HEADER SIGNALING PROTEIN 07-OCT-18 6IIV
TITLE CRYSTAL STRUCTURE OF THE HUMAN THROMBOXANE A2 RECEPTOR BOUND TO
TITLE 2 DALTROBAN
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 6IIV 1 JRNL
REVDAT 1 19-DEC-18 6IIV 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. 3.00 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) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.35
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 3 NUMBER OF REFLECTIONS : 15644
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) : 0.212
REMARK 3 R VALUE (WORKING SET) : 0.209
REMARK 3 FREE R VALUE : 0.237
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.130
REMARK 3 FREE R VALUE TEST SET COUNT : 1584
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 : 8
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 3.21
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 90.26
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2567
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2260
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2305
REMARK 3 BIN R VALUE (WORKING SET) : 0.2240
REMARK 3 BIN FREE R VALUE : 0.2430
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.21
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 262
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 : 3476
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 58
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 114.7
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 109.6
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 10.04080
REMARK 3 B22 (A**2) : -17.48760
REMARK 3 B33 (A**2) : 7.44680
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) : 0.420
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.891
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.331
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.963
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.339
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 : 0.929
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.914
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 3616 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 4937 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 1202 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 71 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 530 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 3616 ; 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 : 473 ; 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 : 4509 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.15
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.43
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 20.74
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): 20.5457 158.0030 139.0230
REMARK 3 T TENSOR
REMARK 3 T11: -0.2237 T22: -0.4968
REMARK 3 T33: -0.2584 T12: -0.0381
REMARK 3 T13: -0.0039 T23: 0.0121
REMARK 3 L TENSOR
REMARK 3 L11: 0.8980 L22: 4.8193
REMARK 3 L33: 0.8149 L12: 1.3620
REMARK 3 L13: -0.0909 L23: -0.7253
REMARK 3 S TENSOR
REMARK 3 S11: 0.0712 S12: -0.0447 S13: 0.0076
REMARK 3 S21: 0.3007 S22: -0.1077 S23: -0.1159
REMARK 3 S31: -0.0176 S32: -0.0366 S33: 0.0366
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6IIV 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_1300009247.
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) : 1.0
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 : 15664
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
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 (%) : 97.2
REMARK 200 DATA REDUNDANCY : 9.600
REMARK 200 R MERGE (I) : 0.24200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.16
REMARK 200 COMPLETENESS FOR SHELL (%) : 86.3
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.82000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.000
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 (%): 67.94
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.84
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MAGNESIUM ACETATE, PEG 400, LIPIDIC
REMARK 280 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 62.61000
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 62.61000
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 40.76500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 76.08500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 40.76500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 76.08500
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 62.61000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 40.76500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 76.08500
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 62.61000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 40.76500
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 76.08500
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: 690 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21360 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -1.0 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 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 THR A 59
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 PRO A1000 CG CD
REMARK 470 LEU A1010 CG CD1 CD2
REMARK 470 LEU A1014 CD1 CD2
REMARK 470 ASP A1054 CG OD1 OD2
REMARK 470 GLU A1057 CG CD OE1 OE2
REMARK 470 LEU A1068 CG CD1 CD2
REMARK 470 LYS A1083 CG CD CE NZ
REMARK 470 ARG A 23 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 53 CG CD NE CZ NH1 NH2
REMARK 470 PHE A 138 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG A 140 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 173 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 LYS A2003 CG CD CE NZ
REMARK 470 THR A2005 OG1 CG2
REMARK 470 ILE A2012 CG1 CG2 CD1
REMARK 470 LYS A2031 CG CD CE NZ
REMARK 470 LEU A2041 CG CD1 CD2
REMARK 470 GLU A2050 CB CG CD OE1 OE2
REMARK 470 ASN A 272 CG OD1 ND2
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 LYS A1083 81.86 -66.08
REMARK 500 ILE A1102 -58.68 -120.13
REMARK 500 ASN A 16 53.27 -111.07
REMARK 500 ARG A 140 68.26 -111.97
REMARK 500 VAL A 143 -52.31 82.81
REMARK 500 TYR A 226 22.02 -78.54
REMARK 500 ASP A2019 62.97 -158.32
REMARK 500 VAL A2024 70.94 -104.55
REMARK 500 ASP A2036 28.42 -74.39
REMARK 500 LEU A2041 -66.82 -94.72
REMARK 500 LEU A 319 53.73 -114.25
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A9002 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A2006 SG
REMARK 620 2 CYS A2009 SG 124.6
REMARK 620 3 CYS A2039 SG 113.4 95.8
REMARK 620 4 CYS A2042 SG 102.1 114.0 106.0
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 A90 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 GOL A 9004
DBREF 6IIV A 1001 1106 UNP P0ABE7 C562_ECOLX 23 128
DBREF 6IIV A 10 228 UNP P21731 TA2R_HUMAN 10 228
DBREF 6IIV A 2001 2054 UNP P00268 RUBR_CLOPA 1 54
DBREF 6IIV A 237 323 UNP P21731 TA2R_HUMAN 237 323
SEQADV 6IIV ASP A 991 UNP P0ABE7 EXPRESSION TAG
SEQADV 6IIV TYR A 992 UNP P0ABE7 EXPRESSION TAG
SEQADV 6IIV LYS A 993 UNP P0ABE7 EXPRESSION TAG
SEQADV 6IIV ASP A 994 UNP P0ABE7 EXPRESSION TAG
SEQADV 6IIV ASP A 995 UNP P0ABE7 EXPRESSION TAG
SEQADV 6IIV ASP A 996 UNP P0ABE7 EXPRESSION TAG
SEQADV 6IIV ASP A 997 UNP P0ABE7 EXPRESSION TAG
SEQADV 6IIV GLY A 998 UNP P0ABE7 EXPRESSION TAG
SEQADV 6IIV ALA A 999 UNP P0ABE7 EXPRESSION TAG
SEQADV 6IIV PRO A 1000 UNP P0ABE7 EXPRESSION TAG
SEQADV 6IIV TRP A 1007 UNP P0ABE7 MET 29 ENGINEERED MUTATION
SEQADV 6IIV ILE A 1102 UNP P0ABE7 HIS 124 ENGINEERED MUTATION
SEQADV 6IIV LEU A 1106 UNP P0ABE7 ARG 128 ENGINEERED MUTATION
SEQADV 6IIV ALA A 247 UNP P21731 LEU 247 ENGINEERED MUTATION
SEQADV 6IIV GLU A 324 UNP P21731 EXPRESSION TAG
SEQADV 6IIV PHE A 325 UNP P21731 EXPRESSION TAG
SEQADV 6IIV LEU A 326 UNP P21731 EXPRESSION TAG
SEQADV 6IIV GLU A 327 UNP P21731 EXPRESSION TAG
SEQADV 6IIV VAL A 328 UNP P21731 EXPRESSION TAG
SEQADV 6IIV LEU A 329 UNP P21731 EXPRESSION TAG
SEQADV 6IIV PHE A 330 UNP P21731 EXPRESSION TAG
SEQADV 6IIV 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 A90 A9001 23
HET ZN A9002 1
HET CLR A9003 28
HET GOL A9004 6
HETNAM A90 2-[4-[2-[(4-CHLOROPHENYL)
HETNAM 2 A90 SULFONYLAMINO]ETHYL]PHENYL]ETHANOIC ACID
HETNAM ZN ZINC ION
HETNAM CLR CHOLESTEROL
HETNAM GOL GLYCEROL
HETSYN A90 DALTROBAN
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 A90 C16 H16 CL N O4 S
FORMUL 3 ZN ZN 2+
FORMUL 4 CLR C27 H46 O
FORMUL 5 GOL C3 H8 O3
HELIX 1 AA1 ASP A 1002 ALA A 1020 1 19
HELIX 2 AA2 ASN A 1022 ALA A 1043 1 22
HELIX 3 AA3 PRO A 1045 GLU A 1049 5 5
HELIX 4 AA4 SER A 1055 ASN A 1080 1 26
HELIX 5 AA5 LYS A 1083 ALA A 1091 1 9
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 ARG A 53 1 27
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 VAL A 143 LEU A 165 1 23
HELIX 14 AB5 LEU A 166 GLY A 170 5 5
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 LEU A 270 1 34
HELIX 20 AC2 SER A 283 PHE A 311 1 29
HELIX 21 AC3 ARG A 312 LEU A 319 1 8
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 2.03
LINK SG CYS A2006 ZN ZN A9002 1555 1555 2.21
LINK SG CYS A2009 ZN ZN A9002 1555 1555 2.53
LINK SG CYS A2039 ZN ZN A9002 1555 1555 2.45
LINK SG CYS A2042 ZN ZN A9002 1555 1555 2.29
CISPEP 1 TYR A 178 PRO A 179 0 7.81
SITE 1 AC1 15 GLY A 77 LEU A 78 THR A 81 VAL A 85
SITE 2 AC1 15 HIS A 89 MET A 112 SER A 181 TRP A 182
SITE 3 AC1 15 PHE A 184 TRP A 258 LEU A 291 LEU A 294
SITE 4 AC1 15 ARG A 295 THR A 298 GLN A 301
SITE 1 AC2 4 CYS A2006 CYS A2009 CYS A2039 CYS A2042
SITE 1 AC3 8 ARG A 103 PHE A 107 VAL A 110 TRP A 150
SITE 2 AC3 8 GLY A 154 TRP A 157 LEU A 161 LEU A 168
SITE 1 AC4 5 GLU A 94 TRP A 95 HIS A 96 GLN A1103
SITE 2 AC4 5 ASP A2036
CRYST1 81.530 152.170 125.220 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 0.012265 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006572 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007986 0.00000
ATOM 1 N PRO A1000 14.820 187.558 119.375 1.00142.46 N
ANISOU 1 N PRO A1000 19627 14475 20025 -830 -2614 1950 N
ATOM 2 CA PRO A1000 16.162 187.344 119.943 1.00140.21 C
ANISOU 2 CA PRO A1000 19416 14351 19506 -803 -2278 1766 C
ATOM 3 C PRO A1000 16.577 185.867 120.081 1.00142.29 C
ANISOU 3 C PRO A1000 19737 14783 19546 -830 -2115 1651 C
ATOM 4 O PRO A1000 15.759 184.960 119.867 1.00142.17 O
ANISOU 4 O PRO A1000 19682 14772 19565 -852 -2237 1693 O
ATOM 5 CB PRO A1000 16.099 188.068 121.295 1.00141.20 C
ANISOU 5 CB PRO A1000 19283 14461 19905 -617 -2096 1668 C
ATOM 6 N ALA A1001 17.871 185.634 120.422 1.00136.40 N
ANISOU 6 N ALA A1001 19076 14160 18588 -834 -1847 1514 N
ATOM 7 CA ALA A1001 18.461 184.299 120.596 1.00133.98 C
ANISOU 7 CA ALA A1001 18819 14001 18087 -853 -1661 1399 C
ATOM 8 C ALA A1001 18.696 183.968 122.070 1.00134.05 C
ANISOU 8 C ALA A1001 18600 14113 18219 -699 -1437 1251 C
ATOM 9 O ALA A1001 18.896 184.883 122.884 1.00134.40 O
ANISOU 9 O ALA A1001 18529 14130 18407 -608 -1357 1208 O
ATOM 10 CB ALA A1001 19.771 184.195 119.827 1.00134.54 C
ANISOU 10 CB ALA A1001 19148 14108 17863 -983 -1523 1368 C
ATOM 11 N ASP A1002 18.673 182.650 122.400 1.00125.98 N
ANISOU 11 N ASP A1002 17543 13198 17127 -685 -1343 1175 N
ATOM 12 CA ASP A1002 18.898 182.095 123.738 1.00122.40 C
ANISOU 12 CA ASP A1002 16919 12843 16743 -569 -1148 1042 C
ATOM 13 C ASP A1002 20.312 182.465 124.190 1.00119.33 C
ANISOU 13 C ASP A1002 16569 12508 16261 -566 -958 953 C
ATOM 14 O ASP A1002 21.248 182.432 123.390 1.00118.98 O
ANISOU 14 O ASP A1002 16688 12476 16045 -665 -910 966 O
ATOM 15 CB ASP A1002 18.690 180.556 123.714 1.00124.41 C
ANISOU 15 CB ASP A1002 17181 13189 16899 -590 -1114 1002 C
ATOM 16 CG ASP A1002 18.810 179.752 125.023 1.00142.61 C
ANISOU 16 CG ASP A1002 19335 15593 19259 -489 -942 879 C
ATOM 17 OD1 ASP A1002 18.622 178.501 124.978 1.00143.04 O1-
ANISOU 17 OD1 ASP A1002 19397 15713 19240 -507 -923 853 O1-
ATOM 18 OD2 ASP A1002 19.103 180.365 126.091 1.00151.94 O1-
ANISOU 18 OD2 ASP A1002 20415 16775 20541 -405 -834 812 O1-
ATOM 19 N LEU A1003 20.449 182.846 125.468 1.00110.71 N
ANISOU 19 N LEU A1003 15340 11431 15295 -464 -850 870 N
ATOM 20 CA LEU A1003 21.701 183.242 126.119 1.00107.61 C
ANISOU 20 CA LEU A1003 14956 11072 14858 -460 -707 794 C
ATOM 21 C LEU A1003 22.826 182.241 125.862 1.00107.83 C
ANISOU 21 C LEU A1003 15049 11196 14727 -523 -589 751 C
ATOM 22 O LEU A1003 23.979 182.638 125.685 1.00107.58 O
ANISOU 22 O LEU A1003 15070 11163 14645 -573 -510 744 O
ATOM 23 CB LEU A1003 21.450 183.356 127.619 1.00106.57 C
ANISOU 23 CB LEU A1003 14698 10944 14851 -359 -624 705 C
ATOM 24 CG LEU A1003 22.307 184.348 128.350 1.00110.85 C
ANISOU 24 CG LEU A1003 15255 11448 15415 -353 -558 660 C
ATOM 25 CD1 LEU A1003 21.464 185.427 128.952 1.00111.67 C
ANISOU 25 CD1 LEU A1003 15307 11435 15686 -280 -574 655 C
ATOM 26 CD2 LEU A1003 23.066 183.671 129.434 1.00113.52 C
ANISOU 26 CD2 LEU A1003 15571 11861 15702 -348 -450 567 C
ATOM 27 N GLU A1004 22.466 180.946 125.828 1.00101.15 N
ANISOU 27 N GLU A1004 14186 10416 13828 -519 -571 727 N
ATOM 28 CA GLU A1004 23.327 179.788 125.604 1.00 99.17 C
ANISOU 28 CA GLU A1004 13980 10242 13460 -565 -450 684 C
ATOM 29 C GLU A1004 23.849 179.739 124.178 1.00100.13 C
ANISOU 29 C GLU A1004 14285 10328 13432 -683 -427 737 C
ATOM 30 O GLU A1004 24.976 179.292 123.964 1.00 98.42 O
ANISOU 30 O GLU A1004 14106 10132 13159 -726 -271 703 O
ATOM 31 CB GLU A1004 22.508 178.535 125.889 1.00100.23 C
ANISOU 31 CB GLU A1004 14061 10433 13589 -530 -467 657 C
ATOM 32 CG GLU A1004 23.287 177.264 126.123 1.00110.77 C
ANISOU 32 CG GLU A1004 15387 11842 14857 -539 -334 593 C
ATOM 33 CD GLU A1004 22.421 176.310 126.910 1.00137.39 C
ANISOU 33 CD GLU A1004 18661 15268 18274 -474 -352 553 C
ATOM 34 OE1 GLU A1004 21.314 175.967 126.427 1.00130.01 O
ANISOU 34 OE1 GLU A1004 17745 14321 17333 -485 -453 593 O
ATOM 35 OE2 GLU A1004 22.789 176.022 128.072 1.00132.64 O1-
ANISOU 35 OE2 GLU A1004 17965 14706 17726 -420 -284 490 O1-
ATOM 36 N ASP A1005 23.018 180.149 123.205 1.00 96.93 N
ANISOU 36 N ASP A1005 14002 9854 12974 -744 -578 825 N
ATOM 37 CA ASP A1005 23.388 180.160 121.797 1.00 98.69 C
ANISOU 37 CA ASP A1005 14463 10018 13016 -883 -573 884 C
ATOM 38 C ASP A1005 24.469 181.210 121.604 1.00104.27 C
ANISOU 38 C ASP A1005 15220 10679 13720 -923 -478 893 C
ATOM 39 O ASP A1005 25.476 180.933 120.954 1.00104.61 O
ANISOU 39 O ASP A1005 15392 10706 13650 -1010 -311 878 O
ATOM 40 CB ASP A1005 22.173 180.490 120.921 1.00102.73 C
ANISOU 40 CB ASP A1005 15094 10446 13493 -948 -818 997 C
ATOM 41 CG ASP A1005 21.098 179.419 120.807 1.00121.02 C
ANISOU 41 CG ASP A1005 17411 12782 15787 -956 -933 1013 C
ATOM 42 OD1 ASP A1005 20.697 178.853 121.853 1.00120.13 O1-
ANISOU 42 OD1 ASP A1005 17093 12739 15811 -842 -910 955 O1-
ATOM 43 OD2 ASP A1005 20.578 179.226 119.692 1.00134.18 O1-
ANISOU 43 OD2 ASP A1005 19297 14380 17306 -1087 -1070 1095 O1-
ATOM 44 N ASN A1006 24.274 182.405 122.216 1.00101.43 N
ANISOU 44 N ASN A1006 14752 10286 13502 -858 -565 915 N
ATOM 45 CA ASN A1006 25.203 183.540 122.191 1.00101.36 C
ANISOU 45 CA ASN A1006 14765 10228 13521 -886 -504 928 C
ATOM 46 C ASN A1006 26.486 183.177 122.903 1.00104.70 C
ANISOU 46 C ASN A1006 15078 10708 13994 -860 -306 846 C
ATOM 47 O ASN A1006 27.563 183.571 122.456 1.00104.13 O
ANISOU 47 O ASN A1006 15064 10599 13903 -930 -188 857 O
ATOM 48 CB ASN A1006 24.577 184.772 122.851 1.00 99.29 C
ANISOU 48 CB ASN A1006 14399 9909 13416 -808 -642 956 C
ATOM 49 CG ASN A1006 23.408 185.343 122.101 1.00122.15 C
ANISOU 49 CG ASN A1006 17376 12711 16325 -835 -858 1065 C
ATOM 50 OD1 ASN A1006 22.353 185.620 122.676 1.00121.22 O
ANISOU 50 OD1 ASN A1006 17127 12561 16371 -743 -977 1081 O
ATOM 51 ND2 ASN A1006 23.562 185.534 120.800 1.00113.50 N
ANISOU 51 ND2 ASN A1006 16503 11550 15070 -970 -912 1150 N
ATOM 52 N TRP A1007 26.366 182.413 124.012 1.00101.68 N
ANISOU 52 N TRP A1007 14536 10405 13693 -768 -280 773 N
ATOM 53 CA TRP A1007 27.498 181.956 124.803 1.00101.80 C
ANISOU 53 CA TRP A1007 14432 10466 13783 -745 -143 711 C
ATOM 54 C TRP A1007 28.423 181.111 123.935 1.00105.30 C
ANISOU 54 C TRP A1007 14948 10906 14155 -824 36 707 C
ATOM 55 O TRP A1007 29.627 181.360 123.927 1.00105.21 O
ANISOU 55 O TRP A1007 14895 10862 14216 -860 163 707 O
ATOM 56 CB TRP A1007 27.038 181.224 126.069 1.00100.53 C
ANISOU 56 CB TRP A1007 14130 10374 13691 -650 -174 646 C
ATOM 57 CG TRP A1007 28.180 180.748 126.917 1.00102.35 C
ANISOU 57 CG TRP A1007 14246 10635 14008 -640 -84 603 C
ATOM 58 CD1 TRP A1007 28.912 181.481 127.810 1.00105.65 C
ANISOU 58 CD1 TRP A1007 14589 11025 14528 -635 -107 594 C
ATOM 59 CD2 TRP A1007 28.764 179.448 126.891 1.00102.29 C
ANISOU 59 CD2 TRP A1007 14190 10669 14007 -646 27 575 C
ATOM 60 NE1 TRP A1007 29.903 180.700 128.365 1.00105.05 N
ANISOU 60 NE1 TRP A1007 14411 10970 14534 -642 -45 576 N
ATOM 61 CE2 TRP A1007 29.836 179.448 127.816 1.00106.31 C
ANISOU 61 CE2 TRP A1007 14573 11170 14650 -641 48 563 C
ATOM 62 CE3 TRP A1007 28.491 178.277 126.164 1.00104.16 C
ANISOU 62 CE3 TRP A1007 14486 10935 14156 -663 104 564 C
ATOM 63 CZ2 TRP A1007 30.635 178.325 128.030 1.00106.16 C
ANISOU 63 CZ2 TRP A1007 14457 11166 14711 -642 139 550 C
ATOM 64 CZ3 TRP A1007 29.283 177.160 126.376 1.00106.24 C
ANISOU 64 CZ3 TRP A1007 14669 11216 14482 -659 224 535 C
ATOM 65 CH2 TRP A1007 30.357 177.198 127.282 1.00107.06 C
ANISOU 65 CH2 TRP A1007 14621 11306 14752 -644 242 533 C
ATOM 66 N GLU A1008 27.849 180.186 123.133 1.00102.06 N
ANISOU 66 N GLU A1008 14660 10508 13612 -861 52 709 N
ATOM 67 CA GLU A1008 28.599 179.339 122.201 1.00102.16 C
ANISOU 67 CA GLU A1008 14792 10492 13533 -946 252 695 C
ATOM 68 C GLU A1008 29.295 180.153 121.140 1.00106.63 C
ANISOU 68 C GLU A1008 15527 10961 14026 -1061 360 742 C
ATOM 69 O GLU A1008 30.490 179.964 120.949 1.00106.46 O
ANISOU 69 O GLU A1008 15480 10900 14069 -1098 583 721 O
ATOM 70 CB GLU A1008 27.722 178.255 121.575 1.00103.63 C
ANISOU 70 CB GLU A1008 15115 10694 13565 -977 220 688 C
ATOM 71 CG GLU A1008 27.467 177.092 122.518 1.00116.48 C
ANISOU 71 CG GLU A1008 16580 12408 15270 -883 224 626 C
ATOM 72 CD GLU A1008 28.655 176.252 122.963 1.00146.95 C
ANISOU 72 CD GLU A1008 20316 16278 19240 -858 433 570 C
ATOM 73 OE1 GLU A1008 29.787 176.466 122.463 1.00136.92 O
ANISOU 73 OE1 GLU A1008 19075 14939 18009 -916 620 575 O
ATOM 74 OE2 GLU A1008 28.436 175.357 123.815 1.00146.43 O1-
ANISOU 74 OE2 GLU A1008 20118 16277 19242 -783 411 528 O1-
ATOM 75 N THR A1009 28.571 181.111 120.509 1.00103.72 N
ANISOU 75 N THR A1009 15313 10541 13554 -1116 200 812 N
ATOM 76 CA THR A1009 29.094 182.041 119.500 1.00104.65 C
ANISOU 76 CA THR A1009 15625 10557 13580 -1238 264 870 C
ATOM 77 C THR A1009 30.357 182.718 120.057 1.00108.54 C
ANISOU 77 C THR A1009 15954 11033 14252 -1216 401 857 C
ATOM 78 O THR A1009 31.405 182.696 119.403 1.00108.53 O
ANISOU 78 O THR A1009 16031 10963 14242 -1304 631 856 O
ATOM 79 CB THR A1009 28.033 183.101 119.131 1.00109.87 C
ANISOU 79 CB THR A1009 16402 11170 14175 -1264 -2 959 C
ATOM 80 OG1 THR A1009 26.739 182.512 119.001 1.00104.46 O
ANISOU 80 OG1 THR A1009 15764 10507 13418 -1250 -192 982 O
ATOM 81 CG2 THR A1009 28.391 183.875 117.874 1.00112.52 C
ANISOU 81 CG2 THR A1009 17016 11388 14350 -1422 36 1033 C
ATOM 82 N LEU A1010 30.258 183.261 121.295 1.00104.88 N
ANISOU 82 N LEU A1010 15268 10621 13961 -1105 268 843 N
ATOM 83 CA LEU A1010 31.360 183.931 121.973 1.00105.09 C
ANISOU 83 CA LEU A1010 15133 10629 14169 -1089 334 839 C
ATOM 84 C LEU A1010 32.559 182.986 122.172 1.00110.55 C
ANISOU 84 C LEU A1010 15689 11324 14990 -1091 556 799 C
ATOM 85 O LEU A1010 33.693 183.427 121.982 1.00111.68 O
ANISOU 85 O LEU A1010 15779 11401 15254 -1144 696 822 O
ATOM 86 CB LEU A1010 30.905 184.613 123.280 1.00103.86 C
ANISOU 86 CB LEU A1010 14821 10511 14131 -987 138 825 C
ATOM 87 N ASN A1011 32.315 181.681 122.456 1.00106.33 N
ANISOU 87 N ASN A1011 15100 10851 14451 -1041 596 748 N
ATOM 88 CA ASN A1011 33.406 180.708 122.616 1.00106.73 C
ANISOU 88 CA ASN A1011 15010 10887 14656 -1036 804 718 C
ATOM 89 C ASN A1011 34.027 180.299 121.295 1.00113.29 C
ANISOU 89 C ASN A1011 16004 11625 15417 -1139 1088 718 C
ATOM 90 O ASN A1011 35.252 180.238 121.199 1.00113.89 O
ANISOU 90 O ASN A1011 15968 11624 15680 -1170 1301 726 O
ATOM 91 CB ASN A1011 32.956 179.462 123.349 1.00105.04 C
ANISOU 91 CB ASN A1011 14695 10754 14460 -951 755 667 C
ATOM 92 CG ASN A1011 32.502 179.716 124.742 1.00122.49 C
ANISOU 92 CG ASN A1011 16752 13036 16751 -861 533 655 C
ATOM 93 OD1 ASN A1011 33.240 180.206 125.598 1.00118.32 O
ANISOU 93 OD1 ASN A1011 16069 12491 16398 -847 485 671 O
ATOM 94 ND2 ASN A1011 31.272 179.374 124.987 1.00110.40 N
ANISOU 94 ND2 ASN A1011 15277 11573 15097 -810 396 630 N
ATOM 95 N ASP A1012 33.178 179.989 120.293 1.00111.26 N
ANISOU 95 N ASP A1012 16015 11359 14900 -1202 1095 713 N
ATOM 96 CA ASP A1012 33.566 179.558 118.950 1.00113.66 C
ANISOU 96 CA ASP A1012 16570 11558 15057 -1327 1363 703 C
ATOM 97 C ASP A1012 34.512 180.577 118.349 1.00119.19 C
ANISOU 97 C ASP A1012 17334 12150 15804 -1423 1527 747 C
ATOM 98 O ASP A1012 35.564 180.208 117.825 1.00120.49 O
ANISOU 98 O ASP A1012 17509 12212 16059 -1483 1853 727 O
ATOM 99 CB ASP A1012 32.325 179.389 118.035 1.00116.53 C
ANISOU 99 CB ASP A1012 17258 11920 15099 -1406 1233 717 C
ATOM 100 CG ASP A1012 31.404 178.194 118.287 1.00129.94 C
ANISOU 100 CG ASP A1012 18955 13695 16720 -1349 1133 673 C
ATOM 101 OD1 ASP A1012 31.782 177.294 119.090 1.00129.34 O
ANISOU 101 OD1 ASP A1012 18657 13668 16817 -1254 1220 619 O
ATOM 102 OD2 ASP A1012 30.311 178.146 117.664 1.00138.08 O1-
ANISOU 102 OD2 ASP A1012 20210 14726 17529 -1409 956 703 O1-
ATOM 103 N ASN A1013 34.156 181.861 118.483 1.00115.20 N
ANISOU 103 N ASN A1013 16846 11655 15270 -1430 1313 805 N
ATOM 104 CA ASN A1013 34.952 182.966 117.990 1.00116.23 C
ANISOU 104 CA ASN A1013 17033 11687 15442 -1520 1424 855 C
ATOM 105 C ASN A1013 36.182 183.247 118.865 1.00119.07 C
ANISOU 105 C ASN A1013 17066 12031 16143 -1466 1518 860 C
ATOM 106 O ASN A1013 37.219 183.607 118.318 1.00120.36 O
ANISOU 106 O ASN A1013 17241 12084 16405 -1551 1763 883 O
ATOM 107 CB ASN A1013 34.079 184.187 117.791 1.00118.09 C
ANISOU 107 CB ASN A1013 17418 11925 15525 -1551 1151 921 C
ATOM 108 CG ASN A1013 33.090 184.000 116.670 1.00144.87 C
ANISOU 108 CG ASN A1013 21168 15277 18600 -1656 1081 948 C
ATOM 109 OD1 ASN A1013 33.463 183.839 115.506 1.00145.07 O
ANISOU 109 OD1 ASN A1013 21473 15193 18453 -1804 1299 956 O
ATOM 110 ND2 ASN A1013 31.810 183.990 116.995 1.00134.35 N
ANISOU 110 ND2 ASN A1013 19846 14014 17187 -1595 779 968 N
ATOM 111 N LEU A1014 36.096 183.033 120.200 1.00113.55 N
ANISOU 111 N LEU A1014 16089 11426 15629 -1339 1333 843 N
ATOM 112 CA LEU A1014 37.238 183.218 121.108 1.00113.71 C
ANISOU 112 CA LEU A1014 15805 11421 15980 -1303 1365 863 C
ATOM 113 C LEU A1014 38.366 182.243 120.727 1.00120.99 C
ANISOU 113 C LEU A1014 16612 12253 17105 -1328 1700 848 C
ATOM 114 O LEU A1014 39.539 182.627 120.735 1.00122.02 O
ANISOU 114 O LEU A1014 16576 12287 17499 -1366 1849 891 O
ATOM 115 CB LEU A1014 36.822 183.017 122.574 1.00111.70 C
ANISOU 115 CB LEU A1014 15345 11269 15826 -1186 1091 846 C
ATOM 116 CG LEU A1014 36.714 184.280 123.416 1.00115.33 C
ANISOU 116 CG LEU A1014 15750 11742 16328 -1171 843 880 C
ATOM 117 N LYS A1015 37.987 180.997 120.341 1.00118.45 N
ANISOU 117 N LYS A1015 16384 11949 16674 -1311 1829 791 N
ATOM 118 CA LYS A1015 38.871 179.920 119.877 1.00119.73 C
ANISOU 118 CA LYS A1015 16479 12011 17002 -1328 2180 761 C
ATOM 119 C LYS A1015 39.506 180.288 118.530 1.00127.26 C
ANISOU 119 C LYS A1015 17648 12812 17891 -1465 2535 767 C
ATOM 120 O LYS A1015 40.657 179.923 118.297 1.00128.75 O
ANISOU 120 O LYS A1015 17692 12871 18355 -1488 2860 768 O
ATOM 121 CB LYS A1015 38.105 178.587 119.759 1.00120.76 C
ANISOU 121 CB LYS A1015 16715 12199 16971 -1283 2196 692 C
ATOM 122 CG LYS A1015 37.691 177.973 121.100 1.00130.26 C
ANISOU 122 CG LYS A1015 17684 13526 18282 -1153 1924 681 C
ATOM 123 CD LYS A1015 38.569 176.777 121.493 1.00139.04 C
ANISOU 123 CD LYS A1015 18560 14583 19688 -1096 2105 664 C
ATOM 124 CE LYS A1015 38.388 176.323 122.928 1.00142.02 C
ANISOU 124 CE LYS A1015 18687 15056 20218 -987 1822 676 C
ATOM 125 NZ LYS A1015 37.066 175.681 123.164 1.00147.00 N
ANISOU 125 NZ LYS A1015 19457 15814 20584 -936 1645 622 N
ATOM 126 N VAL A1016 38.761 181.015 117.653 1.00125.09 N
ANISOU 126 N VAL A1016 17721 12535 17270 -1564 2475 777 N
ATOM 127 CA VAL A1016 39.232 181.476 116.335 1.00127.87 C
ANISOU 127 CA VAL A1016 18359 12737 17487 -1723 2783 787 C
ATOM 128 C VAL A1016 40.426 182.414 116.533 1.00134.48 C
ANISOU 128 C VAL A1016 18978 13486 18634 -1750 2904 847 C
ATOM 129 O VAL A1016 41.533 182.066 116.126 1.00136.46 O
ANISOU 129 O VAL A1016 19142 13593 19112 -1795 3288 839 O
ATOM 130 CB VAL A1016 38.113 182.144 115.478 1.00131.83 C
ANISOU 130 CB VAL A1016 19278 13254 17557 -1829 2603 810 C
ATOM 131 CG1 VAL A1016 38.676 182.754 114.193 1.00134.52 C
ANISOU 131 CG1 VAL A1016 19929 13426 17754 -2013 2902 834 C
ATOM 132 CG2 VAL A1016 36.989 181.171 115.158 1.00130.90 C
ANISOU 132 CG2 VAL A1016 19390 13194 17152 -1830 2500 763 C
ATOM 133 N ILE A1017 40.193 183.578 117.195 1.00130.62 N
ANISOU 133 N ILE A1017 18386 13069 18174 -1720 2580 907 N
ATOM 134 CA ILE A1017 41.167 184.637 117.508 1.00131.66 C
ANISOU 134 CA ILE A1017 18316 13133 18576 -1749 2598 976 C
ATOM 135 C ILE A1017 42.486 184.065 118.077 1.00138.41 C
ANISOU 135 C ILE A1017 18780 13909 19900 -1701 2799 990 C
ATOM 136 O ILE A1017 43.570 184.546 117.724 1.00140.45 O
ANISOU 136 O ILE A1017 18930 14031 20405 -1774 3038 1037 O
ATOM 137 CB ILE A1017 40.530 185.717 118.443 1.00132.37 C
ANISOU 137 CB ILE A1017 18331 13334 18630 -1689 2160 1019 C
ATOM 138 CG1 ILE A1017 39.211 186.259 117.857 1.00130.94 C
ANISOU 138 CG1 ILE A1017 18497 13208 18047 -1725 1954 1020 C
ATOM 139 CG2 ILE A1017 41.519 186.875 118.736 1.00134.76 C
ANISOU 139 CG2 ILE A1017 18460 13556 19189 -1738 2160 1093 C
ATOM 140 CD1 ILE A1017 38.243 186.722 118.839 1.00129.38 C
ANISOU 140 CD1 ILE A1017 18223 13133 17801 -1621 1553 1025 C
ATOM 141 N GLU A1018 42.369 183.024 118.930 1.00134.17 N
ANISOU 141 N GLU A1018 18033 13447 19499 -1584 2696 958 N
ATOM 142 CA GLU A1018 43.461 182.306 119.586 1.00135.06 C
ANISOU 142 CA GLU A1018 17761 13488 20067 -1523 2812 983 C
ATOM 143 C GLU A1018 44.420 181.694 118.566 1.00141.96 C
ANISOU 143 C GLU A1018 18635 14175 21128 -1590 3331 965 C
ATOM 144 O GLU A1018 45.621 181.960 118.620 1.00143.39 O
ANISOU 144 O GLU A1018 18549 14218 21717 -1618 3516 1029 O
ATOM 145 CB GLU A1018 42.877 181.191 120.475 1.00134.65 C
ANISOU 145 CB GLU A1018 17595 13553 20010 -1400 2607 941 C
ATOM 146 CG GLU A1018 43.366 181.188 121.910 1.00144.49 C
ANISOU 146 CG GLU A1018 18466 14826 21610 -1323 2335 1004 C
ATOM 147 CD GLU A1018 42.458 180.405 122.836 1.00161.14 C
ANISOU 147 CD GLU A1018 20557 17080 23589 -1220 2044 963 C
ATOM 148 OE1 GLU A1018 41.463 180.990 123.323 1.00145.25 O
ANISOU 148 OE1 GLU A1018 18691 15195 21303 -1198 1743 945 O
ATOM 149 OE2 GLU A1018 42.719 179.198 123.047 1.00158.03 O1-
ANISOU 149 OE2 GLU A1018 20008 16660 23378 -1161 2133 950 O1-
ATOM 150 N LYS A1019 43.882 180.892 117.629 1.00139.57 N
ANISOU 150 N LYS A1019 18644 13852 20533 -1626 3571 881 N
ATOM 151 CA LYS A1019 44.654 180.173 116.614 1.00142.48 C
ANISOU 151 CA LYS A1019 19087 14028 21021 -1694 4109 838 C
ATOM 152 C LYS A1019 44.931 180.984 115.352 1.00149.61 C
ANISOU 152 C LYS A1019 20313 14795 21735 -1862 4426 838 C
ATOM 153 O LYS A1019 45.856 180.645 114.615 1.00151.65 O
ANISOU 153 O LYS A1019 20581 14855 22184 -1931 4920 817 O
ATOM 154 CB LYS A1019 43.992 178.825 116.278 1.00144.26 C
ANISOU 154 CB LYS A1019 19505 14278 21031 -1660 4223 740 C
ATOM 155 CG LYS A1019 44.034 177.838 117.444 1.00150.72 C
ANISOU 155 CG LYS A1019 19967 15177 22122 -1504 4019 743 C
ATOM 156 CD LYS A1019 43.427 176.499 117.086 1.00158.09 C
ANISOU 156 CD LYS A1019 21080 16112 22875 -1476 4168 648 C
ATOM 157 CE LYS A1019 43.368 175.567 118.272 1.00165.48 C
ANISOU 157 CE LYS A1019 21687 17133 24057 -1327 3939 656 C
ATOM 158 NZ LYS A1019 44.716 175.117 118.703 1.00174.34 N
ANISOU 158 NZ LYS A1019 22375 18097 25767 -1271 4146 713 N
ATOM 159 N ALA A1020 44.165 182.068 115.123 1.00146.95 N
ANISOU 159 N ALA A1020 20235 14546 21052 -1929 4155 868 N
ATOM 160 CA ALA A1020 44.313 182.966 113.969 1.00149.77 C
ANISOU 160 CA ALA A1020 20939 14785 21182 -2101 4379 884 C
ATOM 161 C ALA A1020 45.723 183.589 113.874 1.00157.64 C
ANISOU 161 C ALA A1020 21683 15610 22602 -2156 4690 946 C
ATOM 162 O ALA A1020 46.409 183.709 114.896 1.00157.05 O
ANISOU 162 O ALA A1020 21148 15549 22975 -2059 4560 1006 O
ATOM 163 CB ALA A1020 43.254 184.058 114.019 1.00148.73 C
ANISOU 163 CB ALA A1020 21035 14786 20690 -2132 3946 927 C
ATOM 164 N ASP A1021 46.161 183.951 112.642 1.00157.37 N
ANISOU 164 N ASP A1021 21962 15400 22432 -2326 5104 935 N
ATOM 165 CA ASP A1021 47.483 184.537 112.396 1.00159.97 C
ANISOU 165 CA ASP A1021 22088 15540 23153 -2399 5461 991 C
ATOM 166 C ASP A1021 47.435 185.993 111.894 1.00165.05 C
ANISOU 166 C ASP A1021 22968 16158 23586 -2539 5384 1057 C
ATOM 167 O ASP A1021 48.421 186.715 112.076 1.00166.37 O
ANISOU 167 O ASP A1021 22869 16224 24118 -2570 5501 1131 O
ATOM 168 CB ASP A1021 48.329 183.649 111.464 1.00165.06 C
ANISOU 168 CB ASP A1021 22813 15946 23957 -2474 6130 923 C
ATOM 169 CG ASP A1021 49.070 182.531 112.182 1.00173.72 C
ANISOU 169 CG ASP A1021 23429 16991 25586 -2324 6275 912 C
ATOM 170 OD1 ASP A1021 50.298 182.668 112.390 1.00176.25 O
ANISOU 170 OD1 ASP A1021 23343 17156 26467 -2309 6521 976 O
ATOM 171 OD2 ASP A1021 48.427 181.510 112.519 1.00175.84 O1-
ANISOU 171 OD2 ASP A1021 23718 17364 25729 -2225 6131 849 O1-
ATOM 172 N ASN A1022 46.299 186.436 111.296 1.00160.70 N
ANISOU 172 N ASN A1022 22894 15688 22476 -2624 5160 1043 N
ATOM 173 CA ASN A1022 46.160 187.812 110.797 1.00161.17 C
ANISOU 173 CA ASN A1022 23208 15719 22312 -2758 5051 1112 C
ATOM 174 C ASN A1022 44.936 188.556 111.356 1.00161.90 C
ANISOU 174 C ASN A1022 23385 16011 22120 -2697 4438 1155 C
ATOM 175 O ASN A1022 43.979 187.929 111.819 1.00158.87 O
ANISOU 175 O ASN A1022 23008 15777 21579 -2589 4144 1116 O
ATOM 176 CB ASN A1022 46.201 187.877 109.259 1.00165.41 C
ANISOU 176 CB ASN A1022 24302 16069 22476 -2983 5471 1080 C
ATOM 177 CG ASN A1022 45.123 187.103 108.537 1.00188.92 C
ANISOU 177 CG ASN A1022 27755 19074 24951 -3044 5435 1008 C
ATOM 178 OD1 ASN A1022 44.151 187.675 108.040 1.00182.86 O
ANISOU 178 OD1 ASN A1022 27385 18358 23736 -3136 5133 1041 O
ATOM 179 ND2 ASN A1022 45.329 185.804 108.360 1.00180.28 N
ANISOU 179 ND2 ASN A1022 26653 17917 23929 -3013 5763 914 N
ATOM 180 N ALA A1023 44.987 189.904 111.301 1.00159.26 N
ANISOU 180 N ALA A1023 23111 15659 21740 -2770 4273 1237 N
ATOM 181 CA ALA A1023 43.966 190.846 111.780 1.00157.08 C
ANISOU 181 CA ALA A1023 22906 15525 21253 -2725 3739 1290 C
ATOM 182 C ALA A1023 42.590 190.771 111.054 1.00161.67 C
ANISOU 182 C ALA A1023 23964 16153 21309 -2790 3524 1280 C
ATOM 183 O ALA A1023 41.613 191.312 111.575 1.00159.70 O
ANISOU 183 O ALA A1023 23713 16028 20937 -2714 3070 1315 O
ATOM 184 CB ALA A1023 44.510 192.271 111.735 1.00158.64 C
ANISOU 184 CB ALA A1023 23076 15647 21552 -2811 3698 1380 C
ATOM 185 N ALA A1024 42.513 190.119 109.870 1.00160.00 N
ANISOU 185 N ALA A1024 24163 15824 20805 -2939 3844 1237 N
ATOM 186 CA ALA A1024 41.269 189.990 109.093 1.00159.19 C
ANISOU 186 CA ALA A1024 24542 15735 20208 -3034 3632 1243 C
ATOM 187 C ALA A1024 40.328 188.964 109.719 1.00158.99 C
ANISOU 187 C ALA A1024 24406 15869 20133 -2883 3370 1188 C
ATOM 188 O ALA A1024 39.127 189.221 109.840 1.00156.78 O
ANISOU 188 O ALA A1024 24263 15682 19624 -2857 2947 1228 O
ATOM 189 CB ALA A1024 41.583 189.613 107.650 1.00163.32 C
ANISOU 189 CB ALA A1024 25574 16056 20423 -3268 4072 1214 C
ATOM 190 N GLN A1025 40.892 187.803 110.111 1.00154.49 N
ANISOU 190 N GLN A1025 23576 15315 19807 -2783 3627 1102 N
ATOM 191 CA GLN A1025 40.197 186.693 110.758 1.00151.80 C
ANISOU 191 CA GLN A1025 23091 15115 19473 -2636 3445 1041 C
ATOM 192 C GLN A1025 39.791 187.149 112.155 1.00151.66 C
ANISOU 192 C GLN A1025 22662 15277 19684 -2441 3006 1074 C
ATOM 193 O GLN A1025 38.653 186.923 112.563 1.00149.54 O
ANISOU 193 O GLN A1025 22407 15138 19275 -2355 2659 1069 O
ATOM 194 CB GLN A1025 41.124 185.467 110.895 1.00154.10 C
ANISOU 194 CB GLN A1025 23169 15347 20034 -2582 3865 953 C
ATOM 195 CG GLN A1025 41.890 185.056 109.642 1.00172.37 C
ANISOU 195 CG GLN A1025 25819 17441 22233 -2765 4426 905 C
ATOM 196 CD GLN A1025 43.091 184.215 110.000 1.00190.20 C
ANISOU 196 CD GLN A1025 27716 19613 24940 -2684 4856 847 C
ATOM 197 OE1 GLN A1025 44.068 184.699 110.586 1.00184.00 O
ANISOU 197 OE1 GLN A1025 26526 18800 24584 -2619 4936 891 O
ATOM 198 NE2 GLN A1025 43.054 182.941 109.642 1.00183.93 N
ANISOU 198 NE2 GLN A1025 27059 18752 24075 -2695 5140 755 N
ATOM 199 N VAL A1026 40.737 187.795 112.879 1.00146.85 N
ANISOU 199 N VAL A1026 21699 14661 19436 -2383 3037 1108 N
ATOM 200 CA VAL A1026 40.564 188.307 114.237 1.00143.70 C
ANISOU 200 CA VAL A1026 20932 14398 19272 -2224 2668 1136 C
ATOM 201 C VAL A1026 39.429 189.340 114.280 1.00146.53 C
ANISOU 201 C VAL A1026 21469 14821 19385 -2226 2258 1192 C
ATOM 202 O VAL A1026 38.531 189.187 115.103 1.00144.85 O
ANISOU 202 O VAL A1026 21142 14739 19153 -2098 1934 1177 O
ATOM 203 CB VAL A1026 41.905 188.806 114.857 1.00148.00 C
ANISOU 203 CB VAL A1026 21108 14882 20245 -2204 2803 1172 C
ATOM 204 CG1 VAL A1026 41.681 189.635 116.117 1.00145.85 C
ANISOU 204 CG1 VAL A1026 20569 14717 20132 -2092 2396 1213 C
ATOM 205 CG2 VAL A1026 42.837 187.638 115.162 1.00148.43 C
ANISOU 205 CG2 VAL A1026 20877 14892 20628 -2148 3106 1127 C
ATOM 206 N LYS A1027 39.434 190.342 113.376 1.00144.21 N
ANISOU 206 N LYS A1027 21459 14421 18911 -2373 2283 1258 N
ATOM 207 CA LYS A1027 38.386 191.373 113.308 1.00143.08 C
ANISOU 207 CA LYS A1027 21495 14305 18564 -2386 1905 1327 C
ATOM 208 C LYS A1027 37.002 190.742 113.072 1.00146.10 C
ANISOU 208 C LYS A1027 22088 14755 18668 -2363 1667 1316 C
ATOM 209 O LYS A1027 36.064 191.066 113.803 1.00144.23 O
ANISOU 209 O LYS A1027 21736 14614 18452 -2246 1308 1335 O
ATOM 210 CB LYS A1027 38.715 192.436 112.235 1.00147.39 C
ANISOU 210 CB LYS A1027 22353 14699 18950 -2575 2013 1406 C
ATOM 211 CG LYS A1027 37.694 193.571 112.105 1.00154.69 C
ANISOU 211 CG LYS A1027 23463 15620 19694 -2598 1621 1496 C
ATOM 212 CD LYS A1027 38.128 194.633 111.095 1.00164.55 C
ANISOU 212 CD LYS A1027 25016 16707 20798 -2793 1735 1581 C
ATOM 213 CE LYS A1027 37.771 194.315 109.659 1.00172.47 C
ANISOU 213 CE LYS A1027 26535 17592 21404 -2998 1848 1611 C
ATOM 214 NZ LYS A1027 38.359 195.306 108.719 1.00181.02 N
ANISOU 214 NZ LYS A1027 27920 18505 22355 -3203 2012 1688 N
ATOM 215 N ASP A1028 36.892 189.824 112.085 1.00143.51 N
ANISOU 215 N ASP A1028 22061 14366 18101 -2477 1880 1284 N
ATOM 216 CA ASP A1028 35.640 189.146 111.747 1.00142.87 C
ANISOU 216 CA ASP A1028 22207 14328 17751 -2486 1665 1282 C
ATOM 217 C ASP A1028 35.081 188.328 112.912 1.00141.65 C
ANISOU 217 C ASP A1028 21718 14337 17765 -2282 1484 1220 C
ATOM 218 O ASP A1028 33.883 188.401 113.172 1.00139.81 O
ANISOU 218 O ASP A1028 21504 14172 17447 -2222 1137 1253 O
ATOM 219 CB ASP A1028 35.797 188.292 110.477 1.00148.28 C
ANISOU 219 CB ASP A1028 23302 14891 18146 -2669 1970 1250 C
ATOM 220 CG ASP A1028 34.674 187.284 110.257 1.00167.96 C
ANISOU 220 CG ASP A1028 25977 17433 20409 -2671 1789 1229 C
ATOM 221 OD1 ASP A1028 33.499 187.715 110.130 1.00169.72 O1-
ANISOU 221 OD1 ASP A1028 26343 17673 20469 -2689 1389 1312 O1-
ATOM 222 OD2 ASP A1028 34.965 186.063 110.241 1.00176.63 O1-
ANISOU 222 OD2 ASP A1028 27052 18540 21518 -2650 2037 1136 O1-
ATOM 223 N ALA A1029 35.949 187.565 113.614 1.00136.03 N
ANISOU 223 N ALA A1029 20700 13673 17313 -2183 1717 1141 N
ATOM 224 CA ALA A1029 35.588 186.748 114.782 1.00132.47 C
ANISOU 224 CA ALA A1029 19930 13366 17036 -2000 1577 1081 C
ATOM 225 C ALA A1029 35.089 187.645 115.926 1.00132.40 C
ANISOU 225 C ALA A1029 19672 13450 17185 -1868 1232 1114 C
ATOM 226 O ALA A1029 34.139 187.281 116.623 1.00130.72 O
ANISOU 226 O ALA A1029 19351 13342 16976 -1751 993 1092 O
ATOM 227 CB ALA A1029 36.784 185.928 115.236 1.00133.16 C
ANISOU 227 CB ALA A1029 19751 13448 17397 -1946 1893 1015 C
ATOM 228 N LEU A1030 35.703 188.835 116.079 1.00127.03 N
ANISOU 228 N LEU A1030 18925 12714 16625 -1896 1222 1164 N
ATOM 229 CA LEU A1030 35.326 189.830 117.074 1.00124.16 C
ANISOU 229 CA LEU A1030 18377 12402 16396 -1796 931 1192 C
ATOM 230 C LEU A1030 34.027 190.532 116.688 1.00125.43 C
ANISOU 230 C LEU A1030 18747 12550 16362 -1810 635 1254 C
ATOM 231 O LEU A1030 33.254 190.890 117.574 1.00123.78 O
ANISOU 231 O LEU A1030 18392 12403 16237 -1688 381 1251 O
ATOM 232 CB LEU A1030 36.454 190.840 117.303 1.00125.01 C
ANISOU 232 CB LEU A1030 18358 12439 16700 -1836 1022 1227 C
ATOM 233 CG LEU A1030 37.621 190.386 118.184 1.00129.43 C
ANISOU 233 CG LEU A1030 18585 13020 17573 -1777 1171 1188 C
ATOM 234 CD1 LEU A1030 38.787 191.334 118.049 1.00131.41 C
ANISOU 234 CD1 LEU A1030 18766 13164 17998 -1865 1307 1241 C
ATOM 235 CD2 LEU A1030 37.214 190.291 119.651 1.00129.57 C
ANISOU 235 CD2 LEU A1030 18352 13145 17732 -1627 911 1152 C
ATOM 236 N THR A1031 33.767 190.699 115.377 1.00122.00 N
ANISOU 236 N THR A1031 18660 12019 15676 -1963 668 1314 N
ATOM 237 CA THR A1031 32.517 191.286 114.873 1.00121.87 C
ANISOU 237 CA THR A1031 18859 11962 15485 -1998 360 1400 C
ATOM 238 C THR A1031 31.357 190.323 115.190 1.00124.61 C
ANISOU 238 C THR A1031 19159 12399 15789 -1904 176 1372 C
ATOM 239 O THR A1031 30.279 190.771 115.597 1.00124.82 O
ANISOU 239 O THR A1031 19113 12442 15871 -1819 -120 1414 O
ATOM 240 CB THR A1031 32.615 191.547 113.367 1.00130.76 C
ANISOU 240 CB THR A1031 20407 12947 16330 -2217 444 1476 C
ATOM 241 OG1 THR A1031 33.750 192.370 113.123 1.00137.04 O
ANISOU 241 OG1 THR A1031 21221 13658 17188 -2301 650 1496 O
ATOM 242 CG2 THR A1031 31.363 192.205 112.796 1.00127.82 C
ANISOU 242 CG2 THR A1031 20264 12506 15797 -2274 82 1594 C
ATOM 243 N LYS A1032 31.602 189.000 115.010 1.00118.32 N
ANISOU 243 N LYS A1032 18392 11645 14918 -1919 372 1300 N
ATOM 244 CA LYS A1032 30.661 187.914 115.261 1.00115.85 C
ANISOU 244 CA LYS A1032 18042 11415 14560 -1846 247 1265 C
ATOM 245 C LYS A1032 30.361 187.842 116.757 1.00115.27 C
ANISOU 245 C LYS A1032 17594 11463 14740 -1643 123 1209 C
ATOM 246 O LYS A1032 29.268 187.422 117.158 1.00114.15 O
ANISOU 246 O LYS A1032 17386 11378 14610 -1559 -81 1209 O
ATOM 247 CB LYS A1032 31.264 186.583 114.779 1.00118.82 C
ANISOU 247 CB LYS A1032 18521 11795 14829 -1908 544 1188 C
ATOM 248 CG LYS A1032 31.308 186.419 113.267 1.00133.05 C
ANISOU 248 CG LYS A1032 20771 13465 16318 -2126 664 1229 C
ATOM 249 CD LYS A1032 32.182 185.244 112.853 1.00143.26 C
ANISOU 249 CD LYS A1032 22147 14731 17555 -2184 1055 1135 C
ATOM 250 CE LYS A1032 32.006 184.903 111.394 1.00159.10 C
ANISOU 250 CE LYS A1032 24654 16596 19201 -2411 1169 1161 C
ATOM 251 NZ LYS A1032 32.619 183.595 111.044 1.00169.35 N
ANISOU 251 NZ LYS A1032 26039 17862 20442 -2450 1533 1056 N
ATOM 252 N MET A1033 31.348 188.250 117.574 1.00108.96 N
ANISOU 252 N MET A1033 16566 10689 14145 -1580 250 1167 N
ATOM 253 CA MET A1033 31.250 188.271 119.020 1.00106.11 C
ANISOU 253 CA MET A1033 15897 10419 14002 -1419 154 1113 C
ATOM 254 C MET A1033 30.353 189.400 119.464 1.00108.90 C
ANISOU 254 C MET A1033 16215 10746 14416 -1357 -108 1160 C
ATOM 255 O MET A1033 29.339 189.131 120.091 1.00107.75 O
ANISOU 255 O MET A1033 15961 10654 14327 -1248 -263 1137 O
ATOM 256 CB MET A1033 32.637 188.344 119.671 1.00108.11 C
ANISOU 256 CB MET A1033 15951 10678 14447 -1405 344 1071 C
ATOM 257 CG MET A1033 33.150 186.983 120.111 1.00110.76 C
ANISOU 257 CG MET A1033 16132 11086 14867 -1352 500 997 C
ATOM 258 SD MET A1033 34.950 186.835 120.281 1.00115.48 S
ANISOU 258 SD MET A1033 16552 11633 15692 -1395 786 984 S
ATOM 259 CE MET A1033 35.235 187.775 121.765 1.00110.99 C
ANISOU 259 CE MET A1033 15735 11087 15349 -1314 586 990 C
ATOM 260 N ARG A1034 30.677 190.649 119.083 1.00106.18 N
ANISOU 260 N ARG A1034 15969 10306 14068 -1428 -143 1228 N
ATOM 261 CA ARG A1034 29.921 191.864 119.431 1.00105.47 C
ANISOU 261 CA ARG A1034 15856 10158 14059 -1376 -371 1280 C
ATOM 262 C ARG A1034 28.403 191.767 119.223 1.00108.15 C
ANISOU 262 C ARG A1034 16247 10481 14363 -1330 -609 1330 C
ATOM 263 O ARG A1034 27.670 192.219 120.095 1.00106.62 O
ANISOU 263 O ARG A1034 15901 10283 14324 -1210 -747 1318 O
ATOM 264 CB ARG A1034 30.476 193.088 118.695 1.00105.50 C
ANISOU 264 CB ARG A1034 16016 10045 14024 -1492 -362 1361 C
ATOM 265 CG ARG A1034 29.989 194.408 119.263 1.00106.87 C
ANISOU 265 CG ARG A1034 16122 10151 14335 -1426 -551 1398 C
ATOM 266 CD ARG A1034 30.408 195.562 118.384 1.00110.62 C
ANISOU 266 CD ARG A1034 16782 10500 14747 -1553 -564 1493 C
ATOM 267 NE ARG A1034 30.272 196.827 119.099 1.00118.21 N
ANISOU 267 NE ARG A1034 17648 11395 15873 -1486 -689 1506 N
ATOM 268 CZ ARG A1034 29.189 197.592 119.062 1.00130.67 C
ANISOU 268 CZ ARG A1034 19254 12886 17509 -1436 -914 1572 C
ATOM 269 NH1 ARG A1034 28.148 197.248 118.316 1.00118.11 N
ANISOU 269 NH1 ARG A1034 17778 11265 15834 -1454 -1072 1647 N
ATOM 270 NH2 ARG A1034 29.143 198.715 119.765 1.00114.80 N
ANISOU 270 NH2 ARG A1034 17160 10802 15657 -1373 -988 1569 N
ATOM 271 N ALA A1035 27.937 191.187 118.092 1.00105.58 N
ANISOU 271 N ALA A1035 16138 10128 13847 -1433 -651 1388 N
ATOM 272 CA ALA A1035 26.501 191.045 117.814 1.00105.69 C
ANISOU 272 CA ALA A1035 16197 10109 13849 -1411 -909 1459 C
ATOM 273 C ALA A1035 25.857 190.046 118.764 1.00109.49 C
ANISOU 273 C ALA A1035 16457 10699 14443 -1269 -921 1377 C
ATOM 274 O ALA A1035 24.706 190.255 119.151 1.00109.78 O
ANISOU 274 O ALA A1035 16384 10708 14620 -1178 -1114 1412 O
ATOM 275 CB ALA A1035 26.259 190.631 116.372 1.00107.72 C
ANISOU 275 CB ALA A1035 16778 10301 13850 -1586 -960 1543 C
ATOM 276 N ALA A1036 26.606 188.981 119.159 1.00104.60 N
ANISOU 276 N ALA A1036 15764 10189 13790 -1248 -704 1272 N
ATOM 277 CA ALA A1036 26.147 187.940 120.082 1.00102.73 C
ANISOU 277 CA ALA A1036 15335 10060 13639 -1127 -686 1187 C
ATOM 278 C ALA A1036 25.991 188.506 121.494 1.00105.92 C
ANISOU 278 C ALA A1036 15502 10487 14257 -983 -712 1129 C
ATOM 279 O ALA A1036 25.022 188.182 122.177 1.00104.29 O
ANISOU 279 O ALA A1036 15167 10307 14153 -880 -797 1104 O
ATOM 280 CB ALA A1036 27.114 186.762 120.079 1.00102.76 C
ANISOU 280 CB ALA A1036 15335 10147 13563 -1156 -448 1103 C
ATOM 281 N ALA A1037 26.928 189.381 121.908 1.00104.07 N
ANISOU 281 N ALA A1037 15230 10225 14088 -988 -633 1110 N
ATOM 282 CA ALA A1037 26.923 190.068 123.203 1.00103.85 C
ANISOU 282 CA ALA A1037 15041 10189 14229 -886 -651 1056 C
ATOM 283 C ALA A1037 25.770 191.063 123.242 1.00109.84 C
ANISOU 283 C ALA A1037 15795 10844 15095 -829 -828 1114 C
ATOM 284 O ALA A1037 25.120 191.223 124.279 1.00109.26 O
ANISOU 284 O ALA A1037 15592 10760 15160 -717 -853 1061 O
ATOM 285 CB ALA A1037 28.242 190.797 123.413 1.00104.67 C
ANISOU 285 CB ALA A1037 15146 10264 14361 -941 -551 1046 C
ATOM 286 N LEU A1038 25.496 191.705 122.093 1.00108.44 N
ANISOU 286 N LEU A1038 15769 10573 14860 -912 -945 1227 N
ATOM 287 CA LEU A1038 24.407 192.666 121.959 1.00109.75 C
ANISOU 287 CA LEU A1038 15928 10613 15160 -870 -1139 1312 C
ATOM 288 C LEU A1038 23.080 191.961 121.943 1.00116.39 C
ANISOU 288 C LEU A1038 16696 11455 16072 -809 -1266 1342 C
ATOM 289 O LEU A1038 22.102 192.484 122.482 1.00116.85 O
ANISOU 289 O LEU A1038 16628 11426 16344 -708 -1366 1365 O
ATOM 290 CB LEU A1038 24.582 193.548 120.720 1.00110.90 C
ANISOU 290 CB LEU A1038 16275 10646 15215 -997 -1250 1440 C
ATOM 291 CG LEU A1038 25.648 194.622 120.850 1.00114.59 C
ANISOU 291 CG LEU A1038 16783 11067 15691 -1039 -1163 1431 C
ATOM 292 CD1 LEU A1038 26.034 195.154 119.515 1.00115.92 C
ANISOU 292 CD1 LEU A1038 17191 11152 15702 -1198 -1213 1544 C
ATOM 293 CD2 LEU A1038 25.229 195.713 121.816 1.00116.83 C
ANISOU 293 CD2 LEU A1038 16936 11258 16195 -925 -1222 1412 C
ATOM 294 N ASP A1039 23.062 190.750 121.360 1.00114.37 N
ANISOU 294 N ASP A1039 16511 11285 15658 -870 -1246 1341 N
ATOM 295 CA ASP A1039 21.887 189.893 121.295 1.00114.82 C
ANISOU 295 CA ASP A1039 16505 11355 15766 -832 -1366 1370 C
ATOM 296 C ASP A1039 21.600 189.363 122.696 1.00114.98 C
ANISOU 296 C ASP A1039 16301 11452 15935 -685 -1247 1248 C
ATOM 297 O ASP A1039 20.472 189.494 123.166 1.00115.05 O
ANISOU 297 O ASP A1039 16166 11399 16148 -590 -1336 1268 O
ATOM 298 CB ASP A1039 22.102 188.734 120.298 1.00117.74 C
ANISOU 298 CB ASP A1039 17054 11787 15893 -957 -1357 1390 C
ATOM 299 CG ASP A1039 20.822 188.125 119.751 1.00138.33 C
ANISOU 299 CG ASP A1039 19677 14355 18527 -978 -1575 1481 C
ATOM 300 OD1 ASP A1039 20.054 187.522 120.550 1.00139.71 O
ANISOU 300 OD1 ASP A1039 19649 14572 18861 -863 -1581 1435 O
ATOM 301 OD2 ASP A1039 20.608 188.204 118.518 1.00148.47 O1-
ANISOU 301 OD2 ASP A1039 21191 15557 19664 -1124 -1742 1600 O1-
ATOM 302 N ALA A1040 22.635 188.840 123.385 1.00108.26 N
ANISOU 302 N ALA A1040 15421 10712 15001 -672 -1046 1130 N
ATOM 303 CA ALA A1040 22.525 188.278 124.730 1.00106.29 C
ANISOU 303 CA ALA A1040 15009 10534 14843 -562 -930 1013 C
ATOM 304 C ALA A1040 22.013 189.280 125.766 1.00109.11 C
ANISOU 304 C ALA A1040 15256 10798 15401 -457 -923 977 C
ATOM 305 O ALA A1040 21.424 188.880 126.769 1.00108.07 O
ANISOU 305 O ALA A1040 15010 10683 15368 -367 -854 900 O
ATOM 306 CB ALA A1040 23.853 187.686 125.162 1.00105.80 C
ANISOU 306 CB ALA A1040 14958 10580 14662 -595 -760 924 C
ATOM 307 N GLN A1041 22.208 190.577 125.495 1.00105.96 N
ANISOU 307 N GLN A1041 14910 10288 15061 -477 -981 1030 N
ATOM 308 CA GLN A1041 21.770 191.695 126.333 1.00105.96 C
ANISOU 308 CA GLN A1041 14839 10165 15254 -389 -964 1001 C
ATOM 309 C GLN A1041 20.237 191.845 126.277 1.00111.42 C
ANISOU 309 C GLN A1041 15413 10743 16179 -301 -1066 1064 C
ATOM 310 O GLN A1041 19.610 192.234 127.266 1.00109.57 O
ANISOU 310 O GLN A1041 15073 10423 16134 -197 -979 1002 O
ATOM 311 CB GLN A1041 22.455 192.964 125.834 1.00107.41 C
ANISOU 311 CB GLN A1041 15128 10261 15421 -453 -1010 1057 C
ATOM 312 CG GLN A1041 22.500 194.099 126.825 1.00105.32 C
ANISOU 312 CG GLN A1041 14838 9884 15294 -390 -944 995 C
ATOM 313 CD GLN A1041 23.258 195.233 126.208 1.00115.53 C
ANISOU 313 CD GLN A1041 16244 11103 16549 -471 -1003 1062 C
ATOM 314 OE1 GLN A1041 23.030 195.620 125.051 1.00109.35 O
ANISOU 314 OE1 GLN A1041 15527 10259 15760 -526 -1143 1187 O
ATOM 315 NE2 GLN A1041 24.216 195.751 126.945 1.00106.17 N
ANISOU 315 NE2 GLN A1041 15102 9918 15321 -499 -909 988 N
ATOM 316 N LYS A1042 19.649 191.518 125.112 1.00112.03 N
ANISOU 316 N LYS A1042 15515 10803 16247 -355 -1247 1192 N
ATOM 317 CA LYS A1042 18.205 191.552 124.850 1.00114.86 C
ANISOU 317 CA LYS A1042 15746 11045 16851 -296 -1401 1292 C
ATOM 318 C LYS A1042 17.506 190.360 125.529 1.00120.88 C
ANISOU 318 C LYS A1042 16365 11881 17681 -223 -1318 1223 C
ATOM 319 O LYS A1042 16.317 190.435 125.845 1.00122.08 O
ANISOU 319 O LYS A1042 16345 11925 18116 -130 -1347 1255 O
ATOM 320 CB LYS A1042 17.926 191.553 123.327 1.00118.58 C
ANISOU 320 CB LYS A1042 16341 11470 17245 -417 -1663 1464 C
ATOM 321 CG LYS A1042 18.220 192.882 122.626 1.00125.32 C
ANISOU 321 CG LYS A1042 17314 12195 18105 -480 -1787 1567 C
ATOM 322 CD LYS A1042 18.398 192.700 121.124 1.00132.22 C
ANISOU 322 CD LYS A1042 18413 13059 18764 -652 -1994 1708 C
ATOM 323 CE LYS A1042 18.891 193.956 120.446 1.00148.33 C
ANISOU 323 CE LYS A1042 20611 14985 20762 -735 -2090 1800 C
ATOM 324 NZ LYS A1042 20.294 194.303 120.824 1.00157.22 N
ANISOU 324 NZ LYS A1042 21833 16198 21706 -765 -1862 1686 N
ATOM 325 N ALA A1043 18.256 189.273 125.765 1.00117.38 N
ANISOU 325 N ALA A1043 15984 11609 17004 -264 -1204 1132 N
ATOM 326 CA ALA A1043 17.765 188.062 126.410 1.00117.02 C
ANISOU 326 CA ALA A1043 15835 11652 16975 -212 -1114 1060 C
ATOM 327 C ALA A1043 17.383 188.325 127.852 1.00122.64 C
ANISOU 327 C ALA A1043 16426 12316 17857 -94 -923 943 C
ATOM 328 O ALA A1043 17.835 189.296 128.460 1.00122.37 O
ANISOU 328 O ALA A1043 16433 12221 17843 -71 -826 884 O
ATOM 329 CB ALA A1043 18.819 186.964 126.343 1.00116.01 C
ANISOU 329 CB ALA A1043 15816 11699 16564 -287 -1027 990 C
ATOM 330 N THR A1044 16.501 187.483 128.373 1.00120.83 N
ANISOU 330 N THR A1044 16065 12095 17751 -30 -867 913 N
ATOM 331 CA THR A1044 16.062 187.539 129.753 1.00121.23 C
ANISOU 331 CA THR A1044 16029 12092 17940 68 -651 794 C
ATOM 332 C THR A1044 16.444 186.183 130.317 1.00122.29 C
ANISOU 332 C THR A1044 16195 12390 17880 45 -545 699 C
ATOM 333 O THR A1044 15.896 185.157 129.900 1.00121.20 O
ANISOU 333 O THR A1044 15990 12314 17747 35 -614 741 O
ATOM 334 CB THR A1044 14.573 187.904 129.866 1.00138.35 C
ANISOU 334 CB THR A1044 17997 14085 20485 166 -656 855 C
ATOM 335 OG1 THR A1044 14.339 189.111 129.135 1.00142.29 O
ANISOU 335 OG1 THR A1044 18473 14435 21156 170 -812 973 O
ATOM 336 CG2 THR A1044 14.123 188.089 131.321 1.00139.48 C
ANISOU 336 CG2 THR A1044 18084 14134 20778 261 -374 719 C
ATOM 337 N PRO A1045 17.460 186.146 131.193 1.00117.54 N
ANISOU 337 N PRO A1045 15707 11855 17097 22 -407 583 N
ATOM 338 CA PRO A1045 17.888 184.853 131.747 1.00116.09 C
ANISOU 338 CA PRO A1045 15556 11813 16738 -5 -328 505 C
ATOM 339 C PRO A1045 16.771 184.170 132.544 1.00121.35 C
ANISOU 339 C PRO A1045 16116 12448 17542 64 -207 456 C
ATOM 340 O PRO A1045 15.847 184.873 132.977 1.00122.58 O
ANISOU 340 O PRO A1045 16190 12454 17932 138 -120 448 O
ATOM 341 CB PRO A1045 19.092 185.220 132.625 1.00117.25 C
ANISOU 341 CB PRO A1045 15840 11983 16729 -47 -235 412 C
ATOM 342 CG PRO A1045 18.937 186.657 132.920 1.00122.93 C
ANISOU 342 CG PRO A1045 16587 12547 17574 -15 -198 403 C
ATOM 343 CD PRO A1045 18.235 187.269 131.757 1.00119.32 C
ANISOU 343 CD PRO A1045 16040 12013 17284 11 -337 527 C
ATOM 344 N PRO A1046 16.791 182.817 132.727 1.00117.15 N
ANISOU 344 N PRO A1046 15575 12040 16898 43 -186 426 N
ATOM 345 CA PRO A1046 15.718 182.183 133.526 1.00116.90 C
ANISOU 345 CA PRO A1046 15446 11968 17002 102 -53 378 C
ATOM 346 C PRO A1046 15.817 182.620 134.996 1.00120.43 C
ANISOU 346 C PRO A1046 15987 12334 17437 123 171 249 C
ATOM 347 O PRO A1046 14.806 182.903 135.640 1.00121.83 O
ANISOU 347 O PRO A1046 16093 12378 17818 189 331 212 O
ATOM 348 CB PRO A1046 15.963 180.685 133.331 1.00117.35 C
ANISOU 348 CB PRO A1046 15511 12183 16895 57 -96 375 C
ATOM 349 CG PRO A1046 17.421 180.567 132.988 1.00121.00 C
ANISOU 349 CG PRO A1046 16107 12755 17114 -19 -165 368 C
ATOM 350 CD PRO A1046 17.809 181.830 132.285 1.00117.22 C
ANISOU 350 CD PRO A1046 15661 12208 16668 -33 -254 428 C
ATOM 351 N LYS A1047 17.074 182.779 135.468 1.00114.71 N
ANISOU 351 N LYS A1047 15433 11666 16485 57 176 189 N
ATOM 352 CA LYS A1047 17.554 183.205 136.780 1.00113.95 C
ANISOU 352 CA LYS A1047 15508 11503 16285 27 324 76 C
ATOM 353 C LYS A1047 16.948 184.542 137.234 1.00120.05 C
ANISOU 353 C LYS A1047 16303 12077 17234 79 460 39 C
