151 1.00104.50 C
ANISOU 3049 C PRO A 273 14484 8933 16289 715 4509 -345 C
ATOM 3050 O PRO A 273 3.630 178.874 150.803 1.00102.13 O
ANISOU 3050 O PRO A 273 14477 8759 15571 581 4463 -438 O
ATOM 3051 CB PRO A 273 1.893 181.169 151.964 1.00111.09 C
ANISOU 3051 CB PRO A 273 15656 9127 17425 738 5540 -542 C
ATOM 3052 CG PRO A 273 1.306 180.364 153.117 1.00118.02 C
ANISOU 3052 CG PRO A 273 16754 9870 18221 653 5954 -654 C
ATOM 3053 CD PRO A 273 1.166 178.945 152.642 1.00111.76 C
ANISOU 3053 CD PRO A 273 15704 9335 17423 651 5642 -556 C
ATOM 3054 N PRO A 274 3.486 180.105 148.923 1.00 97.86 N
ANISOU 3054 N PRO A 274 13415 8265 15504 771 4082 -222 N
ATOM 3055 CA PRO A 274 4.711 179.479 148.382 1.00 93.51 C
ANISOU 3055 CA PRO A 274 12968 8041 14520 676 3605 -213 C
ATOM 3056 C PRO A 274 5.949 179.562 149.277 1.00 95.21 C
ANISOU 3056 C PRO A 274 13678 8308 14190 516 3605 -370 C
ATOM 3057 O PRO A 274 6.219 180.596 149.886 1.00 96.34 O
ANISOU 3057 O PRO A 274 14092 8273 14242 479 3828 -464 O
ATOM 3058 CB PRO A 274 4.912 180.187 147.040 1.00 93.91 C
ANISOU 3058 CB PRO A 274 12753 8180 14750 757 3263 -76 C
ATOM 3059 CG PRO A 274 3.538 180.614 146.650 1.00101.20 C
ANISOU 3059 CG PRO A 274 13294 8889 16268 903 3441 50 C
ATOM 3060 CD PRO A 274 2.904 181.048 147.949 1.00 99.99 C
ANISOU 3060 CD PRO A 274 13324 8431 16238 914 4008 -77 C
ATOM 3061 N ALA A 275 6.663 178.424 149.385 1.00 88.73 N
ANISOU 3061 N ALA A 275 12975 7713 13024 413 3357 -390 N
ATOM 3062 CA ALA A 275 7.906 178.236 150.142 1.00 86.67 C
ANISOU 3062 CA ALA A 275 13139 7536 12256 245 3253 -500 C
ATOM 3063 C ALA A 275 9.025 179.128 149.582 1.00 87.41 C
ANISOU 3063 C ALA A 275 13306 7722 12182 217 2977 -487 C
ATOM 3064 O ALA A 275 9.897 179.582 150.325 1.00 85.93 O
ANISOU 3064 O ALA A 275 13490 7487 11670 87 2992 -580 O
ATOM 3065 CB ALA A 275 8.331 176.775 150.054 1.00 85.16 C
ANISOU 3065 CB ALA A 275 12929 7578 11852 180 2989 -475 C
ATOM 3066 N MET A 276 8.994 179.337 148.255 1.00 83.00 N
ANISOU 3066 N MET A 276 12403 7289 11843 324 2711 -363 N
ATOM 3067 CA MET A 276 9.938 180.116 147.473 1.00 81.17 C
ANISOU 3067 CA MET A 276 12165 7160 11516 316 2433 -325 C
ATOM 3068 C MET A 276 9.282 181.387 146.943 1.00 84.63 C
ANISOU 3068 C MET A 276 12432 7427 12297 433 2556 -270 C
ATOM 3069 O MET A 276 8.167 181.351 146.416 1.00 85.25 O
ANISOU 3069 O MET A 276 12194 7429 12767 555 2633 -175 O
ATOM 3070 CB MET A 276 10.468 179.268 146.305 1.00 81.12 C
ANISOU 3070 CB MET A 276 11931 7430 11463 326 2023 -223 C
ATOM 3071 CG MET A 276 11.766 179.788 145.736 1.00 83.27 C
ANISOU 3071 CG MET A 276 12285 7833 11521 268 1740 -212 C
ATOM 3072 SD MET A 276 12.407 178.840 144.326 1.00 84.92 S
ANISOU 3072 SD MET A 276 12259 8328 11678 272 1323 -106 S
ATOM 3073 CE MET A 276 13.429 177.641 145.180 1.00 79.91 C
ANISOU 3073 CE MET A 276 11853 7826 10684 142 1232 -183 C
ATOM 3074 N SER A 277 9.999 182.507 147.069 1.00 79.99 N
ANISOU 3074 N SER A 277 12048 6773 11572 388 2553 -317 N
ATOM 3075 CA SER A 277 9.590 183.835 146.614 1.00 79.99 C
ANISOU 3075 CA SER A 277 11939 6604 11848 482 2650 -273 C
ATOM 3076 C SER A 277 9.575 183.867 145.066 1.00 84.39 C
ANISOU 3076 C SER A 277 12142 7317 12603 566 2295 -112 C
ATOM 3077 O SER A 277 10.220 183.011 144.455 1.00 81.28 O
ANISOU 3077 O SER A 277 11691 7167 12023 517 1981 -71 O
ATOM 3078 CB SER A 277 10.560 184.883 147.159 1.00 79.03 C
ANISOU 3078 CB SER A 277 12172 6405 11449 380 2688 -372 C
ATOM 3079 OG SER A 277 11.793 184.897 146.457 1.00 75.49 O
ANISOU 3079 OG SER A 277 11743 6180 10759 310 2301 -334 O
ATOM 3080 N PRO A 278 8.886 184.841 144.407 1.00 84.11 N
ANISOU 3080 N PRO A 278 11890 7135 12934 679 2333 -16 N
ATOM 3081 CA PRO A 278 8.913 184.890 142.926 1.00 83.35 C
ANISOU 3081 CA PRO A 278 11511 7176 12984 725 1967 146 C
ATOM 3082 C PRO A 278 10.326 184.934 142.302 1.00 86.28 C
ANISOU 3082 C PRO A 278 12020 7771 12992 623 1633 138 C
ATOM 3083 O PRO A 278 10.539 184.366 141.231 1.00 84.61 O
ANISOU 3083 O PRO A 278 11648 7740 12759 612 1327 236 O
ATOM 3084 CB PRO A 278 8.134 186.172 142.609 1.00 87.28 C
ANISOU 3084 CB PRO A 278 11854 7429 13880 835 2098 226 C
ATOM 3085 CG PRO A 278 7.276 186.408 143.795 1.00 93.37 C
ANISOU 3085 CG PRO A 278 12688 7935 14853 889 2564 139 C
ATOM 3086 CD PRO A 278 8.069 185.945 144.962 1.00 88.04 C
ANISOU 3086 CD PRO A 278 12400 7317 13735 761 2709 -42 C
ATOM 3087 N ALA A 279 11.287 185.609 142.978 1.00 83.35 N
ANISOU 3087 N ALA A 279 11955 7371 12342 539 1704 23 N
ATOM 3088 CA ALA A 279 12.688 185.736 142.560 1.00 81.02 C
ANISOU 3088 CA ALA A 279 11803 7255 11724 434 1435 6 C
ATOM 3089 C ALA A 279 13.430 184.404 142.639 1.00 83.08 C
ANISOU 3089 C ALA A 279 12112 7744 11712 348 1260 -23 C
ATOM 3090 O ALA A 279 14.441 184.224 141.965 1.00 83.03 O
ANISOU 3090 O ALA A 279 12108 7912 11529 286 1002 4 O
ATOM 3091 CB ALA A 279 13.395 186.774 143.420 1.00 82.60 C
ANISOU 3091 CB ALA A 279 12321 7331 11732 356 1578 -105 C
ATOM 3092 N GLY A 280 12.919 183.484 143.452 1.00 77.82 N
ANISOU 3092 N GLY A 280 11480 7058 11029 345 1419 -76 N
ATOM 3093 CA GLY A 280 13.505 182.166 143.631 1.00 74.46 C
ANISOU 3093 CA GLY A 280 11097 6820 10375 271 1279 -101 C
ATOM 3094 C GLY A 280 14.190 181.981 144.970 1.00 76.04 C
ANISOU 3094 C GLY A 280 11628 6984 10280 149 1386 -222 C
ATOM 3095 O GLY A 280 15.019 181.085 145.119 1.00 75.03 O
ANISOU 3095 O GLY A 280 11571 7008 9929 65 1216 -235 O
ATOM 3096 N GLN A 281 13.822 182.782 145.970 1.00 71.84 N
ANISOU 3096 N GLN A 281 11314 6233 9750 130 1673 -305 N
ATOM 3097 CA GLN A 281 14.442 182.689 147.281 1.00 70.54 C
ANISOU 3097 CA GLN A 281 11523 6002 9275 -18 1767 -416 C
ATOM 3098 C GLN A 281 13.627 181.894 148.295 1.00 72.76 C
ANISOU 3098 C GLN A 281 11915 6184 9545 -35 2027 -480 C
ATOM 3099 O GLN A 281 12.435 182.155 148.507 1.00 73.54 O
ANISOU 3099 O GLN A 281 11940 6107 9896 58 2335 -495 O
ATOM 3100 CB GLN A 281 14.786 184.088 147.813 1.00 73.19 C
ANISOU 3100 CB GLN A 281 12132 6153 9526 -81 1902 -483 C
ATOM 3101 CG GLN A 281 15.562 184.072 149.128 1.00 79.05 C
ANISOU 3101 CG GLN A 281 13311 6819 9905 -276 1939 -584 C
ATOM 3102 CD GLN A 281 16.171 185.393 149.465 1.00 93.11 C
ANISOU 3102 CD GLN A 281 15359 8460 11558 -367 1971 -633 C
ATOM 3103 OE1 GLN A 281 15.522 186.445 149.410 1.00 92.10 O
ANISOU 3103 OE1 GLN A 281 15236 8146 11613 -290 2209 -658 O
ATOM 3104 NE2 GLN A 281 17.429 185.355 149.862 1.00 82.28 N
ANISOU 3104 NE2 GLN A 281 14218 7160 9885 -539 1729 -641 N
ATOM 3105 N LEU A 282 14.307 180.939 148.953 1.00 66.75 N
ANISOU 3105 N LEU A 282 11339 5522 8501 -162 1905 -514 N
ATOM 3106 CA LEU A 282 13.753 180.121 150.035 1.00 66.19 C
ANISOU 3106 CA LEU A 282 11451 5363 8334 -223 2118 -581 C
ATOM 3107 C LEU A 282 14.209 180.751 151.345 1.00 72.87 C
ANISOU 3107 C LEU A 282 12781 6018 8889 -398 2277 -691 C
ATOM 3108 O LEU A 282 15.170 181.532 151.346 1.00 71.78 O
ANISOU 3108 O LEU A 282 12804 5880 8590 -485 2119 -697 O
ATOM 3109 CB LEU A 282 14.299 178.691 149.977 1.00 63.52 C
ANISOU 3109 CB LEU A 282 11059 5234 7841 -278 1856 -542 C
ATOM 3110 CG LEU A 282 13.925 177.851 148.784 1.00 64.46 C
ANISOU 3110 CG LEU A 282 10770 5541 8182 -144 1692 -444 C
ATOM 3111 CD1 LEU A 282 14.923 176.745 148.594 1.00 62.33 C
ANISOU 3111 CD1 LEU A 282 10481 5476 7725 -214 1379 -405 C
ATOM 3112 CD2 LEU A 282 12.503 177.300 148.909 1.00 65.16 C
ANISOU 3112 CD2 LEU A 282 10704 5546 8509 -49 1950 -442 C