ATOM 354 O LYS A1047 16.999 184.847 138.427 1.00120.42 O
ANISOU 354 O LYS A1047 16509 12026 17218 56 635 -69 O
ATOM 355 CB LYS A1047 19.082 183.328 136.679 1.00114.31 C
ANISOU 355 CB LYS A1047 15681 11637 16115 -64 202 81 C
ATOM 356 CG LYS A1047 19.849 183.126 137.959 1.00114.86 C
ANISOU 356 CG LYS A1047 15941 11697 16003 -140 266 -10 C
ATOM 357 CD LYS A1047 21.296 182.813 137.639 1.00112.54 C
ANISOU 357 CD LYS A1047 15690 11512 15559 -225 106 31 C
ATOM 358 CE LYS A1047 22.207 183.078 138.810 1.00113.96 C
ANISOU 358 CE LYS A1047 16070 11637 15592 -321 102 -30 C
ATOM 359 NZ LYS A1047 23.201 181.985 139.007 1.00114.11 N
ANISOU 359 NZ LYS A1047 16098 11766 15491 -396 -15 -2 N
ATOM 360 N LEU A1048 16.402 185.344 136.276 1.00118.35 N
ANISOU 360 N LEU A1048 15949 11787 17234 138 376 131 N
ATOM 361 CA LEU A1048 15.809 186.681 136.494 1.00120.02 C
ANISOU 361 CA LEU A1048 16144 11792 17666 200 482 119 C
ATOM 362 C LEU A1048 14.430 186.847 135.814 1.00129.61 C
ANISOU 362 C LEU A1048 17112 12895 19240 300 467 214 C
ATOM 363 O LEU A1048 14.123 187.928 135.304 1.00130.11 O
ANISOU 363 O LEU A1048 17106 12824 19504 344 414 279 O
ATOM 364 CB LEU A1048 16.781 187.792 136.013 1.00118.73 C
ANISOU 364 CB LEU A1048 16080 11613 17420 155 352 154 C
ATOM 365 CG LEU A1048 18.178 187.832 136.616 1.00120.27 C
ANISOU 365 CG LEU A1048 16492 11880 17324 50 336 84 C
ATOM 366 CD1 LEU A1048 19.084 188.703 135.804 1.00119.14 C
ANISOU 366 CD1 LEU A1048 16385 11749 17133 5 172 154 C
ATOM 367 CD2 LEU A1048 18.146 188.291 138.064 1.00122.91 C
ANISOU 367 CD2 LEU A1048 17018 12075 17608 30 554 -54 C
ATOM 368 N GLU A1049 13.603 185.782 135.816 1.00130.33 N
ANISOU 368 N GLU A1049 17064 13026 19430 330 499 232 N
ATOM 369 CA GLU A1049 12.262 185.790 135.217 1.00133.57 C
ANISOU 369 CA GLU A1049 17214 13324 20211 413 460 338 C
ATOM 370 C GLU A1049 11.256 186.696 135.958 1.00144.48 C
ANISOU 370 C GLU A1049 18502 14448 21946 512 718 292 C
ATOM 371 O GLU A1049 10.428 187.346 135.310 1.00146.49 O
ANISOU 371 O GLU A1049 18554 14554 22553 581 636 405 O
ATOM 372 CB GLU A1049 11.715 184.364 135.067 1.00134.32 C
ANISOU 372 CB GLU A1049 17195 13530 20309 404 425 367 C
ATOM 373 CG GLU A1049 12.172 183.692 133.781 1.00144.99 C
ANISOU 373 CG GLU A1049 18544 15057 21489 332 118 481 C
ATOM 374 CD GLU A1049 11.737 182.253 133.564 1.00171.37 C
ANISOU 374 CD GLU A1049 21808 18515 24792 308 63 507 C
ATOM 375 OE1 GLU A1049 11.657 181.486 134.551 1.00172.89 O
ANISOU 375 OE1 GLU A1049 22034 18743 24912 312 260 402 O
ATOM 376 OE2 GLU A1049 11.528 181.878 132.388 1.00166.27 O1-
ANISOU 376 OE2 GLU A1049 21098 17922 24157 268 -186 633 O1-
ATOM 377 N ASP A1050 11.345 186.751 137.306 1.00143.35 N
ANISOU 377 N ASP A1050 18522 14236 21711 508 1029 129 N
ATOM 378 CA ASP A1050 10.466 187.551 138.175 1.00146.08 C
ANISOU 378 CA ASP A1050 18834 14317 22352 590 1357 49 C
ATOM 379 C ASP A1050 10.817 189.054 138.229 1.00152.42 C
ANISOU 379 C ASP A1050 19740 14959 23215 609 1397 26 C
ATOM 380 O ASP A1050 10.030 189.848 138.753 1.00154.35 O
ANISOU 380 O ASP A1050 19927 14952 23767 690 1658 -21 O
ATOM 381 CB ASP A1050 10.408 186.948 139.594 1.00147.91 C
ANISOU 381 CB ASP A1050 19257 14523 22421 553 1691 -121 C
ATOM 382 CG ASP A1050 11.715 186.377 140.118 1.00152.73 C
ANISOU 382 CG ASP A1050 20176 15322 22533 423 1625 -208 C
ATOM 383 OD1 ASP A1050 12.791 186.908 139.748 1.00150.64 O
ANISOU 383 OD1 ASP A1050 20038 15140 22056 365 1424 -186 O
ATOM 384 OD2 ASP A1050 11.662 185.409 140.911 1.00158.60 O1-
ANISOU 384 OD2 ASP A1050 21029 16116 23117 375 1772 -292 O1-
ATOM 385 N LYS A1051 11.993 189.442 137.697 1.00148.48 N
ANISOU 385 N LYS A1051 19388 14587 22440 534 1158 58 N
ATOM 386 CA LYS A1051 12.432 190.843 137.682 1.00149.22 C
ANISOU 386 CA LYS A1051 19592 14544 22562 538 1162 45 C
ATOM 387 C LYS A1051 11.837 191.567 136.490 1.00155.85 C
ANISOU 387 C LYS A1051 20187 15288 23743 613 957 214 C
ATOM 388 O LYS A1051 11.711 190.981 135.409 1.00154.60 O
ANISOU 388 O LYS A1051 19875 15257 23608 601 683 356 O
ATOM 389 CB LYS A1051 13.978 190.984 137.634 1.00148.59 C
ANISOU 389 CB LYS A1051 19767 14627 22064 415 995 16 C
ATOM 390 CG LYS A1051 14.781 190.045 138.533 1.00154.41 C
ANISOU 390 CG LYS A1051 20723 15516 22430 312 1055 -95 C
ATOM 391 CD LYS A1051 14.608 190.303 140.025 1.00161.03 C
ANISOU 391 CD LYS A1051 21792 16193 23199 287 1382 -265 C
ATOM 392 CE LYS A1051 15.111 189.125 140.818 1.00164.90 C
ANISOU 392 CE LYS A1051 22453 16828 23372 189 1409 -340 C
ATOM 393 NZ LYS A1051 14.121 188.680 141.834 1.00171.73 N
ANISOU 393 NZ LYS A1051 23378 17559 24313 211 1744 -453 N
ATOM 394 N SER A1052 11.491 192.851 136.688 1.00155.52 N
ANISOU 394 N SER A1052 20132 15004 23953 679 1082 202 N
ATOM 395 CA SER A1052 11.000 193.749 135.643 1.00156.85 C
ANISOU 395 CA SER A1052 20098 15042 24456 744 879 367 C
ATOM 396 C SER A1052 12.243 194.237 134.831 1.00158.64 C
ANISOU 396 C SER A1052 20491 15410 24377 646 588 431 C
ATOM 397 O SER A1052 13.343 194.215 135.391 1.00156.51 O
ANISOU 397 O SER A1052 20476 15250 23740 557 642 317 O
ATOM 398 CB SER A1052 10.260 194.931 136.269 1.00163.72 C
ANISOU 398 CB SER A1052 20913 15586 25706 850 1157 314 C
ATOM 399 OG SER A1052 11.100 195.750 137.068 1.00173.32 O
ANISOU 399 OG SER A1052 22429 16739 26685 800 1323 170 O
ATOM 400 N PRO A1053 12.138 194.659 133.538 1.00155.18 N
ANISOU 400 N PRO A1053 19928 14964 24070 644 276 614 N
ATOM 401 CA PRO A1053 13.354 195.114 132.818 1.00153.21 C
ANISOU 401 CA PRO A1053 19859 14838 23517 539 49 662 C
ATOM 402 C PRO A1053 14.068 196.279 133.503 1.00155.35 C
ANISOU 402 C PRO A1053 20330 14996 23699 524 197 554 C
ATOM 403 O PRO A1053 15.295 196.335 133.479 1.00153.35 O
ANISOU 403 O PRO A1053 20279 14882 23104 420 125 515 O
ATOM 404 CB PRO A1053 12.842 195.526 131.434 1.00156.31 C
ANISOU 404 CB PRO A1053 20092 15163 24135 547 -266 877 C
ATOM 405 CG PRO A1053 11.485 194.961 131.319 1.00162.40 C
ANISOU 405 CG PRO A1053 20594 15842 25270 631 -274 958 C
ATOM 406 CD PRO A1053 10.933 194.754 132.687 1.00158.70 C
ANISOU 406 CD PRO A1053 20080 15272 24948 721 108 793 C
ATOM 407 N ASP A1054 13.291 197.172 134.153 1.00152.36 N
ANISOU 407 N ASP A1054 19893 14351 23645 626 420 503 N
ATOM 408 CA ASP A1054 13.763 198.336 134.896 1.00152.11 C
ANISOU 408 CA ASP A1054 20057 14158 23578 620 600 390 C
ATOM 409 C ASP A1054 14.586 197.952 136.128 1.00153.11 C
ANISOU 409 C ASP A1054 20465 14369 23340 535 814 194 C
ATOM 410 O ASP A1054 15.452 198.727 136.526 1.00152.46 O
ANISOU 410 O ASP A1054 20613 14241 23074 466 847 120 O
ATOM 411 CB ASP A1054 12.573 199.213 135.306 1.00156.86 C
ANISOU 411 CB ASP A1054 20508 14431 24660 759 828 379 C
ATOM 412 N SER A1055 14.330 196.754 136.712 1.00148.31 N
ANISOU 412 N SER A1055 19849 13876 22625 527 934 122 N
ATOM 413 CA SER A1055 14.983 196.201 137.912 1.00147.15 C
ANISOU 413 CA SER A1055 19967 13803 22138 436 1114 -47 C
ATOM 414 C SER A1055 16.494 196.427 138.016 1.00149.52 C
ANISOU 414 C SER A1055 20524 14236 22051 293 959 -77 C
ATOM 415 O SER A1055 17.188 196.330 136.997 1.00147.76 O
ANISOU 415 O SER A1055 20239 14177 21726 247 679 42 O
ATOM 416 CB SER A1055 14.704 194.707 138.051 1.00148.55 C
ANISOU 416 CB SER A1055 20065 14159 22220 427 1126 -56 C
ATOM 417 OG SER A1055 13.315 194.440 138.120 1.00158.48 O
ANISOU 417 OG SER A1055 21091 15283 23842 547 1298 -39 O
ATOM 418 N PRO A1056 17.032 196.669 139.246 1.00146.19 N
ANISOU 418 N PRO A1056 20401 13738 21406 207 1137 -231 N
ATOM 419 CA PRO A1056 18.490 196.829 139.394 1.00144.07 C
ANISOU 419 CA PRO A1056 20357 13584 20797 58 961 -245 C
ATOM 420 C PRO A1056 19.225 195.521 139.106 1.00141.55 C
ANISOU 420 C PRO A1056 19995 13543 20243 -16 769 -195 C
ATOM 421 O PRO A1056 20.361 195.565 138.646 1.00139.43 O
ANISOU 421 O PRO A1056 19762 13405 19809 -105 549 -131 O
ATOM 422 CB PRO A1056 18.659 197.273 140.856 1.00147.83 C
ANISOU 422 CB PRO A1056 21172 13884 21111 -24 1201 -418 C
ATOM 423 CG PRO A1056 17.287 197.731 141.293 1.00155.09 C
ANISOU 423 CG PRO A1056 22039 14548 22341 103 1532 -492 C
ATOM 424 CD PRO A1056 16.361 196.813 140.553 1.00150.05 C
ANISOU 424 CD PRO A1056 21058 14015 21940 224 1501 -394 C
ATOM 425 N GLU A1057 18.554 194.364 139.338 1.00134.94 N
ANISOU 425 N GLU A1057 19065 12783 19423 26 863 -218 N
ATOM 426 CA GLU A1057 19.074 193.024 139.054 1.00131.07 C
ANISOU 426 CA GLU A1057 18512 12539 18752 -24 710 -173 C
ATOM 427 C GLU A1057 19.194 192.828 137.529 1.00130.80 C
ANISOU 427 C GLU A1057 18244 12649 18804 11 468 -15 C
ATOM 428 O GLU A1057 20.189 192.274 137.061 1.00127.66 O
ANISOU 428 O GLU A1057 17854 12428 18223 -68 291 38 O
ATOM 429 CB GLU A1057 18.167 191.955 139.685 1.00132.36 C
ANISOU 429 CB GLU A1057 18630 12711 18950 21 894 -237 C
ATOM 430 N MET A1058 18.201 193.340 136.763 1.00127.99 N
ANISOU 430 N MET A1058 17699 12192 18738 118 464 65 N
ATOM 431 CA MET A1058 18.131 193.286 135.297 1.00126.93 C
ANISOU 431 CA MET A1058 17384 12146 18696 139 232 224 C
ATOM 432 C MET A1058 19.108 194.230 134.580 1.00129.62 C
ANISOU 432 C MET A1058 17803 12492 18955 71 62 294 C
ATOM 433 O MET A1058 19.723 193.803 133.601 1.00128.59 O
ANISOU 433 O MET A1058 17638 12513 18709 15 -121 388 O
ATOM 434 CB MET A1058 16.696 193.516 134.787 1.00130.84 C
ANISOU 434 CB MET A1058 17659 12502 19553 261 251 303 C
ATOM 435 CG MET A1058 15.895 192.237 134.577 1.00134.22 C
ANISOU 435 CG MET A1058 17919 13024 20054 302 246 336 C
ATOM 436 SD MET A1058 16.595 190.967 133.472 1.00136.44 S
ANISOU 436 SD MET A1058 18175 13581 20086 215 -9 434 S
ATOM 437 CE MET A1058 16.881 191.920 131.951 1.00133.60 C
ANISOU 437 CE MET A1058 17797 13189 19776 179 -278 600 C
ATOM 438 N LYS A1059 19.238 195.505 135.024 1.00125.51 N
ANISOU 438 N LYS A1059 17395 11796 18498 72 136 250 N
ATOM 439 CA LYS A1059 20.186 196.419 134.378 1.00124.37 C
ANISOU 439 CA LYS A1059 17328 11649 18279 0 -19 317 C
ATOM 440 C LYS A1059 21.645 196.053 134.732 1.00125.26 C
ANISOU 440 C LYS A1059 17594 11906 18094 -133 -79 275 C
ATOM 441 O LYS A1059 22.526 196.221 133.890 1.00123.90 O
ANISOU 441 O LYS A1059 17422 11817 17836 -204 -234 360 O
ATOM 442 CB LYS A1059 19.852 197.908 134.625 1.00128.60 C
ANISOU 442 CB LYS A1059 17923 11942 18998 43 58 298 C
ATOM 443 CG LYS A1059 20.677 198.912 133.780 1.00138.15 C
ANISOU 443 CG LYS A1059 19184 13133 20173 -23 -119 393 C
ATOM 444 CD LYS A1059 20.709 198.635 132.244 1.00145.23 C
ANISOU 444 CD LYS A1059 19951 14142 21087 -38 -347 563 C
ATOM 445 CE LYS A1059 19.662 199.409 131.466 1.00155.97 C
ANISOU 445 CE LYS A1059 21183 15334 22746 50 -426 679 C
ATOM 446 NZ LYS A1059 19.729 199.154 129.999 1.00158.83 N
ANISOU 446 NZ LYS A1059 21488 15785 23074 -2 -668 847 N
ATOM 447 N ASP A1060 21.878 195.483 135.938 1.00121.13 N
ANISOU 447 N ASP A1060 17191 11403 17428 -172 39 155 N
ATOM 448 CA ASP A1060 23.185 194.981 136.394 1.00120.31 C
ANISOU 448 CA ASP A1060 17209 11420 17082 -300 -39 128 C
ATOM 449 C ASP A1060 23.647 193.831 135.454 1.00119.68 C
ANISOU 449 C ASP A1060 16982 11557 16932 -319 -171 219 C
ATOM 450 O ASP A1060 24.850 193.641 135.250 1.00118.56 O
ANISOU 450 O ASP A1060 16867 11510 16672 -415 -280 256 O
ATOM 451 CB ASP A1060 23.066 194.467 137.844 1.00123.94 C
ANISOU 451 CB ASP A1060 17833 11838 17420 -335 103 -5 C
ATOM 452 CG ASP A1060 24.371 194.196 138.574 1.00142.92 C
ANISOU 452 CG ASP A1060 20409 14295 19601 -485 3 -34 C
ATOM 453 OD1 ASP A1060 24.807 193.014 138.599 1.00143.28 O
ANISOU 453 OD1 ASP A1060 20397 14498 19546 -523 -74 -9 O
ATOM 454 OD2 ASP A1060 24.904 195.141 139.208 1.00152.53 O1-
ANISOU 454 OD2 ASP A1060 21825 15375 20754 -568 1 -82 O1-
ATOM 455 N PHE A1061 22.675 193.085 134.879 1.00113.26 N
ANISOU 455 N PHE A1061 16015 10803 16216 -231 -152 257 N
ATOM 456 CA PHE A1061 22.892 192.004 133.919 1.00110.58 C
ANISOU 456 CA PHE A1061 15557 10639 15819 -243 -253 337 C
ATOM 457 C PHE A1061 23.276 192.594 132.554 1.00113.03 C
ANISOU 457 C PHE A1061 15830 10959 16155 -274 -389 458 C
ATOM 458 O PHE A1061 24.269 192.160 131.956 1.00111.86 O
ANISOU 458 O PHE A1061 15688 10925 15889 -353 -458 504 O
ATOM 459 CB PHE A1061 21.629 191.112 133.812 1.00111.83 C
ANISOU 459 CB PHE A1061 15588 10824 16079 -151 -199 339 C
ATOM 460 CG PHE A1061 21.493 190.305 132.539 1.00112.24 C
ANISOU 460 CG PHE A1061 15527 11000 16121 -153 -320 443 C
ATOM 461 CD1 PHE A1061 22.134 189.077 132.401 1.00113.70 C
ANISOU 461 CD1 PHE A1061 15705 11346 16150 -204 -342 439 C
ATOM 462 CD2 PHE A1061 20.722 190.770 131.480 1.00115.04 C
ANISOU 462 CD2 PHE A1061 15799 11288 16622 -115 -419 550 C
ATOM 463 CE1 PHE A1061 22.014 188.333 131.222 1.00113.66 C
ANISOU 463 CE1 PHE A1061 15637 11435 16113 -220 -432 524 C
ATOM 464 CE2 PHE A1061 20.615 190.033 130.297 1.00117.33 C
ANISOU 464 CE2 PHE A1061 16041 11674 16864 -146 -544 646 C
ATOM 465 CZ PHE A1061 21.255 188.814 130.180 1.00113.77 C
ANISOU 465 CZ PHE A1061 15608 11382 16237 -199 -535 625 C
ATOM 466 N ARG A1062 22.467 193.566 132.061 1.00109.49 N
ANISOU 466 N ARG A1062 15348 10377 15876 -215 -416 513 N
ATOM 467 CA ARG A1062 22.654 194.247 130.775 1.00109.31 C
ANISOU 467 CA ARG A1062 15321 10327 15885 -249 -554 637 C
ATOM 468 C ARG A1062 23.951 195.042 130.717 1.00113.21 C
ANISOU 468 C ARG A1062 15927 10809 16279 -347 -585 643 C
ATOM 469 O ARG A1062 24.540 195.140 129.643 1.00111.83 O
ANISOU 469 O ARG A1062 15771 10679 16042 -417 -675 736 O
ATOM 470 CB ARG A1062 21.458 195.143 130.432 1.00110.47 C
ANISOU 470 CB ARG A1062 15402 10302 16272 -163 -590 698 C
ATOM 471 CG ARG A1062 20.195 194.375 130.063 1.00120.25 C
ANISOU 471 CG ARG A1062 16493 11542 17653 -84 -617 745 C
ATOM 472 CD ARG A1062 19.177 195.240 129.354 1.00128.19 C
ANISOU 472 CD ARG A1062 17411 12378 18916 -26 -733 864 C
ATOM 473 NE ARG A1062 18.639 196.287 130.221 1.00142.10 N
ANISOU 473 NE ARG A1062 19151 13939 20903 62 -603 804 N
ATOM 474 CZ ARG A1062 17.478 196.217 130.864 1.00162.90 C
ANISOU 474 CZ ARG A1062 21652 16449 23795 175 -479 768 C
ATOM 475 NH1 ARG A1062 16.708 195.141 130.745 1.00151.26 N
ANISOU 475 NH1 ARG A1062 20040 15040 22392 213 -493 794 N
ATOM 476 NH2 ARG A1062 17.069 197.228 131.617 1.00154.05 N
ANISOU 476 NH2 ARG A1062 20534 15122 22877 248 -326 706 N
ATOM 477 N HIS A1063 24.406 195.582 131.872 1.00111.50 N
ANISOU 477 N HIS A1063 15802 10523 16041 -366 -508 547 N
ATOM 478 CA HIS A1063 25.658 196.332 131.990 1.00112.43 C
ANISOU 478 CA HIS A1063 16021 10615 16081 -469 -549 551 C
ATOM 479 C HIS A1063 26.874 195.453 131.724 1.00112.15 C
ANISOU 479 C HIS A1063 15964 10737 15912 -564 -588 577 C
ATOM 480 O HIS A1063 27.871 195.922 131.180 1.00111.91 O
ANISOU 480 O HIS A1063 15956 10709 15856 -651 -641 637 O
ATOM 481 CB HIS A1063 25.788 197.020 133.355 1.00115.46 C
ANISOU 481 CB HIS A1063 16538 10873 16459 -484 -474 441 C
ATOM 482 CG HIS A1063 27.034 197.849 133.469 1.00120.79 C
ANISOU 482 CG HIS A1063 17315 11506 17075 -601 -546 458 C
ATOM 483 ND1 HIS A1063 27.398 198.756 132.474 1.00123.69 N
ANISOU 483 ND1 HIS A1063 17672 11833 17491 -636 -626 556 N
ATOM 484 CD2 HIS A1063 27.978 197.865 134.440 1.00124.06 C
ANISOU 484 CD2 HIS A1063 17842 11905 17390 -701 -566 400 C
ATOM 485 CE1 HIS A1063 28.542 199.292 132.875 1.00124.19 C
ANISOU 485 CE1 HIS A1063 17823 11864 17501 -747 -674 550 C
ATOM 486 NE2 HIS A1063 28.930 198.795 134.056 1.00124.64 N
ANISOU 486 NE2 HIS A1063 17954 11929 17474 -793 -655 462 N
ATOM 487 N GLY A1064 26.776 194.188 132.108 1.00105.53 N
ANISOU 487 N GLY A1064 15072 10013 15012 -546 -548 534 N
ATOM 488 CA GLY A1064 27.819 193.207 131.861 1.00103.11 C
ANISOU 488 CA GLY A1064 14716 9842 14619 -617 -567 558 C
ATOM 489 C GLY A1064 28.094 193.096 130.380 1.00103.21 C
ANISOU 489 C GLY A1064 14684 9910 14622 -649 -593 660 C
ATOM 490 O GLY A1064 29.252 193.052 129.964 1.00103.14 O
ANISOU 490 O GLY A1064 14665 9936 14589 -736 -594 703 O
ATOM 491 N PHE A1065 27.026 193.123 129.570 1.00 96.88 N
ANISOU 491 N PHE A1065 13868 9091 13849 -590 -615 707 N
ATOM 492 CA PHE A1065 27.140 193.078 128.120 1.00 95.40 C
ANISOU 492 CA PHE A1065 13701 8928 13618 -640 -654 808 C
ATOM 493 C PHE A1065 27.703 194.362 127.575 1.00 99.18 C
ANISOU 493 C PHE A1065 14257 9308 14118 -707 -697 873 C
ATOM 494 O PHE A1065 28.383 194.309 126.553 1.00 99.81 O
ANISOU 494 O PHE A1065 14384 9412 14129 -794 -687 942 O
ATOM 495 CB PHE A1065 25.827 192.671 127.452 1.00 96.71 C
ANISOU 495 CB PHE A1065 13846 9094 13806 -580 -712 854 C
ATOM 496 CG PHE A1065 25.524 191.251 127.808 1.00 96.64 C
ANISOU 496 CG PHE A1065 13766 9201 13752 -541 -660 800 C
ATOM 497 CD1 PHE A1065 24.695 190.952 128.883 1.00 99.82 C
ANISOU 497 CD1 PHE A1065 14101 9594 14233 -447 -626 725 C
ATOM 498 CD2 PHE A1065 26.182 190.206 127.169 1.00 98.17 C
ANISOU 498 CD2 PHE A1065 13968 9504 13828 -604 -615 813 C
ATOM 499 CE1 PHE A1065 24.503 189.630 129.290 1.00100.39 C
ANISOU 499 CE1 PHE A1065 14115 9772 14256 -420 -573 673 C
ATOM 500 CE2 PHE A1065 25.985 188.885 127.570 1.00100.56 C
ANISOU 500 CE2 PHE A1065 14206 9908 14093 -570 -565 759 C
ATOM 501 CZ PHE A1065 25.134 188.601 128.620 1.00 98.72 C
ANISOU 501 CZ PHE A1065 13906 9674 13929 -479 -557 694 C
ATOM 502 N ASP A1066 27.490 195.502 128.280 1.00 94.34 N
ANISOU 502 N ASP A1066 13675 8574 13595 -676 -722 844 N
ATOM 503 CA ASP A1066 28.081 196.783 127.897 1.00 94.31 C
ANISOU 503 CA ASP A1066 13749 8466 13619 -743 -764 900 C
ATOM 504 C ASP A1066 29.593 196.643 128.070 1.00 96.36 C
ANISOU 504 C ASP A1066 14007 8779 13828 -850 -719 893 C
ATOM 505 O ASP A1066 30.326 196.986 127.151 1.00 96.18 O
ANISOU 505 O ASP A1066 14020 8745 13780 -938 -715 970 O
ATOM 506 CB ASP A1066 27.525 197.955 128.734 1.00 97.18 C
ANISOU 506 CB ASP A1066 14152 8677 14097 -684 -780 854 C
ATOM 507 CG ASP A1066 26.059 198.305 128.505 1.00110.32 C
ANISOU 507 CG ASP A1066 15786 10241 15891 -576 -818 881 C
ATOM 508 OD1 ASP A1066 25.600 198.235 127.333 1.00111.30 O
ANISOU 508 OD1 ASP A1066 15902 10366 16020 -583 -907 988 O
ATOM 509 OD2 ASP A1066 25.381 198.707 129.488 1.00117.22 O1-
ANISOU 509 OD2 ASP A1066 16654 11012 16872 -494 -761 802 O1-
ATOM 510 N ILE A1067 30.042 196.051 129.203 1.00 92.70 N
ANISOU 510 N ILE A1067 13496 8365 13359 -849 -688 812 N
ATOM 511 CA ILE A1067 31.455 195.763 129.525 1.00 92.97 C
ANISOU 511 CA ILE A1067 13487 8439 13397 -947 -674 815 C
ATOM 512 C ILE A1067 32.053 194.791 128.502 1.00 97.38 C
ANISOU 512 C ILE A1067 13973 9099 13927 -989 -597 871 C
ATOM 513 O ILE A1067 33.111 195.082 127.945 1.00 97.68 O
ANISOU 513 O ILE A1067 13995 9117 14002 -1082 -559 930 O
ATOM 514 CB ILE A1067 31.645 195.254 130.985 1.00 95.70 C
ANISOU 514 CB ILE A1067 13821 8800 13741 -941 -696 728 C
ATOM 515 CG1 ILE A1067 31.172 196.307 132.023 1.00 97.16 C
ANISOU 515 CG1 ILE A1067 14132 8852 13933 -925 -737 662 C
ATOM 516 CG2 ILE A1067 33.094 194.829 131.243 1.00 95.69 C
ANISOU 516 CG2 ILE A1067 13741 8831 13787 -1045 -719 759 C
ATOM 517 CD1 ILE A1067 30.398 195.699 133.224 1.00104.65 C
ANISOU 517 CD1 ILE A1067 15127 9802 14832 -863 -706 556 C
ATOM 518 N LEU A1068 31.377 193.644 128.256 1.00 93.93 N
ANISOU 518 N LEU A1068 13499 8758 13432 -926 -556 848 N
ATOM 519 CA LEU A1068 31.832 192.667 127.277 1.00 93.60 C
ANISOU 519 CA LEU A1068 13422 8797 13346 -965 -459 887 C
ATOM 520 C LEU A1068 31.962 193.375 125.914 1.00 98.27 C
ANISOU 520 C LEU A1068 14118 9329 13891 -1036 -432 973 C
ATOM 521 O LEU A1068 33.086 193.466 125.440 1.00 98.82 O
ANISOU 521 O LEU A1068 14174 9382 13991 -1128 -338 1013 O
ATOM 522 CB LEU A1068 30.954 191.398 127.248 1.00 92.70 C
ANISOU 522 CB LEU A1068 13280 8778 13165 -889 -438 848 C
ATOM 523 N VAL A1069 30.887 194.033 125.388 1.00 95.11 N
ANISOU 523 N VAL A1069 13820 8871 13448 -1005 -521 1010 N
ATOM 524 CA VAL A1069 30.930 194.807 124.119 1.00 96.24 C
ANISOU 524 CA VAL A1069 14101 8935 13530 -1088 -534 1105 C
ATOM 525 C VAL A1069 32.094 195.822 124.152 1.00104.42 C
ANISOU 525 C VAL A1069 15146 9895 14632 -1177 -497 1136 C
ATOM 526 O VAL A1069 32.827 195.934 123.169 1.00106.02 O
ANISOU 526 O VAL A1069 15424 10071 14787 -1284 -402 1197 O
ATOM 527 CB VAL A1069 29.567 195.458 123.710 1.00 99.14 C
ANISOU 527 CB VAL A1069 14553 9225 13891 -1037 -687 1157 C
ATOM 528 CG1 VAL A1069 29.732 196.583 122.689 1.00100.27 C
ANISOU 528 CG1 VAL A1069 14845 9252 14001 -1131 -742 1261 C
ATOM 529 CG2 VAL A1069 28.594 194.423 123.191 1.00 98.14 C
ANISOU 529 CG2 VAL A1069 14446 9157 13686 -1004 -724 1171 C
ATOM 530 N GLY A1070 32.273 196.487 125.297 1.00101.34 N
ANISOU 530 N GLY A1070 14694 9463 14346 -1143 -560 1090 N
ATOM 531 CA GLY A1070 33.330 197.464 125.542 1.00102.18 C
ANISOU 531 CA GLY A1070 14798 9490 14536 -1226 -559 1115 C
ATOM 532 C GLY A1070 34.716 196.895 125.330 1.00106.56 C
ANISOU 532 C GLY A1070 15260 10082 15145 -1319 -430 1136 C
ATOM 533 O GLY A1070 35.558 197.545 124.712 1.00108.34 O
ANISOU 533 O GLY A1070 15516 10241 15408 -1421 -369 1201 O
ATOM 534 N GLN A1071 34.942 195.660 125.792 1.00101.20 N
ANISOU 534 N GLN A1071 14463 9498 14490 -1285 -376 1088 N
ATOM 535 CA GLN A1071 36.210 194.954 125.635 1.00101.35 C
ANISOU 535 CA GLN A1071 14353 9541 14614 -1355 -241 1110 C
ATOM 536 C GLN A1071 36.366 194.439 124.213 1.00106.43 C
ANISOU 536 C GLN A1071 15067 10194 15177 -1408 -54 1152 C
ATOM 537 O GLN A1071 37.481 194.414 123.697 1.00106.12 O
ANISOU 537 O GLN A1071 14973 10109 15238 -1499 103 1197 O
ATOM 538 CB GLN A1071 36.273 193.766 126.589 1.00101.75 C
ANISOU 538 CB GLN A1071 14267 9676 14717 -1294 -261 1050 C
ATOM 539 CG GLN A1071 36.312 194.143 128.054 1.00113.98 C
ANISOU 539 CG GLN A1071 15777 11198 16332 -1278 -430 1009 C
ATOM 540 CD GLN A1071 36.229 192.915 128.906 1.00130.93 C
ANISOU 540 CD GLN A1071 17828 13424 18497 -1228 -456 958 C
ATOM 541 OE1 GLN A1071 36.600 191.810 128.486 1.00128.67 O
ANISOU 541 OE1 GLN A1071 17436 13195 18258 -1226 -344 970 O
ATOM 542 NE2 GLN A1071 35.764 193.086 130.130 1.00120.51 N
ANISOU 542 NE2 GLN A1071 16558 12092 17137 -1194 -592 898 N
ATOM 543 N ILE A1072 35.254 193.965 123.604 1.00104.74 N
ANISOU 543 N ILE A1072 14978 10027 14790 -1360 -63 1139 N
ATOM 544 CA ILE A1072 35.213 193.453 122.229 1.00106.03 C
ANISOU 544 CA ILE A1072 15283 10186 14816 -1428 91 1175 C
ATOM 545 C ILE A1072 35.623 194.605 121.330 1.00115.41 C
ANISOU 545 C ILE A1072 16618 11263 15970 -1541 130 1253 C
ATOM 546 O ILE A1072 36.499 194.411 120.503 1.00118.09 O
ANISOU 546 O ILE A1072 17003 11558 16309 -1645 343 1284 O
ATOM 547 CB ILE A1072 33.834 192.847 121.824 1.00107.74 C
ANISOU 547 CB ILE A1072 15623 10456 14857 -1369 4 1160 C
ATOM 548 CG1 ILE A1072 33.480 191.632 122.690 1.00106.89 C
ANISOU 548 CG1 ILE A1072 15372 10458 14784 -1265 -8 1082 C
ATOM 549 CG2 ILE A1072 33.804 192.460 120.349 1.00108.29 C
ANISOU 549 CG2 ILE A1072 15909 10490 14746 -1476 133 1207 C
ATOM 550 CD1 ILE A1072 31.959 191.348 122.817 1.00114.62 C
ANISOU 550 CD1 ILE A1072 16403 11480 15668 -1174 -168 1064 C
ATOM 551 N ASP A1073 35.052 195.809 121.549 1.00112.73 N
ANISOU 551 N ASP A1073 16345 10863 15622 -1524 -53 1284 N
ATOM 552 CA ASP A1073 35.372 197.026 120.814 1.00114.96 C
ANISOU 552 CA ASP A1073 16769 11031 15879 -1628 -53 1364 C
ATOM 553 C ASP A1073 36.822 197.467 121.068 1.00122.43 C
ANISOU 553 C ASP A1073 17593 11925 17001 -1709 72 1381 C
ATOM 554 O ASP A1073 37.475 197.927 120.131 1.00124.32 O
ANISOU 554 O ASP A1073 17940 12080 17215 -1832 208 1444 O
ATOM 555 CB ASP A1073 34.390 198.157 121.167 1.00116.96 C
ANISOU 555 CB ASP A1073 17088 11223 16127 -1569 -288 1386 C
ATOM 556 CG ASP A1073 33.122 198.203 120.325 1.00128.62 C
ANISOU 556 CG ASP A1073 18747 12673 17450 -1559 -413 1440 C
ATOM 557 OD1 ASP A1073 33.231 198.122 119.073 1.00130.96 O
ANISOU 557 OD1 ASP A1073 19239 12925 17594 -1677 -342 1509 O
ATOM 558 OD2 ASP A1073 32.026 198.411 120.909 1.00132.63 O1-
ANISOU 558 OD2 ASP A1073 19214 13179 18002 -1445 -586 1423 O1-
ATOM 559 N ASP A1074 37.329 197.304 122.317 1.00119.42 N
ANISOU 559 N ASP A1074 16995 11579 16800 -1655 21 1332 N
ATOM 560 CA ASP A1074 38.712 197.632 122.719 1.00120.98 C
ANISOU 560 CA ASP A1074 17032 11719 17214 -1733 92 1360 C
ATOM 561 C ASP A1074 39.720 196.760 121.927 1.00126.50 C
ANISOU 561 C ASP A1074 17659 12412 17994 -1809 376 1384 C
ATOM 562 O ASP A1074 40.802 197.236 121.583 1.00128.36 O
ANISOU 562 O ASP A1074 17838 12556 18376 -1914 511 1441 O
ATOM 563 CB ASP A1074 38.901 197.421 124.248 1.00122.60 C
ANISOU 563 CB ASP A1074 17054 11961 17568 -1667 -66 1309 C
ATOM 564 CG ASP A1074 39.100 198.670 125.112 1.00137.03 C
ANISOU 564 CG ASP A1074 18888 13704 19472 -1692 -253 1318 C
ATOM 565 OD1 ASP A1074 38.248 199.592 125.041 1.00138.08 O
ANISOU 565 OD1 ASP A1074 19182 13791 19491 -1669 -352 1318 O
ATOM 566 OD2 ASP A1074 40.044 198.677 125.939 1.00143.60 O1-
ANISOU 566 OD2 ASP A1074 19570 14509 20483 -1733 -320 1324 O1-
ATOM 567 N ALA A1075 39.338 195.493 121.636 1.00122.13 N
ANISOU 567 N ALA A1075 17109 11940 17357 -1757 480 1337 N
ATOM 568 CA ALA A1075 40.101 194.486 120.888 1.00122.68 C
ANISOU 568 CA ALA A1075 17133 11996 17484 -1810 777 1339 C
ATOM 569 C ALA A1075 39.881 194.629 119.379 1.00127.91 C
ANISOU 569 C ALA A1075 18083 12596 17923 -1913 964 1370 C
ATOM 570 O ALA A1075 40.784 194.336 118.598 1.00129.20 O
ANISOU 570 O ALA A1075 18257 12680 18154 -2011 1263 1391 O
ATOM 571 CB ALA A1075 39.678 193.097 121.334 1.00121.98 C
ANISOU 571 CB ALA A1075 16952 12014 17381 -1708 779 1269 C
ATOM 572 N LEU A1076 38.667 195.055 118.982 1.00124.17 N
ANISOU 572 N LEU A1076 17846 12140 17191 -1899 789 1378 N
ATOM 573 CA LEU A1076 38.222 195.290 117.607 1.00125.26 C
ANISOU 573 CA LEU A1076 18315 12210 17068 -2010 867 1425 C
ATOM 574 C LEU A1076 38.904 196.546 117.072 1.00132.32 C
ANISOU 574 C LEU A1076 19307 12978 17992 -2136 928 1503 C
ATOM 575 O LEU A1076 39.126 196.652 115.866 1.00134.04 O
ANISOU 575 O LEU A1076 19778 13103 18049 -2276 1116 1545 O
ATOM 576 CB LEU A1076 36.687 195.440 117.568 1.00123.88 C
ANISOU 576 CB LEU A1076 18302 12081 16686 -1944 581 1432 C
ATOM 577 CG LEU A1076 35.980 195.324 116.222 1.00129.09 C
ANISOU 577 CG LEU A1076 19315 12683 17051 -2052 585 1484 C
ATOM 578 CD1 LEU A1076 36.149 193.945 115.618 1.00129.42 C
ANISOU 578 CD1 LEU A1076 19449 12750 16974 -2096 819 1435 C
ATOM 579 CD2 LEU A1076 34.506 195.648 116.361 1.00129.56 C
ANISOU 579 CD2 LEU A1076 19453 12765 17009 -1975 248 1516 C
ATOM 580 N LYS A1077 39.240 197.490 117.978 1.00129.37 N
ANISOU 580 N LYS A1077 18756 12589 17811 -2099 773 1520 N
ATOM 581 CA LYS A1077 39.977 198.722 117.688 1.00131.04 C
ANISOU 581 CA LYS A1077 19007 12681 18101 -2210 812 1592 C
ATOM 582 C LYS A1077 41.437 198.315 117.362 1.00138.48 C
ANISOU 582 C LYS A1077 19812 13558 19247 -2307 1156 1603 C
ATOM 583 O LYS A1077 41.997 198.803 116.374 1.00140.02 O
ANISOU 583 O LYS A1077 20168 13637 19395 -2450 1364 1660 O
ATOM 584 CB LYS A1077 39.883 199.678 118.895 1.00131.71 C
ANISOU 584 CB LYS A1077 18935 12770 18340 -2135 540 1592 C
ATOM 585 CG LYS A1077 40.861 200.846 118.915 1.00142.61 C
ANISOU 585 CG LYS A1077 20269 14034 19882 -2240 573 1658 C
ATOM 586 CD LYS A1077 41.144 201.315 120.352 1.00151.38 C
ANISOU 586 CD LYS A1077 21151 15156 21210 -2174 365 1634 C
ATOM 587 CE LYS A1077 42.045 200.399 121.169 1.00158.81 C
ANISOU 587 CE LYS A1077 21799 16144 22396 -2147 435 1602 C
ATOM 588 NZ LYS A1077 43.453 200.407 120.687 1.00165.56 N
ANISOU 588 NZ LYS A1077 22517 16906 23483 -2270 684 1665 N
ATOM 589 N LEU A1078 42.008 197.364 118.159 1.00135.24 N
ANISOU 589 N LEU A1078 19110 13207 19068 -2231 1226 1554 N
ATOM 590 CA LEU A1078 43.356 196.796 118.001 1.00136.87 C
ANISOU 590 CA LEU A1078 19112 13343 19550 -2293 1545 1567 C
ATOM 591 C LEU A1078 43.483 195.948 116.735 1.00143.74 C
ANISOU 591 C LEU A1078 20179 14162 20273 -2372 1913 1546 C
ATOM 592 O LEU A1078 44.576 195.848 116.181 1.00145.32 O
ANISOU 592 O LEU A1078 20317 14244 20653 -2472 2253 1573 O
ATOM 593 CB LEU A1078 43.739 195.947 119.221 1.00135.69 C
ANISOU 593 CB LEU A1078 18614 13265 19677 -2183 1459 1531 C
ATOM 594 CG LEU A1078 44.038 196.698 120.506 1.00139.84 C
ANISOU 594 CG LEU A1078 18927 13793 20413 -2151 1164 1560 C
ATOM 595 CD1 LEU A1078 43.928 195.787 121.698 1.00138.22 C
ANISOU 595 CD1 LEU A1078 18501 13682 20334 -2036 993 1513 C
ATOM 596 CD2 LEU A1078 45.412 197.328 120.463 1.00145.83 C
ANISOU 596 CD2 LEU A1078 19499 14415 21495 -2266 1295 1644 C
ATOM 597 N ALA A1079 42.382 195.303 116.305 1.00140.97 N
ANISOU 597 N ALA A1079 20064 13888 19612 -2334 1854 1498 N
ATOM 598 CA ALA A1079 42.351 194.489 115.090 1.00142.92 C
ANISOU 598 CA ALA A1079 20574 14079 19651 -2425 2170 1471 C
ATOM 599 C ALA A1079 42.294 195.427 113.889 1.00150.31 C
ANISOU 599 C ALA A1079 21880 14890 20342 -2599 2266 1535 C
ATOM 600 O ALA A1079 42.930 195.146 112.874 1.00152.74 O
ANISOU 600 O ALA A1079 22363 15072 20599 -2737 2650 1536 O
ATOM 601 CB ALA A1079 41.147 193.555 115.100 1.00141.99 C
ANISOU 601 CB ALA A1079 20592 14076 19282 -2340 2012 1412 C
ATOM 602 N ASN A1080 41.573 196.567 114.027 1.00147.11 N
ANISOU 602 N ASN A1080 21593 14497 19803 -2597 1932 1592 N
ATOM 603 CA ASN A1080 41.454 197.614 113.001 1.00149.46 C
ANISOU 603 CA ASN A1080 22236 14673 19879 -2758 1943 1672 C
ATOM 604 C ASN A1080 42.732 198.479 112.919 1.00155.70 C
ANISOU 604 C ASN A1080 22911 15340 20908 -2861 2159 1725 C
ATOM 605 O ASN A1080 42.884 199.274 111.987 1.00156.31 O
ANISOU 605 O ASN A1080 23277 15291 20824 -3023 2266 1790 O
ATOM 606 CB ASN A1080 40.194 198.466 113.213 1.00149.93 C
ANISOU 606 CB ASN A1080 22427 14775 19766 -2704 1503 1721 C
ATOM 607 CG ASN A1080 38.962 197.899 112.539 1.00171.49 C
ANISOU 607 CG ASN A1080 25457 17536 22166 -2715 1357 1721 C
ATOM 608 OD1 ASN A1080 38.810 197.948 111.310 1.00171.26 O
ANISOU 608 OD1 ASN A1080 25815 17401 21854 -2883 1462 1768 O
ATOM 609 ND2 ASN A1080 38.040 197.372 113.330 1.00156.84 N
ANISOU 609 ND2 ASN A1080 23445 15809 20337 -2550 1100 1676 N
ATOM 610 N GLU A1081 43.651 198.286 113.896 1.00152.94 N
ANISOU 610 N GLU A1081 22143 15019 20949 -2777 2212 1704 N
ATOM 611 CA GLU A1081 44.978 198.900 114.020 1.00154.68 C
ANISOU 611 CA GLU A1081 22148 15126 21497 -2856 2410 1756 C
ATOM 612 C GLU A1081 46.040 197.979 113.383 1.00160.12 C
ANISOU 612 C GLU A1081 22772 15711 22355 -2935 2916 1731 C
ATOM 613 O GLU A1081 47.186 198.388 113.196 1.00161.38 O
ANISOU 613 O GLU A1081 22799 15738 22781 -3033 3179 1781 O
ATOM 614 CB GLU A1081 45.325 199.100 115.508 1.00154.74 C
ANISOU 614 CB GLU A1081 21734 15206 21853 -2729 2149 1757 C
ATOM 615 CG GLU A1081 44.936 200.454 116.082 1.00167.11 C
ANISOU 615 CG GLU A1081 23321 16780 23395 -2715 1785 1804 C
ATOM 616 CD GLU A1081 45.126 200.617 117.582 1.00194.11 C
ANISOU 616 CD GLU A1081 26409 20267 27079 -2602 1495 1792 C
ATOM 617 OE1 GLU A1081 46.063 200.002 118.145 1.00195.50 O
ANISOU 617 OE1 GLU A1081 26268 20434 27579 -2584 1598 1791 O
ATOM 618 OE2 GLU A1081 44.346 201.384 118.193 1.00187.69 O1-
ANISOU 618 OE2 GLU A1081 25663 19496 26156 -2541 1162 1788 O1-
ATOM 619 N GLY A1082 45.653 196.735 113.100 1.00156.56 N
ANISOU 619 N GLY A1082 22394 15311 21780 -2887 3052 1656 N
ATOM 620 CA GLY A1082 46.532 195.722 112.532 1.00158.52 C
ANISOU 620 CA GLY A1082 22588 15455 22187 -2940 3545 1614 C
ATOM 621 C GLY A1082 47.389 195.019 113.568 1.00162.58 C
ANISOU 621 C GLY A1082 22587 15991 23193 -2817 3593 1602 C
ATOM 622 O GLY A1082 48.086 194.052 113.240 1.00163.79 O
ANISOU 622 O GLY A1082 22630 16058 23546 -2828 3987 1566 O
ATOM 623 N LYS A1083 47.339 195.502 114.831 1.00157.45 N
ANISOU 623 N LYS A1083 21635 15442 22748 -2707 3188 1636 N
ATOM 624 CA LYS A1083 48.058 194.966 115.988 1.00156.76 C
ANISOU 624 CA LYS A1083 21070 15379 23113 -2600 3107 1647 C
ATOM 625 C LYS A1083 47.531 193.550 116.334 1.00159.07 C
ANISOU 625 C LYS A1083 21300 15780 23359 -2470 3090 1563 C
ATOM 626 O LYS A1083 46.675 193.389 117.212 1.00155.97 O
ANISOU 626 O LYS A1083 20870 15541 22851 -2350 2712 1532 O
ATOM 627 CB LYS A1083 47.924 195.940 117.168 1.00157.53 C
ANISOU 627 CB LYS A1083 20991 15546 23318 -2549 2643 1698 C
ATOM 628 N VAL A1084 48.046 192.535 115.593 1.00157.18 N
ANISOU 628 N VAL A1084 21070 15445 23208 -2502 3534 1523 N
ATOM 629 CA VAL A1084 47.682 191.109 115.634 1.00155.91 C
ANISOU 629 CA VAL A1084 20892 15343 23004 -2406 3633 1441 C
ATOM 630 C VAL A1084 47.851 190.490 117.032 1.00156.48 C
ANISOU 630 C VAL A1084 20543 15507 23405 -2255 3352 1450 C
ATOM 631 O VAL A1084 46.898 189.902 117.552 1.00152.84 O
ANISOU 631 O VAL A1084 20138 15199 22737 -2148 3091 1393 O
ATOM 632 CB VAL A1084 48.438 190.317 114.523 1.00163.05 C
ANISOU 632 CB VAL A1084 21876 16067 24007 -2495 4234 1404 C
ATOM 633 CG1 VAL A1084 48.397 188.804 114.752 1.00162.30 C
ANISOU 633 CG1 VAL A1084 21653 16000 24013 -2386 4364 1330 C
ATOM 634 CG2 VAL A1084 47.882 190.662 113.145 1.00164.21 C
ANISOU 634 CG2 VAL A1084 22570 16151 23673 -2649 4452 1372 C
ATOM 635 N LYS A1085 49.051 190.618 117.624 1.00154.29 N
ANISOU 635 N LYS A1085 19857 15126 23641 -2260 3394 1530 N
ATOM 636 CA LYS A1085 49.342 190.074 118.945 1.00153.07 C
ANISOU 636 CA LYS A1085 19309 15024 23827 -2148 3110 1563 C
ATOM 637 C LYS A1085 48.542 190.796 120.030 1.00155.22 C
ANISOU 637 C LYS A1085 19616 15452 23909 -2093 2565 1572 C
ATOM 638 O LYS A1085 48.045 190.139 120.948 1.00153.56 O
ANISOU 638 O LYS A1085 19307 15354 23685 -1987 2299 1542 O
ATOM 639 CB LYS A1085 50.852 190.116 119.245 1.00157.71 C
ANISOU 639 CB LYS A1085 19456 15430 25037 -2192 3264 1672 C
ATOM 640 CG LYS A1085 51.375 188.863 119.946 1.00166.06 C
ANISOU 640 CG LYS A1085 20138 16453 26504 -2095 3273 1691 C
ATOM 641 CD LYS A1085 51.089 188.827 121.457 1.00171.10 C
ANISOU 641 CD LYS A1085 20582 17211 27218 -2015 2718 1733 C
ATOM 642 CE LYS A1085 50.869 187.428 121.999 1.00180.36 C
ANISOU 642 CE LYS A1085 21621 18441 28466 -1896 2664 1693 C
ATOM 643 NZ LYS A1085 49.580 186.829 121.553 1.00184.76 N
ANISOU 643 NZ LYS A1085 22550 19158 28492 -1828 2698 1557 N
ATOM 644 N GLU A1086 48.398 192.136 119.918 1.00151.40 N
ANISOU 644 N GLU A1086 19289 14963 23274 -2170 2417 1608 N
ATOM 645 CA GLU A1086 47.649 192.945 120.885 1.00148.86 C
ANISOU 645 CA GLU A1086 19031 14755 22772 -2128 1946 1610 C
ATOM 646 C GLU A1086 46.170 192.516 120.934 1.00148.93 C
ANISOU 646 C GLU A1086 19312 14930 22344 -2029 1779 1512 C
ATOM 647 O GLU A1086 45.681 192.170 122.014 1.00146.40 O
ANISOU 647 O GLU A1086 18903 14712 22011 -1934 1483 1484 O
ATOM 648 CB GLU A1086 47.822 194.457 120.624 1.00151.18 C
ANISOU 648 CB GLU A1086 19445 14982 23014 -2234 1871 1669 C
ATOM 649 CG GLU A1086 49.239 194.967 120.870 1.00166.85 C
ANISOU 649 CG GLU A1086 21114 16811 25470 -2327 1935 1779 C
ATOM 650 CD GLU A1086 49.453 196.473 120.844 1.00194.54 C
ANISOU 650 CD GLU A1086 24702 20251 28963 -2431 1803 1844 C
ATOM 651 OE1 GLU A1086 49.864 197.029 121.888 1.00194.49 O
ANISOU 651 OE1 GLU A1086 24512 20225 29160 -2446 1484 1903 O
ATOM 652 OE2 GLU A1086 49.261 197.092 119.773 1.00189.12 O1-
ANISOU 652 OE2 GLU A1086 24274 19515 28067 -2513 2017 1843 O1-
ATOM 653 N ALA A1087 45.501 192.440 119.755 1.00144.69 N
ANISOU 653 N ALA A1087 19104 14402 21468 -2063 1982 1465 N
ATOM 654 CA ALA A1087 44.103 192.009 119.618 1.00141.90 C
ANISOU 654 CA ALA A1087 19013 14181 20721 -1988 1844 1388 C
ATOM 655 C ALA A1087 43.910 190.560 120.077 1.00144.29 C
ANISOU 655 C ALA A1087 19181 14562 21079 -1882 1865 1327 C
ATOM 656 O ALA A1087 42.849 190.229 120.600 1.00142.14 O
ANISOU 656 O ALA A1087 18986 14418 20603 -1788 1624 1275 O
ATOM 657 CB ALA A1087 43.635 192.175 118.181 1.00143.45 C
ANISOU 657 CB ALA A1087 19585 14330 20589 -2083 2065 1375 C
ATOM 658 N GLN A1088 44.942 189.712 119.908 1.00141.66 N
ANISOU 658 N GLN A1088 18632 14140 21051 -1894 2158 1337 N
ATOM 659 CA GLN A1088 44.946 188.317 120.342 1.00140.72 C
ANISOU 659 CA GLN A1088 18348 14066 21053 -1799 2204 1292 C
ATOM 660 C GLN A1088 44.856 188.236 121.876 1.00143.44 C
ANISOU 660 C GLN A1088 18446 14497 21558 -1707 1814 1311 C
ATOM 661 O GLN A1088 44.217 187.323 122.407 1.00140.93 O
ANISOU 661 O GLN A1088 18117 14282 21149 -1612 1689 1257 O
ATOM 662 CB GLN A1088 46.246 187.640 119.886 1.00144.46 C
ANISOU 662 CB GLN A1088 18595 14379 21913 -1840 2607 1321 C
ATOM 663 CG GLN A1088 46.085 186.638 118.758 1.00153.76 C
ANISOU 663 CG GLN A1088 19981 15510 22931 -1859 3006 1245 C
ATOM 664 CD GLN A1088 47.068 185.494 118.867 1.00168.71 C
ANISOU 664 CD GLN A1088 21565 17288 25249 -1821 3298 1251 C
ATOM 665 OE1 GLN A1088 47.951 185.453 119.737 1.00162.66 O
ANISOU 665 OE1 GLN A1088 20403 16462 24938 -1789 3205 1329 O
ATOM 666 NE2 GLN A1088 46.920 184.518 117.990 1.00162.15 N
ANISOU 666 NE2 GLN A1088 20914 16407 24289 -1830 3649 1173 N
ATOM 667 N ALA A1089 45.515 189.193 122.577 1.00141.42 N
ANISOU 667 N ALA A1089 18015 14186 21533 -1751 1625 1390 N
ATOM 668 CA ALA A1089 45.576 189.284 124.041 1.00140.35 C
ANISOU 668 CA ALA A1089 17686 14093 21547 -1707 1246 1421 C
ATOM 669 C ALA A1089 44.328 189.925 124.630 1.00141.72 C
ANISOU 669 C ALA A1089 18091 14390 21366 -1662 923 1367 C
ATOM 670 O ALA A1089 43.771 189.394 125.589 1.00139.52 O
ANISOU 670 O ALA A1089 17786 14198 21028 -1586 695 1330 O
ATOM 671 CB ALA A1089 46.820 190.051 124.475 1.00142.99 C
ANISOU 671 CB ALA A1089 17768 14292 22271 -1798 1178 1534 C
ATOM 672 N ALA A1090 43.877 191.058 124.060 1.00138.58 N
ANISOU 672 N ALA A1090 17922 13985 20746 -1710 916 1365 N
ATOM 673 CA ALA A1090 42.679 191.756 124.533 1.00136.67 C
ANISOU 673 CA ALA A1090 17891 13830 20207 -1663 645 1318 C
ATOM 674 C ALA A1090 41.427 190.861 124.461 1.00138.37 C
ANISOU 674 C ALA A1090 18254 14170 20149 -1560 624 1231 C
ATOM 675 O ALA A1090 40.545 190.976 125.313 1.00137.17 O
ANISOU 675 O ALA A1090 18164 14093 19861 -1491 386 1186 O
ATOM 676 CB ALA A1090 42.471 193.046 123.756 1.00137.94 C
ANISOU 676 CB ALA A1090 18257 13936 20219 -1736 672 1345 C
ATOM 677 N ALA A1091 41.378 189.942 123.481 1.00133.86 N
ANISOU 677 N ALA A1091 17738 13608 19513 -1558 886 1207 N
ATOM 678 CA ALA A1091 40.268 189.004 123.338 1.00131.71 C
ANISOU 678 CA ALA A1091 17596 13443 19006 -1475 875 1134 C
ATOM 679 C ALA A1091 40.458 187.790 124.252 1.00133.95 C
ANISOU 679 C ALA A1091 17670 13780 19445 -1397 825 1105 C
ATOM 680 O ALA A1091 39.495 187.072 124.518 1.00131.56 O
ANISOU 680 O ALA A1091 17439 13577 18973 -1317 738 1045 O
ATOM 681 CB ALA A1091 40.129 188.568 121.891 1.00133.35 C
ANISOU 681 CB ALA A1091 18001 13619 19048 -1529 1160 1121 C
ATOM 682 N GLU A1092 41.694 187.568 124.740 1.00131.82 N
ANISOU 682 N GLU A1092 17136 13434 19517 -1426 865 1160 N
ATOM 683 CA GLU A1092 42.006 186.459 125.641 1.00131.29 C
ANISOU 683 CA GLU A1092 16853 13390 19641 -1367 790 1157 C
ATOM 684 C GLU A1092 41.367 186.690 127.009 1.00131.97 C
ANISOU 684 C GLU A1092 16953 13550 19640 -1321 436 1136 C
ATOM 685 O GLU A1092 40.804 185.752 127.581 1.00129.93 O
ANISOU 685 O GLU A1092 16685 13370 19312 -1248 354 1090 O
ATOM 686 CB GLU A1092 43.532 186.232 125.745 1.00135.08 C
ANISOU 686 CB GLU A1092 17030 13736 20560 -1421 909 1245 C
ATOM 687 CG GLU A1092 43.972 185.097 126.665 1.00150.12 C
ANISOU 687 CG GLU A1092 18689 15635 22715 -1371 809 1269 C
ATOM 688 CD GLU A1092 43.168 183.808 126.608 1.00180.17 C
ANISOU 688 CD GLU A1092 22569 19539 26349 -1278 873 1187 C
ATOM 689 OE1 GLU A1092 43.028 183.228 125.505 1.00185.07 O
ANISOU 689 OE1 GLU A1092 23282 20150 26887 -1268 1181 1141 O
ATOM 690 OE2 GLU A1092 42.656 183.391 127.671 1.00175.54 O1-
ANISOU 690 OE2 GLU A1092 21973 19029 25694 -1226 614 1167 O1-
ATOM 691 N GLN A1093 41.414 187.948 127.506 1.00127.81 N
ANISOU 691 N GLN A1093 16477 12989 19096 -1370 246 1164 N
ATOM 692 CA GLN A1093 40.831 188.321 128.800 1.00126.06 C
ANISOU 692 CA GLN A1093 16319 12805 18771 -1347 -59 1136 C
ATOM 693 C GLN A1093 39.289 188.265 128.789 1.00125.51 C
ANISOU 693 C GLN A1093 16473 12844 18371 -1259 -101 1041 C
ATOM 694 O GLN A1093 38.665 188.315 129.852 1.00124.86 O
ANISOU 694 O GLN A1093 16454 12794 18192 -1225 -294 998 O
ATOM 695 CB GLN A1093 41.370 189.675 129.310 1.00128.54 C
ANISOU 695 CB GLN A1093 16641 13026 19172 -1436 -229 1190 C
ATOM 696 CG GLN A1093 41.070 190.889 128.428 1.00144.93 C
ANISOU 696 CG GLN A1093 18883 15075 21109 -1466 -148 1189 C
ATOM 697 CD GLN A1093 42.145 191.956 128.522 1.00163.26 C
ANISOU 697 CD GLN A1093 21124 17274 23634 -1579 -208 1274 C
ATOM 698 OE1 GLN A1093 41.904 193.096 128.942 1.00154.00 O
ANISOU 698 OE1 GLN A1093 20077 16062 22374 -1613 -372 1270 O
ATOM 699 NE2 GLN A1093 43.357 191.618 128.109 1.00160.24 N
ANISOU 699 NE2 GLN A1093 20527 16813 23545 -1641 -60 1354 N
ATOM 700 N LEU A1094 38.690 188.100 127.592 1.00118.67 N
ANISOU 700 N LEU A1094 15728 12016 17345 -1232 83 1015 N
ATOM 701 CA LEU A1094 37.247 187.977 127.414 1.00115.76 C
ANISOU 701 CA LEU A1094 15540 11733 16711 -1155 44 948 C
ATOM 702 C LEU A1094 36.722 186.646 127.960 1.00117.50 C
ANISOU 702 C LEU A1094 15713 12041 16891 -1077 24 894 C
ATOM 703 O LEU A1094 35.533 186.551 128.257 1.00116.31 O
ANISOU 703 O LEU A1094 15669 11954 16571 -1010 -62 839 O
ATOM 704 CB LEU A1094 36.851 188.172 125.947 1.00115.81 C
ANISOU 704 CB LEU A1094 15703 11732 16568 -1180 209 959 C
ATOM 705 CG LEU A1094 36.152 189.485 125.660 1.00120.49 C
ANISOU 705 CG LEU A1094 16462 12289 17030 -1194 107 974 C
ATOM 706 CD1 LEU A1094 36.853 190.266 124.570 1.00121.62 C
ANISOU 706 CD1 LEU A1094 16668 12341 17200 -1297 240 1040 C
ATOM 707 CD2 LEU A1094 34.693 189.259 125.345 1.00122.81 C
ANISOU 707 CD2 LEU A1094 16908 12640 17115 -1130 52 941 C
ATOM 708 N LYS A1095 37.615 185.630 128.108 1.00112.87 N
ANISOU 708 N LYS A1095 14952 11445 16488 -1086 107 915 N
ATOM 709 CA LYS A1095 37.324 184.303 128.668 1.00110.43 C
ANISOU 709 CA LYS A1095 14576 11204 16181 -1023 87 877 C
ATOM 710 C LYS A1095 36.854 184.470 130.125 1.00111.20 C
ANISOU 710 C LYS A1095 14696 11326 16229 -998 -160 847 C
ATOM 711 O LYS A1095 35.881 183.843 130.542 1.00109.12 O
ANISOU 711 O LYS A1095 14504 11138 15818 -932 -205 786 O
ATOM 712 CB LYS A1095 38.585 183.415 128.623 1.00113.58 C
ANISOU 712 CB LYS A1095 14752 11542 16859 -1049 201 928 C
ATOM 713 CG LYS A1095 38.750 182.567 127.368 1.00123.30 C
ANISOU 713 CG LYS A1095 15985 12763 18099 -1043 496 916 C
ATOM 714 CD LYS A1095 39.802 181.480 127.608 1.00133.92 C
ANISOU 714 CD LYS A1095 17088 14047 19748 -1038 590 955 C
ATOM 715 CE LYS A1095 40.036 180.545 126.443 1.00140.74 C
ANISOU 715 CE LYS A1095 17962 14878 20634 -1031 917 929 C
ATOM 716 NZ LYS A1095 40.994 179.457 126.793 1.00144.32 N
ANISOU 716 NZ LYS A1095 18158 15257 21421 -1009 1002 967 N
ATOM 717 N THR A1096 37.543 185.349 130.876 1.00107.31 N
ANISOU 717 N THR A1096 14166 10755 15851 -1066 -312 891 N
ATOM 718 CA THR A1096 37.260 185.696 132.269 1.00106.42 C
ANISOU 718 CA THR A1096 14128 10627 15681 -1082 -541 867 C
ATOM 719 C THR A1096 35.926 186.439 132.343 1.00108.92 C
ANISOU 719 C THR A1096 14651 10975 15760 -1029 -561 790 C
ATOM 720 O THR A1096 35.051 186.054 133.127 1.00108.21 O
ANISOU 720 O THR A1096 14650 10923 15542 -983 -626 725 O
ATOM 721 CB THR A1096 38.396 186.568 132.793 1.00113.35 C
ANISOU 721 CB THR A1096 14938 11389 16741 -1191 -684 945 C
ATOM 722 OG1 THR A1096 39.621 186.083 132.242 1.00115.71 O
ANISOU 722 OG1 THR A1096 15010 11638 17316 -1230 -589 1032 O
ATOM 723 CG2 THR A1096 38.449 186.630 134.322 1.00110.00 C
ANISOU 723 CG2 THR A1096 14585 10919 16292 -1247 -939 941 C
ATOM 724 N THR A1097 35.791 187.500 131.506 1.00104.39 N
ANISOU 724 N THR A1097 14143 10369 15149 -1039 -495 805 N
ATOM 725 CA THR A1097 34.630 188.376 131.329 1.00103.12 C
ANISOU 725 CA THR A1097 14146 10207 14829 -992 -504 759 C
ATOM 726 C THR A1097 33.351 187.575 131.008 1.00104.61 C
ANISOU 726 C THR A1097 14382 10484 14881 -894 -438 704 C
ATOM 727 O THR A1097 32.328 187.809 131.659 1.00104.35 O
ANISOU 727 O THR A1097 14440 10449 14760 -840 -492 646 O
ATOM 728 CB THR A1097 34.988 189.428 130.271 1.00111.77 C
ANISOU 728 CB THR A1097 15271 11243 15953 -1040 -443 814 C
ATOM 729 OG1 THR A1097 36.034 190.236 130.798 1.00116.10 O
ANISOU 729 OG1 THR A1097 15784 11700 16628 -1129 -536 858 O
ATOM 730 CG2 THR A1097 33.810 190.303 129.844 1.00108.26 C
ANISOU 730 CG2 THR A1097 14974 10781 15378 -990 -452 792 C
ATOM 731 N ARG A1098 33.415 186.614 130.045 1.00 98.38 N
ANISOU 731 N ARG A1098 13536 9757 14086 -879 -314 721 N
ATOM 732 CA ARG A1098 32.260 185.791 129.690 1.00 96.23 C
ANISOU 732 CA ARG A1098 13309 9562 13692 -803 -272 680 C
ATOM 733 C ARG A1098 31.780 184.941 130.857 1.00 98.65 C
ANISOU 733 C ARG A1098 13589 9918 13977 -752 -333 621 C
ATOM 734 O ARG A1098 30.581 184.715 130.953 1.00 97.91 O
ANISOU 734 O ARG A1098 13549 9859 13792 -685 -339 578 O
ATOM 735 CB ARG A1098 32.466 184.954 128.412 1.00 95.85 C
ANISOU 735 CB ARG A1098 13251 9550 13617 -819 -124 707 C
ATOM 736 CG ARG A1098 33.561 183.899 128.448 1.00106.58 C
ANISOU 736 CG ARG A1098 14477 10919 15101 -846 -23 720 C
ATOM 737 CD ARG A1098 33.028 182.478 128.402 1.00115.91 C
ANISOU 737 CD ARG A1098 15638 12176 16224 -793 27 679 C
ATOM 738 NE ARG A1098 34.022 181.522 127.892 1.00123.50 N
ANISOU 738 NE ARG A1098 16502 13122 17299 -821 191 699 N
ATOM 739 CZ ARG A1098 34.969 180.925 128.619 1.00134.98 C
ANISOU 739 CZ ARG A1098 17789 14553 18945 -826 184 717 C
ATOM 740 NH1 ARG A1098 35.105 181.207 129.906 1.00116.62 N
ANISOU 740 NH1 ARG A1098 15404 12219 16686 -825 -1 722 N
ATOM 741 NH2 ARG A1098 35.805 180.065 128.053 1.00124.40 N
ANISOU 741 NH2 ARG A1098 16350 13177 17740 -842 364 735 N
ATOM 742 N ASN A1099 32.685 184.517 131.768 1.00 95.27 N
ANISOU 742 N ASN A1099 13082 9474 13640 -791 -390 626 N
ATOM 743 CA ASN A1099 32.289 183.732 132.941 1.00 94.86 C
ANISOU 743 CA ASN A1099 13040 9453 13549 -765 -462 577 C
ATOM 744 C ASN A1099 31.481 184.550 133.941 1.00 99.93 C
ANISOU 744 C ASN A1099 13823 10046 14100 -755 -541 519 C
ATOM 745 O ASN A1099 30.539 184.030 134.560 1.00 99.92 O
ANISOU 745 O ASN A1099 13878 10074 14013 -705 -532 457 O
ATOM 746 CB ASN A1099 33.482 183.097 133.636 1.00 94.07 C
ANISOU 746 CB ASN A1099 12833 9328 13582 -828 -538 619 C
ATOM 747 CG ASN A1099 34.171 182.056 132.823 1.00119.28 C
ANISOU 747 CG ASN A1099 15876 12554 16893 -821 -425 662 C
ATOM 748 OD1 ASN A1099 35.392 182.070 132.681 1.00115.45 O
ANISOU 748 OD1 ASN A1099 15259 12009 16597 -879 -426 731 O
ATOM 749 ND2 ASN A1099 33.410 181.116 132.280 1.00115.28 N
ANISOU 749 ND2 ASN A1099 15380 12125 16295 -754 -318 624 N
ATOM 750 N ALA A1100 31.854 185.826 134.101 1.00 96.43 N
ANISOU 750 N ALA A1100 13442 9515 13683 -806 -598 535 N
ATOM 751 CA ALA A1100 31.196 186.725 135.039 1.00 96.56 C
ANISOU 751 CA ALA A1100 13615 9451 13624 -808 -645 474 C
ATOM 752 C ALA A1100 29.890 187.272 134.507 1.00 99.45 C
ANISOU 752 C ALA A1100 14031 9810 13946 -717 -559 437 C
ATOM 753 O ALA A1100 28.990 187.565 135.294 1.00 99.11 O
ANISOU 753 O ALA A1100 14092 9714 13853 -680 -534 367 O
ATOM 754 CB ALA A1100 32.127 187.872 135.391 1.00 98.41 C
ANISOU 754 CB ALA A1100 13901 9579 13911 -905 -744 508 C
ATOM 755 N TYR A1101 29.781 187.418 133.179 1.00 95.44 N
ANISOU 755 N TYR A1101 13458 9336 13470 -690 -510 491 N
ATOM 756 CA TYR A1101 28.635 188.070 132.566 1.00 94.76 C
ANISOU 756 CA TYR A1101 13409 9218 13379 -621 -477 490 C
ATOM 757 C TYR A1101 27.698 187.179 131.782 1.00 96.09 C
ANISOU 757 C TYR A1101 13523 9463 13523 -554 -433 501 C
ATOM 758 O TYR A1101 26.569 187.605 131.530 1.00 96.40 O
ANISOU 758 O TYR A1101 13578 9460 13588 -491 -433 500 O
ATOM 759 CB TYR A1101 29.114 189.242 131.691 1.00 96.49 C
ANISOU 759 CB TYR A1101 13651 9372 13639 -665 -501 557 C
ATOM 760 CG TYR A1101 29.913 190.285 132.449 1.00 98.71 C
ANISOU 760 CG TYR A1101 13997 9555 13953 -735 -559 549 C
ATOM 761 CD1 TYR A1101 29.464 190.791 133.669 1.00100.63 C
ANISOU 761 CD1 TYR A1101 14346 9714 14176 -724 -577 474 C
ATOM 762 CD2 TYR A1101 31.103 190.784 131.938 1.00100.66 C
ANISOU 762 CD2 TYR A1101 14217 9778 14253 -822 -585 616 C
ATOM 763 CE1 TYR A1101 30.183 191.763 134.358 1.00101.87 C
ANISOU 763 CE1 TYR A1101 14598 9765 14342 -805 -644 467 C
ATOM 764 CE2 TYR A1101 31.836 191.754 132.622 1.00102.78 C
ANISOU 764 CE2 TYR A1101 14545 9948 14560 -897 -660 618 C
ATOM 765 CZ TYR A1101 31.368 192.244 133.827 1.00111.13 C
ANISOU 765 CZ TYR A1101 15727 10923 15575 -892 -702 543 C
ATOM 766 OH TYR A1101 32.088 193.202 134.493 1.00115.72 O
ANISOU 766 OH TYR A1101 16400 11394 16175 -984 -789 545 O
ATOM 767 N ILE A1102 28.142 185.980 131.379 1.00 90.68 N
ANISOU 767 N ILE A1102 12773 8874 12808 -570 -401 517 N
ATOM 768 CA ILE A1102 27.288 185.058 130.628 1.00 89.57 C
ANISOU 768 CA ILE A1102 12605 8800 12626 -524 -371 527 C
ATOM 769 C ILE A1102 27.105 183.736 131.365 1.00 92.94 C
ANISOU 769 C ILE A1102 12984 9302 13026 -494 -343 474 C
ATOM 770 O ILE A1102 25.967 183.369 131.652 1.00 92.65 O
ANISOU 770 O ILE A1102 12944 9277 12984 -432 -336 441 O
ATOM 771 CB ILE A1102 27.716 184.833 129.147 1.00 92.65 C
ANISOU 771 CB ILE A1102 13010 9215 12978 -576 -338 596 C
ATOM 772 CG1 ILE A1102 28.147 186.139 128.453 1.00 93.87 C
ANISOU 772 CG1 ILE A1102 13228 9290 13150 -631 -359 655 C
ATOM 773 CG2 ILE A1102 26.590 184.132 128.373 1.00 93.23 C
ANISOU 773 CG2 ILE A1102 13105 9324 12994 -544 -352 615 C
ATOM 774 CD1 ILE A1102 28.860 185.974 127.078 1.00101.28 C
ANISOU 774 CD1 ILE A1102 14216 10232 14034 -712 -286 715 C
ATOM 775 N GLN A1103 28.219 183.024 131.656 1.00 89.16 N
ANISOU 775 N GLN A1103 12458 8863 12556 -541 -327 476 N
ATOM 776 CA GLN A1103 28.260 181.698 132.284 1.00 88.69 C
ANISOU 776 CA GLN A1103 12351 8869 12480 -526 -312 442 C
ATOM 777 C GLN A1103 27.325 181.544 133.506 1.00 93.06 C
ANISOU 777 C GLN A1103 12951 9413 12994 -483 -329 373 C
ATOM 778 O GLN A1103 26.668 180.498 133.624 1.00 95.04 O
ANISOU 778 O GLN A1103 13177 9723 13211 -443 -297 348 O
ATOM 779 CB GLN A1103 29.714 181.278 132.613 1.00 90.26 C
ANISOU 779 CB GLN A1103 12479 9062 12752 -590 -327 470 C
ATOM 780 CG GLN A1103 29.949 180.462 133.905 1.00103.85 C
ANISOU 780 CG GLN A1103 14188 10793 14477 -602 -391 441 C
ATOM 781 CD GLN A1103 29.607 178.982 133.849 1.00116.59 C
ANISOU 781 CD GLN A1103 15749 12482 16066 -563 -344 424 C
ATOM 782 OE1 GLN A1103 28.955 178.477 132.927 1.00106.87 O
ANISOU 782 OE1 GLN A1103 14510 11304 14792 -519 -264 418 O
ATOM 783 NE2 GLN A1103 30.028 178.254 134.876 1.00111.53 N
ANISOU 783 NE2 GLN A1103 15091 11837 15448 -591 -413 421 N
ATOM 784 N LYS A1104 27.242 182.555 134.384 1.00 86.43 N
ANISOU 784 N LYS A1104 12194 8489 12154 -496 -360 341 N
ATOM 785 CA LYS A1104 26.393 182.437 135.564 1.00 85.12 C
ANISOU 785 CA LYS A1104 12109 8289 11944 -470 -331 266 C
ATOM 786 C LYS A1104 24.901 182.523 135.262 1.00 87.77 C
ANISOU 786 C LYS A1104 12426 8611 12310 -382 -254 241 C
ATOM 787 O LYS A1104 24.124 182.165 136.129 1.00 88.51 O
ANISOU 787 O LYS A1104 12563 8681 12387 -353 -188 179 O
ATOM 788 CB LYS A1104 26.788 183.406 136.704 1.00 88.40 C
ANISOU 788 CB LYS A1104 12665 8594 12328 -533 -369 227 C
ATOM 789 CG LYS A1104 27.198 184.829 136.335 1.00101.98 C
ANISOU 789 CG LYS A1104 14422 10230 14096 -559 -402 253 C
ATOM 790 CD LYS A1104 27.471 185.658 137.612 1.00118.64 C
ANISOU 790 CD LYS A1104 16714 12217 16149 -632 -434 199 C
ATOM 791 CE LYS A1104 28.875 185.500 138.185 1.00130.20 C
ANISOU 791 CE LYS A1104 18210 13665 17593 -753 -581 241 C
ATOM 792 NZ LYS A1104 29.021 186.105 139.544 1.00132.60 N