ATOM 3113 N SER A 283 13.549 180.400 152.468 1.00 72.12 N
ANISOU 3113 N SER A 283 12942 5752 8709 -467 2585 -777 N
ATOM 3114 CA SER A 283 13.970 180.892 153.780 1.00 73.48 C
ANISOU 3114 CA SER A 283 13644 5724 8551 -671 2735 -885 C
ATOM 3115 C SER A 283 15.216 180.083 154.171 1.00 78.22 C
ANISOU 3115 C SER A 283 14439 6478 8802 -854 2357 -854 C
ATOM 3116 O SER A 283 15.400 178.962 153.652 1.00 76.01 O
ANISOU 3116 O SER A 283 13900 6411 8569 -803 2118 -776 O
ATOM 3117 CB SER A 283 12.865 180.684 154.808 1.00 77.87 C
ANISOU 3117 CB SER A 283 14423 6041 9123 -699 3199 -985 C
ATOM 3118 OG SER A 283 12.701 179.323 155.174 1.00 86.18 O
ANISOU 3118 OG SER A 283 15480 7185 10079 -745 3152 -973 O
ATOM 3119 N ARG A 284 16.070 180.638 155.066 1.00 76.56 N
ANISOU 3119 N ARG A 284 14680 6148 8262 -1070 2291 -903 N
ATOM 3120 CA ARG A 284 17.271 179.938 155.537 1.00 76.29 C
ANISOU 3120 CA ARG A 284 14849 6219 7919 -1267 1914 -855 C
ATOM 3121 C ARG A 284 16.924 178.605 156.209 1.00 79.28 C
ANISOU 3121 C ARG A 284 15329 6612 8180 -1334 1944 -860 C
ATOM 3122 O ARG A 284 17.665 177.640 156.034 1.00 76.33 O
ANISOU 3122 O ARG A 284 14841 6421 7741 -1374 1596 -773 O
ATOM 3123 CB ARG A 284 18.103 180.801 156.494 1.00 80.87 C
ANISOU 3123 CB ARG A 284 15938 6622 8168 -1515 1854 -901 C
ATOM 3124 CG ARG A 284 19.538 180.289 156.665 1.00 99.28 C
ANISOU 3124 CG ARG A 284 18358 9086 10279 -1694 1359 -801 C
ATOM 3125 CD ARG A 284 20.528 180.911 155.676 1.00118.36 C
ANISOU 3125 CD ARG A 284 20501 11652 12819 -1639 1045 -714 C
ATOM 3126 NE ARG A 284 21.875 180.343 155.806 1.00131.88 N
ANISOU 3126 NE ARG A 284 22237 13480 14391 -1796 585 -602 N
ATOM 3127 CZ ARG A 284 22.772 180.707 156.723 1.00147.71 C
ANISOU 3127 CZ ARG A 284 24653 15358 16111 -2062 379 -583 C
ATOM 3128 NH1 ARG A 284 22.479 181.648 157.615 1.00135.86 N
ANISOU 3128 NH1 ARG A 284 23623 13608 14389 -2215 607 -685 N
ATOM 3129 NH2 ARG A 284 23.962 180.122 156.764 1.00132.01 N
ANISOU 3129 NH2 ARG A 284 22614 13473 14070 -2186 -57 -455 N
ATOM 3130 N THR A 285 15.793 178.545 156.947 1.00 78.38 N
ANISOU 3130 N THR A 285 15414 6299 8065 -1340 2373 -959 N
ATOM 3131 CA THR A 285 15.384 177.307 157.612 1.00 79.59 C
ANISOU 3131 CA THR A 285 15681 6450 8109 -1407 2440 -970 C
ATOM 3132 C THR A 285 15.010 176.242 156.563 1.00 80.83 C
ANISOU 3132 C THR A 285 15298 6853 8559 -1197 2306 -880 C
ATOM 3133 O THR A 285 15.348 175.078 156.765 1.00 80.08 O
ANISOU 3133 O THR A 285 15204 6874 8349 -1261 2095 -831 O
ATOM 3134 CB THR A 285 14.316 177.504 158.725 1.00 91.78 C
ANISOU 3134 CB THR A 285 17612 7697 9563 -1490 2962 -1103 C
ATOM 3135 OG1 THR A 285 13.001 177.528 158.167 1.00 99.24 O
ANISOU 3135 OG1 THR A 285 18195 8609 10904 -1257 3324 -1124 O
ATOM 3136 CG2 THR A 285 14.573 178.727 159.619 1.00 85.51 C
ANISOU 3136 CG2 THR A 285 17345 6631 8515 -1677 3156 -1205 C
ATOM 3137 N THR A 286 14.386 176.642 155.429 1.00 75.02 N
ANISOU 3137 N THR A 286 14120 6193 8192 -964 2391 -849 N
ATOM 3138 CA THR A 286 14.034 175.693 154.363 1.00 72.07 C
ANISOU 3138 CA THR A 286 13261 6040 8080 -786 2243 -759 C
ATOM 3139 C THR A 286 15.312 175.113 153.757 1.00 73.11 C
ANISOU 3139 C THR A 286 13257 6411 8113 -818 1767 -663 C
ATOM 3140 O THR A 286 15.402 173.894 153.601 1.00 72.43 O
ANISOU 3140 O THR A 286 13034 6463 8022 -807 1606 -613 O
ATOM 3141 CB THR A 286 13.117 176.340 153.309 1.00 75.97 C
ANISOU 3141 CB THR A 286 13358 6533 8973 -564 2405 -731 C
ATOM 3142 OG1 THR A 286 11.898 176.725 153.930 1.00 79.10 O
ANISOU 3142 OG1 THR A 286 13849 6691 9515 -528 2867 -809 O
ATOM 3143 CG2 THR A 286 12.810 175.412 152.136 1.00 67.88 C
ANISOU 3143 CG2 THR A 286 11871 5729 8192 -409 2211 -629 C
ATOM 3144 N GLU A 287 16.302 175.992 153.459 1.00 67.62 N
ANISOU 3144 N GLU A 287 12605 5741 7347 -864 1561 -640 N
ATOM 3145 CA GLU A 287 17.595 175.642 152.875 1.00 64.77 C
ANISOU 3145 CA GLU A 287 12108 5572 6931 -896 1142 -548 C
ATOM 3146 C GLU A 287 18.386 174.732 153.800 1.00 67.77 C
ANISOU 3146 C GLU A 287 12746 5958 7045 -1084 928 -523 C
ATOM 3147 O GLU A 287 18.918 173.725 153.344 1.00 64.73 O
ANISOU 3147 O GLU A 287 12150 5741 6705 -1057 674 -443 O
ATOM 3148 CB GLU A 287 18.409 176.896 152.557 1.00 66.29 C
ANISOU 3148 CB GLU A 287 12344 5744 7101 -930 1022 -537 C
ATOM 3149 CG GLU A 287 17.835 177.787 151.462 1.00 79.78 C
ANISOU 3149 CG GLU A 287 13757 7471 9084 -744 1147 -532 C
ATOM 3150 CD GLU A 287 18.493 179.153 151.322 1.00101.94 C
ANISOU 3150 CD GLU A 287 16667 10211 11854 -788 1094 -538 C
ATOM 3151 OE1 GLU A 287 18.809 179.775 152.367 1.00 97.25 O
ANISOU 3151 OE1 GLU A 287 16468 9447 11037 -953 1162 -599 O
ATOM 3152 OE2 GLU A 287 18.656 179.618 150.167 1.00 84.31 O
ANISOU 3152 OE2 GLU A 287 14143 8084 9806 -670 991 -484 O
ATOM 3153 N LYS A 288 18.432 175.070 155.103 1.00 67.37 N
ANISOU 3153 N LYS A 288 13166 5707 6723 -1281 1039 -588 N
ATOM 3154 CA LYS A 288 19.128 174.303 156.133 1.00 68.10 C
ANISOU 3154 CA LYS A 288 13583 5760 6533 -1499 831 -557 C
ATOM 3155 C LYS A 288 18.537 172.903 156.325 1.00 73.30 C
ANISOU 3155 C LYS A 288 14160 6478 7211 -1465 876 -545 C
ATOM 3156 O LYS A 288 19.297 171.957 156.541 1.00 73.95 O
ANISOU 3156 O LYS A 288 14257 6642 7199 -1556 571 -462 O
ATOM 3157 CB LYS A 288 19.200 175.084 157.448 1.00 72.63 C
ANISOU 3157 CB LYS A 288 14731 6077 6789 -1737 966 -636 C
ATOM 3158 CG LYS A 288 20.381 176.053 157.496 1.00 83.21 C
ANISOU 3158 CG LYS A 288 16224 7385 8008 -1874 696 -593 C
ATOM 3159 CD LYS A 288 20.455 176.859 158.809 1.00100.40 C
ANISOU 3159 CD LYS A 288 19023 9286 9838 -2137 825 -674 C
ATOM 3160 CE LYS A 288 21.198 176.155 159.933 1.00114.75 C
ANISOU 3160 CE LYS A 288 21247 11026 11327 -2426 532 -612 C
ATOM 3161 NZ LYS A 288 21.226 176.964 161.186 1.00125.82 N
ANISOU 3161 NZ LYS A 288 23307 12141 12359 -2709 661 -694 N
ATOM 3162 N GLU A 289 17.199 172.760 156.194 1.00 69.21 N
ANISOU 3162 N GLU A 289 13528 5919 6850 -1328 1243 -615 N
ATOM 3163 CA GLU A 289 16.500 171.475 156.298 1.00 68.02 C
ANISOU 3163 CA GLU A 289 13274 5822 6749 -1282 1320 -607 C
ATOM 3164 C GLU A 289 16.793 170.642 155.052 1.00 67.68 C
ANISOU 3164 C GLU A 289 12747 6030 6938 -1115 1062 -509 C
ATOM 3165 O GLU A 289 17.101 169.456 155.173 1.00 67.62 O
ANISOU 3165 O GLU A 289 12702 6110 6879 -1151 878 -454 O
ATOM 3166 CB GLU A 289 14.983 171.684 156.412 1.00 70.71 C
ANISOU 3166 CB GLU A 289 13583 6034 7250 -1177 1792 -697 C
ATOM 3167 CG GLU A 289 14.477 172.137 157.770 1.00 82.83 C
ANISOU 3167 CG GLU A 289 15626 7291 8557 -1348 2141 -809 C
ATOM 3168 CD GLU A 289 13.038 172.626 157.780 1.00115.18 C
ANISOU 3168 CD GLU A 289 19642 11229 12893 -1220 2647 -896 C
ATOM 3169 OE1 GLU A 289 12.518 172.989 156.699 1.00115.01 O
ANISOU 3169 OE1 GLU A 289 19185 11291 13221 -1004 2698 -862 O
ATOM 3170 OE2 GLU A 289 12.443 172.687 158.880 1.00118.56 O
ANISOU 3170 OE2 GLU A 289 20454 11427 13166 -1347 2999 -992 O
ATOM 3171 N LEU A 290 16.699 171.257 153.850 1.00 60.63 N
ANISOU 3171 N LEU A 290 11505 5238 6294 -941 1053 -487 N
ATOM 3172 CA LEU A 290 16.995 170.570 152.588 1.00 57.29 C
ANISOU 3172 CA LEU A 290 10664 5033 6071 -798 830 -403 C
ATOM 3173 C LEU A 290 18.409 169.990 152.606 1.00 61.27 C
ANISOU 3173 C LEU A 290 11184 5637 6459 -895 454 -323 C
ATOM 3174 O LEU A 290 18.608 168.864 152.156 1.00 63.07 O
ANISOU 3174 O LEU A 290 11211 5994 6760 -845 304 -265 O
ATOM 3175 CB LEU A 290 16.786 171.480 151.352 1.00 55.66 C
ANISOU 3175 CB LEU A 290 10156 4890 6101 -639 859 -388 C
ATOM 3176 CG LEU A 290 16.964 170.818 149.959 1.00 56.82 C
ANISOU 3176 CG LEU A 290 9908 5239 6442 -503 670 -310 C
ATOM 3177 CD1 LEU A 290 15.967 169.654 149.730 1.00 54.43 C
ANISOU 3177 CD1 LEU A 290 9435 4988 6259 -422 766 -300 C
ATOM 3178 CD2 LEU A 290 16.812 171.845 148.859 1.00 58.05 C
ANISOU 3178 CD2 LEU A 290 9848 5425 6782 -388 686 -292 C
ATOM 3179 N LEU A 291 19.362 170.716 153.191 1.00 56.52 N
ANISOU 3179 N LEU A 291 10832 4956 5686 -1044 309 -313 N
ATOM 3180 CA LEU A 291 20.725 170.243 153.320 1.00 55.67 C
ANISOU 3180 CA LEU A 291 10742 4907 5504 -1154 -56 -219 C
ATOM 3181 C LEU A 291 20.774 169.025 154.253 1.00 60.51 C
ANISOU 3181 C LEU A 291 11542 5484 5965 -1275 -150 -189 C
ATOM 3182 O LEU A 291 21.511 168.084 153.975 1.00 58.75 O
ANISOU 3182 O LEU A 291 11150 5362 5811 -1270 -406 -98 O
ATOM 3183 CB LEU A 291 21.644 171.365 153.857 1.00 56.77 C
ANISOU 3183 CB LEU A 291 11141 4939 5492 -1314 -191 -208 C
ATOM 3184 CG LEU A 291 23.147 171.012 153.928 1.00 61.68 C
ANISOU 3184 CG LEU A 291 11727 5607 6100 -1428 -599 -84 C
ATOM 3185 CD1 LEU A 291 23.676 170.478 152.558 1.00 60.26 C
ANISOU 3185 CD1 LEU A 291 11073 5620 6203 -1253 -736 -12 C
ATOM 3186 CD2 LEU A 291 23.968 172.166 154.404 1.00 62.60 C
ANISOU 3186 CD2 LEU A 291 12084 5612 6087 -1589 -735 -67 C
ATOM 3187 N ILE A 292 19.998 169.055 155.357 1.00 59.15 N
ANISOU 3187 N ILE A 292 11729 5153 5594 -1388 72 -265 N
ATOM 3188 CA ILE A 292 19.986 167.987 156.350 1.00 60.55 C
ANISOU 3188 CA ILE A 292 12153 5267 5587 -1531 2 -242 C
ATOM 3189 C ILE A 292 19.472 166.711 155.735 1.00 63.34 C
ANISOU 3189 C ILE A 292 12192 5759 6114 -1382 22 -217 C
ATOM 3190 O ILE A 292 20.161 165.691 155.811 1.00 62.94 O
ANISOU 3190 O ILE A 292 12083 5772 6061 -1426 -248 -126 O
ATOM 3191 CB ILE A 292 19.261 168.398 157.661 1.00 66.28 C
ANISOU 3191 CB ILE A 292 13378 5766 6040 -1703 279 -342 C
ATOM 3192 CG1 ILE A 292 20.157 169.368 158.468 1.00 68.77 C
ANISOU 3192 CG1 ILE A 292 14093 5930 6105 -1932 117 -330 C
ATOM 3193 CG2 ILE A 292 18.869 167.168 158.501 1.00 66.98 C
ANISOU 3193 CG2 ILE A 292 13670 5802 5977 -1808 302 -335 C
ATOM 3194 CD1 ILE A 292 19.423 170.251 159.516 1.00 82.20 C
ANISOU 3194 CD1 ILE A 292 16292 7383 7557 -2081 471 -459 C
ATOM 3195 N TYR A 293 18.317 166.790 155.054 1.00 59.17 N
ANISOU 3195 N TYR A 293 11437 5276 5767 -1204 316 -283 N
ATOM 3196 CA TYR A 293 17.706 165.653 154.375 1.00 56.98 C
ANISOU 3196 CA TYR A 293 10857 5126 5666 -1063 349 -261 C
ATOM 3197 C TYR A 293 18.561 165.131 153.243 1.00 58.37 C
ANISOU 3197 C TYR A 293 10682 5482 6015 -959 69 -172 C
ATOM 3198 O TYR A 293 18.657 163.921 153.074 1.00 57.60 O
ANISOU 3198 O TYR A 293 10466 5459 5959 -937 -46 -124 O
ATOM 3199 CB TYR A 293 16.276 165.968 153.920 1.00 58.07 C
ANISOU 3199 CB TYR A 293 10832 5250 5984 -915 701 -333 C
ATOM 3200 CG TYR A 293 15.345 166.281 155.070 1.00 63.24 C
ANISOU 3200 CG TYR A 293 11819 5705 6504 -1011 1037 -424 C
ATOM 3201 CD1 TYR A 293 15.229 165.415 156.159 1.00 67.57 C
ANISOU 3201 CD1 TYR A 293 12664 6166 6843 -1160 1066 -435 C
ATOM 3202 CD2 TYR A 293 14.568 167.436 155.069 1.00 64.87 C
ANISOU 3202 CD2 TYR A 293 12053 5792 6801 -958 1346 -498 C
ATOM 3203 CE1 TYR A 293 14.396 165.712 157.236 1.00 71.41 C
ANISOU 3203 CE1 TYR A 293 13496 6447 7188 -1267 1412 -528 C
ATOM 3204 CE2 TYR A 293 13.714 167.732 156.132 1.00 68.18 C
ANISOU 3204 CE2 TYR A 293 12789 6000 7116 -1047 1707 -590 C
ATOM 3205 CZ TYR A 293 13.633 166.868 157.213 1.00 77.27 C
ANISOU 3205 CZ TYR A 293 14258 7064 8036 -1207 1750 -610 C
ATOM 3206 OH TYR A 293 12.793 167.143 158.259 1.00 82.24 O
ANISOU 3206 OH TYR A 293 15230 7467 8552 -1308 2142 -708 O
ATOM 3207 N LEU A 294 19.226 166.021 152.506 1.00 55.69 N
ANISOU 3207 N LEU A 294 10197 5193 5768 -908 -32 -152 N
ATOM 3208 CA LEU A 294 20.112 165.586 151.429 1.00 54.61 C
ANISOU 3208 CA LEU A 294 9751 5203 5797 -822 -263 -74 C
ATOM 3209 C LEU A 294 21.318 164.792 151.998 1.00 59.60 C
ANISOU 3209 C LEU A 294 10463 5823 6358 -945 -567 19 C
ATOM 3210 O LEU A 294 21.688 163.740 151.459 1.00 58.22 O
ANISOU 3210 O LEU A 294 10074 5739 6310 -883 -695 78 O
ATOM 3211 CB LEU A 294 20.545 166.758 150.560 1.00 53.83 C
ANISOU 3211 CB LEU A 294 9506 5142 5803 -756 -280 -74 C
ATOM 3212 CG LEU A 294 21.618 166.422 149.554 1.00 57.19 C
ANISOU 3212 CG LEU A 294 9663 5685 6381 -698 -495 3 C
ATOM 3213 CD1 LEU A 294 21.055 165.687 148.335 1.00 54.40 C
ANISOU 3213 CD1 LEU A 294 9017 5454 6199 -543 -419 1 C
ATOM 3214 CD2 LEU A 294 22.439 167.624 149.247 1.00 58.85 C
ANISOU 3214 CD2 LEU A 294 9864 5881 6615 -723 -578 19 C
ATOM 3215 N ARG A 295 21.854 165.261 153.135 1.00 57.19 N
ANISOU 3215 N ARG A 295 10487 5388 5854 -1131 -675 36 N
ATOM 3216 CA ARG A 295 22.930 164.590 153.855 1.00 57.57 C
ANISOU 3216 CA ARG A 295 10655 5387 5831 -1281 -991 143 C
ATOM 3217 C ARG A 295 22.479 163.207 154.390 1.00 62.52 C
ANISOU 3217 C ARG A 295 11352 6003 6398 -1310 -993 160 C
ATOM 3218 O ARG A 295 23.265 162.261 154.334 1.00 61.70 O
ANISOU 3218 O ARG A 295 11131 5928 6385 -1326 -1240 264 O
ATOM 3219 CB ARG A 295 23.492 165.485 154.966 1.00 54.40 C
ANISOU 3219 CB ARG A 295 10637 4829 5204 -1501 -1114 160 C
ATOM 3220 CG ARG A 295 24.446 166.531 154.399 1.00 57.40 C
ANISOU 3220 CG ARG A 295 10888 5232 5690 -1494 -1251 199 C
ATOM 3221 CD ARG A 295 25.028 167.394 155.474 1.00 59.73 C
ANISOU 3221 CD ARG A 295 11572 5365 5758 -1729 -1400 224 C
ATOM 3222 NE ARG A 295 26.051 168.293 154.966 1.00 69.75 N
ANISOU 3222 NE ARG A 295 12705 6652 7145 -1740 -1578 283 N
ATOM 3223 CZ ARG A 295 26.309 169.490 155.482 1.00 90.01 C
ANISOU 3223 CZ ARG A 295 15548 9102 9551 -1884 -1603 263 C
ATOM 3224 NH1 ARG A 295 25.610 169.938 156.520 1.00 83.52 N
ANISOU 3224 NH1 ARG A 295 15171 8127 8436 -2029 -1437 175 N
ATOM 3225 NH2 ARG A 295 27.251 170.259 154.952 1.00 70.60 N
ANISOU 3225 NH2 ARG A 295 12934 6668 7225 -1887 -1768 324 N
ATOM 3226 N VAL A 296 21.214 163.091 154.859 1.00 59.80 N
ANISOU 3226 N VAL A 296 11176 5611 5934 -1306 -706 63 N
ATOM 3227 CA VAL A 296 20.622 161.836 155.360 1.00 60.36 C
ANISOU 3227 CA VAL A 296 11324 5667 5941 -1332 -658 65 C
ATOM 3228 C VAL A 296 20.519 160.830 154.204 1.00 62.70 C
ANISOU 3228 C VAL A 296 11216 6123 6485 -1145 -680 95 C
ATOM 3229 O VAL A 296 20.898 159.665 154.377 1.00 60.73 O
ANISOU 3229 O VAL A 296 10933 5886 6256 -1173 -852 168 O
ATOM 3230 CB VAL A 296 19.258 162.066 156.096 1.00 65.63 C
ANISOU 3230 CB VAL A 296 12259 6228 6451 -1374 -298 -52 C
ATOM 3231 CG1 VAL A 296 18.546 160.745 156.427 1.00 65.47 C
ANISOU 3231 CG1 VAL A 296 12262 6210 6403 -1375 -219 -52 C
ATOM 3232 CG2 VAL A 296 19.446 162.897 157.371 1.00 67.50 C
ANISOU 3232 CG2 VAL A 296 12979 6273 6397 -1599 -278 -82 C
ATOM 3233 N ALA A 297 20.054 161.309 153.015 1.00 58.69 N
ANISOU 3233 N ALA A 297 10419 5720 6158 -969 -521 46 N
ATOM 3234 CA ALA A 297 19.900 160.525 151.783 1.00 56.91 C
ANISOU 3234 CA ALA A 297 9843 5634 6148 -805 -520 63 C
ATOM 3235 C ALA A 297 21.221 160.004 151.240 1.00 61.06 C
ANISOU 3235 C ALA A 297 10179 6215 6807 -786 -787 158 C
ATOM 3236 O ALA A 297 21.237 158.922 150.667 1.00 61.76 O
ANISOU 3236 O ALA A 297 10082 6370 7015 -708 -821 187 O
ATOM 3237 CB ALA A 297 19.177 161.335 150.715 1.00 56.78 C
ANISOU 3237 CB ALA A 297 9624 5686 6265 -663 -323 2 C
ATOM 3238 N THR A 298 22.326 160.744 151.434 1.00 57.87 N