ANISOU 792 NZ LYS A1104 18745 13841 17797 -849 -634 185 N
ATOM 793 N TYR A1105 24.487 182.939 134.058 1.00 83.91 N
ANISOU 793 N TYR A1105 11878 8125 11881 -347 -266 298 N
ATOM 794 CA TYR A1105 23.055 183.056 133.721 1.00 84.33 C
ANISOU 794 CA TYR A1105 11885 8144 12014 -270 -234 302 C
ATOM 795 C TYR A1105 22.548 181.915 132.850 1.00 91.68 C
ANISOU 795 C TYR A1105 12736 9165 12935 -251 -254 342 C
ATOM 796 O TYR A1105 21.342 181.834 132.553 1.00 92.80 O
ANISOU 796 O TYR A1105 12819 9279 13163 -196 -255 361 O
ATOM 797 CB TYR A1105 22.755 184.389 133.036 1.00 85.10 C
ANISOU 797 CB TYR A1105 11987 8148 12201 -254 -273 352 C
ATOM 798 CG TYR A1105 23.119 185.599 133.859 1.00 85.97 C
ANISOU 798 CG TYR A1105 12188 8146 12329 -271 -246 308 C
ATOM 799 CD1 TYR A1105 22.268 186.072 134.850 1.00 87.85 C
ANISOU 799 CD1 TYR A1105 12469 8275 12635 -222 -146 236 C
ATOM 800 CD2 TYR A1105 24.299 186.293 133.624 1.00 86.59 C
ANISOU 800 CD2 TYR A1105 12320 8213 12367 -342 -306 338 C
ATOM 801 CE1 TYR A1105 22.593 187.191 135.603 1.00 89.47 C
ANISOU 801 CE1 TYR A1105 12796 8359 12838 -249 -109 187 C
ATOM 802 CE2 TYR A1105 24.632 187.418 134.366 1.00 88.81 C
ANISOU 802 CE2 TYR A1105 12702 8383 12658 -370 -297 300 C
ATOM 803 CZ TYR A1105 23.767 187.877 135.344 1.00 98.84 C
ANISOU 803 CZ TYR A1105 14042 9542 13972 -325 -201 222 C
ATOM 804 OH TYR A1105 24.074 189.017 136.056 1.00103.92 O
ANISOU 804 OH TYR A1105 14819 10055 14610 -362 -180 176 O
ATOM 805 N LEU A1106 23.472 181.023 132.454 1.00 87.91 N
ANISOU 805 N LEU A1106 12254 8779 12371 -300 -269 359 N
ATOM 806 CA LEU A1106 23.183 179.879 131.611 1.00 86.90 C
ANISOU 806 CA LEU A1106 12086 8728 12203 -301 -276 389 C
ATOM 807 C LEU A1106 22.099 179.006 132.248 1.00 91.86 C
ANISOU 807 C LEU A1106 12669 9380 12855 -249 -243 348 C
ATOM 808 O LEU A1106 21.990 179.019 133.481 1.00 91.01 O
ANISOU 808 O LEU A1106 12579 9246 12754 -231 -186 283 O
ATOM 809 CB LEU A1106 24.465 179.112 131.262 1.00 86.10 C
ANISOU 809 CB LEU A1106 11989 8692 12033 -359 -253 399 C
ATOM 810 CG LEU A1106 25.491 179.838 130.397 1.00 89.92 C
ANISOU 810 CG LEU A1106 12508 9147 12513 -418 -254 450 C
ATOM 811 CD1 LEU A1106 26.664 178.948 130.130 1.00 89.69 C
ANISOU 811 CD1 LEU A1106 12451 9159 12470 -463 -190 455 C
ATOM 812 CD2 LEU A1106 24.893 180.311 129.085 1.00 91.02 C
ANISOU 812 CD2 LEU A1106 12704 9256 12624 -436 -294 513 C
ATOM 813 N PRO A 10 21.227 178.366 131.406 1.00 90.13 N
ANISOU 813 N PRO A 10 12409 9187 12650 -236 -281 389 N
ATOM 814 CA PRO A 10 20.040 177.659 131.911 1.00 90.14 C
ANISOU 814 CA PRO A 10 12343 9190 12716 -186 -253 365 C
ATOM 815 C PRO A 10 20.161 176.862 133.205 1.00 95.45 C
ANISOU 815 C PRO A 10 13022 9900 13347 -174 -161 284 C
ATOM 816 O PRO A 10 19.358 177.079 134.116 1.00 95.64 O
ANISOU 816 O PRO A 10 13027 9865 13445 -132 -85 239 O
ATOM 817 CB PRO A 10 19.678 176.750 130.745 1.00 91.78 C
ANISOU 817 CB PRO A 10 12542 9446 12886 -215 -330 425 C
ATOM 818 CG PRO A 10 20.017 177.538 129.557 1.00 96.84 C
ANISOU 818 CG PRO A 10 13246 10050 13499 -263 -415 499 C
ATOM 819 CD PRO A 10 21.222 178.366 129.925 1.00 92.49 C
ANISOU 819 CD PRO A 10 12743 9490 12909 -282 -361 470 C
ATOM 820 N CYS A 11 21.159 175.978 133.298 1.00 92.96 N
ANISOU 820 N CYS A 11 12737 9660 12924 -216 -157 269 N
ATOM 821 CA CYS A 11 21.380 175.077 134.428 1.00 93.83 C
ANISOU 821 CA CYS A 11 12867 9803 12981 -224 -107 212 C
ATOM 822 C CYS A 11 21.742 175.776 135.740 1.00 93.25 C
ANISOU 822 C CYS A 11 12879 9665 12888 -241 -72 158 C
ATOM 823 O CYS A 11 21.917 175.115 136.768 1.00 91.11 O
ANISOU 823 O CYS A 11 12664 9400 12553 -268 -49 117 O
ATOM 824 CB CYS A 11 22.425 174.039 134.053 1.00 95.80 C
ANISOU 824 CB CYS A 11 13112 10126 13164 -263 -129 229 C
ATOM 825 SG CYS A 11 24.070 174.740 133.814 1.00101.33 S
ANISOU 825 SG CYS A 11 13831 10805 13866 -317 -162 259 S
ATOM 826 N PHE A 12 21.853 177.101 135.713 1.00 89.34 N
ANISOU 826 N PHE A 12 12416 9094 12434 -240 -78 162 N
ATOM 827 CA PHE A 12 22.176 177.858 136.914 1.00 88.98 C
ANISOU 827 CA PHE A 12 12490 8966 12354 -273 -48 108 C
ATOM 828 C PHE A 12 20.939 178.529 137.511 1.00 94.18 C
ANISOU 828 C PHE A 12 13181 9519 13083 -224 72 54 C
ATOM 829 O PHE A 12 20.415 179.515 136.967 1.00 96.02 O
ANISOU 829 O PHE A 12 13366 9687 13430 -178 85 77 O
ATOM 830 CB PHE A 12 23.346 178.834 136.682 1.00 90.10 C
ANISOU 830 CB PHE A 12 12668 9077 12488 -323 -129 142 C
ATOM 831 CG PHE A 12 24.624 178.088 136.395 1.00 90.30 C
ANISOU 831 CG PHE A 12 12655 9174 12482 -376 -210 186 C
ATOM 832 CD1 PHE A 12 25.316 177.444 137.414 1.00 92.12 C
ANISOU 832 CD1 PHE A 12 12944 9402 12656 -436 -257 172 C
ATOM 833 CD2 PHE A 12 25.091 177.953 135.094 1.00 92.16 C
ANISOU 833 CD2 PHE A 12 12802 9460 12756 -373 -231 248 C
ATOM 834 CE1 PHE A 12 26.464 176.700 137.139 1.00 92.71 C
ANISOU 834 CE1 PHE A 12 12944 9521 12761 -476 -329 225 C
ATOM 835 CE2 PHE A 12 26.246 177.212 134.819 1.00 94.28 C
ANISOU 835 CE2 PHE A 12 13016 9770 13035 -415 -260 285 C
ATOM 836 CZ PHE A 12 26.917 176.583 135.842 1.00 92.05 C
ANISOU 836 CZ PHE A 12 12748 9482 12746 -457 -310 277 C
ATOM 837 N ARG A 13 20.446 177.932 138.611 1.00 88.62 N
ANISOU 837 N ARG A 13 12556 8788 12327 -235 173 -13 N
ATOM 838 CA ARG A 13 19.322 178.440 139.378 1.00 88.91 C
ANISOU 838 CA ARG A 13 12643 8703 12437 -198 347 -81 C
ATOM 839 C ARG A 13 19.890 179.454 140.391 1.00 96.22 C
ANISOU 839 C ARG A 13 13781 9509 13271 -264 390 -144 C
ATOM 840 O ARG A 13 21.092 179.394 140.675 1.00 95.34 O
ANISOU 840 O ARG A 13 13772 9427 13024 -351 263 -130 O
ATOM 841 CB ARG A 13 18.683 177.299 140.153 1.00 86.37 C
ANISOU 841 CB ARG A 13 12352 8397 12069 -206 454 -128 C
ATOM 842 CG ARG A 13 17.831 176.334 139.347 1.00 87.65 C
ANISOU 842 CG ARG A 13 12322 8642 12338 -145 442 -79 C
ATOM 843 CD ARG A 13 17.115 175.316 140.236 1.00 87.14 C
ANISOU 843 CD ARG A 13 12296 8571 12244 -155 577 -132 C
ATOM 844 NE ARG A 13 18.011 174.562 141.118 1.00 89.93 N
ANISOU 844 NE ARG A 13 12824 8963 12384 -247 538 -165 N
ATOM 845 CZ ARG A 13 18.203 174.829 142.407 1.00115.05 C
ANISOU 845 CZ ARG A 13 16234 12044 15434 -321 634 -239 C
ATOM 846 NH1 ARG A 13 17.558 175.836 142.989 1.00104.75 N
ANISOU 846 NH1 ARG A 13 15020 10593 14189 -307 819 -306 N
ATOM 847 NH2 ARG A 13 19.052 174.101 143.123 1.00112.66 N
ANISOU 847 NH2 ARG A 13 16088 11771 14947 -418 542 -243 N
ATOM 848 N PRO A 14 19.084 180.371 140.985 1.00 96.42 N
ANISOU 848 N PRO A 14 13882 9380 13374 -235 568 -211 N
ATOM 849 CA PRO A 14 19.656 181.296 141.982 1.00 98.43 C
ANISOU 849 CA PRO A 14 14389 9505 13507 -319 613 -279 C
ATOM 850 C PRO A 14 20.043 180.581 143.290 1.00108.53 C
ANISOU 850 C PRO A 14 15915 10760 14560 -436 639 -343 C
ATOM 851 O PRO A 14 19.462 179.531 143.606 1.00109.55 O
ANISOU 851 O PRO A 14 16027 10927 14669 -427 725 -364 O
ATOM 852 CB PRO A 14 18.536 182.316 142.202 1.00100.99 C
ANISOU 852 CB PRO A 14 14715 9655 14002 -244 841 -339 C
ATOM 853 CG PRO A 14 17.523 182.047 141.137 1.00104.25 C
ANISOU 853 CG PRO A 14 14833 10116 14661 -120 847 -269 C
ATOM 854 CD PRO A 14 17.641 180.621 140.803 1.00 98.42 C
ANISOU 854 CD PRO A 14 14000 9546 13851 -132 742 -224 C
ATOM 855 N THR A 15 21.058 181.113 144.018 1.00107.88 N
ANISOU 855 N THR A 15 16069 10613 14306 -560 538 -361 N
ATOM 856 CA THR A 15 21.545 180.579 145.303 1.00109.45 C
ANISOU 856 CA THR A 15 16558 10760 14269 -707 508 -404 C
ATOM 857 C THR A 15 22.093 181.674 146.202 1.00119.99 C
ANISOU 857 C THR A 15 18209 11927 15456 -834 497 -458 C
ATOM 858 O THR A 15 22.802 182.587 145.742 1.00119.99 O
ANISOU 858 O THR A 15 18173 11914 15503 -844 367 -417 O
ATOM 859 CB THR A 15 22.638 179.517 145.136 1.00110.71 C
ANISOU 859 CB THR A 15 16648 11061 14356 -769 248 -312 C
ATOM 860 OG1 THR A 15 23.479 179.854 144.033 1.00105.17 O
ANISOU 860 OG1 THR A 15 15732 10453 13776 -729 71 -219 O
ATOM 861 CG2 THR A 15 22.094 178.073 145.048 1.00108.17 C
ANISOU 861 CG2 THR A 15 16208 10846 14044 -723 294 -301 C
ATOM 862 N ASN A 16 21.756 181.570 147.497 1.00121.01 N
ANISOU 862 N ASN A 16 18674 11915 15391 -946 638 -552 N
ATOM 863 CA ASN A 16 22.237 182.477 148.535 1.00123.65 C
ANISOU 863 CA ASN A 16 19396 12062 15523 -1107 631 -615 C
ATOM 864 C ASN A 16 23.193 181.654 149.431 1.00128.37 C
ANISOU 864 C ASN A 16 20243 12662 15869 -1299 386 -571 C
ATOM 865 O ASN A 16 23.013 181.531 150.655 1.00130.73 O
ANISOU 865 O ASN A 16 20933 12811 15927 -1450 474 -648 O
ATOM 866 CB ASN A 16 21.072 183.160 149.309 1.00128.70 C
ANISOU 866 CB ASN A 16 20276 12488 16135 -1100 1017 -764 C
ATOM 867 CG ASN A 16 21.319 184.598 149.772 1.00160.31 C
ANISOU 867 CG ASN A 16 24554 16290 20065 -1180 1078 -834 C
ATOM 868 OD1 ASN A 16 22.359 185.216 149.503 1.00155.77 O
ANISOU 868 OD1 ASN A 16 23990 15733 19464 -1242 819 -768 O
ATOM 869 ND2 ASN A 16 20.347 185.179 150.473 1.00154.15 N
ANISOU 869 ND2 ASN A 16 24001 15300 19269 -1180 1445 -971 N
ATOM 870 N ILE A 17 24.176 181.022 148.760 1.00121.31 N
ANISOU 870 N ILE A 17 19109 11931 15053 -1292 85 -440 N
ATOM 871 CA ILE A 17 25.277 180.280 149.363 1.00120.07 C
ANISOU 871 CA ILE A 17 19084 11784 14753 -1456 -222 -354 C
ATOM 872 C ILE A 17 26.487 181.210 149.193 1.00122.23 C
ANISOU 872 C ILE A 17 19365 12015 15061 -1539 -480 -279 C
ATOM 873 O ILE A 17 26.852 181.552 148.064 1.00120.24 O
ANISOU 873 O ILE A 17 18793 11869 15025 -1423 -536 -215 O
ATOM 874 CB ILE A 17 25.487 178.844 148.783 1.00120.89 C
ANISOU 874 CB ILE A 17 18898 12070 14963 -1384 -344 -261 C
ATOM 875 CG1 ILE A 17 26.835 178.242 149.252 1.00121.72 C
ANISOU 875 CG1 ILE A 17 19075 12169 15004 -1544 -709 -139 C
ATOM 876 CG2 ILE A 17 25.378 178.813 147.260 1.00119.42 C
ANISOU 876 CG2 ILE A 17 18276 12052 15046 -1190 -313 -210 C
ATOM 877 CD1 ILE A 17 26.982 176.724 149.160 1.00130.09 C
ANISOU 877 CD1 ILE A 17 19976 13344 16108 -1522 -811 -65 C
ATOM 878 N THR A 18 27.048 181.684 150.310 1.00119.25 N
ANISOU 878 N THR A 18 19378 11465 14466 -1749 -621 -290 N
ATOM 879 CA THR A 18 28.193 182.582 150.246 1.00119.64 C
ANISOU 879 CA THR A 18 19457 11451 14548 -1851 -882 -214 C
ATOM 880 C THR A 18 29.461 181.839 149.877 1.00122.20 C
ANISOU 880 C THR A 18 19535 11877 15017 -1893 -1241 -43 C
ATOM 881 O THR A 18 29.547 180.631 150.073 1.00121.47 O
ANISOU 881 O THR A 18 19374 11857 14924 -1899 -1324 9 O
ATOM 882 CB THR A 18 28.383 183.345 151.563 1.00135.04 C
ANISOU 882 CB THR A 18 21934 13164 16212 -2083 -934 -277 C
ATOM 883 OG1 THR A 18 28.559 182.428 152.647 1.00135.54 O
ANISOU 883 OG1 THR A 18 22301 13155 16043 -2263 -1075 -256 O
ATOM 884 CG2 THR A 18 27.260 184.342 151.841 1.00137.77 C
ANISOU 884 CG2 THR A 18 22503 13372 16470 -2034 -549 -449 C
ATOM 885 N LEU A 19 30.463 182.579 149.379 1.00118.82 N
ANISOU 885 N LEU A 19 18975 11437 14734 -1925 -1444 46 N
ATOM 886 CA LEU A 19 31.807 182.102 149.049 1.00118.36 C
ANISOU 886 CA LEU A 19 18676 11427 14867 -1981 -1781 216 C
ATOM 887 C LEU A 19 32.397 181.420 150.300 1.00123.01 C
ANISOU 887 C LEU A 19 19549 11899 15291 -2202 -2074 288 C
ATOM 888 O LEU A 19 33.187 180.483 150.175 1.00122.89 O
ANISOU 888 O LEU A 19 19322 11936 15436 -2222 -2306 423 O
ATOM 889 CB LEU A 19 32.670 183.329 148.691 1.00119.44 C
ANISOU 889 CB LEU A 19 18769 11494 15119 -2038 -1925 272 C
ATOM 890 CG LEU A 19 33.435 183.325 147.367 1.00122.82 C
ANISOU 890 CG LEU A 19 18743 12047 15876 -1917 -1974 379 C
ATOM 891 CD1 LEU A 19 32.552 183.796 146.227 1.00121.25 C
ANISOU 891 CD1 LEU A 19 18356 11959 15756 -1708 -1654 291 C
ATOM 892 CD2 LEU A 19 34.646 184.248 147.453 1.00126.24 C
ANISOU 892 CD2 LEU A 19 19188 12365 16414 -2061 -2242 481 C
ATOM 893 N GLU A 20 31.972 181.895 151.501 1.00120.39 N
ANISOU 893 N GLU A 20 19713 11392 14638 -2373 -2049 196 N
ATOM 894 CA GLU A 20 32.363 181.433 152.836 1.00122.14 C
ANISOU 894 CA GLU A 20 20339 11456 14612 -2626 -2311 243 C
ATOM 895 C GLU A 20 31.825 180.032 153.115 1.00123.71 C
ANISOU 895 C GLU A 20 20532 11730 14741 -2590 -2244 239 C
ATOM 896 O GLU A 20 32.573 179.191 153.618 1.00124.65 O
ANISOU 896 O GLU A 20 20691 11810 14861 -2726 -2570 372 O
ATOM 897 CB GLU A 20 31.884 182.422 153.919 1.00126.09 C
ANISOU 897 CB GLU A 20 21411 11738 14760 -2806 -2209 112 C
ATOM 898 CG GLU A 20 32.549 183.794 153.852 1.00143.50 C
ANISOU 898 CG GLU A 20 23702 13826 16993 -2897 -2343 130 C
ATOM 899 CD GLU A 20 31.926 184.824 152.919 1.00168.96 C
ANISOU 899 CD GLU A 20 26730 17115 20354 -2692 -2006 19 C
ATOM 900 OE1 GLU A 20 30.760 185.207 153.167 1.00170.57 O
ANISOU 900 OE1 GLU A 20 27151 17259 20397 -2631 -1633 -152 O
ATOM 901 OE2 GLU A 20 32.614 185.288 151.978 1.00158.28 O1-
ANISOU 901 OE2 GLU A 20 25018 15848 19275 -2603 -2115 107 O1-
ATOM 902 N GLU A 21 30.531 179.787 152.789 1.00116.75 N
ANISOU 902 N GLU A 21 19599 10943 13817 -2413 -1834 96 N
ATOM 903 CA GLU A 21 29.843 178.502 152.969 1.00114.92 C
ANISOU 903 CA GLU A 21 19349 10791 13526 -2358 -1707 72 C
ATOM 904 C GLU A 21 30.483 177.448 152.078 1.00115.74 C
ANISOU 904 C GLU A 21 18983 11067 13926 -2237 -1881 212 C
ATOM 905 O GLU A 21 30.774 176.349 152.542 1.00115.96 O
ANISOU 905 O GLU A 21 19048 11092 13921 -2315 -2061 293 O
ATOM 906 CB GLU A 21 28.344 178.625 152.636 1.00115.14 C
ANISOU 906 CB GLU A 21 19344 10878 13525 -2177 -1231 -98 C
ATOM 907 CG GLU A 21 27.517 179.364 153.674 1.00130.87 C
ANISOU 907 CG GLU A 21 21826 12675 15223 -2292 -976 -255 C
ATOM 908 CD GLU A 21 26.153 179.846 153.211 1.00159.30 C
ANISOU 908 CD GLU A 21 25319 16302 18904 -2096 -512 -406 C
ATOM 909 OE1 GLU A 21 25.346 179.005 152.750 1.00164.17 O
ANISOU 909 OE1 GLU A 21 25695 17048 19634 -1940 -318 -429 O
ATOM 910 OE2 GLU A 21 25.875 181.059 153.351 1.00153.26 O1-
ANISOU 910 OE2 GLU A 21 24720 15411 18101 -2106 -348 -498 O1-
ATOM 911 N ARG A 22 30.733 177.805 150.805 1.00109.44 N
ANISOU 911 N ARG A 22 17766 10402 13415 -2058 -1823 242 N
ATOM 912 CA ARG A 22 31.363 176.956 149.798 1.00106.80 C
ANISOU 912 CA ARG A 22 16979 10215 13384 -1932 -1926 359 C
ATOM 913 C ARG A 22 32.721 176.426 150.279 1.00110.91 C
ANISOU 913 C ARG A 22 17476 10653 14012 -2092 -2346 537 C
ATOM 914 O ARG A 22 32.939 175.218 150.199 1.00110.29 O
ANISOU 914 O ARG A 22 17230 10630 14044 -2062 -2435 614 O
ATOM 915 CB ARG A 22 31.510 177.709 148.458 1.00104.08 C
ANISOU 915 CB ARG A 22 16292 9972 13280 -1768 -1804 359 C
ATOM 916 CG ARG A 22 30.247 177.749 147.603 1.00109.04 C
ANISOU 916 CG ARG A 22 16787 10724 13920 -1566 -1437 236 C
ATOM 917 CD ARG A 22 30.508 178.461 146.285 1.00116.64 C
ANISOU 917 CD ARG A 22 17447 11768 15102 -1436 -1366 259 C
ATOM 918 NE ARG A 22 29.460 178.199 145.295 1.00127.81 N
ANISOU 918 NE ARG A 22 18668 13315 16581 -1247 -1092 190 N
ATOM 919 CZ ARG A 22 29.588 178.420 143.989 1.00145.00 C
ANISOU 919 CZ ARG A 22 20561 15590 18944 -1123 -1022 221 C
ATOM 920 NH1 ARG A 22 30.726 178.896 143.497 1.00136.96 N
ANISOU 920 NH1 ARG A 22 19401 14558 18081 -1156 -1167 312 N
ATOM 921 NH2 ARG A 22 28.585 178.154 143.163 1.00130.35 N
ANISOU 921 NH2 ARG A 22 18571 13835 17122 -978 -810 167 N
ATOM 922 N ARG A 23 33.602 177.318 150.825 1.00107.82 N
ANISOU 922 N ARG A 23 17258 10110 13598 -2270 -2613 606 N
ATOM 923 CA ARG A 23 34.945 176.987 151.325 1.00108.62 C
ANISOU 923 CA ARG A 23 17337 10096 13840 -2447 -3060 797 C
ATOM 924 C ARG A 23 34.963 175.787 152.298 1.00113.77 C
ANISOU 924 C ARG A 23 18193 10678 14355 -2580 -3263 864 C
ATOM 925 O ARG A 23 35.707 174.826 152.072 1.00112.73 O
ANISOU 925 O ARG A 23 17780 10566 14485 -2563 -3474 1012 O
ATOM 926 CB ARG A 23 35.629 178.222 151.937 1.00108.63 C
ANISOU 926 CB ARG A 23 17597 9920 13758 -2647 -3299 837 C
ATOM 927 N LEU A 24 34.112 175.819 153.337 1.00112.33 N
ANISOU 927 N LEU A 24 18493 10409 13779 -2704 -3170 752 N
ATOM 928 CA LEU A 24 34.046 174.751 154.335 1.00114.61 C
ANISOU 928 CA LEU A 24 19050 10615 13882 -2854 -3346 806 C
ATOM 929 C LEU A 24 33.314 173.488 153.839 1.00118.77 C
ANISOU 929 C LEU A 24 19341 11307 14478 -2667 -3109 764 C
ATOM 930 O LEU A 24 33.744 172.384 154.186 1.00119.18 O
ANISOU 930 O LEU A 24 19361 11331 14589 -2732 -3343 885 O
ATOM 931 CB LEU A 24 33.488 175.238 155.682 1.00117.15 C
ANISOU 931 CB LEU A 24 20024 10752 13736 -3090 -3332 707 C
ATOM 932 CG LEU A 24 32.255 176.123 155.658 1.00121.35 C
ANISOU 932 CG LEU A 24 20775 11295 14037 -3008 -2865 480 C
ATOM 933 CD1 LEU A 24 31.026 175.349 156.118 1.00121.42 C
ANISOU 933 CD1 LEU A 24 21007 11325 13801 -2979 -2546 349 C
ATOM 934 CD2 LEU A 24 32.475 177.380 156.497 1.00125.52 C
ANISOU 934 CD2 LEU A 24 21776 11610 14306 -3234 -2965 437 C
ATOM 935 N ILE A 25 32.242 173.646 153.015 1.00114.27 N
ANISOU 935 N ILE A 25 18600 10896 13923 -2441 -2673 608 N
ATOM 936 CA ILE A 25 31.479 172.542 152.403 1.00112.27 C
ANISOU 936 CA ILE A 25 18102 10805 13750 -2254 -2431 561 C
ATOM 937 C ILE A 25 32.380 171.753 151.413 1.00116.20 C
ANISOU 937 C ILE A 25 18104 11406 14640 -2129 -2584 704 C
ATOM 938 O ILE A 25 32.242 170.522 151.308 1.00115.45 O
ANISOU 938 O ILE A 25 17885 11369 14613 -2077 -2591 744 O
ATOM 939 CB ILE A 25 30.158 173.035 151.738 1.00113.46 C
ANISOU 939 CB ILE A 25 18192 11072 13847 -2064 -1970 378 C
ATOM 940 CG1 ILE A 25 29.159 173.562 152.784 1.00115.60 C
ANISOU 940 CG1 ILE A 25 18944 11219 13760 -2178 -1759 233 C
ATOM 941 CG2 ILE A 25 29.507 171.926 150.917 1.00112.25 C
ANISOU 941 CG2 ILE A 25 17726 11090 13833 -1869 -1768 356 C
ATOM 942 CD1 ILE A 25 27.995 174.461 152.179 1.00124.08 C
ANISOU 942 CD1 ILE A 25 19959 12348 14836 -2010 -1333 66 C
ATOM 943 N ALA A 26 33.301 172.471 150.701 1.00112.95 N
ANISOU 943 N ALA A 26 17425 11000 14491 -2089 -2690 778 N
ATOM 944 CA ALA A 26 34.268 171.892 149.757 1.00112.28 C
ANISOU 944 CA ALA A 26 16880 10974 14806 -1984 -2801 911 C
ATOM 945 C ALA A 26 35.171 170.885 150.477 1.00119.39 C
ANISOU 945 C ALA A 26 17778 11759 15827 -2121 -3175 1085 C
ATOM 946 O ALA A 26 35.895 171.246 151.413 1.00122.61 O
ANISOU 946 O ALA A 26 18404 11996 16185 -2334 -3524 1193 O
ATOM 947 CB ALA A 26 35.104 172.983 149.098 1.00113.03 C
ANISOU 947 CB ALA A 26 16776 11048 15122 -1969 -2859 961 C
ATOM 948 N SER A 27 35.053 169.607 150.082 1.00114.42 N
ANISOU 948 N SER A 27 16930 11208 15337 -2010 -3108 1113 N
ATOM 949 CA SER A 27 35.799 168.484 150.643 1.00115.67 C
ANISOU 949 CA SER A 27 17038 11263 15647 -2105 -3427 1279 C
ATOM 950 C SER A 27 36.048 167.404 149.561 1.00117.21 C
ANISOU 950 C SER A 27 16781 11557 16194 -1908 -3292 1321 C
ATOM 951 O SER A 27 35.336 166.392 149.523 1.00115.37 O
ANISOU 951 O SER A 27 16562 11401 15871 -1833 -3143 1265 O
ATOM 952 CB SER A 27 35.093 167.921 151.881 1.00120.52 C
ANISOU 952 CB SER A 27 18091 11814 15888 -2253 -3502 1244 C
ATOM 953 OG SER A 27 33.681 168.056 151.806 1.00127.64 O
ANISOU 953 OG SER A 27 19168 12838 16492 -2159 -3109 1043 O
ATOM 954 N PRO A 28 37.035 167.622 148.644 1.00113.06 N
ANISOU 954 N PRO A 28 15864 11021 16071 -1825 -3312 1411 N
ATOM 955 CA PRO A 28 37.293 166.616 147.599 1.00111.79 C
ANISOU 955 CA PRO A 28 15307 10929 16241 -1647 -3142 1439 C
ATOM 956 C PRO A 28 37.794 165.293 148.163 1.00117.71 C
ANISOU 956 C PRO A 28 15985 11571 17167 -1700 -3390 1583 C
ATOM 957 O PRO A 28 37.378 164.231 147.727 1.00115.83 O
ANISOU 957 O PRO A 28 15626 11407 16976 -1579 -3212 1544 O
ATOM 958 CB PRO A 28 38.337 167.296 146.696 1.00113.62 C
ANISOU 958 CB PRO A 28 15197 11124 16849 -1592 -3123 1512 C
ATOM 959 CG PRO A 28 38.987 168.301 147.538 1.00119.27 C
ANISOU 959 CG PRO A 28 16077 11701 17541 -1782 -3451 1606 C
ATOM 960 CD PRO A 28 37.957 168.772 148.515 1.00114.83 C
ANISOU 960 CD PRO A 28 15999 11159 16473 -1896 -3468 1489 C
ATOM 961 N TRP A 29 38.646 165.378 149.172 1.00118.32 N
ANISOU 961 N TRP A 29 16163 11464 17328 -1894 -3821 1752 N
ATOM 962 CA TRP A 29 39.261 164.237 149.809 1.00120.09 C
ANISOU 962 CA TRP A 29 16325 11547 17758 -1975 -4138 1927 C
ATOM 963 C TRP A 29 38.300 163.334 150.511 1.00123.90 C
ANISOU 963 C TRP A 29 17113 12070 17895 -2012 -4115 1861 C
ATOM 964 O TRP A 29 38.549 162.139 150.514 1.00124.18 O
ANISOU 964 O TRP A 29 16986 12061 18137 -1971 -4189 1950 O
ATOM 965 CB TRP A 29 40.376 164.694 150.730 1.00121.89 C
ANISOU 965 CB TRP A 29 16613 11551 18147 -2199 -4647 2138 C
ATOM 966 CG TRP A 29 41.644 164.879 149.966 1.00123.71 C
ANISOU 966 CG TRP A 29 16359 11691 18953 -2133 -4716 2283 C
ATOM 967 CD1 TRP A 29 42.306 166.049 149.741 1.00127.23 C
ANISOU 967 CD1 TRP A 29 16713 12086 19542 -2183 -4788 2323 C
ATOM 968 CD2 TRP A 29 42.336 163.873 149.213 1.00123.97 C
ANISOU 968 CD2 TRP A 29 15921 11676 19506 -1986 -4646 2387 C
ATOM 969 NE1 TRP A 29 43.410 165.824 148.949 1.00127.71 N
ANISOU 969 NE1 TRP A 29 16269 12061 20196 -2088 -4784 2459 N
ATOM 970 CE2 TRP A 29 43.449 164.497 148.605 1.00129.10 C
ANISOU 970 CE2 TRP A 29 16204 12231 20618 -1964 -4683 2497 C
ATOM 971 CE3 TRP A 29 42.145 162.488 149.027 1.00124.69 C
ANISOU 971 CE3 TRP A 29 15870 11776 19731 -1879 -4552 2401 C
ATOM 972 CZ2 TRP A 29 44.365 163.789 147.815 1.00129.47 C
ANISOU 972 CZ2 TRP A 29 15745 12181 21264 -1834 -4599 2614 C
ATOM 973 CZ3 TRP A 29 43.051 161.789 148.247 1.00127.18 C
ANISOU 973 CZ3 TRP A 29 15697 11998 20629 -1750 -4482 2515 C
ATOM 974 CH2 TRP A 29 44.144 162.435 147.648 1.00129.26 C
ANISOU 974 CH2 TRP A 29 15600 12158 21356 -1726 -4491 2617 C
ATOM 975 N PHE A 30 37.201 163.874 151.075 1.00120.66 N
ANISOU 975 N PHE A 30 17127 11731 16986 -2082 -3985 1705 N
ATOM 976 CA PHE A 30 36.164 163.069 151.722 1.00120.90 C
ANISOU 976 CA PHE A 30 17462 11804 16672 -2116 -3899 1623 C
ATOM 977 C PHE A 30 35.274 162.413 150.622 1.00120.29 C
ANISOU 977 C PHE A 30 17156 11925 16623 -1872 -3455 1473 C
ATOM 978 O PHE A 30 34.891 161.226 150.730 1.00119.95 O
ANISOU 978 O PHE A 30 17104 11903 16570 -1834 -3419 1479 O
ATOM 979 CB PHE A 30 35.331 163.904 152.734 1.00124.39 C
ANISOU 979 CB PHE A 30 18439 12221 16601 -2284 -3880 1508 C
ATOM 980 CG PHE A 30 33.942 163.349 152.978 1.00126.59 C
ANISOU 980 CG PHE A 30 18964 12605 16531 -2243 -3574 1345 C
ATOM 981 CD1 PHE A 30 33.758 162.194 153.743 1.00131.98 C
ANISOU 981 CD1 PHE A 30 19823 13220 17102 -2336 -3716 1408 C
ATOM 982 CD2 PHE A 30 32.828 163.915 152.356 1.00128.42 C
ANISOU 982 CD2 PHE A 30 19208 12995 16592 -2100 -3144 1143 C
ATOM 983 CE1 PHE A 30 32.485 161.624 153.894 1.00132.14 C
ANISOU 983 CE1 PHE A 30 20029 13337 16840 -2289 -3413 1263 C
ATOM 984 CE2 PHE A 30 31.552 163.346 152.510 1.00130.91 C
ANISOU 984 CE2 PHE A 30 19690 13397 16653 -2051 -2856 1007 C
ATOM 985 CZ PHE A 30 31.390 162.205 153.283 1.00129.95 C
ANISOU 985 CZ PHE A 30 19743 13213 16420 -2147 -2983 1065 C
ATOM 986 N ALA A 31 34.937 163.209 149.578 1.00111.63 N
ANISOU 986 N ALA A 31 15897 10964 15555 -1721 -3138 1347 N
ATOM 987 CA ALA A 31 34.130 162.763 148.448 1.00107.01 C
ANISOU 987 CA ALA A 31 15115 10553 14990 -1511 -2745 1213 C
ATOM 988 C ALA A 31 34.845 161.600 147.777 1.00108.17 C
ANISOU 988 C ALA A 31 14900 10678 15522 -1404 -2759 1312 C
ATOM 989 O ALA A 31 34.227 160.565 147.549 1.00106.59 O
ANISOU 989 O ALA A 31 14668 10550 15282 -1318 -2596 1258 O
ATOM 990 CB ALA A 31 33.920 163.907 147.471 1.00106.00 C
ANISOU 990 CB ALA A 31 14879 10528 14867 -1406 -2493 1105 C
ATOM 991 N ALA A 32 36.169 161.741 147.572 1.00104.96 N
ANISOU 991 N ALA A 32 14233 10147 15500 -1425 -2966 1466 N
ATOM 992 CA ALA A 32 37.060 160.736 146.994 1.00105.17 C
ANISOU 992 CA ALA A 32 13890 10098 15971 -1334 -2988 1581 C
ATOM 993 C ALA A 32 37.050 159.472 147.839 1.00110.47 C
ANISOU 993 C ALA A 32 14649 10679 16646 -1405 -3210 1678 C
ATOM 994 O ALA A 32 36.878 158.378 147.303 1.00109.20 O
ANISOU 994 O ALA A 32 14321 10547 16624 -1286 -3050 1662 O
ATOM 995 CB ALA A 32 38.477 161.288 146.901 1.00107.69 C
ANISOU 995 CB ALA A 32 13945 10265 16707 -1379 -3203 1744 C
ATOM 996 N SER A 33 37.210 159.634 149.166 1.00109.16 N
ANISOU 996 N SER A 33 14778 10393 16306 -1611 -3581 1777 N
ATOM 997 CA SER A 33 37.227 158.561 150.150 1.00110.41 C
ANISOU 997 CA SER A 33 15094 10439 16418 -1725 -3858 1889 C
ATOM 998 C SER A 33 35.950 157.739 150.052 1.00114.54 C
ANISOU 998 C SER A 33 15772 11105 16642 -1644 -3572 1736 C
ATOM 999 O SER A 33 36.022 156.524 149.872 1.00113.43 O
ANISOU 999 O SER A 33 15480 10937 16680 -1577 -3565 1787 O
ATOM 1000 CB SER A 33 37.410 159.131 151.554 1.00113.89 C
ANISOU 1000 CB SER A 33 15936 10743 16595 -1987 -4255 1981 C
ATOM 1001 OG SER A 33 38.701 159.693 151.716 1.00118.26 O
ANISOU 1001 OG SER A 33 16326 11128 17481 -2086 -4603 2165 O
ATOM 1002 N PHE A 34 34.793 158.420 150.083 1.00112.27 N
ANISOU 1002 N PHE A 34 15752 10962 15943 -1638 -3316 1551 N
ATOM 1003 CA PHE A 34 33.472 157.810 149.986 1.00111.94 C
ANISOU 1003 CA PHE A 34 15861 11058 15614 -1568 -3024 1398 C
ATOM 1004 C PHE A 34 33.282 157.068 148.662 1.00112.26 C
ANISOU 1004 C PHE A 34 15559 11213 15882 -1350 -2720 1332 C
ATOM 1005 O PHE A 34 32.790 155.943 148.643 1.00111.53 O
ANISOU 1005 O PHE A 34 15468 11148 15761 -1306 -2640 1313 O
ATOM 1006 CB PHE A 34 32.411 158.895 150.152 1.00114.19 C
ANISOU 1006 CB PHE A 34 16430 11446 15513 -1594 -2804 1228 C
ATOM 1007 CG PHE A 34 31.302 158.510 151.098 1.00117.74 C
ANISOU 1007 CG PHE A 34 17264 11903 15570 -1696 -2741 1149 C
ATOM 1008 CD1 PHE A 34 31.500 158.537 152.476 1.00124.28 C
ANISOU 1008 CD1 PHE A 34 18467 12576 16177 -1925 -3033 1232 C
ATOM 1009 CD2 PHE A 34 30.051 158.134 150.613 1.00119.04 C
ANISOU 1009 CD2 PHE A 34 17431 12213 15584 -1577 -2386 996 C
ATOM 1010 CE1 PHE A 34 30.470 158.189 153.352 1.00125.95 C
ANISOU 1010 CE1 PHE A 34 19062 12779 16015 -2031 -2933 1152 C
ATOM 1011 CE2 PHE A 34 29.019 157.798 151.492 1.00122.68 C
ANISOU 1011 CE2 PHE A 34 18235 12668 15711 -1673 -2296 923 C
ATOM 1012 CZ PHE A 34 29.235 157.839 152.853 1.00123.23 C
ANISOU 1012 CZ PHE A 34 18686 12582 15554 -1898 -2549 995 C
ATOM 1013 N CYS A 35 33.723 157.693 147.575 1.00107.07 N
ANISOU 1013 N CYS A 35 14628 10603 15449 -1231 -2560 1304 N
ATOM 1014 CA CYS A 35 33.708 157.185 146.213 1.00105.62 C
ANISOU 1014 CA CYS A 35 14143 10500 15486 -1045 -2268 1244 C
ATOM 1015 C CYS A 35 34.532 155.880 146.116 1.00106.82 C
ANISOU 1015 C CYS A 35 14064 10528 15993 -1009 -2382 1374 C
ATOM 1016 O CYS A 35 33.992 154.862 145.692 1.00104.63 O
ANISOU 1016 O CYS A 35 13754 10304 15697 -925 -2209 1316 O
ATOM 1017 CB CYS A 35 34.239 158.268 145.277 1.00106.97 C
ANISOU 1017 CB CYS A 35 14117 10697 15829 -975 -2140 1222 C
ATOM 1018 SG CYS A 35 34.243 157.816 143.530 1.00110.18 S
ANISOU 1018 SG CYS A 35 14235 11191 16436 -776 -1743 1129 S
ATOM 1019 N VAL A 36 35.813 155.909 146.583 1.00103.69 N
ANISOU 1019 N VAL A 36 13518 9951 15927 -1085 -2693 1559 N
ATOM 1020 CA VAL A 36 36.774 154.788 146.646 1.00103.89 C
ANISOU 1020 CA VAL A 36 13294 9805 16374 -1067 -2865 1722 C
ATOM 1021 C VAL A 36 36.205 153.599 147.451 1.00106.14 C
ANISOU 1021 C VAL A 36 13773 10067 16487 -1124 -2989 1748 C
ATOM 1022 O VAL A 36 36.326 152.455 147.017 1.00105.68 O
ANISOU 1022 O VAL A 36 13537 9971 16646 -1026 -2887 1765 O
ATOM 1023 CB VAL A 36 38.151 155.289 147.163 1.00109.40 C
ANISOU 1023 CB VAL A 36 13835 10303 17429 -1175 -3236 1930 C
ATOM 1024 CG1 VAL A 36 38.963 154.194 147.858 1.00111.56 C
ANISOU 1024 CG1 VAL A 36 13980 10364 18042 -1235 -3575 2140 C
ATOM 1025 CG2 VAL A 36 38.945 155.918 146.030 1.00109.06 C
ANISOU 1025 CG2 VAL A 36 13448 10243 17746 -1062 -3034 1927 C
ATOM 1026 N VAL A 37 35.563 153.895 148.599 1.00101.30 N
ANISOU 1026 N VAL A 37 13545 9468 15474 -1287 -3182 1740 N
ATOM 1027 CA VAL A 37 34.882 152.944 149.473 1.00100.66 C
ANISOU 1027 CA VAL A 37 13731 9372 15143 -1374 -3287 1750 C
ATOM 1028 C VAL A 37 33.779 152.250 148.647 1.00101.91 C
ANISOU 1028 C VAL A 37 13866 9700 15156 -1222 -2887 1575 C
ATOM 1029 O VAL A 37 33.708 151.021 148.631 1.00101.55 O
ANISOU 1029 O VAL A 37 13759 9613 15211 -1184 -2888 1611 O
ATOM 1030 CB VAL A 37 34.327 153.676 150.730 1.00105.12 C
ANISOU 1030 CB VAL A 37 14755 9929 15256 -1581 -3472 1733 C
ATOM 1031 CG1 VAL A 37 33.203 152.895 151.403 1.00104.56 C
ANISOU 1031 CG1 VAL A 37 15008 9904 14818 -1647 -3407 1663 C
ATOM 1032 CG2 VAL A 37 35.435 153.962 151.728 1.00108.02 C
ANISOU 1032 CG2 VAL A 37 15197 10082 15761 -1773 -3958 1945 C
ATOM 1033 N GLY A 38 32.974 153.046 147.936 1.00 95.77 N
ANISOU 1033 N GLY A 38 13123 9095 14171 -1140 -2570 1401 N
ATOM 1034 CA GLY A 38 31.899 152.544 147.086 1.00 92.47 C
ANISOU 1034 CA GLY A 38 12685 8833 13618 -1010 -2214 1241 C
ATOM 1035 C GLY A 38 32.394 151.607 146.002 1.00 92.29 C
ANISOU 1035 C GLY A 38 12343 8783 13939 -861 -2060 1255 C
ATOM 1036 O GLY A 38 31.889 150.496 145.881 1.00 90.72 O
ANISOU 1036 O GLY A 38 12156 8604 13710 -818 -1963 1223 O
ATOM 1037 N LEU A 39 33.428 152.039 145.246 1.00 86.97 N
ANISOU 1037 N LEU A 39 11393 8044 13607 -792 -2032 1307 N
ATOM 1038 CA LEU A 39 34.066 151.295 144.157 1.00 85.47 C
ANISOU 1038 CA LEU A 39 10898 7793 13785 -655 -1842 1317 C
ATOM 1039 C LEU A 39 34.687 149.994 144.666 1.00 90.09 C
ANISOU 1039 C LEU A 39 11371 8207 14652 -666 -2031 1458 C
ATOM 1040 O LEU A 39 34.340 148.909 144.167 1.00 90.62 O
ANISOU 1040 O LEU A 39 11385 8277 14771 -581 -1850 1408 O
ATOM 1041 CB LEU A 39 35.115 152.166 143.449 1.00 85.86 C
ANISOU 1041 CB LEU A 39 10700 7780 14145 -607 -1784 1357 C
ATOM 1042 CG LEU A 39 34.639 153.536 142.950 1.00 88.67 C
ANISOU 1042 CG LEU A 39 11146 8282 14261 -598 -1616 1235 C
ATOM 1043 CD1 LEU A 39 35.796 154.434 142.607 1.00 89.01 C
ANISOU 1043 CD1 LEU A 39 10971 8233 14614 -592 -1647 1312 C
ATOM 1044 CD2 LEU A 39 33.669 153.406 141.804 1.00 89.72 C
ANISOU 1044 CD2 LEU A 39 11320 8564 14207 -494 -1252 1065 C
ATOM 1045 N ALA A 40 35.562 150.093 145.689 1.00 85.79 N
ANISOU 1045 N ALA A 40 10811 7504 14283 -781 -2414 1640 N
ATOM 1046 CA ALA A 40 36.187 148.944 146.325 1.00 86.01 C
ANISOU 1046 CA ALA A 40 10746 7343 14592 -817 -2672 1808 C
ATOM 1047 C ALA A 40 35.109 147.872 146.640 1.00 90.79 C
ANISOU 1047 C ALA A 40 11572 8020 14904 -825 -2609 1736 C
ATOM 1048 O ALA A 40 35.229 146.758 146.132 1.00 91.37 O
ANISOU 1048 O ALA A 40 11483 8029 15205 -727 -2484 1743 O
ATOM 1049 CB ALA A 40 36.907 149.377 147.587 1.00 88.09 C
ANISOU 1049 CB ALA A 40 11099 7458 14914 -995 -3148 2001 C
ATOM 1050 N SER A 41 34.017 148.247 147.375 1.00 86.67 N
ANISOU 1050 N SER A 41 11414 7632 13885 -933 -2642 1650 N
ATOM 1051 CA SER A 41 32.887 147.386 147.757 1.00 85.89 C
ANISOU 1051 CA SER A 41 11556 7610 13467 -963 -2571 1575 C
ATOM 1052 C SER A 41 32.334 146.640 146.561 1.00 92.80 C
ANISOU 1052 C SER A 41 12292 8579 14390 -802 -2206 1443 C
ATOM 1053 O SER A 41 32.161 145.408 146.622 1.00 95.23 O
ANISOU 1053 O SER A 41 12596 8833 14753 -782 -2203 1466 O
ATOM 1054 CB SER A 41 31.744 148.209 148.344 1.00 86.67 C
ANISOU 1054 CB SER A 41 12005 7857 13069 -1062 -2515 1457 C
ATOM 1055 OG SER A 41 32.141 148.999 149.448 1.00 98.28 O
ANISOU 1055 OG SER A 41 13682 9239 14423 -1234 -2829 1557 O
ATOM 1056 N ASN A 42 32.032 147.396 145.474 1.00 87.04 N
ANISOU 1056 N ASN A 42 11472 7978 13620 -700 -1908 1305 N
ATOM 1057 CA ASN A 42 31.470 146.840 144.250 1.00 84.94 C
ANISOU 1057 CA ASN A 42 11118 7799 13358 -570 -1562 1171 C
ATOM 1058 C ASN A 42 32.452 145.865 143.605 1.00 89.64 C
ANISOU 1058 C ASN A 42 11436 8230 14393 -471 -1502 1242 C
ATOM 1059 O ASN A 42 32.078 144.706 143.347 1.00 87.89 O
ANISOU 1059 O ASN A 42 11219 7989 14188 -426 -1393 1210 O
ATOM 1060 CB ASN A 42 30.951 147.932 143.308 1.00 79.96 C
ANISOU 1060 CB ASN A 42 10495 7324 12563 -513 -1306 1028 C
ATOM 1061 CG ASN A 42 29.579 148.408 143.731 1.00 98.18 C
ANISOU 1061 CG ASN A 42 13068 9795 14443 -574 -1259 921 C
ATOM 1062 OD1 ASN A 42 28.566 147.728 143.540 1.00 94.80 O
ANISOU 1062 OD1 ASN A 42 12735 9445 13840 -557 -1120 837 O
ATOM 1063 ND2 ASN A 42 29.518 149.540 144.410 1.00 89.40 N
ANISOU 1063 ND2 ASN A 42 12085 8712 13169 -657 -1382 931 N
ATOM 1064 N LEU A 43 33.734 146.284 143.472 1.00 87.39 N
ANISOU 1064 N LEU A 43 10913 7805 14488 -450 -1593 1354 N
ATOM 1065 CA LEU A 43 34.778 145.399 142.947 1.00 89.08 C
ANISOU 1065 CA LEU A 43 10831 7820 15194 -357 -1530 1439 C
ATOM 1066 C LEU A 43 34.896 144.107 143.782 1.00 94.20 C
ANISOU 1066 C LEU A 43 11490 8329 15973 -394 -1759 1562 C
ATOM 1067 O LEU A 43 35.056 143.015 143.228 1.00 93.43 O
ANISOU 1067 O LEU A 43 11256 8127 16116 -303 -1597 1556 O
ATOM 1068 CB LEU A 43 36.111 146.145 142.820 1.00 90.60 C
ANISOU 1068 CB LEU A 43 10756 7872 15795 -344 -1615 1557 C
ATOM 1069 CG LEU A 43 36.656 146.310 141.387 1.00 95.17 C
ANISOU 1069 CG LEU A 43 11101 8407 16650 -212 -1225 1476 C
ATOM 1070 CD1 LEU A 43 35.547 146.655 140.367 1.00 92.43 C
ANISOU 1070 CD1 LEU A 43 10949 8272 15899 -167 -872 1257 C
ATOM 1071 CD2 LEU A 43 37.746 147.360 141.339 1.00 99.07 C
ANISOU 1071 CD2 LEU A 43 11382 8811 17450 -223 -1304 1572 C
ATOM 1072 N LEU A 44 34.697 144.238 145.100 1.00 92.32 N
ANISOU 1072 N LEU A 44 11461 8094 15523 -538 -2112 1657 N
ATOM 1073 CA LEU A 44 34.676 143.124 146.022 1.00 94.54 C
ANISOU 1073 CA LEU A 44 11825 8257 15840 -608 -2368 1777 C
ATOM 1074 C LEU A 44 33.472 142.217 145.721 1.00100.43 C
ANISOU 1074 C LEU A 44 12745 9123 16292 -572 -2138 1636 C
ATOM 1075 O LEU A 44 33.618 140.993 145.759 1.00102.40 O
ANISOU 1075 O LEU A 44 12927 9249 16730 -540 -2165 1694 O
ATOM 1076 CB LEU A 44 34.645 143.618 147.483 1.00 95.21 C
ANISOU 1076 CB LEU A 44 12164 8316 15694 -803 -2786 1900 C
ATOM 1077 CG LEU A 44 34.677 142.536 148.582 1.00100.48 C
ANISOU 1077 CG LEU A 44 12969 8839 16370 -915 -3116 2053 C
ATOM 1078 CD1 LEU A 44 35.901 141.657 148.460 1.00102.27 C
ANISOU 1078 CD1 LEU A 44 12855 8809 17193 -850 -3272 2237 C
ATOM 1079 CD2 LEU A 44 34.622 143.159 149.957 1.00103.78 C
ANISOU 1079 CD2 LEU A 44 13703 9229 16502 -1132 -3501 2157 C
ATOM 1080 N ALA A 45 32.296 142.802 145.412 1.00 94.64 N
ANISOU 1080 N ALA A 45 12218 8611 15128 -578 -1923 1459 N
ATOM 1081 CA ALA A 45 31.130 141.979 145.106 1.00 92.68 C
ANISOU 1081 CA ALA A 45 12119 8472 14625 -553 -1718 1334 C
ATOM 1082 C ALA A 45 31.402 141.178 143.851 1.00 95.18 C
ANISOU 1082 C ALA A 45 12229 8730 15206 -409 -1430 1269 C
ATOM 1083 O ALA A 45 31.199 139.978 143.874 1.00 94.15 O
ANISOU 1083 O ALA A 45 12115 8534 15123 -390 -1405 1277 O
ATOM 1084 CB ALA A 45 29.901 142.843 144.921 1.00 91.31 C
ANISOU 1084 CB ALA A 45 12153 8521 14019 -581 -1548 1175 C
ATOM 1085 N LEU A 46 31.927 141.827 142.781 1.00 92.41 N
ANISOU 1085 N LEU A 46 11698 8380 15033 -315 -1210 1210 N
ATOM 1086 CA LEU A 46 32.256 141.183 141.500 1.00 92.36 C
ANISOU 1086 CA LEU A 46 11528 8295 15268 -190 -888 1135 C
ATOM 1087 C LEU A 46 33.305 140.105 141.720 1.00100.24 C
ANISOU 1087 C LEU A 46 12312 9041 16734 -143 -979 1275 C
ATOM 1088 O LEU A 46 33.193 139.029 141.123 1.00100.88 O
ANISOU 1088 O LEU A 46 12365 9044 16920 -75 -777 1221 O
ATOM 1089 CB LEU A 46 32.706 142.195 140.422 1.00 91.73 C
ANISOU 1089 CB LEU A 46 11327 8244 15281 -125 -650 1061 C
ATOM 1090 CG LEU A 46 31.636 143.208 139.950 1.00 93.71 C
ANISOU 1090 CG LEU A 46 11774 8728 15105 -153 -511 912 C
ATOM 1091 CD1 LEU A 46 32.239 144.536 139.569 1.00 92.53 C
ANISOU 1091 CD1 LEU A 46 11523 8599 15034 -141 -469 913 C
ATOM 1092 CD2 LEU A 46 30.757 142.649 138.829 1.00 95.67 C
ANISOU 1092 CD2 LEU A 46 12135 9045 15170 -109 -204 756 C
ATOM 1093 N SER A 47 34.284 140.364 142.630 1.00 98.14 N
ANISOU 1093 N SER A 47 11906 8634 16749 -192 -1307 1463 N
ATOM 1094 CA SER A 47 35.317 139.398 143.021 1.00 99.99 C
ANISOU 1094 CA SER A 47 11914 8603 17476 -163 -1477 1639 C
ATOM 1095 C SER A 47 34.619 138.105 143.548 1.00102.97 C
ANISOU 1095 C SER A 47 12458 8961 17706 -198 -1569 1651 C
ATOM 1096 O SER A 47 34.830 137.023 142.997 1.00103.01 O
ANISOU 1096 O SER A 47 12342 8825 17972 -107 -1396 1641 O
ATOM 1097 CB SER A 47 36.255 140.018 144.057 1.00104.55 C
ANISOU 1097 CB SER A 47 12379 9059 18284 -253 -1892 1849 C
ATOM 1098 OG SER A 47 37.056 139.071 144.747 1.00116.49 O
ANISOU 1098 OG SER A 47 13728 10320 20211 -267 -2176 2054 O
ATOM 1099 N VAL A 48 33.712 138.257 144.534 1.00 98.45 N
ANISOU 1099 N VAL A 48 12182 8532 16692 -330 -1792 1652 N
ATOM 1100 CA VAL A 48 32.902 137.183 145.124 1.00 98.20 C
ANISOU 1100 CA VAL A 48 12357 8510 16443 -389 -1882 1656 C
ATOM 1101 C VAL A 48 32.050 136.490 144.043 1.00103.97 C
ANISOU 1101 C VAL A 48 13143 9333 17030 -299 -1497 1469 C
ATOM 1102 O VAL A 48 31.986 135.260 144.007 1.00104.47 O
ANISOU 1102 O VAL A 48 13196 9286 17213 -270 -1471 1490 O
ATOM 1103 CB VAL A 48 32.027 137.712 146.296 1.00 99.97 C
ANISOU 1103 CB VAL A 48 12914 8882 16188 -558 -2121 1665 C
ATOM 1104 CG1 VAL A 48 31.124 136.622 146.858 1.00 99.28 C
ANISOU 1104 CG1 VAL A 48 13051 8810 15861 -625 -2169 1658 C
ATOM 1105 CG2 VAL A 48 32.887 138.318 147.400 1.00101.33 C
ANISOU 1105 CG2 VAL A 48 13087 8934 16479 -676 -2532 1858 C
ATOM 1106 N LEU A 49 31.423 137.284 143.158 1.00101.50 N
ANISOU 1106 N LEU A 49 12894 9206 16466 -264 -1219 1297 N
ATOM 1107 CA LEU A 49 30.581 136.791 142.070 1.00101.23 C
ANISOU 1107 CA LEU A 49 12944 9264 16256 -203 -879 1120 C
ATOM 1108 C LEU A 49 31.368 135.953 141.090 1.00111.00 C
ANISOU 1108 C LEU A 49 13984 10309 17880 -83 -636 1103 C
ATOM 1109 O LEU A 49 30.847 134.945 140.618 1.00111.09 O
ANISOU 1109 O LEU A 49 14080 10298 17830 -59 -473 1025 O
ATOM 1110 CB LEU A 49 29.875 137.940 141.339 1.00 98.93 C
ANISOU 1110 CB LEU A 49 12748 9182 15661 -204 -686 972 C
ATOM 1111 CG LEU A 49 28.358 137.882 141.359 1.00101.25 C
ANISOU 1111 CG LEU A 49 13288 9671 15512 -266 -620 854 C
ATOM 1112 CD1 LEU A 49 27.755 139.209 140.988 1.00 98.83 C
ANISOU 1112 CD1 LEU A 49 13057 9550 14943 -287 -542 762 C
ATOM 1113 CD2 LEU A 49 27.834 136.765 140.475 1.00104.89 C
ANISOU 1113 CD2 LEU A 49 13795 10104 15952 -221 -386 753 C
ATOM 1114 N ALA A 50 32.635 136.340 140.828 1.00111.77 N
ANISOU 1114 N ALA A 50 13823 10251 18395 -13 -606 1179 N
ATOM 1115 CA ALA A 50 33.553 135.645 139.927 1.00114.88 C
ANISOU 1115 CA ALA A 50 13997 10418 19233 106 -337 1171 C
ATOM 1116 C ALA A 50 33.822 134.209 140.367 1.00123.63 C
ANISOU 1116 C ALA A 50 15032 11318 20624 132 -436 1273 C
ATOM 1117 O ALA A 50 33.938 133.332 139.511 1.00123.73 O
ANISOU 1117 O ALA A 50 14996 11192 20826 217 -140 1198 O
ATOM 1118 CB ALA A 50 34.854 136.415 139.808 1.00117.29 C
ANISOU 1118 CB ALA A 50 14020 10590 19955 158 -334 1264 C
ATOM 1119 N GLY A 51 33.885 133.990 141.683 1.00124.42 N
ANISOU 1119 N GLY A 51 15154 11390 20729 47 -847 1438 N
ATOM 1120 CA GLY A 51 34.078 132.675 142.291 1.00128.16 C
ANISOU 1120 CA GLY A 51 15588 11674 21433 46 -1021 1562 C
ATOM 1121 C GLY A 51 32.820 131.823 142.297 1.00135.95 C
ANISOU 1121 C GLY A 51 16854 12780 22020 -1 -958 1455 C
ATOM 1122 O GLY A 51 32.882 130.619 142.020 1.00136.93 O
ANISOU 1122 O GLY A 51 16947 12749 22333 51 -858 1456 O
ATOM 1123 N ALA A 52 31.658 132.453 142.600 1.00133.79 N
ANISOU 1123 N ALA A 52 16849 12774 21211 -101 -1003 1361 N
ATOM 1124 CA ALA A 52 30.332 131.816 142.647 1.00133.42 C
ANISOU 1124 CA ALA A 52 17069 12869 20758 -163 -944 1257 C
ATOM 1125 C ALA A 52 29.797 131.421 141.257 1.00138.44 C
ANISOU 1125 C ALA A 52 17751 13535 21316 -87 -543 1067 C
ATOM 1126 O ALA A 52 29.304 130.297 141.099 1.00139.11 O
ANISOU 1126 O ALA A 52 17927 13563 21366 -87 -471 1032 O
ATOM 1127 CB ALA A 52 29.332 132.724 143.355 1.00132.20 C
ANISOU 1127 CB ALA A 52 17143 12961 20125 -283 -1075 1217 C
ATOM 1128 N ARG A 53 29.885 132.342 140.263 1.00134.03 N
ANISOU 1128 N ARG A 53 17153 13056 20717 -38 -296 951 N
ATOM 1129 CA ARG A 53 29.418 132.125 138.890 1.00163.03 C
ANISOU 1129 CA ARG A 53 20915 16749 24281 7 71 774 C
ATOM 1130 C ARG A 53 30.467 132.536 137.845 1.00177.95 C
ANISOU 1130 C ARG A 53 22636 18521 26457 102 346 728 C
ATOM 1131 O ARG A 53 30.649 133.721 137.558 1.00131.27 O
ANISOU 1131 O ARG A 53 16699 12722 20456 95 369 702 O
ATOM 1132 CB ARG A 53 28.080 132.844 138.653 1.00161.05 C
ANISOU 1132 CB ARG A 53 20904 16763 23525 -77 102 650 C
ATOM 1133 N ARG A 60 25.684 131.499 136.730 1.00120.42 N
ANISOU 1133 N ARG A 60 16218 11777 17758 -171 489 344 N
ATOM 1134 CA ARG A 60 24.809 130.909 135.707 1.00120.39 C
ANISOU 1134 CA ARG A 60 16417 11788 17537 -217 675 214 C
ATOM 1135 C ARG A 60 23.275 131.202 135.926 1.00122.21 C
ANISOU 1135 C ARG A 60 16810 12239 17385 -327 542 180 C
ATOM 1136 O ARG A 60 22.482 131.016 134.987 1.00121.66 O
ANISOU 1136 O ARG A 60 16908 12204 17113 -384 655 81 O
ATOM 1137 CB ARG A 60 25.083 129.388 135.524 1.00122.54 C
ANISOU 1137 CB ARG A 60 16722 11845 17991 -188 791 202 C
ATOM 1138 CG ARG A 60 25.057 128.549 136.807 1.00130.46 C
ANISOU 1138 CG ARG A 60 17659 12790 19121 -193 560 327 C
ATOM 1139 CD ARG A 60 24.466 127.155 136.615 1.00136.24 C
ANISOU 1139 CD ARG A 60 18540 13431 19794 -231 616 284 C
ATOM 1140 NE ARG A 60 23.050 127.171 136.221 1.00143.39 N
ANISOU 1140 NE ARG A 60 19657 14513 20313 -342 599 200 N
ATOM 1141 CZ ARG A 60 22.022 127.336 137.054 1.00157.70 C
ANISOU 1141 CZ ARG A 60 21518 16490 21910 -426 387 249 C
ATOM 1142 NH1 ARG A 60 22.232 127.518 138.354 1.00146.89 N
ANISOU 1142 NH1 ARG A 60 20050 15141 20622 -425 171 375 N
ATOM 1143 NH2 ARG A 60 20.776 127.332 136.591 1.00139.26 N
ANISOU 1143 NH2 ARG A 60 19341 14287 19286 -522 392 178 N
ATOM 1144 N SER A 61 22.884 131.694 137.149 1.00115.79 N
ANISOU 1144 N SER A 61 15952 11556 16486 -364 309 266 N
ATOM 1145 CA SER A 61 21.507 132.044 137.551 1.00112.02 C
ANISOU 1145 CA SER A 61 15586 11267 15712 -459 202 250 C
ATOM 1146 C SER A 61 20.999 133.312 136.864 1.00111.24 C
ANISOU 1146 C SER A 61 15510 11313 15442 -477 260 182 C
ATOM 1147 O SER A 61 21.808 134.175 136.501 1.00111.53 O
ANISOU 1147 O SER A 61 15464 11336 15575 -419 324 176 O
ATOM 1148 CB SER A 61 21.429 132.234 139.065 1.00113.38 C
ANISOU 1148 CB SER A 61 15723 11493 15863 -495 -15 356 C
ATOM 1149 OG SER A 61 21.492 130.991 139.745 1.00120.88 O
ANISOU 1149 OG SER A 61 16693 12323 16911 -511 -103 425 O
ATOM 1150 N SER A 62 19.655 133.432 136.704 1.00103.00 N
ANISOU 1150 N SER A 62 14569 10397 14169 -560 229 143 N
ATOM 1151 CA SER A 62 19.005 134.628 136.146 1.00 99.60 C
ANISOU 1151 CA SER A 62 14155 10101 13587 -587 244 99 C
ATOM 1152 C SER A 62 19.108 135.705 137.206 1.00 98.35 C
ANISOU 1152 C SER A 62 13900 10042 13428 -572 135 157 C
ATOM 1153 O SER A 62 19.353 136.848 136.873 1.00 98.00 O
ANISOU 1153 O SER A 62 13809 10054 13373 -544 159 142 O
ATOM 1154 CB SER A 62 17.532 134.379 135.833 1.00103.12 C
ANISOU 1154 CB SER A 62 14702 10627 13853 -683 211 68 C
ATOM 1155 OG SER A 62 17.225 132.997 135.726 1.00118.85 O
ANISOU 1155 OG SER A 62 16780 12532 15846 -725 218 61 O
ATOM 1156 N PHE A 63 18.998 135.319 138.491 1.00 91.73 N
ANISOU 1156 N PHE A 63 13054 9205 12595 -598 18 226 N
ATOM 1157 CA PHE A 63 19.097 136.195 139.654 1.00 89.10 C
ANISOU 1157 CA PHE A 63 12687 8934 12233 -610 -89 284 C
ATOM 1158 C PHE A 63 20.451 136.870 139.700 1.00 90.88 C
ANISOU 1158 C PHE A 63 12813 9103 12616 -540 -115 321 C
ATOM 1159 O PHE A 63 20.539 138.102 139.785 1.00 89.87 O
ANISOU 1159 O PHE A 63 12649 9050 12447 -531 -130 318 O
ATOM 1160 CB PHE A 63 18.883 135.379 140.940 1.00 90.97 C
ANISOU 1160 CB PHE A 63 12989 9131 12445 -671 -201 354 C
ATOM 1161 CG PHE A 63 18.828 136.217 142.197 1.00 91.78 C
ANISOU 1161 CG PHE A 63 13127 9281 12462 -718 -302 406 C
ATOM 1162 CD1 PHE A 63 17.706 136.984 142.493 1.00 92.79 C
ANISOU 1162 CD1 PHE A 63 13303 9525 12429 -772 -255 369 C
ATOM 1163 CD2 PHE A 63 19.911 136.264 143.068 1.00 94.21 C
ANISOU 1163 CD2 PHE A 63 13429 9501 12867 -716 -444 496 C
ATOM 1164 CE1 PHE A 63 17.662 137.766 143.647 1.00 93.18 C
ANISOU 1164 CE1 PHE A 63 13424 9596 12385 -824 -312 403 C
ATOM 1165 CE2 PHE A 63 19.859 137.040 144.227 1.00 96.45 C
ANISOU 1165 CE2 PHE A 63 13799 9810 13037 -784 -545 541 C
ATOM 1166 CZ PHE A 63 18.739 137.788 144.504 1.00 93.27 C
ANISOU 1166 CZ PHE A 63 13473 9520 12446 -838 -459 485 C
ATOM 1167 N LEU A 64 21.504 136.051 139.639 1.00 86.97 N
ANISOU 1167 N LEU A 64 12259 8459 12326 -490 -118 362 N
ATOM 1168 CA LEU A 64 22.883 136.493 139.671 1.00 87.32 C
ANISOU 1168 CA LEU A 64 12172 8410 12595 -422 -145 417 C
ATOM 1169 C LEU A 64 23.255 137.428 138.527 1.00 90.21 C
ANISOU 1169 C LEU A 64 12478 8804 12993 -368 8 348 C
ATOM 1170 O LEU A 64 24.144 138.267 138.687 1.00 89.54 O
ANISOU 1170 O LEU A 64 12286 8694 13042 -330 -28 392 O
ATOM 1171 CB LEU A 64 23.801 135.287 139.703 1.00 89.20 C
ANISOU 1171 CB LEU A 64 12340 8458 13094 -376 -152 475 C
ATOM 1172 CG LEU A 64 23.913 134.619 141.057 1.00 95.23 C
ANISOU 1172 CG LEU A 64 13131 9155 13897 -428 -372 592 C
ATOM 1173 CD1 LEU A 64 24.544 133.258 140.919 1.00 97.34 C
ANISOU 1173 CD1 LEU A 64 13349 9236 14401 -386 -352 632 C
ATOM 1174 CD2 LEU A 64 24.660 135.506 142.074 1.00 97.34 C
ANISOU 1174 CD2 LEU A 64 13336 9402 14247 -447 -578 703 C
ATOM 1175 N THR A 65 22.559 137.300 137.387 1.00 86.11 N
ANISOU 1175 N THR A 65 12045 8328 12345 -379 162 249 N
ATOM 1176 CA THR A 65 22.747 138.153 136.218 1.00 85.51 C
ANISOU 1176 CA THR A 65 11969 8277 12246 -353 309 180 C
ATOM 1177 C THR A 65 22.318 139.578 136.576 1.00 88.35 C
ANISOU 1177 C THR A 65 12312 8785 12473 -374 222 188 C
ATOM 1178 O THR A 65 23.061 140.525 136.308 1.00 89.07 O
ANISOU 1178 O THR A 65 12325 8872 12644 -335 255 193 O
ATOM 1179 CB THR A 65 22.009 137.557 135.034 1.00 94.41 C
ANISOU 1179 CB THR A 65 13243 9393 13235 -393 446 89 C
ATOM 1180 OG1 THR A 65 22.626 136.320 134.672 1.00 96.45 O
ANISOU 1180 OG1 THR A 65 13519 9483 13646 -363 561 75 O
ATOM 1181 CG2 THR A 65 21.962 138.484 133.860 1.00 93.72 C
ANISOU 1181 CG2 THR A 65 13215 9344 13052 -403 563 23 C
ATOM 1182 N PHE A 66 21.145 139.709 137.231 1.00 83.10 N
ANISOU 1182 N PHE A 66 11711 8234 11628 -437 125 190 N
ATOM 1183 CA PHE A 66 20.595 140.976 137.709 1.00 81.22 C
ANISOU 1183 CA PHE A 66 11467 8121 11272 -461 58 195 C
ATOM 1184 C PHE A 66 21.423 141.499 138.849 1.00 88.52 C
ANISOU 1184 C PHE A 66 12333 9022 12278 -450 -60 269 C
ATOM 1185 O PHE A 66 21.574 142.714 138.964 1.00 88.97 O
ANISOU 1185 O PHE A 66 12363 9138 12304 -444 -82 270 O
ATOM 1186 CB PHE A 66 19.154 140.811 138.203 1.00 81.08 C
ANISOU 1186 CB PHE A 66 11523 8190 11096 -530 18 185 C
ATOM 1187 CG PHE A 66 18.175 140.459 137.124 1.00 80.07 C
ANISOU 1187 CG PHE A 66 11451 8090 10882 -564 83 129 C
ATOM 1188 CD1 PHE A 66 17.849 141.378 136.133 1.00 82.29 C
ANISOU 1188 CD1 PHE A 66 11735 8422 11109 -565 124 91 C
ATOM 1189 CD2 PHE A 66 17.536 139.236 137.126 1.00 78.17 C
ANISOU 1189 CD2 PHE A 66 11273 7818 10610 -611 80 125 C
ATOM 1190 CE1 PHE A 66 16.945 141.046 135.132 1.00 82.27 C
ANISOU 1190 CE1 PHE A 66 11808 8427 11024 -621 140 57 C
ATOM 1191 CE2 PHE A 66 16.651 138.902 136.125 1.00 80.28 C
ANISOU 1191 CE2 PHE A 66 11606 8097 10800 -662 108 84 C
ATOM 1192 CZ PHE A 66 16.356 139.806 135.137 1.00 79.33 C
ANISOU 1192 CZ PHE A 66 11498 8017 10625 -671 127 54 C
ATOM 1193 N LEU A 67 21.932 140.596 139.717 1.00 86.22 N
ANISOU 1193 N LEU A 67 12038 8637 12085 -459 -157 338 N
ATOM 1194 CA LEU A 67 22.765 141.009 140.839 1.00 87.15 C
ANISOU 1194 CA LEU A 67 12127 8706 12283 -474 -318 429 C
ATOM 1195 C LEU A 67 24.060 141.613 140.295 1.00 92.02 C
ANISOU 1195 C LEU A 67 12598 9249 13115 -404 -298 455 C
ATOM 1196 O LEU A 67 24.500 142.652 140.784 1.00 91.82 O
ANISOU 1196 O LEU A 67 12545 9241 13102 -415 -391 494 O
ATOM 1197 CB LEU A 67 23.062 139.822 141.754 1.00 88.46 C
ANISOU 1197 CB LEU A 67 12329 8764 12519 -510 -450 513 C
ATOM 1198 CG LEU A 67 23.277 140.156 143.220 1.00 93.82 C
ANISOU 1198 CG LEU A 67 13089 9413 13146 -590 -659 607 C
ATOM 1199 CD1 LEU A 67 22.985 138.963 144.070 1.00 95.17 C
ANISOU 1199 CD1 LEU A 67 13371 9518 13270 -660 -761 664 C
ATOM 1200 CD2 LEU A 67 24.680 140.624 143.479 1.00 96.43 C
ANISOU 1200 CD2 LEU A 67 13299 9633 13708 -563 -799 703 C
ATOM 1201 N CYS A 68 24.628 140.982 139.248 1.00 89.05 N
ANISOU 1201 N CYS A 68 12144 8784 12906 -338 -154 426 N
ATOM 1202 CA CYS A 68 25.838 141.426 138.572 1.00 89.29 C
ANISOU 1202 CA CYS A 68 12030 8723 13173 -269 -69 439 C
ATOM 1203 C CYS A 68 25.612 142.765 137.918 1.00 90.42 C
ANISOU 1203 C CYS A 68 12184 8976 13196 -265 15 377 C
ATOM 1204 O CYS A 68 26.464 143.640 138.042 1.00 89.79 O
ANISOU 1204 O CYS A 68 12003 8870 13243 -244 -27 422 O
ATOM 1205 CB CYS A 68 26.293 140.389 137.557 1.00 91.28 C
ANISOU 1205 CB CYS A 68 12242 8843 13597 -212 126 399 C
ATOM 1206 SG CYS A 68 27.909 140.738 136.829 1.00 97.29 S
ANISOU 1206 SG CYS A 68 12803 9439 14725 -125 277 426 S
ATOM 1207 N GLY A 69 24.467 142.899 137.238 1.00 85.73 N
ANISOU 1207 N GLY A 69 11711 8492 12373 -291 113 287 N
ATOM 1208 CA GLY A 69 24.025 144.110 136.559 1.00 84.41 C
ANISOU 1208 CA GLY A 69 11577 8429 12067 -298 176 231 C
ATOM 1209 C GLY A 69 23.912 145.277 137.516 1.00 88.22 C
ANISOU 1209 C GLY A 69 12043 8994 12483 -322 35 270 C
ATOM 1210 O GLY A 69 24.419 146.363 137.226 1.00 87.68 O
ANISOU 1210 O GLY A 69 11922 8940 12454 -302 53 271 O
ATOM 1211 N LEU A 70 23.292 145.026 138.697 1.00 84.77 N
ANISOU 1211 N LEU A 70 11669 8592 11946 -372 -97 303 N
ATOM 1212 CA LEU A 70 23.075 145.965 139.812 1.00 83.38 C
ANISOU 1212 CA LEU A 70 11537 8470 11673 -418 -220 335 C
ATOM 1213 C LEU A 70 24.385 146.393 140.459 1.00 87.88 C
ANISOU 1213 C LEU A 70 12035 8954 12401 -416 -352 420 C
ATOM 1214 O LEU A 70 24.528 147.570 140.742 1.00 88.23 O
ANISOU 1214 O LEU A 70 12086 9035 12402 -431 -395 424 O
ATOM 1215 CB LEU A 70 22.134 145.330 140.840 1.00 82.84 C
ANISOU 1215 CB LEU A 70 11589 8425 11462 -486 -284 344 C
ATOM 1216 CG LEU A 70 21.932 145.984 142.185 1.00 86.63 C
ANISOU 1216 CG LEU A 70 12174 8916 11823 -559 -393 377 C
ATOM 1217 CD1 LEU A 70 21.205 147.253 142.058 1.00 85.17 C
ANISOU 1217 CD1 LEU A 70 12016 8823 11521 -562 -316 318 C
ATOM 1218 CD2 LEU A 70 21.127 145.080 143.070 1.00 90.38 C
ANISOU 1218 CD2 LEU A 70 12779 9382 12182 -631 -420 388 C
ATOM 1219 N VAL A 71 25.342 145.465 140.662 1.00 84.75 N
ANISOU 1219 N VAL A 71 11562 8431 12209 -401 -425 495 N
ATOM 1220 CA VAL A 71 26.680 145.747 141.212 1.00 85.94 C
ANISOU 1220 CA VAL A 71 11606 8466 12581 -403 -582 602 C
ATOM 1221 C VAL A 71 27.495 146.584 140.204 1.00 90.73 C
ANISOU 1221 C VAL A 71 12067 9055 13352 -337 -464 584 C
ATOM 1222 O VAL A 71 28.206 147.506 140.593 1.00 91.23 O
ANISOU 1222 O VAL A 71 12078 9096 13491 -355 -574 639 O
ATOM 1223 CB VAL A 71 27.412 144.424 141.573 1.00 91.55 C
ANISOU 1223 CB VAL A 71 12240 9022 13521 -393 -677 694 C
ATOM 1224 CG1 VAL A 71 28.926 144.608 141.648 1.00 92.91 C
ANISOU 1224 CG1 VAL A 71 12217 9041 14041 -364 -787 808 C
ATOM 1225 CG2 VAL A 71 26.871 143.820 142.870 1.00 91.55 C
ANISOU 1225 CG2 VAL A 71 12404 9015 13367 -488 -863 749 C
ATOM 1226 N LEU A 72 27.386 146.240 138.912 1.00 87.34 N
ANISOU 1226 N LEU A 72 11596 8626 12963 -274 -238 506 N
ATOM 1227 CA LEU A 72 28.079 146.887 137.798 1.00 86.75 C
ANISOU 1227 CA LEU A 72 11419 8521 13022 -219 -69 473 C
ATOM 1228 C LEU A 72 27.511 148.248 137.536 1.00 87.36 C
ANISOU 1228 C LEU A 72 11568 8729 12897 -240 -46 419 C
ATOM 1229 O LEU A 72 28.244 149.127 137.082 1.00 87.08 O
ANISOU 1229 O LEU A 72 11446 8667 12974 -219 5 428 O
ATOM 1230 CB LEU A 72 27.938 146.013 136.542 1.00 87.22 C
ANISOU 1230 CB LEU A 72 11500 8534 13108 -177 175 394 C
ATOM 1231 CG LEU A 72 29.148 145.853 135.623 1.00 93.79 C
ANISOU 1231 CG LEU A 72 12194 9216 14225 -116 375 395 C
ATOM 1232 CD1 LEU A 72 30.438 145.628 136.410 1.00 96.00 C