ANISOU 3238 N THR A 298 9821 5769 6399 -861 -968 212 N
ATOM 3239 CA THR A 298 23.671 160.340 151.003 1.00 57.18 C
ANISOU 3239 CA THR A 298 9540 5702 6482 -853 -1215 317 C
ATOM 3240 C THR A 298 24.044 159.003 151.632 1.00 61.55 C
ANISOU 3240 C THR A 298 10135 6210 7043 -917 -1391 401 C
ATOM 3241 O THR A 298 24.591 158.151 150.942 1.00 61.19 O
ANISOU 3241 O THR A 298 9844 6209 7199 -832 -1467 456 O
ATOM 3242 CB THR A 298 24.690 161.448 151.304 1.00 65.90 C
ANISOU 3242 CB THR A 298 10717 6747 7577 -951 -1381 367 C
ATOM 3243 OG1 THR A 298 24.284 162.628 150.623 1.00 61.29 O
ANISOU 3243 OG1 THR A 298 10077 6208 7001 -875 -1203 286 O
ATOM 3244 CG2 THR A 298 26.094 161.100 150.860 1.00 68.02 C
ANISOU 3244 CG2 THR A 298 10751 7017 8076 -941 -1619 487 C
ATOM 3245 N TRP A 299 23.677 158.796 152.912 1.00 58.65 N
ANISOU 3245 N TRP A 299 10090 5742 6453 -1067 -1429 406 N
ATOM 3246 CA TRP A 299 23.965 157.580 153.666 1.00 59.16 C
ANISOU 3246 CA TRP A 299 10252 5740 6486 -1158 -1613 493 C
ATOM 3247 C TRP A 299 23.396 156.310 153.067 1.00 63.03 C
ANISOU 3247 C TRP A 299 10552 6307 7090 -1029 -1507 475 C
ATOM 3248 O TRP A 299 23.935 155.244 153.331 1.00 63.37 O
ANISOU 3248 O TRP A 299 10562 6309 7205 -1061 -1691 569 O
ATOM 3249 CB TRP A 299 23.535 157.734 155.107 1.00 59.51 C
ANISOU 3249 CB TRP A 299 10734 5653 6225 -1359 -1626 481 C
ATOM 3250 CG TRP A 299 24.540 158.508 155.880 1.00 62.61 C
ANISOU 3250 CG TRP A 299 11338 5930 6521 -1543 -1889 568 C
ATOM 3251 CD1 TRP A 299 24.658 159.865 155.949 1.00 65.54 C
ANISOU 3251 CD1 TRP A 299 11828 6269 6803 -1595 -1842 522 C
ATOM 3252 CD2 TRP A 299 25.644 157.968 156.611 1.00 64.78 C
ANISOU 3252 CD2 TRP A 299 11699 6099 6816 -1700 -2274 733 C
ATOM 3253 NE1 TRP A 299 25.724 160.205 156.745 1.00 67.01 N
ANISOU 3253 NE1 TRP A 299 12205 6335 6921 -1793 -2171 643 N
ATOM 3254 CE2 TRP A 299 26.342 159.060 157.177 1.00 70.11 C
ANISOU 3254 CE2 TRP A 299 12579 6676 7382 -1866 -2454 782 C
ATOM 3255 CE3 TRP A 299 26.071 156.659 156.906 1.00 67.16 C
ANISOU 3255 CE3 TRP A 299 11944 6360 7212 -1731 -2496 854 C
ATOM 3256 CZ2 TRP A 299 27.452 158.887 158.014 1.00 72.14 C
ANISOU 3256 CZ2 TRP A 299 12982 6798 7631 -2071 -2871 958 C
ATOM 3257 CZ3 TRP A 299 27.162 156.484 157.742 1.00 71.51 C
ANISOU 3257 CZ3 TRP A 299 12626 6774 7771 -1922 -2901 1031 C
ATOM 3258 CH2 TRP A 299 27.857 157.587 158.266 1.00 74.04 C
ANISOU 3258 CH2 TRP A 299 13136 7000 7994 -2092 -3099 1088 C
ATOM 3259 N ASN A 300 22.347 156.413 152.233 1.00 58.30 N
ANISOU 3259 N ASN A 300 9818 5808 6525 -890 -1232 367 N
ATOM 3260 CA ASN A 300 21.789 155.255 151.549 1.00 56.92 C
ANISOU 3260 CA ASN A 300 9462 5706 6459 -775 -1136 349 C
ATOM 3261 C ASN A 300 22.859 154.651 150.616 1.00 59.03 C
ANISOU 3261 C ASN A 300 9442 6010 6977 -684 -1275 422 C
ATOM 3262 O ASN A 300 22.971 153.430 150.536 1.00 57.81 O
ANISOU 3262 O ASN A 300 9211 5848 6908 -657 -1330 465 O
ATOM 3263 CB ASN A 300 20.561 155.658 150.747 1.00 57.15 C
ANISOU 3263 CB ASN A 300 9395 5822 6498 -662 -859 240 C
ATOM 3264 CG ASN A 300 19.928 154.505 150.020 1.00 66.77 C
ANISOU 3264 CG ASN A 300 10452 7108 7811 -566 -771 223 C
ATOM 3265 OD1 ASN A 300 19.105 153.785 150.572 1.00 67.73 O
ANISOU 3265 OD1 ASN A 300 10684 7205 7845 -601 -694 205 O
ATOM 3266 ND2 ASN A 300 20.306 154.292 148.772 1.00 54.26 N
ANISOU 3266 ND2 ASN A 300 8622 5597 6398 -456 -777 230 N
ATOM 3267 N GLN A 301 23.650 155.521 149.940 1.00 54.58 N
ANISOU 3267 N GLN A 301 8730 5471 6537 -641 -1311 436 N
ATOM 3268 CA GLN A 301 24.726 155.152 149.010 1.00 54.38 C
ANISOU 3268 CA GLN A 301 8433 5458 6771 -558 -1392 497 C
ATOM 3269 C GLN A 301 25.930 154.563 149.745 1.00 61.46 C
ANISOU 3269 C GLN A 301 9321 6244 7788 -643 -1670 640 C
ATOM 3270 O GLN A 301 26.710 153.813 149.147 1.00 61.39 O
ANISOU 3270 O GLN A 301 9087 6213 8027 -571 -1719 703 O
ATOM 3271 CB GLN A 301 25.142 156.358 148.121 1.00 54.88 C
ANISOU 3271 CB GLN A 301 8368 5567 6916 -505 -1327 467 C
ATOM 3272 CG GLN A 301 24.125 156.717 147.027 1.00 55.93 C
ANISOU 3272 CG GLN A 301 8430 5804 7017 -398 -1080 355 C
ATOM 3273 CD GLN A 301 22.790 157.161 147.600 1.00 75.53 C
ANISOU 3273 CD GLN A 301 11105 8302 9291 -430 -951 279 C
ATOM 3274 OE1 GLN A 301 21.817 156.399 147.649 1.00 68.90 O
ANISOU 3274 OE1 GLN A 301 10296 7484 8398 -406 -849 242 O
ATOM 3275 NE2 GLN A 301 22.748 158.363 148.159 1.00 69.31 N
ANISOU 3275 NE2 GLN A 301 10462 7480 8392 -495 -949 259 N
ATOM 3276 N ILE A 302 26.074 154.893 151.043 1.00 60.70 N
ANISOU 3276 N ILE A 302 9481 6059 7525 -805 -1851 697 N
ATOM 3277 CA ILE A 302 27.157 154.398 151.906 1.00 62.84 C
ANISOU 3277 CA ILE A 302 9788 6202 7887 -925 -2175 858 C
ATOM 3278 C ILE A 302 26.765 153.084 152.572 1.00 67.25 C
ANISOU 3278 C ILE A 302 10462 6709 8379 -969 -2240 897 C
ATOM 3279 O ILE A 302 27.637 152.238 152.772 1.00 69.21 O
ANISOU 3279 O ILE A 302 10599 6870 8827 -989 -2462 1033 O
ATOM 3280 CB ILE A 302 27.562 155.478 152.968 1.00 67.24 C
ANISOU 3280 CB ILE A 302 10611 6669 8268 -1115 -2373 911 C
ATOM 3281 CG1 ILE A 302 28.240 156.676 152.323 1.00 67.12 C
ANISOU 3281 CG1 ILE A 302 10443 6681 8378 -1082 -2373 911 C
ATOM 3282 CG2 ILE A 302 28.436 154.928 154.109 1.00 70.18 C
ANISOU 3282 CG2 ILE A 302 11121 6887 8655 -1294 -2747 1088 C
ATOM 3283 CD1 ILE A 302 27.495 157.870 152.493 1.00 75.95 C
ANISOU 3283 CD1 ILE A 302 11774 7834 9250 -1122 -2211 794 C
ATOM 3284 N LEU A 303 25.471 152.931 152.953 1.00 62.07 N
ANISOU 3284 N LEU A 303 10028 6092 7464 -990 -2050 788 N
ATOM 3285 CA LEU A 303 24.965 151.800 153.734 1.00 61.62 C
ANISOU 3285 CA LEU A 303 10144 5981 7288 -1060 -2095 814 C
ATOM 3286 C LEU A 303 24.438 150.637 152.922 1.00 64.41 C
ANISOU 3286 C LEU A 303 10298 6403 7770 -912 -1937 771 C
ATOM 3287 O LEU A 303 24.479 149.510 153.427 1.00 65.18 O
ANISOU 3287 O LEU A 303 10449 6435 7881 -955 -2054 842 O
ATOM 3288 CB LEU A 303 23.913 152.255 154.754 1.00 61.90 C
ANISOU 3288 CB LEU A 303 10562 5984 6975 -1196 -1974 732 C
ATOM 3289 CG LEU A 303 24.415 153.213 155.838 1.00 68.61 C
ANISOU 3289 CG LEU A 303 11719 6718 7632 -1398 -2158 785 C
ATOM 3290 CD1 LEU A 303 23.249 153.920 156.541 1.00 68.53 C
ANISOU 3290 CD1 LEU A 303 12053 6682 7302 -1491 -1909 655 C
ATOM 3291 CD2 LEU A 303 25.348 152.512 156.821 1.00 73.74 C
ANISOU 3291 CD2 LEU A 303 12519 7221 8278 -1572 -2538 961 C
ATOM 3292 N ASP A 304 23.951 150.872 151.680 1.00 58.94 N
ANISOU 3292 N ASP A 304 9398 5831 7167 -754 -1692 665 N
ATOM 3293 CA ASP A 304 23.484 149.771 150.826 1.00 56.68 C
ANISOU 3293 CA ASP A 304 8940 5601 6995 -630 -1552 625 C
ATOM 3294 C ASP A 304 24.600 148.705 150.709 1.00 61.42 C
ANISOU 3294 C ASP A 304 9369 6116 7851 -600 -1736 747 C
ATOM 3295 O ASP A 304 24.278 147.544 151.006 1.00 61.52 O
ANISOU 3295 O ASP A 304 9424 6094 7858 -607 -1754 770 O
ATOM 3296 CB ASP A 304 23.029 150.247 149.440 1.00 56.31 C
ANISOU 3296 CB ASP A 304 8707 5670 7019 -493 -1319 519 C
ATOM 3297 CG ASP A 304 21.647 150.878 149.310 1.00 66.00 C
ANISOU 3297 CG ASP A 304 10032 6978 8066 -483 -1101 403 C
ATOM 3298 OD1 ASP A 304 20.788 150.648 150.204 1.00 66.61 O
ANISOU 3298 OD1 ASP A 304 10309 7029 7969 -560 -1056 381 O
ATOM 3299 OD2 ASP A 304 21.403 151.562 148.287 1.00 70.53 O
ANISOU 3299 OD2 ASP A 304 10478 7629 8692 -399 -967 341 O
ATOM 3300 N PRO A 305 25.915 149.053 150.437 1.00 57.35 N
ANISOU 3300 N PRO A 305 8672 5542 7574 -583 -1885 840 N
ATOM 3301 CA PRO A 305 26.964 148.009 150.400 1.00 58.46 C