ANISOU 1232 CD1 LEU A 72 12262 9336 14878 -84 253 522 C
ATOM 1233 CD2 LEU A 72 28.941 144.676 134.692 1.00 97.16 C
ANISOU 1233 CD2 LEU A 72 12701 9570 14644 -95 604 314 C
ATOM 1234 N THR A 73 26.194 148.416 137.784 1.00 81.79 N
ANISOU 1234 N THR A 73 11007 8150 11918 -281 -72 364 N
ATOM 1235 CA THR A 73 25.501 149.689 137.605 1.00 80.74 C
ANISOU 1235 CA THR A 73 10938 8132 11609 -299 -59 317 C
ATOM 1236 C THR A 73 25.948 150.633 138.699 1.00 85.97 C
ANISOU 1236 C THR A 73 11591 8790 12283 -333 -223 377 C
ATOM 1237 O THR A 73 26.276 151.777 138.403 1.00 86.97 O
ANISOU 1237 O THR A 73 11686 8937 12420 -326 -208 372 O
ATOM 1238 CB THR A 73 23.991 149.492 137.578 1.00 86.28 C
ANISOU 1238 CB THR A 73 11761 8936 12086 -329 -33 257 C
ATOM 1239 OG1 THR A 73 23.647 148.802 136.376 1.00 88.43 O
ANISOU 1239 OG1 THR A 73 12060 9201 12339 -313 104 204 O
ATOM 1240 CG2 THR A 73 23.221 150.802 137.666 1.00 79.84 C
ANISOU 1240 CG2 THR A 73 10992 8215 11129 -347 -44 226 C
ATOM 1241 N ASP A 74 26.003 150.139 139.952 1.00 82.04 N
ANISOU 1241 N ASP A 74 11142 8253 11777 -383 -385 438 N
ATOM 1242 CA ASP A 74 26.442 150.881 141.129 1.00 81.81 C
ANISOU 1242 CA ASP A 74 11162 8192 11730 -448 -572 504 C
ATOM 1243 C ASP A 74 27.888 151.377 141.012 1.00 85.44 C
ANISOU 1243 C ASP A 74 11470 8552 12440 -433 -655 585 C
ATOM 1244 O ASP A 74 28.147 152.547 141.302 1.00 84.91 O
ANISOU 1244 O ASP A 74 11423 8497 12341 -464 -724 598 O
ATOM 1245 CB ASP A 74 26.257 150.021 142.385 1.00 84.56 C
ANISOU 1245 CB ASP A 74 11627 8489 12012 -523 -730 561 C
ATOM 1246 CG ASP A 74 24.810 149.747 142.746 1.00 99.42 C
ANISOU 1246 CG ASP A 74 13670 10460 13645 -559 -650 488 C
ATOM 1247 OD1 ASP A 74 23.910 150.361 142.123 1.00100.54 O
ANISOU 1247 OD1 ASP A 74 13824 10701 13676 -528 -501 401 O
ATOM 1248 OD2 ASP A 74 24.572 148.901 143.631 1.00107.06 O1-
ANISOU 1248 OD2 ASP A 74 14744 11385 14549 -621 -739 525 O1-
ATOM 1249 N PHE A 75 28.808 150.500 140.563 1.00 82.51 N
ANISOU 1249 N PHE A 75 10941 8072 12337 -384 -631 638 N
ATOM 1250 CA PHE A 75 30.219 150.796 140.373 1.00 84.32 C
ANISOU 1250 CA PHE A 75 10977 8177 12883 -360 -682 726 C
ATOM 1251 C PHE A 75 30.404 151.973 139.424 1.00 93.07 C
ANISOU 1251 C PHE A 75 12030 9336 13997 -324 -530 671 C
ATOM 1252 O PHE A 75 31.049 152.947 139.812 1.00 94.21 O
ANISOU 1252 O PHE A 75 12127 9448 14221 -358 -653 730 O
ATOM 1253 CB PHE A 75 30.974 149.559 139.859 1.00 87.01 C
ANISOU 1253 CB PHE A 75 11150 8383 13528 -296 -599 769 C
ATOM 1254 CG PHE A 75 32.433 149.833 139.596 1.00 90.14 C
ANISOU 1254 CG PHE A 75 11306 8626 14317 -263 -616 865 C
ATOM 1255 CD1 PHE A 75 33.372 149.728 140.615 1.00 95.43 C
ANISOU 1255 CD1 PHE A 75 11872 9159 15228 -314 -904 1022 C
ATOM 1256 CD2 PHE A 75 32.867 150.235 138.337 1.00 92.11 C
ANISOU 1256 CD2 PHE A 75 11441 8854 14703 -196 -352 809 C
ATOM 1257 CE1 PHE A 75 34.719 150.041 140.385 1.00 97.90 C
ANISOU 1257 CE1 PHE A 75 11930 9318 15951 -289 -934 1127 C
ATOM 1258 CE2 PHE A 75 34.211 150.552 138.108 1.00 96.56 C
ANISOU 1258 CE2 PHE A 75 11766 9266 15658 -169 -343 900 C
ATOM 1259 CZ PHE A 75 35.130 150.440 139.130 1.00 96.40 C
ANISOU 1259 CZ PHE A 75 11604 9110 15915 -211 -635 1062 C
ATOM 1260 N LEU A 76 29.840 151.896 138.188 1.00 91.78 N
ANISOU 1260 N LEU A 76 11893 9242 13739 -270 -280 565 N
ATOM 1261 CA LEU A 76 29.925 152.970 137.179 1.00 92.35 C
ANISOU 1261 CA LEU A 76 11947 9356 13784 -247 -125 510 C
ATOM 1262 C LEU A 76 29.254 154.248 137.649 1.00 95.05 C
ANISOU 1262 C LEU A 76 12406 9811 13899 -291 -219 484 C
ATOM 1263 O LEU A 76 29.739 155.333 137.329 1.00 95.92 O
ANISOU 1263 O LEU A 76 12471 9919 14056 -291 -197 490 O
ATOM 1264 CB LEU A 76 29.334 152.542 135.832 1.00 92.61 C
ANISOU 1264 CB LEU A 76 12041 9421 13725 -209 127 411 C
ATOM 1265 CG LEU A 76 30.088 151.434 135.123 1.00100.59 C
ANISOU 1265 CG LEU A 76 12953 10295 14973 -163 291 418 C
ATOM 1266 CD1 LEU A 76 29.250 150.836 134.013 1.00101.51 C
ANISOU 1266 CD1 LEU A 76 13214 10446 14910 -159 481 317 C
ATOM 1267 CD2 LEU A 76 31.446 151.915 134.617 1.00104.70 C
ANISOU 1267 CD2 LEU A 76 13302 10689 15791 -132 414 459 C
ATOM 1268 N GLY A 77 28.153 154.096 138.397 1.00 88.11 N
ANISOU 1268 N GLY A 77 11673 9012 12794 -329 -303 455 N
ATOM 1269 CA GLY A 77 27.402 155.182 138.998 1.00 85.98 C
ANISOU 1269 CA GLY A 77 11526 8822 12319 -372 -371 425 C
ATOM 1270 C GLY A 77 28.271 155.990 139.931 1.00 89.31 C
ANISOU 1270 C GLY A 77 11938 9179 12818 -427 -553 502 C
ATOM 1271 O GLY A 77 28.408 157.204 139.764 1.00 88.35 O
ANISOU 1271 O GLY A 77 11818 9077 12674 -434 -548 490 O
ATOM 1272 N LEU A 78 28.917 155.299 140.882 1.00 86.00 N
ANISOU 1272 N LEU A 78 11509 8665 12504 -475 -733 592 N
ATOM 1273 CA LEU A 78 29.806 155.930 141.858 1.00 86.00 C
ANISOU 1273 CA LEU A 78 11518 8574 12586 -555 -965 689 C
ATOM 1274 C LEU A 78 31.032 156.487 141.175 1.00 89.22 C
ANISOU 1274 C LEU A 78 11717 8908 13274 -519 -954 746 C
ATOM 1275 O LEU A 78 31.433 157.592 141.506 1.00 90.09 O
ANISOU 1275 O LEU A 78 11849 9002 13381 -568 -1053 774 O
ATOM 1276 CB LEU A 78 30.186 154.970 143.003 1.00 86.98 C
ANISOU 1276 CB LEU A 78 11693 8593 12762 -631 -1195 791 C
ATOM 1277 CG LEU A 78 29.035 154.482 143.894 1.00 90.12 C
ANISOU 1277 CG LEU A 78 12335 9040 12867 -696 -1221 745 C
ATOM 1278 CD1 LEU A 78 29.341 153.122 144.496 1.00 90.96 C
ANISOU 1278 CD1 LEU A 78 12442 9055 13064 -730 -1362 831 C
ATOM 1279 CD2 LEU A 78 28.661 155.521 144.947 1.00 91.00 C
ANISOU 1279 CD2 LEU A 78 12685 9149 12744 -810 -1336 735 C
ATOM 1280 N LEU A 79 31.581 155.774 140.176 1.00 83.83 N
ANISOU 1280 N LEU A 79 10847 8178 12825 -438 -801 754 N
ATOM 1281 CA LEU A 79 32.746 156.245 139.436 1.00 83.60 C
ANISOU 1281 CA LEU A 79 10610 8063 13091 -401 -729 801 C
ATOM 1282 C LEU A 79 32.493 157.498 138.592 1.00 86.55 C
ANISOU 1282 C LEU A 79 11017 8523 13346 -382 -573 723 C
ATOM 1283 O LEU A 79 33.277 158.434 138.697 1.00 87.22 O
ANISOU 1283 O LEU A 79 11022 8554 13561 -413 -652 780 O
ATOM 1284 CB LEU A 79 33.333 155.128 138.577 1.00 83.92 C
ANISOU 1284 CB LEU A 79 10473 8010 13401 -322 -546 811 C
ATOM 1285 CG LEU A 79 34.583 155.435 137.770 1.00 88.44 C
ANISOU 1285 CG LEU A 79 10810 8457 14336 -281 -417 863 C
ATOM 1286 CD1 LEU A 79 35.687 156.021 138.633 1.00 89.32 C
ANISOU 1286 CD1 LEU A 79 10778 8450 14710 -342 -688 1011 C
ATOM 1287 CD2 LEU A 79 35.067 154.193 137.099 1.00 91.50 C
ANISOU 1287 CD2 LEU A 79 11054 8728 14985 -208 -218 865 C
ATOM 1288 N VAL A 80 31.434 157.523 137.761 1.00 81.44 N
ANISOU 1288 N VAL A 80 10483 7992 12468 -342 -375 606 N
ATOM 1289 CA VAL A 80 31.180 158.677 136.892 1.00 80.47 C
ANISOU 1289 CA VAL A 80 10398 7936 12240 -330 -242 545 C
ATOM 1290 C VAL A 80 30.721 159.887 137.700 1.00 84.07 C
ANISOU 1290 C VAL A 80 10973 8449 12520 -385 -394 541 C
ATOM 1291 O VAL A 80 31.345 160.936 137.576 1.00 85.02 O
ANISOU 1291 O VAL A 80 11041 8536 12728 -405 -427 574 O
ATOM 1292 CB VAL A 80 30.281 158.394 135.666 1.00 83.72 C
ANISOU 1292 CB VAL A 80 10898 8427 12483 -288 -19 443 C
ATOM 1293 CG1 VAL A 80 30.782 157.183 134.881 1.00 84.50 C
ANISOU 1293 CG1 VAL A 80 10917 8444 12744 -247 156 437 C
ATOM 1294 CG2 VAL A 80 28.839 158.186 136.065 1.00 82.72 C
ANISOU 1294 CG2 VAL A 80 10930 8410 12090 -300 -67 384 C
ATOM 1295 N THR A 81 29.704 159.737 138.571 1.00 79.36 N
ANISOU 1295 N THR A 81 10538 7919 11698 -415 -475 504 N
ATOM 1296 CA THR A 81 29.212 160.844 139.406 1.00 78.28 C
ANISOU 1296 CA THR A 81 10543 7812 11387 -471 -580 486 C
ATOM 1297 C THR A 81 30.273 161.262 140.424 1.00 82.25 C
ANISOU 1297 C THR A 81 11037 8210 12005 -552 -805 583 C
ATOM 1298 O THR A 81 30.499 162.451 140.596 1.00 82.64 O
ANISOU 1298 O THR A 81 11122 8246 12032 -588 -857 588 O
ATOM 1299 CB THR A 81 27.850 160.547 140.055 1.00 82.58 C
ANISOU 1299 CB THR A 81 11260 8423 11695 -488 -569 421 C
ATOM 1300 OG1 THR A 81 28.015 159.562 141.068 1.00 91.06 O
ANISOU 1300 OG1 THR A 81 12383 9443 12774 -539 -702 471 O
ATOM 1301 CG2 THR A 81 26.785 160.121 139.058 1.00 72.37 C
ANISOU 1301 CG2 THR A 81 9961 7218 10316 -422 -387 345 C
ATOM 1302 N GLY A 82 30.951 160.294 141.031 1.00 78.98 N
ANISOU 1302 N GLY A 82 10568 7709 11732 -584 -949 668 N
ATOM 1303 CA GLY A 82 32.019 160.561 141.984 1.00 80.92 C
ANISOU 1303 CA GLY A 82 10795 7830 12121 -678 -1214 788 C
ATOM 1304 C GLY A 82 33.075 161.493 141.413 1.00 87.16 C
ANISOU 1304 C GLY A 82 11416 8563 13139 -672 -1221 842 C
ATOM 1305 O GLY A 82 33.389 162.521 142.020 1.00 87.45 O
ANISOU 1305 O GLY A 82 11535 8559 13133 -755 -1376 876 O
ATOM 1306 N THR A 83 33.578 161.173 140.204 1.00 83.22 N
ANISOU 1306 N THR A 83 10702 8053 12865 -580 -1025 840 N
ATOM 1307 CA THR A 83 34.578 161.974 139.501 1.00 83.06 C
ANISOU 1307 CA THR A 83 10505 7971 13084 -568 -968 885 C
ATOM 1308 C THR A 83 34.130 163.441 139.338 1.00 85.94 C
ANISOU 1308 C THR A 83 10997 8412 13244 -591 -933 820 C
ATOM 1309 O THR A 83 34.934 164.331 139.625 1.00 86.57 O
ANISOU 1309 O THR A 83 11024 8418 13449 -649 -1064 890 O
ATOM 1310 CB THR A 83 34.954 161.301 138.177 1.00 84.22 C
ANISOU 1310 CB THR A 83 10468 8095 13438 -470 -689 861 C
ATOM 1311 OG1 THR A 83 35.471 160.007 138.467 1.00 80.78 O
ANISOU 1311 OG1 THR A 83 9902 7560 13233 -452 -739 932 O
ATOM 1312 CG2 THR A 83 35.983 162.093 137.384 1.00 81.86 C
ANISOU 1312 CG2 THR A 83 9991 7719 13394 -461 -579 901 C
ATOM 1313 N ILE A 84 32.852 163.682 138.906 1.00 79.76 N
ANISOU 1313 N ILE A 84 10374 7760 12171 -548 -774 698 N
ATOM 1314 CA ILE A 84 32.280 165.025 138.692 1.00 78.65 C
ANISOU 1314 CA ILE A 84 10352 7684 11848 -557 -726 634 C
ATOM 1315 C ILE A 84 32.275 165.731 140.020 1.00 85.04 C
ANISOU 1315 C ILE A 84 11315 8452 12545 -656 -951 661 C
ATOM 1316 O ILE A 84 32.843 166.813 140.139 1.00 86.84 O
ANISOU 1316 O ILE A 84 11540 8632 12824 -704 -1031 695 O
ATOM 1317 CB ILE A 84 30.823 165.006 138.142 1.00 80.23 C
ANISOU 1317 CB ILE A 84 10679 8007 11798 -500 -556 519 C
ATOM 1318 CG1 ILE A 84 30.627 164.015 136.931 1.00 80.52 C
ANISOU 1318 CG1 ILE A 84 10632 8078 11885 -427 -355 486 C
ATOM 1319 CG2 ILE A 84 30.315 166.426 137.838 1.00 79.44 C
ANISOU 1319 CG2 ILE A 84 10668 7947 11567 -502 -512 470 C
ATOM 1320 CD1 ILE A 84 30.929 164.463 135.529 1.00 87.34 C
ANISOU 1320 CD1 ILE A 84 11432 8940 12815 -394 -173 470 C
ATOM 1321 N VAL A 85 31.633 165.093 141.018 1.00 81.26 N
ANISOU 1321 N VAL A 85 10992 7980 11904 -697 -1045 646 N
ATOM 1322 CA VAL A 85 31.445 165.551 142.394 1.00 81.25 C
ANISOU 1322 CA VAL A 85 11217 7925 11729 -812 -1235 656 C
ATOM 1323 C VAL A 85 32.781 165.904 143.082 1.00 86.86 C
ANISOU 1323 C VAL A 85 11889 8497 12616 -923 -1510 786 C
ATOM 1324 O VAL A 85 32.876 166.967 143.684 1.00 85.86 O
ANISOU 1324 O VAL A 85 11915 8322 12386 -1011 -1622 788 O
ATOM 1325 CB VAL A 85 30.598 164.512 143.167 1.00 84.03 C
ANISOU 1325 CB VAL A 85 11727 8297 11903 -835 -1246 622 C
ATOM 1326 CG1 VAL A 85 30.613 164.763 144.665 1.00 85.13 C
ANISOU 1326 CG1 VAL A 85 12137 8345 11863 -984 -1451 647 C
ATOM 1327 CG2 VAL A 85 29.170 164.506 142.642 1.00 81.94 C
ANISOU 1327 CG2 VAL A 85 11519 8153 11463 -748 -999 498 C
ATOM 1328 N VAL A 86 33.805 165.043 142.962 1.00 86.07 N
ANISOU 1328 N VAL A 86 11578 8319 12804 -919 -1618 900 N
ATOM 1329 CA VAL A 86 35.130 165.270 143.552 1.00 88.20 C
ANISOU 1329 CA VAL A 86 11758 8437 13318 -1024 -1906 1052 C
ATOM 1330 C VAL A 86 35.761 166.514 142.917 1.00 94.05 C
ANISOU 1330 C VAL A 86 12381 9159 14194 -1019 -1864 1065 C
ATOM 1331 O VAL A 86 36.247 167.376 143.653 1.00 95.06 O
ANISOU 1331 O VAL A 86 12614 9199 14304 -1141 -2089 1126 O
ATOM 1332 CB VAL A 86 36.051 164.018 143.464 1.00 92.42 C
ANISOU 1332 CB VAL A 86 12043 8874 14199 -1001 -2002 1178 C
ATOM 1333 CG1 VAL A 86 37.479 164.341 143.894 1.00 94.37 C
ANISOU 1333 CG1 VAL A 86 12123 8946 14786 -1098 -2294 1354 C
ATOM 1334 CG2 VAL A 86 35.498 162.874 144.292 1.00 91.99 C
ANISOU 1334 CG2 VAL A 86 12143 8814 13995 -1039 -2109 1185 C
ATOM 1335 N SER A 87 35.704 166.620 141.559 1.00 90.30 N
ANISOU 1335 N SER A 87 11727 8760 13822 -894 -1576 1005 N
ATOM 1336 CA SER A 87 36.238 167.748 140.783 1.00 90.96 C
ANISOU 1336 CA SER A 87 11701 8832 14026 -880 -1486 1009 C
ATOM 1337 C SER A 87 35.623 169.073 141.232 1.00 95.50 C
ANISOU 1337 C SER A 87 12520 9443 14322 -942 -1534 941 C
ATOM 1338 O SER A 87 36.336 170.066 141.349 1.00 96.28 O
ANISOU 1338 O SER A 87 12597 9467 14517 -1013 -1655 999 O
ATOM 1339 CB SER A 87 35.994 167.547 139.293 1.00 94.17 C
ANISOU 1339 CB SER A 87 11976 9321 14482 -752 -1148 932 C
ATOM 1340 OG SER A 87 36.572 166.332 138.854 1.00107.47 O
ANISOU 1340 OG SER A 87 13455 10955 16423 -695 -1061 980 O
ATOM 1341 N GLN A 88 34.307 169.066 141.498 1.00 91.11 N
ANISOU 1341 N GLN A 88 12188 8986 13444 -916 -1434 822 N
ATOM 1342 CA GLN A 88 33.534 170.201 141.985 1.00 90.71 C
ANISOU 1342 CA GLN A 88 12383 8955 13125 -960 -1432 740 C
ATOM 1343 C GLN A 88 34.002 170.637 143.365 1.00 97.29 C
ANISOU 1343 C GLN A 88 13416 9666 13883 -1122 -1719 802 C
ATOM 1344 O GLN A 88 34.192 171.827 143.586 1.00 99.07 O
ANISOU 1344 O GLN A 88 13750 9844 14049 -1186 -1777 793 O
ATOM 1345 CB GLN A 88 32.044 169.847 142.041 1.00 90.54 C
ANISOU 1345 CB GLN A 88 12520 9037 12843 -897 -1255 616 C
ATOM 1346 CG GLN A 88 31.371 169.733 140.683 1.00 99.60 C
ANISOU 1346 CG GLN A 88 13546 10299 14000 -763 -995 546 C
ATOM 1347 CD GLN A 88 31.718 170.887 139.796 1.00107.99 C
ANISOU 1347 CD GLN A 88 14534 11361 15136 -740 -922 545 C
ATOM 1348 OE1 GLN A 88 32.327 170.710 138.748 1.00104.11 O
ANISOU 1348 OE1 GLN A 88 13860 10878 14818 -692 -828 579 O
ATOM 1349 NE2 GLN A 88 31.411 172.093 140.238 1.00 91.86 N
ANISOU 1349 NE2 GLN A 88 12646 9289 12969 -785 -959 510 N
ATOM 1350 N HIS A 89 34.188 169.683 144.287 1.00 93.74 N
ANISOU 1350 N HIS A 89 13039 9154 13425 -1200 -1908 866 N
ATOM 1351 CA HIS A 89 34.672 169.943 145.637 1.00 95.37 C
ANISOU 1351 CA HIS A 89 13476 9220 13539 -1385 -2221 941 C
ATOM 1352 C HIS A 89 36.103 170.488 145.563 1.00101.10 C
ANISOU 1352 C HIS A 89 14023 9827 14562 -1462 -2454 1086 C
ATOM 1353 O HIS A 89 36.437 171.462 146.253 1.00101.97 O
ANISOU 1353 O HIS A 89 14319 9842 14583 -1597 -2636 1112 O
ATOM 1354 CB HIS A 89 34.579 168.664 146.479 1.00 96.96 C
ANISOU 1354 CB HIS A 89 13780 9378 13683 -1449 -2374 993 C
ATOM 1355 CG HIS A 89 33.195 168.385 146.974 1.00 99.50 C
ANISOU 1355 CG HIS A 89 14376 9770 13661 -1438 -2200 858 C
ATOM 1356 ND1 HIS A 89 32.790 168.773 148.237 1.00102.60 N
ANISOU 1356 ND1 HIS A 89 15161 10073 13750 -1596 -2310 825 N
ATOM 1357 CD2 HIS A 89 32.150 167.805 146.342 1.00 99.46 C
ANISOU 1357 CD2 HIS A 89 14306 9899 13586 -1297 -1916 752 C
ATOM 1358 CE1 HIS A 89 31.519 168.427 148.329 1.00100.98 C
ANISOU 1358 CE1 HIS A 89 15093 9949 13325 -1535 -2062 698 C
ATOM 1359 NE2 HIS A 89 31.093 167.835 147.214 1.00 99.41 N
ANISOU 1359 NE2 HIS A 89 14617 9889 13267 -1356 -1840 657 N
ATOM 1360 N ALA A 90 36.907 169.920 144.640 1.00 97.79 N
ANISOU 1360 N ALA A 90 13240 9408 14509 -1372 -2411 1171 N
ATOM 1361 CA ALA A 90 38.281 170.345 144.366 1.00 99.39 C
ANISOU 1361 CA ALA A 90 13188 9493 15082 -1418 -2573 1315 C
ATOM 1362 C ALA A 90 38.324 171.763 143.776 1.00103.02 C
ANISOU 1362 C ALA A 90 13648 9979 15516 -1407 -2452 1262 C
ATOM 1363 O ALA A 90 39.271 172.498 144.057 1.00105.35 O
ANISOU 1363 O ALA A 90 13886 10155 15990 -1514 -2667 1370 O
ATOM 1364 CB ALA A 90 38.957 169.363 143.417 1.00100.10 C
ANISOU 1364 CB ALA A 90 12897 9576 15562 -1300 -2446 1385 C
ATOM 1365 N ALA A 91 37.292 172.139 142.972 1.00 96.04 N
ANISOU 1365 N ALA A 91 12827 9240 14423 -1285 -2130 1107 N
ATOM 1366 CA ALA A 91 37.131 173.439 142.303 1.00 93.99 C
ANISOU 1366 CA ALA A 91 12585 9019 14109 -1255 -1982 1043 C
ATOM 1367 C ALA A 91 36.255 174.417 143.095 1.00 96.67 C
ANISOU 1367 C ALA A 91 13275 9362 14093 -1323 -2009 942 C
ATOM 1368 O ALA A 91 35.923 175.493 142.577 1.00 96.56 O
ANISOU 1368 O ALA A 91 13303 9381 14004 -1289 -1873 875 O
ATOM 1369 CB ALA A 91 36.550 173.237 140.912 1.00 92.72 C
ANISOU 1369 CB ALA A 91 12278 8988 13963 -1091 -1635 955 C
ATOM 1370 N LEU A 92 35.890 174.047 144.349 1.00 92.32 N
ANISOU 1370 N LEU A 92 12988 8761 13328 -1425 -2172 932 N
ATOM 1371 CA LEU A 92 35.053 174.826 145.275 1.00 91.73 C
ANISOU 1371 CA LEU A 92 13290 8655 12909 -1507 -2172 829 C
ATOM 1372 C LEU A 92 33.710 175.250 144.663 1.00 94.91 C
ANISOU 1372 C LEU A 92 13754 9178 13130 -1369 -1836 670 C
ATOM 1373 O LEU A 92 33.266 176.378 144.838 1.00 95.20 O
ANISOU 1373 O LEU A 92 13968 9183 13021 -1391 -1769 595 O
ATOM 1374 CB LEU A 92 35.816 176.024 145.855 1.00 93.05 C
ANISOU 1374 CB LEU A 92 13601 8685 13070 -1661 -2393 883 C
ATOM 1375 CG LEU A 92 36.957 175.674 146.780 1.00 99.00 C
ANISOU 1375 CG LEU A 92 14382 9284 13949 -1843 -2787 1046 C
ATOM 1376 CD1 LEU A 92 38.274 176.133 146.208 1.00 99.60 C
ANISOU 1376 CD1 LEU A 92 14164 9295 14384 -1865 -2927 1180 C
ATOM 1377 CD2 LEU A 92 36.737 176.259 148.128 1.00102.19 C
ANISOU 1377 CD2 LEU A 92 15233 9556 14040 -2039 -2977 1019 C
ATOM 1378 N PHE A 93 33.089 174.322 143.921 1.00 90.96 N
ANISOU 1378 N PHE A 93 13099 8800 12663 -1230 -1640 628 N
ATOM 1379 CA PHE A 93 31.788 174.368 143.237 1.00 89.81 C
ANISOU 1379 CA PHE A 93 12959 8769 12396 -1094 -1351 505 C
ATOM 1380 C PHE A 93 31.701 175.431 142.111 1.00 94.48 C
ANISOU 1380 C PHE A 93 13433 9402 13063 -1011 -1205 477 C
ATOM 1381 O PHE A 93 30.603 175.735 141.613 1.00 94.11 O
ANISOU 1381 O PHE A 93 13412 9420 12924 -917 -1006 388 O
ATOM 1382 CB PHE A 93 30.633 174.475 144.243 1.00 91.85 C
ANISOU 1382 CB PHE A 93 13524 8998 12378 -1135 -1280 400 C
ATOM 1383 CG PHE A 93 30.858 173.576 145.437 1.00 94.64 C
ANISOU 1383 CG PHE A 93 14051 9280 12629 -1257 -1458 441 C
ATOM 1384 CD1 PHE A 93 31.081 172.213 145.271 1.00 97.40 C
ANISOU 1384 CD1 PHE A 93 14247 9680 13083 -1224 -1507 501 C
ATOM 1385 CD2 PHE A 93 30.907 174.099 146.720 1.00 98.48 C
ANISOU 1385 CD2 PHE A 93 14876 9631 12909 -1420 -1588 425 C
ATOM 1386 CE1 PHE A 93 31.334 171.394 146.368 1.00 99.68 C
ANISOU 1386 CE1 PHE A 93 14700 9890 13285 -1346 -1699 554 C
ATOM 1387 CE2 PHE A 93 31.155 173.275 147.817 1.00102.50 C
ANISOU 1387 CE2 PHE A 93 15581 10059 13305 -1558 -1780 476 C
ATOM 1388 CZ PHE A 93 31.358 171.930 147.634 1.00100.26 C
ANISOU 1388 CZ PHE A 93 15124 9832 13139 -1517 -1841 545 C
ATOM 1389 N GLU A 94 32.875 175.878 141.628 1.00 91.00 N
ANISOU 1389 N GLU A 94 12836 8918 12822 -1045 -1306 568 N
ATOM 1390 CA GLU A 94 32.996 176.805 140.515 1.00 90.23 C
ANISOU 1390 CA GLU A 94 12621 8847 12816 -985 -1185 563 C
ATOM 1391 C GLU A 94 33.000 175.982 139.216 1.00 94.16 C
ANISOU 1391 C GLU A 94 12890 9439 13448 -874 -1017 576 C
ATOM 1392 O GLU A 94 34.044 175.460 138.835 1.00 94.05 O
ANISOU 1392 O GLU A 94 12685 9397 13653 -886 -1055 662 O
ATOM 1393 CB GLU A 94 34.255 177.707 140.677 1.00 92.46 C
ANISOU 1393 CB GLU A 94 12864 9020 13248 -1092 -1362 655 C
ATOM 1394 CG GLU A 94 34.073 178.864 141.660 1.00 98.19 C
ANISOU 1394 CG GLU A 94 13855 9650 13802 -1193 -1469 615 C
ATOM 1395 CD GLU A 94 33.021 179.927 141.358 1.00117.55 C
ANISOU 1395 CD GLU A 94 16432 12126 16104 -1126 -1285 508 C
ATOM 1396 OE1 GLU A 94 32.556 180.018 140.200 1.00106.27 O
ANISOU 1396 OE1 GLU A 94 14864 10787 14727 -1008 -1101 483 O
ATOM 1397 OE2 GLU A 94 32.671 180.685 142.288 1.00115.77 O1-
ANISOU 1397 OE2 GLU A 94 16459 11812 15717 -1201 -1328 453 O1-
ATOM 1398 N TRP A 95 31.828 175.846 138.560 1.00 91.54 N
ANISOU 1398 N TRP A 95 12587 9200 12996 -775 -830 494 N
ATOM 1399 CA TRP A 95 31.645 175.032 137.351 1.00 92.97 C
ANISOU 1399 CA TRP A 95 12622 9462 13239 -687 -669 491 C
ATOM 1400 C TRP A 95 32.533 175.382 136.193 1.00 97.46 C
ANISOU 1400 C TRP A 95 13042 10014 13975 -681 -590 546 C
ATOM 1401 O TRP A 95 33.033 174.467 135.544 1.00 97.39 O
ANISOU 1401 O TRP A 95 12897 10016 14092 -655 -505 576 O
ATOM 1402 CB TRP A 95 30.188 175.003 136.881 1.00 92.37 C
ANISOU 1402 CB TRP A 95 12626 9464 13005 -607 -531 408 C
ATOM 1403 CG TRP A 95 29.342 174.170 137.782 1.00 94.48 C
ANISOU 1403 CG TRP A 95 12985 9758 13155 -597 -544 360 C
ATOM 1404 CD1 TRP A 95 28.890 174.518 139.024 1.00 98.34 C
ANISOU 1404 CD1 TRP A 95 13644 10198 13524 -645 -609 319 C
ATOM 1405 CD2 TRP A 95 28.988 172.791 137.596 1.00 94.17 C
ANISOU 1405 CD2 TRP A 95 12888 9781 13112 -555 -492 352 C
ATOM 1406 NE1 TRP A 95 28.262 173.447 139.617 1.00 98.26 N
ANISOU 1406 NE1 TRP A 95 13683 10218 13433 -637 -593 288 N
ATOM 1407 CE2 TRP A 95 28.299 172.374 138.762 1.00 98.35 C
ANISOU 1407 CE2 TRP A 95 13546 10303 13519 -578 -531 310 C
ATOM 1408 CE3 TRP A 95 29.132 171.883 136.535 1.00 95.18 C
ANISOU 1408 CE3 TRP A 95 12892 9959 13312 -507 -396 369 C
ATOM 1409 CZ2 TRP A 95 27.755 171.093 138.898 1.00 96.41 C
ANISOU 1409 CZ2 TRP A 95 13288 10107 13236 -549 -493 292 C
ATOM 1410 CZ3 TRP A 95 28.606 170.603 136.684 1.00 96.21 C
ANISOU 1410 CZ3 TRP A 95 13016 10136 13403 -478 -366 348 C
ATOM 1411 CH2 TRP A 95 27.941 170.220 137.860 1.00 96.54 C
ANISOU 1411 CH2 TRP A 95 13166 10178 13338 -497 -423 315 C
ATOM 1412 N HIS A 96 32.732 176.674 135.920 1.00 95.08 N
ANISOU 1412 N HIS A 96 12773 9673 13678 -709 -596 554 N
ATOM 1413 CA HIS A 96 33.579 177.130 134.808 1.00 95.90 C
ANISOU 1413 CA HIS A 96 12758 9748 13931 -717 -501 606 C
ATOM 1414 C HIS A 96 35.004 176.555 134.868 1.00101.68 C
ANISOU 1414 C HIS A 96 13297 10406 14929 -761 -537 696 C
ATOM 1415 O HIS A 96 35.655 176.415 133.821 1.00102.34 O
ANISOU 1415 O HIS A 96 13257 10468 15161 -750 -379 729 O
ATOM 1416 CB HIS A 96 33.624 178.666 134.745 1.00 96.96 C
ANISOU 1416 CB HIS A 96 12972 9835 14032 -755 -541 609 C
ATOM 1417 CG HIS A 96 34.273 179.306 135.937 1.00101.29 C
ANISOU 1417 CG HIS A 96 13560 10294 14629 -846 -742 646 C
ATOM 1418 ND1 HIS A 96 33.530 179.747 137.012 1.00103.00 N
ANISOU 1418 ND1 HIS A 96 13969 10493 14673 -869 -843 589 N
ATOM 1419 CD2 HIS A 96 35.584 179.539 136.188 1.00104.48 C
ANISOU 1419 CD2 HIS A 96 13847 10608 15241 -929 -857 738 C
ATOM 1420 CE1 HIS A 96 34.408 180.234 137.874 1.00103.75 C
ANISOU 1420 CE1 HIS A 96 14092 10490 14839 -977 -1029 644 C
ATOM 1421 NE2 HIS A 96 35.654 180.126 137.424 1.00104.92 N
ANISOU 1421 NE2 HIS A 96 14043 10594 15229 -1015 -1064 742 N
ATOM 1422 N ALA A 97 35.480 176.247 136.104 1.00 98.03 N
ANISOU 1422 N ALA A 97 12822 9888 14538 -821 -745 743 N
ATOM 1423 CA ALA A 97 36.815 175.727 136.390 1.00 99.08 C
ANISOU 1423 CA ALA A 97 12755 9923 14969 -873 -847 853 C
ATOM 1424 C ALA A 97 37.000 174.370 135.762 1.00102.47 C
ANISOU 1424 C ALA A 97 13032 10370 15531 -805 -689 860 C
ATOM 1425 O ALA A 97 37.992 174.139 135.065 1.00102.87 O
ANISOU 1425 O ALA A 97 12882 10351 15853 -800 -570 922 O
ATOM 1426 CB ALA A 97 37.026 175.644 137.892 1.00100.65 C
ANISOU 1426 CB ALA A 97 13036 10057 15149 -964 -1139 899 C
ATOM 1427 N VAL A 98 35.996 173.499 135.976 1.00 98.03 N
ANISOU 1427 N VAL A 98 12575 9893 14778 -751 -663 790 N
ATOM 1428 CA VAL A 98 35.884 172.126 135.488 1.00 96.91 C
ANISOU 1428 CA VAL A 98 12350 9782 14690 -684 -523 774 C
ATOM 1429 C VAL A 98 35.474 172.174 134.011 1.00100.93 C
ANISOU 1429 C VAL A 98 12878 10345 15127 -625 -244 712 C
ATOM 1430 O VAL A 98 36.269 171.807 133.140 1.00101.20 O
ANISOU 1430 O VAL A 98 12772 10317 15364 -615 -70 744 O
ATOM 1431 CB VAL A 98 34.871 171.321 136.351 1.00 98.74 C
ANISOU 1431 CB VAL A 98 12725 10084 14709 -667 -617 720 C
ATOM 1432 CG1 VAL A 98 35.106 169.818 136.214 1.00 98.61 C
ANISOU 1432 CG1 VAL A 98 12592 10057 14818 -624 -558 739 C
ATOM 1433 CG2 VAL A 98 34.932 171.747 137.816 1.00 98.73 C
ANISOU 1433 CG2 VAL A 98 12838 10034 14642 -756 -888 753 C
ATOM 1434 N ASP A 99 34.255 172.666 133.734 1.00 97.53 N
ANISOU 1434 N ASP A 99 12629 10008 14420 -597 -204 630 N
ATOM 1435 CA ASP A 99 33.721 172.785 132.386 1.00 98.73 C
ANISOU 1435 CA ASP A 99 12851 10203 14459 -565 1 582 C
ATOM 1436 C ASP A 99 32.884 174.074 132.265 1.00105.11 C
ANISOU 1436 C ASP A 99 13808 11051 15080 -572 -45 548 C
ATOM 1437 O ASP A 99 31.825 174.157 132.898 1.00104.99 O
ANISOU 1437 O ASP A 99 13897 11091 14903 -549 -135 502 O
ATOM 1438 CB ASP A 99 32.885 171.520 132.024 1.00100.55 C
ANISOU 1438 CB ASP A 99 13134 10498 14571 -514 96 526 C
ATOM 1439 CG ASP A 99 31.944 171.638 130.821 1.00116.62 C
ANISOU 1439 CG ASP A 99 15314 12586 16411 -500 228 474 C
ATOM 1440 OD1 ASP A 99 32.433 171.516 129.666 1.00120.04 O
ANISOU 1440 OD1 ASP A 99 15755 12974 16880 -519 413 478 O
ATOM 1441 OD2 ASP A 99 30.708 171.826 131.037 1.00119.17 O1-
ANISOU 1441 OD2 ASP A 99 15748 12979 16552 -478 148 435 O1-
ATOM 1442 N PRO A 100 33.301 175.092 131.468 1.00103.23 N
ANISOU 1442 N PRO A 100 13580 10772 14871 -604 27 572 N
ATOM 1443 CA PRO A 100 32.437 176.273 131.308 1.00102.67 C
ANISOU 1443 CA PRO A 100 13647 10727 14636 -604 -21 546 C
ATOM 1444 C PRO A 100 31.256 175.892 130.406 1.00104.03 C
ANISOU 1444 C PRO A 100 13934 10962 14630 -567 62 502 C
ATOM 1445 O PRO A 100 31.435 175.227 129.375 1.00102.90 O
ANISOU 1445 O PRO A 100 13804 10815 14478 -576 209 502 O
ATOM 1446 CB PRO A 100 33.368 177.344 130.699 1.00105.51 C
ANISOU 1446 CB PRO A 100 13976 11012 15099 -659 32 596 C
ATOM 1447 CG PRO A 100 34.739 176.713 130.638 1.00111.17 C
ANISOU 1447 CG PRO A 100 14517 11659 16063 -687 110 650 C
ATOM 1448 CD PRO A 100 34.518 175.220 130.646 1.00106.36 C
ANISOU 1448 CD PRO A 100 13867 11085 15459 -642 173 624 C
ATOM 1449 N GLY A 101 30.057 176.232 130.867 1.00 99.32 N
ANISOU 1449 N GLY A 101 13422 10406 13907 -533 -33 466 N
ATOM 1450 CA GLY A 101 28.811 175.920 130.183 1.00 98.65 C
ANISOU 1450 CA GLY A 101 13425 10368 13687 -502 -9 441 C
ATOM 1451 C GLY A 101 27.911 175.003 130.979 1.00102.10 C
ANISOU 1451 C GLY A 101 13855 10861 14077 -454 -55 398 C
ATOM 1452 O GLY A 101 28.203 174.684 132.138 1.00102.53 O
ANISOU 1452 O GLY A 101 13865 10916 14176 -449 -109 383 O
ATOM 1453 N CYS A 102 26.817 174.568 130.359 1.00 97.32 N
ANISOU 1453 N CYS A 102 13305 10292 13382 -433 -45 386 N
ATOM 1454 CA CYS A 102 25.851 173.683 131.011 1.00 96.48 C
ANISOU 1454 CA CYS A 102 13187 10233 13239 -391 -74 349 C
ATOM 1455 C CYS A 102 25.949 172.197 130.576 1.00 96.84 C
ANISOU 1455 C CYS A 102 13222 10315 13257 -395 -8 340 C
ATOM 1456 O CYS A 102 25.180 171.377 131.080 1.00 96.35 O
ANISOU 1456 O CYS A 102 13149 10292 13167 -366 -29 312 O
ATOM 1457 CB CYS A 102 24.434 174.226 130.826 1.00 97.48 C
ANISOU 1457 CB CYS A 102 13351 10355 13332 -362 -130 351 C
ATOM 1458 SG CYS A 102 23.989 175.575 131.952 1.00101.88 S
ANISOU 1458 SG CYS A 102 13906 10857 13945 -328 -177 328 S
ATOM 1459 N ARG A 103 26.872 171.867 129.653 1.00 91.27 N
ANISOU 1459 N ARG A 103 12530 9584 12565 -434 92 358 N
ATOM 1460 CA ARG A 103 27.073 170.534 129.068 1.00 90.37 C
ANISOU 1460 CA ARG A 103 12431 9476 12429 -446 193 344 C
ATOM 1461 C ARG A 103 27.376 169.430 130.090 1.00 92.08 C
ANISOU 1461 C ARG A 103 12549 9714 12724 -412 187 323 C
ATOM 1462 O ARG A 103 26.725 168.377 130.048 1.00 91.57 O
ANISOU 1462 O ARG A 103 12509 9683 12601 -399 197 299 O
ATOM 1463 CB ARG A 103 28.154 170.566 127.972 1.00 92.66 C
ANISOU 1463 CB ARG A 103 12759 9699 12746 -499 350 362 C
ATOM 1464 CG ARG A 103 27.754 171.360 126.727 1.00113.46 C
ANISOU 1464 CG ARG A 103 15557 12304 15250 -560 365 384 C
ATOM 1465 CD ARG A 103 28.954 171.716 125.865 1.00136.69 C
ANISOU 1465 CD ARG A 103 18542 15163 18230 -621 541 401 C
ATOM 1466 NE ARG A 103 29.416 170.571 125.076 1.00156.10 N
ANISOU 1466 NE ARG A 103 21068 17573 20669 -655 737 373 N
ATOM 1467 CZ ARG A 103 29.390 170.508 123.747 1.00173.42 C
ANISOU 1467 CZ ARG A 103 23470 19698 22726 -744 879 369 C
ATOM 1468 NH1 ARG A 103 28.941 171.537 123.034 1.00161.99 N
ANISOU 1468 NH1 ARG A 103 22177 18224 21148 -811 822 406 N
ATOM 1469 NH2 ARG A 103 29.829 169.423 123.120 1.00158.30 N
ANISOU 1469 NH2 ARG A 103 21628 17721 20797 -775 1086 330 N
ATOM 1470 N LEU A 104 28.373 169.661 130.987 1.00 86.85 N
ANISOU 1470 N LEU A 104 11783 9021 12195 -409 152 343 N
ATOM 1471 CA LEU A 104 28.805 168.724 132.036 1.00 84.93 C
ANISOU 1471 CA LEU A 104 11452 8774 12043 -394 105 346 C
ATOM 1472 C LEU A 104 27.720 168.553 133.054 1.00 89.72 C
ANISOU 1472 C LEU A 104 12106 9433 12549 -373 -1 315 C
ATOM 1473 O LEU A 104 27.534 167.444 133.572 1.00 90.58 O
ANISOU 1473 O LEU A 104 12199 9560 12657 -361 -14 303 O
ATOM 1474 CB LEU A 104 30.070 169.218 132.732 1.00 84.71 C
ANISOU 1474 CB LEU A 104 11320 8679 12186 -420 42 397 C
ATOM 1475 CG LEU A 104 30.672 168.300 133.767 1.00 88.06 C
ANISOU 1475 CG LEU A 104 11653 9072 12734 -423 -44 428 C
ATOM 1476 CD1 LEU A 104 31.296 167.083 133.111 1.00 88.46 C
ANISOU 1476 CD1 LEU A 104 11612 9083 12914 -403 93 439 C
ATOM 1477 CD2 LEU A 104 31.676 169.036 134.602 1.00 89.39 C
ANISOU 1477 CD2 LEU A 104 11750 9168 13046 -470 -180 491 C
ATOM 1478 N CYS A 105 27.005 169.656 133.340 1.00 85.95 N
ANISOU 1478 N CYS A 105 11691 8967 12000 -370 -58 300 N
ATOM 1479 CA CYS A 105 25.887 169.670 134.248 1.00 85.74 C
ANISOU 1479 CA CYS A 105 11717 8966 11893 -351 -110 263 C
ATOM 1480 C CYS A 105 24.754 168.839 133.682 1.00 87.30 C
ANISOU 1480 C CYS A 105 11931 9213 12025 -324 -65 241 C
ATOM 1481 O CYS A 105 24.138 168.060 134.416 1.00 87.97 O
ANISOU 1481 O CYS A 105 12023 9321 12080 -313 -75 216 O
ATOM 1482 CB CYS A 105 25.420 171.085 134.533 1.00 87.70 C
ANISOU 1482 CB CYS A 105 12018 9187 12118 -349 -141 252 C
ATOM 1483 SG CYS A 105 23.897 171.126 135.502 1.00 92.49 S
ANISOU 1483 SG CYS A 105 12685 9795 12661 -319 -132 197 S
ATOM 1484 N ARG A 106 24.468 169.005 132.379 1.00 80.60 N
ANISOU 1484 N ARG A 106 11105 8370 11149 -327 -28 256 N
ATOM 1485 CA ARG A 106 23.422 168.229 131.728 1.00 78.89 C
ANISOU 1485 CA ARG A 106 10919 8185 10871 -323 -19 250 C
ATOM 1486 C ARG A 106 23.793 166.766 131.652 1.00 82.65 C
ANISOU 1486 C ARG A 106 11385 8677 11340 -330 35 237 C
ATOM 1487 O ARG A 106 22.975 165.921 132.023 1.00 82.28 O
ANISOU 1487 O ARG A 106 11336 8661 11263 -318 18 219 O
ATOM 1488 CB ARG A 106 23.029 168.820 130.392 1.00 76.57 C
ANISOU 1488 CB ARG A 106 10691 7871 10531 -352 -30 283 C
ATOM 1489 CG ARG A 106 21.995 169.886 130.620 1.00 84.46 C
ANISOU 1489 CG ARG A 106 11676 8853 11560 -327 -108 298 C
ATOM 1490 CD ARG A 106 21.366 170.344 129.360 1.00 88.39 C
ANISOU 1490 CD ARG A 106 12240 9321 12024 -363 -172 350 C
ATOM 1491 NE ARG A 106 22.247 171.263 128.663 1.00 95.57 N
ANISOU 1491 NE ARG A 106 13211 10192 12910 -401 -152 377 N
ATOM 1492 CZ ARG A 106 22.117 172.581 128.693 1.00112.70 C
ANISOU 1492 CZ ARG A 106 15375 12320 15126 -392 -204 404 C
ATOM 1493 NH1 ARG A 106 21.148 173.142 129.406 1.00 95.41 N
ANISOU 1493 NH1 ARG A 106 13116 10111 13025 -339 -262 404 N
ATOM 1494 NH2 ARG A 106 22.947 173.348 128.007 1.00107.66 N
ANISOU 1494 NH2 ARG A 106 14802 11645 14459 -436 -180 432 N
ATOM 1495 N PHE A 107 25.056 166.463 131.272 1.00 78.80 N
ANISOU 1495 N PHE A 107 10876 8156 10907 -347 108 248 N
ATOM 1496 CA PHE A 107 25.567 165.093 131.275 1.00 77.81 C
ANISOU 1496 CA PHE A 107 10724 8021 10821 -345 175 238 C
ATOM 1497 C PHE A 107 25.362 164.532 132.673 1.00 83.99 C
ANISOU 1497 C PHE A 107 11455 8827 11632 -322 96 229 C
ATOM 1498 O PHE A 107 24.818 163.429 132.813 1.00 83.60 O
ANISOU 1498 O PHE A 107 11416 8799 11548 -315 104 212 O
ATOM 1499 CB PHE A 107 27.068 165.050 130.925 1.00 78.59 C
ANISOU 1499 CB PHE A 107 10761 8049 11051 -357 276 260 C
ATOM 1500 CG PHE A 107 27.756 163.735 131.241 1.00 78.16 C
ANISOU 1500 CG PHE A 107 10630 7957 11110 -341 333 261 C
ATOM 1501 CD1 PHE A 107 27.589 162.626 130.417 1.00 78.10 C
ANISOU 1501 CD1 PHE A 107 10684 7932 11059 -348 452 232 C
ATOM 1502 CD2 PHE A 107 28.588 163.614 132.356 1.00 79.03 C
ANISOU 1502 CD2 PHE A 107 10617 8032 11378 -330 253 300 C
ATOM 1503 CE1 PHE A 107 28.248 161.430 130.694 1.00 78.42 C
ANISOU 1503 CE1 PHE A 107 10647 7920 11231 -327 515 234 C
ATOM 1504 CE2 PHE A 107 29.225 162.403 132.646 1.00 80.67 C
ANISOU 1504 CE2 PHE A 107 10740 8187 11725 -314 284 317 C
ATOM 1505 CZ PHE A 107 29.062 161.326 131.806 1.00 77.83 C
ANISOU 1505 CZ PHE A 107 10423 7809 11340 -305 428 282 C
ATOM 1506 N MET A 108 25.764 165.308 133.709 1.00 81.16 N
ANISOU 1506 N MET A 108 11066 8453 11317 -324 15 243 N
ATOM 1507 CA MET A 108 25.619 164.820 135.065 1.00 81.90 C
ANISOU 1507 CA MET A 108 11164 8550 11406 -329 -65 239 C
ATOM 1508 C MET A 108 24.175 164.531 135.446 1.00 85.79 C
ANISOU 1508 C MET A 108 11716 9089 11792 -316 -64 199 C
ATOM 1509 O MET A 108 23.934 163.546 136.126 1.00 85.72 O
ANISOU 1509 O MET A 108 11718 9089 11763 -321 -78 191 O
ATOM 1510 CB MET A 108 26.306 165.699 136.091 1.00 84.87 C
ANISOU 1510 CB MET A 108 11547 8880 11820 -360 -163 262 C
ATOM 1511 CG MET A 108 26.976 164.866 137.123 1.00 89.73 C
ANISOU 1511 CG MET A 108 12146 9454 12494 -392 -256 297 C
ATOM 1512 SD MET A 108 26.657 165.467 138.757 1.00 95.64 S
ANISOU 1512 SD MET A 108 13038 10169 13130 -453 -378 285 S
ATOM 1513 CE MET A 108 27.041 164.059 139.674 1.00 93.03 C
ANISOU 1513 CE MET A 108 12720 9806 12822 -492 -477 325 C
ATOM 1514 N GLY A 109 23.239 165.338 134.964 1.00 81.90 N
ANISOU 1514 N GLY A 109 11248 8613 11256 -301 -47 184 N
ATOM 1515 CA GLY A 109 21.825 165.111 135.218 1.00 81.34 C
ANISOU 1515 CA GLY A 109 11196 8567 11143 -285 -33 158 C
ATOM 1516 C GLY A 109 21.339 163.788 134.646 1.00 84.42 C
ANISOU 1516 C GLY A 109 11576 8990 11510 -286 -12 157 C
ATOM 1517 O GLY A 109 20.650 163.046 135.344 1.00 84.84 O
ANISOU 1517 O GLY A 109 11634 9057 11545 -286 -5 138 O
ATOM 1518 N VAL A 110 21.706 163.471 133.375 1.00 79.25 N
ANISOU 1518 N VAL A 110 10929 8336 10846 -298 9 174 N
ATOM 1519 CA VAL A 110 21.323 162.234 132.675 1.00 78.08 C
ANISOU 1519 CA VAL A 110 10807 8201 10657 -315 32 170 C
ATOM 1520 C VAL A 110 21.909 161.045 133.390 1.00 83.72 C
ANISOU 1520 C VAL A 110 11501 8913 11395 -310 56 157 C
ATOM 1521 O VAL A 110 21.196 160.085 133.674 1.00 85.36 O
ANISOU 1521 O VAL A 110 11717 9139 11575 -314 50 145 O
ATOM 1522 CB VAL A 110 21.732 162.246 131.201 1.00 81.35 C
ANISOU 1522 CB VAL A 110 11291 8588 11030 -350 73 183 C
ATOM 1523 CG1 VAL A 110 21.256 160.985 130.493 1.00 80.79 C
ANISOU 1523 CG1 VAL A 110 11289 8514 10893 -384 93 172 C
ATOM 1524 CG2 VAL A 110 21.178 163.479 130.513 1.00 81.70 C
ANISOU 1524 CG2 VAL A 110 11369 8623 11050 -366 18 211 C
ATOM 1525 N VAL A 111 23.193 161.138 133.733 1.00 79.14 N
ANISOU 1525 N VAL A 111 10885 8299 10887 -305 68 171 N
ATOM 1526 CA VAL A 111 23.928 160.142 134.490 1.00 78.28 C
ANISOU 1526 CA VAL A 111 10737 8161 10844 -303 58 182 C
ATOM 1527 C VAL A 111 23.248 159.893 135.857 1.00 81.57 C
ANISOU 1527 C VAL A 111 11181 8599 11213 -312 -15 174 C
ATOM 1528 O VAL A 111 23.152 158.738 136.271 1.00 83.09 O
ANISOU 1528 O VAL A 111 11379 8786 11405 -318 -23 175 O
ATOM 1529 CB VAL A 111 25.401 160.599 134.577 1.00 82.36 C
ANISOU 1529 CB VAL A 111 11184 8617 11492 -303 55 219 C
ATOM 1530 CG1 VAL A 111 26.049 160.247 135.893 1.00 82.33 C
ANISOU 1530 CG1 VAL A 111 11142 8574 11568 -317 -52 257 C
ATOM 1531 CG2 VAL A 111 26.195 160.031 133.428 1.00 82.84 C
ANISOU 1531 CG2 VAL A 111 11214 8625 11635 -296 183 222 C
ATOM 1532 N MET A 112 22.721 160.954 136.513 1.00 75.90 N
ANISOU 1532 N MET A 112 10498 7890 10450 -319 -47 162 N
ATOM 1533 CA MET A 112 22.048 160.854 137.817 1.00 75.63 C
ANISOU 1533 CA MET A 112 10530 7852 10353 -342 -71 144 C
ATOM 1534 C MET A 112 20.762 160.050 137.714 1.00 80.54 C
ANISOU 1534 C MET A 112 11158 8509 10933 -335 -18 118 C
ATOM 1535 O MET A 112 20.499 159.222 138.578 1.00 80.65 O
ANISOU 1535 O MET A 112 11217 8515 10910 -360 -22 112 O
ATOM 1536 CB MET A 112 21.729 162.246 138.405 1.00 77.98 C
ANISOU 1536 CB MET A 112 10882 8129 10620 -351 -70 125 C
ATOM 1537 CG MET A 112 22.911 162.966 138.992 1.00 81.67 C
ANISOU 1537 CG MET A 112 11379 8544 11107 -385 -153 152 C
ATOM 1538 SD MET A 112 23.814 162.033 140.241 1.00 86.10 S
ANISOU 1538 SD MET A 112 12010 9047 11656 -455 -277 194 S
ATOM 1539 CE MET A 112 22.834 162.398 141.694 1.00 83.11 C
ANISOU 1539 CE MET A 112 11830 8631 11116 -516 -244 142 C
ATOM 1540 N ILE A 113 19.950 160.315 136.667 1.00 76.99 N
ANISOU 1540 N ILE A 113 10668 8087 10496 -312 15 113 N
ATOM 1541 CA ILE A 113 18.678 159.635 136.419 1.00 76.32 C
ANISOU 1541 CA ILE A 113 10566 8024 10407 -314 40 105 C
ATOM 1542 C ILE A 113 18.961 158.217 135.976 1.00 82.14 C
ANISOU 1542 C ILE A 113 11311 8773 11125 -328 34 111 C
ATOM 1543 O ILE A 113 18.288 157.287 136.432 1.00 83.24 O
ANISOU 1543 O ILE A 113 11459 8919 11250 -343 46 103 O
ATOM 1544 CB ILE A 113 17.777 160.418 135.425 1.00 78.49 C
ANISOU 1544 CB ILE A 113 10796 8301 10725 -302 28 121 C
ATOM 1545 CG1 ILE A 113 17.501 161.864 135.905 1.00 77.73 C
ANISOU 1545 CG1 ILE A 113 10683 8175 10676 -279 49 115 C
ATOM 1546 CG2 ILE A 113 16.480 159.661 135.088 1.00 79.48 C
ANISOU 1546 CG2 ILE A 113 10884 8434 10882 -316 18 134 C
ATOM 1547 CD1 ILE A 113 16.939 162.055 137.231 1.00 79.40 C
ANISOU 1547 CD1 ILE A 113 10916 8355 10898 -278 124 80 C
ATOM 1548 N PHE A 114 19.981 158.040 135.125 1.00 78.22 N
ANISOU 1548 N PHE A 114 10817 8263 10638 -326 37 122 N
ATOM 1549 CA PHE A 114 20.370 156.714 134.683 1.00 78.16 C
ANISOU 1549 CA PHE A 114 10827 8241 10629 -336 62 120 C
ATOM 1550 C PHE A 114 20.755 155.835 135.890 1.00 85.52 C
ANISOU 1550 C PHE A 114 11755 9156 11583 -338 41 126 C
ATOM 1551 O PHE A 114 20.138 154.790 136.091 1.00 86.30 O
ANISOU 1551 O PHE A 114 11874 9261 11656 -353 45 119 O
ATOM 1552 CB PHE A 114 21.517 156.778 133.674 1.00 79.30 C
ANISOU 1552 CB PHE A 114 10978 8345 10808 -332 117 125 C
ATOM 1553 CG PHE A 114 21.890 155.399 133.198 1.00 80.42 C
ANISOU 1553 CG PHE A 114 11146 8446 10965 -339 180 114 C
ATOM 1554 CD1 PHE A 114 21.159 154.772 132.195 1.00 82.98 C
ANISOU 1554 CD1 PHE A 114 11557 8766 11206 -376 208 94 C
ATOM 1555 CD2 PHE A 114 22.940 154.705 133.785 1.00 81.53 C
ANISOU 1555 CD2 PHE A 114 11230 8534 11214 -317 196 130 C
ATOM 1556 CE1 PHE A 114 21.489 153.492 131.773 1.00 83.60 C
ANISOU 1556 CE1 PHE A 114 11682 8790 11291 -387 284 75 C
ATOM 1557 CE2 PHE A 114 23.258 153.422 133.370 1.00 84.35 C
ANISOU 1557 CE2 PHE A 114 11603 8835 11612 -317 269 119 C
ATOM 1558 CZ PHE A 114 22.539 152.830 132.357 1.00 82.65 C
ANISOU 1558 CZ PHE A 114 11490 8616 11295 -350 328 84 C
ATOM 1559 N PHE A 115 21.733 156.291 136.713 1.00 82.56 N
ANISOU 1559 N PHE A 115 11365 8750 11255 -336 -2 148 N
ATOM 1560 CA PHE A 115 22.210 155.578 137.896 1.00 82.34 C
ANISOU 1560 CA PHE A 115 11355 8684 11246 -358 -68 175 C
ATOM 1561 C PHE A 115 21.268 155.705 139.102 1.00 86.75 C
ANISOU 1561 C PHE A 115 12000 9256 11705 -396 -88 159 C
ATOM 1562 O PHE A 115 21.510 155.090 140.144 1.00 87.09 O
ANISOU 1562 O PHE A 115 12105 9261 11725 -437 -151 183 O
ATOM 1563 CB PHE A 115 23.639 155.988 138.227 1.00 84.53 C
ANISOU 1563 CB PHE A 115 11586 8899 11631 -360 -137 223 C
ATOM 1564 CG PHE A 115 24.594 155.586 137.129 1.00 86.79 C
ANISOU 1564 CG PHE A 115 11781 9143 12054 -324 -71 238 C
ATOM 1565 CD1 PHE A 115 24.843 154.245 136.856 1.00 89.58 C
ANISOU 1565 CD1 PHE A 115 12107 9452 12478 -312 -33 246 C
ATOM 1566 CD2 PHE A 115 25.246 156.548 136.361 1.00 89.72 C
ANISOU 1566 CD2 PHE A 115 12103 9500 12487 -307 -22 241 C
ATOM 1567 CE1 PHE A 115 25.733 153.872 135.840 1.00 91.00 C
ANISOU 1567 CE1 PHE A 115 12215 9564 12798 -280 77 250 C
ATOM 1568 CE2 PHE A 115 26.124 156.170 135.333 1.00 92.92 C
ANISOU 1568 CE2 PHE A 115 12441 9844 13021 -282 88 247 C
ATOM 1569 CZ PHE A 115 26.359 154.835 135.079 1.00 90.94 C
ANISOU 1569 CZ PHE A 115 12166 9538 12847 -268 150 248 C
ATOM 1570 N GLY A 116 20.178 156.449 138.932 1.00 82.59 N
ANISOU 1570 N GLY A 116 11482 8767 11131 -389 -28 124 N
ATOM 1571 CA GLY A 116 19.147 156.582 139.948 1.00 82.74 C
ANISOU 1571 CA GLY A 116 11575 8781 11083 -421 17 98 C
ATOM 1572 C GLY A 116 18.155 155.452 139.786 1.00 86.80 C
ANISOU 1572 C GLY A 116 12072 9318 11592 -427 63 89 C
ATOM 1573 O GLY A 116 18.111 154.519 140.596 1.00 87.05 O
ANISOU 1573 O GLY A 116 12168 9327 11578 -466 54 95 O
ATOM 1574 N LEU A 117 17.408 155.506 138.681 1.00 82.01 N
ANISOU 1574 N LEU A 117 11385 8744 11031 -399 90 84 N
ATOM 1575 CA LEU A 117 16.413 154.523 138.300 1.00 81.49 C
ANISOU 1575 CA LEU A 117 11290 8695 10979 -413 109 85 C
ATOM 1576 C LEU A 117 16.936 153.112 138.076 1.00 83.66 C
ANISOU 1576 C LEU A 117 11591 8965 11232 -428 76 95 C
ATOM 1577 O LEU A 117 16.233 152.178 138.450 1.00 83.63 O
ANISOU 1577 O LEU A 117 11603 8958 11214 -457 95 94 O
ATOM 1578 CB LEU A 117 15.695 154.999 137.056 1.00 81.85 C
ANISOU 1578 CB LEU A 117 11263 8757 11080 -399 92 97 C
ATOM 1579 CG LEU A 117 14.419 155.730 137.313 1.00 87.83 C
ANISOU 1579 CG LEU A 117 11952 9500 11920 -394 136 99 C
ATOM 1580 CD1 LEU A 117 14.271 156.886 136.352 1.00 88.55 C
ANISOU 1580 CD1 LEU A 117 11986 9587 12072 -370 88 122 C
ATOM 1581 CD2 LEU A 117 13.240 154.776 137.209 1.00 91.23 C
ANISOU 1581 CD2 LEU A 117 12333 9925 12406 -425 143 115 C
ATOM 1582 N SER A 118 18.131 152.939 137.456 1.00 78.72 N
ANISOU 1582 N SER A 118 10964 8324 10621 -408 46 106 N
ATOM 1583 CA SER A 118 18.679 151.604 137.182 1.00 78.88 C
ANISOU 1583 CA SER A 118 11001 8314 10655 -413 41 113 C
ATOM 1584 C SER A 118 18.726 150.662 138.432 1.00 85.19 C
ANISOU 1584 C SER A 118 11843 9086 11438 -442 12 130 C
ATOM 1585 O SER A 118 18.003 149.655 138.394 1.00 83.88 O
ANISOU 1585 O SER A 118 11697 8923 11250 -466 28 124 O
ATOM 1586 CB SER A 118 20.032 151.677 136.492 1.00 80.69 C
ANISOU 1586 CB SER A 118 11206 8502 10949 -383 53 122 C
ATOM 1587 OG SER A 118 19.890 152.245 135.208 1.00 87.98 O
ANISOU 1587 OG SER A 118 12136 9437 11855 -378 95 105 O
ATOM 1588 N PRO A 119 19.463 150.972 139.556 1.00 83.11 N
ANISOU 1588 N PRO A 119 11616 8789 11174 -457 -45 156 N
ATOM 1589 CA PRO A 119 19.444 150.060 140.722 1.00 83.79 C
ANISOU 1589 CA PRO A 119 11781 8834 11219 -507 -93 182 C
ATOM 1590 C PRO A 119 18.048 149.764 141.310 1.00 90.68 C
ANISOU 1590 C PRO A 119 12717 9732 12005 -551 -24 155 C
ATOM 1591 O PRO A 119 17.856 148.720 141.965 1.00 92.38 O
ANISOU 1591 O PRO A 119 12997 9918 12186 -595 -40 172 O
ATOM 1592 CB PRO A 119 20.376 150.738 141.741 1.00 85.47 C
ANISOU 1592 CB PRO A 119 12054 8997 11424 -539 -191 222 C
ATOM 1593 CG PRO A 119 20.555 152.100 141.273 1.00 89.43 C
ANISOU 1593 CG PRO A 119 12510 9527 11943 -506 -166 201 C
ATOM 1594 CD PRO A 119 20.378 152.105 139.798 1.00 84.35 C
ANISOU 1594 CD PRO A 119 11761 8927 11360 -446 -90 173 C
ATOM 1595 N LEU A 120 17.071 150.664 141.049 1.00 85.54 N
ANISOU 1595 N LEU A 120 12034 9122 11346 -541 59 119 N
ATOM 1596 CA LEU A 120 15.689 150.516 141.489 1.00 84.45 C
ANISOU 1596 CA LEU A 120 11911 8991 11187 -575 155 97 C
ATOM 1597 C LEU A 120 14.937 149.552 140.583 1.00 87.37 C
ANISOU 1597 C LEU A 120 12204 9384 11607 -571 162 100 C
ATOM 1598 O LEU A 120 14.264 148.636 141.063 1.00 86.83 O
ANISOU 1598 O LEU A 120 12166 9301 11523 -614 196 103 O
ATOM 1599 CB LEU A 120 15.009 151.878 141.526 1.00 84.32 C
ANISOU 1599 CB LEU A 120 11857 8981 11201 -556 240 69 C
ATOM 1600 CG LEU A 120 15.524 152.783 142.623 1.00 89.77 C
ANISOU 1600 CG LEU A 120 12669 9627 11813 -585 260 55 C
ATOM 1601 CD1 LEU A 120 15.043 154.232 142.432 1.00 90.19 C
ANISOU 1601 CD1 LEU A 120 12669 9677 11921 -549 341 26 C
ATOM 1602 CD2 LEU A 120 15.164 152.228 143.985 1.00 92.08 C
ANISOU 1602 CD2 LEU A 120 13122 9861 12002 -668 329 46 C
ATOM 1603 N LEU A 121 15.082 149.737 139.267 1.00 83.24 N
ANISOU 1603 N LEU A 121 11607 8887 11131 -533 123 101 N
ATOM 1604 CA LEU A 121 14.432 148.884 138.281 1.00 82.54 C
ANISOU 1604 CA LEU A 121 11485 8807 11070 -550 103 107 C
ATOM 1605 C LEU A 121 15.038 147.488 138.297 1.00 87.61 C
ANISOU 1605 C LEU A 121 12187 9419 11681 -565 77 112 C
ATOM 1606 O LEU A 121 14.298 146.520 138.176 1.00 88.12 O
ANISOU 1606 O LEU A 121 12258 9476 11746 -604 77 116 O
ATOM 1607 CB LEU A 121 14.526 149.488 136.883 1.00 81.65 C
ANISOU 1607 CB LEU A 121 11336 8709 10978 -530 62 108 C
ATOM 1608 CG LEU A 121 13.905 150.851 136.673 1.00 84.98 C
ANISOU 1608 CG LEU A 121 11686 9147 11456 -513 63 116 C
ATOM 1609 CD1 LEU A 121 14.455 151.491 135.416 1.00 84.85 C
ANISOU 1609 CD1 LEU A 121 11681 9132 11424 -501 10 123 C
ATOM 1610 CD2 LEU A 121 12.401 150.771 136.646 1.00 84.58 C
ANISOU 1610 CD2 LEU A 121 11554 9087 11495 -546 65 140 C
ATOM 1611 N LEU A 122 16.371 147.382 138.475 1.00 83.78 N
ANISOU 1611 N LEU A 122 11732 8904 11197 -537 51 120 N
ATOM 1612 CA LEU A 122 17.065 146.096 138.552 1.00 83.12 C
ANISOU 1612 CA LEU A 122 11685 8766 11130 -541 28 134 C
ATOM 1613 C LEU A 122 16.735 145.400 139.874 1.00 87.71 C
ANISOU 1613 C LEU A 122 12328 9325 11673 -589 8 157 C
ATOM 1614 O LEU A 122 16.684 144.164 139.917 1.00 88.69 O
ANISOU 1614 O LEU A 122 12484 9411 11802 -610 -4 169 O
ATOM 1615 CB LEU A 122 18.573 146.254 138.372 1.00 82.71 C
ANISOU 1615 CB LEU A 122 11611 8664 11152 -494 6 151 C
ATOM 1616 CG LEU A 122 19.031 146.486 136.959 1.00 86.15 C
ANISOU 1616 CG LEU A 122 12022 9086 11625 -460 63 124 C
ATOM 1617 CD1 LEU A 122 20.090 147.538 136.914 1.00 86.35 C
ANISOU 1617 CD1 LEU A 122 11995 9102 11712 -420 63 136 C
ATOM 1618 CD2 LEU A 122 19.557 145.240 136.371 1.00 87.89 C
ANISOU 1618 CD2 LEU A 122 12263 9226 11905 -451 107 119 C
ATOM 1619 N GLY A 123 16.472 146.190 140.919 1.00 82.89 N
ANISOU 1619 N GLY A 123 11756 8726 11011 -615 18 161 N
ATOM 1620 CA GLY A 123 16.044 145.664 142.212 1.00 83.09 C
ANISOU 1620 CA GLY A 123 11886 8719 10964 -684 25 178 C
ATOM 1621 C GLY A 123 14.681 145.001 142.089 1.00 85.76 C
ANISOU 1621 C GLY A 123 12209 9077 11301 -720 105 161 C
ATOM 1622 O GLY A 123 14.444 143.931 142.667 1.00 84.98 O
ANISOU 1622 O GLY A 123 12178 8942 11167 -772 101 179 O
ATOM 1623 N ALA A 124 13.790 145.640 141.280 1.00 81.67 N
ANISOU 1623 N ALA A 124 11589 8605 10838 -698 161 136 N
ATOM 1624 CA ALA A 124 12.440 145.188 140.950 1.00 81.66 C
ANISOU 1624 CA ALA A 124 11523 8614 10889 -731 213 134 C
ATOM 1625 C ALA A 124 12.509 143.979 140.034 1.00 87.49 C
ANISOU 1625 C ALA A 124 12258 9344 11639 -740 143 144 C
ATOM 1626 O ALA A 124 11.721 143.058 140.208 1.00 89.11 O
ANISOU 1626 O ALA A 124 12471 9531 11855 -792 160 155 O
ATOM 1627 CB ALA A 124 11.654 146.306 140.290 1.00 82.12 C
ANISOU 1627 CB ALA A 124 11462 8701 11038 -704 242 127 C
ATOM 1628 N ALA A 125 13.465 143.967 139.074 1.00 83.43 N
ANISOU 1628 N ALA A 125 11749 8828 11123 -697 84 136 N
ATOM 1629 CA ALA A 125 13.724 142.862 138.152 1.00 83.10 C
ANISOU 1629 CA ALA A 125 11744 8753 11079 -706 48 132 C
ATOM 1630 C ALA A 125 14.075 141.585 138.948 1.00 91.85 C
ANISOU 1630 C ALA A 125 12920 9808 12171 -729 41 148 C
ATOM 1631 O ALA A 125 13.560 140.510 138.635 1.00 92.93 O
ANISOU 1631 O ALA A 125 13087 9917 12305 -771 33 149 O
ATOM 1632 CB ALA A 125 14.865 143.226 137.224 1.00 82.85 C
ANISOU 1632 CB ALA A 125 11722 8703 11053 -654 41 114 C
ATOM 1633 N MET A 126 14.922 141.723 139.995 1.00 90.49 N
ANISOU 1633 N MET A 126 12782 9612 11990 -712 23 170 N
ATOM 1634 CA MET A 126 15.344 140.659 140.911 1.00 91.56 C
ANISOU 1634 CA MET A 126 12991 9682 12114 -742 -17 207 C
ATOM 1635 C MET A 126 14.170 140.135 141.725 1.00 93.28 C
ANISOU 1635 C MET A 126 13262 9906 12275 -821 21 215 C
ATOM 1636 O MET A 126 14.091 138.937 141.969 1.00 92.71 O
ANISOU 1636 O MET A 126 13244 9784 12197 -858 -1 236 O
ATOM 1637 CB MET A 126 16.382 141.212 141.879 1.00 95.21 C
ANISOU 1637 CB MET A 126 13489 10112 12574 -731 -81 244 C
ATOM 1638 CG MET A 126 17.781 140.772 141.573 1.00100.87 C
ANISOU 1638 CG MET A 126 14174 10752 13402 -679 -152 277 C
ATOM 1639 SD MET A 126 19.019 141.721 142.488 1.00106.98 S
ANISOU 1639 SD MET A 126 14952 11485 14211 -671 -264 335 S
ATOM 1640 CE MET A 126 18.528 141.336 144.132 1.00104.79 C
ANISOU 1640 CE MET A 126 14851 11173 13793 -785 -338 384 C
ATOM 1641 N ALA A 127 13.279 141.042 142.175 1.00 89.41 N
ANISOU 1641 N ALA A 127 12753 9460 11757 -847 97 200 N
ATOM 1642 CA ALA A 127 12.087 140.708 142.956 1.00 90.03 C
ANISOU 1642 CA ALA A 127 12865 9531 11811 -923 186 204 C
ATOM 1643 C ALA A 127 11.121 139.838 142.131 1.00 94.92 C
ANISOU 1643 C ALA A 127 13413 10157 12497 -950 191 203 C
ATOM 1644 O ALA A 127 10.464 138.936 142.682 1.00 96.01 O
ANISOU 1644 O ALA A 127 13595 10262 12624 -1018 230 220 O
ATOM 1645 CB ALA A 127 11.400 141.978 143.415 1.00 90.82 C
ANISOU 1645 CB ALA A 127 12934 9655 11916 -928 299 180 C
ATOM 1646 N SER A 128 11.080 140.113 140.799 1.00 89.72 N
ANISOU 1646 N SER A 128 12666 9528 11897 -909 142 188 N
ATOM 1647 CA SER A 128 10.312 139.416 139.769 1.00 89.01 C
ANISOU 1647 CA SER A 128 12531 9431 11856 -946 100 193 C
ATOM 1648 C SER A 128 10.963 138.066 139.410 1.00 93.06 C
ANISOU 1648 C SER A 128 13139 9890 12328 -956 46 191 C
ATOM 1649 O SER A 128 10.216 137.118 139.172 1.00 94.05 O
ANISOU 1649 O SER A 128 13278 9987 12469 -1020 28 202 O
ATOM 1650 CB SER A 128 10.161 140.284 138.525 1.00 90.63 C
ANISOU 1650 CB SER A 128 12665 9668 12104 -919 50 183 C
ATOM 1651 OG SER A 128 9.505 141.505 138.823 1.00 97.23 O
ANISOU 1651 OG SER A 128 13395 10537 13010 -905 98 191 O
ATOM 1652 N GLU A 129 12.332 137.963 139.375 1.00 87.91 N
ANISOU 1652 N GLU A 129 12543 9208 11652 -896 24 181 N
ATOM 1653 CA GLU A 129 13.010 136.681 139.136 1.00 87.71 C
ANISOU 1653 CA GLU A 129 12594 9102 11630 -894 -1 181 C
ATOM 1654 C GLU A 129 12.630 135.751 140.293 1.00 94.18 C
ANISOU 1654 C GLU A 129 13466 9887 12429 -952 -5 218 C
ATOM 1655 O GLU A 129 12.237 134.606 140.051 1.00 95.33 O
ANISOU 1655 O GLU A 129 13656 9988 12578 -999 -17 221 O
ATOM 1656 CB GLU A 129 14.542 136.809 139.050 1.00 88.47 C
ANISOU 1656 CB GLU A 129 12698 9149 11769 -814 -9 181 C
ATOM 1657 CG GLU A 129 15.255 135.499 138.679 1.00 98.60 C
ANISOU 1657 CG GLU A 129 14036 10321 13106 -799 -8 180 C
ATOM 1658 CD GLU A 129 15.658 134.499 139.764 1.00118.97 C
ANISOU 1658 CD GLU A 129 16657 12824 15723 -814 -60 234 C
ATOM 1659 OE1 GLU A 129 15.338 134.741 140.952 1.00112.48 O
ANISOU 1659 OE1 GLU A 129 15854 12035 14850 -854 -102 277 O
ATOM 1660 OE2 GLU A 129 16.339 133.495 139.434 1.00101.50 O1-
ANISOU 1660 OE2 GLU A 129 14472 10503 13592 -789 -53 237 O1-
ATOM 1661 N ARG A 130 12.751 136.251 141.543 1.00 90.62 N
ANISOU 1661 N ARG A 130 13039 9448 11943 -963 5 247 N
ATOM 1662 CA ARG A 130 12.394 135.503 142.743 1.00 90.95 C
ANISOU 1662 CA ARG A 130 13173 9450 11935 -1038 10 285 C
ATOM 1663 C ARG A 130 10.936 135.117 142.693 1.00 95.03 C
ANISOU 1663 C ARG A 130 13662 9987 12459 -1113 81 279 C
ATOM 1664 O ARG A 130 10.647 133.935 142.840 1.00 94.86 O
ANISOU 1664 O ARG A 130 13697 9915 12432 -1167 65 300 O
ATOM 1665 CB ARG A 130 12.696 136.289 144.035 1.00 91.46 C
ANISOU 1665 CB ARG A 130 13314 9511 11924 -1061 19 310 C
ATOM 1666 CG ARG A 130 14.175 136.486 144.376 1.00 99.19 C
ANISOU 1666 CG ARG A 130 14333 10442 12914 -1014 -96 346 C
ATOM 1667 CD ARG A 130 15.119 135.334 144.042 1.00107.13 C
ANISOU 1667 CD ARG A 130 15342 11357 14007 -982 -195 384 C
ATOM 1668 NE ARG A 130 14.809 134.068 144.702 1.00115.39 N
ANISOU 1668 NE ARG A 130 16491 12332 15018 -1057 -228 427 N
ATOM 1669 CZ ARG A 130 15.041 132.877 144.158 1.00130.07 C
ANISOU 1669 CZ ARG A 130 18339 14123 16959 -1039 -256 436 C
ATOM 1670 NH1 ARG A 130 15.581 132.786 142.947 1.00108.70 N
ANISOU 1670 NH1 ARG A 130 15539 11401 14362 -954 -235 397 N
ATOM 1671 NH2 ARG A 130 14.725 131.768 144.815 1.00122.70 N
ANISOU 1671 NH2 ARG A 130 17507 13123 15990 -1114 -290 479 N
ATOM 1672 N TYR A 131 10.022 136.082 142.418 1.00 91.78 N
ANISOU 1672 N TYR A 131 13146 9637 12089 -1115 150 259 N
ATOM 1673 CA TYR A 131 8.597 135.771 142.338 1.00 92.58 C
ANISOU 1673 CA TYR A 131 13176 9741 12260 -1187 211 268 C
ATOM 1674 C TYR A 131 8.304 134.651 141.342 1.00 97.65 C
ANISOU 1674 C TYR A 131 13814 10352 12935 -1220 126 274 C
ATOM 1675 O TYR A 131 7.727 133.643 141.736 1.00 97.57 O
ANISOU 1675 O TYR A 131 13846 10300 12928 -1292 140 298 O
ATOM 1676 CB TYR A 131 7.724 137.011 142.081 1.00 93.79 C
ANISOU 1676 CB TYR A 131 13183 9940 12513 -1173 278 260 C
ATOM 1677 CG TYR A 131 6.283 136.664 141.757 1.00 96.64 C
ANISOU 1677 CG TYR A 131 13421 10283 13013 -1243 306 288 C
ATOM 1678 CD1 TYR A 131 5.324 136.554 142.764 1.00 99.03 C
ANISOU 1678 CD1 TYR A 131 13700 10550 13376 -1309 460 305 C
ATOM 1679 CD2 TYR A 131 5.883 136.413 140.444 1.00 97.99 C
ANISOU 1679 CD2 TYR A 131 13513 10456 13261 -1259 177 304 C
ATOM 1680 CE1 TYR A 131 4.000 136.216 142.470 1.00100.08 C
ANISOU 1680 CE1 TYR A 131 13687 10651 13688 -1375 487 344 C
ATOM 1681 CE2 TYR A 131 4.570 136.052 140.142 1.00100.16 C
ANISOU 1681 CE2 TYR A 131 13665 10699 13691 -1338 162 350 C
ATOM 1682 CZ TYR A 131 3.630 135.961 141.154 1.00107.54 C
ANISOU 1682 CZ TYR A 131 14532 11601 14729 -1389 318 373 C
ATOM 1683 OH TYR A 131 2.338 135.636 140.815 1.00108.68 O
ANISOU 1683 OH TYR A 131 14519 11700 15073 -1467 300 429 O
ATOM 1684 N LEU A 132 8.715 134.806 140.073 1.00 95.02 N
ANISOU 1684 N LEU A 132 13461 10030 12613 -1179 44 251 N
ATOM 1685 CA LEU A 132 8.458 133.786 139.053 1.00 95.43 C
ANISOU 1685 CA LEU A 132 13556 10034 12668 -1226 -35 248 C
ATOM 1686 C LEU A 132 9.143 132.454 139.375 1.00 98.72 C
ANISOU 1686 C LEU A 132 14097 10376 13036 -1233 -44 247 C
ATOM 1687 O LEU A 132 8.460 131.445 139.428 1.00 99.38 O
ANISOU 1687 O LEU A 132 14213 10417 13131 -1310 -61 266 O
ATOM 1688 CB LEU A 132 8.792 134.280 137.632 1.00 95.28 C
ANISOU 1688 CB LEU A 132 13548 10020 12633 -1198 -101 217 C
ATOM 1689 CG LEU A 132 7.967 135.484 137.123 1.00100.09 C
ANISOU 1689 CG LEU A 132 14036 10685 13310 -1209 -136 235 C
ATOM 1690 CD1 LEU A 132 8.769 136.325 136.146 1.00 99.89 C
ANISOU 1690 CD1 LEU A 132 14049 10673 13234 -1154 -168 202 C
ATOM 1691 CD2 LEU A 132 6.671 135.051 136.485 1.00102.72 C
ANISOU 1691 CD2 LEU A 132 14323 10988 13719 -1317 -231 277 C
ATOM 1692 N GLY A 133 10.437 132.482 139.696 1.00 93.62 N
ANISOU 1692 N GLY A 133 13505 9704 12361 -1157 -37 238 N
ATOM 1693 CA GLY A 133 11.229 131.294 140.024 1.00 92.95 C
ANISOU 1693 CA GLY A 133 13517 9527 12275 -1149 -58 252 C
ATOM 1694 C GLY A 133 10.754 130.457 141.196 1.00 94.88 C
ANISOU 1694 C GLY A 133 13815 9737 12496 -1221 -56 300 C
ATOM 1695 O GLY A 133 11.044 129.258 141.262 1.00 93.23 O
ANISOU 1695 O GLY A 133 13685 9441 12297 -1241 -88 316 O
ATOM 1696 N ILE A 134 10.040 131.103 142.133 1.00 92.53 N
ANISOU 1696 N ILE A 134 13490 9497 12172 -1264 -3 322 N
ATOM 1697 CA ILE A 134 9.477 130.508 143.348 1.00 93.57 C
ANISOU 1697 CA ILE A 134 13698 9595 12260 -1352 36 364 C
ATOM 1698 C ILE A 134 8.034 130.069 143.109 1.00102.69 C
ANISOU 1698 C ILE A 134 14793 10759 13464 -1440 89 368 C
ATOM 1699 O ILE A 134 7.708 128.917 143.394 1.00104.77 O
ANISOU 1699 O ILE A 134 15127 10963 13720 -1511 79 395 O
ATOM 1700 CB ILE A 134 9.616 131.470 144.572 1.00 95.59 C
ANISOU 1700 CB ILE A 134 14001 9874 12443 -1362 96 381 C
ATOM 1701 CG1 ILE A 134 11.067 131.521 145.060 1.00 95.44 C
ANISOU 1701 CG1 ILE A 134 14074 9806 12384 -1313 -9 411 C
ATOM 1702 CG2 ILE A 134 8.670 131.104 145.713 1.00 96.49 C
ANISOU 1702 CG2 ILE A 134 14200 9959 12502 -1478 202 409 C
ATOM 1703 CD1 ILE A 134 11.391 132.692 145.871 1.00104.21 C
ANISOU 1703 CD1 ILE A 134 15226 10943 13427 -1309 11 415 C
ATOM 1704 N THR A 135 7.176 130.977 142.595 1.00100.69 N
ANISOU 1704 N THR A 135 14403 10571 13286 -1440 132 351 N
ATOM 1705 CA THR A 135 5.760 130.692 142.376 1.00102.27 C
ANISOU 1705 CA THR A 135 14503 10766 13590 -1528 167 373 C
ATOM 1706 C THR A 135 5.557 129.706 141.228 1.00110.80 C
ANISOU 1706 C THR A 135 15596 11805 14697 -1567 44 374 C
ATOM 1707 O THR A 135 4.784 128.760 141.382 1.00111.53 O
ANISOU 1707 O THR A 135 15696 11850 14830 -1658 44 405 O
ATOM 1708 CB THR A 135 4.912 131.972 142.250 1.00105.76 C
ANISOU 1708 CB THR A 135 14774 11260 14149 -1517 241 374 C
ATOM 1709 OG1 THR A 135 5.271 132.714 141.085 1.00104.05 O
ANISOU 1709 OG1 THR A 135 14495 11087 13953 -1452 138 351 O
ATOM 1710 CG2 THR A 135 4.977 132.845 143.499 1.00102.28 C
ANISOU 1710 CG2 THR A 135 14359 10833 13669 -1501 401 365 C
ATOM 1711 N ARG A 136 6.259 129.899 140.108 1.00110.81 N
ANISOU 1711 N ARG A 136 15624 11811 14667 -1509 -48 338 N
ATOM 1712 CA ARG A 136 6.170 129.007 138.954 1.00113.27 C
ANISOU 1712 CA ARG A 136 16007 12063 14967 -1558 -153 326 C
ATOM 1713 C ARG A 136 7.174 127.866 139.175 1.00123.61 C
ANISOU 1713 C ARG A 136 17470 13291 16204 -1533 -151 307 C
ATOM 1714 O ARG A 136 8.100 128.067 139.967 1.00121.44 O
ANISOU 1714 O ARG A 136 17223 13019 15899 -1459 -106 308 O
ATOM 1715 CB ARG A 136 6.445 129.763 137.635 1.00113.65 C
ANISOU 1715 CB ARG A 136 16055 12130 14998 -1527 -226 292 C
ATOM 1716 CG ARG A 136 5.787 131.158 137.506 1.00129.31 C
ANISOU 1716 CG ARG A 136 17877 14190 17064 -1515 -233 314 C
ATOM 1717 CD ARG A 136 4.277 131.124 137.289 1.00147.43 C
ANISOU 1717 CD ARG A 136 20041 16475 19502 -1623 -300 377 C
ATOM 1718 NE ARG A 136 3.665 132.451 137.412 1.00158.70 N
ANISOU 1718 NE ARG A 136 21283 17957 21060 -1596 -277 408 N
ATOM 1719 CZ ARG A 136 3.468 133.290 136.397 1.00176.06 C
ANISOU 1719 CZ ARG A 136 23432 20166 23297 -1598 -393 423 C
ATOM 1720 NH1 ARG A 136 3.853 132.960 135.167 1.00163.72 N
ANISOU 1720 NH1 ARG A 136 22022 18564 21621 -1639 -532 404 N
ATOM 1721 NH2 ARG A 136 2.895 134.469 136.604 1.00163.82 N
ANISOU 1721 NH2 ARG A 136 21698 18650 21894 -1567 -364 457 N
ATOM 1722 N PRO A 137 7.009 126.650 138.558 1.00128.12 N
ANISOU 1722 N PRO A 137 18145 13774 16760 -1599 -207 299 N
ATOM 1723 CA PRO A 137 7.979 125.557 138.820 1.00130.22 C
ANISOU 1723 CA PRO A 137 18543 13941 16994 -1564 -192 286 C
ATOM 1724 C PRO A 137 9.452 125.989 138.827 1.00139.22 C
ANISOU 1724 C PRO A 137 19704 15063 18129 -1435 -154 256 C
ATOM 1725 O PRO A 137 9.859 126.842 138.021 1.00139.66 O
ANISOU 1725 O PRO A 137 19735 15154 18176 -1380 -141 215 O
ATOM 1726 CB PRO A 137 7.684 124.519 137.712 1.00132.31 C
ANISOU 1726 CB PRO A 137 18929 14109 17235 -1642 -248 256 C
ATOM 1727 CG PRO A 137 6.618 125.131 136.831 1.00136.36 C
ANISOU 1727 CG PRO A 137 19384 14673 17754 -1726 -326 262 C
ATOM 1728 CD PRO A 137 5.943 126.195 137.633 1.00131.15 C
ANISOU 1728 CD PRO A 137 18537 14126 17168 -1716 -298 310 C
ATOM 1729 N PHE A 138 10.242 125.440 139.766 1.00138.34 N
ANISOU 1729 N PHE A 138 19632 14888 18042 -1393 -146 288 N
ATOM 1730 CA PHE A 138 11.669 125.752 139.849 1.00138.99 C
ANISOU 1730 CA PHE A 138 19707 14928 18176 -1276 -131 282 C
ATOM 1731 C PHE A 138 12.459 125.009 138.742 1.00144.82 C
ANISOU 1731 C PHE A 138 20523 15534 18968 -1229 -89 227 C
ATOM 1732 O PHE A 138 13.172 124.024 138.988 1.00144.56 O
ANISOU 1732 O PHE A 138 20535 15371 19020 -1193 -86 246 O
ATOM 1733 CB PHE A 138 12.227 125.528 141.264 1.00141.21 C
ANISOU 1733 CB PHE A 138 19997 15174 18481 -1262 -175 359 C
ATOM 1734 N SER A 139 12.267 125.495 137.505 1.00142.75 N
ANISOU 1734 N SER A 139 20289 15293 18656 -1240 -51 159 N
ATOM 1735 CA SER A 139 12.895 125.040 136.266 1.00143.76 C
ANISOU 1735 CA SER A 139 20531 15297 18794 -1215 33 84 C
ATOM 1736 C SER A 139 13.909 126.143 135.928 1.00147.11 C
ANISOU 1736 C SER A 139 20883 15748 19265 -1108 103 58 C
ATOM 1737 O SER A 139 13.505 127.283 135.631 1.00146.29 O
ANISOU 1737 O SER A 139 20730 15763 19091 -1120 80 49 O
ATOM 1738 CB SER A 139 11.848 124.902 135.155 1.00148.21 C
ANISOU 1738 CB SER A 139 21216 15864 19234 -1334 5 37 C
ATOM 1739 OG SER A 139 10.607 124.393 135.628 1.00156.77 O
ANISOU 1739 OG SER A 139 22271 17015 20280 -1446 -103 87 O
ATOM 1740 N ARG A 140 15.222 125.835 136.067 1.00143.09 N
ANISOU 1740 N ARG A 140 20342 15121 18904 -1002 180 60 N
ATOM 1741 CA ARG A 140 16.300 126.813 135.838 1.00141.76 C
ANISOU 1741 CA ARG A 140 20082 14956 18824 -898 251 48 C
ATOM 1742 C ARG A 140 17.168 126.504 134.594 1.00144.25 C
ANISOU 1742 C ARG A 140 20487 15111 19208 -851 437 -36 C
ATOM 1743 O ARG A 140 18.357 126.183 134.771 1.00145.01 O
ANISOU 1743 O ARG A 140 20509 15071 19516 -751 520 -20 O
ATOM 1744 CB ARG A 140 17.172 126.989 137.103 1.00141.20 C
ANISOU 1744 CB ARG A 140 19864 14879 18906 -818 176 140 C
ATOM 1745 N PRO A 141 16.629 126.613 133.334 1.00137.84 N
ANISOU 1745 N PRO A 141 19844 14293 18237 -929 509 -122 N
ATOM 1746 CA PRO A 141 17.478 126.347 132.161 1.00137.40 C
ANISOU 1746 CA PRO A 141 19921 14064 18221 -900 727 -213 C
ATOM 1747 C PRO A 141 18.363 127.548 131.858 1.00135.88 C
ANISOU 1747 C PRO A 141 19626 13902 18100 -814 821 -224 C
ATOM 1748 O PRO A 141 18.012 128.364 130.999 1.00136.42 O
ANISOU 1748 O PRO A 141 19784 14044 18006 -870 832 -266 O
ATOM 1749 CB PRO A 141 16.475 126.040 131.030 1.00139.93 C
ANISOU 1749 CB PRO A 141 20500 14368 18299 -1050 726 -286 C
ATOM 1750 CG PRO A 141 15.118 126.343 131.583 1.00143.83 C
ANISOU 1750 CG PRO A 141 20939 15039 18672 -1143 492 -219 C
ATOM 1751 CD PRO A 141 15.273 127.018 132.909 1.00138.30 C
ANISOU 1751 CD PRO A 141 19987 14477 18085 -1055 395 -131 C
ATOM 1752 N ALA A 142 19.503 127.661 132.597 1.00127.06 N
ANISOU 1752 N ALA A 142 18316 12722 17239 -685 863 -171 N
ATOM 1753 CA ALA A 142 20.525 128.711 132.485 1.00124.57 C
ANISOU 1753 CA ALA A 142 17865 12411 17056 -593 950 -165 C
ATOM 1754 C ALA A 142 20.986 128.846 131.030 1.00124.97 C
ANISOU 1754 C ALA A 142 18086 12339 17060 -607 1209 -278 C
ATOM 1755 O ALA A 142 20.634 127.995 130.214 1.00127.21 O
ANISOU 1755 O ALA A 142 18599 12511 17223 -686 1317 -357 O
ATOM 1756 CB ALA A 142 21.704 128.354 133.369 1.00126.06 C
ANISOU 1756 CB ALA A 142 17845 12479 17573 -473 953 -84 C
ATOM 1757 N VAL A 143 21.766 129.889 130.694 1.00115.69 N
ANISOU 1757 N VAL A 143 16825 11170 15961 -547 1314 -287 N
ATOM 1758 CA VAL A 143 22.244 130.196 129.323 1.00113.89 C
ANISOU 1758 CA VAL A 143 16775 10828 15670 -572 1579 -393 C
ATOM 1759 C VAL A 143 21.130 130.942 128.625 1.00113.00 C
ANISOU 1759 C VAL A 143 16861 10866 15209 -707 1466 -428 C
ATOM 1760 O VAL A 143 21.367 132.040 128.134 1.00113.02 O
ANISOU 1760 O VAL A 143 16872 10927 15146 -711 1508 -443 O
ATOM 1761 CB VAL A 143 22.910 129.054 128.449 1.00118.48 C
ANISOU 1761 CB VAL A 143 17527 11127 16363 -564 1901 -489 C
ATOM 1762 CG1 VAL A 143 21.922 128.318 127.544 1.00118.45 C
ANISOU 1762 CG1 VAL A 143 17876 11070 16061 -716 1927 -578 C
ATOM 1763 CG2 VAL A 143 24.043 129.615 127.607 1.00119.45 C
ANISOU 1763 CG2 VAL A 143 17667 11112 16605 -515 2210 -553 C
ATOM 1764 N ALA A 144 19.913 130.366 128.643 1.00105.52 N
ANISOU 1764 N ALA A 144 16049 9978 14066 -816 1301 -426 N
ATOM 1765 CA ALA A 144 18.691 130.918 128.085 1.00103.55 C
ANISOU 1765 CA ALA A 144 15958 9856 13532 -956 1135 -431 C
ATOM 1766 C ALA A 144 18.178 131.915 129.105 1.00103.89 C
ANISOU 1766 C ALA A 144 15755 10121 13597 -917 905 -336 C
ATOM 1767 O ALA A 144 17.973 133.094 128.779 1.00103.28 O
ANISOU 1767 O ALA A 144 15667 10146 13428 -938 851 -327 O
ATOM 1768 CB ALA A 144 17.670 129.808 127.872 1.00104.89 C
ANISOU 1768 CB ALA A 144 16312 9982 13559 -1079 1038 -446 C
ATOM 1769 N SER A 145 18.045 131.449 130.364 1.00 97.50 N
ANISOU 1769 N SER A 145 14763 9367 12915 -862 788 -266 N
ATOM 1770 CA SER A 145 17.610 132.261 131.481 1.00 94.80 C
ANISOU 1770 CA SER A 145 14215 9205 12601 -830 605 -182 C
ATOM 1771 C SER A 145 18.552 133.432 131.744 1.00 97.26 C
ANISOU 1771 C SER A 145 14372 9561 13021 -731 650 -162 C
ATOM 1772 O SER A 145 18.071 134.521 132.050 1.00 96.68 O
ANISOU 1772 O SER A 145 14220 9633 12883 -739 540 -129 O
ATOM 1773 CB SER A 145 17.393 131.402 132.714 1.00 97.22 C
ANISOU 1773 CB SER A 145 14418 9515 13006 -807 509 -119 C
ATOM 1774 OG SER A 145 16.124 130.784 132.564 1.00107.06 O
ANISOU 1774 OG SER A 145 15771 10789 14117 -920 410 -120 O
ATOM 1775 N GLN A 146 19.871 133.234 131.538 1.00 92.65 N
ANISOU 1775 N GLN A 146 13747 8837 12619 -643 822 -182 N
ATOM 1776 CA GLN A 146 20.889 134.265 131.690 1.00 90.99 C
ANISOU 1776 CA GLN A 146 13386 8636 12550 -553 880 -160 C
ATOM 1777 C GLN A 146 20.793 135.267 130.521 1.00 92.59 C
ANISOU 1777 C GLN A 146 13709 8869 12602 -598 970 -220 C
ATOM 1778 O GLN A 146 21.020 136.464 130.726 1.00 92.45 O
ANISOU 1778 O GLN A 146 13579 8947 12602 -562 924 -190 O
ATOM 1779 CB GLN A 146 22.287 133.629 131.770 1.00 93.93 C
ANISOU 1779 CB GLN A 146 13659 8815 13213 -452 1045 -153 C
ATOM 1780 CG GLN A 146 23.373 134.621 132.182 1.00121.81 C
ANISOU 1780 CG GLN A 146 16972 12354 16957 -358 1037 -92 C
ATOM 1781 CD GLN A 146 24.764 134.047 132.238 1.00153.19 C
ANISOU 1781 CD GLN A 146 20812 16114 21278 -258 1206 -72 C
ATOM 1782 OE1 GLN A 146 25.248 133.397 131.299 1.00148.43 O
ANISOU 1782 OE1 GLN A 146 20311 15338 20748 -248 1468 -151 O
ATOM 1783 NE2 GLN A 146 25.472 134.361 133.315 1.00153.72 N
ANISOU 1783 NE2 GLN A 146 20649 16174 21582 -189 1065 37 N
ATOM 1784 N ARG A 147 20.457 134.786 129.308 1.00 86.84 N
ANISOU 1784 N ARG A 147 13233 8048 11714 -689 1089 -302 N
ATOM 1785 CA ARG A 147 20.308 135.651 128.144 1.00 86.09 C
ANISOU 1785 CA ARG A 147 13310 7961 11441 -761 1157 -352 C
ATOM 1786 C ARG A 147 19.082 136.510 128.326 1.00 90.04 C
ANISOU 1786 C ARG A 147 13790 8650 11773 -831 907 -302 C
ATOM 1787 O ARG A 147 19.159 137.726 128.156 1.00 89.86 O
ANISOU 1787 O ARG A 147 13717 8708 11719 -820 877 -285 O
ATOM 1788 CB ARG A 147 20.160 134.833 126.878 1.00 86.26 C
ANISOU 1788 CB ARG A 147 13658 7818 11299 -872 1318 -445 C
ATOM 1789 CG ARG A 147 21.468 134.659 126.164 1.00 96.15 C
ANISOU 1789 CG ARG A 147 14981 8868 12683 -819 1655 -520 C
ATOM 1790 CD ARG A 147 21.267 134.089 124.791 1.00 98.22 C
ANISOU 1790 CD ARG A 147 15634 8956 12729 -955 1842 -626 C
ATOM 1791 NE ARG A 147 20.953 132.662 124.824 1.00100.53 N
ANISOU 1791 NE ARG A 147 16047 9140 13009 -995 1855 -657 N
ATOM 1792 CZ ARG A 147 19.731 132.164 124.664 1.00109.53 C
ANISOU 1792 CZ ARG A 147 17366 10330 13919 -1132 1647 -651 C
ATOM 1793 NH1 ARG A 147 18.693 132.978 124.477 1.00 97.77 N
ANISOU 1793 NH1 ARG A 147 15934 8994 12221 -1236 1400 -604 N
ATOM 1794 NH2 ARG A 147 19.535 130.847 124.693 1.00 79.94 N
ANISOU 1794 NH2 ARG A 147 13729 6469 10175 -1167 1676 -681 N
ATOM 1795 N ARG A 148 17.952 135.881 128.705 1.00 85.79 N
ANISOU 1795 N ARG A 148 13272 8169 11155 -899 734 -272 N
ATOM 1796 CA ARG A 148 16.698 136.558 129.005 1.00 84.05 C
ANISOU 1796 CA ARG A 148 12989 8106 10842 -959 506 -212 C
ATOM 1797 C ARG A 148 16.965 137.665 130.063 1.00 82.77 C
ANISOU 1797 C ARG A 148 12574 8076 10800 -855 445 -155 C
ATOM 1798 O ARG A 148 16.523 138.793 129.871 1.00 81.84 O
ANISOU 1798 O ARG A 148 12421 8050 10625 -876 358 -131 O
ATOM 1799 CB ARG A 148 15.654 135.527 129.491 1.00 87.49 C
ANISOU 1799 CB ARG A 148 13431 8555 11255 -1023 375 -183 C
ATOM 1800 CG ARG A 148 14.222 136.052 129.499 1.00107.72 C
ANISOU 1800 CG ARG A 148 15953 11233 13744 -1112 162 -124 C
ATOM 1801 CD ARG A 148 13.204 134.977 129.841 1.00127.12 C
ANISOU 1801 CD ARG A 148 18426 13680 16195 -1190 55 -97 C
ATOM 1802 NE ARG A 148 11.944 135.575 130.296 1.00142.72 N
ANISOU 1802 NE ARG A 148 20257 15769 18202 -1235 -121 -22 N
ATOM 1803 CZ ARG A 148 10.917 134.893 130.800 1.00158.54 C
ANISOU 1803 CZ ARG A 148 22207 17786 20244 -1298 -221 22 C
ATOM 1804 NH1 ARG A 148 10.979 133.571 130.912 1.00148.45 N
ANISOU 1804 NH1 ARG A 148 21027 16426 18952 -1330 -185 -1 N
ATOM 1805 NH2 ARG A 148 9.820 135.529 131.196 1.00140.83 N
ANISOU 1805 NH2 ARG A 148 19806 15628 18076 -1330 -344 92 N
ATOM 1806 N ALA A 149 17.779 137.354 131.105 1.00 76.33 N
ANISOU 1806 N ALA A 149 11602 7246 10152 -752 489 -131 N
ATOM 1807 CA ALA A 149 18.156 138.257 132.195 1.00 73.99 C
ANISOU 1807 CA ALA A 149 11107 7045 9961 -670 427 -77 C
ATOM 1808 C ALA A 149 19.087 139.381 131.781 1.00 80.63 C
ANISOU 1808 C ALA A 149 11903 7883 10850 -615 511 -88 C
ATOM 1809 O ALA A 149 18.859 140.517 132.192 1.00 81.15 O
ANISOU 1809 O ALA A 149 11876 8057 10902 -599 427 -56 O
ATOM 1810 CB ALA A 149 18.740 137.487 133.350 1.00 73.99 C
ANISOU 1810 CB ALA A 149 11002 7000 10110 -609 413 -35 C
ATOM 1811 N TRP A 150 20.116 139.110 130.969 1.00 78.06 N
ANISOU 1811 N TRP A 150 11645 7425 10589 -589 692 -135 N
ATOM 1812 CA TRP A 150 20.977 140.204 130.528 1.00 78.47 C
ANISOU 1812 CA TRP A 150 11655 7467 10694 -546 789 -145 C
ATOM 1813 C TRP A 150 20.196 141.134 129.597 1.00 81.69 C
ANISOU 1813 C TRP A 150 12196 7944 10896 -629 746 -167 C
ATOM 1814 O TRP A 150 20.347 142.351 129.700 1.00 81.72 O
ANISOU 1814 O TRP A 150 12117 8024 10908 -603 708 -142 O
ATOM 1815 CB TRP A 150 22.255 139.697 129.847 1.00 79.50 C
ANISOU 1815 CB TRP A 150 11820 7414 10974 -501 1037 -191 C
ATOM 1816 CG TRP A 150 23.390 139.430 130.792 1.00 81.30 C
ANISOU 1816 CG TRP A 150 11825 7570 11493 -393 1058 -135 C
ATOM 1817 CD1 TRP A 150 23.977 138.224 131.052 1.00 85.38 C
ANISOU 1817 CD1 TRP A 150 12299 7941 12199 -348 1139 -128 C
ATOM 1818 CD2 TRP A 150 24.059 140.390 131.622 1.00 80.60 C
ANISOU 1818 CD2 TRP A 150 11531 7539 11555 -326 966 -64 C
ATOM 1819 NE1 TRP A 150 24.956 138.371 132.007 1.00 84.99 N
ANISOU 1819 NE1 TRP A 150 12017 7853 12421 -260 1078 -44 N
ATOM 1820 CE2 TRP A 150 25.038 139.691 132.365 1.00 85.06 C
ANISOU 1820 CE2 TRP A 150 11933 7983 12401 -252 969 -5 C
ATOM 1821 CE3 TRP A 150 23.921 141.776 131.814 1.00 81.20 C
ANISOU 1821 CE3 TRP A 150 11551 7744 11559 -329 867 -38 C
ATOM 1822 CZ2 TRP A 150 25.861 140.323 133.295 1.00 84.37 C
ANISOU 1822 CZ2 TRP A 150 11642 7901 12515 -196 852 85 C
ATOM 1823 CZ3 TRP A 150 24.744 142.407 132.732 1.00 82.93 C
ANISOU 1823 CZ3 TRP A 150 11578 7970 11960 -268 779 36 C
ATOM 1824 CH2 TRP A 150 25.697 141.681 133.467 1.00 84.60 C
ANISOU 1824 CH2 TRP A 150 11642 8061 12440 -210 759 101 C
ATOM 1825 N ALA A 151 19.328 140.560 128.724 1.00 76.86 N
ANISOU 1825 N ALA A 151 11796 7299 10107 -739 727 -202 N
ATOM 1826 CA ALA A 151 18.485 141.310 127.798 1.00 76.21 C
ANISOU 1826 CA ALA A 151 11863 7260 9834 -843 635 -202 C
ATOM 1827 C ALA A 151 17.558 142.249 128.586 1.00 80.66 C
ANISOU 1827 C ALA A 151 12255 7984 10409 -832 422 -131 C
ATOM 1828 O ALA A 151 17.466 143.433 128.239 1.00 80.76 O
ANISOU 1828 O ALA A 151 12258 8047 10380 -842 374 -112 O
ATOM 1829 CB ALA A 151 17.690 140.362 126.924 1.00 77.72 C
ANISOU 1829 CB ALA A 151 12306 7370 9855 -977 604 -234 C
ATOM 1830 N THR A 152 16.950 141.747 129.696 1.00 75.95 N
ANISOU 1830 N THR A 152 11521 7452 9885 -806 321 -94 N
ATOM 1831 CA THR A 152 16.118 142.549 130.590 1.00 74.50 C
ANISOU 1831 CA THR A 152 11172 7395 9741 -788 177 -36 C
ATOM 1832 C THR A 152 16.953 143.686 131.189 1.00 80.74 C
ANISOU 1832 C THR A 152 11825 8236 10618 -694 216 -23 C
ATOM 1833 O THR A 152 16.457 144.812 131.191 1.00 81.27 O
ANISOU 1833 O THR A 152 11836 8372 10670 -698 141 4 O
ATOM 1834 CB THR A 152 15.476 141.692 131.667 1.00 75.37 C
ANISOU 1834 CB THR A 152 11198 7535 9906 -786 119 -9 C
ATOM 1835 OG1 THR A 152 14.908 140.543 131.056 1.00 75.33 O
ANISOU 1835 OG1 THR A 152 11329 7463 9830 -873 96 -25 O
ATOM 1836 CG2 THR A 152 14.401 142.432 132.437 1.00 69.56 C
ANISOU 1836 CG2 THR A 152 10325 6899 9206 -791 10 41 C
ATOM 1837 N VAL A 153 18.223 143.411 131.655 1.00 77.58 N
ANISOU 1837 N VAL A 153 11366 7783 10326 -615 322 -34 N
ATOM 1838 CA VAL A 153 19.164 144.429 132.206 1.00 76.73 C
ANISOU 1838 CA VAL A 153 11133 7701 10318 -537 344 -14 C
ATOM 1839 C VAL A 153 19.394 145.552 131.154 1.00 82.38 C
ANISOU 1839 C VAL A 153 11903 8420 10976 -551 388 -31 C
ATOM 1840 O VAL A 153 19.229 146.736 131.460 1.00 81.55 O
ANISOU 1840 O VAL A 153 11722 8390 10873 -533 322 -5 O
ATOM 1841 CB VAL A 153 20.509 143.832 132.699 1.00 79.68 C
ANISOU 1841 CB VAL A 153 11434 7983 10859 -468 427 -5 C
ATOM 1842 CG1 VAL A 153 21.449 144.916 133.197 1.00 78.58 C
ANISOU 1842 CG1 VAL A 153 11168 7858 10830 -407 418 29 C
ATOM 1843 CG2 VAL A 153 20.295 142.781 133.768 1.00 79.24 C
ANISOU 1843 CG2 VAL A 153 11340 7917 10853 -464 356 26 C
ATOM 1844 N GLY A 154 19.709 145.152 129.923 1.00 79.89 N
ANISOU 1844 N GLY A 154 11746 8011 10597 -596 505 -77 N
ATOM 1845 CA GLY A 154 19.878 146.067 128.806 1.00 79.76 C
ANISOU 1845 CA GLY A 154 11841 7974 10490 -637 557 -95 C
ATOM 1846 C GLY A 154 18.645 146.921 128.581 1.00 82.46 C
ANISOU 1846 C GLY A 154 12206 8406 10719 -699 382 -58 C
ATOM 1847 O GLY A 154 18.789 148.127 128.368 1.00 82.56 O
ANISOU 1847 O GLY A 154 12191 8453 10725 -689 361 -40 O
ATOM 1848 N LEU A 155 17.415 146.316 128.665 1.00 77.54 N
ANISOU 1848 N LEU A 155 11614 7811 10036 -763 247 -37 N
ATOM 1849 CA LEU A 155 16.143 147.063 128.521 1.00 76.00 C
ANISOU 1849 CA LEU A 155 11395 7680 9801 -820 63 17 C
ATOM 1850 C LEU A 155 15.984 148.017 129.692 1.00 78.17 C
ANISOU 1850 C LEU A 155 11451 8051 10198 -733 17 52 C
ATOM 1851 O LEU A 155 15.610 149.177 129.500 1.00 76.60 O
ANISOU 1851 O LEU A 155 11210 7888 10008 -737 -58 86 O
ATOM 1852 CB LEU A 155 14.901 146.162 128.447 1.00 75.61 C
ANISOU 1852 CB LEU A 155 11390 7623 9717 -905 -65 43 C
ATOM 1853 CG LEU A 155 14.749 145.228 127.256 1.00 80.57 C
ANISOU 1853 CG LEU A 155 12273 8144 10197 -1023 -58 13 C
ATOM 1854 CD1 LEU A 155 13.504 144.402 127.404 1.00 81.51 C
ANISOU 1854 CD1 LEU A 155 12390 8262 10319 -1100 -206 50 C
ATOM 1855 CD2 LEU A 155 14.636 145.971 125.967 1.00 81.01 C
ANISOU 1855 CD2 LEU A 155 12534 8139 10105 -1125 -110 22 C
ATOM 1856 N VAL A 156 16.323 147.541 130.899 1.00 74.54 N
ANISOU 1856 N VAL A 156 10877 7620 9827 -664 64 45 N
ATOM 1857 CA VAL A 156 16.259 148.342 132.107 1.00 74.36 C
ANISOU 1857 CA VAL A 156 10699 7665 9890 -599 42 68 C
ATOM 1858 C VAL A 156 17.120 149.581 131.941 1.00 81.66 C
ANISOU 1858 C VAL A 156 11596 8598 10834 -553 80 66 C
ATOM 1859 O VAL A 156 16.625 150.691 132.173 1.00 84.46 O
ANISOU 1859 O VAL A 156 11882 8998 11213 -541 26 89 O
ATOM 1860 CB VAL A 156 16.619 147.536 133.352 1.00 77.53 C
ANISOU 1860 CB VAL A 156 11044 8067 10347 -561 76 64 C
ATOM 1861 CG1 VAL A 156 16.872 148.460 134.541 1.00 76.94 C
ANISOU 1861 CG1 VAL A 156 10872 8035 10326 -510 70 81 C
ATOM 1862 CG2 VAL A 156 15.527 146.512 133.664 1.00 77.16 C
ANISOU 1862 CG2 VAL A 156 11006 8024 10289 -612 32 75 C
ATOM 1863 N TRP A 157 18.366 149.406 131.450 1.00 76.10 N
ANISOU 1863 N TRP A 157 10944 7836 10136 -532 183 39 N
ATOM 1864 CA TRP A 157 19.283 150.515 131.162 1.00 73.83 C
ANISOU 1864 CA TRP A 157 10634 7540 9878 -498 233 40 C
ATOM 1865 C TRP A 157 18.758 151.448 130.082 1.00 77.53 C
ANISOU 1865 C TRP A 157 11187 8015 10255 -552 189 49 C
ATOM 1866 O TRP A 157 18.778 152.658 130.274 1.00 76.37 O
ANISOU 1866 O TRP A 157 10976 7905 10135 -526 151 71 O
ATOM 1867 CB TRP A 157 20.650 149.986 130.760 1.00 71.66 C
ANISOU 1867 CB TRP A 157 10388 7175 9666 -473 381 13 C
ATOM 1868 CG TRP A 157 21.415 149.432 131.904 1.00 71.43 C
ANISOU 1868 CG TRP A 157 10237 7125 9778 -412 388 31 C
ATOM 1869 CD1 TRP A 157 21.268 149.741 133.227 1.00 73.59 C
ANISOU 1869 CD1 TRP A 157 10409 7455 10096 -384 282 66 C
ATOM 1870 CD2 TRP A 157 22.473 148.484 131.824 1.00 71.83 C
ANISOU 1870 CD2 TRP A 157 10269 7070 9953 -381 501 22 C
ATOM 1871 NE1 TRP A 157 22.180 149.041 133.980 1.00 73.49 N
ANISOU 1871 NE1 TRP A 157 10328 7381 10213 -350 286 91 N
ATOM 1872 CE2 TRP A 157 22.922 148.243 133.146 1.00 75.86 C
ANISOU 1872 CE2 TRP A 157 10653 7581 10589 -338 416 69 C
ATOM 1873 CE3 TRP A 157 23.080 147.792 130.761 1.00 73.75 C
ANISOU 1873 CE3 TRP A 157 10603 7199 10221 -392 677 -20 C
ATOM 1874 CZ2 TRP A 157 23.962 147.347 133.431 1.00 75.81 C
ANISOU 1874 CZ2 TRP A 157 10574 7465 10766 -299 469 91 C
ATOM 1875 CZ3 TRP A 157 24.105 146.905 131.045 1.00 75.86 C
ANISOU 1875 CZ3 TRP A 157 10789 7353 10681 -342 774 -13 C
ATOM 1876 CH2 TRP A 157 24.526 146.676 132.366 1.00 76.31 C
ANISOU 1876 CH2 TRP A 157 10688 7415 10893 -292 654 50 C
ATOM 1877 N ALA A 158 18.276 150.882 128.960 1.00 75.45 N
ANISOU 1877 N ALA A 158 11086 7703 9879 -637 176 40 N
ATOM 1878 CA ALA A 158 17.720 151.646 127.847 1.00 76.12 C
ANISOU 1878 CA ALA A 158 11295 7769 9857 -719 92 65 C
ATOM 1879 C ALA A 158 16.558 152.523 128.334 1.00 81.09 C
ANISOU 1879 C ALA A 158 11790 8469 10552 -709 -73 125 C
ATOM 1880 O ALA A 158 16.551 153.714 128.030 1.00 80.60 O
ANISOU 1880 O ALA A 158 11710 8416 10497 -703 -114 152 O
ATOM 1881 CB ALA A 158 17.262 150.712 126.742 1.00 77.69 C
ANISOU 1881 CB ALA A 158 11707 7895 9918 -835 62 55 C
ATOM 1882 N ALA A 159 15.632 151.959 129.161 1.00 77.99 N
ANISOU 1882 N ALA A 159 11289 8114 10230 -699 -143 143 N
ATOM 1883 CA ALA A 159 14.483 152.683 129.720 1.00 77.16 C
ANISOU 1883 CA ALA A 159 11032 8049 10234 -682 -252 194 C
ATOM 1884 C ALA A 159 14.953 153.777 130.663 1.00 82.21 C
ANISOU 1884 C ALA A 159 11548 8732 10955 -591 -189 185 C
ATOM 1885 O ALA A 159 14.383 154.873 130.648 1.00 82.08 O
ANISOU 1885 O ALA A 159 11461 8719 11005 -581 -254 223 O
ATOM 1886 CB ALA A 159 13.550 151.725 130.444 1.00 77.35 C
ANISOU 1886 CB ALA A 159 10974 8088 10325 -689 -275 202 C
ATOM 1887 N ALA A 160 16.025 153.490 131.455 1.00 79.14 N
ANISOU 1887 N ALA A 160 11142 8360 10569 -533 -76 141 N
ATOM 1888 CA ALA A 160 16.602 154.432 132.425 1.00 78.54 C
ANISOU 1888 CA ALA A 160 10981 8310 10551 -465 -32 133 C
ATOM 1889 C ALA A 160 17.360 155.566 131.742 1.00 83.32 C
ANISOU 1889 C ALA A 160 11614 8901 11140 -455 -22 138 C
ATOM 1890 O ALA A 160 17.404 156.659 132.281 1.00 83.74 O
ANISOU 1890 O ALA A 160 11603 8971 11244 -419 -30 146 O
ATOM 1891 CB ALA A 160 17.503 153.701 133.404 1.00 78.72 C
ANISOU 1891 CB ALA A 160 10991 8331 10588 -431 34 107 C
ATOM 1892 N LEU A 161 17.962 155.312 130.575 1.00 80.34 N
ANISOU 1892 N LEU A 161 11352 8483 10690 -495 12 130 N
ATOM 1893 CA LEU A 161 18.660 156.331 129.816 1.00 80.88 C
ANISOU 1893 CA LEU A 161 11471 8528 10733 -501 39 136 C
ATOM 1894 C LEU A 161 17.605 157.191 129.112 1.00 87.49 C
ANISOU 1894 C LEU A 161 12335 9361 11544 -548 -90 185 C
ATOM 1895 O LEU A 161 17.671 158.414 129.197 1.00 87.88 O
ANISOU 1895 O LEU A 161 12333 9420 11638 -520 -117 206 O
ATOM 1896 CB LEU A 161 19.612 155.695 128.801 1.00 81.83 C
ANISOU 1896 CB LEU A 161 11732 8579 10781 -542 157 106 C
ATOM 1897 CG LEU A 161 20.395 156.691 127.940 1.00 87.88 C
ANISOU 1897 CG LEU A 161 12570 9304 11516 -561 221 110 C
ATOM 1898 CD1 LEU A 161 21.660 157.178 128.655 1.00 87.62 C
ANISOU 1898 CD1 LEU A 161 12407 9272 11611 -486 312 102 C
ATOM 1899 CD2 LEU A 161 20.710 156.108 126.591 1.00 92.03 C
ANISOU 1899 CD2 LEU A 161 13311 9741 11917 -647 326 83 C
ATOM 1900 N ALA A 162 16.605 156.547 128.468 1.00 85.36 N
ANISOU 1900 N ALA A 162 12141 9069 11223 -622 -187 211 N
ATOM 1901 CA ALA A 162 15.475 157.193 127.797 1.00 85.94 C
ANISOU 1901 CA ALA A 162 12228 9117 11309 -682 -359 282 C
ATOM 1902 C ALA A 162 14.762 158.191 128.715 1.00 91.31 C
ANISOU 1902 C ALA A 162 12710 9827 12157 -610 -408 315 C
ATOM 1903 O ALA A 162 14.373 159.261 128.250 1.00 92.30 O
ANISOU 1903 O ALA A 162 12820 9922 12327 -623 -503 369 O
ATOM 1904 CB ALA A 162 14.490 156.148 127.309 1.00 87.18 C
ANISOU 1904 CB ALA A 162 12448 9243 11433 -768 -471 312 C
ATOM 1905 N LEU A 163 14.616 157.865 130.013 1.00 87.60 N
ANISOU 1905 N LEU A 163 12108 9399 11779 -541 -330 282 N
ATOM 1906 CA LEU A 163 13.997 158.804 130.945 1.00 88.15 C
ANISOU 1906 CA LEU A 163 12021 9474 11998 -477 -319 294 C
ATOM 1907 C LEU A 163 14.971 159.936 131.302 1.00 90.38 C
ANISOU 1907 C LEU A 163 12302 9767 12270 -422 -247 267 C
ATOM 1908 O LEU A 163 14.569 161.095 131.207 1.00 92.21 O
ANISOU 1908 O LEU A 163 12474 9971 12589 -401 -287 299 O
ATOM 1909 CB LEU A 163 13.364 158.126 132.175 1.00 88.76 C
ANISOU 1909 CB LEU A 163 11999 9568 12156 -447 -248 269 C
ATOM 1910 CG LEU A 163 12.240 157.103 131.855 1.00 95.48 C
ANISOU 1910 CG LEU A 163 12825 10402 13053 -505 -328 307 C
ATOM 1911 CD1 LEU A 163 11.717 156.447 133.094 1.00 95.68 C
ANISOU 1911 CD1 LEU A 163 12764 10438 13153 -480 -226 279 C
ATOM 1912 CD2 LEU A 163 11.081 157.734 131.086 1.00100.66 C
ANISOU 1912 CD2 LEU A 163 13405 10998 13845 -547 -488 398 C
ATOM 1913 N GLY A 164 16.249 159.619 131.567 1.00 82.43 N
ANISOU 1913 N GLY A 164 11358 8783 11177 -407 -158 219 N
ATOM 1914 CA GLY A 164 17.291 160.620 131.794 1.00 80.54 C
ANISOU 1914 CA GLY A 164 11123 8544 10935 -372 -109 203 C
ATOM 1915 C GLY A 164 17.439 161.591 130.625 1.00 82.82 C
ANISOU 1915 C GLY A 164 11468 8802 11198 -401 -164 241 C
ATOM 1916 O GLY A 164 17.881 162.734 130.793 1.00 82.41 O
ANISOU 1916 O GLY A 164 11394 8741 11178 -373 -153 244 O
ATOM 1917 N LEU A 165 17.025 161.142 129.422 1.00 76.70 N
ANISOU 1917 N LEU A 165 10790 8000 10353 -472 -236 274 N
ATOM 1918 CA LEU A 165 17.037 161.932 128.204 1.00 74.94 C
ANISOU 1918 CA LEU A 165 10672 7730 10072 -532 -313 322 C
ATOM 1919 C LEU A 165 15.829 162.878 128.062 1.00 78.82 C
ANISOU 1919 C LEU A 165 11085 8188 10675 -536 -466 396 C
ATOM 1920 O LEU A 165 15.851 163.738 127.187 1.00 78.73 O
ANISOU 1920 O LEU A 165 11151 8130 10632 -581 -551 448 O
ATOM 1921 CB LEU A 165 17.179 161.015 126.973 1.00 74.67 C
ANISOU 1921 CB LEU A 165 10832 7655 9883 -633 -324 325 C
ATOM 1922 CG LEU A 165 18.568 160.444 126.667 1.00 77.35 C
ANISOU 1922 CG LEU A 165 11280 7980 10130 -642 -144 263 C
ATOM 1923 CD1 LEU A 165 18.609 159.879 125.299 1.00 77.11 C
ANISOU 1923 CD1 LEU A 165 11491 7877 9931 -760 -140 267 C
ATOM 1924 CD2 LEU A 165 19.650 161.509 126.759 1.00 81.42 C
ANISOU 1924 CD2 LEU A 165 11768 8491 10678 -603 -53 254 C
ATOM 1925 N LEU A 166 14.794 162.746 128.907 1.00 76.43 N
ANISOU 1925 N LEU A 166 10628 7893 10520 -491 -493 407 N
ATOM 1926 CA LEU A 166 13.617 163.622 128.816 1.00 78.18 C
ANISOU 1926 CA LEU A 166 10732 8056 10917 -482 -618 484 C
ATOM 1927 C LEU A 166 13.927 165.088 129.066 1.00 82.99 C
ANISOU 1927 C LEU A 166 11291 8641 11601 -426 -591 489 C
ATOM 1928 O LEU A 166 13.508 165.875 128.238 1.00 83.14 O
ANISOU 1928 O LEU A 166 11324 8596 11670 -462 -732 570 O
ATOM 1929 CB LEU A 166 12.434 163.173 129.683 1.00 78.89 C
ANISOU 1929 CB LEU A 166 10649 8136 11188 -444 -605 492 C
ATOM 1930 CG LEU A 166 11.719 161.930 129.223 1.00 84.34 C
ANISOU 1930 CG LEU A 166 11361 8819 11866 -517 -704 528 C
ATOM 1931 CD1 LEU A 166 10.960 161.317 130.365 1.00 84.99 C
ANISOU 1931 CD1 LEU A 166 11292 8913 12086 -470 -605 499 C
ATOM 1932 CD2 LEU A 166 10.824 162.223 128.045 1.00 86.78 C
ANISOU 1932 CD2 LEU A 166 11676 9043 12253 -602 -946 649 C
ATOM 1933 N PRO A 167 14.657 165.517 130.127 1.00 81.72 N
ANISOU 1933 N PRO A 167 11094 8513 11441 -353 -438 415 N
ATOM 1934 CA PRO A 167 14.941 166.967 130.284 1.00 82.10 C
ANISOU 1934 CA PRO A 167 11117 8524 11552 -313 -424 422 C
ATOM 1935 C PRO A 167 15.639 167.605 129.092 1.00 85.98 C
ANISOU 1935 C PRO A 167 11733 8995 11938 -368 -503 465 C
ATOM 1936 O PRO A 167 15.537 168.816 128.883 1.00 87.82 O
ANISOU 1936 O PRO A 167 11946 9177 12245 -353 -551 504 O
ATOM 1937 CB PRO A 167 15.806 167.025 131.542 1.00 83.30 C
ANISOU 1937 CB PRO A 167 11269 8715 11665 -261 -267 334 C
ATOM 1938 CG PRO A 167 15.366 165.801 132.334 1.00 88.00 C
ANISOU 1938 CG PRO A 167 11828 9345 12263 -255 -204 296 C
ATOM 1939 CD PRO A 167 15.221 164.750 131.263 1.00 83.55 C
ANISOU 1939 CD PRO A 167 11321 8803 11621 -318 -294 332 C
ATOM 1940 N LEU A 168 16.292 166.782 128.283 1.00 80.75 N
ANISOU 1940 N LEU A 168 11213 8360 11108 -438 -504 458 N
ATOM 1941 CA LEU A 168 16.946 167.214 127.061 1.00 80.40 C
ANISOU 1941 CA LEU A 168 11331 8281 10934 -514 -545 492 C
ATOM 1942 C LEU A 168 15.888 167.491 126.002 1.00 85.80 C
ANISOU 1942 C LEU A 168 12074 8892 11635 -594 -754 597 C
ATOM 1943 O LEU A 168 16.021 168.457 125.261 1.00 87.54 O
ANISOU 1943 O LEU A 168 12379 9056 11828 -638 -836 654 O
ATOM 1944 CB LEU A 168 17.906 166.126 126.580 1.00 79.70 C
ANISOU 1944 CB LEU A 168 11384 8219 10679 -566 -435 442 C
ATOM 1945 CG LEU A 168 19.355 166.237 126.984 1.00 82.31 C
ANISOU 1945 CG LEU A 168 11716 8574 10982 -531 -264 380 C
ATOM 1946 CD1 LEU A 168 19.541 166.025 128.461 1.00 80.71 C
ANISOU 1946 CD1 LEU A 168 11358 8423 10885 -440 -195 328 C
ATOM 1947 CD2 LEU A 168 20.138 165.216 126.260 1.00 85.49 C
ANISOU 1947 CD2 LEU A 168 12255 8964 11264 -589 -152 345 C
ATOM 1948 N LEU A 169 14.830 166.666 125.949 1.00 82.54 N
ANISOU 1948 N LEU A 169 11615 8467 11279 -620 -859 633 N
ATOM 1949 CA LEU A 169 13.708 166.793 125.007 1.00 84.59 C
ANISOU 1949 CA LEU A 169 11910 8640 11591 -710 -1107 754 C
ATOM 1950 C LEU A 169 12.670 167.847 125.448 1.00 92.95 C
ANISOU 1950 C LEU A 169 12748 9633 12937 -642 -1218 832 C
ATOM 1951 O LEU A 169 11.615 168.009 124.808 1.00 94.79 O
ANISOU 1951 O LEU A 169 12945 9774 13296 -704 -1451 954 O
ATOM 1952 CB LEU A 169 13.018 165.436 124.819 1.00 84.45 C
ANISOU 1952 CB LEU A 169 11916 8626 11544 -772 -1179 765 C
ATOM 1953 CG LEU A 169 13.887 164.323 124.293 1.00 88.15 C
ANISOU 1953 CG LEU A 169 12610 9127 11754 -847 -1075 695 C
ATOM 1954 CD1 LEU A 169 13.325 162.971 124.690 1.00 87.33 C
ANISOU 1954 CD1 LEU A 169 12451 9057 11674 -848 -1062 666 C
ATOM 1955 CD2 LEU A 169 14.100 164.460 122.796 1.00 92.45 C
ANISOU 1955 CD2 LEU A 169 13450 9588 12090 -1006 -1206 756 C
ATOM 1956 N GLY A 170 12.978 168.537 126.539 1.00 90.05 N
ANISOU 1956 N GLY A 170 12238 9293 12683 -522 -1053 766 N
ATOM 1957 CA GLY A 170 12.113 169.567 127.086 1.00 91.45 C
ANISOU 1957 CA GLY A 170 12212 9392 13144 -443 -1085 815 C
ATOM 1958 C GLY A 170 11.109 169.108 128.126 1.00 96.11 C
ANISOU 1958 C GLY A 170 12585 9969 13962 -366 -1001 794 C
ATOM 1959 O GLY A 170 10.278 169.918 128.560 1.00 98.65 O
ANISOU 1959 O GLY A 170 12724 10199 14558 -297 -993 833 O
ATOM 1960 N VAL A 171 11.155 167.822 128.532 1.00 89.54 N
ANISOU 1960 N VAL A 171 11771 9211 13038 -380 -921 735 N
ATOM 1961 CA VAL A 171 10.284 167.329 129.598 1.00 88.67 C
ANISOU 1961 CA VAL A 171 11479 9091 13122 -317 -804 704 C
ATOM 1962 C VAL A 171 11.148 167.291 130.837 1.00 89.83 C
ANISOU 1962 C VAL A 171 11664 9310 13157 -248 -554 570 C
ATOM 1963 O VAL A 171 11.868 166.331 131.070 1.00 87.94 O
ANISOU 1963 O VAL A 171 11529 9159 12723 -271 -483 503 O
ATOM 1964 CB VAL A 171 9.569 165.993 129.296 1.00 92.89 C
ANISOU 1964 CB VAL A 171 11994 9637 13664 -382 -896 741 C
ATOM 1965 CG1 VAL A 171 8.771 165.513 130.514 1.00 92.64 C
ANISOU 1965 CG1 VAL A 171 11779 9591 13831 -316 -730 700 C
ATOM 1966 CG2 VAL A 171 8.661 166.136 128.077 1.00 94.61 C
ANISOU 1966 CG2 VAL A 171 12190 9758 14001 -473 -1193 895 C
ATOM 1967 N GLY A 172 11.117 168.377 131.584 1.00 86.98 N
ANISOU 1967 N GLY A 172 11235 8896 12917 -175 -438 539 N
ATOM 1968 CA GLY A 172 11.935 168.515 132.777 1.00 86.03 C
ANISOU 1968 CA GLY A 172 11185 8819 12684 -132 -233 423 C
ATOM 1969 C GLY A 172 13.134 169.379 132.476 1.00 88.80 C
ANISOU 1969 C GLY A 172 11658 9194 12890 -138 -253 406 C
ATOM 1970 O GLY A 172 13.217 169.955 131.377 1.00 89.30 O
ANISOU 1970 O GLY A 172 11745 9230 12954 -169 -401 481 O
ATOM 1971 N ARG A 173 14.053 169.500 133.470 1.00 82.79 N
ANISOU 1971 N ARG A 173 10981 8468 12008 -121 -114 315 N
ATOM 1972 CA ARG A 173 15.244 170.351 133.347 1.00 81.32 C
ANISOU 1972 CA ARG A 173 10894 8294 11710 -128 -121 297 C
ATOM 1973 C ARG A 173 16.378 169.899 134.266 1.00 84.28 C
ANISOU 1973 C ARG A 173 11369 8726 11929 -143 -31 220 C
ATOM 1974 O ARG A 173 16.123 169.507 135.399 1.00 84.72 O
ANISOU 1974 O ARG A 173 11435 8769 11985 -133 75 164 O
ATOM 1975 CB ARG A 173 14.885 171.846 133.624 1.00 78.46 C
ANISOU 1975 CB ARG A 173 10487 7828 11495 -81 -86 303 C
ATOM 1976 N TYR A 174 17.627 169.961 133.789 1.00 79.47 N
ANISOU 1976 N TYR A 174 10835 8159 11199 -177 -76 225 N
ATOM 1977 CA TYR A 174 18.784 169.698 134.633 1.00 78.54 C
ANISOU 1977 CA TYR A 174 10788 8070 10982 -196 -32 177 C
ATOM 1978 C TYR A 174 19.424 171.033 134.975 1.00 82.44 C
ANISOU 1978 C TYR A 174 11326 8513 11486 -196 -27 167 C
ATOM 1979 O TYR A 174 19.681 171.874 134.083 1.00 81.32 O
ANISOU 1979 O TYR A 174 11178 8352 11368 -198 -78 209 O
ATOM 1980 CB TYR A 174 19.804 168.754 134.001 1.00 79.52 C
ANISOU 1980 CB TYR A 174 10939 8254 11022 -232 -63 193 C
ATOM 1981 CG TYR A 174 19.290 167.352 133.821 1.00 82.63 C
ANISOU 1981 CG TYR A 174 11315 8690 11390 -240 -60 191 C
ATOM 1982 CD1 TYR A 174 18.701 166.660 134.879 1.00 84.87 C
ANISOU 1982 CD1 TYR A 174 11588 8978 11679 -230 -12 155 C
ATOM 1983 CD2 TYR A 174 19.391 166.707 132.593 1.00 84.17 C
ANISOU 1983 CD2 TYR A 174 11530 8908 11542 -269 -94 223 C
ATOM 1984 CE1 TYR A 174 18.200 165.370 134.709 1.00 85.46 C
ANISOU 1984 CE1 TYR A 174 11646 9088 11736 -240 -12 157 C
ATOM 1985 CE2 TYR A 174 18.897 165.416 132.413 1.00 85.46 C
ANISOU 1985 CE2 TYR A 174 11694 9100 11677 -284 -96 220 C
ATOM 1986 CZ TYR A 174 18.315 164.748 133.476 1.00 94.02 C
ANISOU 1986 CZ TYR A 174 12741 10197 12786 -266 -61 189 C
ATOM 1987 OH TYR A 174 17.830 163.483 133.289 1.00 98.26 O
ANISOU 1987 OH TYR A 174 13276 10758 13299 -284 -66 189 O
ATOM 1988 N THR A 175 19.576 171.248 136.296 1.00 78.83 N
ANISOU 1988 N THR A 175 10932 8017 11001 -204 33 113 N
ATOM 1989 CA THR A 175 20.149 172.427 136.931 1.00 78.54 C
ANISOU 1989 CA THR A 175 10975 7914 10953 -220 43 90 C
ATOM 1990 C THR A 175 21.031 171.990 138.084 1.00 83.14 C
ANISOU 1990 C THR A 175 11665 8491 11432 -280 29 59 C
ATOM 1991 O THR A 175 20.768 170.952 138.714 1.00 82.69 O
ANISOU 1991 O THR A 175 11637 8457 11326 -295 56 38 O
ATOM 1992 CB THR A 175 19.077 173.372 137.471 1.00 83.78 C
ANISOU 1992 CB THR A 175 11650 8480 11701 -183 144 52 C
ATOM 1993 OG1 THR A 175 18.325 172.728 138.491 1.00 81.75 O
ANISOU 1993 OG1 THR A 175 11434 8197 11431 -184 258 -2 O
ATOM 1994 CG2 THR A 175 18.170 173.924 136.397 1.00 85.99 C
ANISOU 1994 CG2 THR A 175 11808 8735 12128 -127 123 104 C
ATOM 1995 N VAL A 176 22.062 172.816 138.378 1.00 79.09 N
ANISOU 1995 N VAL A 176 11221 7937 10892 -324 -31 66 N
ATOM 1996 CA VAL A 176 23.023 172.587 139.450 1.00 77.48 C
ANISOU 1996 CA VAL A 176 11132 7701 10605 -403 -101 61 C
ATOM 1997 C VAL A 176 22.272 172.694 140.750 1.00 83.16 C
ANISOU 1997 C VAL A 176 12016 8344 11238 -436 -12 -9 C
ATOM 1998 O VAL A 176 21.401 173.548 140.888 1.00 85.47 O
ANISOU 1998 O VAL A 176 12343 8570 11561 -403 105 -55 O
ATOM 1999 CB VAL A 176 24.238 173.537 139.385 1.00 80.11 C
ANISOU 1999 CB VAL A 176 11486 7992 10959 -451 -203 98 C
ATOM 2000 CG1 VAL A 176 25.201 173.232 140.509 1.00 80.79 C
ANISOU 2000 CG1 VAL A 176 11687 8030 10981 -551 -323 114 C
ATOM 2001 CG2 VAL A 176 24.959 173.442 138.047 1.00 78.78 C
ANISOU 2001 CG2 VAL A 176 11165 7884 10883 -424 -241 162 C
ATOM 2002 N GLN A 177 22.547 171.786 141.663 1.00 80.06 N
ANISOU 2002 N GLN A 177 11725 7945 10749 -501 -50 -16 N
ATOM 2003 CA GLN A 177 21.872 171.708 142.948 1.00 81.50 C
ANISOU 2003 CA GLN A 177 12109 8044 10814 -556 53 -84 C
ATOM 2004 C GLN A 177 22.857 172.014 144.063 1.00 87.94 C
ANISOU 2004 C GLN A 177 13151 8770 11493 -688 -74 -78 C
ATOM 2005 O GLN A 177 24.053 171.747 143.916 1.00 86.45 O
ANISOU 2005 O GLN A 177 12915 8605 11327 -733 -267 -3 O
ATOM 2006 CB GLN A 177 21.252 170.295 143.166 1.00 82.06 C
ANISOU 2006 CB GLN A 177 12158 8167 10856 -548 107 -92 C
ATOM 2007 CG GLN A 177 20.469 169.695 141.989 1.00 81.20 C
ANISOU 2007 CG GLN A 177 11821 8155 10877 -443 162 -71 C
ATOM 2008 CD GLN A 177 19.105 170.293 141.744 1.00 97.29 C
ANISOU 2008 CD GLN A 177 13790 10157 13020 -370 331 -112 C
ATOM 2009 OE1 GLN A 177 18.334 170.570 142.663 1.00 92.08 O
ANISOU 2009 OE1 GLN A 177 13243 9405 12338 -386 492 -176 O
ATOM 2010 NE2 GLN A 177 18.742 170.427 140.484 1.00 91.61 N
ANISOU 2010 NE2 GLN A 177 12884 9493 12431 -294 303 -68 N
ATOM 2011 N TYR A 178 22.344 172.530 145.200 1.00 88.03 N
ANISOU 2011 N TYR A 178 13417 8659 11370 -760 38 -154 N
ATOM 2012 CA TYR A 178 23.144 172.816 146.394 1.00 90.15 C
ANISOU 2012 CA TYR A 178 13976 8813 11462 -919 -88 -154 C
ATOM 2013 C TYR A 178 23.886 171.521 146.843 1.00 95.06 C
ANISOU 2013 C TYR A 178 14629 9467 12022 -1001 -284 -79 C
ATOM 2014 O TYR A 178 23.274 170.447 146.809 1.00 95.17 O
ANISOU 2014 O TYR A 178 14583 9541 12036 -962 -205 -88 O
ATOM 2015 CB TYR A 178 22.249 173.420 147.504 1.00 93.23 C
ANISOU 2015 CB TYR A 178 14671 9055 11699 -985 132 -266 C
ATOM 2016 CG TYR A 178 22.878 173.486 148.881 1.00 97.18 C
ANISOU 2016 CG TYR A 178 15556 9416 11954 -1183 16 -274 C
ATOM 2017 CD1 TYR A 178 23.682 174.561 149.253 1.00100.34 C
ANISOU 2017 CD1 TYR A 178 16135 9709 12279 -1284 -112 -267 C
ATOM 2018 CD2 TYR A 178 22.640 172.489 149.825 1.00 98.87 C
ANISOU 2018 CD2 TYR A 178 15981 9588 11995 -1287 24 -285 C
ATOM 2019 CE1 TYR A 178 24.272 174.620 150.516 1.00103.56 C
ANISOU 2019 CE1 TYR A 178 16932 9972 12445 -1494 -256 -264 C
ATOM 2020 CE2 TYR A 178 23.223 172.537 151.089 1.00101.87 C
ANISOU 2020 CE2 TYR A 178 16759 9824 12125 -1495 -114 -280 C
ATOM 2021 CZ TYR A 178 24.034 173.606 151.432 1.00111.24 C
ANISOU 2021 CZ TYR A 178 18129 10901 13236 -1603 -262 -268 C
ATOM 2022 OH TYR A 178 24.609 173.640 152.677 1.00114.96 O
ANISOU 2022 OH TYR A 178 19022 11214 13444 -1833 -432 -253 O
ATOM 2023 N PRO A 179 25.195 171.561 147.189 1.00 91.44 N
ANISOU 2023 N PRO A 179 14231 8967 11546 -1110 -552 7 N
ATOM 2024 CA PRO A 179 26.066 172.745 147.363 1.00 91.93 C
ANISOU 2024 CA PRO A 179 14385 8942 11603 -1190 -694 35 C
ATOM 2025 C PRO A 179 26.678 173.327 146.095 1.00 94.97 C
ANISOU 2025 C PRO A 179 14476 9405 12206 -1089 -743 89 C
ATOM 2026 O PRO A 179 27.305 174.405 146.153 1.00 96.42 O
ANISOU 2026 O PRO A 179 14716 9517 12401 -1146 -840 109 O
ATOM 2027 CB PRO A 179 27.133 172.244 148.330 1.00 94.99 C
ANISOU 2027 CB PRO A 179 14951 9239 11900 -1364 -988 126 C
ATOM 2028 CG PRO A 179 27.256 170.771 148.001 1.00 99.01 C
ANISOU 2028 CG PRO A 179 15264 9846 12511 -1310 -1048 192 C
ATOM 2029 CD PRO A 179 25.873 170.318 147.616 1.00 93.13 C
ANISOU 2029 CD PRO A 179 14451 9189 11745 -1184 -753 94 C
ATOM 2030 N GLY A 180 26.460 172.638 144.975 1.00 87.79 N
ANISOU 2030 N GLY A 180 13282 8625 11447 -954 -666 109 N
ATOM 2031 CA GLY A 180 26.967 173.045 143.672 1.00 86.37 C
ANISOU 2031 CA GLY A 180 12844 8518 11455 -863 -676 156 C
ATOM 2032 C GLY A 180 27.899 172.011 143.102 1.00 90.06 C
ANISOU 2032 C GLY A 180 13105 9044 12072 -848 -800 251 C
ATOM 2033 O GLY A 180 28.564 172.247 142.094 1.00 88.94 O
ANISOU 2033 O GLY A 180 12768 8935 12089 -801 -814 302 O
ATOM 2034 N SER A 181 27.955 170.860 143.775 1.00 88.30 N
ANISOU 2034 N SER A 181 12935 8814 11803 -895 -875 276 N
ATOM 2035 CA SER A 181 28.782 169.698 143.457 1.00 87.78 C
ANISOU 2035 CA SER A 181 12690 8773 11888 -886 -988 366 C
ATOM 2036 C SER A 181 28.100 168.745 142.476 1.00 91.39 C
ANISOU 2036 C SER A 181 12980 9344 12400 -763 -819 335 C
ATOM 2037 O SER A 181 28.731 167.769 142.050 1.00 91.32 O
ANISOU 2037 O SER A 181 12813 9353 12532 -738 -865 397 O
ATOM 2038 CB SER A 181 29.091 168.940 144.738 1.00 90.89 C
ANISOU 2038 CB SER A 181 13257 9086 12193 -1009 -1170 412 C
ATOM 2039 OG SER A 181 27.869 168.562 145.347 1.00 97.50 O
ANISOU 2039 OG SER A 181 14281 9939 12826 -1013 -1033 323 O
ATOM 2040 N TRP A 182 26.820 169.029 142.104 1.00 87.29 N
ANISOU 2040 N TRP A 182 12494 8885 11788 -690 -629 246 N
ATOM 2041 CA TRP A 182 26.031 168.142 141.240 1.00 86.05 C
ANISOU 2041 CA TRP A 182 12214 8822 11658 -594 -492 218 C
ATOM 2042 C TRP A 182 24.769 168.753 140.594 1.00 87.52 C
ANISOU 2042 C TRP A 182 12387 9054 11814 -517 -325 151 C
ATOM 2043 O TRP A 182 24.214 169.701 141.128 1.00 86.47 O
ANISOU 2043 O TRP A 182 12369 8870 11615 -533 -275 104 O
ATOM 2044 CB TRP A 182 25.598 166.929 142.088 1.00 84.96 C
ANISOU 2044 CB TRP A 182 12165 8683 11434 -628 -505 209 C
ATOM 2045 CG TRP A 182 24.630 167.275 143.194 1.00 85.81 C
ANISOU 2045 CG TRP A 182 12492 8741 11369 -679 -432 138 C
ATOM 2046 CD1 TRP A 182 24.860 168.077 144.272 1.00 89.60 C
ANISOU 2046 CD1 TRP A 182 13190 9120 11734 -781 -493 124 C
ATOM 2047 CD2 TRP A 182 23.289 166.796 143.326 1.00 84.93 C
ANISOU 2047 CD2 TRP A 182 12417 8661 11193 -641 -266 72 C
ATOM 2048 NE1 TRP A 182 23.734 168.151 145.049 1.00 89.37 N
ANISOU 2048 NE1 TRP A 182 13343 9051 11564 -804 -339 41 N
ATOM 2049 CE2 TRP A 182 22.756 167.367 144.496 1.00 89.74 C
ANISOU 2049 CE2 TRP A 182 13262 9177 11657 -715 -196 12 C
ATOM 2050 CE3 TRP A 182 22.473 165.961 142.548 1.00 84.92 C
ANISOU 2050 CE3 TRP A 182 12275 8743 11249 -558 -164 59 C
ATOM 2051 CZ2 TRP A 182 21.449 167.110 144.922 1.00 89.25 C
ANISOU 2051 CZ2 TRP A 182 13275 9101 11536 -700 -2 -59 C
ATOM 2052 CZ3 TRP A 182 21.188 165.698 142.977 1.00 86.30 C
ANISOU 2052 CZ3 TRP A 182 12511 8910 11369 -548 -13 0 C
ATOM 2053 CH2 TRP A 182 20.683 166.275 144.146 1.00 88.03 C
ANISOU 2053 CH2 TRP A 182 12940 9034 11474 -612 81 -59 C
ATOM 2054 N CYS A 183 24.259 168.103 139.531 1.00 83.95 N
ANISOU 2054 N CYS A 183 11808 8678 11412 -444 -245 149 N
ATOM 2055 CA CYS A 183 23.038 168.469 138.822 1.00 85.24 C
ANISOU 2055 CA CYS A 183 11933 8876 11581 -380 -132 113 C
ATOM 2056 C CYS A 183 21.979 167.423 138.946 1.00 88.76 C
ANISOU 2056 C CYS A 183 12368 9357 11998 -356 -63 86 C
ATOM 2057 O CYS A 183 22.290 166.247 139.086 1.00 89.90 O
ANISOU 2057 O CYS A 183 12498 9529 12129 -371 -94 103 O
ATOM 2058 CB CYS A 183 23.330 168.763 137.362 1.00 86.87 C
ANISOU 2058 CB CYS A 183 12027 9118 11861 -340 -128 148 C
ATOM 2059 SG CYS A 183 24.525 170.090 137.129 1.00 92.56 S
ANISOU 2059 SG CYS A 183 12746 9789 12633 -369 -187 182 S
ATOM 2060 N PHE A 184 20.718 167.833 138.850 1.00 83.65 N
ANISOU 2060 N PHE A 184 11713 8700 11371 -318 32 53 N
ATOM 2061 CA PHE A 184 19.597 166.904 138.933 1.00 82.85 C
ANISOU 2061 CA PHE A 184 11581 8622 11277 -298 103 34 C
ATOM 2062 C PHE A 184 18.359 167.520 138.280 1.00 88.53 C
ANISOU 2062 C PHE A 184 12208 9324 12104 -243 167 35 C
ATOM 2063 O PHE A 184 18.416 168.677 137.828 1.00 90.21 O
ANISOU 2063 O PHE A 184 12399 9506 12371 -221 152 48 O
ATOM 2064 CB PHE A 184 19.323 166.543 140.413 1.00 84.42 C
ANISOU 2064 CB PHE A 184 11919 8769 11389 -349 168 -12 C
ATOM 2065 CG PHE A 184 18.638 165.219 140.661 1.00 84.81 C
ANISOU 2065 CG PHE A 184 11955 8848 11420 -354 214 -20 C
ATOM 2066 CD1 PHE A 184 19.122 164.046 140.088 1.00 85.85 C
ANISOU 2066 CD1 PHE A 184 12024 9046 11547 -354 130 19 C
ATOM 2067 CD2 PHE A 184 17.517 165.141 141.482 1.00 86.01 C
ANISOU 2067 CD2 PHE A 184 12161 8948 11572 -362 361 -67 C
ATOM 2068 CE1 PHE A 184 18.474 162.832 140.297 1.00 85.59 C
ANISOU 2068 CE1 PHE A 184 11983 9037 11500 -362 168 13 C
ATOM 2069 CE2 PHE A 184 16.879 163.921 141.698 1.00 87.81 C
ANISOU 2069 CE2 PHE A 184 12373 9200 11792 -373 406 -70 C
ATOM 2070 CZ PHE A 184 17.356 162.778 141.096 1.00 84.78 C
ANISOU 2070 CZ PHE A 184 11927 8892 11393 -373 297 -28 C
ATOM 2071 N LEU A 185 17.245 166.744 138.211 1.00 82.80 N
ANISOU 2071 N LEU A 185 11420 8610 11431 -225 221 33 N
ATOM 2072 CA LEU A 185 15.957 167.214 137.717 1.00 82.12 C
ANISOU 2072 CA LEU A 185 11220 8484 11499 -180 264 51 C
ATOM 2073 C LEU A 185 15.586 168.410 138.582 1.00 88.49 C
ANISOU 2073 C LEU A 185 12070 9188 12365 -162 387 5 C
ATOM 2074 O LEU A 185 15.878 168.409 139.783 1.00 87.85 O
ANISOU 2074 O LEU A 185 12129 9066 12182 -201 477 -54 O
ATOM 2075 CB LEU A 185 14.870 166.113 137.746 1.00 81.84 C
ANISOU 2075 CB LEU A 185 11109 8460 11529 -178 306 58 C
ATOM 2076 CG LEU A 185 14.714 165.200 138.995 1.00 85.28 C
ANISOU 2076 CG LEU A 185 11631 8886 11886 -213 419 5 C
ATOM 2077 CD1 LEU A 185 13.728 165.785 140.018 1.00 86.46 C
ANISOU 2077 CD1 LEU A 185 11791 8927 12133 -200 614 -44 C
ATOM 2078 CD2 LEU A 185 14.211 163.844 138.606 1.00 83.72 C
ANISOU 2078 CD2 LEU A 185 11372 8743 11697 -226 383 31 C
ATOM 2079 N THR A 186 15.074 169.471 137.960 1.00 88.33 N
ANISOU 2079 N THR A 186 11958 9112 12490 -117 379 36 N
ATOM 2080 CA THR A 186 14.755 170.712 138.665 1.00 90.58 C
ANISOU 2080 CA THR A 186 12282 9280 12855 -92 508 -8 C
ATOM 2081 C THR A 186 13.498 170.527 139.493 1.00 98.15 C
ANISOU 2081 C THR A 186 13200 10144 13947 -71 709 -50 C
ATOM 2082 O THR A 186 12.482 170.093 138.947 1.00100.27 O
ANISOU 2082 O THR A 186 13298 10407 14393 -37 701 0 O
ATOM 2083 CB THR A 186 14.705 171.880 137.681 1.00101.31 C
ANISOU 2083 CB THR A 186 13552 10601 14340 -51 421 48 C
ATOM 2084 OG1 THR A 186 15.846 171.808 136.830 1.00101.92 O
ANISOU 2084 OG1 THR A 186 13667 10770 14289 -83 257 90 O
ATOM 2085 CG2 THR A 186 14.693 173.225 138.371 1.00 99.82 C
ANISOU 2085 CG2 THR A 186 13432 10290 14205 -31 542 -2 C
ATOM 2086 N LEU A 187 13.578 170.789 140.813 1.00 94.55 N
ANISOU 2086 N LEU A 187 12916 9605 13404 -104 889 -139 N
ATOM 2087 CA LEU A 187 12.436 170.609 141.706 1.00 95.91 C
ANISOU 2087 CA LEU A 187 13085 9665 13692 -96 1139 -193 C
ATOM 2088 C LEU A 187 11.524 171.841 141.673 1.00106.03 C
ANISOU 2088 C LEU A 187 14256 10790 15241 -23 1296 -201 C
ATOM 2089 O LEU A 187 11.297 172.499 142.698 1.00108.60 O
ANISOU 2089 O LEU A 187 14722 10972 15567 -36 1535 -289 O
ATOM 2090 CB LEU A 187 12.908 170.313 143.140 1.00 95.77 C
ANISOU 2090 CB LEU A 187 13351 9603 13433 -188 1277 -286 C
ATOM 2091 CG LEU A 187 13.408 168.918 143.483 1.00 97.93 C
ANISOU 2091 CG LEU A 187 13718 9982 13510 -259 1188 -279 C
ATOM 2092 CD1 LEU A 187 13.868 168.861 144.927 1.00 97.97 C
ANISOU 2092 CD1 LEU A 187 14042 9911 13272 -369 1292 -358 C
ATOM 2093 CD2 LEU A 187 12.341 167.877 143.257 1.00 99.76 C
ANISOU 2093 CD2 LEU A 187 13785 10234 13885 -231 1261 -255 C
ATOM 2094 N GLY A 188 11.018 172.157 140.491 1.00104.06 N
ANISOU 2094 N GLY A 188 13770 10549 15218 44 1158 -106 N
ATOM 2095 CA GLY A 188 10.156 173.313 140.305 1.00106.27 C
ANISOU 2095 CA GLY A 188 13901 10672 15805 121 1259 -85 C
ATOM 2096 C GLY A 188 8.685 172.991 140.245 1.00114.18 C
ANISOU 2096 C GLY A 188 14662 11567 17153 176 1391 -45 C
ATOM 2097 O GLY A 188 8.272 171.845 140.442 1.00114.00 O
ANISOU 2097 O GLY A 188 14602 11592 17120 148 1427 -44 O
ATOM 2098 N ALA A 189 7.889 174.018 139.968 1.00114.41 N
ANISOU 2098 N ALA A 189 14514 11437 17518 253 1458 -4 N
ATOM 2099 CA ALA A 189 6.441 173.897 139.837 1.00116.72 C
ANISOU 2099 CA ALA A 189 14521 11590 18238 315 1572 58 C
ATOM 2100 C ALA A 189 6.035 173.855 138.349 1.00119.37 C
ANISOU 2100 C ALA A 189 14604 11964 18788 337 1226 230 C
ATOM 2101 O ALA A 189 4.876 173.523 138.060 1.00121.17 O
ANISOU 2101 O ALA A 189 14570 12100 19369 368 1224 318 O
ATOM 2102 CB ALA A 189 5.756 175.055 140.552 1.00120.17 C
ANISOU 2102 CB ALA A 189 14910 11785 18965 385 1886 1 C
ATOM 2103 N GLU A 190 6.997 174.171 137.409 1.00111.63 N
ANISOU 2103 N GLU A 190 13717 11106 17590 306 932 284 N
ATOM 2104 CA GLU A 190 6.803 174.158 135.950 1.00110.00 C
ANISOU 2104 CA GLU A 190 13366 10937 17491 293 581 442 C
ATOM 2105 C GLU A 190 6.267 172.794 135.495 1.00113.08 C
ANISOU 2105 C GLU A 190 13658 11406 17902 243 446 511 C
ATOM 2106 O GLU A 190 6.715 171.766 136.006 1.00112.23 O
ANISOU 2106 O GLU A 190 13686 11419 17537 198 524 430 O
ATOM 2107 CB GLU A 190 8.099 174.521 135.218 1.00109.26 C
ANISOU 2107 CB GLU A 190 13467 10973 17074 244 365 451 C