ANISOU 3301 CA PRO A 305 8632 5571 8011 -553 -2049 972 C
ATOM 3302 C PRO A 305 27.140 147.228 151.703 1.00 63.24 C
ANISOU 3302 C PRO A 305 9415 6056 8557 -687 -2316 1099 C
ATOM 3303 O PRO A 305 27.326 146.024 151.628 1.00 63.52 O
ANISOU 3303 O PRO A 305 9357 6027 8749 -642 -2354 1156 O
ATOM 3304 CB PRO A 305 28.230 148.787 150.024 1.00 60.81 C
ANISOU 3304 CB PRO A 305 8724 5821 8560 -534 -2152 1051 C
ATOM 3305 CG PRO A 305 27.955 150.150 150.411 1.00 64.57 C
ANISOU 3305 CG PRO A 305 9373 6351 8810 -622 -2166 1004 C
ATOM 3306 CD PRO A 305 26.507 150.357 150.092 1.00 58.07 C
ANISOU 3306 CD PRO A 305 8692 5657 7716 -582 -1896 837 C
ATOM 3307 N TRP A 306 27.001 147.887 152.881 1.00 60.76 N
ANISOU 3307 N TRP A 306 9389 5703 7992 -861 -2483 1134 N
ATOM 3308 CA TRP A 306 27.105 147.235 154.196 1.00 62.75 C
ANISOU 3308 CA TRP A 306 9885 5829 8126 -1029 -2750 1256 C
ATOM 3309 C TRP A 306 25.996 146.222 154.486 1.00 65.90 C
ANISOU 3309 C TRP A 306 10450 6251 8339 -1034 -2616 1189 C
ATOM 3310 O TRP A 306 26.278 145.224 155.148 1.00 65.73 O
ANISOU 3310 O TRP A 306 10501 6118 8356 -1108 -2819 1306 O
ATOM 3311 CB TRP A 306 27.235 148.242 155.335 1.00 62.85 C
ANISOU 3311 CB TRP A 306 10216 5776 7887 -1237 -2944 1303 C
ATOM 3312 CG TRP A 306 28.605 148.831 155.346 1.00 65.15 C
ANISOU 3312 CG TRP A 306 10349 5982 8422 -1280 -3219 1450 C
ATOM 3313 CD1 TRP A 306 28.976 150.023 154.805 1.00 67.26 C
ANISOU 3313 CD1 TRP A 306 10503 6305 8747 -1242 -3156 1408 C
ATOM 3314 CD2 TRP A 306 29.816 148.152 155.696 1.00 67.41 C
ANISOU 3314 CD2 TRP A 306 10487 6113 9011 -1331 -3576 1669 C
ATOM 3315 NE1 TRP A 306 30.340 150.162 154.865 1.00 68.46 N
ANISOU 3315 NE1 TRP A 306 10466 6346 9200 -1283 -3454 1586 N
ATOM 3316 CE2 TRP A 306 30.882 149.032 155.417 1.00 71.59 C
ANISOU 3316 CE2 TRP A 306 10828 6607 9768 -1338 -3722 1755 C
ATOM 3317 CE3 TRP A 306 30.104 146.898 156.274 1.00 70.91 C
ANISOU 3317 CE3 TRP A 306 10946 6430 9567 -1385 -3804 1814 C
ATOM 3318 CZ2 TRP A 306 32.217 148.706 155.691 1.00 73.48 C
ANISOU 3318 CZ2 TRP A 306 10868 6682 10368 -1394 -4087 1988 C
ATOM 3319 CZ3 TRP A 306 31.428 146.581 156.563 1.00 74.79 C
ANISOU 3319 CZ3 TRP A 306 11252 6755 10411 -1440 -4179 2049 C
ATOM 3320 CH2 TRP A 306 32.468 147.471 156.250 1.00 76.15 C
ANISOU 3320 CH2 TRP A 306 11208 6891 10836 -1440 -4313 2136 C
ATOM 3321 N VAL A 307 24.765 146.436 153.958 1.00 60.85 N
ANISOU 3321 N VAL A 307 9848 5744 7528 -956 -2287 1014 N
ATOM 3322 CA VAL A 307 23.676 145.467 154.110 1.00 59.80 C
ANISOU 3322 CA VAL A 307 9829 5635 7255 -951 -2139 949 C
ATOM 3323 C VAL A 307 24.152 144.155 153.459 1.00 65.43 C
ANISOU 3323 C VAL A 307 10297 6315 8249 -835 -2177 1011 C
ATOM 3324 O VAL A 307 24.058 143.114 154.094 1.00 66.96 O
ANISOU 3324 O VAL A 307 10600 6428 8415 -897 -2290 1080 O
ATOM 3325 CB VAL A 307 22.347 145.981 153.511 1.00 61.09 C
ANISOU 3325 CB VAL A 307 10011 5937 7264 -879 -1796 773 C
ATOM 3326 CG1 VAL A 307 21.350 144.848 153.275 1.00 60.08 C
ANISOU 3326 CG1 VAL A 307 9882 5845 7102 -831 -1636 716 C
ATOM 3327 CG2 VAL A 307 21.737 147.075 154.378 1.00 60.70 C
ANISOU 3327 CG2 VAL A 307 10252 5878 6932 -1009 -1731 716 C
ATOM 3328 N TYR A 308 24.745 144.221 152.248 1.00 61.78 N
ANISOU 3328 N TYR A 308 9524 5890 8059 -680 -2089 994 N
ATOM 3329 CA TYR A 308 25.285 143.032 151.592 1.00 62.32 C
ANISOU 3329 CA TYR A 308 9365 5897 8415 -569 -2088 1046 C
ATOM 3330 C TYR A 308 26.494 142.465 152.348 1.00 69.47 C
ANISOU 3330 C TYR A 308 10222 6629 9545 -634 -2418 1245 C
ATOM 3331 O TYR A 308 26.580 141.255 152.495 1.00 69.53 O
ANISOU 3331 O TYR A 308 10206 6551 9661 -619 -2480 1309 O
ATOM 3332 CB TYR A 308 25.635 143.276 150.110 1.00 62.34 C
ANISOU 3332 CB TYR A 308 9087 5957 8642 -406 -1879 972 C
ATOM 3333 CG TYR A 308 26.205 142.045 149.436 1.00 65.55 C
ANISOU 3333 CG TYR A 308 9287 6270 9347 -297 -1835 1015 C
ATOM 3334 CD1 TYR A 308 25.440 140.891 149.283 1.00 67.20 C
ANISOU 3334 CD1 TYR A 308 9558 6483 9493 -270 -1723 965 C
ATOM 3335 CD2 TYR A 308 27.534 142.002 149.030 1.00 68.17 C
ANISOU 3335 CD2 TYR A 308 9367 6486 10046 -231 -1906 1116 C
ATOM 3336 CE1 TYR A 308 25.968 139.743 148.697 1.00 68.71 C
ANISOU 3336 CE1 TYR A 308 9584 6567 9957 -175 -1669 1000 C
ATOM 3337 CE2 TYR A 308 28.079 140.853 148.454 1.00 70.38 C
ANISOU 3337 CE2 TYR A 308 9461 6648 10632 -130 -1836 1156 C
ATOM 3338 CZ TYR A 308 27.292 139.723 148.292 1.00 78.37 C
ANISOU 3338 CZ TYR A 308 10559 7665 11553 -102 -1716 1095 C
ATOM 3339 OH TYR A 308 27.821 138.577 147.734 1.00 80.59 O
ANISOU 3339 OH TYR A 308 10678 7812 12131 -5 -1628 1128 O
ATOM 3340 N ILE A 309 27.417 143.326 152.815 1.00 68.05 N
ANISOU 3340 N ILE A 309 10023 6385 9447 -711 -2643 1352 N
ATOM 3341 CA ILE A 309 28.616 142.893 153.540 1.00 70.88 C
ANISOU 3341 CA ILE A 309 10317 6562 10054 -791 -3006 1572 C
ATOM 3342 C ILE A 309 28.265 142.148 154.848 1.00 77.46 C
ANISOU 3342 C ILE A 309 11456 7301 10675 -961 -3240 1666 C
ATOM 3343 O ILE A 309 28.802 141.074 155.093 1.00 78.87 O
ANISOU 3343 O ILE A 309 11545 7343 11077 -960 -3424 1807 O
ATOM 3344 CB ILE A 309 29.624 144.072 153.782 1.00 74.62 C
ANISOU 3344 CB ILE A 309 10729 6988 10635 -866 -3218 1672 C
ATOM 3345 CG1 ILE A 309 30.138 144.682 152.462 1.00 73.27 C
ANISOU 3345 CG1 ILE A 309 10231 6881 10728 -699 -2997 1602 C
ATOM 3346 CG2 ILE A 309 30.810 143.624 154.652 1.00 78.38 C
ANISOU 3346 CG2 ILE A 309 11156 7257 11366 -983 -3654 1929 C
ATOM 3347 CD1 ILE A 309 30.561 146.218 152.584 1.00 78.28 C
ANISOU 3347 CD1 ILE A 309 10902 7554 11287 -777 -3076 1604 C
ATOM 3348 N LEU A 310 27.360 142.717 155.658 1.00 74.90 N
ANISOU 3348 N LEU A 310 11495 7035 9929 -1109 -3214 1588 N
ATOM 3349 CA LEU A 310 26.971 142.211 156.976 1.00 76.61 C
ANISOU 3349 CA LEU A 310 12077 7155 9875 -1309 -3412 1662 C
ATOM 3350 C LEU A 310 25.868 141.163 157.000 1.00 80.22 C
ANISOU 3350 C LEU A 310 12652 7654 10176 -1280 -3214 1570 C
ATOM 3351 O LEU A 310 25.949 140.260 157.830 1.00 81.88 O
ANISOU 3351 O LEU A 310 13024 7740 10346 -1392 -3424 1688 O
ATOM 3352 CB LEU A 310 26.574 143.369 157.919 1.00 76.94 C
ANISOU 3352 CB LEU A 310 12501 7202 9531 -1509 -3457 1623 C
ATOM 3353 CG LEU A 310 27.601 144.463 158.172 1.00 82.57 C
ANISOU 3353 CG LEU A 310 13197 7854 10320 -1600 -3702 1725 C
ATOM 3354 CD1 LEU A 310 26.980 145.588 158.951 1.00 82.89 C
ANISOU 3354 CD1 LEU A 310 13638 7914 9945 -1775 -3639 1634 C
ATOM 3355 CD2 LEU A 310 28.823 143.929 158.907 1.00 87.75 C
ANISOU 3355 CD2 LEU A 310 13839 8311 11192 -1733 -4180 1987 C
ATOM 3356 N PHE A 311 24.819 141.293 156.156 1.00 73.99 N
ANISOU 3356 N PHE A 311 11800 7025 9288 -1150 -2835 1374 N
ATOM 3357 CA PHE A 311 23.686 140.351 156.190 1.00 72.72 C
ANISOU 3357 CA PHE A 311 11753 6904 8972 -1137 -2643 1287 C
ATOM 3358 C PHE A 311 23.946 139.076 155.400 1.00 74.05 C
ANISOU 3358 C PHE A 311 11658 7045 9432 -987 -2611 1318 C
ATOM 3359 O PHE A 311 23.188 138.730 154.501 1.00 71.58 O
ANISOU 3359 O PHE A 311 11230 6836 9131 -862 -2334 1188 O
ATOM 3360 CB PHE A 311 22.364 141.020 155.769 1.00 73.00 C
ANISOU 3360 CB PHE A 311 11861 7098 8779 -1095 -2285 1088 C
ATOM 3361 CG PHE A 311 21.867 142.180 156.608 1.00 75.43 C
ANISOU 3361 CG PHE A 311 12469 7414 8779 -1243 -2240 1034 C
ATOM 3362 CD1 PHE A 311 22.737 142.897 157.427 1.00 80.27 C
ANISOU 3362 CD1 PHE A 311 13239 7928 9334 -1387 -2503 1140 C
ATOM 3363 CD2 PHE A 311 20.541 142.586 156.541 1.00 77.42 C
ANISOU 3363 CD2 PHE A 311 12837 7757 8821 -1239 -1926 880 C
ATOM 3364 CE1 PHE A 311 22.285 143.985 158.171 1.00 82.42 C
ANISOU 3364 CE1 PHE A 311 13818 8190 9310 -1530 -2435 1078 C
ATOM 3365 CE2 PHE A 311 20.089 143.680 157.283 1.00 81.20 C
ANISOU 3365 CE2 PHE A 311 13589 8219 9043 -1367 -1840 822 C
ATOM 3366 CZ PHE A 311 20.964 144.371 158.093 1.00 81.23 C
ANISOU 3366 CZ PHE A 311 13782 8122 8960 -1513 -2084 913 C
ATOM 3367 N ARG A 312 24.993 138.346 155.793 1.00 71.91 N
ANISOU 3367 N ARG A 312 11313 6614 9396 -1016 -2907 1500 N
ATOM 3368 CA ARG A 312 25.388 137.089 155.174 1.00 71.46 C
ANISOU 3368 CA ARG A 312 11018 6483 9650 -885 -2897 1553 C
ATOM 3369 C ARG A 312 25.555 135.971 156.221 1.00 79.85 C
ANISOU 3369 C ARG A 312 12251 7384 10705 -1008 -3169 1710 C
ATOM 3370 O ARG A 312 25.983 136.251 157.351 1.00 81.10 O
ANISOU 3370 O ARG A 312 12621 7437 10756 -1191 -3483 1850 O
ATOM 3371 CB ARG A 312 26.673 137.299 154.379 1.00 67.69 C
ANISOU 3371 CB ARG A 312 10180 5940 9598 -753 -2953 1632 C
ATOM 3372 CG ARG A 312 26.426 137.882 152.995 1.00 68.19 C
ANISOU 3372 CG ARG A 312 10038 6147 9723 -587 -2608 1460 C
ATOM 3373 CD ARG A 312 27.661 138.508 152.381 1.00 75.26 C
ANISOU 3373 CD ARG A 312 10643 6991 10960 -502 -2652 1526 C
ATOM 3374 NE ARG A 312 28.841 137.644 152.432 1.00 88.87 N
ANISOU 3374 NE ARG A 312 12137 8515 13116 -454 -2842 1707 N
ATOM 3375 CZ ARG A 312 29.988 137.987 153.008 1.00 99.56 C
ANISOU 3375 CZ ARG A 312 13384 9733 14712 -519 -3158 1899 C
ATOM 3376 NH1 ARG A 312 30.127 139.183 153.566 1.00 74.05 N
ANISOU 3376 NH1 ARG A 312 10281 6551 11304 -642 -3315 1923 N
ATOM 3377 NH2 ARG A 312 31.016 137.148 153.004 1.00 90.42 N
ANISOU 3377 NH2 ARG A 312 11979 8376 13999 -462 -3316 2073 N
ATOM 3378 N ARG A 313 25.229 134.705 155.839 1.00 77.83 N
ANISOU 3378 N ARG A 313 11921 7097 10554 -921 -3062 1692 N
ATOM 3379 CA ARG A 313 25.341 133.528 156.720 1.00 80.67 C
ANISOU 3379 CA ARG A 313 12426 7299 10927 -1021 -3300 1838 C
ATOM 3380 C ARG A 313 26.754 133.392 157.306 1.00 89.35 C
ANISOU 3380 C ARG A 313 13417 8193 12337 -1080 -3714 2089 C
ATOM 3381 O ARG A 313 26.887 133.206 158.517 1.00 90.57 O
ANISOU 3381 O ARG A 313 13841 8230 12341 -1278 -4033 2236 O
ATOM 3382 CB ARG A 313 24.899 132.232 156.015 1.00 79.95 C
ANISOU 3382 CB ARG A 313 12215 7199 10964 -889 -3099 1777 C
ATOM 3383 N ALA A 314 27.800 133.579 156.459 1.00 87.38 N
ANISOU 3383 N ALA A 314 12788 7895 12517 -923 -3710 2142 N
ATOM 3384 CA ALA A 314 29.214 133.530 156.847 1.00 90.24 C
ANISOU 3384 CA ALA A 314 12960 8055 13275 -952 -4085 2391 C
ATOM 3385 C ALA A 314 29.543 134.573 157.925 1.00 97.26 C
ANISOU 3385 C ALA A 314 14087 8917 13952 -1175 -4420 2504 C
ATOM 3386 O ALA A 314 30.348 134.274 158.805 1.00 99.57 O
ANISOU 3386 O ALA A 314 14421 9015 14395 -1312 -4845 2745 O
ATOM 3387 CB ALA A 314 30.102 133.726 155.629 1.00 90.74 C
ANISOU 3387 CB ALA A 314 12579 8095 13803 -740 -3916 2381 C
ATOM 3388 N VAL A 315 28.902 135.781 157.874 1.00 93.18 N
ANISOU 3388 N VAL A 315 13745 8578 13083 -1224 -4238 2337 N
ATOM 3389 CA VAL A 315 29.078 136.848 158.878 1.00 94.37 C
ANISOU 3389 CA VAL A 315 14182 8708 12968 -1448 -4500 2409 C
ATOM 3390 C VAL A 315 28.437 136.413 160.212 1.00102.53 C
ANISOU 3390 C VAL A 315 15694 9666 13598 -1693 -4691 2463 C
ATOM 3391 O VAL A 315 29.069 136.541 161.257 1.00103.92 O
ANISOU 3391 O VAL A 315 16072 9680 13731 -1907 -5110 2664 O
ATOM 3392 CB VAL A 315 28.604 138.250 158.393 1.00 94.68 C
ANISOU 3392 CB VAL A 315 14256 8936 12782 -1416 -4226 2214 C
ATOM 3393 CG1 VAL A 315 28.575 139.269 159.532 1.00 95.11 C
ANISOU 3393 CG1 VAL A 315 14694 8957 12485 -1670 -4452 2261 C
ATOM 3394 CG2 VAL A 315 29.479 138.756 157.256 1.00 93.62 C
ANISOU 3394 CG2 VAL A 315 13685 8831 13056 -1224 -4129 2211 C
ATOM 3395 N LEU A 316 27.212 135.863 160.155 1.00101.19 N
ANISOU 3395 N LEU A 316 15702 9597 13147 -1670 -4392 2296 N
ATOM 3396 CA LEU A 316 26.474 135.354 161.316 1.00103.68 C
ANISOU 3396 CA LEU A 316 16470 9846 13077 -1887 -4488 2319 C
ATOM 3397 C LEU A 316 27.203 134.183 161.980 1.00111.98 C
ANISOU 3397 C LEU A 316 17540 10676 14330 -1978 -4891 2567 C
ATOM 3398 O LEU A 316 27.319 134.188 163.203 1.00113.84 O
ANISOU 3398 O LEU A 316 18158 10774 14321 -2241 -5214 2705 O
ATOM 3399 CB LEU A 316 25.032 134.955 160.926 1.00101.80 C
ANISOU 3399 CB LEU A 316 16326 9762 12592 -1806 -4050 2092 C
ATOM 3400 CG LEU A 316 24.003 134.840 162.067 1.00107.56 C
ANISOU 3400 CG LEU A 316 17563 10466 12841 -2036 -4009 2044 C
ATOM 3401 CD1 LEU A 316 23.604 136.229 162.612 1.00107.77 C
ANISOU 3401 CD1 LEU A 316 17893 10545 12511 -2187 -3912 1946 C
ATOM 3402 CD2 LEU A 316 22.758 134.073 161.606 1.00107.25 C
ANISOU 3402 CD2 LEU A 316 17515 10536 12701 -1934 -3637 1878 C
ATOM 3403 N ARG A 317 27.743 133.219 161.188 1.00110.15 N
ANISOU 3403 N ARG A 317 16910 10388 14553 -1773 -4883 2634 N
ATOM 3404 CA ARG A 317 28.492 132.064 161.721 1.00113.65 C
ANISOU 3404 CA ARG A 317 17307 10602 15273 -1827 -5260 2883 C
ATOM 3405 C ARG A 317 29.783 132.496 162.443 1.00123.93 C
ANISOU 3405 C ARG A 317 18589 11709 16789 -1985 -5783 3162 C
ATOM 3406 O ARG A 317 30.228 131.800 163.353 1.00126.22 O
ANISOU 3406 O ARG A 317 19033 11794 17132 -2151 -6194 3393 O
ATOM 3407 CB ARG A 317 28.814 131.011 160.632 1.00112.21 C
ANISOU 3407 CB ARG A 317 16680 10386 15567 -1556 -5084 2880 C
ATOM 3408 CG ARG A 317 27.621 130.424 159.861 1.00118.65 C
ANISOU 3408 CG ARG A 317 17499 11365 16218 -1409 -4614 2634 C
ATOM 3409 CD ARG A 317 26.673 129.564 160.680 1.00129.72 C
ANISOU 3409 CD ARG A 317 19274 12740 17273 -1557 -4630 2622 C
ATOM 3410 NE ARG A 317 25.337 129.506 160.079 1.00136.71 N
ANISOU 3410 NE ARG A 317 20235 13827 17881 -1475 -4174 2360 N
ATOM 3411 CZ ARG A 317 24.930 128.576 159.217 1.00148.81 C
ANISOU 3411 CZ ARG A 317 21588 15393 19562 -1306 -3918 2265 C
ATOM 3412 NH1 ARG A 317 25.753 127.604 158.840 1.00133.96 N
ANISOU 3412 NH1 ARG A 317 19442 13351 18106 -1186 -4034 2395 N
ATOM 3413 NH2 ARG A 317 23.698 128.611 158.727 1.00134.66 N
ANISOU 3413 NH2 ARG A 317 19878 13777 17509 -1262 -3547 2046 N
ATOM 3414 N ARG A 318 30.364 133.646 162.039 1.00123.32 N
ANISOU 3414 N ARG A 318 18328 11690 16837 -1943 -5783 3149 N
ATOM 3415 CA ARG A 318 31.583 134.226 162.617 1.00127.83 C
ANISOU 3415 CA ARG A 318 18851 12092 17626 -2091 -6264 3404 C
ATOM 3416 C ARG A 318 31.271 135.409 163.566 1.00136.27 C
ANISOU 3416 C ARG A 318 20400 13198 18179 -2370 -6402 3374 C
ATOM 3417 O ARG A 318 32.127 136.266 163.806 1.00137.66 O
ANISOU 3417 O ARG A 318 20535 13301 18467 -2475 -6692 3510 O
ATOM 3418 CB ARG A 318 32.575 134.637 161.511 1.00128.49 C
ANISOU 3418 CB ARG A 318 18377 12183 18262 -1858 -6183 3432 C
ATOM 3419 CG ARG A 318 33.064 133.477 160.649 1.00141.31 C
ANISOU 3419 CG ARG A 318 19539 13712 20441 -1604 -6064 3488 C
ATOM 3420 CD ARG A 318 34.228 133.899 159.778 1.00157.24 C
ANISOU 3420 CD ARG A 318 21040 15664 23041 -1431 -6061 3577 C
ATOM 3421 NE ARG A 318 34.441 132.976 158.661 1.00169.36 N
ANISOU 3421 NE ARG A 318 22160 17160 25028 -1148 -5739 3521 N
ATOM 3422 CZ ARG A 318 35.503 132.998 157.861 1.00187.64 C
ANISOU 3422 CZ ARG A 318 23990 19360 27944 -972 -5690 3614 C
ATOM 3423 NH1 ARG A 318 35.610 132.124 156.869 1.00174.70 N
ANISOU 3423 NH1 ARG A 318 22039 17671 26669 -731 -5351 3541 N
ATOM 3424 NH2 ARG A 318 36.470 133.888 158.051 1.00177.90 N
ANISOU 3424 NH2 ARG A 318 22590 18045 26960 -1044 -5969 3780 N