ATOM 2108 N SER A 191 5.244 172.794 134.604 1.00109.56 N
ANISOU 2108 N SER A 191 12970 10869 17788 248 241 665 N
ATOM 2109 CA SER A 191 4.531 171.609 134.093 1.00108.46 C
ANISOU 2109 CA SER A 191 12705 10763 17743 193 79 757 C
ATOM 2110 C SER A 191 5.441 170.405 133.839 1.00107.15 C
ANISOU 2110 C SER A 191 12763 10805 17145 105 -26 708 C
ATOM 2111 O SER A 191 5.151 169.311 134.325 1.00105.63 O
ANISOU 2111 O SER A 191 12557 10658 16919 80 67 671 O
ATOM 2112 CB SER A 191 3.720 171.964 132.851 1.00113.76 C
ANISOU 2112 CB SER A 191 13174 11325 18723 172 -256 954 C
ATOM 2113 OG SER A 191 2.767 170.959 132.555 1.00124.26 O
ANISOU 2113 OG SER A 191 14328 12625 20259 127 -376 1051 O
ATOM 2114 N GLY A 192 6.554 170.652 133.139 1.00101.07 N
ANISOU 2114 N GLY A 192 12196 10143 16063 61 -189 704 N
ATOM 2115 CA GLY A 192 7.582 169.668 132.826 1.00 97.94 C
ANISOU 2115 CA GLY A 192 12019 9922 15274 -15 -269 656 C
ATOM 2116 C GLY A 192 8.262 169.134 134.071 1.00 99.01 C
ANISOU 2116 C GLY A 192 12287 10140 15191 1 -11 506 C
ATOM 2117 O GLY A 192 8.359 167.914 134.230 1.00 99.02 O
ANISOU 2117 O GLY A 192 12343 10228 15051 -42 -2 477 O
ATOM 2118 N ASP A 193 8.709 170.054 134.981 1.00 92.52 N
ANISOU 2118 N ASP A 193 11535 9276 14344 52 189 415 N
ATOM 2119 CA ASP A 193 9.382 169.755 136.256 1.00 89.49 C
ANISOU 2119 CA ASP A 193 11316 8939 13749 49 414 281 C
ATOM 2120 C ASP A 193 8.516 168.858 137.099 1.00 92.21 C
ANISOU 2120 C ASP A 193 11593 9248 14196 48 592 245 C
ATOM 2121 O ASP A 193 9.026 167.906 137.694 1.00 91.78 O
ANISOU 2121 O ASP A 193 11676 9281 13916 4 653 179 O
ATOM 2122 CB ASP A 193 9.701 171.039 137.034 1.00 91.05 C
ANISOU 2122 CB ASP A 193 11589 9043 13963 91 585 208 C
ATOM 2123 CG ASP A 193 10.577 172.033 136.307 1.00101.84 C
ANISOU 2123 CG ASP A 193 13020 10427 15247 92 433 240 C
ATOM 2124 OD1 ASP A 193 11.204 171.647 135.291 1.00100.92 O
ANISOU 2124 OD1 ASP A 193 12932 10409 15004 51 213 305 O
ATOM 2125 OD2 ASP A 193 10.678 173.189 136.780 1.00112.57 O1-
ANISOU 2125 OD2 ASP A 193 14422 11691 16657 127 551 195 O1-
ATOM 2126 N VAL A 194 7.195 169.128 137.103 1.00 88.30 N
ANISOU 2126 N VAL A 194 10873 8614 14065 93 668 299 N
ATOM 2127 CA VAL A 194 6.223 168.318 137.823 1.00 88.73 C
ANISOU 2127 CA VAL A 194 10823 8609 14280 92 855 279 C
ATOM 2128 C VAL A 194 6.089 166.922 137.170 1.00 93.53 C
ANISOU 2128 C VAL A 194 11399 9330 14809 29 659 343 C
ATOM 2129 O VAL A 194 6.187 165.920 137.877 1.00 93.67 O
ANISOU 2129 O VAL A 194 11508 9404 14680 -8 777 279 O
ATOM 2130 CB VAL A 194 4.871 169.039 138.001 1.00 93.89 C
ANISOU 2130 CB VAL A 194 11212 9056 15404 162 1009 328 C
ATOM 2131 CG1 VAL A 194 3.875 168.167 138.773 1.00 94.66 C
ANISOU 2131 CG1 VAL A 194 11196 9082 15689 155 1237 307 C
ATOM 2132 CG2 VAL A 194 5.067 170.378 138.699 1.00 94.31 C
ANISOU 2132 CG2 VAL A 194 11337 8987 15508 220 1234 247 C
ATOM 2133 N ALA A 195 5.898 166.864 135.836 1.00 89.30 N
ANISOU 2133 N ALA A 195 10765 8817 14346 5 357 467 N
ATOM 2134 CA ALA A 195 5.771 165.623 135.081 1.00 88.21 C
ANISOU 2134 CA ALA A 195 10627 8766 14124 -69 149 531 C
ATOM 2135 C ALA A 195 7.009 164.721 135.250 1.00 91.17 C
ANISOU 2135 C ALA A 195 11252 9302 14086 -117 149 443 C
ATOM 2136 O ALA A 195 6.872 163.517 135.504 1.00 89.86 O
ANISOU 2136 O ALA A 195 11114 9188 13841 -157 182 421 O
ATOM 2137 CB ALA A 195 5.551 165.940 133.615 1.00 89.31 C
ANISOU 2137 CB ALA A 195 10702 8882 14349 -108 -180 671 C
ATOM 2138 N PHE A 196 8.211 165.312 135.137 1.00 87.01 N
ANISOU 2138 N PHE A 196 10894 8840 13328 -113 117 399 N
ATOM 2139 CA PHE A 196 9.453 164.566 135.253 1.00 85.26 C
ANISOU 2139 CA PHE A 196 10876 8745 12774 -152 108 331 C
ATOM 2140 C PHE A 196 9.760 164.152 136.669 1.00 89.91 C
ANISOU 2140 C PHE A 196 11561 9349 13253 -146 328 228 C
ATOM 2141 O PHE A 196 10.254 163.042 136.885 1.00 89.79 O
ANISOU 2141 O PHE A 196 11644 9413 13059 -187 320 198 O
ATOM 2142 CB PHE A 196 10.631 165.314 134.632 1.00 86.09 C
ANISOU 2142 CB PHE A 196 11106 8896 12709 -155 12 328 C
ATOM 2143 CG PHE A 196 11.815 164.395 134.448 1.00 86.77 C
ANISOU 2143 CG PHE A 196 11353 9092 12523 -200 -26 288 C
ATOM 2144 CD1 PHE A 196 11.741 163.296 133.592 1.00 89.69 C
ANISOU 2144 CD1 PHE A 196 11749 9507 12821 -256 -147 327 C
ATOM 2145 CD2 PHE A 196 12.995 164.607 135.148 1.00 88.16 C
ANISOU 2145 CD2 PHE A 196 11652 9307 12538 -191 59 217 C
ATOM 2146 CE1 PHE A 196 12.827 162.444 133.429 1.00 89.17 C
ANISOU 2146 CE1 PHE A 196 11819 9518 12544 -288 -149 287 C
ATOM 2147 CE2 PHE A 196 14.085 163.751 134.982 1.00 89.96 C
ANISOU 2147 CE2 PHE A 196 11990 9611 12578 -225 27 194 C
ATOM 2148 CZ PHE A 196 13.995 162.680 134.121 1.00 87.61 C
ANISOU 2148 CZ PHE A 196 11706 9352 12229 -266 -60 225 C
ATOM 2149 N GLY A 197 9.481 165.043 137.615 1.00 86.52 N
ANISOU 2149 N GLY A 197 11122 8828 12923 -105 522 176 N
ATOM 2150 CA GLY A 197 9.684 164.773 139.028 1.00 86.15 C
ANISOU 2150 CA GLY A 197 11212 8762 12759 -122 741 78 C
ATOM 2151 C GLY A 197 8.850 163.593 139.489 1.00 90.35 C
ANISOU 2151 C GLY A 197 11691 9283 13353 -151 838 75 C
ATOM 2152 O GLY A 197 9.358 162.698 140.171 1.00 89.94 O
ANISOU 2152 O GLY A 197 11791 9284 13098 -200 885 26 O
ATOM 2153 N LEU A 198 7.561 163.585 139.106 1.00 87.36 N
ANISOU 2153 N LEU A 198 11088 8825 13278 -126 855 140 N
ATOM 2154 CA LEU A 198 6.630 162.526 139.451 1.00 87.58 C
ANISOU 2154 CA LEU A 198 11026 8827 13423 -155 946 152 C
ATOM 2155 C LEU A 198 6.967 161.280 138.674 1.00 94.50 C
ANISOU 2155 C LEU A 198 11930 9825 14151 -208 724 199 C
ATOM 2156 O LEU A 198 7.046 160.224 139.278 1.00 94.31 O
ANISOU 2156 O LEU A 198 11991 9838 14004 -252 796 162 O
ATOM 2157 CB LEU A 198 5.183 162.943 139.230 1.00 88.76 C
ANISOU 2157 CB LEU A 198 10896 8834 13994 -114 1016 224 C
ATOM 2158 CG LEU A 198 4.610 163.895 140.250 1.00 93.12 C
ANISOU 2158 CG LEU A 198 11413 9227 14743 -64 1340 160 C
ATOM 2159 CD1 LEU A 198 3.302 164.427 139.778 1.00 94.44 C
ANISOU 2159 CD1 LEU A 198 11256 9241 15385 -10 1357 258 C
ATOM 2160 CD2 LEU A 198 4.486 163.241 141.614 1.00 94.55 C
ANISOU 2160 CD2 LEU A 198 11750 9372 14802 -110 1641 57 C
ATOM 2161 N LEU A 199 7.279 161.393 137.368 1.00 92.38 N
ANISOU 2161 N LEU A 199 11632 9612 13857 -214 464 272 N
ATOM 2162 CA LEU A 199 7.700 160.223 136.584 1.00 91.42 C
ANISOU 2162 CA LEU A 199 11582 9589 13562 -274 277 302 C
ATOM 2163 C LEU A 199 8.846 159.485 137.291 1.00 92.75 C
ANISOU 2163 C LEU A 199 11958 9845 13438 -295 348 217 C
ATOM 2164 O LEU A 199 8.735 158.286 137.496 1.00 92.23 O
ANISOU 2164 O LEU A 199 11927 9812 13304 -337 352 209 O
ATOM 2165 CB LEU A 199 8.148 160.646 135.186 1.00 91.25 C
ANISOU 2165 CB LEU A 199 11585 9599 13489 -289 35 369 C
ATOM 2166 CG LEU A 199 7.693 159.741 134.077 1.00 96.43 C
ANISOU 2166 CG LEU A 199 12220 10268 14151 -362 -177 450 C
ATOM 2167 CD1 LEU A 199 7.423 160.538 132.807 1.00 97.68 C
ANISOU 2167 CD1 LEU A 199 12344 10380 14390 -388 -403 549 C
ATOM 2168 CD2 LEU A 199 8.705 158.685 133.812 1.00 97.65 C
ANISOU 2168 CD2 LEU A 199 12564 10518 14022 -407 -210 402 C
ATOM 2169 N PHE A 200 9.901 160.216 137.716 1.00 88.11 N
ANISOU 2169 N PHE A 200 11498 9277 12702 -272 397 161 N
ATOM 2170 CA PHE A 200 11.060 159.665 138.413 1.00 87.15 C
ANISOU 2170 CA PHE A 200 11558 9213 12341 -297 429 100 C
ATOM 2171 C PHE A 200 10.690 159.033 139.752 1.00 92.85 C
ANISOU 2171 C PHE A 200 12351 9900 13028 -328 603 49 C
ATOM 2172 O PHE A 200 11.045 157.878 139.978 1.00 93.38 O
ANISOU 2172 O PHE A 200 12499 10011 12969 -369 571 43 O
ATOM 2173 CB PHE A 200 12.172 160.723 138.583 1.00 88.17 C
ANISOU 2173 CB PHE A 200 11788 9348 12365 -276 421 70 C
ATOM 2174 CG PHE A 200 13.442 160.218 139.238 1.00 88.58 C
ANISOU 2174 CG PHE A 200 12004 9441 12212 -309 404 33 C
ATOM 2175 CD1 PHE A 200 14.417 159.564 138.493 1.00 90.98 C
ANISOU 2175 CD1 PHE A 200 12334 9810 12424 -320 274 57 C
ATOM 2176 CD2 PHE A 200 13.671 160.414 140.595 1.00 90.68 C
ANISOU 2176 CD2 PHE A 200 12407 9659 12390 -339 517 -19 C
ATOM 2177 CE1 PHE A 200 15.588 159.084 139.099 1.00 91.54 C
ANISOU 2177 CE1 PHE A 200 12518 9896 12367 -347 245 42 C
ATOM 2178 CE2 PHE A 200 14.846 159.946 141.198 1.00 93.19 C
ANISOU 2178 CE2 PHE A 200 12870 9996 12541 -384 452 -28 C
ATOM 2179 CZ PHE A 200 15.801 159.287 140.445 1.00 90.48 C
ANISOU 2179 CZ PHE A 200 12504 9717 12158 -381 309 9 C
ATOM 2180 N SER A 201 9.997 159.777 140.630 1.00 90.17 N
ANISOU 2180 N SER A 201 11999 9465 12797 -315 798 13 N
ATOM 2181 CA SER A 201 9.588 159.299 141.948 1.00 91.46 C
ANISOU 2181 CA SER A 201 12270 9568 12912 -361 1006 -43 C
ATOM 2182 C SER A 201 8.560 158.153 141.903 1.00 99.08 C
ANISOU 2182 C SER A 201 13127 10526 13995 -387 1048 -12 C
ATOM 2183 O SER A 201 8.687 157.212 142.684 1.00 98.65 O
ANISOU 2183 O SER A 201 13205 10477 13802 -446 1116 -41 O
ATOM 2184 CB SER A 201 9.088 160.449 142.809 1.00 95.42 C
ANISOU 2184 CB SER A 201 12806 9944 13506 -345 1242 -99 C
ATOM 2185 OG SER A 201 8.049 161.180 142.184 1.00103.49 O
ANISOU 2185 OG SER A 201 13590 10895 14838 -280 1289 -58 O
ATOM 2186 N MET A 202 7.568 158.218 140.979 1.00 98.34 N
ANISOU 2186 N MET A 202 12796 10412 14158 -354 984 57 N
ATOM 2187 CA MET A 202 6.543 157.186 140.781 1.00 99.61 C
ANISOU 2187 CA MET A 202 12820 10558 14471 -385 986 105 C
ATOM 2188 C MET A 202 7.220 155.911 140.352 1.00101.04 C
ANISOU 2188 C MET A 202 13100 10845 14444 -432 809 119 C
ATOM 2189 O MET A 202 6.941 154.877 140.936 1.00101.20 O
ANISOU 2189 O MET A 202 13169 10863 14418 -481 884 106 O
ATOM 2190 CB MET A 202 5.486 157.580 139.727 1.00103.93 C
ANISOU 2190 CB MET A 202 13097 11051 15340 -355 875 201 C
ATOM 2191 CG MET A 202 4.684 158.845 140.052 1.00111.07 C
ANISOU 2191 CG MET A 202 13845 11819 16536 -296 1050 204 C
ATOM 2192 SD MET A 202 3.509 158.752 141.432 1.00119.50 S
ANISOU 2192 SD MET A 202 14844 12733 17827 -304 1447 154 S
ATOM 2193 CE MET A 202 4.445 159.575 142.757 1.00116.12 C
ANISOU 2193 CE MET A 202 14721 12271 17131 -301 1704 15 C
ATOM 2194 N LEU A 203 8.148 155.989 139.374 1.00 95.38 N
ANISOU 2194 N LEU A 203 12429 10209 13604 -420 598 141 N
ATOM 2195 CA LEU A 203 8.899 154.840 138.867 1.00 93.67 C
ANISOU 2195 CA LEU A 203 12311 10073 13206 -457 452 149 C
ATOM 2196 C LEU A 203 9.771 154.169 139.900 1.00 97.94 C
ANISOU 2196 C LEU A 203 13033 10638 13540 -484 522 94 C
ATOM 2197 O LEU A 203 9.732 152.945 139.989 1.00 97.87 O
ANISOU 2197 O LEU A 203 13064 10648 13475 -526 499 100 O
ATOM 2198 CB LEU A 203 9.714 155.185 137.637 1.00 92.47 C
ANISOU 2198 CB LEU A 203 12183 9972 12980 -441 270 175 C
ATOM 2199 CG LEU A 203 9.147 154.625 136.373 1.00 97.20 C
ANISOU 2199 CG LEU A 203 12716 10575 13641 -480 102 241 C
ATOM 2200 CD1 LEU A 203 9.079 155.660 135.346 1.00 97.84 C
ANISOU 2200 CD1 LEU A 203 12732 10633 13809 -465 -18 293 C
ATOM 2201 CD2 LEU A 203 9.955 153.466 135.878 1.00 98.43 C
ANISOU 2201 CD2 LEU A 203 13008 10782 13609 -515 17 227 C
ATOM 2202 N GLY A 204 10.533 154.957 140.665 1.00 94.20 N
ANISOU 2202 N GLY A 204 12676 10152 12964 -470 588 50 N
ATOM 2203 CA GLY A 204 11.378 154.447 141.742 1.00 93.67 C
ANISOU 2203 CA GLY A 204 12798 10083 12708 -514 621 15 C
ATOM 2204 C GLY A 204 10.534 153.853 142.860 1.00 97.96 C
ANISOU 2204 C GLY A 204 13407 10565 13249 -572 793 -9 C
ATOM 2205 O GLY A 204 10.791 152.736 143.320 1.00 97.37 O
ANISOU 2205 O GLY A 204 13441 10498 13058 -625 769 -6 O
ATOM 2206 N GLY A 205 9.494 154.593 143.248 1.00 94.58 N
ANISOU 2206 N GLY A 205 12905 10062 12969 -561 977 -30 N
ATOM 2207 CA GLY A 205 8.534 154.207 144.272 1.00 95.21 C
ANISOU 2207 CA GLY A 205 13031 10057 13089 -615 1205 -59 C
ATOM 2208 C GLY A 205 7.787 152.941 143.925 1.00 97.93 C
ANISOU 2208 C GLY A 205 13266 10421 13522 -643 1179 -16 C
ATOM 2209 O GLY A 205 7.748 152.014 144.728 1.00 97.45 O
ANISOU 2209 O GLY A 205 13341 10339 13346 -713 1251 -31 O
ATOM 2210 N LEU A 206 7.232 152.876 142.715 1.00 94.74 N
ANISOU 2210 N LEU A 206 12639 10049 13310 -601 1053 42 N
ATOM 2211 CA LEU A 206 6.538 151.691 142.224 1.00 95.69 C
ANISOU 2211 CA LEU A 206 12652 10184 13523 -636 983 92 C
ATOM 2212 C LEU A 206 7.475 150.519 142.171 1.00 98.26 C
ANISOU 2212 C LEU A 206 13130 10582 13623 -674 841 92 C
ATOM 2213 O LEU A 206 7.041 149.445 142.532 1.00 98.42 O
ANISOU 2213 O LEU A 206 13166 10590 13640 -728 872 103 O
ATOM 2214 CB LEU A 206 5.940 151.925 140.843 1.00 96.59 C
ANISOU 2214 CB LEU A 206 12546 10310 13845 -605 812 166 C
ATOM 2215 CG LEU A 206 4.434 152.137 140.782 1.00104.88 C
ANISOU 2215 CG LEU A 206 13356 11264 15231 -607 907 218 C
ATOM 2216 CD1 LEU A 206 3.987 153.378 141.587 1.00106.65 C
ANISOU 2216 CD1 LEU A 206 13524 11385 15612 -561 1158 179 C
ATOM 2217 CD2 LEU A 206 3.996 152.299 139.351 1.00109.95 C
ANISOU 2217 CD2 LEU A 206 13822 11912 16042 -600 657 311 C
ATOM 2218 N SER A 207 8.765 150.729 141.755 1.00 93.37 N
ANISOU 2218 N SER A 207 12612 10023 12841 -645 698 81 N
ATOM 2219 CA SER A 207 9.836 149.720 141.703 1.00 91.74 C
ANISOU 2219 CA SER A 207 12536 9862 12458 -666 572 83 C
ATOM 2220 C SER A 207 10.042 149.098 143.076 1.00 96.06 C
ANISOU 2220 C SER A 207 13259 10369 12871 -729 668 61 C
ATOM 2221 O SER A 207 10.061 147.876 143.190 1.00 95.49 O
ANISOU 2221 O SER A 207 13235 10299 12747 -772 625 78 O
ATOM 2222 CB SER A 207 11.151 150.337 141.242 1.00 93.76 C
ANISOU 2222 CB SER A 207 12843 10158 12625 -619 457 76 C
ATOM 2223 OG SER A 207 11.274 150.303 139.832 1.00104.01 O
ANISOU 2223 OG SER A 207 14051 11495 13974 -588 330 102 O
ATOM 2224 N VAL A 208 10.166 149.943 144.117 1.00 93.22 N
ANISOU 2224 N VAL A 208 13017 9959 12444 -748 793 24 N
ATOM 2225 CA VAL A 208 10.320 149.527 145.512 1.00 93.38 C
ANISOU 2225 CA VAL A 208 13261 9916 12303 -835 887 4 C
ATOM 2226 C VAL A 208 9.017 148.878 146.029 1.00 97.97 C
ANISOU 2226 C VAL A 208 13824 10441 12960 -892 1079 -3 C
ATOM 2227 O VAL A 208 9.083 147.912 146.784 1.00 98.15 O
ANISOU 2227 O VAL A 208 14002 10432 12860 -973 1098 4 O
ATOM 2228 CB VAL A 208 10.798 150.707 146.394 1.00 97.29 C
ANISOU 2228 CB VAL A 208 13924 10355 12688 -857 964 -37 C
ATOM 2229 CG1 VAL A 208 10.822 150.336 147.873 1.00 98.49 C
ANISOU 2229 CG1 VAL A 208 14361 10415 12646 -978 1072 -58 C
ATOM 2230 CG2 VAL A 208 12.173 151.175 145.953 1.00 95.85 C
ANISOU 2230 CG2 VAL A 208 13759 10221 12440 -815 757 -17 C
ATOM 2231 N GLY A 209 7.870 149.408 145.597 1.00 94.75 N
ANISOU 2231 N GLY A 209 13215 10010 12775 -853 1209 -6 N
ATOM 2232 CA GLY A 209 6.540 148.936 145.970 1.00 95.76 C
ANISOU 2232 CA GLY A 209 13261 10069 13055 -897 1410 -4 C
ATOM 2233 C GLY A 209 6.310 147.530 145.487 1.00 99.44 C
ANISOU 2233 C GLY A 209 13663 10577 13544 -928 1287 45 C
ATOM 2234 O GLY A 209 6.112 146.619 146.290 1.00100.39 O
ANISOU 2234 O GLY A 209 13910 10656 13578 -1009 1377 42 O
ATOM 2235 N LEU A 210 6.422 147.349 144.175 1.00 95.22 N
ANISOU 2235 N LEU A 210 12965 10115 13099 -875 1074 89 N
ATOM 2236 CA LEU A 210 6.329 146.082 143.462 1.00 94.89 C
ANISOU 2236 CA LEU A 210 12874 10113 13068 -901 919 133 C
ATOM 2237 C LEU A 210 7.325 145.073 144.034 1.00 98.92 C
ANISOU 2237 C LEU A 210 13601 10639 13345 -944 849 124 C
ATOM 2238 O LEU A 210 6.960 143.923 144.210 1.00100.32 O
ANISOU 2238 O LEU A 210 13805 10799 13514 -1002 847 145 O
ATOM 2239 CB LEU A 210 6.591 146.324 141.972 1.00 94.16 C
ANISOU 2239 CB LEU A 210 12654 10080 13041 -845 705 165 C
ATOM 2240 CG LEU A 210 6.573 145.122 141.065 1.00 99.56 C
ANISOU 2240 CG LEU A 210 13321 10791 13716 -878 536 203 C
ATOM 2241 CD1 LEU A 210 5.141 144.645 140.787 1.00101.13 C
ANISOU 2241 CD1 LEU A 210 13348 10942 14135 -930 552 255 C
ATOM 2242 CD2 LEU A 210 7.319 145.412 139.793 1.00102.26 C
ANISOU 2242 CD2 LEU A 210 13665 11183 14008 -836 351 210 C
ATOM 2243 N SER A 211 8.549 145.504 144.371 1.00 94.51 N
ANISOU 2243 N SER A 211 13190 10098 12622 -923 785 103 N
ATOM 2244 CA SER A 211 9.555 144.660 145.010 1.00 94.11 C
ANISOU 2244 CA SER A 211 13333 10035 12387 -965 697 112 C
ATOM 2245 C SER A 211 9.055 144.118 146.347 1.00102.42 C
ANISOU 2245 C SER A 211 14555 11012 13348 -1068 848 107 C
ATOM 2246 O SER A 211 9.304 142.955 146.650 1.00102.46 O
ANISOU 2246 O SER A 211 14656 10999 13274 -1121 779 136 O
ATOM 2247 CB SER A 211 10.836 145.440 145.239 1.00 96.00 C
ANISOU 2247 CB SER A 211 13676 10282 12515 -935 606 104 C
ATOM 2248 OG SER A 211 11.609 145.477 144.056 1.00105.59 O
ANISOU 2248 OG SER A 211 14786 11554 13780 -858 448 119 O
ATOM 2249 N PHE A 212 8.331 144.952 147.134 1.00102.14 N
ANISOU 2249 N PHE A 212 14565 10917 13327 -1102 1071 69 N
ATOM 2250 CA PHE A 212 7.760 144.558 148.424 1.00104.13 C
ANISOU 2250 CA PHE A 212 15008 11074 13482 -1216 1273 52 C
ATOM 2251 C PHE A 212 6.608 143.561 148.239 1.00104.81 C
ANISOU 2251 C PHE A 212 14966 11144 13713 -1251 1367 76 C
ATOM 2252 O PHE A 212 6.566 142.534 148.924 1.00104.51 O
ANISOU 2252 O PHE A 212 15086 11064 13561 -1343 1387 94 O
ATOM 2253 CB PHE A 212 7.321 145.780 149.271 1.00108.62 C
ANISOU 2253 CB PHE A 212 15679 11558 14034 -1244 1531 -8 C
ATOM 2254 CG PHE A 212 6.716 145.360 150.595 1.00114.51 C
ANISOU 2254 CG PHE A 212 16669 12185 14656 -1380 1778 -33 C
ATOM 2255 CD1 PHE A 212 5.354 145.080 150.703 1.00120.64 C
ANISOU 2255 CD1 PHE A 212 17318 12899 15620 -1407 2039 -44 C
ATOM 2256 CD2 PHE A 212 7.520 145.155 151.712 1.00119.23 C
ANISOU 2256 CD2 PHE A 212 17629 12718 14954 -1496 1733 -34 C
ATOM 2257 CE1 PHE A 212 4.805 144.619 151.908 1.00124.01 C
ANISOU 2257 CE1 PHE A 212 17987 13205 15927 -1543 2295 -69 C
ATOM 2258 CE2 PHE A 212 6.968 144.695 152.919 1.00124.80 C
ANISOU 2258 CE2 PHE A 212 18606 13300 15511 -1644 1959 -54 C
ATOM 2259 CZ PHE A 212 5.612 144.447 153.012 1.00124.23 C
ANISOU 2259 CZ PHE A 212 18415 13171 15617 -1665 2261 -79 C
ATOM 2260 N LEU A 213 5.661 143.893 147.345 1.00 98.69 N
ANISOU 2260 N LEU A 213 13910 10390 13199 -1189 1413 84 N
ATOM 2261 CA LEU A 213 4.501 143.066 147.040 1.00 97.96 C
ANISOU 2261 CA LEU A 213 13649 10274 13298 -1223 1475 120 C
ATOM 2262 C LEU A 213 4.952 141.665 146.650 1.00101.00 C
ANISOU 2262 C LEU A 213 14085 10705 13586 -1252 1265 160 C
ATOM 2263 O LEU A 213 4.564 140.712 147.323 1.00102.56 O
ANISOU 2263 O LEU A 213 14380 10853 13737 -1340 1347 174 O
ATOM 2264 CB LEU A 213 3.694 143.702 145.907 1.00 97.41 C
ANISOU 2264 CB LEU A 213 13264 10224 13525 -1148 1439 148 C
ATOM 2265 CG LEU A 213 2.205 143.452 145.927 1.00102.98 C
ANISOU 2265 CG LEU A 213 13758 10849 14519 -1187 1606 183 C
ATOM 2266 CD1 LEU A 213 1.457 144.703 145.512 1.00103.97 C
ANISOU 2266 CD1 LEU A 213 13637 10929 14938 -1118 1699 194 C
ATOM 2267 CD2 LEU A 213 1.817 142.236 145.069 1.00102.75 C
ANISOU 2267 CD2 LEU A 213 13612 10855 14576 -1221 1406 250 C
ATOM 2268 N LEU A 214 5.826 141.546 145.618 1.00 95.22 N
ANISOU 2268 N LEU A 214 13311 10053 12814 -1183 1014 176 N
ATOM 2269 CA LEU A 214 6.349 140.262 145.116 1.00 94.12 C
ANISOU 2269 CA LEU A 214 13219 9942 12601 -1197 825 206 C
ATOM 2270 C LEU A 214 7.085 139.445 146.189 1.00 98.67 C
ANISOU 2270 C LEU A 214 14042 10475 12973 -1264 817 212 C
ATOM 2271 O LEU A 214 6.697 138.310 146.457 1.00 97.57 O
ANISOU 2271 O LEU A 214 13951 10299 12822 -1334 831 237 O
ATOM 2272 CB LEU A 214 7.261 140.451 143.882 1.00 92.16 C
ANISOU 2272 CB LEU A 214 12915 9760 12343 -1113 616 207 C
ATOM 2273 CG LEU A 214 6.666 141.122 142.642 1.00 95.27 C
ANISOU 2273 CG LEU A 214 13105 10189 12905 -1065 556 217 C
ATOM 2274 CD1 LEU A 214 7.772 141.577 141.710 1.00 93.55 C
ANISOU 2274 CD1 LEU A 214 12903 10020 12621 -991 407 204 C
ATOM 2275 CD2 LEU A 214 5.642 140.223 141.937 1.00 96.40 C
ANISOU 2275 CD2 LEU A 214 13135 10312 13179 -1120 497 259 C
ATOM 2276 N ASN A 215 8.121 140.053 146.813 1.00 95.86 N
ANISOU 2276 N ASN A 215 13844 10111 12465 -1252 782 198 N
ATOM 2277 CA ASN A 215 8.979 139.464 147.841 1.00 95.96 C
ANISOU 2277 CA ASN A 215 14108 10068 12285 -1323 717 223 C
ATOM 2278 C ASN A 215 8.248 138.879 149.026 1.00101.74 C
ANISOU 2278 C ASN A 215 15015 10717 12927 -1451 882 229 C
ATOM 2279 O ASN A 215 8.681 137.847 149.533 1.00102.72 O
ANISOU 2279 O ASN A 215 15300 10793 12938 -1519 786 272 O
ATOM 2280 CB ASN A 215 10.013 140.466 148.316 1.00 95.83 C
ANISOU 2280 CB ASN A 215 14215 10043 12154 -1306 657 214 C
ATOM 2281 CG ASN A 215 11.196 140.568 147.414 1.00118.67 C
ANISOU 2281 CG ASN A 215 17016 12984 15087 -1209 444 234 C
ATOM 2282 OD1 ASN A 215 11.314 139.849 146.416 1.00118.37 O
ANISOU 2282 OD1 ASN A 215 16846 12981 15148 -1154 352 246 O
ATOM 2283 ND2 ASN A 215 12.117 141.436 147.774 1.00111.61 N
ANISOU 2283 ND2 ASN A 215 16209 12077 14119 -1198 371 237 N
ATOM 2284 N THR A 216 7.168 139.536 149.491 1.00 98.29 N
ANISOU 2284 N THR A 216 14554 10244 12548 -1488 1141 189 N
ATOM 2285 CA THR A 216 6.370 139.037 150.607 1.00 99.36 C
ANISOU 2285 CA THR A 216 14860 10282 12610 -1619 1359 186 C
ATOM 2286 C THR A 216 5.686 137.751 150.167 1.00102.69 C
ANISOU 2286 C THR A 216 15164 10708 13144 -1645 1333 225 C
ATOM 2287 O THR A 216 5.806 136.747 150.860 1.00103.13 O
ANISOU 2287 O THR A 216 15415 10707 13064 -1744 1313 258 O
ATOM 2288 CB THR A 216 5.437 140.109 151.143 1.00109.92 C
ANISOU 2288 CB THR A 216 16189 11558 14018 -1642 1679 127 C
ATOM 2289 OG1 THR A 216 4.693 140.658 150.060 1.00110.77 O
ANISOU 2289 OG1 THR A 216 15955 11722 14411 -1532 1711 118 O
ATOM 2290 CG2 THR A 216 6.196 141.217 151.868 1.00110.02 C
ANISOU 2290 CG2 THR A 216 16439 11528 13834 -1665 1712 88 C
ATOM 2291 N VAL A 217 5.104 137.745 148.945 1.00 97.13 N
ANISOU 2291 N VAL A 217 14162 10070 12674 -1563 1283 232 N
ATOM 2292 CA VAL A 217 4.463 136.572 148.336 1.00 95.98 C
ANISOU 2292 CA VAL A 217 13889 9929 12651 -1589 1221 272 C
ATOM 2293 C VAL A 217 5.489 135.426 148.127 1.00 99.07 C
ANISOU 2293 C VAL A 217 14407 10334 12903 -1591 978 307 C
ATOM 2294 O VAL A 217 5.172 134.283 148.429 1.00100.31 O
ANISOU 2294 O VAL A 217 14630 10446 13038 -1669 978 339 O
ATOM 2295 CB VAL A 217 3.716 136.965 147.032 1.00 98.14 C
ANISOU 2295 CB VAL A 217 13848 10253 13187 -1515 1174 281 C
ATOM 2296 CG1 VAL A 217 3.156 135.750 146.302 1.00 97.38 C
ANISOU 2296 CG1 VAL A 217 13645 10155 13199 -1555 1061 327 C
ATOM 2297 CG2 VAL A 217 2.621 137.989 147.310 1.00 98.95 C
ANISOU 2297 CG2 VAL A 217 13797 10310 13489 -1515 1424 263 C
ATOM 2298 N SER A 218 6.709 135.737 147.646 1.00 93.83 N
ANISOU 2298 N SER A 218 13768 9717 12167 -1507 789 303 N
ATOM 2299 CA SER A 218 7.781 134.752 147.435 1.00 93.06 C
ANISOU 2299 CA SER A 218 13763 9607 11987 -1493 579 338 C
ATOM 2300 C SER A 218 8.261 134.169 148.782 1.00 99.11 C
ANISOU 2300 C SER A 218 14798 10286 12571 -1593 568 377 C
ATOM 2301 O SER A 218 8.564 132.974 148.862 1.00 99.47 O
ANISOU 2301 O SER A 218 14922 10285 12587 -1628 457 421 O
ATOM 2302 CB SER A 218 8.964 135.373 146.697 1.00 94.80 C
ANISOU 2302 CB SER A 218 13929 9875 12214 -1381 423 326 C
ATOM 2303 OG SER A 218 8.577 136.128 145.562 1.00105.69 O
ANISOU 2303 OG SER A 218 15108 11325 13724 -1304 435 293 O
ATOM 2304 N VAL A 219 8.338 135.011 149.835 1.00 95.77 N
ANISOU 2304 N VAL A 219 14540 9828 12020 -1649 675 363 N
ATOM 2305 CA VAL A 219 8.756 134.540 151.149 1.00 96.74 C
ANISOU 2305 CA VAL A 219 14969 9850 11938 -1775 651 407 C
ATOM 2306 C VAL A 219 7.619 133.671 151.672 1.00104.99 C
ANISOU 2306 C VAL A 219 16081 10837 12971 -1890 828 415 C
ATOM 2307 O VAL A 219 7.864 132.541 152.122 1.00107.00 O
ANISOU 2307 O VAL A 219 16490 11025 13139 -1969 728 473 O
ATOM 2308 CB VAL A 219 9.160 135.690 152.106 1.00100.42 C
ANISOU 2308 CB VAL A 219 15640 10276 12241 -1827 713 387 C
ATOM 2309 CG1 VAL A 219 9.325 135.203 153.543 1.00101.80 C
ANISOU 2309 CG1 VAL A 219 16186 10322 12170 -2003 722 432 C
ATOM 2310 CG2 VAL A 219 10.447 136.344 151.633 1.00 98.99 C
ANISOU 2310 CG2 VAL A 219 15403 10135 12075 -1727 489 402 C
ATOM 2311 N ALA A 220 6.366 134.157 151.507 1.00100.85 N
ANISOU 2311 N ALA A 220 15406 10333 12578 -1892 1080 365 N
ATOM 2312 CA ALA A 220 5.148 133.453 151.904 1.00101.23 C
ANISOU 2312 CA ALA A 220 15458 10324 12682 -1993 1288 370 C
ATOM 2313 C ALA A 220 5.101 132.068 151.262 1.00103.72 C
ANISOU 2313 C ALA A 220 15684 10651 13074 -1991 1123 419 C
ATOM 2314 O ALA A 220 4.714 131.101 151.922 1.00105.99 O
ANISOU 2314 O ALA A 220 16114 10862 13293 -2106 1183 454 O
ATOM 2315 CB ALA A 220 3.919 134.261 151.509 1.00102.26 C
ANISOU 2315 CB ALA A 220 15340 10473 13041 -1957 1536 323 C
ATOM 2316 N THR A 221 5.544 131.964 149.999 1.00 96.25 N
ANISOU 2316 N THR A 221 14534 9785 12251 -1870 922 420 N
ATOM 2317 CA THR A 221 5.564 130.704 149.281 1.00 95.23 C
ANISOU 2317 CA THR A 221 14338 9655 12190 -1864 769 455 C
ATOM 2318 C THR A 221 6.708 129.824 149.780 1.00100.27 C
ANISOU 2318 C THR A 221 15191 10231 12676 -1889 583 505 C
ATOM 2319 O THR A 221 6.506 128.635 149.961 1.00 99.84 O
ANISOU 2319 O THR A 221 15208 10118 12609 -1957 545 545 O
ATOM 2320 CB THR A 221 5.552 130.962 147.787 1.00 97.87 C
ANISOU 2320 CB THR A 221 14425 10071 12690 -1750 658 431 C
ATOM 2321 OG1 THR A 221 4.450 131.814 147.497 1.00 93.81 O
ANISOU 2321 OG1 THR A 221 13722 9589 12334 -1746 815 406 O
ATOM 2322 CG2 THR A 221 5.424 129.690 146.973 1.00 98.16 C
ANISOU 2322 CG2 THR A 221 14413 10091 12794 -1760 527 455 C
ATOM 2323 N LEU A 222 7.886 130.407 150.043 1.00 98.25 N
ANISOU 2323 N LEU A 222 15033 9973 12323 -1841 461 514 N
ATOM 2324 CA LEU A 222 9.046 129.662 150.531 1.00 98.94 C
ANISOU 2324 CA LEU A 222 15298 9981 12315 -1863 253 583 C
ATOM 2325 C LEU A 222 8.826 129.114 151.931 1.00107.73 C
ANISOU 2325 C LEU A 222 16700 10987 13247 -2028 298 637 C
ATOM 2326 O LEU A 222 9.279 128.016 152.229 1.00107.40 O
ANISOU 2326 O LEU A 222 16776 10860 13170 -2075 150 707 O
ATOM 2327 CB LEU A 222 10.328 130.517 150.478 1.00 97.83 C
ANISOU 2327 CB LEU A 222 15166 9851 12155 -1780 100 592 C
ATOM 2328 CG LEU A 222 11.112 130.565 149.153 1.00 99.72 C
ANISOU 2328 CG LEU A 222 15186 10143 12560 -1625 -24 572 C
ATOM 2329 CD1 LEU A 222 12.304 131.438 149.299 1.00 99.28 C
ANISOU 2329 CD1 LEU A 222 15147 10083 12492 -1567 -146 590 C
ATOM 2330 CD2 LEU A 222 11.634 129.198 148.744 1.00100.12 C
ANISOU 2330 CD2 LEU A 222 15220 10121 12699 -1599 -164 616 C
ATOM 2331 N CYS A 223 8.131 129.866 152.787 1.00108.92 N
ANISOU 2331 N CYS A 223 16980 11123 13280 -2121 513 604 N
ATOM 2332 CA CYS A 223 7.842 129.432 154.152 1.00112.57 C
ANISOU 2332 CA CYS A 223 17768 11468 13533 -2303 605 644 C
ATOM 2333 C CYS A 223 6.803 128.331 154.191 1.00120.42 C
ANISOU 2333 C CYS A 223 18748 12427 14578 -2384 733 657 C
ATOM 2334 O CYS A 223 6.943 127.405 154.991 1.00122.50 O
ANISOU 2334 O CYS A 223 19256 12587 14703 -2510 669 725 O
ATOM 2335 CB CYS A 223 7.436 130.610 155.024 1.00114.00 C
ANISOU 2335 CB CYS A 223 18113 11626 13577 -2382 844 590 C
ATOM 2336 SG CYS A 223 8.761 131.798 155.287 1.00117.60 S
ANISOU 2336 SG CYS A 223 18706 12078 13900 -2349 655 598 S
ATOM 2337 N HIS A 224 5.757 128.437 153.344 1.00116.85 N
ANISOU 2337 N HIS A 224 18015 12050 14332 -2324 899 602 N
ATOM 2338 CA HIS A 224 4.680 127.454 153.251 1.00117.60 C
ANISOU 2338 CA HIS A 224 18042 12115 14524 -2396 1021 615 C
ATOM 2339 C HIS A 224 5.216 126.127 152.694 1.00119.84 C
ANISOU 2339 C HIS A 224 18306 12382 14847 -2370 769 672 C
ATOM 2340 O HIS A 224 4.935 125.070 153.257 1.00121.09 O
ANISOU 2340 O HIS A 224 18613 12455 14941 -2485 779 722 O
ATOM 2341 CB HIS A 224 3.526 128.013 152.389 1.00118.29 C
ANISOU 2341 CB HIS A 224 17804 12279 14863 -2332 1201 560 C
ATOM 2342 CG HIS A 224 2.577 126.972 151.877 1.00122.48 C
ANISOU 2342 CG HIS A 224 18182 12795 15561 -2374 1228 585 C
ATOM 2343 ND1 HIS A 224 2.596 126.568 150.551 1.00123.11 N
ANISOU 2343 ND1 HIS A 224 18036 12939 15803 -2281 1038 588 N
ATOM 2344 CD2 HIS A 224 1.633 126.262 152.537 1.00126.23 C
ANISOU 2344 CD2 HIS A 224 18724 13187 16051 -2511 1418 610 C
ATOM 2345 CE1 HIS A 224 1.662 125.637 150.446 1.00123.64 C
ANISOU 2345 CE1 HIS A 224 18036 12962 15980 -2366 1096 618 C
ATOM 2346 NE2 HIS A 224 1.063 125.410 151.616 1.00125.83 N
ANISOU 2346 NE2 HIS A 224 18467 13153 16187 -2500 1325 635 N
ATOM 2347 N VAL A 225 6.036 126.212 151.635 1.00113.66 N
ANISOU 2347 N VAL A 225 17362 11663 14162 -2224 558 663 N
ATOM 2348 CA VAL A 225 6.633 125.123 150.868 1.00112.41 C
ANISOU 2348 CA VAL A 225 17147 11482 14081 -2166 344 695 C
ATOM 2349 C VAL A 225 7.872 124.483 151.528 1.00118.84 C
ANISOU 2349 C VAL A 225 18174 12194 14786 -2186 129 775 C
ATOM 2350 O VAL A 225 7.934 123.256 151.574 1.00120.38 O
ANISOU 2350 O VAL A 225 18433 12308 14996 -2228 38 825 O
ATOM 2351 CB VAL A 225 6.922 125.635 149.439 1.00114.02 C
ANISOU 2351 CB VAL A 225 17101 11781 14442 -2011 269 640 C
ATOM 2352 CG1 VAL A 225 8.032 124.866 148.756 1.00113.15 C
ANISOU 2352 CG1 VAL A 225 16981 11626 14386 -1925 58 661 C
ATOM 2353 CG2 VAL A 225 5.655 125.640 148.594 1.00113.65 C
ANISOU 2353 CG2 VAL A 225 16847 11791 14543 -2018 388 599 C
ATOM 2354 N TYR A 226 8.850 125.271 152.026 1.00115.69 N
ANISOU 2354 N TYR A 226 17874 11783 14299 -2160 30 796 N
ATOM 2355 CA TYR A 226 10.060 124.697 152.639 1.00116.29 C
ANISOU 2355 CA TYR A 226 18126 11742 14317 -2183 -218 895 C
ATOM 2356 C TYR A 226 9.809 124.204 154.083 1.00123.07 C
ANISOU 2356 C TYR A 226 19320 12483 14959 -2379 -211 972 C
ATOM 2357 O TYR A 226 10.754 124.052 154.858 1.00124.26 O
ANISOU 2357 O TYR A 226 19673 12526 15014 -2438 -423 1067 O
ATOM 2358 CB TYR A 226 11.274 125.667 152.537 1.00116.60 C
ANISOU 2358 CB TYR A 226 18123 11797 14382 -2086 -369 905 C
ATOM 2359 CG TYR A 226 11.961 125.722 151.180 1.00116.61 C
ANISOU 2359 CG TYR A 226 17852 11849 14604 -1903 -449 867 C
ATOM 2360 CD1 TYR A 226 11.345 125.208 150.039 1.00118.12 C
ANISOU 2360 CD1 TYR A 226 17861 12095 14925 -1835 -357 802 C
ATOM 2361 CD2 TYR A 226 13.229 126.282 151.038 1.00116.36 C
ANISOU 2361 CD2 TYR A 226 17765 11797 14652 -1811 -614 900 C
ATOM 2362 CE1 TYR A 226 11.970 125.252 148.792 1.00117.67 C
ANISOU 2362 CE1 TYR A 226 17608 12063 15036 -1689 -405 760 C
ATOM 2363 CE2 TYR A 226 13.866 126.330 149.794 1.00115.84 C
ANISOU 2363 CE2 TYR A 226 17467 11759 14788 -1652 -644 859 C
ATOM 2364 CZ TYR A 226 13.228 125.815 148.672 1.00121.39 C
ANISOU 2364 CZ TYR A 226 18028 12511 15585 -1594 -529 784 C
ATOM 2365 OH TYR A 226 13.820 125.848 147.431 1.00118.39 O
ANISOU 2365 OH TYR A 226 17471 12140 15370 -1459 -532 736 O
ATOM 2366 N HIS A 227 8.536 123.925 154.426 1.00120.65 N
ANISOU 2366 N HIS A 227 19072 12180 14587 -2491 26 940 N
ATOM 2367 CA HIS A 227 8.108 123.425 155.729 1.00122.94 C
ANISOU 2367 CA HIS A 227 19693 12355 14664 -2694 100 997 C
ATOM 2368 C HIS A 227 6.935 122.457 155.598 1.00124.10 C
ANISOU 2368 C HIS A 227 19793 12489 14869 -2765 275 985 C
ATOM 2369 O HIS A 227 5.970 122.733 154.878 1.00123.62 O
ANISOU 2369 O HIS A 227 19488 12522 14958 -2710 472 906 O
ATOM 2370 CB HIS A 227 7.751 124.580 156.684 1.00125.97 C
ANISOU 2370 CB HIS A 227 20284 12732 14846 -2801 305 957 C
ATOM 2371 CG HIS A 227 8.944 125.322 157.230 1.00130.80 C
ANISOU 2371 CG HIS A 227 21073 13301 15324 -2807 94 1003 C
ATOM 2372 ND1 HIS A 227 9.173 126.661 156.919 1.00132.03 N
ANISOU 2372 ND1 HIS A 227 21111 13547 15508 -2712 153 932 N
ATOM 2373 CD2 HIS A 227 9.933 124.892 158.053 1.00134.58 C
ANISOU 2373 CD2 HIS A 227 21830 13646 15659 -2906 -191 1124 C
ATOM 2374 CE1 HIS A 227 10.284 126.995 157.560 1.00132.42 C
ANISOU 2374 CE1 HIS A 227 21369 13518 15425 -2759 -90 1006 C
ATOM 2375 NE2 HIS A 227 10.779 125.964 158.254 1.00134.34 N
ANISOU 2375 NE2 HIS A 227 21851 13622 15569 -2878 -315 1129 N
ATOM 2376 N GLY A 228 7.036 121.332 156.297 1.00118.21 N
ANISOU 2376 N GLY A 228 19279 11617 14018 -2894 181 1075 N
ATOM 2377 CA GLY A 228 5.984 120.326 156.316 1.00116.92 C
ANISOU 2377 CA GLY A 228 19110 11420 13894 -2986 330 1079 C
ATOM 2378 C GLY A 228 6.225 119.105 155.454 1.00115.63 C
ANISOU 2378 C GLY A 228 18794 11236 13904 -2908 142 1113 C
ATOM 2379 O GLY A 228 7.375 118.713 155.224 1.00115.62 O
ANISOU 2379 O GLY A 228 18796 11184 13949 -2825 -132 1169 O
ATOM 2380 N MET A2001 5.120 118.487 154.978 1.00107.01 N
ANISOU 2380 N MET A2001 17563 10167 12930 -2938 295 1080 N
ATOM 2381 CA MET A2001 5.121 117.286 154.135 1.00103.49 C
ANISOU 2381 CA MET A2001 16993 9691 12638 -2888 158 1099 C
ATOM 2382 C MET A2001 5.705 117.549 152.754 1.00103.84 C
ANISOU 2382 C MET A2001 16767 9819 12868 -2691 31 1040 C
ATOM 2383 O MET A2001 5.912 118.701 152.396 1.00102.82 O
ANISOU 2383 O MET A2001 16516 9790 12763 -2597 70 982 O
ATOM 2384 CB MET A2001 3.714 116.680 154.051 1.00105.67 C
ANISOU 2384 CB MET A2001 17205 9961 12982 -2997 358 1085 C
ATOM 2385 CG MET A2001 3.231 116.159 155.370 1.00110.30 C
ANISOU 2385 CG MET A2001 18086 10434 13389 -3199 482 1151 C
ATOM 2386 SD MET A2001 1.476 115.803 155.377 1.00115.03 S
ANISOU 2386 SD MET A2001 18564 11035 14106 -3329 799 1124 S
ATOM 2387 CE MET A2001 1.465 114.109 154.783 1.00112.17 C
ANISOU 2387 CE MET A2001 18182 10592 13845 -3348 599 1181 C
ATOM 2388 N LYS A2002 6.023 116.489 151.997 1.00100.08 N
ANISOU 2388 N LYS A2002 16225 9288 12512 -2636 -112 1052 N
ATOM 2389 CA LYS A2002 6.606 116.624 150.664 1.00 98.29 C
ANISOU 2389 CA LYS A2002 15793 9108 12444 -2468 -208 991 C
ATOM 2390 C LYS A2002 5.597 117.199 149.682 1.00103.16 C
ANISOU 2390 C LYS A2002 16189 9849 13159 -2440 -69 902 C
ATOM 2391 O LYS A2002 4.627 116.544 149.311 1.00102.97 O
ANISOU 2391 O LYS A2002 16109 9813 13202 -2510 -16 893 O
ATOM 2392 CB LYS A2002 7.228 115.307 150.166 1.00100.35 C
ANISOU 2392 CB LYS A2002 16084 9241 12802 -2428 -370 1025 C
ATOM 2393 N LYS A2003 5.792 118.467 149.335 1.00101.22 N
ANISOU 2393 N LYS A2003 15822 9710 12925 -2351 -24 847 N
ATOM 2394 CA LYS A2003 4.924 119.167 148.400 1.00100.79 C
ANISOU 2394 CA LYS A2003 15553 9766 12976 -2319 74 777 C
ATOM 2395 C LYS A2003 5.401 118.891 146.957 1.00105.24 C
ANISOU 2395 C LYS A2003 16012 10333 13643 -2212 -49 727 C
ATOM 2396 O LYS A2003 6.596 118.671 146.720 1.00105.12 O
ANISOU 2396 O LYS A2003 16047 10265 13630 -2116 -163 727 O
ATOM 2397 CB LYS A2003 4.856 120.672 148.735 1.00101.59 C
ANISOU 2397 CB LYS A2003 15590 9967 13043 -2279 184 745 C
ATOM 2398 N TYR A2004 4.443 118.811 146.022 1.00101.05 N
ANISOU 2398 N TYR A2004 15351 9837 13206 -2246 -24 693 N
ATOM 2399 CA TYR A2004 4.682 118.589 144.601 1.00 99.61 C
ANISOU 2399 CA TYR A2004 15113 9647 13089 -2184 -121 640 C
ATOM 2400 C TYR A2004 3.949 119.665 143.873 1.00102.83 C
ANISOU 2400 C TYR A2004 15346 10160 13564 -2174 -87 603 C
ATOM 2401 O TYR A2004 2.781 119.889 144.163 1.00104.21 O
ANISOU 2401 O TYR A2004 15419 10368 13808 -2264 -7 631 O
ATOM 2402 CB TYR A2004 4.128 117.235 144.160 1.00101.28 C
ANISOU 2402 CB TYR A2004 15384 9759 13336 -2279 -177 653 C
ATOM 2403 CG TYR A2004 5.059 116.079 144.421 1.00102.53 C
ANISOU 2403 CG TYR A2004 15708 9785 13462 -2256 -248 674 C
ATOM 2404 CD1 TYR A2004 5.691 115.421 143.374 1.00103.96 C
ANISOU 2404 CD1 TYR A2004 15945 9878 13678 -2199 -320 626 C
ATOM 2405 CD2 TYR A2004 5.291 115.624 145.715 1.00104.00 C
ANISOU 2405 CD2 TYR A2004 16010 9915 13591 -2302 -239 747 C
ATOM 2406 CE1 TYR A2004 6.516 114.324 143.606 1.00105.44 C
ANISOU 2406 CE1 TYR A2004 16263 9919 13882 -2172 -372 650 C
ATOM 2407 CE2 TYR A2004 6.112 114.528 145.961 1.00105.61 C
ANISOU 2407 CE2 TYR A2004 16352 9977 13798 -2285 -329 785 C
ATOM 2408 CZ TYR A2004 6.733 113.888 144.905 1.00113.75 C
ANISOU 2408 CZ TYR A2004 17398 10918 14903 -2210 -391 736 C
ATOM 2409 OH TYR A2004 7.560 112.823 145.160 1.00118.12 O
ANISOU 2409 OH TYR A2004 18067 11311 15502 -2182 -466 777 O
ATOM 2410 N THR A2005 4.605 120.346 142.948 1.00 97.28 N
ANISOU 2410 N THR A2005 14603 9498 12863 -2071 -140 548 N
ATOM 2411 CA THR A2005 3.935 121.412 142.212 1.00 96.43 C
ANISOU 2411 CA THR A2005 14338 9480 12820 -2065 -135 524 C
ATOM 2412 C THR A2005 3.603 120.945 140.812 1.00 99.82 C
ANISOU 2412 C THR A2005 14778 9868 13281 -2109 -250 497 C
ATOM 2413 O THR A2005 4.356 120.147 140.239 1.00 99.95 O
ANISOU 2413 O THR A2005 14936 9799 13241 -2083 -305 460 O
ATOM 2414 CB THR A2005 4.775 122.707 142.232 1.00101.86 C
ANISOU 2414 CB THR A2005 14979 10249 13474 -1940 -104 490 C
ATOM 2415 N CYS A2006 2.479 121.435 140.254 1.00 95.37 N
ANISOU 2415 N CYS A2006 14075 9344 12816 -2184 -288 519 N
ATOM 2416 CA CYS A2006 2.091 121.136 138.877 1.00 95.03 C
ANISOU 2416 CA CYS A2006 14065 9255 12788 -2254 -436 505 C
ATOM 2417 C CYS A2006 3.027 121.939 137.989 1.00100.69 C
ANISOU 2417 C CYS A2006 14831 10003 13422 -2150 -465 440 C
ATOM 2418 O CYS A2006 3.108 123.158 138.138 1.00 99.13 O
ANISOU 2418 O CYS A2006 14509 9899 13256 -2079 -422 440 O
ATOM 2419 CB CYS A2006 0.635 121.510 138.624 1.00 95.29 C
ANISOU 2419 CB CYS A2006 13909 9309 12989 -2368 -500 574 C
ATOM 2420 SG CYS A2006 0.126 121.336 136.896 1.00 99.51 S
ANISOU 2420 SG CYS A2006 14504 9778 13529 -2483 -743 579 S
ATOM 2421 N THR A2007 3.766 121.267 137.094 1.00100.01 N
ANISOU 2421 N THR A2007 14937 9828 13233 -2141 -511 380 N
ATOM 2422 CA THR A2007 4.700 121.981 136.218 1.00 99.94 C
ANISOU 2422 CA THR A2007 14999 9828 13146 -2051 -504 312 C
ATOM 2423 C THR A2007 3.990 122.649 135.049 1.00106.53 C
ANISOU 2423 C THR A2007 15821 10679 13975 -2135 -634 317 C
ATOM 2424 O THR A2007 4.660 123.199 134.180 1.00107.57 O
ANISOU 2424 O THR A2007 16047 10804 14021 -2089 -634 262 O
ATOM 2425 CB THR A2007 5.862 121.104 135.763 1.00110.49 C
ANISOU 2425 CB THR A2007 16543 11039 14397 -1999 -450 239 C
ATOM 2426 OG1 THR A2007 5.358 120.073 134.917 1.00112.57 O
ANISOU 2426 OG1 THR A2007 16978 11184 14609 -2131 -534 222 O
ATOM 2427 CG2 THR A2007 6.674 120.540 136.927 1.00110.71 C
ANISOU 2427 CG2 THR A2007 16567 11036 14462 -1909 -357 254 C
ATOM 2428 N VAL A2008 2.646 122.632 135.039 1.00103.79 N
ANISOU 2428 N VAL A2008 15356 10344 13736 -2262 -748 395 N
ATOM 2429 CA VAL A2008 1.825 123.265 134.006 1.00104.01 C
ANISOU 2429 CA VAL A2008 15344 10371 13804 -2364 -924 435 C
ATOM 2430 C VAL A2008 1.167 124.567 134.539 1.00107.79 C
ANISOU 2430 C VAL A2008 15537 10964 14455 -2319 -908 500 C
ATOM 2431 O VAL A2008 1.178 125.564 133.821 1.00108.08 O
ANISOU 2431 O VAL A2008 15545 11033 14487 -2302 -984 502 O
ATOM 2432 CB VAL A2008 0.821 122.267 133.371 1.00109.08 C
ANISOU 2432 CB VAL A2008 16068 10904 14474 -2557 -1108 487 C
ATOM 2433 CG1 VAL A2008 -0.136 122.960 132.403 1.00109.83 C
ANISOU 2433 CG1 VAL A2008 16095 10986 14650 -2682 -1340 563 C
ATOM 2434 CG2 VAL A2008 1.564 121.141 132.666 1.00109.40 C
ANISOU 2434 CG2 VAL A2008 16431 10814 14321 -2598 -1109 404 C
ATOM 2435 N CYS A2009 0.621 124.574 135.773 1.00103.93 N
ANISOU 2435 N CYS A2009 14857 10519 14113 -2303 -793 549 N
ATOM 2436 CA CYS A2009 -0.019 125.777 136.317 1.00103.78 C
ANISOU 2436 CA CYS A2009 14577 10579 14274 -2262 -732 602 C
ATOM 2437 C CYS A2009 0.546 126.203 137.683 1.00105.37 C
ANISOU 2437 C CYS A2009 14725 10854 14458 -2138 -497 570 C
ATOM 2438 O CYS A2009 0.017 127.131 138.305 1.00105.09 O
ANISOU 2438 O CYS A2009 14496 10867 14566 -2106 -396 602 O
ATOM 2439 CB CYS A2009 -1.547 125.656 136.333 1.00106.46 C
ANISOU 2439 CB CYS A2009 14705 10874 14871 -2395 -822 710 C
ATOM 2440 SG CYS A2009 -2.246 124.704 137.720 1.00111.49 S
ANISOU 2440 SG CYS A2009 15256 11476 15629 -2453 -647 751 S
ATOM 2441 N GLY A2010 1.626 125.549 138.113 1.00100.17 N
ANISOU 2441 N GLY A2010 14247 10184 13631 -2076 -418 511 N
ATOM 2442 CA GLY A2010 2.290 125.853 139.378 1.00 98.51 C
ANISOU 2442 CA GLY A2010 14042 10019 13367 -1982 -244 491 C
ATOM 2443 C GLY A2010 1.586 125.365 140.636 1.00102.03 C
ANISOU 2443 C GLY A2010 14440 10445 13883 -2047 -113 537 C
ATOM 2444 O GLY A2010 2.180 125.478 141.714 1.00101.89 O
ANISOU 2444 O GLY A2010 14486 10444 13785 -1996 15 524 O
ATOM 2445 N TYR A2011 0.316 124.809 140.523 1.00 96.92 N
ANISOU 2445 N TYR A2011 13693 9746 13386 -2174 -148 597 N
ATOM 2446 CA TYR A2011 -0.519 124.298 141.636 1.00 95.98 C
ANISOU 2446 CA TYR A2011 13518 9588 13360 -2258 -2 647 C
ATOM 2447 C TYR A2011 0.300 123.452 142.605 1.00 98.79 C
ANISOU 2447 C TYR A2011 14086 9912 13536 -2247 78 626 C
ATOM 2448 O TYR A2011 0.751 122.364 142.234 1.00 99.87 O
ANISOU 2448 O TYR A2011 14371 9991 13582 -2270 -30 616 O
ATOM 2449 CB TYR A2011 -1.773 123.517 141.142 1.00 97.63 C
ANISOU 2449 CB TYR A2011 13621 9724 13751 -2403 -101 716 C
ATOM 2450 CG TYR A2011 -2.468 122.710 142.229 1.00100.05 C
ANISOU 2450 CG TYR A2011 13918 9970 14126 -2501 52 761 C
ATOM 2451 CD1 TYR A2011 -3.411 123.297 143.069 1.00103.06 C
ANISOU 2451 CD1 TYR A2011 14110 10343 14704 -2535 260 804 C
ATOM 2452 CD2 TYR A2011 -2.180 121.359 142.420 1.00100.87 C
ANISOU 2452 CD2 TYR A2011 14210 10009 14106 -2561 10 761 C
ATOM 2453 CE1 TYR A2011 -4.033 122.568 144.089 1.00104.11 C
ANISOU 2453 CE1 TYR A2011 14260 10409 14887 -2634 437 840 C
ATOM 2454 CE2 TYR A2011 -2.780 120.626 143.450 1.00102.68 C
ANISOU 2454 CE2 TYR A2011 14456 10179 14379 -2657 157 804 C
ATOM 2455 CZ TYR A2011 -3.706 121.235 144.282 1.00107.07 C
ANISOU 2455 CZ TYR A2011 14839 10731 15112 -2698 376 843 C
ATOM 2456 OH TYR A2011 -4.311 120.524 145.292 1.00103.23 O
ANISOU 2456 OH TYR A2011 14387 10173 14663 -2806 552 883 O
ATOM 2457 N ILE A2012 0.521 123.955 143.831 1.00 92.31 N
ANISOU 2457 N ILE A2012 13299 9114 12660 -2217 257 622 N
ATOM 2458 CA ILE A2012 1.280 123.189 144.809 1.00 90.29 C
ANISOU 2458 CA ILE A2012 13260 8813 12234 -2226 299 623 C
ATOM 2459 C ILE A2012 0.318 122.257 145.506 1.00 93.22 C
ANISOU 2459 C ILE A2012 13649 9108 12661 -2365 395 676 C
ATOM 2460 O ILE A2012 -0.633 122.728 146.136 1.00 93.21 O
ANISOU 2460 O ILE A2012 13542 9103 12771 -2425 581 699 O
ATOM 2461 CB ILE A2012 2.057 124.089 145.794 1.00 92.46 C
ANISOU 2461 CB ILE A2012 13623 9123 12384 -2159 409 602 C
ATOM 2462 N TYR A2013 0.526 120.924 145.320 1.00 89.12 N
ANISOU 2462 N TYR A2013 13256 8516 12088 -2416 282 693 N
ATOM 2463 CA TYR A2013 -0.236 119.844 145.952 1.00 88.97 C
ANISOU 2463 CA TYR A2013 13290 8413 12100 -2553 348 747 C
ATOM 2464 C TYR A2013 0.292 119.719 147.347 1.00 93.81 C
ANISOU 2464 C TYR A2013 14104 8991 12548 -2575 470 763 C
ATOM 2465 O TYR A2013 1.440 119.299 147.529 1.00 91.76 O
ANISOU 2465 O TYR A2013 14024 8702 12139 -2521 360 759 O
ATOM 2466 CB TYR A2013 -0.099 118.479 145.238 1.00 88.98 C
ANISOU 2466 CB TYR A2013 13383 8338 12087 -2598 174 757 C
ATOM 2467 CG TYR A2013 -0.794 117.393 146.042 1.00 90.68 C
ANISOU 2467 CG TYR A2013 13673 8463 12316 -2739 251 815 C
ATOM 2468 CD1 TYR A2013 -2.178 117.242 145.994 1.00 93.31 C
ANISOU 2468 CD1 TYR A2013 13839 8773 12841 -2860 330 862 C
ATOM 2469 CD2 TYR A2013 -0.086 116.612 146.953 1.00 91.04 C
ANISOU 2469 CD2 TYR A2013 13948 8440 12203 -2757 258 837 C
ATOM 2470 CE1 TYR A2013 -2.833 116.325 146.808 1.00 94.13 C
ANISOU 2470 CE1 TYR A2013 14008 8792 12966 -2996 437 917 C
ATOM 2471 CE2 TYR A2013 -0.732 115.706 147.783 1.00 93.21 C
ANISOU 2471 CE2 TYR A2013 14312 8631 12474 -2896 349 895 C
ATOM 2472 CZ TYR A2013 -2.108 115.572 147.714 1.00101.21 C
ANISOU 2472 CZ TYR A2013 15162 9628 13667 -3015 454 929 C
ATOM 2473 OH TYR A2013 -2.741 114.656 148.511 1.00104.12 O
ANISOU 2473 OH TYR A2013 15618 9906 14039 -3159 559 987 O
ATOM 2474 N ASN A2014 -0.534 120.089 148.331 1.00 93.66 N
ANISOU 2474 N ASN A2014 14065 8956 12566 -2662 699 786 N
ATOM 2475 CA ASN A2014 -0.137 120.044 149.727 1.00 95.26 C
ANISOU 2475 CA ASN A2014 14507 9109 12580 -2718 831 803 C
ATOM 2476 C ASN A2014 -0.807 118.844 150.326 1.00101.45 C
ANISOU 2476 C ASN A2014 15397 9791 13360 -2869 902 859 C
ATOM 2477 O ASN A2014 -2.041 118.832 150.378 1.00101.05 O
ANISOU 2477 O ASN A2014 15194 9715 13484 -2960 1073 878 O
ATOM 2478 CB ASN A2014 -0.538 121.333 150.455 1.00101.96 C
ANISOU 2478 CB ASN A2014 15316 9986 13438 -2721 1080 776 C
ATOM 2479 CG ASN A2014 0.496 121.885 151.411 1.00141.36 C
ANISOU 2479 CG ASN A2014 20558 14971 18183 -2699 1099 762 C
ATOM 2480 OD1 ASN A2014 1.707 121.995 151.111 1.00139.31 O
ANISOU 2480 OD1 ASN A2014 20370 14744 17818 -2597 888 753 O
ATOM 2481 ND2 ASN A2014 0.009 122.340 152.555 1.00135.67 N
ANISOU 2481 ND2 ASN A2014 19968 14195 17384 -2799 1364 760 N
ATOM 2482 N PRO A2015 -0.013 117.795 150.712 1.00100.10 N
ANISOU 2482 N PRO A2015 15463 9545 13023 -2897 760 895 N
ATOM 2483 CA PRO A2015 -0.605 116.579 151.312 1.00102.00 C
ANISOU 2483 CA PRO A2015 15834 9679 13244 -3050 814 955 C
ATOM 2484 C PRO A2015 -1.492 116.909 152.505 1.00110.42 C
ANISOU 2484 C PRO A2015 16979 10697 14281 -3189 1125 974 C
ATOM 2485 O PRO A2015 -2.565 116.337 152.679 1.00111.53 O
ANISOU 2485 O PRO A2015 17062 10776 14537 -3313 1269 1008 O
ATOM 2486 CB PRO A2015 0.624 115.773 151.748 1.00103.26 C
ANISOU 2486 CB PRO A2015 16260 9764 13210 -3037 619 994 C
ATOM 2487 CG PRO A2015 1.716 116.244 150.899 1.00105.73 C
ANISOU 2487 CG PRO A2015 16500 10141 13533 -2865 427 951 C
ATOM 2488 CD PRO A2015 1.464 117.701 150.682 1.00100.39 C
ANISOU 2488 CD PRO A2015 15654 9578 12912 -2794 550 893 C
ATOM 2489 N GLU A2016 -1.045 117.919 153.258 1.00109.44 N
ANISOU 2489 N GLU A2016 16976 10593 14013 -3166 1240 947 N
ATOM 2490 CA GLU A2016 -1.603 118.571 154.435 1.00112.02 C
ANISOU 2490 CA GLU A2016 17437 10870 14256 -3277 1563 939 C
ATOM 2491 C GLU A2016 -3.067 118.955 154.204 1.00118.15 C
ANISOU 2491 C GLU A2016 17926 11646 15320 -3320 1843 922 C
ATOM 2492 O GLU A2016 -3.870 118.781 155.114 1.00120.48 O
ANISOU 2492 O GLU A2016 18320 11843 15613 -3467 2137 939 O
ATOM 2493 CB GLU A2016 -0.739 119.810 154.754 1.00112.96 C
ANISOU 2493 CB GLU A2016 17655 11042 14224 -3189 1558 892 C
ATOM 2494 CG GLU A2016 0.761 119.499 154.768 1.00128.04 C
ANISOU 2494 CG GLU A2016 19764 12951 15935 -3121 1233 922 C
ATOM 2495 CD GLU A2016 1.764 120.641 154.746 1.00158.81 C
ANISOU 2495 CD GLU A2016 23695 16911 19732 -3007 1138 886 C
ATOM 2496 OE1 GLU A2016 1.708 121.509 155.649 1.00161.83 O
ANISOU 2496 OE1 GLU A2016 24245 17268 19976 -3071 1328 863 O
ATOM 2497 OE2 GLU A2016 2.660 120.620 153.869 1.00152.30 O
ANISOU 2497 OE2 GLU A2016 22763 16145 18959 -2866 877 883 O
ATOM 2498 N ASP A2017 -3.417 119.408 152.967 1.00113.72 N
ANISOU 2498 N ASP A2017 17013 11176 15021 -3204 1742 899 N
ATOM 2499 CA ASP A2017 -4.774 119.798 152.535 1.00114.63 C
ANISOU 2499 CA ASP A2017 16787 11285 15482 -3228 1929 905 C
ATOM 2500 C ASP A2017 -5.475 118.688 151.719 1.00118.19 C
ANISOU 2500 C ASP A2017 17058 11706 16142 -3289 1778 963 C
ATOM 2501 O ASP A2017 -6.685 118.489 151.851 1.00119.50 O
ANISOU 2501 O ASP A2017 17042 11802 16562 -3391 1972 1004 O
ATOM 2502 CB ASP A2017 -4.724 121.070 151.654 1.00115.30 C
ANISOU 2502 CB ASP A2017 16605 11473 15730 -3077 1869 861 C
ATOM 2503 CG ASP A2017 -3.998 122.278 152.220 1.00128.92 C
ANISOU 2503 CG ASP A2017 18468 13241 17276 -2996 1969 798 C
ATOM 2504 OD1 ASP A2017 -4.204 122.587 153.419 1.00132.42 O
ANISOU 2504 OD1 ASP A2017 19112 13607 17595 -3084 2260 782 O
ATOM 2505 OD2 ASP A2017 -3.297 122.975 151.436 1.00131.70 O
ANISOU 2505 OD2 ASP A2017 18725 13693 17621 -2855 1773 764 O
ATOM 2506 N GLY A2018 -4.709 118.041 150.839 1.00112.15 N
ANISOU 2506 N GLY A2018 16336 10986 15292 -3224 1439 965 N
ATOM 2507 CA GLY A2018 -5.182 117.031 149.903 1.00111.23 C
ANISOU 2507 CA GLY A2018 16092 10842 15329 -3272 1240 1008 C
ATOM 2508 C GLY A2018 -5.895 117.664 148.719 1.00113.30 C
ANISOU 2508 C GLY A2018 16010 11154 15884 -3225 1141 1013 C
ATOM 2509 O GLY A2018 -5.441 118.667 148.156 1.00111.45 O
ANISOU 2509 O GLY A2018 15692 11007 15648 -3098 1060 969 O
ATOM 2510 N ASP A2019 -7.001 117.043 148.319 1.00110.54 N
ANISOU 2510 N ASP A2019 15472 10739 15791 -3338 1121 1078 N
ATOM 2511 CA ASP A2019 -7.955 117.433 147.279 1.00110.38 C
ANISOU 2511 CA ASP A2019 15112 10720 16109 -3352 1008 1124 C
ATOM 2512 C ASP A2019 -9.220 116.667 147.678 1.00115.69 C
ANISOU 2512 C ASP A2019 15643 11274 17038 -3521 1149 1210 C
ATOM 2513 O ASP A2019 -9.610 115.753 146.956 1.00115.13 O
ANISOU 2513 O ASP A2019 15526 11155 17064 -3610 927 1262 O
ATOM 2514 CB ASP A2019 -7.448 117.008 145.883 1.00110.50 C
ANISOU 2514 CB ASP A2019 15158 10769 16057 -3314 624 1113 C
ATOM 2515 CG ASP A2019 -8.232 117.553 144.705 1.00117.64 C
ANISOU 2515 CG ASP A2019 15768 11678 17254 -3327 439 1162 C
ATOM 2516 OD1 ASP A2019 -9.243 118.263 144.934 1.00118.86 O
ANISOU 2516 OD1 ASP A2019 15634 11804 17724 -3357 598 1217 O
ATOM 2517 OD2 ASP A2019 -7.840 117.268 143.552 1.00122.14 O
ANISOU 2517 OD2 ASP A2019 16404 12261 17742 -3316 139 1149 O
ATOM 2518 N PRO A2020 -9.816 116.953 148.874 1.00114.80 N
ANISOU 2518 N PRO A2020 15504 11099 17014 -3581 1531 1221 N
ATOM 2519 CA PRO A2020 -10.942 116.134 149.353 1.00118.34 C
ANISOU 2519 CA PRO A2020 15847 11420 17694 -3751 1705 1300 C
ATOM 2520 C PRO A2020 -12.170 116.125 148.453 1.00127.38 C
ANISOU 2520 C PRO A2020 16590 12508 19302 -3820 1580 1397 C
ATOM 2521 O PRO A2020 -12.900 115.123 148.421 1.00128.64 O
ANISOU 2521 O PRO A2020 16688 12573 19617 -3964 1538 1473 O
ATOM 2522 CB PRO A2020 -11.235 116.702 150.744 1.00121.18 C
ANISOU 2522 CB PRO A2020 16270 11722 18051 -3783 2175 1274 C
ATOM 2523 CG PRO A2020 -10.655 118.059 150.733 1.00123.33 C
ANISOU 2523 CG PRO A2020 16527 12085 18247 -3629 2227 1201 C
ATOM 2524 CD PRO A2020 -9.451 117.974 149.879 1.00115.89 C
ANISOU 2524 CD PRO A2020 15748 11263 17024 -3513 1839 1157 C
ATOM 2525 N ASP A2021 -12.360 117.220 147.688 1.00125.70 N
ANISOU 2525 N ASP A2021 16112 12344 19304 -3725 1483 1403 N
ATOM 2526 CA ASP A2021 -13.451 117.378 146.730 1.00127.78 C
ANISOU 2526 CA ASP A2021 15981 12547 20023 -3783 1296 1511 C
ATOM 2527 C ASP A2021 -13.300 116.361 145.597 1.00130.50 C
ANISOU 2527 C ASP A2021 16410 12890 20282 -3856 851 1550 C
ATOM 2528 O ASP A2021 -14.306 115.971 145.001 1.00133.55 O
ANISOU 2528 O ASP A2021 16547 13182 21013 -3982 687 1663 O
ATOM 2529 CB ASP A2021 -13.524 118.827 146.204 1.00129.69 C
ANISOU 2529 CB ASP A2021 15977 12841 20458 -3655 1266 1506 C
ATOM 2530 CG ASP A2021 -14.101 119.807 147.215 1.00145.58 C
ANISOU 2530 CG ASP A2021 17802 14795 22716 -3620 1730 1497 C
ATOM 2531 OD1 ASP A2021 -13.310 120.497 147.890 1.00145.97 O
ANISOU 2531 OD1 ASP A2021 18065 14914 22484 -3514 1944 1391 O
ATOM 2532 OD2 ASP A2021 -15.345 119.863 147.349 1.00155.40 O
ANISOU 2532 OD2 ASP A2021 18694 15907 24444 -3707 1891 1596 O
ATOM 2533 N ASN A2022 -12.052 115.888 145.350 1.00122.46 N
ANISOU 2533 N ASN A2022 15755 11956 18818 -3790 670 1460 N
ATOM 2534 CA ASN A2022 -11.743 114.860 144.353 1.00120.75 C
ANISOU 2534 CA ASN A2022 15699 11722 18458 -3855 297 1470 C
ATOM 2535 C ASN A2022 -11.220 113.551 145.024 1.00121.14 C
ANISOU 2535 C ASN A2022 16074 11733 18222 -3914 359 1438 C
ATOM 2536 O ASN A2022 -10.389 112.838 144.455 1.00119.28 O
ANISOU 2536 O ASN A2022 16096 11507 17718 -3897 130 1390 O
ATOM 2537 CB ASN A2022 -10.815 115.398 143.241 1.00120.34 C
ANISOU 2537 CB ASN A2022 15761 11762 18199 -3737 10 1404 C
ATOM 2538 CG ASN A2022 -11.295 116.665 142.525 1.00146.78 C
ANISOU 2538 CG ASN A2022 18815 15141 21814 -3687 -88 1446 C
ATOM 2539 OD1 ASN A2022 -12.489 117.017 142.502 1.00140.05 O
ANISOU 2539 OD1 ASN A2022 17621 14213 21380 -3771 -73 1556 O
ATOM 2540 ND2 ASN A2022 -10.362 117.373 141.895 1.00137.59 N
ANISOU 2540 ND2 ASN A2022 17769 14075 20433 -3552 -201 1368 N
ATOM 2541 N GLY A2023 -11.750 113.258 146.219 1.00116.80 N
ANISOU 2541 N GLY A2023 15506 11120 17754 -3991 680 1469 N
ATOM 2542 CA GLY A2023 -11.481 112.054 147.002 1.00116.14 C
ANISOU 2542 CA GLY A2023 15698 10975 17456 -4076 770 1464 C