ATOM 3425 N LEU A 319 30.037 135.434 164.108 1.00134.70 N
ANISOU 3425 N LEU A 319 20660 13095 17424 -2495 -6177 3197 N
ATOM 3426 CA LEU A 319 29.537 136.442 165.048 1.00136.43 C
ANISOU 3426 CA LEU A 319 21405 13331 17101 -2766 -6216 3133 C
ATOM 3427 C LEU A 319 28.917 135.746 166.259 1.00144.81 C
ANISOU 3427 C LEU A 319 23005 14269 17748 -3032 -6370 3190 C
ATOM 3428 O LEU A 319 29.100 136.228 167.373 1.00147.15 O
ANISOU 3428 O LEU A 319 23756 14429 17727 -3345 -6687 3305 O
ATOM 3429 CB LEU A 319 28.515 137.375 164.372 1.00133.33 C
ANISOU 3429 CB LEU A 319 21032 13186 16440 -2638 -5671 2816 C
ATOM 3430 CG LEU A 319 27.991 138.546 165.200 1.00138.80 C
ANISOU 3430 CG LEU A 319 22227 13894 16618 -2882 -5630 2722 C
ATOM 3431 CD1 LEU A 319 28.111 139.846 164.436 1.00137.22 C
ANISOU 3431 CD1 LEU A 319 21815 13841 16482 -2755 -5415 2588 C
ATOM 3432 CD2 LEU A 319 26.551 138.311 165.625 1.00140.63 C
ANISOU 3432 CD2 LEU A 319 22858 14194 16382 -2959 -5266 2522 C
ATOM 3433 N GLN A 320 28.171 134.630 166.040 1.00142.25 N
ANISOU 3433 N GLN A 320 22658 13982 17408 -2925 -6141 3109 N
ATOM 3434 CA GLN A 320 27.535 133.835 167.104 1.00144.64 C
ANISOU 3434 CA GLN A 320 23447 14168 17342 -3158 -6245 3156 C
ATOM 3435 C GLN A 320 28.563 133.472 168.214 1.00155.30 C
ANISOU 3435 C GLN A 320 25025 15235 18745 -3439 -6906 3495 C
ATOM 3436 O GLN A 320 28.316 133.856 169.362 1.00157.04 O
ANISOU 3436 O GLN A 320 25824 15349 18495 -3769 -7083 3536 O
ATOM 3437 CB GLN A 320 26.805 132.577 166.560 1.00144.24 C
ANISOU 3437 CB GLN A 320 23229 14183 17393 -2968 -5953 3057 C
ATOM 3438 CG GLN A 320 25.727 132.825 165.495 1.00152.61 C
ANISOU 3438 CG GLN A 320 24087 15502 18395 -2720 -5345 2746 C
ATOM 3439 CD GLN A 320 24.374 133.207 166.041 1.00167.52 C
ANISOU 3439 CD GLN A 320 26428 17477 19743 -2864 -5004 2541 C
ATOM 3440 OE1 GLN A 320 23.462 132.379 166.140 1.00161.71 O
ANISOU 3440 OE1 GLN A 320 25825 16764 18855 -2864 -4790 2457 O
ATOM 3441 NE2 GLN A 320 24.187 134.484 166.337 1.00158.68 N
ANISOU 3441 NE2 GLN A 320 25531 16406 18352 -2976 -4909 2448 N
ATOM 3442 N PRO A 321 29.749 132.855 167.919 1.00155.48 N
ANISOU 3442 N PRO A 321 24624 15116 19333 -3337 -7285 3748 N
ATOM 3443 CA PRO A 321 30.712 132.580 169.003 1.00160.19 C
ANISOU 3443 CA PRO A 321 25440 15430 19996 -3626 -7957 4095 C
ATOM 3444 C PRO A 321 31.452 133.828 169.499 1.00166.70 C
ANISOU 3444 C PRO A 321 26421 16182 20735 -3840 -8292 4213 C
ATOM 3445 O PRO A 321 31.922 133.834 170.638 1.00169.18 O
ANISOU 3445 O PRO A 321 27140 16273 20866 -4181 -8814 4452 O
ATOM 3446 CB PRO A 321 31.673 131.551 168.382 1.00162.97 C
ANISOU 3446 CB PRO A 321 25212 15658 21050 -3402 -8176 4308 C
ATOM 3447 CG PRO A 321 31.037 131.132 167.072 1.00163.84 C
ANISOU 3447 CG PRO A 321 24908 15984 21357 -3025 -7579 4044 C
ATOM 3448 CD PRO A 321 30.261 132.327 166.639 1.00156.03 C
ANISOU 3448 CD PRO A 321 24024 15245 20016 -2975 -7128 3745 C
ATOM 3449 N ARG A 322 31.542 134.884 168.656 1.00161.47 N
ANISOU 3449 N ARG A 322 25467 15699 20187 -3658 -8005 4049 N
ATOM 3450 CA ARG A 322 32.204 136.158 168.980 1.00162.99 C
ANISOU 3450 CA ARG A 322 25770 15849 20312 -3831 -8262 4129 C
ATOM 3451 C ARG A 322 31.217 137.217 169.537 1.00165.39 C
ANISOU 3451 C ARG A 322 26657 16255 19928 -4033 -7975 3891 C
ATOM 3452 O ARG A 322 31.399 138.422 169.314 1.00163.80 O
ANISOU 3452 O ARG A 322 26437 16133 19666 -4038 -7894 3808 O
ATOM 3453 CB ARG A 322 32.990 136.687 167.764 1.00162.49 C
ANISOU 3453 CB ARG A 322 25045 15887 20809 -3530 -8149 4118 C
ATOM 3454 N LEU A 323 30.171 136.745 170.267 1.00162.64 N
ANISOU 3454 N LEU A 323 26826 15890 19082 -4199 -7806 3783 N
ATOM 3455 CA LEU A 323 29.121 137.548 170.909 1.00188.00 C
ANISOU 3455 CA LEU A 323 29808 19739 21885 -3797 -6527 3203 C
ATOM 3456 C LEU A 323 28.374 136.724 171.960 1.00198.27 C
ANISOU 3456 C LEU A 323 31005 21329 22999 -3592 -5899 2980 C
ATOM 3457 O LEU A 323 27.870 135.641 171.663 1.00166.32 O
ANISOU 3457 O LEU A 323 28309 16322 18561 -4507 -7332 3530 O
ATOM 3458 CB LEU A 323 28.129 138.118 169.880 1.00187.80 C
ANISOU 3458 CB LEU A 323 30045 19634 21677 -3879 -6442 3081 C
TER 3459 LEU A 323
HETATM 3460 F A8X A9001 20.030 162.974 145.363 1.00 56.84 F
ANISOU 3460 F A8X A9001 8709 6033 6853 -258 -360 33 F
HETATM 3461 C11 A8X A9001 27.638 163.130 147.976 1.00 58.20 C
ANISOU 3461 C11 A8X A9001 8924 5913 7275 -726 -1513 480 C
HETATM 3462 C12 A8X A9001 26.191 162.878 147.446 1.00 54.49 C
ANISOU 3462 C12 A8X A9001 8468 5528 6707 -614 -1253 362 C
HETATM 3463 C16 A8X A9001 21.199 162.421 145.592 1.00 51.75 C
ANISOU 3463 C16 A8X A9001 8059 5385 6218 -302 -515 80 C
HETATM 3464 C15 A8X A9001 21.604 162.265 146.925 1.00 48.56 C
ANISOU 3464 C15 A8X A9001 7843 4903 5704 -409 -609 102 C
HETATM 3465 C14 A8X A9001 22.829 161.649 147.149 1.00 47.86 C
ANISOU 3465 C14 A8X A9001 7718 4796 5669 -457 -802 177 C
HETATM 3466 C17 A8X A9001 21.994 161.969 144.488 1.00 50.17 C
ANISOU 3466 C17 A8X A9001 7673 5241 6147 -251 -575 112 C
HETATM 3467 C18 A8X A9001 23.232 161.352 144.742 1.00 47.16 C
ANISOU 3467 C18 A8X A9001 7250 4834 5835 -288 -722 174 C
HETATM 3468 C13 A8X A9001 23.668 161.198 146.081 1.00 48.78 C
ANISOU 3468 C13 A8X A9001 7606 4963 5965 -389 -857 217 C
HETATM 3469 S A8X A9001 25.149 160.558 146.406 1.00 53.61 S
ANISOU 3469 S A8X A9001 8140 5520 6709 -440 -1073 321 S
HETATM 3470 O2 A8X A9001 25.133 160.027 147.723 1.00 56.49 O
ANISOU 3470 O2 A8X A9001 8687 5812 6966 -544 -1202 364 O
HETATM 3471 O3 A8X A9001 25.624 159.747 145.349 1.00 54.36 O
ANISOU 3471 O3 A8X A9001 8015 5649 6991 -352 -1039 340 O
HETATM 3472 N1 A8X A9001 26.149 161.867 146.427 1.00 55.47 N
ANISOU 3472 N1 A8X A9001 8372 5719 6987 -497 -1172 358 N
HETATM 3473 C19 A8X A9001 25.525 164.194 146.937 1.00 52.24 C
ANISOU 3473 C19 A8X A9001 8225 5278 6346 -574 -1083 276 C
HETATM 3474 C20 A8X A9001 25.254 165.111 148.149 1.00 53.81 C
ANISOU 3474 C20 A8X A9001 8719 5386 6342 -699 -1107 254 C
HETATM 3475 C3 A8X A9001 26.484 165.164 149.041 1.00 57.55 C
ANISOU 3475 C3 A8X A9001 9291 5766 6808 -850 -1377 357 C
HETATM 3476 C4 A8X A9001 27.544 164.250 148.983 1.00 59.98 C
ANISOU 3476 C4 A8X A9001 9433 6063 7294 -865 -1580 468 C
HETATM 3477 C5 A8X A9001 28.453 164.574 150.016 1.00 63.66 C
ANISOU 3477 C5 A8X A9001 10058 6415 7713 -1040 -1845 567 C
HETATM 3478 C10 A8X A9001 27.915 165.728 150.699 1.00 63.97 C
ANISOU 3478 C10 A8X A9001 10401 6398 7506 -1138 -1778 497 C
HETATM 3479 C9 A8X A9001 28.591 166.264 151.826 1.00 66.92 C
ANISOU 3479 C9 A8X A9001 11041 6640 7745 -1347 -2016 570 C
HETATM 3480 C8 A8X A9001 29.782 165.632 152.244 1.00 68.20 C
ANISOU 3480 C8 A8X A9001 11131 6735 8048 -1453 -2349 732 C
HETATM 3481 C7 A8X A9001 30.319 164.503 151.567 1.00 66.95 C
ANISOU 3481 C7 A8X A9001 10631 6628 8178 -1338 -2411 811 C
HETATM 3482 C6 A8X A9001 29.670 163.972 150.457 1.00 65.95 C
ANISOU 3482 C6 A8X A9001 10269 6627 8162 -1132 -2146 721 C
HETATM 3483 N A8X A9001 26.693 166.130 150.076 1.00 61.99 N
ANISOU 3483 N A8X A9001 10137 6222 7193 -1008 -1469 363 N
HETATM 3484 C2 A8X A9001 26.566 167.544 149.626 1.00 64.11 C
ANISOU 3484 C2 A8X A9001 10423 6496 7441 -984 -1354 304 C
HETATM 3485 C1 A8X A9001 25.834 168.500 150.518 1.00 66.17 C
ANISOU 3485 C1 A8X A9001 11018 6659 7465 -1078 -1234 225 C
HETATM 3486 C A8X A9001 26.905 169.280 151.216 1.00 70.00 C
ANISOU 3486 C A8X A9001 11678 7041 7878 -1255 -1465 295 C
HETATM 3487 O A8X A9001 27.679 170.080 150.726 1.00 68.79 O
ANISOU 3487 O A8X A9001 11411 6897 7828 -1259 -1553 332 O
HETATM 3488 O1 A8X A9001 27.066 169.067 152.515 1.00 74.27 O
ANISOU 3488 O1 A8X A9001 12544 7456 8219 -1445 -1608 329 O
HETATM 3489 ZN ZN A9002 -2.471 124.565 140.346 1.00 71.99 ZN2+
HETATM 3490 C1 CLR A9003 24.469 139.501 129.200 1.00108.68 C
HETATM 3491 C2 CLR A9003 24.454 138.035 129.673 1.00109.21 C
HETATM 3492 C3 CLR A9003 25.462 137.712 130.780 1.00108.47 C
HETATM 3493 C4 CLR A9003 25.497 138.799 131.874 1.00107.57 C
HETATM 3494 C5 CLR A9003 25.350 140.227 131.327 1.00107.13 C
HETATM 3495 C6 CLR A9003 26.213 141.175 131.775 1.00105.74 C
HETATM 3496 C7 CLR A9003 26.368 142.528 131.097 1.00104.58 C
HETATM 3497 C8 CLR A9003 24.997 143.033 130.621 1.00103.04 C
HETATM 3498 C9 CLR A9003 24.316 141.994 129.699 1.00102.92 C
HETATM 3499 C10 CLR A9003 24.254 140.550 130.293 1.00107.44 C
HETATM 3500 C11 CLR A9003 22.936 142.530 129.202 1.00 99.49 C
HETATM 3501 C12 CLR A9003 22.804 144.031 128.827 1.00 98.50 C
HETATM 3502 C13 CLR A9003 23.610 145.001 129.708 1.00100.07 C
HETATM 3503 C14 CLR A9003 25.008 144.370 129.853 1.00101.77 C
HETATM 3504 C15 CLR A9003 25.903 145.518 130.327 1.00101.73 C
HETATM 3505 C16 CLR A9003 25.352 146.729 129.560 1.00100.64 C
HETATM 3506 C17 CLR A9003 23.923 146.388 129.095 1.00 98.11 C
HETATM 3507 C18 CLR A9003 22.870 145.189 131.040 1.00101.45 C
HETATM 3508 C19 CLR A9003 22.875 140.287 130.900 1.00110.22 C
HETATM 3509 C20 CLR A9003 22.840 147.490 129.266 1.00 93.26 C
HETATM 3510 C21 CLR A9003 22.385 147.905 127.869 1.00 93.02 C
HETATM 3511 C22 CLR A9003 23.188 148.646 130.236 1.00 90.29 C
HETATM 3512 C23 CLR A9003 23.549 150.031 129.675 1.00 88.72 C
HETATM 3513 C24 CLR A9003 22.450 151.088 129.900 1.00 87.85 C
HETATM 3514 C25 CLR A9003 22.911 152.542 130.130 1.00 87.12 C
HETATM 3515 C26 CLR A9003 24.039 152.999 129.206 1.00 89.10 C
HETATM 3516 C27 CLR A9003 21.765 153.555 130.061 1.00 84.51 C
HETATM 3517 O1 CLR A9003 25.105 136.427 131.318 1.00107.78 O
HETATM 3518 C24 OLC A9004 24.366 171.538 130.693 1.00 95.64 C
HETATM 3519 C6 OLC A9004 25.076 160.774 132.499 1.00 88.36 C
HETATM 3520 C5 OLC A9004 25.194 161.869 131.429 1.00 88.31 C
HETATM 3521 C4 OLC A9004 24.963 163.247 132.058 1.00 88.43 C
HETATM 3522 C3 OLC A9004 24.222 164.167 131.075 1.00 90.14 C
HETATM 3523 C2 OLC A9004 24.958 165.520 130.972 1.00 92.37 C
HETATM 3524 C21 OLC A9004 24.359 169.031 130.960 1.00 93.21 C
HETATM 3525 C1 OLC A9004 24.009 166.712 130.741 1.00 93.24 C
HETATM 3526 C22 OLC A9004 24.959 170.218 130.204 1.00 93.93 C
HETATM 3527 O19 OLC A9004 22.805 166.625 130.985 1.00 94.76 O
HETATM 3528 O25 OLC A9004 24.665 172.614 129.794 1.00 96.72 O
HETATM 3529 O23 OLC A9004 26.382 170.232 130.324 1.00 93.91 O
HETATM 3530 O20 OLC A9004 24.603 167.825 130.213 1.00 92.79 O
HETATM 3531 C10 OLC A9005 8.212 151.132 139.573 1.00 88.29 C
HETATM 3532 C9 OLC A9005 9.173 150.246 138.737 1.00 88.64 C
HETATM 3533 C11 OLC A9005 8.463 151.365 141.069 1.00 86.36 C
HETATM 3534 C8 OLC A9005 10.395 149.602 139.402 1.00 88.25 C
HETATM 3535 C24 OLC A9005 14.371 138.711 137.111 1.00 98.64 C
HETATM 3536 C12 OLC A9005 7.556 152.509 141.531 1.00 85.37 C
HETATM 3537 C7 OLC A9005 10.219 148.088 139.384 1.00 87.78 C
HETATM 3538 C6 OLC A9005 11.364 147.444 138.601 1.00 87.33 C
HETATM 3539 C5 OLC A9005 10.792 146.324 137.723 1.00 86.34 C
HETATM 3540 C4 OLC A9005 10.923 144.964 138.413 1.00 85.33 C
HETATM 3541 C3 OLC A9005 11.023 143.889 137.343 1.00 87.84 C
HETATM 3542 C2 OLC A9005 10.612 142.530 137.913 1.00 92.68 C
HETATM 3543 C21 OLC A9005 12.321 139.391 138.447 1.00 98.82 C
HETATM 3544 C1 OLC A9005 11.850 141.690 138.267 1.00 97.26 C
HETATM 3545 C22 OLC A9005 12.977 138.270 137.630 1.00100.53 C
HETATM 3546 O19 OLC A9005 12.670 142.105 139.092 1.00 99.37 O
HETATM 3547 O25 OLC A9005 14.963 137.694 136.280 1.00 95.31 O
HETATM 3548 O23 OLC A9005 13.068 137.083 138.445 1.00101.24 O
HETATM 3549 O20 OLC A9005 11.948 140.492 137.600 1.00 98.47 O
HETATM 3550 C1 GOL A9006 28.891 182.545 141.119 1.00 61.61 C
HETATM 3551 O1 GOL A9006 30.238 182.113 140.950 1.00 54.45 O
HETATM 3552 C2 GOL A9006 28.634 183.228 142.449 1.00 70.27 C
HETATM 3553 O2 GOL A9006 29.757 184.048 142.839 1.00 71.88 O
HETATM 3554 C3 GOL A9006 27.407 184.091 142.242 1.00 71.49 C
HETATM 3555 O3 GOL A9006 26.932 184.677 143.451 1.00 73.14 O
HETATM 3556 O HOH A9101 2.125 121.957 157.650 1.00 85.71 O
HETATM 3557 O HOH A9102 25.164 193.792 135.672 1.00 59.29 O
HETATM 3558 O HOH A9103 3.484 116.277 153.097 1.00 58.01 O
HETATM 3559 O HOH A9104 -0.810 111.183 155.845 1.00 53.83 O
HETATM 3560 O HOH A9105 -3.438 122.686 151.492 1.00 59.37 O
HETATM 3561 O HOH A9106 29.608 168.273 127.532 1.00 77.71 O
HETATM 3562 O HOH A9107 5.971 116.331 156.930 1.00 71.52 O
HETATM 3563 O HOH A9108 14.783 127.203 157.027 1.00 90.40 O
HETATM 3564 O HOH A9109 13.050 135.368 140.875 1.00 71.42 O
HETATM 3565 O HOH A9110 -1.739 116.760 135.227 1.00 65.81 O
HETATM 3566 O HOH A9111 10.580 183.269 150.983 1.00 71.36 O
CONECT 807 1432
CONECT 1432 807
CONECT 1457 2039
CONECT 2039 1457
CONECT 2406 3489
CONECT 2426 3489
CONECT 2660 3489
CONECT 2681 3489
CONECT 3460 3463
CONECT 3461 3462 3476
CONECT 3462 3461 3472 3473
CONECT 3463 3460 3464 3466
CONECT 3464 3463 3465
CONECT 3465 3464 3468
CONECT 3466 3463 3467
CONECT 3467 3466 3468
CONECT 3468 3465 3467 3469
CONECT 3469 3468 3470 3471 3472
CONECT 3470 3469
CONECT 3471 3469
CONECT 3472 3462 3469
CONECT 3473 3462 3474
CONECT 3474 3473 3475
CONECT 3475 3474 3476 3483
CONECT 3476 3461 3475 3477
CONECT 3477 3476 3478 3482
CONECT 3478 3477 3479 3483
CONECT 3479 3478 3480
CONECT 3480 3479 3481
CONECT 3481 3480 3482
CONECT 3482 3477 3481
CONECT 3483 3475 3478 3484
CONECT 3484 3483 3485
CONECT 3485 3484 3486
CONECT 3486 3485 3487 3488
CONECT 3487 3486
CONECT 3488 3486
CONECT 3489 2406 2426 2660 2681
CONECT 3490 3491 3499
CONECT 3491 3490 3492
CONECT 3492 3491 3493 3517
CONECT 3493 3492 3494
CONECT 3494 3493 3495 3499
CONECT 3495 3494 3496
CONECT 3496 3495 3497
CONECT 3497 3496 3498 3503
CONECT 3498 3497 3499 3500
CONECT 3499 3490 3494 3498 3508
CONECT 3500 3498 3501
CONECT 3501 3500 3502
CONECT 3502 3501 3503 3506 3507
CONECT 3503 3497 3502 3504
CONECT 3504 3503 3505
CONECT 3505 3504 3506
CONECT 3506 3502 3505 3509
CONECT 3507 3502
CONECT 3508 3499
CONECT 3509 3506 3510 3511
CONECT 3510 3509
CONECT 3511 3509 3512
CONECT 3512 3511 3513
CONECT 3513 3512 3514
CONECT 3514 3513 3515 3516
CONECT 3515 3514
CONECT 3516 3514
CONECT 3517 3492
CONECT 3518 3526 3528
CONECT 3519 3520
CONECT 3520 3519 3521
CONECT 3521 3520 3522
CONECT 3522 3521 3523
CONECT 3523 3522 3525
CONECT 3524 3526 3530
CONECT 3525 3523 3527 3530
CONECT 3526 3518 3524 3529
CONECT 3527 3525
CONECT 3528 3518
CONECT 3529 3526
CONECT 3530 3524 3525
CONECT 3531 3532 3533
CONECT 3532 3531 3534
CONECT 3533 3531 3536
CONECT 3534 3532 3537
CONECT 3535 3545 3547
CONECT 3536 3533
CONECT 3537 3534 3538
CONECT 3538 3537 3539
CONECT 3539 3538 3540
CONECT 3540 3539 3541
CONECT 3541 3540 3542
CONECT 3542 3541 3544
CONECT 3543 3545 3549
CONECT 3544 3542 3546 3549
CONECT 3545 3535 3543 3548
CONECT 3546 3544
CONECT 3547 3535
CONECT 3548 3545
CONECT 3549 3543 3544
CONECT 3550 3551 3552
CONECT 3551 3550
CONECT 3552 3550 3553 3554
CONECT 3553 3552
CONECT 3554 3552 3555
CONECT 3555 3554
MASTER 390 0 6 21 5 0 12 6 3565 1 104 38
END