ATOM 2543 C GLY A2023 -10.101 111.839 147.596 1.00116.10 C
ANISOU 2543 C GLY A2023 16074 11025 17014 -3974 791 1374 C
ATOM 2544 O GLY A2023 -9.799 110.732 148.069 1.00116.42 O
ANISOU 2544 O GLY A2023 16358 11003 16873 -4043 771 1381 O
ATOM 2545 N VAL A2024 -9.273 112.894 147.613 1.00108.79 N
ANISOU 2545 N VAL A2024 15193 10203 15940 -3817 829 1300 N
ATOM 2546 CA VAL A2024 -7.908 112.880 148.150 1.00105.66 C
ANISOU 2546 CA VAL A2024 15121 9855 15172 -3711 829 1227 C
ATOM 2547 C VAL A2024 -7.914 113.591 149.497 1.00110.36 C
ANISOU 2547 C VAL A2024 15789 10453 15690 -3709 1175 1212 C
ATOM 2548 O VAL A2024 -7.399 114.692 149.607 1.00108.42 O
ANISOU 2548 O VAL A2024 15542 10288 15367 -3590 1236 1157 O
ATOM 2549 CB VAL A2024 -6.900 113.512 147.159 1.00106.14 C
ANISOU 2549 CB VAL A2024 15208 10016 15106 -3547 593 1156 C
ATOM 2550 CG1 VAL A2024 -5.468 113.202 147.557 1.00104.09 C
ANISOU 2550 CG1 VAL A2024 15263 9771 14516 -3453 538 1102 C
ATOM 2551 CG2 VAL A2024 -7.160 113.027 145.747 1.00105.94 C
ANISOU 2551 CG2 VAL A2024 15098 9968 15186 -3579 292 1170 C
ATOM 2552 N ASN A2025 -8.514 112.959 150.521 1.00109.96 N
ANISOU 2552 N ASN A2025 15825 10301 15653 -3854 1409 1259 N
ATOM 2553 CA ASN A2025 -8.653 113.504 151.878 1.00111.35 C
ANISOU 2553 CA ASN A2025 16128 10441 15739 -3899 1779 1247 C
ATOM 2554 C ASN A2025 -7.328 114.027 152.475 1.00113.80 C
ANISOU 2554 C ASN A2025 16741 10808 15688 -3796 1762 1184 C
ATOM 2555 O ASN A2025 -6.269 113.528 152.085 1.00112.04 O
ANISOU 2555 O ASN A2025 16689 10617 15263 -3723 1478 1169 O
ATOM 2556 CB ASN A2025 -9.330 112.484 152.794 1.00116.88 C
ANISOU 2556 CB ASN A2025 16964 11008 16438 -4088 1983 1308 C
ATOM 2557 CG ASN A2025 -10.794 112.316 152.463 1.00153.07 C
ANISOU 2557 CG ASN A2025 21200 15518 21442 -4200 2111 1375 C
ATOM 2558 OD1 ASN A2025 -11.202 111.358 151.791 1.00152.39 O
ANISOU 2558 OD1 ASN A2025 21020 15392 21490 -4271 1898 1432 O
ATOM 2559 ND2 ASN A2025 -11.609 113.289 152.863 1.00147.17 N
ANISOU 2559 ND2 ASN A2025 20238 14740 20941 -4214 2451 1374 N
ATOM 2560 N PRO A2026 -7.344 115.074 153.352 1.00110.87 N
ANISOU 2560 N PRO A2026 16432 10441 15254 -3787 2054 1146 N
ATOM 2561 CA PRO A2026 -6.074 115.614 153.877 1.00108.75 C
ANISOU 2561 CA PRO A2026 16452 10219 14650 -3702 1997 1097 C
ATOM 2562 C PRO A2026 -5.210 114.580 154.582 1.00110.60 C
ANISOU 2562 C PRO A2026 17073 10384 14567 -3774 1866 1132 C
ATOM 2563 O PRO A2026 -5.706 113.720 155.328 1.00111.01 O
ANISOU 2563 O PRO A2026 17282 10323 14573 -3936 2003 1184 O
ATOM 2564 CB PRO A2026 -6.507 116.744 154.816 1.00111.80 C
ANISOU 2564 CB PRO A2026 16866 10575 15037 -3736 2385 1059 C
ATOM 2565 CG PRO A2026 -7.877 117.079 154.412 1.00117.95 C
ANISOU 2565 CG PRO A2026 17261 11328 16227 -3765 2596 1075 C
ATOM 2566 CD PRO A2026 -8.497 115.826 153.888 1.00114.55 C
ANISOU 2566 CD PRO A2026 16711 10848 15965 -3856 2452 1147 C
ATOM 2567 N GLY A2027 -3.923 114.672 154.285 1.00104.46 N
ANISOU 2567 N GLY A2027 16425 9664 13601 -3651 1591 1112 N
ATOM 2568 CA GLY A2027 -2.888 113.786 154.788 1.00104.20 C
ANISOU 2568 CA GLY A2027 16720 9563 13309 -3680 1389 1156 C
ATOM 2569 C GLY A2027 -2.378 112.802 153.755 1.00106.03 C
ANISOU 2569 C GLY A2027 16883 9798 13606 -3603 1065 1172 C
ATOM 2570 O GLY A2027 -1.491 111.998 154.065 1.00106.31 O
ANISOU 2570 O GLY A2027 17152 9760 13480 -3611 878 1216 O
ATOM 2571 N THR A2028 -2.948 112.844 152.525 1.00 99.88 N
ANISOU 2571 N THR A2028 15797 9084 13070 -3540 996 1142 N
ATOM 2572 CA THR A2028 -2.568 111.949 151.434 1.00 97.56 C
ANISOU 2572 CA THR A2028 15453 8777 12837 -3481 720 1141 C
ATOM 2573 C THR A2028 -1.260 112.384 150.808 1.00 98.60 C
ANISOU 2573 C THR A2028 15606 8969 12888 -3302 512 1092 C
ATOM 2574 O THR A2028 -1.157 113.470 150.245 1.00 94.83 O
ANISOU 2574 O THR A2028 14963 8595 12472 -3195 519 1037 O
ATOM 2575 CB THR A2028 -3.691 111.756 150.405 1.00 99.14 C
ANISOU 2575 CB THR A2028 15376 8994 13299 -3523 706 1140 C
ATOM 2576 OG1 THR A2028 -4.891 111.393 151.070 1.00102.79 O
ANISOU 2576 OG1 THR A2028 15796 9387 13872 -3690 924 1195 O
ATOM 2577 CG2 THR A2028 -3.365 110.674 149.401 1.00 95.65 C
ANISOU 2577 CG2 THR A2028 14963 8503 12879 -3507 446 1139 C
ATOM 2578 N ASP A2029 -0.264 111.504 150.897 1.00 97.19 N
ANISOU 2578 N ASP A2029 15625 8709 12593 -3273 330 1118 N
ATOM 2579 CA ASP A2029 1.052 111.700 150.318 1.00 96.08 C
ANISOU 2579 CA ASP A2029 15508 8585 12413 -3108 138 1084 C
ATOM 2580 C ASP A2029 0.873 111.625 148.830 1.00 99.65 C
ANISOU 2580 C ASP A2029 15776 9075 13012 -3035 39 1022 C
ATOM 2581 O ASP A2029 -0.004 110.907 148.353 1.00 98.91 O
ANISOU 2581 O ASP A2029 15625 8940 13014 -3128 31 1031 O
ATOM 2582 CB ASP A2029 2.012 110.593 150.780 1.00 98.89 C
ANISOU 2582 CB ASP A2029 16096 8802 12677 -3114 -22 1146 C
ATOM 2583 CG ASP A2029 2.445 110.719 152.226 1.00115.58 C
ANISOU 2583 CG ASP A2029 18445 10861 14610 -3185 4 1220 C
ATOM 2584 OD1 ASP A2029 2.966 111.817 152.606 1.00115.05 O
ANISOU 2584 OD1 ASP A2029 18387 10862 14466 -3121 27 1203 O
ATOM 2585 OD2 ASP A2029 2.282 109.721 152.985 1.00124.27 O
ANISOU 2585 OD2 ASP A2029 19745 11840 15634 -3315 -12 1300 O
ATOM 2586 N PHE A2030 1.678 112.379 148.092 1.00 96.99 N
ANISOU 2586 N PHE A2030 15360 8807 12685 -2883 -38 960 N
ATOM 2587 CA PHE A2030 1.584 112.375 146.648 1.00 96.76 C
ANISOU 2587 CA PHE A2030 15205 8802 12758 -2826 -130 897 C
ATOM 2588 C PHE A2030 1.758 110.953 146.101 1.00103.84 C
ANISOU 2588 C PHE A2030 16218 9562 13673 -2860 -250 900 C
ATOM 2589 O PHE A2030 0.943 110.494 145.287 1.00104.98 O
ANISOU 2589 O PHE A2030 16307 9686 13896 -2936 -291 884 O
ATOM 2590 CB PHE A2030 2.589 113.346 146.068 1.00 96.94 C
ANISOU 2590 CB PHE A2030 15172 8896 12763 -2662 -175 834 C
ATOM 2591 CG PHE A2030 2.234 113.746 144.667 1.00 98.04 C
ANISOU 2591 CG PHE A2030 15178 9087 12985 -2632 -226 769 C
ATOM 2592 CD1 PHE A2030 1.132 114.554 144.417 1.00101.29 C
ANISOU 2592 CD1 PHE A2030 15409 9593 13485 -2686 -168 770 C
ATOM 2593 CD2 PHE A2030 2.999 113.317 143.592 1.00 99.81 C
ANISOU 2593 CD2 PHE A2030 15471 9246 13206 -2557 -330 711 C
ATOM 2594 CE1 PHE A2030 0.785 114.904 143.114 1.00101.91 C
ANISOU 2594 CE1 PHE A2030 15387 9702 13633 -2680 -258 728 C
ATOM 2595 CE2 PHE A2030 2.679 113.709 142.293 1.00102.33 C
ANISOU 2595 CE2 PHE A2030 15721 9599 13561 -2553 -384 653 C
ATOM 2596 CZ PHE A2030 1.556 114.474 142.063 1.00100.50 C
ANISOU 2596 CZ PHE A2030 15321 9461 13402 -2623 -371 669 C
ATOM 2597 N LYS A2031 2.735 110.212 146.679 1.00100.39 N
ANISOU 2597 N LYS A2031 15954 9016 13174 -2826 -311 937 N
ATOM 2598 CA LYS A2031 3.049 108.816 146.386 1.00100.38 C
ANISOU 2598 CA LYS A2031 16088 8857 13197 -2849 -409 951 C
ATOM 2599 C LYS A2031 1.827 107.916 146.563 1.00105.77 C
ANISOU 2599 C LYS A2031 16797 9489 13904 -3027 -382 995 C
ATOM 2600 O LYS A2031 1.876 106.766 146.135 1.00109.41 O
ANISOU 2600 O LYS A2031 17360 9820 14393 -3065 -461 996 O
ATOM 2601 CB LYS A2031 4.179 108.327 147.320 1.00102.83 C
ANISOU 2601 CB LYS A2031 16553 9055 13462 -2799 -477 1019 C
ATOM 2602 N ASP A2032 0.754 108.408 147.214 1.00 99.65 N
ANISOU 2602 N ASP A2032 15931 8797 13135 -3138 -258 1032 N
ATOM 2603 CA ASP A2032 -0.454 107.623 147.479 1.00100.10 C
ANISOU 2603 CA ASP A2032 15985 8801 13247 -3316 -206 1085 C
ATOM 2604 C ASP A2032 -1.690 108.046 146.674 1.00103.80 C
ANISOU 2604 C ASP A2032 16237 9341 13864 -3390 -180 1066 C
ATOM 2605 O ASP A2032 -2.776 107.521 146.913 1.00104.96 O
ANISOU 2605 O ASP A2032 16335 9446 14100 -3543 -127 1119 O
ATOM 2606 CB ASP A2032 -0.780 107.628 148.976 1.00102.53 C
ANISOU 2606 CB ASP A2032 16386 9095 13475 -3420 -58 1162 C
ATOM 2607 CG ASP A2032 0.261 107.001 149.874 1.00113.00 C
ANISOU 2607 CG ASP A2032 17958 10316 14662 -3402 -127 1217 C
ATOM 2608 OD1 ASP A2032 0.816 105.939 149.495 1.00112.12 O
ANISOU 2608 OD1 ASP A2032 17952 10083 14564 -3378 -274 1227 O
ATOM 2609 OD2 ASP A2032 0.475 107.532 150.990 1.00124.21 O
ANISOU 2609 OD2 ASP A2032 19479 11754 15962 -3430 -37 1259 O
ATOM 2610 N ILE A2033 -1.542 108.976 145.733 1.00 98.84 N
ANISOU 2610 N ILE A2033 15473 8804 13276 -3292 -228 1002 N
ATOM 2611 CA ILE A2033 -2.688 109.424 144.939 1.00 99.18 C
ANISOU 2611 CA ILE A2033 15305 8900 13479 -3367 -248 1003 C
ATOM 2612 C ILE A2033 -2.766 108.546 143.675 1.00106.45 C
ANISOU 2612 C ILE A2033 16296 9729 14421 -3419 -441 975 C
ATOM 2613 O ILE A2033 -1.713 108.334 143.069 1.00106.81 O
ANISOU 2613 O ILE A2033 16489 9734 14362 -3315 -524 908 O
ATOM 2614 CB ILE A2033 -2.584 110.945 144.581 1.00 99.96 C
ANISOU 2614 CB ILE A2033 15232 9135 13613 -3256 -214 960 C
ATOM 2615 CG1 ILE A2033 -2.100 111.798 145.752 1.00 97.69 C
ANISOU 2615 CG1 ILE A2033 14954 8920 13243 -3177 -42 963 C
ATOM 2616 CG2 ILE A2033 -3.914 111.462 144.070 1.00101.81 C
ANISOU 2616 CG2 ILE A2033 15217 9406 14059 -3353 -221 997 C
ATOM 2617 CD1 ILE A2033 -1.776 113.041 145.358 1.00 95.09 C
ANISOU 2617 CD1 ILE A2033 14504 8700 12927 -3063 -32 916 C
ATOM 2618 N PRO A2034 -3.954 108.061 143.211 1.00104.52 N
ANISOU 2618 N PRO A2034 15960 9436 14318 -3581 -513 1022 N
ATOM 2619 CA PRO A2034 -3.979 107.252 141.977 1.00105.44 C
ANISOU 2619 CA PRO A2034 16196 9449 14417 -3647 -713 990 C
ATOM 2620 C PRO A2034 -3.623 108.063 140.726 1.00111.74 C
ANISOU 2620 C PRO A2034 16981 10295 15179 -3572 -831 918 C
ATOM 2621 O PRO A2034 -3.619 109.293 140.773 1.00111.20 O
ANISOU 2621 O PRO A2034 16751 10351 15151 -3488 -776 912 O
ATOM 2622 CB PRO A2034 -5.421 106.747 141.914 1.00108.63 C
ANISOU 2622 CB PRO A2034 16469 9798 15005 -3851 -771 1079 C
ATOM 2623 CG PRO A2034 -5.981 106.982 143.255 1.00113.16 C
ANISOU 2623 CG PRO A2034 16881 10425 15689 -3883 -561 1152 C
ATOM 2624 CD PRO A2034 -5.310 108.193 143.768 1.00107.07 C
ANISOU 2624 CD PRO A2034 16073 9774 14835 -3719 -414 1110 C
ATOM 2625 N ASP A2035 -3.308 107.374 139.614 1.00110.31 N
ANISOU 2625 N ASP A2035 16999 10004 14912 -3610 -981 862 N
ATOM 2626 CA ASP A2035 -2.971 107.992 138.324 1.00110.09 C
ANISOU 2626 CA ASP A2035 17033 9984 14814 -3576 -1097 789 C
ATOM 2627 C ASP A2035 -4.181 108.728 137.774 1.00113.59 C
ANISOU 2627 C ASP A2035 17270 10482 15409 -3701 -1235 859 C
ATOM 2628 O ASP A2035 -4.016 109.792 137.184 1.00112.57 O
ANISOU 2628 O ASP A2035 17075 10429 15267 -3640 -1279 832 O
ATOM 2629 CB ASP A2035 -2.526 106.933 137.300 1.00113.96 C
ANISOU 2629 CB ASP A2035 17827 10301 15171 -3635 -1202 716 C
ATOM 2630 CG ASP A2035 -1.819 105.728 137.897 1.00132.36 C
ANISOU 2630 CG ASP A2035 20337 12513 17441 -3587 -1107 692 C
ATOM 2631 OD1 ASP A2035 -2.417 104.623 137.893 1.00135.65 O
ANISOU 2631 OD1 ASP A2035 20844 12811 17884 -3732 -1175 731 O
ATOM 2632 OD2 ASP A2035 -0.680 105.892 138.389 1.00139.00 O
ANISOU 2632 OD2 ASP A2035 21217 13370 18228 -3411 -979 646 O
ATOM 2633 N ASP A2036 -5.403 108.188 138.009 1.00111.50 N
ANISOU 2633 N ASP A2036 16883 10168 15314 -3875 -1304 959 N
ATOM 2634 CA ASP A2036 -6.646 108.801 137.549 1.00112.69 C
ANISOU 2634 CA ASP A2036 16793 10340 15683 -4008 -1455 1054 C
ATOM 2635 C ASP A2036 -7.030 110.037 138.379 1.00115.56 C
ANISOU 2635 C ASP A2036 16831 10846 16231 -3919 -1289 1106 C
ATOM 2636 O ASP A2036 -8.210 110.387 138.489 1.00117.49 O
ANISOU 2636 O ASP A2036 16802 11091 16749 -4026 -1327 1213 O
ATOM 2637 CB ASP A2036 -7.805 107.780 137.416 1.00117.33 C
ANISOU 2637 CB ASP A2036 17353 10801 16426 -4236 -1605 1151 C
ATOM 2638 CG ASP A2036 -8.178 106.923 138.615 1.00129.96 C
ANISOU 2638 CG ASP A2036 18900 12366 18114 -4283 -1438 1206 C
ATOM 2639 OD1 ASP A2036 -8.961 105.958 138.431 1.00130.50 O
ANISOU 2639 OD1 ASP A2036 18991 12314 18278 -4468 -1565 1273 O
ATOM 2640 OD2 ASP A2036 -7.721 107.234 139.740 1.00137.01 O
ANISOU 2640 OD2 ASP A2036 19737 13342 18977 -4153 -1188 1189 O
ATOM 2641 N TRP A2037 -6.010 110.712 138.933 1.00108.52 N
ANISOU 2641 N TRP A2037 15969 10058 15205 -3725 -1106 1031 N
ATOM 2642 CA TRP A2037 -6.131 111.968 139.648 1.00106.59 C
ANISOU 2642 CA TRP A2037 15484 9942 15074 -3620 -935 1051 C
ATOM 2643 C TRP A2037 -5.363 112.974 138.842 1.00109.09 C
ANISOU 2643 C TRP A2037 15839 10334 15275 -3494 -1002 978 C
ATOM 2644 O TRP A2037 -4.200 112.758 138.460 1.00106.58 O
ANISOU 2644 O TRP A2037 15760 10005 14732 -3397 -1011 884 O
ATOM 2645 CB TRP A2037 -5.601 111.906 141.086 1.00104.05 C
ANISOU 2645 CB TRP A2037 15195 9663 14676 -3527 -666 1035 C
ATOM 2646 CG TRP A2037 -5.618 113.231 141.807 1.00103.79 C
ANISOU 2646 CG TRP A2037 14972 9747 14715 -3421 -475 1037 C
ATOM 2647 CD1 TRP A2037 -6.612 113.715 142.606 1.00107.70 C
ANISOU 2647 CD1 TRP A2037 15230 10260 15432 -3475 -299 1107 C
ATOM 2648 CD2 TRP A2037 -4.587 114.238 141.792 1.00101.43 C
ANISOU 2648 CD2 TRP A2037 14717 9549 14274 -3247 -420 961 C
ATOM 2649 NE1 TRP A2037 -6.267 114.960 143.093 1.00105.91 N
ANISOU 2649 NE1 TRP A2037 14915 10132 15192 -3346 -135 1073 N
ATOM 2650 CE2 TRP A2037 -5.033 115.307 142.603 1.00105.24 C
ANISOU 2650 CE2 TRP A2037 14997 10107 14884 -3208 -223 988 C
ATOM 2651 CE3 TRP A2037 -3.337 114.350 141.153 1.00100.56 C
ANISOU 2651 CE3 TRP A2037 14791 9457 13958 -3123 -505 874 C
ATOM 2652 CZ2 TRP A2037 -4.268 116.456 142.808 1.00102.67 C
ANISOU 2652 CZ2 TRP A2037 14663 9880 14465 -3057 -135 931 C
ATOM 2653 CZ3 TRP A2037 -2.570 115.474 141.380 1.00100.06 C
ANISOU 2653 CZ3 TRP A2037 14700 9496 13823 -2972 -415 825 C
ATOM 2654 CH2 TRP A2037 -3.040 116.517 142.187 1.00100.77 C
ANISOU 2654 CH2 TRP A2037 14599 9666 14023 -2943 -247 855 C
ATOM 2655 N VAL A2038 -6.033 114.091 138.622 1.00107.21 N
ANISOU 2655 N VAL A2038 15351 10161 15221 -3494 -1032 1029 N
ATOM 2656 CA VAL A2038 -5.577 115.231 137.848 1.00106.45 C
ANISOU 2656 CA VAL A2038 15237 10139 15071 -3398 -1109 986 C
ATOM 2657 C VAL A2038 -5.515 116.478 138.713 1.00110.33 C
ANISOU 2657 C VAL A2038 15513 10750 15655 -3263 -897 988 C
ATOM 2658 O VAL A2038 -6.239 116.581 139.715 1.00110.74 O
ANISOU 2658 O VAL A2038 15375 10811 15892 -3290 -723 1047 O
ATOM 2659 CB VAL A2038 -6.505 115.444 136.629 1.00112.08 C
ANISOU 2659 CB VAL A2038 15865 10791 15931 -3546 -1401 1062 C
ATOM 2660 CG1 VAL A2038 -6.148 114.487 135.496 1.00112.61 C
ANISOU 2660 CG1 VAL A2038 16258 10742 15786 -3651 -1619 1015 C
ATOM 2661 CG2 VAL A2038 -7.974 115.294 137.026 1.00114.00 C
ANISOU 2661 CG2 VAL A2038 15811 10982 16523 -3692 -1433 1201 C
ATOM 2662 N CYS A2039 -4.663 117.437 138.294 1.00105.90 N
ANISOU 2662 N CYS A2039 14997 10269 14969 -3128 -900 920 N
ATOM 2663 CA CYS A2039 -4.456 118.735 138.918 1.00104.66 C
ANISOU 2663 CA CYS A2039 14676 10224 14867 -2995 -727 906 C
ATOM 2664 C CYS A2039 -5.786 119.470 139.051 1.00109.02 C
ANISOU 2664 C CYS A2039 14894 10775 15754 -3063 -716 1010 C
ATOM 2665 O CYS A2039 -6.447 119.703 138.045 1.00109.51 O
ANISOU 2665 O CYS A2039 14854 10796 15961 -3151 -946 1072 O
ATOM 2666 CB CYS A2039 -3.457 119.545 138.106 1.00104.11 C
ANISOU 2666 CB CYS A2039 14712 10214 14630 -2876 -801 830 C
ATOM 2667 SG CYS A2039 -3.395 121.293 138.557 1.00107.61 S
ANISOU 2667 SG CYS A2039 14934 10781 15171 -2735 -651 825 S
ATOM 2668 N PRO A2040 -6.223 119.822 140.270 1.00106.68 N
ANISOU 2668 N PRO A2040 14431 10500 15602 -3039 -454 1036 N
ATOM 2669 CA PRO A2040 -7.526 120.499 140.407 1.00109.06 C
ANISOU 2669 CA PRO A2040 14385 10771 16283 -3100 -404 1137 C
ATOM 2670 C PRO A2040 -7.566 121.932 139.871 1.00115.56 C
ANISOU 2670 C PRO A2040 15029 11651 17229 -3012 -455 1145 C
ATOM 2671 O PRO A2040 -8.644 122.523 139.786 1.00117.60 O
ANISOU 2671 O PRO A2040 14977 11863 17845 -3058 -457 1240 O
ATOM 2672 CB PRO A2040 -7.828 120.416 141.902 1.00111.28 C
ANISOU 2672 CB PRO A2040 14610 11040 16631 -3097 -52 1138 C
ATOM 2673 CG PRO A2040 -6.515 120.257 142.546 1.00113.65 C
ANISOU 2673 CG PRO A2040 15204 11406 16570 -2989 66 1033 C
ATOM 2674 CD PRO A2040 -5.581 119.602 141.577 1.00107.69 C
ANISOU 2674 CD PRO A2040 14693 10658 15565 -2969 -188 982 C
ATOM 2675 N LEU A2041 -6.402 122.484 139.491 1.00111.19 N
ANISOU 2675 N LEU A2041 14658 11183 16407 -2886 -499 1053 N
ATOM 2676 CA LEU A2041 -6.335 123.813 138.903 1.00110.68 C
ANISOU 2676 CA LEU A2041 14466 11172 16416 -2803 -570 1055 C
ATOM 2677 C LEU A2041 -6.350 123.701 137.363 1.00116.15 C
ANISOU 2677 C LEU A2041 15242 11825 17064 -2882 -934 1086 C
ATOM 2678 O LEU A2041 -7.374 124.051 136.767 1.00118.13 O
ANISOU 2678 O LEU A2041 15271 12011 17601 -2979 -1116 1198 O
ATOM 2679 CB LEU A2041 -5.154 124.646 139.446 1.00108.34 C
ANISOU 2679 CB LEU A2041 14296 10982 15885 -2630 -387 947 C
ATOM 2680 N CYS A2042 -5.286 123.127 136.728 1.00111.42 N
ANISOU 2680 N CYS A2042 14968 11238 16130 -2863 -1041 997 N
ATOM 2681 CA CYS A2042 -5.196 123.036 135.260 1.00111.95 C
ANISOU 2681 CA CYS A2042 15189 11250 16096 -2952 -1353 1008 C
ATOM 2682 C CYS A2042 -5.763 121.756 134.628 1.00117.63 C
ANISOU 2682 C CYS A2042 16034 11845 16813 -3143 -1571 1059 C
ATOM 2683 O CYS A2042 -6.071 121.786 133.434 1.00119.33 O
ANISOU 2683 O CYS A2042 16323 11988 17029 -3268 -1864 1110 O
ATOM 2684 CB CYS A2042 -3.775 123.289 134.775 1.00110.64 C
ANISOU 2684 CB CYS A2042 15301 11136 15599 -2838 -1330 884 C
ATOM 2685 SG CYS A2042 -2.685 121.854 134.882 1.00113.87 S
ANISOU 2685 SG CYS A2042 16062 11500 15706 -2823 -1243 774 S
ATOM 2686 N GLY A2043 -5.837 120.655 135.376 1.00113.20 N
ANISOU 2686 N GLY A2043 15537 11252 16223 -3174 -1445 1043 N
ATOM 2687 CA GLY A2043 -6.388 119.401 134.866 1.00113.76 C
ANISOU 2687 CA GLY A2043 15729 11199 16297 -3357 -1633 1089 C
ATOM 2688 C GLY A2043 -5.420 118.385 134.294 1.00115.40 C
ANISOU 2688 C GLY A2043 16329 11347 16169 -3375 -1680 984 C
ATOM 2689 O GLY A2043 -5.859 117.343 133.812 1.00115.17 O
ANISOU 2689 O GLY A2043 16436 11202 16122 -3537 -1847 1015 O
ATOM 2690 N VAL A2044 -4.105 118.662 134.330 1.00110.98 N
ANISOU 2690 N VAL A2044 15953 10849 15363 -3214 -1530 862 N
ATOM 2691 CA VAL A2044 -3.108 117.705 133.822 1.00110.72 C
ANISOU 2691 CA VAL A2044 16279 10739 15052 -3210 -1524 755 C
ATOM 2692 C VAL A2044 -2.891 116.572 134.839 1.00115.49 C
ANISOU 2692 C VAL A2044 16935 11310 15637 -3191 -1363 737 C
ATOM 2693 O VAL A2044 -3.122 116.763 136.038 1.00115.00 O
ANISOU 2693 O VAL A2044 16677 11320 15699 -3126 -1193 772 O
ATOM 2694 CB VAL A2044 -1.764 118.336 133.350 1.00112.45 C
ANISOU 2694 CB VAL A2044 16674 11000 15053 -3059 -1431 640 C
ATOM 2695 CG1 VAL A2044 -1.989 119.446 132.327 1.00112.54 C
ANISOU 2695 CG1 VAL A2044 16671 11030 15058 -3096 -1602 662 C
ATOM 2696 CG2 VAL A2044 -0.926 118.826 134.524 1.00110.18 C
ANISOU 2696 CG2 VAL A2044 16267 10827 14768 -2857 -1174 597 C
ATOM 2697 N GLY A2045 -2.411 115.433 134.351 1.00112.41 N
ANISOU 2697 N GLY A2045 16832 10798 15080 -3248 -1406 677 N
ATOM 2698 CA GLY A2045 -2.148 114.262 135.176 1.00112.18 C
ANISOU 2698 CA GLY A2045 16890 10709 15022 -3240 -1285 661 C
ATOM 2699 C GLY A2045 -1.001 114.367 136.160 1.00113.52 C
ANISOU 2699 C GLY A2045 17074 10939 15121 -3048 -1055 602 C
ATOM 2700 O GLY A2045 -0.221 115.325 136.145 1.00110.40 O
ANISOU 2700 O GLY A2045 16651 10626 14671 -2905 -975 553 O
ATOM 2701 N LYS A2046 -0.897 113.338 137.019 1.00111.99 N
ANISOU 2701 N LYS A2046 16932 10689 14931 -3056 -969 617 N
ATOM 2702 CA LYS A2046 0.145 113.169 138.039 1.00111.18 C
ANISOU 2702 CA LYS A2046 16869 10603 14772 -2908 -798 588 C
ATOM 2703 C LYS A2046 1.568 113.125 137.434 1.00117.27 C
ANISOU 2703 C LYS A2046 17828 11319 15411 -2773 -754 486 C
ATOM 2704 O LYS A2046 2.544 113.434 138.126 1.00116.21 O
ANISOU 2704 O LYS A2046 17673 11221 15262 -2626 -640 470 O
ATOM 2705 CB LYS A2046 -0.124 111.894 138.855 1.00112.76 C
ANISOU 2705 CB LYS A2046 17135 10712 14995 -2985 -767 634 C
ATOM 2706 CG LYS A2046 -0.982 112.130 140.082 1.00101.99 C
ANISOU 2706 CG LYS A2046 15580 9424 13746 -3030 -671 724 C
ATOM 2707 CD LYS A2046 -0.866 111.010 141.108 1.00102.14 C
ANISOU 2707 CD LYS A2046 15706 9360 13742 -3068 -603 762 C
ATOM 2708 CE LYS A2046 0.486 110.918 141.777 1.00 99.00 C
ANISOU 2708 CE LYS A2046 15433 8944 13237 -2923 -526 733 C
ATOM 2709 NZ LYS A2046 0.630 109.673 142.567 1.00104.88 N
ANISOU 2709 NZ LYS A2046 16320 9573 13959 -2977 -513 777 N
ATOM 2710 N ASP A2047 1.672 112.723 136.149 1.00116.04 N
ANISOU 2710 N ASP A2047 17863 11056 15170 -2834 -840 422 N
ATOM 2711 CA ASP A2047 2.924 112.639 135.402 1.00116.08 C
ANISOU 2711 CA ASP A2047 18063 10974 15068 -2727 -765 316 C
ATOM 2712 C ASP A2047 3.575 114.046 135.214 1.00119.24 C
ANISOU 2712 C ASP A2047 18357 11495 15452 -2590 -702 282 C
ATOM 2713 O ASP A2047 4.802 114.143 135.198 1.00119.62 O
ANISOU 2713 O ASP A2047 18466 11506 15478 -2445 -579 220 O
ATOM 2714 CB ASP A2047 2.712 111.883 134.061 1.00119.62 C
ANISOU 2714 CB ASP A2047 18784 11261 15406 -2866 -857 254 C
ATOM 2715 CG ASP A2047 1.779 112.560 133.060 1.00134.20 C
ANISOU 2715 CG ASP A2047 20632 13147 17212 -3013 -1038 277 C
ATOM 2716 OD1 ASP A2047 2.261 113.406 132.273 1.00136.60 O
ANISOU 2716 OD1 ASP A2047 20992 13477 17431 -2967 -1028 223 O
ATOM 2717 OD2 ASP A2047 0.581 112.215 133.036 1.00139.22 O
ANISOU 2717 OD2 ASP A2047 21217 13770 17911 -3182 -1201 357 O
ATOM 2718 N GLN A2048 2.755 115.125 135.146 1.00113.50 N
ANISOU 2718 N GLN A2048 17453 10904 14768 -2632 -783 332 N
ATOM 2719 CA GLN A2048 3.204 116.514 134.970 1.00111.35 C
ANISOU 2719 CA GLN A2048 17070 10751 14488 -2520 -743 310 C
ATOM 2720 C GLN A2048 3.529 117.234 136.302 1.00112.75 C
ANISOU 2720 C GLN A2048 17037 11057 14745 -2388 -627 350 C
ATOM 2721 O GLN A2048 3.686 118.465 136.315 1.00110.88 O
ANISOU 2721 O GLN A2048 16677 10932 14522 -2309 -601 347 O
ATOM 2722 CB GLN A2048 2.159 117.325 134.179 1.00113.38 C
ANISOU 2722 CB GLN A2048 17247 11065 14768 -2636 -903 352 C
ATOM 2723 CG GLN A2048 1.857 116.840 132.756 1.00142.98 C
ANISOU 2723 CG GLN A2048 21242 14683 18400 -2792 -1058 319 C
ATOM 2724 CD GLN A2048 2.990 117.045 131.769 1.00175.10 C
ANISOU 2724 CD GLN A2048 25552 18678 22300 -2728 -978 206 C
ATOM 2725 OE1 GLN A2048 3.453 118.170 131.507 1.00168.66 O
ANISOU 2725 OE1 GLN A2048 24679 17945 21460 -2640 -940 183 O
ATOM 2726 NE2 GLN A2048 3.431 115.952 131.162 1.00175.51 N
ANISOU 2726 NE2 GLN A2048 25891 18558 22237 -2781 -938 131 N
ATOM 2727 N PHE A2049 3.619 116.474 137.421 1.00108.19 N
ANISOU 2727 N PHE A2049 16446 10453 14208 -2377 -566 391 N
ATOM 2728 CA PHE A2049 3.912 117.018 138.750 1.00105.64 C
ANISOU 2728 CA PHE A2049 15991 10222 13924 -2288 -468 434 C
ATOM 2729 C PHE A2049 5.336 116.741 139.149 1.00111.64 C
ANISOU 2729 C PHE A2049 16841 10921 14654 -2153 -400 404 C
ATOM 2730 O PHE A2049 5.800 115.604 139.021 1.00111.87 O
ANISOU 2730 O PHE A2049 17013 10814 14680 -2158 -404 390 O
ATOM 2731 CB PHE A2049 2.967 116.437 139.790 1.00106.78 C
ANISOU 2731 CB PHE A2049 16076 10366 14128 -2393 -451 514 C
ATOM 2732 CG PHE A2049 1.693 117.211 139.989 1.00107.39 C
ANISOU 2732 CG PHE A2049 15957 10539 14309 -2475 -448 569 C
ATOM 2733 CD1 PHE A2049 0.666 117.143 139.056 1.00110.53 C
ANISOU 2733 CD1 PHE A2049 16300 10916 14780 -2596 -569 590 C
ATOM 2734 CD2 PHE A2049 1.495 117.969 141.135 1.00108.75 C
ANISOU 2734 CD2 PHE A2049 16004 10797 14520 -2444 -323 607 C
ATOM 2735 CE1 PHE A2049 -0.520 117.850 139.248 1.00111.98 C
ANISOU 2735 CE1 PHE A2049 16261 11164 15124 -2667 -568 656 C
ATOM 2736 CE2 PHE A2049 0.309 118.681 141.326 1.00111.99 C
ANISOU 2736 CE2 PHE A2049 16214 11269 15069 -2512 -280 655 C
ATOM 2737 CZ PHE A2049 -0.694 118.612 140.385 1.00110.96 C
ANISOU 2737 CZ PHE A2049 15985 11114 15059 -2617 -404 685 C
ATOM 2738 N GLU A2050 6.035 117.795 139.621 1.00109.41 N
ANISOU 2738 N GLU A2050 16469 10727 14374 -2035 -346 402 N
ATOM 2739 CA GLU A2050 7.435 117.750 140.058 1.00109.35 C
ANISOU 2739 CA GLU A2050 16503 10665 14381 -1902 -306 394 C
ATOM 2740 C GLU A2050 7.543 117.937 141.563 1.00114.11 C
ANISOU 2740 C GLU A2050 17064 11309 14985 -1894 -294 473 C
ATOM 2741 O GLU A2050 6.776 118.712 142.138 1.00113.21 O
ANISOU 2741 O GLU A2050 16858 11308 14848 -1939 -262 502 O
ATOM 2742 N GLU A2051 8.490 117.235 142.201 1.00112.47 N
ANISOU 2742 N GLU A2051 16935 10990 14809 -1846 -318 512 N
ATOM 2743 CA GLU A2051 8.685 117.351 143.640 1.00113.45 C
ANISOU 2743 CA GLU A2051 17076 11124 14905 -1861 -338 597 C
ATOM 2744 C GLU A2051 9.298 118.690 143.988 1.00119.55 C
ANISOU 2744 C GLU A2051 17769 11993 15663 -1775 -326 597 C
ATOM 2745 O GLU A2051 10.241 119.119 143.322 1.00119.83 O
ANISOU 2745 O GLU A2051 17756 12015 15761 -1659 -329 555 O
ATOM 2746 CB GLU A2051 9.572 116.227 144.164 1.00115.80 C
ANISOU 2746 CB GLU A2051 17481 11255 15262 -1839 -412 657 C
ATOM 2747 CG GLU A2051 9.507 116.092 145.673 1.00127.34 C
ANISOU 2747 CG GLU A2051 19025 12704 16656 -1914 -462 761 C
ATOM 2748 CD GLU A2051 10.702 115.390 146.277 1.00147.24 C
ANISOU 2748 CD GLU A2051 21624 15061 19258 -1867 -585 844 C
ATOM 2749 OE1 GLU A2051 10.814 114.151 146.123 1.00128.67 O
ANISOU 2749 OE1 GLU A2051 19346 12568 16975 -1888 -625 867 O
ATOM 2750 OE2 GLU A2051 11.528 116.087 146.911 1.00143.06 O
ANISOU 2750 OE2 GLU A2051 21083 14534 18739 -1815 -656 896 O
ATOM 2751 N VAL A2052 8.775 119.351 145.027 1.00117.07 N
ANISOU 2751 N VAL A2052 17452 11763 15267 -1837 -294 640 N
ATOM 2752 CA VAL A2052 9.345 120.626 145.452 1.00116.54 C
ANISOU 2752 CA VAL A2052 17334 11775 15170 -1769 -285 641 C
ATOM 2753 C VAL A2052 10.560 120.365 146.351 1.00121.73 C
ANISOU 2753 C VAL A2052 18086 12330 15835 -1735 -398 719 C
ATOM 2754 O VAL A2052 10.414 119.923 147.499 1.00122.54 O
ANISOU 2754 O VAL A2052 18323 12378 15857 -1832 -437 797 O
ATOM 2755 CB VAL A2052 8.338 121.637 146.048 1.00120.29 C
ANISOU 2755 CB VAL A2052 17768 12371 15565 -1840 -176 636 C
ATOM 2756 CG1 VAL A2052 9.010 122.992 146.219 1.00119.20 C
ANISOU 2756 CG1 VAL A2052 17577 12309 15404 -1756 -169 619 C
ATOM 2757 CG2 VAL A2052 7.102 121.772 145.159 1.00120.00 C
ANISOU 2757 CG2 VAL A2052 17612 12404 15580 -1884 -103 586 C
ATOM 2758 N GLU A2053 11.759 120.596 145.787 1.00117.87 N
ANISOU 2758 N GLU A2053 17530 11796 15458 -1607 -456 707 N
ATOM 2759 CA GLU A2053 13.036 120.363 146.453 1.00118.54 C
ANISOU 2759 CA GLU A2053 17656 11760 15625 -1559 -595 795 C
ATOM 2760 C GLU A2053 13.488 121.573 147.233 1.00121.10 C
ANISOU 2760 C GLU A2053 17982 12147 15882 -1555 -645 833 C
ATOM 2761 O GLU A2053 13.401 122.686 146.725 1.00120.04 O
ANISOU 2761 O GLU A2053 17748 12132 15729 -1500 -566 765 O
ATOM 2762 CB GLU A2053 14.115 119.957 145.434 1.00120.43 C
ANISOU 2762 CB GLU A2053 17800 11886 16072 -1423 -608 768 C
ATOM 2763 CG GLU A2053 13.889 118.596 144.783 1.00136.19 C
ANISOU 2763 CG GLU A2053 19842 13762 18141 -1433 -575 742 C
ATOM 2764 CD GLU A2053 14.218 117.343 145.581 1.00162.83 C
ANISOU 2764 CD GLU A2053 23318 16968 21583 -1479 -696 848 C
ATOM 2765 OE1 GLU A2053 14.490 117.445 146.800 1.00158.65 O
ANISOU 2765 OE1 GLU A2053 22859 16413 21010 -1535 -831 958 O
ATOM 2766 OE2 GLU A2053 14.192 116.246 144.974 1.00157.72 O1-
ANISOU 2766 OE2 GLU A2053 22702 16200 21025 -1470 -663 822 O1-
ATOM 2767 N GLU A2054 13.973 121.358 148.467 1.00117.94 N
ANISOU 2767 N GLU A2054 17717 11657 15438 -1624 -791 946 N
ATOM 2768 CA GLU A2054 14.486 122.423 149.330 1.00117.38 C
ANISOU 2768 CA GLU A2054 17701 11612 15285 -1647 -875 998 C
ATOM 2769 C GLU A2054 15.924 122.749 148.945 1.00119.27 C
ANISOU 2769 C GLU A2054 17805 11777 15735 -1515 -1003 1035 C
ATOM 2770 O GLU A2054 16.793 121.874 148.974 1.00119.10 O
ANISOU 2770 O GLU A2054 17761 11593 15898 -1474 -1139 1115 O
ATOM 2771 CB GLU A2054 14.423 122.014 150.807 1.00120.68 C
ANISOU 2771 CB GLU A2054 18368 11938 15549 -1805 -1002 1115 C
ATOM 2772 CG GLU A2054 13.092 122.277 151.489 1.00133.55 C
ANISOU 2772 CG GLU A2054 20153 13652 16937 -1952 -836 1078 C
ATOM 2773 CD GLU A2054 13.105 122.041 152.989 1.00160.10 C
ANISOU 2773 CD GLU A2054 23816 16912 20103 -2128 -942 1187 C
ATOM 2774 OE1 GLU A2054 14.080 122.466 153.656 1.00147.34 O
ANISOU 2774 OE1 GLU A2054 22299 15220 18463 -2149 -1139 1275 O
ATOM 2775 OE2 GLU A2054 12.129 121.444 153.500 1.00160.52 O1-
ANISOU 2775 OE2 GLU A2054 24018 16950 20023 -2258 -830 1190 O1-
ATOM 2776 N ARG A 237 16.166 124.007 148.561 1.00114.64 N
ANISOU 2776 N ARG A 237 17113 11297 15150 -1445 -949 978 N
ATOM 2777 CA ARG A 237 17.492 124.482 148.157 1.00114.18 C
ANISOU 2777 CA ARG A 237 16905 11178 15300 -1322 -1042 1008 C
ATOM 2778 C ARG A 237 17.891 125.694 148.995 1.00117.15 C
ANISOU 2778 C ARG A 237 17338 11597 15575 -1367 -1145 1057 C
ATOM 2779 O ARG A 237 17.122 126.657 149.107 1.00115.91 O
ANISOU 2779 O ARG A 237 17227 11583 15229 -1410 -1023 984 O
ATOM 2780 CB ARG A 237 17.541 124.832 146.652 1.00113.09 C
ANISOU 2780 CB ARG A 237 16579 11112 15279 -1188 -865 883 C
ATOM 2781 CG ARG A 237 17.156 123.696 145.708 1.00124.39 C
ANISOU 2781 CG ARG A 237 17985 12486 16789 -1155 -754 822 C
ATOM 2782 CD ARG A 237 16.662 124.192 144.355 1.00135.97 C
ANISOU 2782 CD ARG A 237 19369 14065 18228 -1098 -565 685 C
ATOM 2783 NE ARG A 237 15.839 123.182 143.679 1.00151.03 N
ANISOU 2783 NE ARG A 237 21332 15950 20103 -1135 -474 624 N
ATOM 2784 CZ ARG A 237 14.522 123.276 143.508 1.00168.79 C
ANISOU 2784 CZ ARG A 237 23628 18316 22188 -1222 -401 570 C
ATOM 2785 NH1 ARG A 237 13.865 124.350 143.932 1.00160.99 N
ANISOU 2785 NH1 ARG A 237 22628 17473 21069 -1267 -378 561 N
ATOM 2786 NH2 ARG A 237 13.855 122.302 142.900 1.00150.95 N
ANISOU 2786 NH2 ARG A 237 21423 16015 19917 -1266 -350 529 N
ATOM 2787 N ASP A 238 19.101 125.644 149.576 1.00113.98 N
ANISOU 2787 N ASP A 238 16932 11054 15320 -1360 -1378 1185 N
ATOM 2788 CA ASP A 238 19.663 126.743 150.358 1.00113.81 C
ANISOU 2788 CA ASP A 238 16976 11041 15226 -1412 -1523 1249 C
ATOM 2789 C ASP A 238 19.978 127.908 149.412 1.00112.81 C
ANISOU 2789 C ASP A 238 16651 11028 15185 -1286 -1397 1154 C
ATOM 2790 O ASP A 238 20.024 129.056 149.854 1.00111.92 O
ANISOU 2790 O ASP A 238 16596 10983 14945 -1328 -1425 1150 O
ATOM 2791 CB ASP A 238 20.944 126.300 151.095 1.00118.48 C
ANISOU 2791 CB ASP A 238 17583 11424 16010 -1439 -1846 1432 C
ATOM 2792 CG ASP A 238 20.775 125.287 152.215 1.00135.40 C
ANISOU 2792 CG ASP A 238 19968 13432 18047 -1593 -2036 1559 C
ATOM 2793 OD1 ASP A 238 19.639 124.782 152.401 1.00136.92 O
ANISOU 2793 OD1 ASP A 238 20313 13688 18023 -1674 -1887 1497 O
ATOM 2794 OD2 ASP A 238 21.783 124.987 152.900 1.00143.70 O1-
ANISOU 2794 OD2 ASP A 238 21052 14301 19244 -1638 -2344 1730 O1-
ATOM 2795 N SER A 239 20.183 127.603 148.109 1.00105.93 N
ANISOU 2795 N SER A 239 15572 10163 14515 -1143 -1251 1074 N
ATOM 2796 CA SER A 239 20.447 128.591 147.071 1.00103.51 C
ANISOU 2796 CA SER A 239 15091 9951 14288 -1028 -1109 979 C
ATOM 2797 C SER A 239 19.237 129.508 146.912 1.00104.58 C
ANISOU 2797 C SER A 239 15289 10283 14163 -1070 -938 864 C
ATOM 2798 O SER A 239 19.402 130.711 146.759 1.00103.39 O
ANISOU 2798 O SER A 239 15084 10218 13982 -1039 -905 827 O
ATOM 2799 CB SER A 239 20.794 127.909 145.750 1.00106.59 C
ANISOU 2799 CB SER A 239 15319 10280 14903 -900 -965 914 C
ATOM 2800 OG SER A 239 19.687 127.260 145.146 1.00115.53 O
ANISOU 2800 OG SER A 239 16513 11474 15908 -923 -803 818 O
ATOM 2801 N GLU A 240 18.025 128.947 147.016 1.00100.26 N
ANISOU 2801 N GLU A 240 14851 9792 13452 -1146 -838 818 N
ATOM 2802 CA GLU A 240 16.781 129.704 146.899 1.00 98.59 C
ANISOU 2802 CA GLU A 240 14673 9740 13048 -1190 -673 724 C
ATOM 2803 C GLU A 240 16.617 130.638 148.087 1.00100.39 C
ANISOU 2803 C GLU A 240 15044 10001 13099 -1286 -716 757 C
ATOM 2804 O GLU A 240 16.123 131.754 147.927 1.00 98.90 O
ANISOU 2804 O GLU A 240 14825 9924 12828 -1276 -601 688 O
ATOM 2805 CB GLU A 240 15.568 128.760 146.756 1.00100.31 C
ANISOU 2805 CB GLU A 240 14951 9977 13186 -1255 -568 686 C
ATOM 2806 CG GLU A 240 15.582 127.883 145.506 1.00115.12 C
ANISOU 2806 CG GLU A 240 16725 11817 15197 -1181 -508 636 C
ATOM 2807 CD GLU A 240 15.674 128.596 144.167 1.00141.59 C
ANISOU 2807 CD GLU A 240 19940 15244 18615 -1083 -402 544 C
ATOM 2808 OE1 GLU A 240 14.642 129.141 143.713 1.00138.14 O
ANISOU 2808 OE1 GLU A 240 19479 14923 18084 -1110 -299 477 O
ATOM 2809 OE2 GLU A 240 16.779 128.609 143.575 1.00136.23 O1-
ANISOU 2809 OE2 GLU A 240 19174 14492 18093 -985 -419 545 O1-
ATOM 2810 N VAL A 241 17.066 130.179 149.269 1.00 96.95 N
ANISOU 2810 N VAL A 241 14781 9449 12605 -1385 -888 867 N
ATOM 2811 CA VAL A 241 17.033 130.900 150.545 1.00 96.56 C
ANISOU 2811 CA VAL A 241 14950 9384 12355 -1513 -958 915 C
ATOM 2812 C VAL A 241 18.039 132.040 150.471 1.00 99.12 C
ANISOU 2812 C VAL A 241 15198 9711 12751 -1456 -1064 935 C
ATOM 2813 O VAL A 241 17.694 133.173 150.789 1.00 98.64 O
ANISOU 2813 O VAL A 241 15207 9725 12546 -1492 -982 885 O
ATOM 2814 CB VAL A 241 17.339 129.950 151.735 1.00101.77 C
ANISOU 2814 CB VAL A 241 15843 9888 12937 -1652 -1155 1044 C
ATOM 2815 CG1 VAL A 241 17.268 130.686 153.066 1.00102.61 C
ANISOU 2815 CG1 VAL A 241 16242 9958 12787 -1816 -1219 1088 C
ATOM 2816 CG2 VAL A 241 16.411 128.741 151.736 1.00101.76 C
ANISOU 2816 CG2 VAL A 241 15901 9874 12891 -1703 -1052 1029 C
ATOM 2817 N GLU A 242 19.271 131.735 150.025 1.00 95.27 N
ANISOU 2817 N GLU A 242 14554 9132 12512 -1363 -1230 1006 N
ATOM 2818 CA GLU A 242 20.372 132.676 149.855 1.00 94.95 C
ANISOU 2818 CA GLU A 242 14396 9071 12609 -1299 -1347 1043 C
ATOM 2819 C GLU A 242 19.971 133.830 148.927 1.00 98.60 C
ANISOU 2819 C GLU A 242 14720 9692 13050 -1206 -1135 911 C
ATOM 2820 O GLU A 242 20.208 134.992 149.265 1.00 99.06 O
ANISOU 2820 O GLU A 242 14818 9789 13032 -1229 -1165 907 O
ATOM 2821 CB GLU A 242 21.595 131.946 149.297 1.00 96.85 C
ANISOU 2821 CB GLU A 242 14433 9175 13190 -1191 -1481 1125 C
ATOM 2822 CG GLU A 242 22.897 132.589 149.704 1.00110.26 C
ANISOU 2822 CG GLU A 242 16067 10770 15057 -1188 -1717 1241 C
ATOM 2823 CD GLU A 242 24.105 131.976 149.038 1.00141.66 C
ANISOU 2823 CD GLU A 242 19786 14599 19438 -1062 -1798 1316 C
ATOM 2824 OE1 GLU A 242 24.651 132.607 148.104 1.00138.81 O
ANISOU 2824 OE1 GLU A 242 19212 14269 19262 -940 -1689 1264 O
ATOM 2825 OE2 GLU A 242 24.496 130.857 149.441 1.00146.08 O1-
ANISOU 2825 OE2 GLU A 242 20359 15001 20143 -1086 -1954 1426 O1-
ATOM 2826 N MET A 243 19.346 133.508 147.780 1.00 93.64 N
ANISOU 2826 N MET A 243 13954 9146 12479 -1115 -938 810 N
ATOM 2827 CA MET A 243 18.874 134.480 146.809 1.00 92.13 C
ANISOU 2827 CA MET A 243 13642 9092 12270 -1038 -755 696 C
ATOM 2828 C MET A 243 17.712 135.271 147.377 1.00 94.51 C
ANISOU 2828 C MET A 243 14069 9497 12342 -1122 -638 638 C
ATOM 2829 O MET A 243 17.735 136.488 147.304 1.00 93.34 O
ANISOU 2829 O MET A 243 13892 9419 12155 -1101 -591 598 O
ATOM 2830 CB MET A 243 18.483 133.796 145.506 1.00 94.68 C
ANISOU 2830 CB MET A 243 13839 9444 12691 -956 -613 620 C
ATOM 2831 CG MET A 243 19.655 133.209 144.756 1.00100.46 C
ANISOU 2831 CG MET A 243 14433 10064 13673 -854 -653 649 C
ATOM 2832 SD MET A 243 19.082 132.042 143.490 1.00106.51 S
ANISOU 2832 SD MET A 243 15163 10813 14494 -810 -493 567 S
ATOM 2833 CE MET A 243 20.662 131.273 143.000 1.00104.91 C
ANISOU 2833 CE MET A 243 14830 10411 14619 -704 -534 624 C
ATOM 2834 N MET A 244 16.729 134.615 147.996 1.00 92.62 N
ANISOU 2834 N MET A 244 13971 9254 11967 -1221 -578 637 N
ATOM 2835 CA MET A 244 15.600 135.325 148.604 1.00 93.32 C
ANISOU 2835 CA MET A 244 14175 9411 11873 -1304 -424 583 C
ATOM 2836 C MET A 244 16.056 136.370 149.641 1.00 96.37 C
ANISOU 2836 C MET A 244 14724 9765 12127 -1376 -490 612 C
ATOM 2837 O MET A 244 15.496 137.464 149.698 1.00 94.33 O
ANISOU 2837 O MET A 244 14474 9574 11791 -1380 -347 545 O
ATOM 2838 CB MET A 244 14.596 134.343 149.221 1.00 97.12 C
ANISOU 2838 CB MET A 244 14794 9859 12250 -1413 -345 591 C
ATOM 2839 CG MET A 244 13.265 134.977 149.540 1.00102.15 C
ANISOU 2839 CG MET A 244 15483 10557 12772 -1476 -117 521 C
ATOM 2840 SD MET A 244 12.420 135.621 148.073 1.00106.41 S
ANISOU 2840 SD MET A 244 15744 11229 13460 -1360 46 426 S
ATOM 2841 CE MET A 244 12.321 137.333 148.481 1.00103.10 C
ANISOU 2841 CE MET A 244 15339 10853 12979 -1349 143 379 C
ATOM 2842 N ALA A 245 17.092 136.022 150.428 1.00 94.12 N
ANISOU 2842 N ALA A 245 14569 9361 11831 -1438 -720 719 N
ATOM 2843 CA ALA A 245 17.721 136.873 151.437 1.00 95.05 C
ANISOU 2843 CA ALA A 245 14878 9415 11822 -1532 -854 773 C
ATOM 2844 C ALA A 245 18.370 138.091 150.766 1.00 99.51 C
ANISOU 2844 C ALA A 245 15274 10042 12495 -1427 -866 740 C
ATOM 2845 O ALA A 245 18.128 139.220 151.189 1.00100.25 O
ANISOU 2845 O ALA A 245 15477 10163 12452 -1474 -797 697 O
ATOM 2846 CB ALA A 245 18.774 136.081 152.192 1.00 97.19 C
ANISOU 2846 CB ALA A 245 15275 9529 12125 -1612 -1155 920 C
ATOM 2847 N GLN A 246 19.176 137.857 149.705 1.00 94.26 N
ANISOU 2847 N GLN A 246 14351 9386 12077 -1288 -930 754 N
ATOM 2848 CA GLN A 246 19.844 138.896 148.928 1.00 92.08 C
ANISOU 2848 CA GLN A 246 13894 9163 11932 -1182 -928 725 C
ATOM 2849 C GLN A 246 18.794 139.793 148.283 1.00 94.98 C
ANISOU 2849 C GLN A 246 14195 9671 12223 -1132 -682 598 C
ATOM 2850 O GLN A 246 18.933 141.006 148.343 1.00 95.48 O
ANISOU 2850 O GLN A 246 14257 9773 12249 -1122 -660 568 O
ATOM 2851 CB GLN A 246 20.781 138.281 147.875 1.00 92.45 C
ANISOU 2851 CB GLN A 246 13698 9168 12261 -1053 -985 756 C
ATOM 2852 CG GLN A 246 22.008 137.612 148.484 1.00 94.80 C
ANISOU 2852 CG GLN A 246 14002 9299 12718 -1085 -1252 902 C
ATOM 2853 CD GLN A 246 22.701 136.595 147.604 1.00104.87 C
ANISOU 2853 CD GLN A 246 15069 10493 14283 -973 -1258 933 C
ATOM 2854 OE1 GLN A 246 22.275 136.262 146.486 1.00 94.65 O
ANISOU 2854 OE1 GLN A 246 13653 9263 13048 -878 -1059 838 O
ATOM 2855 NE2 GLN A 246 23.808 136.070 148.105 1.00101.23 N
ANISOU 2855 NE2 GLN A 246 14576 9868 14020 -991 -1495 1073 N
ATOM 2856 N ALA A 247 17.703 139.209 147.764 1.00 90.23 N
ANISOU 2856 N ALA A 247 13548 9132 11603 -1115 -516 533 N
ATOM 2857 CA ALA A 247 16.606 139.957 147.150 1.00 89.17 C
ANISOU 2857 CA ALA A 247 13333 9111 11437 -1077 -310 435 C
ATOM 2858 C ALA A 247 15.870 140.822 148.164 1.00 93.94 C
ANISOU 2858 C ALA A 247 14105 9719 11868 -1170 -201 403 C
ATOM 2859 O ALA A 247 15.420 141.900 147.805 1.00 93.15 O
ANISOU 2859 O ALA A 247 13933 9684 11774 -1128 -80 341 O
ATOM 2860 CB ALA A 247 15.633 139.008 146.481 1.00 89.58 C
ANISOU 2860 CB ALA A 247 13309 9199 11529 -1062 -202 398 C
ATOM 2861 N LEU A 248 15.733 140.352 149.415 1.00 91.98 N
ANISOU 2861 N LEU A 248 14096 9386 11467 -1300 -230 445 N
ATOM 2862 CA LEU A 248 15.076 141.116 150.468 1.00 93.11 C
ANISOU 2862 CA LEU A 248 14455 9499 11423 -1410 -92 409 C
ATOM 2863 C LEU A 248 16.031 142.208 150.949 1.00 98.84 C
ANISOU 2863 C LEU A 248 15291 10185 12080 -1436 -217 432 C
ATOM 2864 O LEU A 248 15.600 143.343 151.178 1.00 99.72 O
ANISOU 2864 O LEU A 248 15462 10311 12115 -1452 -70 367 O
ATOM 2865 CB LEU A 248 14.688 140.217 151.652 1.00 94.82 C
ANISOU 2865 CB LEU A 248 14942 9616 11469 -1565 -82 450 C
ATOM 2866 CG LEU A 248 13.506 139.274 151.489 1.00 99.48 C
ANISOU 2866 CG LEU A 248 15488 10226 12083 -1583 96 420 C
ATOM 2867 CD1 LEU A 248 13.509 138.245 152.589 1.00101.11 C
ANISOU 2867 CD1 LEU A 248 15974 10320 12125 -1738 40 485 C
ATOM 2868 CD2 LEU A 248 12.180 140.024 151.474 1.00101.77 C
ANISOU 2868 CD2 LEU A 248 15731 10559 12379 -1582 400 326 C
ATOM 2869 N GLY A 249 17.311 141.842 151.103 1.00 94.59 N
ANISOU 2869 N GLY A 249 14768 9579 11591 -1445 -489 530 N
ATOM 2870 CA GLY A 249 18.392 142.729 151.518 1.00 94.16 C
ANISOU 2870 CA GLY A 249 14795 9470 11512 -1478 -673 580 C
ATOM 2871 C GLY A 249 18.530 143.909 150.576 1.00 94.37 C
ANISOU 2871 C GLY A 249 14609 9592 11655 -1352 -590 514 C
ATOM 2872 O GLY A 249 18.607 145.047 151.030 1.00 94.17 O
ANISOU 2872 O GLY A 249 14703 9553 11525 -1398 -567 486 O
ATOM 2873 N ILE A 250 18.495 143.645 149.260 1.00 87.97 N
ANISOU 2873 N ILE A 250 13512 8870 11043 -1205 -533 483 N
ATOM 2874 CA ILE A 250 18.550 144.654 148.198 1.00 86.22 C
ANISOU 2874 CA ILE A 250 13086 8739 10933 -1086 -448 423 C
ATOM 2875 C ILE A 250 17.299 145.553 148.285 1.00 91.26 C
ANISOU 2875 C ILE A 250 13766 9438 11471 -1097 -214 327 C
ATOM 2876 O ILE A 250 17.411 146.772 148.169 1.00 91.65 O
ANISOU 2876 O ILE A 250 13795 9512 11516 -1070 -174 291 O
ATOM 2877 CB ILE A 250 18.690 143.944 146.811 1.00 87.41 C
ANISOU 2877 CB ILE A 250 12988 8944 11278 -961 -427 413 C
ATOM 2878 CG1 ILE A 250 20.090 143.274 146.617 1.00 87.53 C
ANISOU 2878 CG1 ILE A 250 12921 8876 11462 -927 -623 504 C
ATOM 2879 CG2 ILE A 250 18.317 144.827 145.629 1.00 85.85 C
ANISOU 2879 CG2 ILE A 250 12619 8846 11154 -861 -297 339 C
ATOM 2880 CD1 ILE A 250 21.265 144.083 146.599 1.00 95.37 C
ANISOU 2880 CD1 ILE A 250 13858 9826 12552 -907 -759 554 C
ATOM 2881 N MET A 251 16.139 144.940 148.542 1.00 88.95 N
ANISOU 2881 N MET A 251 13527 9152 11120 -1139 -60 293 N
ATOM 2882 CA MET A 251 14.817 145.564 148.661 1.00 90.01 C
ANISOU 2882 CA MET A 251 13669 9313 11217 -1151 189 213 C
ATOM 2883 C MET A 251 14.721 146.528 149.840 1.00 94.23 C
ANISOU 2883 C MET A 251 14452 9772 11581 -1252 275 185 C
ATOM 2884 O MET A 251 14.107 147.591 149.707 1.00 94.28 O
ANISOU 2884 O MET A 251 14412 9796 11614 -1219 446 119 O
ATOM 2885 CB MET A 251 13.751 144.470 148.819 1.00 93.54 C
ANISOU 2885 CB MET A 251 14130 9753 11661 -1196 310 207 C
ATOM 2886 CG MET A 251 12.416 144.857 148.280 1.00 98.23 C
ANISOU 2886 CG MET A 251 14564 10394 12363 -1152 531 145 C
ATOM 2887 SD MET A 251 11.177 145.172 149.540 1.00105.48 S
ANISOU 2887 SD MET A 251 15672 11223 13183 -1268 828 94 S
ATOM 2888 CE MET A 251 10.996 143.516 150.241 1.00102.90 C
ANISOU 2888 CE MET A 251 15509 10837 12749 -1383 796 144 C
ATOM 2889 N VAL A 252 15.274 146.118 151.007 1.00 89.84 N
ANISOU 2889 N VAL A 252 14178 9113 10845 -1388 158 238 N
ATOM 2890 CA VAL A 252 15.295 146.885 152.259 1.00 89.12 C
ANISOU 2890 CA VAL A 252 14413 8915 10532 -1527 213 218 C
ATOM 2891 C VAL A 252 16.246 148.059 152.100 1.00 90.61 C
ANISOU 2891 C VAL A 252 14589 9105 10733 -1496 78 226 C
ATOM 2892 O VAL A 252 15.913 149.157 152.531 1.00 90.63 O
ANISOU 2892 O VAL A 252 14726 9068 10641 -1535 228 160 O
ATOM 2893 CB VAL A 252 15.630 145.977 153.474 1.00 93.01 C
ANISOU 2893 CB VAL A 252 15238 9286 10818 -1703 82 291 C
ATOM 2894 CG1 VAL A 252 15.924 146.785 154.734 1.00 94.20 C
ANISOU 2894 CG1 VAL A 252 15782 9305 10707 -1874 68 287 C
ATOM 2895 CG2 VAL A 252 14.508 144.984 153.731 1.00 92.85 C
ANISOU 2895 CG2 VAL A 252 15260 9253 10764 -1749 283 266 C
ATOM 2896 N VAL A 253 17.402 147.831 151.442 1.00 86.05 N
ANISOU 2896 N VAL A 253 13836 8562 10296 -1422 -181 302 N
ATOM 2897 CA VAL A 253 18.427 148.840 151.149 1.00 86.00 C
ANISOU 2897 CA VAL A 253 13766 8559 10352 -1382 -333 325 C
ATOM 2898 C VAL A 253 17.787 149.974 150.316 1.00 90.51 C
ANISOU 2898 C VAL A 253 14154 9221 11015 -1266 -122 229 C
ATOM 2899 O VAL A 253 17.891 151.152 150.684 1.00 90.24 O
ANISOU 2899 O VAL A 253 14232 9152 10904 -1298 -83 193 O
ATOM 2900 CB VAL A 253 19.697 148.195 150.499 1.00 89.25 C
ANISOU 2900 CB VAL A 253 13982 8974 10955 -1316 -605 429 C
ATOM 2901 CG1 VAL A 253 20.497 149.181 149.674 1.00 88.34 C
ANISOU 2901 CG1 VAL A 253 13672 8900 10991 -1219 -673 432 C
ATOM 2902 CG2 VAL A 253 20.601 147.587 151.558 1.00 90.83 C
ANISOU 2902 CG2 VAL A 253 14404 9038 11071 -1459 -881 548 C
ATOM 2903 N ALA A 254 17.056 149.594 149.249 1.00 86.37 N
ANISOU 2903 N ALA A 254 13375 8796 10645 -1146 8 191 N
ATOM 2904 CA ALA A 254 16.353 150.526 148.373 1.00 84.91 C
ANISOU 2904 CA ALA A 254 13002 8688 10573 -1041 178 120 C
ATOM 2905 C ALA A 254 15.225 151.215 149.113 1.00 90.29 C
ANISOU 2905 C ALA A 254 13824 9317 11166 -1097 431 44 C
ATOM 2906 O ALA A 254 14.962 152.386 148.853 1.00 90.09 O
ANISOU 2906 O ALA A 254 13744 9299 11189 -1049 534 -5 O
ATOM 2907 CB ALA A 254 15.806 149.791 147.173 1.00 84.37 C
ANISOU 2907 CB ALA A 254 12682 8707 10666 -941 218 117 C
ATOM 2908 N SER A 255 14.563 150.498 150.042 1.00 88.27 N
ANISOU 2908 N SER A 255 13755 8993 10789 -1200 547 34 N
ATOM 2909 CA SER A 255 13.461 151.060 150.827 1.00 89.24 C
ANISOU 2909 CA SER A 255 14032 9036 10841 -1265 843 -44 C
ATOM 2910 C SER A 255 13.963 152.208 151.699 1.00 93.02 C
ANISOU 2910 C SER A 255 14780 9417 11146 -1351 860 -76 C
ATOM 2911 O SER A 255 13.439 153.315 151.646 1.00 91.67 O
ANISOU 2911 O SER A 255 14587 9219 11027 -1315 1057 -147 O
ATOM 2912 CB SER A 255 12.787 149.982 151.678 1.00 92.77 C
ANISOU 2912 CB SER A 255 14655 9415 11177 -1377 963 -42 C
ATOM 2913 OG SER A 255 12.003 149.100 150.890 1.00 98.04 O
ANISOU 2913 OG SER A 255 15069 10156 12025 -1301 1025 -33 O
ATOM 2914 N VAL A 256 15.024 151.934 152.444 1.00 90.85 N
ANISOU 2914 N VAL A 256 14752 9080 10687 -1467 627 -14 N
ATOM 2915 CA VAL A 256 15.662 152.835 153.391 1.00 91.85 C
ANISOU 2915 CA VAL A 256 15199 9092 10606 -1592 568 -23 C
ATOM 2916 C VAL A 256 16.330 154.021 152.694 1.00 94.78 C
ANISOU 2916 C VAL A 256 15410 9513 11089 -1496 467 -27 C
ATOM 2917 O VAL A 256 16.109 155.146 153.117 1.00 94.83 O
ANISOU 2917 O VAL A 256 15572 9447 11013 -1535 612 -95 O
ATOM 2918 CB VAL A 256 16.640 152.025 154.306 1.00 96.06 C
ANISOU 2918 CB VAL A 256 16021 9536 10941 -1756 276 79 C
ATOM 2919 CG1 VAL A 256 17.594 152.929 155.080 1.00 97.28 C
ANISOU 2919 CG1 VAL A 256 16468 9579 10914 -1887 92 106 C
ATOM 2920 CG2 VAL A 256 15.882 151.103 155.254 1.00 96.83 C
ANISOU 2920 CG2 VAL A 256 16388 9546 10858 -1894 426 67 C
ATOM 2921 N CYS A 257 17.131 153.774 151.643 1.00 90.74 N
ANISOU 2921 N CYS A 257 14603 9111 10764 -1377 244 40 N
ATOM 2922 CA CYS A 257 17.920 154.802 150.963 1.00 90.52 C
ANISOU 2922 CA CYS A 257 14424 9125 10845 -1297 124 51 C
ATOM 2923 C CYS A 257 17.160 155.638 149.928 1.00 95.75 C
ANISOU 2923 C CYS A 257 14823 9872 11685 -1148 322 -19 C
ATOM 2924 O CYS A 257 17.307 156.879 149.897 1.00 98.13 O
ANISOU 2924 O CYS A 257 15149 10150 11988 -1133 363 -56 O
ATOM 2925 CB CYS A 257 19.173 154.193 150.344 1.00 90.03 C
ANISOU 2925 CB CYS A 257 14188 9109 10911 -1252 -177 158 C
ATOM 2926 SG CYS A 257 20.220 153.282 151.510 1.00 95.73 S
ANISOU 2926 SG CYS A 257 15177 9706 11490 -1425 -483 277 S
ATOM 2927 N TRP A 258 16.392 154.967 149.060 1.00 89.03 N
ANISOU 2927 N TRP A 258 13730 9110 10988 -1047 417 -28 N
ATOM 2928 CA TRP A 258 15.726 155.607 147.945 1.00 86.99 C
ANISOU 2928 CA TRP A 258 13207 8926 10918 -916 536 -65 C
ATOM 2929 C TRP A 258 14.399 156.238 148.242 1.00 90.59 C
ANISOU 2929 C TRP A 258 13676 9328 11416 -909 825 -142 C
ATOM 2930 O TRP A 258 14.220 157.383 147.838 1.00 90.19 O
ANISOU 2930 O TRP A 258 13540 9273 11456 -847 894 -173 O
ATOM 2931 CB TRP A 258 15.596 154.642 146.779 1.00 84.67 C
ANISOU 2931 CB TRP A 258 12661 8735 10775 -827 465 -26 C
ATOM 2932 CG TRP A 258 16.888 154.500 146.028 1.00 84.65 C
ANISOU 2932 CG TRP A 258 12555 8782 10824 -782 240 34 C
ATOM 2933 CD1 TRP A 258 17.739 153.430 146.036 1.00 87.36 C
ANISOU 2933 CD1 TRP A 258 12906 9126 11162 -803 73 97 C
ATOM 2934 CD2 TRP A 258 17.489 155.487 145.184 1.00 83.32 C
ANISOU 2934 CD2 TRP A 258 12264 8650 10743 -711 178 38 C
ATOM 2935 NE1 TRP A 258 18.826 153.688 145.239 1.00 85.86 N
ANISOU 2935 NE1 TRP A 258 12589 8962 11071 -746 -67 137 N
ATOM 2936 CE2 TRP A 258 18.711 154.953 144.723 1.00 86.76 C
ANISOU 2936 CE2 TRP A 258 12634 9103 11229 -694 -6 101 C
ATOM 2937 CE3 TRP A 258 17.122 156.782 144.790 1.00 83.80 C
ANISOU 2937 CE3 TRP A 258 12264 8718 10859 -661 268 -1 C
ATOM 2938 CZ2 TRP A 258 19.551 155.659 143.873 1.00 85.14 C
ANISOU 2938 CZ2 TRP A 258 12308 8922 11117 -635 -81 121 C
ATOM 2939 CZ3 TRP A 258 17.966 157.484 143.968 1.00 84.31 C
ANISOU 2939 CZ3 TRP A 258 12225 8815 10993 -607 166 22 C
ATOM 2940 CH2 TRP A 258 19.166 156.925 143.524 1.00 84.68 C
ANISOU 2940 CH2 TRP A 258 12215 8880 11079 -598 3 80 C
ATOM 2941 N LEU A 259 13.463 155.513 148.905 1.00 87.67 N
ANISOU 2941 N LEU A 259 13395 8907 11009 -969 1005 -168 N
ATOM 2942 CA LEU A 259 12.117 156.017 149.238 1.00 88.02 C
ANISOU 2942 CA LEU A 259 13427 8872 11144 -963 1327 -238 C
ATOM 2943 C LEU A 259 12.093 157.424 149.850 1.00 92.92 C
ANISOU 2943 C LEU A 259 14214 9383 11709 -990 1488 -307 C
ATOM 2944 O LEU A 259 11.322 158.230 149.324 1.00 92.45 O
ANISOU 2944 O LEU A 259 13961 9307 11858 -898 1647 -339 O
ATOM 2945 CB LEU A 259 11.315 155.058 150.111 1.00 88.95 C
ANISOU 2945 CB LEU A 259 13686 8919 11190 -1057 1510 -257 C
ATOM 2946 CG LEU A 259 10.707 153.850 149.437 1.00 92.06 C
ANISOU 2946 CG LEU A 259 13854 9393 11732 -1011 1477 -212 C
ATOM 2947 CD1 LEU A 259 10.200 152.903 150.475 1.00 93.88 C
ANISOU 2947 CD1 LEU A 259 14289 9544 11835 -1131 1623 -223 C
ATOM 2948 CD2 LEU A 259 9.541 154.241 148.533 1.00 92.62 C
ANISOU 2948 CD2 LEU A 259 13603 9481 12108 -901 1621 -219 C
ATOM 2949 N PRO A 260 12.933 157.790 150.875 1.00 90.66 N
ANISOU 2949 N PRO A 260 14274 9010 11163 -1116 1431 -325 N
ATOM 2950 CA PRO A 260 12.906 159.183 151.379 1.00 91.57 C
ANISOU 2950 CA PRO A 260 14557 9012 11225 -1143 1586 -397 C
ATOM 2951 C PRO A 260 13.094 160.235 150.282 1.00 93.18 C
ANISOU 2951 C PRO A 260 14487 9285 11631 -1002 1511 -388 C
ATOM 2952 O PRO A 260 12.300 161.175 150.228 1.00 94.98 O
ANISOU 2952 O PRO A 260 14648 9439 11999 -947 1750 -449 O
ATOM 2953 CB PRO A 260 14.046 159.222 152.414 1.00 94.09 C
ANISOU 2953 CB PRO A 260 15267 9253 11228 -1308 1404 -380 C
ATOM 2954 CG PRO A 260 14.219 157.830 152.840 1.00 98.35 C
ANISOU 2954 CG PRO A 260 15912 9810 11647 -1395 1284 -323 C
ATOM 2955 CD PRO A 260 13.922 156.987 151.628 1.00 92.22 C
ANISOU 2955 CD PRO A 260 14735 9189 11116 -1248 1206 -271 C
ATOM 2956 N LEU A 261 14.102 160.060 149.393 1.00 85.45 N
ANISOU 2956 N LEU A 261 13345 8433 10688 -944 1201 -311 N
ATOM 2957 CA LEU A 261 14.352 160.992 148.287 1.00 83.35 C
ANISOU 2957 CA LEU A 261 12839 8235 10595 -823 1115 -294 C
ATOM 2958 C LEU A 261 13.159 161.013 147.304 1.00 88.21 C
ANISOU 2958 C LEU A 261 13139 8894 11484 -699 1251 -295 C
ATOM 2959 O LEU A 261 12.685 162.092 146.940 1.00 88.54 O
ANISOU 2959 O LEU A 261 13072 8893 11674 -630 1361 -321 O
ATOM 2960 CB LEU A 261 15.665 160.624 147.554 1.00 81.01 C
ANISOU 2960 CB LEU A 261 12445 8049 10286 -800 793 -211 C
ATOM 2961 CG LEU A 261 15.987 161.376 146.253 1.00 82.01 C
ANISOU 2961 CG LEU A 261 12321 8257 10581 -684 694 -182 C
ATOM 2962 CD1 LEU A 261 16.517 162.755 146.532 1.00 82.27 C
ANISOU 2962 CD1 LEU A 261 12462 8225 10574 -700 693 -210 C
ATOM 2963 CD2 LEU A 261 16.961 160.607 145.404 1.00 79.74 C
ANISOU 2963 CD2 LEU A 261 11906 8071 10321 -655 457 -106 C
ATOM 2964 N LEU A 262 12.674 159.820 146.891 1.00 83.77 N
ANISOU 2964 N LEU A 262 12434 8399 10994 -679 1226 -257 N
ATOM 2965 CA LEU A 262 11.557 159.667 145.955 1.00 82.42 C
ANISOU 2965 CA LEU A 262 11972 8261 11083 -587 1299 -235 C
ATOM 2966 C LEU A 262 10.329 160.348 146.476 1.00 86.08 C
ANISOU 2966 C LEU A 262 12412 8593 11701 -575 1605 -291 C
ATOM 2967 O LEU A 262 9.702 161.084 145.731 1.00 85.81 O
ANISOU 2967 O LEU A 262 12157 8542 11906 -486 1643 -275 O
ATOM 2968 CB LEU A 262 11.267 158.195 145.666 1.00 81.83 C
ANISOU 2968 CB LEU A 262 11816 8255 11021 -601 1229 -191 C
ATOM 2969 CG LEU A 262 12.422 157.391 145.113 1.00 84.60 C
ANISOU 2969 CG LEU A 262 12173 8713 11259 -606 961 -138 C
ATOM 2970 CD1 LEU A 262 12.176 155.915 145.308 1.00 84.66 C
ANISOU 2970 CD1 LEU A 262 12197 8745 11225 -652 943 -114 C
ATOM 2971 CD2 LEU A 262 12.698 157.746 143.656 1.00 85.75 C
ANISOU 2971 CD2 LEU A 262 12107 8943 11531 -517 802 -93 C
ATOM 2972 N VAL A 263 10.021 160.174 147.766 1.00 83.63 N
ANISOU 2972 N VAL A 263 12343 8171 11262 -669 1832 -355 N
ATOM 2973 CA VAL A 263 8.881 160.857 148.380 1.00 85.71 C
ANISOU 2973 CA VAL A 263 12612 8274 11681 -665 2192 -423 C
ATOM 2974 C VAL A 263 9.150 162.382 148.369 1.00 91.23 C
ANISOU 2974 C VAL A 263 13351 8897 12417 -624 2250 -466 C
ATOM 2975 O VAL A 263 8.317 163.144 147.872 1.00 91.60 O
ANISOU 2975 O VAL A 263 13169 8876 12759 -530 2391 -466 O
ATOM 2976 CB VAL A 263 8.519 160.300 149.785 1.00 90.70 C
ANISOU 2976 CB VAL A 263 13550 8782 12129 -798 2454 -491 C
ATOM 2977 CG1 VAL A 263 7.375 161.092 150.415 1.00 92.91 C
ANISOU 2977 CG1 VAL A 263 13848 8867 12589 -792 2883 -574 C
ATOM 2978 CG2 VAL A 263 8.169 158.814 149.716 1.00 89.70 C
ANISOU 2978 CG2 VAL A 263 13354 8725 12003 -831 2402 -442 C
ATOM 2979 N PHE A 264 10.350 162.800 148.820 1.00 87.72 N
ANISOU 2979 N PHE A 264 13168 8463 11699 -691 2103 -485 N
ATOM 2980 CA PHE A 264 10.742 164.205 148.853 1.00 88.61 C
ANISOU 2980 CA PHE A 264 13354 8505 11808 -670 2128 -524 C
ATOM 2981 C PHE A 264 10.567 164.907 147.508 1.00 91.59 C
ANISOU 2981 C PHE A 264 13385 8951 12463 -526 2007 -467 C
ATOM 2982 O PHE A 264 10.004 165.999 147.467 1.00 92.41 O
ANISOU 2982 O PHE A 264 13417 8944 12749 -467 2184 -502 O
ATOM 2983 CB PHE A 264 12.173 164.375 149.384 1.00 90.35 C
ANISOU 2983 CB PHE A 264 13876 8744 11706 -776 1909 -524 C
ATOM 2984 CG PHE A 264 12.609 165.817 149.460 1.00 92.73 C
ANISOU 2984 CG PHE A 264 14276 8969 11990 -768 1923 -563 C
ATOM 2985 CD1 PHE A 264 12.135 166.651 150.465 1.00 97.85 C
ANISOU 2985 CD1 PHE A 264 15180 9423 12574 -832 2228 -666 C
ATOM 2986 CD2 PHE A 264 13.479 166.345 148.514 1.00 94.70 C
ANISOU 2986 CD2 PHE A 264 14372 9324 12286 -703 1652 -502 C
ATOM 2987 CE1 PHE A 264 12.516 167.987 150.520 1.00100.28 C
ANISOU 2987 CE1 PHE A 264 15585 9649 12868 -827 2245 -706 C
ATOM 2988 CE2 PHE A 264 13.864 167.691 148.569 1.00 98.71 C
ANISOU 2988 CE2 PHE A 264 14965 9756 12784 -699 1663 -535 C
ATOM 2989 CZ PHE A 264 13.394 168.499 149.582 1.00 98.91 C
ANISOU 2989 CZ PHE A 264 15246 9593 12743 -761 1947 -636 C
ATOM 2990 N ILE A 265 11.029 164.270 146.418 1.00 85.90 N
ANISOU 2990 N ILE A 265 12468 8396 11774 -477 1716 -378 N
ATOM 2991 CA ILE A 265 10.914 164.796 145.066 1.00 84.21 C
ANISOU 2991 CA ILE A 265 11967 8250 11780 -367 1565 -312 C
ATOM 2992 C ILE A 265 9.442 165.054 144.766 1.00 88.56 C
ANISOU 2992 C ILE A 265 12271 8709 12668 -292 1756 -300 C
ATOM 2993 O ILE A 265 9.085 166.208 144.582 1.00 89.44 O
ANISOU 2993 O ILE A 265 12290 8734 12961 -230 1835 -306 O
ATOM 2994 CB ILE A 265 11.619 163.877 144.018 1.00 85.35 C
ANISOU 2994 CB ILE A 265 11997 8562 11868 -354 1265 -230 C
ATOM 2995 CG1 ILE A 265 13.152 163.894 144.215 1.00 84.83 C
ANISOU 2995 CG1 ILE A 265 12119 8558 11555 -410 1076 -227 C
ATOM 2996 CG2 ILE A 265 11.243 164.266 142.572 1.00 84.87 C
ANISOU 2996 CG2 ILE A 265 11665 8552 12032 -264 1129 -156 C
ATOM 2997 CD1 ILE A 265 13.917 162.837 143.447 1.00 91.18 C
ANISOU 2997 CD1 ILE A 265 12855 9491 12297 -411 849 -164 C
ATOM 2998 N ALA A 266 8.585 164.016 144.838 1.00 85.08 N
ANISOU 2998 N ALA A 266 11733 8267 12328 -305 1844 -283 N
ATOM 2999 CA ALA A 266 7.153 164.119 144.555 1.00 86.81 C
ANISOU 2999 CA ALA A 266 11681 8386 12915 -243 2009 -252 C
ATOM 3000 C ALA A 266 6.437 165.177 145.380 1.00 95.65 C
ANISOU 3000 C ALA A 266 12835 9304 14204 -222 2360 -328 C
ATOM 3001 O ALA A 266 5.585 165.872 144.837 1.00 96.85 O
ANISOU 3001 O ALA A 266 12724 9363 14711 -135 2420 -284 O
ATOM 3002 CB ALA A 266 6.483 162.775 144.721 1.00 87.69 C
ANISOU 3002 CB ALA A 266 11732 8520 13067 -285 2060 -230 C
ATOM 3003 N GLN A 267 6.808 165.335 146.669 1.00 94.34 N
ANISOU 3003 N GLN A 267 13007 9053 13786 -308 2584 -437 N
ATOM 3004 CA GLN A 267 6.214 166.334 147.575 1.00 96.56 C
ANISOU 3004 CA GLN A 267 13403 9115 14170 -309 2967 -534 C
ATOM 3005 C GLN A 267 6.619 167.741 147.183 1.00 99.46 C
ANISOU 3005 C GLN A 267 13748 9439 14605 -243 2908 -540 C
ATOM 3006 O GLN A 267 5.781 168.644 147.219 1.00101.23 O
ANISOU 3006 O GLN A 267 13828 9492 15141 -170 3149 -560 O
ATOM 3007 CB GLN A 267 6.635 166.092 149.036 1.00 99.03 C
ANISOU 3007 CB GLN A 267 14163 9346 14116 -453 3179 -647 C
ATOM 3008 CG GLN A 267 6.098 164.802 149.663 1.00114.18 C
ANISOU 3008 CG GLN A 267 16150 11249 15983 -533 3339 -659 C
ATOM 3009 CD GLN A 267 6.442 164.679 151.130 1.00129.49 C
ANISOU 3009 CD GLN A 267 18574 13073 17555 -695 3560 -767 C
ATOM 3010 OE1 GLN A 267 7.450 165.214 151.629 1.00121.86 O
ANISOU 3010 OE1 GLN A 267 17929 12099 16272 -776 3453 -809 O
ATOM 3011 NE2 GLN A 267 5.595 163.968 151.856 1.00123.04 N
ANISOU 3011 NE2 GLN A 267 17829 12149 16770 -759 3868 -808 N
ATOM 3012 N THR A 268 7.912 167.929 146.845 1.00 93.28 N
ANISOU 3012 N THR A 268 13098 8793 13550 -269 2599 -519 N
ATOM 3013 CA THR A 268 8.482 169.223 146.480 1.00 93.27 C
ANISOU 3013 CA THR A 268 13108 8768 13562 -223 2506 -521 C
ATOM 3014 C THR A 268 7.817 169.737 145.214 1.00 97.91 C
ANISOU 3014 C THR A 268 13309 9363 14530 -94 2390 -422 C
ATOM 3015 O THR A 268 7.465 170.919 145.104 1.00100.82 O
ANISOU 3015 O THR A 268 13599 9604 15104 -27 2495 -432 O
ATOM 3016 CB THR A 268 10.013 169.112 146.350 1.00 98.04 C
ANISOU 3016 CB THR A 268 13915 9522 13815 -291 2193 -505 C
ATOM 3017 OG1 THR A 268 10.542 168.646 147.588 1.00101.25 O
ANISOU 3017 OG1 THR A 268 14683 9890 13897 -426 2280 -580 O
ATOM 3018 CG2 THR A 268 10.669 170.433 146.012 1.00 95.11 C
ANISOU 3018 CG2 THR A 268 13578 9123 13437 -260 2099 -509 C
ATOM 3019 N VAL A 269 7.619 168.824 144.285 1.00 90.94 N
ANISOU 3019 N VAL A 269 12204 8613 13737 -69 2170 -324 N
ATOM 3020 CA VAL A 269 7.041 169.057 142.987 1.00 89.88 C
ANISOU 3020 CA VAL A 269 11735 8499 13916 19 1983 -206 C
ATOM 3021 C VAL A 269 5.524 169.340 143.107 1.00 97.15 C
ANISOU 3021 C VAL A 269 12395 9231 15287 86 2235 -184 C
ATOM 3022 O VAL A 269 5.008 170.182 142.365 1.00 97.94 O
ANISOU 3022 O VAL A 269 12259 9249 15705 167 2167 -108 O
ATOM 3023 CB VAL A 269 7.458 167.849 142.096 1.00 91.16 C
ANISOU 3023 CB VAL A 269 11834 8857 13944 -13 1669 -123 C
ATOM 3024 CG1 VAL A 269 6.283 167.060 141.520 1.00 91.32 C
ANISOU 3024 CG1 VAL A 269 11578 8863 14255 10 1635 -34 C
ATOM 3025 CG2 VAL A 269 8.459 168.274 141.029 1.00 89.14 C
ANISOU 3025 CG2 VAL A 269 11586 8721 13561 -2 1358 -64 C
ATOM 3026 N LEU A 270 4.847 168.718 144.102 1.00 95.43 N
ANISOU 3026 N LEU A 270 12230 8921 15109 49 2541 -251 N
ATOM 3027 CA LEU A 270 3.405 168.865 144.338 1.00 97.91 C
ANISOU 3027 CA LEU A 270 12290 9035 15878 105 2835 -235 C
ATOM 3028 C LEU A 270 3.016 169.832 145.461 1.00110.84 C
ANISOU 3028 C LEU A 270 14064 10435 17614 118 3286 -360 C
ATOM 3029 O LEU A 270 1.827 169.904 145.803 1.00114.06 O
ANISOU 3029 O LEU A 270 14275 10651 18414 161 3602 -362 O
ATOM 3030 CB LEU A 270 2.757 167.500 144.590 1.00 96.88 C
ANISOU 3030 CB LEU A 270 12083 8934 15791 56 2906 -215 C
ATOM 3031 CG LEU A 270 2.766 166.532 143.442 1.00 98.23 C
ANISOU 3031 CG LEU A 270 12054 9277 15992 51 2518 -83 C
ATOM 3032 CD1 LEU A 270 2.227 165.214 143.872 1.00 98.14 C
ANISOU 3032 CD1 LEU A 270 12025 9284 15981 -10 2621 -83 C
ATOM 3033 CD2 LEU A 270 1.994 167.062 142.263 1.00101.27 C
ANISOU 3033 CD2 LEU A 270 12062 9593 16822 134 2329 60 C
ATOM 3034 N ARG A 271 4.000 170.576 146.028 1.00110.10 N
ANISOU 3034 N ARG A 271 14306 10338 17188 76 3327 -460 N
ATOM 3035 CA ARG A 271 3.807 171.540 147.119 1.00113.67 C
ANISOU 3035 CA ARG A 271 14977 10559 17652 64 3746 -595 C
ATOM 3036 C ARG A 271 2.719 172.607 146.793 1.00123.05 C
ANISOU 3036 C ARG A 271 15836 11519 19398 195 3956 -560 C
ATOM 3037 O ARG A 271 2.820 173.275 145.750 1.00120.72 O
ANISOU 3037 O ARG A 271 15310 11264 19293 280 3675 -456 O
ATOM 3038 CB ARG A 271 5.156 172.177 147.509 1.00113.23 C
ANISOU 3038 CB ARG A 271 15309 10561 17152 -10 3631 -674 C
ATOM 3039 CG ARG A 271 5.165 172.818 148.895 1.00131.04 C
ANISOU 3039 CG ARG A 271 17952 12599 19238 -92 4053 -838 C
ATOM 3040 CD ARG A 271 6.557 173.206 149.361 1.00150.00 C
ANISOU 3040 CD ARG A 271 20772 15066 21155 -203 3885 -902 C
ATOM 3041 NE ARG A 271 7.395 172.029 149.618 1.00168.97 N
ANISOU 3041 NE ARG A 271 23388 17656 23156 -324 3643 -885 N
ATOM 3042 CZ ARG A 271 8.517 172.037 150.335 1.00184.78 C
ANISOU 3042 CZ ARG A 271 25801 19687 24720 -464 3532 -940 C
ATOM 3043 NH1 ARG A 271 8.951 173.165 150.888 1.00171.08 N
ANISOU 3043 NH1 ARG A 271 24340 17809 22854 -512 3642 -1023 N
ATOM 3044 NH2 ARG A 271 9.204 170.915 150.518 1.00168.88 N
ANISOU 3044 NH2 ARG A 271 23930 17828 22410 -562 3299 -904 N
ATOM 3045 N ASN A 272 1.655 172.710 147.680 1.00125.98 N
ANISOU 3045 N ASN A 272 16180 11637 20049 206 4458 -639 N
ATOM 3046 CA ASN A 272 0.496 173.635 147.595 1.00129.91 C
ANISOU 3046 CA ASN A 272 16357 11858 21144 329 4760 -618 C
ATOM 3047 C ASN A 272 0.973 175.052 147.248 1.00136.38 C
ANISOU 3047 C ASN A 272 17207 12610 22002 396 4676 -625 C
ATOM 3048 O ASN A 272 0.788 175.432 146.088 1.00135.00 O
ANISOU 3048 O ASN A 272 16691 12481 22121 491 4348 -477 O
ATOM 3049 CB ASN A 272 -0.409 173.568 148.838 1.00133.33 C
ANISOU 3049 CB ASN A 272 16889 12020 21751 300 5382 -746 C
ATOM 3050 N PRO A 273 1.716 175.796 148.117 1.00136.14 N
ANISOU 3050 N PRO A 273 17605 12497 21625 329 4880 -778 N
ATOM 3051 CA PRO A 273 2.344 177.041 147.628 1.00135.80 C
ANISOU 3051 CA PRO A 273 17593 12442 21564 382 4698 -766 C
ATOM 3052 C PRO A 273 3.650 176.593 146.930 1.00135.97 C
ANISOU 3052 C PRO A 273 17744 12788 21132 317 4159 -699 C
ATOM 3053 O PRO A 273 4.403 175.804 147.521 1.00133.79 O
ANISOU 3053 O PRO A 273 17791 12650 20394 191 4106 -763 O
ATOM 3054 CB PRO A 273 2.604 177.858 148.905 1.00139.76 C
ANISOU 3054 CB PRO A 273 18532 12720 21849 310 5136 -959 C
ATOM 3055 CG PRO A 273 2.414 176.888 150.067 1.00145.75 C
ANISOU 3055 CG PRO A 273 19589 13436 22354 182 5467 -1076 C
ATOM 3056 CD PRO A 273 2.119 175.513 149.514 1.00139.37 C
ANISOU 3056 CD PRO A 273 18520 12835 21598 182 5221 -957 C
ATOM 3057 N PRO A 274 3.900 176.965 145.652 1.00131.09 N
ANISOU 3057 N PRO A 274 16863 12288 20657 394 3754 -557 N
ATOM 3058 CA PRO A 274 5.098 176.455 144.957 1.00127.48 C
ANISOU 3058 CA PRO A 274 16508 12122 19805 333 3287 -493 C
ATOM 3059 C PRO A 274 6.387 176.411 145.783 1.00129.16 C
ANISOU 3059 C PRO A 274 17185 12426 19463 204 3267 -610 C
ATOM 3060 O PRO A 274 6.728 177.378 146.470 1.00129.51 O
ANISOU 3060 O PRO A 274 17481 12329 19395 175 3453 -712 O
ATOM 3061 CB PRO A 274 5.214 177.374 143.746 1.00128.89 C
ANISOU 3061 CB PRO A 274 16455 12313 20206 423 2995 -373 C
ATOM 3062 CG PRO A 274 3.802 177.704 143.433 1.00136.21 C
ANISOU 3062 CG PRO A 274 16997 13032 21725 537 3158 -295 C
ATOM 3063 CD PRO A 274 3.102 177.832 144.763 1.00134.33 C
ANISOU 3063 CD PRO A 274 16876 12557 21605 532 3701 -440 C
ATOM 3064 N ALA A 275 7.070 175.241 145.740 1.00122.95 N
ANISOU 3064 N ALA A 275 16509 11857 18349 119 3040 -588 N
ATOM 3065 CA ALA A 275 8.330 174.957 146.439 1.00120.57 C
ANISOU 3065 CA ALA A 275 16606 11659 17548 -15 2942 -661 C
ATOM 3066 C ALA A 275 9.495 175.792 145.894 1.00120.67 C
ANISOU 3066 C ALA A 275 16697 11758 17392 -22 2650 -629 C
ATOM 3067 O ALA A 275 10.461 176.058 146.617 1.00119.43 O
ANISOU 3067 O ALA A 275 16879 11598 16899 -128 2627 -700 O
ATOM 3068 CB ALA A 275 8.659 173.481 146.311 1.00119.33 C
ANISOU 3068 CB ALA A 275 16451 11701 17190 -76 2745 -613 C
ATOM 3069 N MET A 276 9.406 176.176 144.611 1.00115.23 N
ANISOU 3069 N MET A 276 15705 11140 16935 77 2414 -514 N
ATOM 3070 CA MET A 276 10.426 176.942 143.917 1.00113.20 C
ANISOU 3070 CA MET A 276 15480 10966 16564 77 2140 -467 C
ATOM 3071 C MET A 276 9.929 178.324 143.484 1.00119.57 C
ANISOU 3071 C MET A 276 16141 11613 17678 174 2212 -446 C
ATOM 3072 O MET A 276 8.779 178.466 143.056 1.00121.41 O
ANISOU 3072 O MET A 276 16090 11741 18300 271 2309 -391 O
ATOM 3073 CB MET A 276 10.928 176.151 142.710 1.00112.72 C
ANISOU 3073 CB MET A 276 15245 11131 16451 86 1774 -345 C
ATOM 3074 CG MET A 276 12.357 176.426 142.420 1.00114.18 C
ANISOU 3074 CG MET A 276 15585 11438 16359 26 1527 -330 C
ATOM 3075 SD MET A 276 12.969 175.592 140.960 1.00115.29 S
ANISOU 3075 SD MET A 276 15550 11807 16448 31 1162 -200 S
ATOM 3076 CE MET A 276 13.939 174.334 141.710 1.00110.39 C
ANISOU 3076 CE MET A 276 15147 11311 15485 -78 1106 -245 C
ATOM 3077 N SER A 277 10.807 179.336 143.578 1.00115.30 N
ANISOU 3077 N SER A 277 15780 11043 16985 143 2146 -478 N
ATOM 3078 CA SER A 277 10.482 180.699 143.176 1.00116.69 C
ANISOU 3078 CA SER A 277 15847 11066 17425 227 2192 -458 C
ATOM 3079 C SER A 277 10.419 180.800 141.619 1.00121.84 C
ANISOU 3079 C SER A 277 16187 11827 18279 302 1862 -294 C
ATOM 3080 O SER A 277 10.946 179.895 140.963 1.00119.07 O
ANISOU 3080 O SER A 277 15792 11681 17768 265 1605 -223 O
ATOM 3081 CB SER A 277 11.489 181.679 143.788 1.00119.68 C
ANISOU 3081 CB SER A 277 16542 11382 17548 152 2210 -543 C
ATOM 3082 OG SER A 277 12.659 181.924 143.020 1.00123.82 O
ANISOU 3082 OG SER A 277 17085 12063 17898 119 1870 -469 O
ATOM 3083 N PRO A 278 9.806 181.857 140.993 1.00121.87 N
ANISOU 3083 N PRO A 278 15994 11688 18624 396 1857 -228 N
ATOM 3084 CA PRO A 278 9.809 181.952 139.510 1.00121.09 C
ANISOU 3084 CA PRO A 278 15659 11683 18666 436 1512 -63 C
ATOM 3085 C PRO A 278 11.204 182.064 138.859 1.00123.12 C
ANISOU 3085 C PRO A 278 16067 12125 18589 362 1218 -29 C
ATOM 3086 O PRO A 278 11.352 181.794 137.665 1.00122.40 O
ANISOU 3086 O PRO A 278 15852 12154 18501 356 938 93 O
ATOM 3087 CB PRO A 278 8.964 183.201 139.228 1.00124.88 C
ANISOU 3087 CB PRO A 278 15957 11933 19558 537 1593 -14 C
ATOM 3088 CG PRO A 278 8.202 183.444 140.479 1.00131.52 C
ANISOU 3088 CG PRO A 278 16850 12558 20564 573 2024 -144 C
ATOM 3089 CD PRO A 278 9.113 183.022 141.578 1.00126.13 C
ANISOU 3089 CD PRO A 278 16534 11959 19431 462 2157 -294 C
ATOM 3090 N ALA A 279 12.222 182.457 139.644 1.00118.20 N
ANISOU 3090 N ALA A 279 15722 11507 17683 294 1288 -132 N
ATOM 3091 CA ALA A 279 13.607 182.551 139.203 1.00115.73 C
ANISOU 3091 CA ALA A 279 15550 11345 17076 216 1052 -109 C
ATOM 3092 C ALA A 279 14.245 181.140 139.258 1.00117.37 C
ANISOU 3092 C ALA A 279 15822 11753 17021 143 944 -112 C
ATOM 3093 O ALA A 279 15.263 180.869 138.613 1.00115.70 O
ANISOU 3093 O ALA A 279 15640 11688 16634 92 727 -59 O
ATOM 3094 CB ALA A 279 14.359 183.512 140.105 1.00116.93 C
ANISOU 3094 CB ALA A 279 15964 11399 17066 162 1163 -211 C
ATOM 3095 N GLY A 280 13.606 180.249 140.000 1.00113.24 N
ANISOU 3095 N GLY A 280 15307 11218 16500 140 1111 -168 N
ATOM 3096 CA GLY A 280 14.068 178.882 140.180 1.00110.88 C
ANISOU 3096 CA GLY A 280 15067 11080 15983 76 1035 -174 C
ATOM 3097 C GLY A 280 14.834 178.680 141.473 1.00112.99 C
ANISOU 3097 C GLY A 280 15625 11337 15969 -24 1131 -279 C
ATOM 3098 O GLY A 280 15.630 177.750 141.564 1.00112.44 O
ANISOU 3098 O GLY A 280 15631 11402 15691 -92 1001 -269 O
ATOM 3099 N GLN A 281 14.611 179.535 142.490 1.00108.34 N
ANISOU 3099 N GLN A 281 15219 10572 15374 -43 1353 -377 N
ATOM 3100 CA GLN A 281 15.293 179.411 143.778 1.00106.85 C
ANISOU 3100 CA GLN A 281 15363 10339 14895 -166 1430 -474 C
ATOM 3101 C GLN A 281 14.511 178.563 144.776 1.00109.60 C
ANISOU 3101 C GLN A 281 15814 10624 15205 -197 1674 -551 C
ATOM 3102 O GLN A 281 13.280 178.664 144.846 1.00111.32 O
ANISOU 3102 O GLN A 281 15899 10727 15671 -117 1915 -576 O
ATOM 3103 CB GLN A 281 15.611 180.782 144.385 1.00109.21 C
ANISOU 3103 CB GLN A 281 15882 10469 15145 -206 1532 -546 C
ATOM 3104 CG GLN A 281 16.973 180.764 145.052 1.00117.10 C
ANISOU 3104 CG GLN A 281 17181 11499 15812 -357 1378 -572 C
ATOM 3105 CD GLN A 281 17.107 181.597 146.283 1.00129.54 C
ANISOU 3105 CD GLN A 281 19107 12872 17240 -454 1545 -682 C
ATOM 3106 OE1 GLN A 281 16.772 182.789 146.295 1.00127.41 O
ANISOU 3106 OE1 GLN A 281 18847 12460 17103 -407 1667 -717 O
ATOM 3107 NE2 GLN A 281 17.685 180.992 147.324 1.00115.78 N
ANISOU 3107 NE2 GLN A 281 17681 11106 15205 -608 1525 -731 N
ATOM 3108 N LEU A 282 15.236 177.733 145.553 1.00103.17 N
ANISOU 3108 N LEU A 282 15231 9870 14099 -319 1607 -579 N
ATOM 3109 CA LEU A 282 14.685 176.855 146.598 1.00102.55 C
ANISOU 3109 CA LEU A 282 15319 9733 13912 -385 1815 -652 C
ATOM 3110 C LEU A 282 15.134 177.356 147.972 1.00109.22 C
ANISOU 3110 C LEU A 282 16599 10417 14481 -533 1943 -758 C
ATOM 3111 O LEU A 282 16.203 177.972 148.063 1.00109.91 O
ANISOU 3111 O LEU A 282 16846 10506 14407 -609 1750 -746 O
ATOM 3112 CB LEU A 282 15.198 175.418 146.418 1.00 99.75 C
ANISOU 3112 CB LEU A 282 14919 9563 13417 -428 1603 -587 C
ATOM 3113 CG LEU A 282 14.659 174.608 145.266 1.00100.75 C
ANISOU 3113 CG LEU A 282 14693 9833 13754 -319 1509 -498 C
ATOM 3114 CD1 LEU A 282 15.505 173.401 145.053 1.00 98.37 C
ANISOU 3114 CD1 LEU A 282 14390 9701 13285 -373 1268 -437 C
ATOM 3115 CD2 LEU A 282 13.218 174.194 145.497 1.00103.14 C
ANISOU 3115 CD2 LEU A 282 14879 10052 14257 -262 1783 -532 C
ATOM 3116 N SER A 283 14.352 177.073 149.044 1.00106.56 N
ANISOU 3116 N SER A 283 16477 9931 14080 -592 2261 -859 N
ATOM 3117 CA SER A 283 14.722 177.479 150.409 1.00108.25 C
ANISOU 3117 CA SER A 283 17177 9966 13987 -765 2400 -967 C
ATOM 3118 C SER A 283 15.981 176.724 150.803 1.00111.09 C
ANISOU 3118 C SER A 283 17755 10439 14017 -921 2063 -911 C
ATOM 3119 O SER A 283 16.180 175.632 150.266 1.00109.43 O
ANISOU 3119 O SER A 283 17330 10411 13835 -885 1864 -822 O
ATOM 3120 CB SER A 283 13.594 177.171 151.389 1.00114.74 C
ANISOU 3120 CB SER A 283 18180 10607 14809 -801 2831 -1080 C
ATOM 3121 OG SER A 283 13.087 175.855 151.241 1.00124.46 O
ANISOU 3121 OG SER A 283 19240 11953 16096 -773 2839 -1037 O
ATOM 3122 N ARG A 284 16.846 177.271 151.702 1.00108.57 N
ANISOU 3122 N ARG A 284 17849 10002 13401 -1097 1978 -952 N
ATOM 3123 CA ARG A 284 18.055 176.515 152.048 1.00107.93 C
ANISOU 3123 CA ARG A 284 17938 10012 13057 -1248 1615 -871 C
ATOM 3124 C ARG A 284 17.728 175.285 152.874 1.00113.25 C
ANISOU 3124 C ARG A 284 18813 10671 13547 -1353 1692 -890 C
ATOM 3125 O ARG A 284 18.534 174.352 152.892 1.00111.44 O
ANISOU 3125 O ARG A 284 18593 10554 13195 -1429 1383 -796 O
ATOM 3126 CB ARG A 284 19.188 177.339 152.659 1.00110.08 C
ANISOU 3126 CB ARG A 284 18553 10178 13093 -1419 1404 -870 C
ATOM 3127 CG ARG A 284 20.557 176.838 152.151 1.00123.86 C
ANISOU 3127 CG ARG A 284 20159 12091 14812 -1461 933 -721 C
ATOM 3128 CD ARG A 284 21.727 177.732 152.523 1.00142.99 C
ANISOU 3128 CD ARG A 284 22821 14422 17086 -1609 675 -688 C
ATOM 3129 NE ARG A 284 22.079 177.621 153.942 1.00159.34 N
ANISOU 3129 NE ARG A 284 25427 16311 18802 -1862 623 -725 N
ATOM 3130 CZ ARG A 284 23.173 177.026 154.412 1.00172.85 C
ANISOU 3130 CZ ARG A 284 27297 18031 20348 -2033 246 -617 C
ATOM 3131 NH1 ARG A 284 24.058 176.490 153.579 1.00157.48 N
ANISOU 3131 NH1 ARG A 284 24990 16262 18584 -1964 -81 -472 N
ATOM 3132 NH2 ARG A 284 23.402 176.981 155.716 1.00161.61 N
ANISOU 3132 NH2 ARG A 284 26404 16417 18584 -2282 194 -649 N
ATOM 3133 N THR A 285 16.507 175.226 153.464 1.00112.76 N
ANISOU 3133 N THR A 285 18866 10471 13508 -1343 2111 -1001 N
ATOM 3134 CA THR A 285 16.060 174.016 154.162 1.00113.60 C
ANISOU 3134 CA THR A 285 19128 10567 13469 -1429 2220 -1017 C
ATOM 3135 C THR A 285 15.795 172.951 153.103 1.00113.69 C
ANISOU 3135 C THR A 285 18662 10807 13727 -1268 2091 -918 C
ATOM 3136 O THR A 285 16.397 171.883 153.203 1.00113.29 O
ANISOU 3136 O THR A 285 18639 10866 13542 -1339 1841 -840 O
ATOM 3137 CB THR A 285 14.883 174.224 155.144 1.00127.30 C
ANISOU 3137 CB THR A 285 21154 12066 15148 -1487 2730 -1167 C
ATOM 3138 OG1 THR A 285 13.692 174.562 154.430 1.00132.72 O
ANISOU 3138 OG1 THR A 285 21459 12738 16232 -1279 3046 -1204 O
ATOM 3139 CG2 THR A 285 15.191 175.232 156.248 1.00127.04 C
ANISOU 3139 CG2 THR A 285 21672 11784 14815 -1679 2863 -1275 C
ATOM 3140 N THR A 286 14.987 173.255 152.046 1.00106.74 N
ANISOU 3140 N THR A 286 17354 9993 13209 -1062 2218 -906 N
ATOM 3141 CA THR A 286 14.750 172.255 150.995 1.00103.93 C
ANISOU 3141 CA THR A 286 16579 9843 13067 -929 2073 -809 C
ATOM 3142 C THR A 286 16.032 171.941 150.238 1.00105.30 C
ANISOU 3142 C THR A 286 16609 10203 13197 -923 1640 -691 C
ATOM 3143 O THR A 286 16.236 170.782 149.885 1.00104.91 O
ANISOU 3143 O THR A 286 16406 10296 13158 -905 1477 -618 O
ATOM 3144 CB THR A 286 13.578 172.575 150.069 1.00108.52 C
ANISOU 3144 CB THR A 286 16766 10430 14035 -740 2273 -807 C
ATOM 3145 OG1 THR A 286 13.705 173.890 149.535 1.00109.24 O
ANISOU 3145 OG1 THR A 286 16762 10474 14272 -663 2259 -810 O
ATOM 3146 CG2 THR A 286 12.242 172.382 150.746 1.00107.70 C
ANISOU 3146 CG2 THR A 286 16713 10166 14042 -735 2699 -896 C
ATOM 3147 N GLU A 287 16.928 172.933 150.072 1.00 99.92 N
ANISOU 3147 N GLU A 287 15994 9504 12467 -949 1468 -674 N
ATOM 3148 CA GLU A 287 18.228 172.752 149.427 1.00 97.55 C
ANISOU 3148 CA GLU A 287 15572 9346 12145 -956 1087 -564 C
ATOM 3149 C GLU A 287 19.077 171.758 150.233 1.00100.27 C
ANISOU 3149 C GLU A 287 16150 9702 12247 -1115 872 -517 C
ATOM 3150 O GLU A 287 19.752 170.914 149.646 1.00 98.50 O
ANISOU 3150 O GLU A 287 15733 9619 12074 -1089 624 -418 O
ATOM 3151 CB GLU A 287 18.959 174.104 149.251 1.00 99.48 C
ANISOU 3151 CB GLU A 287 15871 9534 12391 -971 982 -562 C
ATOM 3152 CG GLU A 287 18.586 174.857 147.973 1.00111.66 C
ANISOU 3152 CG GLU A 287 17069 11141 14214 -798 1017 -538 C
ATOM 3153 CD GLU A 287 19.465 176.022 147.538 1.00136.93 C
ANISOU 3153 CD GLU A 287 20261 14328 17440 -801 858 -507 C
ATOM 3154 OE1 GLU A 287 20.152 176.613 148.403 1.00134.29 O
ANISOU 3154 OE1 GLU A 287 20232 13876 16916 -938 798 -537 O
ATOM 3155 OE2 GLU A 287 19.431 176.372 146.334 1.00130.69 O1-
ANISOU 3155 OE2 GLU A 287 19174 13628 16853 -677 796 -451 O1-
ATOM 3156 N LYS A 288 18.998 171.829 151.570 1.00 98.39 N
ANISOU 3156 N LYS A 288 16335 9298 11751 -1283 978 -586 N
ATOM 3157 CA LYS A 288 19.716 170.916 152.445 1.00 99.33 C
ANISOU 3157 CA LYS A 288 16727 9392 11623 -1459 766 -535 C
ATOM 3158 C LYS A 288 19.023 169.548 152.503 1.00105.16 C
ANISOU 3158 C LYS A 288 17388 10198 12371 -1435 863 -527 C
ATOM 3159 O LYS A 288 19.701 168.533 152.358 1.00105.32 O
ANISOU 3159 O LYS A 288 17340 10310 12367 -1468 599 -428 O
ATOM 3160 CB LYS A 288 19.903 171.513 153.843 1.00104.18 C
ANISOU 3160 CB LYS A 288 17879 9785 11921 -1679 820 -605 C
ATOM 3161 CG LYS A 288 21.284 172.113 154.061 1.00116.80 C
ANISOU 3161 CG LYS A 288 19631 11338 13410 -1806 462 -530 C
ATOM 3162 CD LYS A 288 21.368 172.847 155.388 1.00131.02 C
ANISOU 3162 CD LYS A 288 22000 12898 14885 -2034 530 -609 C
ATOM 3163 CE LYS A 288 22.665 173.598 155.576 1.00141.41 C
ANISOU 3163 CE LYS A 288 23470 14151 16109 -2171 164 -530 C
ATOM 3164 NZ LYS A 288 22.716 174.270 156.901 1.00151.49 N
ANISOU 3164 NZ LYS A 288 25354 15173 17032 -2420 222 -611 N
ATOM 3165 N GLU A 289 17.677 169.518 152.673 1.00101.90 N
ANISOU 3165 N GLU A 289 16961 9728 12026 -1373 1243 -624 N
ATOM 3166 CA GLU A 289 16.847 168.300 152.720 1.00100.83 C
ANISOU 3166 CA GLU A 289 16739 9644 11929 -1344 1382 -625 C
ATOM 3167 C GLU A 289 17.162 167.396 151.549 1.00100.44 C
ANISOU 3167 C GLU A 289 16281 9806 12074 -1215 1143 -516 C
ATOM 3168 O GLU A 289 17.422 166.221 151.755 1.00100.10 O
ANISOU 3168 O GLU A 289 16269 9818 11947 -1272 996 -458 O
ATOM 3169 CB GLU A 289 15.353 168.654 152.701 1.00103.32 C
ANISOU 3169 CB GLU A 289 16961 9876 12421 -1248 1822 -728 C
ATOM 3170 CG GLU A 289 14.819 169.179 154.022 1.00118.31 C
ANISOU 3170 CG GLU A 289 19303 11535 14114 -1392 2160 -854 C
ATOM 3171 CD GLU A 289 13.458 169.846 153.974 1.00142.32 C
ANISOU 3171 CD GLU A 289 22228 14450 17395 -1284 2619 -959 C
ATOM 3172 OE1 GLU A 289 12.491 169.213 153.490 1.00137.45 O
ANISOU 3172 OE1 GLU A 289 21306 13892 17025 -1168 2776 -945 O
ATOM 3173 OE2 GLU A 289 13.344 170.981 154.492 1.00142.37 O1-
ANISOU 3173 OE2 GLU A 289 22467 14277 17349 -1328 2832 -1053 O1-
ATOM 3174 N LEU A 290 17.211 167.962 150.334 1.00 94.54 N
ANISOU 3174 N LEU A 290 15186 9163 11572 -1057 1091 -486 N
ATOM 3175 CA LEU A 290 17.526 167.241 149.104 1.00 92.28 C
ANISOU 3175 CA LEU A 290 14538 9059 11464 -938 891 -393 C
ATOM 3176 C LEU A 290 18.924 166.637 149.124 1.00 97.47 C
ANISOU 3176 C LEU A 290 15230 9779 12025 -1011 548 -297 C
ATOM 3177 O LEU A 290 19.078 165.476 148.750 1.00 97.11 O
ANISOU 3177 O LEU A 290 15039 9831 12026 -983 436 -236 O
ATOM 3178 CB LEU A 290 17.339 168.144 147.868 1.00 90.69 C
ANISOU 3178 CB LEU A 290 14036 8920 11501 -788 903 -382 C
ATOM 3179 CG LEU A 290 17.669 167.549 146.497 1.00 91.90 C
ANISOU 3179 CG LEU A 290 13858 9241 11818 -680 719 -294 C
ATOM 3180 CD1 LEU A 290 16.721 166.426 146.131 1.00 90.96 C
ANISOU 3180 CD1 LEU A 290 13576 9186 11798 -622 814 -287 C
ATOM 3181 CD2 LEU A 290 17.639 168.612 145.457 1.00 93.83 C
ANISOU 3181 CD2 LEU A 290 13907 9513 12231 -578 703 -279 C
ATOM 3182 N LEU A 291 19.932 167.420 149.533 1.00 95.14 N
ANISOU 3182 N LEU A 291 15110 9415 11623 -1103 381 -276 N
ATOM 3183 CA LEU A 291 21.313 166.963 149.613 1.00 95.45 C
ANISOU 3183 CA LEU A 291 15166 9479 11622 -1181 43 -170 C
ATOM 3184 C LEU A 291 21.426 165.788 150.598 1.00101.36 C
ANISOU 3184 C LEU A 291 16136 10179 12198 -1313 -47 -136 C
ATOM 3185 O LEU A 291 22.029 164.767 150.262 1.00101.22 O
ANISOU 3185 O LEU A 291 15965 10237 12258 -1297 -243 -45 O
ATOM 3186 CB LEU A 291 22.218 168.129 150.023 1.00 97.03 C
ANISOU 3186 CB LEU A 291 15545 9579 11741 -1278 -102 -158 C
ATOM 3187 CG LEU A 291 23.582 167.780 150.599 1.00103.74 C
ANISOU 3187 CG LEU A 291 16534 10376 12508 -1426 -454 -47 C
ATOM 3188 CD1 LEU A 291 24.544 167.364 149.513 1.00102.66 C
ANISOU 3188 CD1 LEU A 291 16037 10356 12613 -1330 -669 64 C
ATOM 3189 CD2 LEU A 291 24.141 168.945 151.373 1.00110.46 C
ANISOU 3189 CD2 LEU A 291 17692 11076 13201 -1575 -547 -62 C
ATOM 3190 N ILE A 292 20.802 165.923 151.786 1.00 98.81 N
ANISOU 3190 N ILE A 292 16179 9719 11647 -1444 119 -213 N
ATOM 3191 CA ILE A 292 20.760 164.905 152.830 1.00 99.31 C
ANISOU 3191 CA ILE A 292 16525 9708 11502 -1595 71 -193 C
ATOM 3192 C ILE A 292 20.078 163.670 152.280 1.00101.76 C
ANISOU 3192 C ILE A 292 16592 10136 11937 -1488 166 -181 C
ATOM 3193 O ILE A 292 20.653 162.591 152.395 1.00102.16 O
ANISOU 3193 O ILE A 292 16630 10215 11970 -1534 -52 -90 O
ATOM 3194 CB ILE A 292 20.097 165.464 154.124 1.00104.95 C
ANISOU 3194 CB ILE A 292 17706 10232 11940 -1755 311 -302 C
ATOM 3195 CG1 ILE A 292 21.128 166.229 155.022 1.00107.59 C
ANISOU 3195 CG1 ILE A 292 18424 10412 12043 -1960 66 -268 C
ATOM 3196 CG2 ILE A 292 19.398 164.366 154.936 1.00105.60 C
ANISOU 3196 CG2 ILE A 292 18004 10260 11861 -1848 462 -329 C
ATOM 3197 CD1 ILE A 292 21.716 167.653 154.533 1.00110.69 C
ANISOU 3197 CD1 ILE A 292 18728 10796 12535 -1916 -22 -272 C
ATOM 3198 N TYR A 293 18.906 163.836 151.604 1.00 96.56 N
ANISOU 3198 N TYR A 293 15713 9539 11436 -1341 462 -259 N
ATOM 3199 CA TYR A 293 18.140 162.739 150.993 1.00 94.43 C
ANISOU 3199 CA TYR A 293 15197 9376 11306 -1237 561 -250 C
ATOM 3200 C TYR A 293 18.878 162.044 149.878 1.00 96.75 C
ANISOU 3200 C TYR A 293 15166 9819 11777 -1133 319 -153 C
ATOM 3201 O TYR A 293 18.719 160.834 149.731 1.00 96.68 O
ANISOU 3201 O TYR A 293 15064 9869 11801 -1116 285 -116 O
ATOM 3202 CB TYR A 293 16.741 163.182 150.540 1.00 95.05 C
ANISOU 3202 CB TYR A 293 15114 9457 11543 -1121 901 -338 C
ATOM 3203 CG TYR A 293 15.800 163.364 151.705 1.00 99.22 C
ANISOU 3203 CG TYR A 293 15947 9825 11926 -1224 1216 -436 C
ATOM 3204 CD1 TYR A 293 15.777 162.451 152.757 1.00103.05 C
ANISOU 3204 CD1 TYR A 293 16725 10238 12191 -1373 1231 -435 C
ATOM 3205 CD2 TYR A 293 14.936 164.448 151.765 1.00101.14 C
ANISOU 3205 CD2 TYR A 293 16193 9972 12264 -1175 1518 -530 C
ATOM 3206 CE1 TYR A 293 14.938 162.629 153.854 1.00106.55 C
ANISOU 3206 CE1 TYR A 293 17490 10515 12481 -1484 1557 -533 C
ATOM 3207 CE2 TYR A 293 14.100 164.645 152.863 1.00104.94 C
ANISOU 3207 CE2 TYR A 293 16972 10278 12623 -1274 1858 -630 C
ATOM 3208 CZ TYR A 293 14.099 163.727 153.904 1.00114.48 C
ANISOU 3208 CZ TYR A 293 18496 11416 13587 -1433 1888 -636 C
ATOM 3209 OH TYR A 293 13.270 163.894 154.986 1.00118.80 O
ANISOU 3209 OH TYR A 293 19367 11774 13999 -1544 2259 -741 O
ATOM 3210 N LEU A 294 19.696 162.794 149.105 1.00 92.78 N
ANISOU 3210 N LEU A 294 14505 9362 11387 -1071 169 -115 N
ATOM 3211 CA LEU A 294 20.512 162.248 148.022 1.00 91.45 C
ANISOU 3211 CA LEU A 294 14052 9307 11389 -982 -27 -30 C
ATOM 3212 C LEU A 294 21.692 161.482 148.608 1.00 94.96 C
ANISOU 3212 C LEU A 294 14600 9709 11772 -1088 -303 67 C
ATOM 3213 O LEU A 294 21.988 160.377 148.153 1.00 94.13 O
ANISOU 3213 O LEU A 294 14336 9663 11765 -1045 -397 127 O
ATOM 3214 CB LEU A 294 21.005 163.329 147.048 1.00 90.93 C
ANISOU 3214 CB LEU A 294 13803 9285 11463 -894 -69 -21 C
ATOM 3215 CG LEU A 294 21.666 162.747 145.795 1.00 95.20 C
ANISOU 3215 CG LEU A 294 14054 9932 12186 -796 -190 48 C
ATOM 3216 CD1 LEU A 294 20.672 162.600 144.647 1.00 94.20 C
ANISOU 3216 CD1 LEU A 294 13711 9899 12180 -670 -30 13 C
ATOM 3217 CD2 LEU A 294 22.887 163.518 145.418 1.00 98.79 C
ANISOU 3217 CD2 LEU A 294 14440 10374 12721 -798 -352 103 C
ATOM 3218 N ARG A 295 22.350 162.065 149.635 1.00 91.33 N
ANISOU 3218 N ARG A 295 14417 9127 11157 -1234 -440 88 N
ATOM 3219 CA ARG A 295 23.468 161.445 150.349 1.00 90.49 C
ANISOU 3219 CA ARG A 295 14443 8943 10998 -1365 -746 200 C
ATOM 3220 C ARG A 295 23.043 160.072 150.912 1.00 93.95 C
ANISOU 3220 C ARG A 295 14985 9366 11344 -1421 -745 221 C
ATOM 3221 O ARG A 295 23.847 159.139 150.923 1.00 94.00 O
ANISOU 3221 O ARG A 295 14921 9361 11433 -1448 -980 330 O
ATOM 3222 CB ARG A 295 23.989 162.377 151.452 1.00 86.33 C
ANISOU 3222 CB ARG A 295 14261 8265 10275 -1541 -877 208 C
ATOM 3223 CG ARG A 295 25.007 163.390 150.980 1.00 84.10 C
ANISOU 3223 CG ARG A 295 13852 7975 10125 -1523 -1041 257 C
ATOM 3224 CD ARG A 295 25.632 164.049 152.193 1.00108.14 C
ANISOU 3224 CD ARG A 295 17276 10850 12962 -1736 -1243 292 C
ATOM 3225 NE ARG A 295 26.147 165.393 151.920 1.00121.13 N
ANISOU 3225 NE ARG A 295 18897 12468 14661 -1733 -1289 283 N
ATOM 3226 CZ ARG A 295 27.412 165.670 151.620 1.00135.69 C
ANISOU 3226 CZ ARG A 295 20588 14289 16678 -1755 -1578 402 C
ATOM 3227 NH1 ARG A 295 28.308 164.692 151.519 1.00128.47 N
ANISOU 3227 NH1 ARG A 295 19508 13371 15934 -1769 -1839 540 N
ATOM 3228 NH2 ARG A 295 27.785 166.918 151.380 1.00117.52 N
ANISOU 3228 NH2 ARG A 295 18278 11960 14414 -1757 -1596 386 N
ATOM 3229 N VAL A 296 21.760 159.952 151.322 1.00 89.77 N
ANISOU 3229 N VAL A 296 14601 8830 10678 -1431 -466 120 N
ATOM 3230 CA VAL A 296 21.151 158.718 151.824 1.00 90.01 C
ANISOU 3230 CA VAL A 296 14736 8849 10616 -1481 -405 122 C
ATOM 3231 C VAL A 296 21.048 157.714 150.662 1.00 94.52 C
ANISOU 3231 C VAL A 296 14939 9558 11416 -1324 -403 155 C
ATOM 3232 O VAL A 296 21.488 156.577 150.811 1.00 94.79 O
ANISOU 3232 O VAL A 296 14960 9585 11472 -1356 -566 235 O
ATOM 3233 CB VAL A 296 19.769 158.988 152.485 1.00 93.68 C
ANISOU 3233 CB VAL A 296 15426 9255 10915 -1527 -58 -1 C
ATOM 3234 CG1 VAL A 296 19.033 157.691 152.811 1.00 93.11 C
ANISOU 3234 CG1 VAL A 296 15402 9188 10789 -1557 43 -2 C
ATOM 3235 CG2 VAL A 296 19.906 159.855 153.730 1.00 95.26 C
ANISOU 3235 CG2 VAL A 296 16061 9286 10848 -1711 -42 -40 C
ATOM 3236 N ALA A 297 20.490 158.151 149.507 1.00 90.50 N
ANISOU 3236 N ALA A 297 14152 9158 11074 -1164 -232 98 N
ATOM 3237 CA ALA A 297 20.325 157.345 148.291 1.00 89.03 C
ANISOU 3237 CA ALA A 297 13651 9093 11083 -1026 -211 115 C
ATOM 3238 C ALA A 297 21.656 156.817 147.804 1.00 93.54 C
ANISOU 3238 C ALA A 297 14072 9678 11792 -1002 -461 217 C
ATOM 3239 O ALA A 297 21.724 155.671 147.371 1.00 94.17 O
ANISOU 3239 O ALA A 297 14025 9795 11959 -959 -495 253 O
ATOM 3240 CB ALA A 297 19.663 158.163 147.200 1.00 88.72 C
ANISOU 3240 CB ALA A 297 13399 9135 11175 -896 -42 53 C
ATOM 3241 N THR A 298 22.725 157.623 147.934 1.00 90.31 N
ANISOU 3241 N THR A 298 13681 9218 11413 -1038 -631 267 N
ATOM 3242 CA THR A 298 24.096 157.243 147.589 1.00 90.53 C
ANISOU 3242 CA THR A 298 13557 9222 11618 -1026 -868 377 C
ATOM 3243 C THR A 298 24.464 155.915 148.278 1.00 94.83 C
ANISOU 3243 C THR A 298 14181 9697 12152 -1105 -1037 464 C
ATOM 3244 O THR A 298 25.103 155.049 147.676 1.00 94.53 O
ANISOU 3244 O THR A 298 13940 9664 12314 -1043 -1129 533 O
ATOM 3245 CB THR A 298 25.064 158.378 147.969 1.00101.55 C
ANISOU 3245 CB THR A 298 15021 10542 13022 -1095 -1034 422 C
ATOM 3246 OG1 THR A 298 24.801 159.514 147.144 1.00104.00 O
ANISOU 3246 OG1 THR A 298 15217 10921 13379 -1004 -879 351 O
ATOM 3247 CG2 THR A 298 26.529 157.978 147.855 1.00 99.08 C
ANISOU 3247 CG2 THR A 298 14555 10165 12927 -1108 -1299 557 C
ATOM 3248 N TRP A 299 23.994 155.737 149.510 1.00 91.64 N
ANISOU 3248 N TRP A 299 14085 9218 11517 -1243 -1054 455 N
ATOM 3249 CA TRP A 299 24.270 154.540 150.287 1.00 92.16 C
ANISOU 3249 CA TRP A 299 14281 9201 11536 -1343 -1229 542 C
ATOM 3250 C TRP A 299 23.732 153.252 149.684 1.00 92.78 C
ANISOU 3250 C TRP A 299 14196 9351 11707 -1251 -1122 531 C
ATOM 3251 O TRP A 299 24.326 152.198 149.908 1.00 93.71 O
ANISOU 3251 O TRP A 299 14291 9407 11908 -1283 -1305 630 O
ATOM 3252 CB TRP A 299 23.801 154.717 151.718 1.00 92.35 C
ANISOU 3252 CB TRP A 299 14723 9117 11250 -1531 -1239 523 C
ATOM 3253 CG TRP A 299 24.878 155.340 152.533 1.00 94.45 C
ANISOU 3253 CG TRP A 299 15184 9247 11455 -1681 -1536 619 C
ATOM 3254 CD1 TRP A 299 25.111 156.668 152.711 1.00 97.32 C
ANISOU 3254 CD1 TRP A 299 15653 9575 11748 -1726 -1543 585 C
ATOM 3255 CD2 TRP A 299 25.969 154.651 153.144 1.00 96.01 C
ANISOU 3255 CD2 TRP A 299 15448 9319 11713 -1799 -1906 782 C
ATOM 3256 NE1 TRP A 299 26.243 156.847 153.464 1.00 98.55 N
ANISOU 3256 NE1 TRP A 299 15972 9589 11885 -1884 -1900 715 N
ATOM 3257 CE2 TRP A 299 26.796 155.624 153.738 1.00101.09 C
ANISOU 3257 CE2 TRP A 299 16261 9849 12299 -1931 -2140 845 C
ATOM 3258 CE3 TRP A 299 26.296 153.291 153.304 1.00 97.88 C
ANISOU 3258 CE3 TRP A 299 15632 9510 12046 -1818 -2075 888 C
ATOM 3259 CZ2 TRP A 299 27.941 155.284 154.467 1.00102.80 C
ANISOU 3259 CZ2 TRP A 299 16585 9906 12570 -2086 -2560 1023 C
ATOM 3260 CZ3 TRP A 299 27.423 152.954 154.037 1.00101.39 C
ANISOU 3260 CZ3 TRP A 299 16178 9794 12551 -1962 -2478 1062 C
ATOM 3261 CH2 TRP A 299 28.241 153.942 154.595 1.00103.58 C
ANISOU 3261 CH2 TRP A 299 16609 9959 12789 -2096 -2729 1134 C
ATOM 3262 N ASN A 300 22.670 153.329 148.882 1.00 84.37 N
ANISOU 3262 N ASN A 300 13003 8402 10653 -1138 -851 425 N
ATOM 3263 CA ASN A 300 22.154 152.139 148.246 1.00 82.16 C
ANISOU 3263 CA ASN A 300 12573 8186 10459 -1059 -758 414 C
ATOM 3264 C ASN A 300 23.266 151.529 147.348 1.00 86.19 C
ANISOU 3264 C ASN A 300 12828 8694 11225 -970 -897 493 C
ATOM 3265 O ASN A 300 23.549 150.338 147.466 1.00 86.69 O
ANISOU 3265 O ASN A 300 12868 8712 11358 -982 -992 556 O
ATOM 3266 CB ASN A 300 20.876 152.475 147.496 1.00 78.53 C
ANISOU 3266 CB ASN A 300 12015 7834 9991 -968 -485 302 C
ATOM 3267 CG ASN A 300 20.305 151.374 146.653 1.00101.54 C
ANISOU 3267 CG ASN A 300 14764 10816 13000 -888 -395 287 C
ATOM 3268 OD1 ASN A 300 19.496 150.557 147.103 1.00100.99 O
ANISOU 3268 OD1 ASN A 300 14784 10739 12848 -931 -319 272 O
ATOM 3269 ND2 ASN A 300 20.626 151.404 145.369 1.00 90.09 N
ANISOU 3269 ND2 ASN A 300 13088 9428 11713 -776 -380 283 N
ATOM 3270 N GLN A 301 23.976 152.368 146.564 1.00 81.70 N
ANISOU 3270 N GLN A 301 12088 8149 10804 -896 -910 497 N
ATOM 3271 CA GLN A 301 25.054 151.944 145.661 1.00 81.07 C
ANISOU 3271 CA GLN A 301 11764 8047 10990 -811 -983 560 C
ATOM 3272 C GLN A 301 26.292 151.389 146.382 1.00 89.65 C
ANISOU 3272 C GLN A 301 12852 8995 12219 -882 -1257 700 C
ATOM 3273 O GLN A 301 27.088 150.666 145.768 1.00 90.13 O
ANISOU 3273 O GLN A 301 12707 9005 12532 -813 -1298 762 O
ATOM 3274 CB GLN A 301 25.439 153.068 144.698 1.00 81.11 C
ANISOU 3274 CB GLN A 301 11617 8100 11100 -732 -905 527 C
ATOM 3275 CG GLN A 301 24.372 153.387 143.657 1.00 91.04 C
ANISOU 3275 CG GLN A 301 12812 9480 12301 -645 -666 418 C
ATOM 3276 CD GLN A 301 23.124 154.020 144.233 1.00106.16 C
ANISOU 3276 CD GLN A 301 14892 11443 14002 -687 -560 341 C
ATOM 3277 OE1 GLN A 301 22.004 153.580 143.981 1.00103.75 O
ANISOU 3277 OE1 GLN A 301 14595 11196 13631 -664 -421 283 O
ATOM 3278 NE2 GLN A 301 23.285 155.029 145.061 1.00 95.29 N
ANISOU 3278 NE2 GLN A 301 13655 10024 12528 -757 -619 342 N
ATOM 3279 N ILE A 302 26.449 151.718 147.683 1.00 88.59 N
ANISOU 3279 N ILE A 302 12957 8776 11928 -1027 -1446 756 N
ATOM 3280 CA ILE A 302 27.543 151.228 148.536 1.00 90.10 C
ANISOU 3280 CA ILE A 302 13194 8811 12231 -1131 -1768 912 C
ATOM 3281 C ILE A 302 27.110 149.914 149.249 1.00 96.35 C
ANISOU 3281 C ILE A 302 14135 9550 12924 -1202 -1836 952 C
ATOM 3282 O ILE A 302 27.931 148.999 149.391 1.00 98.30 O
ANISOU 3282 O ILE A 302 14281 9686 13381 -1211 -2037 1077 O
ATOM 3283 CB ILE A 302 28.008 152.327 149.545 1.00 93.69 C
ANISOU 3283 CB ILE A 302 13870 9179 12551 -1281 -1975 963 C
ATOM 3284 CG1 ILE A 302 28.651 153.523 148.824 1.00 92.70 C
ANISOU 3284 CG1 ILE A 302 13559 9080 12581 -1212 -1952 952 C
ATOM 3285 CG2 ILE A 302 28.956 151.758 150.609 1.00 96.68 C
ANISOU 3285 CG2 ILE A 302 14367 9377 12989 -1432 -2355 1138 C
ATOM 3286 CD1 ILE A 302 28.619 154.789 149.610 1.00 98.56 C
ANISOU 3286 CD1 ILE A 302 14551 9788 13110 -1336 -2028 933 C
ATOM 3287 N LEU A 303 25.824 149.834 149.692 1.00 91.25 N
ANISOU 3287 N LEU A 303 13718 8970 11984 -1251 -1660 851 N
ATOM 3288 CA LEU A 303 25.263 148.710 150.448 1.00 90.88 C
ANISOU 3288 CA LEU A 303 13859 8878 11795 -1337 -1690 875 C
ATOM 3289 C LEU A 303 24.780 147.524 149.608 1.00 95.40 C
ANISOU 3289 C LEU A 303 14240 9516 12491 -1217 -1535 840 C
ATOM 3290 O LEU A 303 24.815 146.400 150.115 1.00 96.16 O
ANISOU 3290 O LEU A 303 14408 9536 12593 -1273 -1651 912 O
ATOM 3291 CB LEU A 303 24.149 149.181 151.381 1.00 90.59 C
ANISOU 3291 CB LEU A 303 14163 8852 11404 -1460 -1549 786 C
ATOM 3292 CG LEU A 303 24.558 150.206 152.432 1.00 96.14 C
ANISOU 3292 CG LEU A 303 15157 9453 11919 -1622 -1706 819 C
ATOM 3293 CD1 LEU A 303 23.347 150.789 153.114 1.00 96.91 C
ANISOU 3293 CD1 LEU A 303 15562 9563 11696 -1711 -1458 695 C
ATOM 3294 CD2 LEU A 303 25.569 149.643 153.427 1.00 98.63 C
ANISOU 3294 CD2 LEU A 303 15645 9593 12236 -1785 -2096 991 C
ATOM 3295 N ASP A 304 24.321 147.748 148.354 1.00 91.00 N
ANISOU 3295 N ASP A 304 13466 9086 12023 -1069 -1291 736 N
ATOM 3296 CA ASP A 304 23.906 146.635 147.498 1.00 90.27 C
ANISOU 3296 CA ASP A 304 13215 9043 12041 -969 -1156 702 C
ATOM 3297 C ASP A 304 25.075 145.626 147.352 1.00 95.99 C
ANISOU 3297 C ASP A 304 13787 9649 13038 -937 -1337 821 C
ATOM 3298 O ASP A 304 24.830 144.469 147.679 1.00 97.02 O
ANISOU 3298 O ASP A 304 13972 9733 13157 -966 -1373 854 O
ATOM 3299 CB ASP A 304 23.399 147.090 146.119 1.00 90.97 C
ANISOU 3299 CB ASP A 304 13118 9258 12188 -837 -917 592 C
ATOM 3300 CG ASP A 304 22.098 147.872 146.078 1.00107.37 C
ANISOU 3300 CG ASP A 304 15285 11442 14069 -844 -720 481 C
ATOM 3301 OD1 ASP A 304 21.157 147.512 146.829 1.00111.16 O
ANISOU 3301 OD1 ASP A 304 15932 11923 14380 -919 -659 455 O
ATOM 3302 OD2 ASP A 304 21.987 148.790 145.233 1.00110.97 O1-
ANISOU 3302 OD2 ASP A 304 15631 11970 14563 -772 -613 423 O1-
ATOM 3303 N PRO A 305 26.356 146.002 147.010 1.00 92.64 N
ANISOU 3303 N PRO A 305 13178 9148 12873 -892 -1464 900 N
ATOM 3304 CA PRO A 305 27.420 144.977 146.942 1.00 92.83 C
ANISOU 3304 CA PRO A 305 13039 9027 13205 -861 -1621 1023 C
ATOM 3305 C PRO A 305 27.626 144.195 148.229 1.00 96.94 C
ANISOU 3305 C PRO A 305 13739 9419 13676 -995 -1895 1151 C
ATOM 3306 O PRO A 305 27.922 143.003 148.160 1.00 97.06 O
ANISOU 3306 O PRO A 305 13670 9344 13866 -967 -1950 1216 O
ATOM 3307 CB PRO A 305 28.675 145.766 146.560 1.00 95.58 C
ANISOU 3307 CB PRO A 305 13183 9305 13830 -819 -1717 1094 C
ATOM 3308 CG PRO A 305 28.356 147.184 146.816 1.00100.26 C
ANISOU 3308 CG PRO A 305 13902 9984 14207 -871 -1699 1036 C
ATOM 3309 CD PRO A 305 26.883 147.326 146.603 1.00 94.27 C
ANISOU 3309 CD PRO A 305 13292 9384 13143 -859 -1452 884 C
ATOM 3310 N TRP A 306 27.391 144.838 149.391 1.00 94.32 N
ANISOU 3310 N TRP A 306 13687 9069 13082 -1150 -2048 1179 N
ATOM 3311 CA TRP A 306 27.525 144.218 150.715 1.00 95.98 C
ANISOU 3311 CA TRP A 306 14150 9144 13172 -1320 -2326 1302 C
ATOM 3312 C TRP A 306 26.431 143.249 151.046 1.00 99.49 C
ANISOU 3312 C TRP A 306 14776 9628 13398 -1361 -2202 1247 C
ATOM 3313 O TRP A 306 26.716 142.259 151.718 1.00100.89 O
ANISOU 3313 O TRP A 306 15052 9677 13605 -1446 -2412 1365 O
ATOM 3314 CB TRP A 306 27.682 145.251 151.813 1.00 95.94 C
ANISOU 3314 CB TRP A 306 14429 9085 12938 -1492 -2519 1345 C
ATOM 3315 CG TRP A 306 29.078 145.772 151.829 1.00 98.24 C
ANISOU 3315 CG TRP A 306 14558 9254 13515 -1504 -2801 1486 C
ATOM 3316 CD1 TRP A 306 29.521 146.932 151.273 1.00100.37 C
ANISOU 3316 CD1 TRP A 306 14674 9572 13889 -1440 -2746 1450 C
ATOM 3317 CD2 TRP A 306 30.248 145.054 152.253 1.00100.49 C
ANISOU 3317 CD2 TRP A 306 14745 9340 14096 -1559 -3167 1693 C
ATOM 3318 NE1 TRP A 306 30.885 147.026 151.403 1.00101.91 N
ANISOU 3318 NE1 TRP A 306 14698 9610 14413 -1466 -3056 1621 N
ATOM 3319 CE2 TRP A 306 31.361 145.882 151.994 1.00105.19 C
ANISOU 3319 CE2 TRP A 306 15132 9866 14970 -1536 -3325 1778 C
ATOM 3320 CE3 TRP A 306 30.457 143.824 152.908 1.00103.46 C
ANISOU 3320 CE3 TRP A 306 15203 9572 14533 -1640 -3401 1829 C
ATOM 3321 CZ2 TRP A 306 32.669 145.510 152.341 1.00106.84 C
ANISOU 3321 CZ2 TRP A 306 15182 9862 15551 -1587 -3707 1999 C
ATOM 3322 CZ3 TRP A 306 31.750 143.468 153.270 1.00107.16 C
ANISOU 3322 CZ3 TRP A 306 15531 9828 15356 -1693 -3794 2050 C
ATOM 3323 CH2 TRP A 306 32.839 144.297 152.972 1.00108.47 C
ANISOU 3323 CH2 TRP A 306 15459 9924 15831 -1662 -3942 2136 C
ATOM 3324 N VAL A 307 25.192 143.483 150.552 1.00 93.77 N
ANISOU 3324 N VAL A 307 14079 9064 12484 -1302 -1876 1082 N
ATOM 3325 CA VAL A 307 24.110 142.513 150.725 1.00 92.97 C
ANISOU 3325 CA VAL A 307 14101 9000 12222 -1329 -1732 1028 C
ATOM 3326 C VAL A 307 24.596 141.205 150.075 1.00 97.14 C
ANISOU 3326 C VAL A 307 14409 9469 13029 -1231 -1774 1088 C
ATOM 3327 O VAL A 307 24.532 140.163 150.709 1.00 97.70 O
ANISOU 3327 O VAL A 307 14600 9449 13072 -1307 -1897 1164 O
ATOM 3328 CB VAL A 307 22.753 142.984 150.160 1.00 94.70 C
ANISOU 3328 CB VAL A 307 14323 9386 12272 -1271 -1389 858 C
ATOM 3329 CG1 VAL A 307 21.713 141.870 150.227 1.00 94.31 C
ANISOU 3329 CG1 VAL A 307 14344 9363 12127 -1289 -1252 818 C
ATOM 3330 CG2 VAL A 307 22.258 144.215 150.902 1.00 94.69 C
ANISOU 3330 CG2 VAL A 307 14555 9409 12015 -1372 -1325 801 C
ATOM 3331 N TYR A 308 25.190 141.280 148.876 1.00 93.17 N
ANISOU 3331 N TYR A 308 13605 8993 12803 -1074 -1685 1063 N
ATOM 3332 CA TYR A 308 25.725 140.085 148.243 1.00 93.93 C
ANISOU 3332 CA TYR A 308 13500 9003 13184 -980 -1693 1112 C
ATOM 3333 C TYR A 308 26.905 139.497 148.983 1.00101.73 C
ANISOU 3333 C TYR A 308 14461 9790 14402 -1037 -2021 1299 C
ATOM 3334 O TYR A 308 26.995 138.278 149.075 1.00102.45 O
ANISOU 3334 O TYR A 308 14532 9785 14611 -1033 -2082 1360 O
ATOM 3335 CB TYR A 308 26.106 140.327 146.784 1.00 94.05 C
ANISOU 3335 CB TYR A 308 13237 9064 13434 -816 -1492 1038 C
ATOM 3336 CG TYR A 308 26.657 139.086 146.113 1.00 96.55 C
ANISOU 3336 CG TYR A 308 13370 9266 14047 -721 -1454 1074 C
ATOM 3337 CD1 TYR A 308 25.885 137.935 145.984 1.00 97.92 C
ANISOU 3337 CD1 TYR A 308 13615 9450 14141 -721 -1357 1032 C
ATOM 3338 CD2 TYR A 308 27.964 139.048 145.643 1.00 98.81 C
ANISOU 3338 CD2 TYR A 308 13412 9417 14715 -637 -1506 1153 C
ATOM 3339 CE1 TYR A 308 26.390 136.791 145.373 1.00 99.01 C
ANISOU 3339 CE1 TYR A 308 13604 9465 14550 -637 -1307 1057 C
ATOM 3340 CE2 TYR A 308 28.485 137.904 145.045 1.00100.52 C
ANISOU 3340 CE2 TYR A 308 13462 9500 15230 -547 -1436 1182 C
ATOM 3341 CZ TYR A 308 27.694 136.778 144.913 1.00107.41 C
ANISOU 3341 CZ TYR A 308 14430 10385 15996 -547 -1336 1129 C
ATOM 3342 OH TYR A 308 28.203 135.666 144.295 1.00111.95 O
ANISOU 3342 OH TYR A 308 14857 10815 16865 -458 -1245 1146 O
ATOM 3343 N ILE A 309 27.835 140.345 149.456 1.00100.37 N
ANISOU 3343 N ILE A 309 14273 9540 14324 -1091 -2245 1399 N
ATOM 3344 CA ILE A 309 29.038 139.887 150.167 1.00102.58 C
ANISOU 3344 CA ILE A 309 14503 9604 14869 -1158 -2612 1606 C
ATOM 3345 C ILE A 309 28.667 139.174 151.475 1.00107.04 C
ANISOU 3345 C ILE A 309 15388 10078 15205 -1338 -2850 1703 C
ATOM 3346 O ILE A 309 29.191 138.102 151.732 1.00107.90 O
ANISOU 3346 O ILE A 309 15433 10029 15534 -1348 -3041 1836 O
ATOM 3347 CB ILE A 309 30.073 141.044 150.406 1.00106.60 C
ANISOU 3347 CB ILE A 309 14933 10047 15525 -1196 -2821 1698 C
ATOM 3348 CG1 ILE A 309 30.589 141.662 149.076 1.00105.88 C
ANISOU 3348 CG1 ILE A 309 14503 10012 15715 -1017 -2587 1621 C
ATOM 3349 CG2 ILE A 309 31.248 140.562 151.270 1.00109.73 C
ANISOU 3349 CG2 ILE A 309 15299 10199 16195 -1297 -3261 1939 C
ATOM 3350 CD1 ILE A 309 30.985 143.221 149.144 1.00109.41 C
ANISOU 3350 CD1 ILE A 309 14947 10504 16121 -1052 -2642 1614 C
ATOM 3351 N LEU A 310 27.745 139.756 152.269 1.00102.89 N
ANISOU 3351 N LEU A 310 15210 9638 14245 -1482 -2817 1635 N
ATOM 3352 CA LEU A 310 27.351 139.279 153.598 1.00103.70 C
ANISOU 3352 CA LEU A 310 15692 9650 14062 -1688 -3018 1716 C
ATOM 3353 C LEU A 310 26.202 138.256 153.643 1.00109.25 C
ANISOU 3353 C LEU A 310 16527 10413 14569 -1696 -2812 1634 C
ATOM 3354 O LEU A 310 26.283 137.309 154.426 1.00110.18 O
ANISOU 3354 O LEU A 310 16817 10398 14649 -1812 -3020 1752 O
ATOM 3355 CB LEU A 310 27.022 140.475 154.510 1.00103.26 C
ANISOU 3355 CB LEU A 310 15981 9616 13637 -1860 -3066 1685 C
ATOM 3356 CG LEU A 310 28.106 141.552 154.709 1.00107.22 C
ANISOU 3356 CG LEU A 310 16433 10039 14267 -1903 -3317 1779 C
ATOM 3357 CD1 LEU A 310 27.755 142.436 155.872 1.00107.95 C
ANISOU 3357 CD1 LEU A 310 16967 10103 13947 -2122 -3404 1766 C
ATOM 3358 CD2 LEU A 310 29.495 140.953 154.941 1.00110.30 C
ANISOU 3358 CD2 LEU A 310 16657 10213 15041 -1931 -3738 2013 C
ATOM 3359 N PHE A 311 25.130 138.454 152.838 1.00105.61 N
ANISOU 3359 N PHE A 311 15996 10141 13990 -1588 -2427 1445 N
ATOM 3360 CA PHE A 311 23.954 137.568 152.783 1.00104.86 C
ANISOU 3360 CA PHE A 311 15997 10116 13730 -1591 -2208 1358 C
ATOM 3361 C PHE A 311 24.260 136.322 151.946 1.00107.07 C
ANISOU 3361 C PHE A 311 16016 10351 14314 -1457 -2189 1387 C
ATOM 3362 O PHE A 311 23.649 136.101 150.897 1.00104.50 O
ANISOU 3362 O PHE A 311 15521 10143 14042 -1327 -1916 1261 O
ATOM 3363 CB PHE A 311 22.712 138.320 152.251 1.00105.05 C
ANISOU 3363 CB PHE A 311 16026 10335 13554 -1537 -1840 1166 C
ATOM 3364 CG PHE A 311 22.070 139.321 153.184 1.00107.94 C
ANISOU 3364 CG PHE A 311 16700 10729 13582 -1681 -1772 1112 C
ATOM 3365 CD1 PHE A 311 22.825 140.322 153.788 1.00112.97 C
ANISOU 3365 CD1 PHE A 311 17462 11300 14163 -1767 -1962 1172 C
ATOM 3366 CD2 PHE A 311 20.698 139.313 153.397 1.00110.57 C
ANISOU 3366 CD2 PHE A 311 17188 11146 13678 -1727 -1493 996 C
ATOM 3367 CE1 PHE A 311 22.226 141.258 154.633 1.00115.05 C
ANISOU 3367 CE1 PHE A 311 18038 11570 14105 -1905 -1867 1108 C
ATOM 3368 CE2 PHE A 311 20.098 140.253 154.240 1.00114.67 C
ANISOU 3368 CE2 PHE A 311 17990 11667 13912 -1855 -1377 935 C
ATOM 3369 CZ PHE A 311 20.865 141.223 154.847 1.00114.09 C
ANISOU 3369 CZ PHE A 311 18070 11521 13757 -1943 -1556 985 C
ATOM 3370 N ARG A 312 25.227 135.518 152.423 1.00105.10 N
ANISOU 3370 N ARG A 312 15748 9912 14273 -1499 -2494 1561 N
ATOM 3371 CA ARG A 312 25.692 134.289 151.782 1.00105.21 C
ANISOU 3371 CA ARG A 312 15529 9830 14616 -1384 -2509 1613 C
ATOM 3372 C ARG A 312 25.840 133.173 152.802 1.00112.64 C
ANISOU 3372 C ARG A 312 16657 10599 15541 -1517 -2779 1769 C
ATOM 3373 O ARG A 312 26.239 133.435 153.945 1.00113.23 O
ANISOU 3373 O ARG A 312 16962 10561 15500 -1687 -3084 1904 O
ATOM 3374 CB ARG A 312 27.021 134.527 151.067 1.00103.45 C
ANISOU 3374 CB ARG A 312 14966 9511 14829 -1248 -2599 1685 C
ATOM 3375 CG ARG A 312 26.884 134.982 149.619 1.00 99.53 C
ANISOU 3375 CG ARG A 312 14214 9151 14453 -1065 -2257 1523 C
ATOM 3376 CD ARG A 312 28.199 135.534 149.097 1.00105.79 C
ANISOU 3376 CD ARG A 312 14718 9850 15629 -963 -2328 1591 C
ATOM 3377 NE ARG A 312 29.338 134.646 149.343 1.00118.10 N
ANISOU 3377 NE ARG A 312 16107 11168 17598 -943 -2574 1774 N
ATOM 3378 CZ ARG A 312 30.476 135.020 149.922 1.00133.44 C
ANISOU 3378 CZ ARG A 312 17960 12951 19790 -994 -2894 1951 C
ATOM 3379 NH1 ARG A 312 30.657 136.278 150.293 1.00113.70 N
ANISOU 3379 NH1 ARG A 312 15539 10514 17149 -1068 -2999 1959 N
ATOM 3380 NH2 ARG A 312 31.455 134.144 150.100 1.00131.67 N
ANISOU 3380 NH2 ARG A 312 17551 12490 19987 -968 -3115 2126 N
ATOM 3381 N ARG A 313 25.516 131.924 152.385 1.00111.11 N
ANISOU 3381 N ARG A 313 16388 10374 15457 -1451 -2677 1753 N
ATOM 3382 CA ARG A 313 25.578 130.731 153.241 1.00114.01 C
ANISOU 3382 CA ARG A 313 16918 10574 15826 -1564 -2909 1895 C
ATOM 3383 C ARG A 313 26.997 130.479 153.767 1.00122.04 C
ANISOU 3383 C ARG A 313 17835 11348 17186 -1594 -3323 2126 C
ATOM 3384 O ARG A 313 27.149 130.061 154.914 1.00123.71 O
ANISOU 3384 O ARG A 313 18299 11413 17292 -1772 -3640 2285 O
ATOM 3385 CB ARG A 313 24.996 129.488 152.533 1.00115.12 C
ANISOU 3385 CB ARG A 313 16958 10727 16054 -1466 -2696 1821 C
ATOM 3386 CG ARG A 313 23.466 129.474 152.422 1.00128.67 C
ANISOU 3386 CG ARG A 313 18855 12632 17403 -1508 -2390 1652 C
ATOM 3387 CD ARG A 313 22.835 128.567 153.473 1.00145.81 C
ANISOU 3387 CD ARG A 313 21331 14726 19343 -1680 -2496 1723 C
ATOM 3388 NE ARG A 313 21.380 128.737 153.589 1.00150.71 N
ANISOU 3388 NE ARG A 313 22143 15510 19610 -1753 -2216 1579 N
ATOM 3389 CZ ARG A 313 20.617 128.100 154.477 1.00160.75 C
ANISOU 3389 CZ ARG A 313 23707 16744 20628 -1916 -2225 1609 C
ATOM 3390 NH1 ARG A 313 21.158 127.244 155.336 1.00151.75 N
ANISOU 3390 NH1 ARG A 313 22732 15414 19513 -2032 -2522 1779 N
ATOM 3391 NH2 ARG A 313 19.309 128.316 154.513 1.00140.73 N
ANISOU 3391 NH2 ARG A 313 21296 14346 17828 -1969 -1938 1476 N
ATOM 3392 N ALA A 314 28.028 130.792 152.949 1.00119.60 N
ANISOU 3392 N ALA A 314 17166 10984 17291 -1435 -3324 2152 N
ATOM 3393 CA ALA A 314 29.442 130.660 153.312 1.00122.11 C
ANISOU 3393 CA ALA A 314 17308 11060 18028 -1442 -3701 2377 C
ATOM 3394 C ALA A 314 29.821 131.600 154.462 1.00128.62 C
ANISOU 3394 C ALA A 314 18375 11833 18662 -1641 -4053 2506 C
ATOM 3395 O ALA A 314 30.632 131.212 155.298 1.00131.09 O
ANISOU 3395 O ALA A 314 18733 11920 19155 -1756 -4478 2735 O
ATOM 3396 CB ALA A 314 30.322 130.936 152.102 1.00122.36 C
ANISOU 3396 CB ALA A 314 16905 11064 18523 -1226 -3534 2343 C
ATOM 3397 N VAL A 315 29.235 132.831 154.501 1.00125.00 N
ANISOU 3397 N VAL A 315 18084 11568 17845 -1690 -3888 2365 N
ATOM 3398 CA VAL A 315 29.474 133.868 155.533 1.00126.07 C
ANISOU 3398 CA VAL A 315 18500 11671 17731 -1888 -4162 2447 C
ATOM 3399 C VAL A 315 28.874 133.423 156.857 1.00134.95 C
ANISOU 3399 C VAL A 315 20106 12722 18447 -2137 -4359 2522 C
ATOM 3400 O VAL A 315 29.531 133.515 157.895 1.00137.56 O
ANISOU 3400 O VAL A 315 20652 12867 18746 -2331 -4789 2717 O
ATOM 3401 CB VAL A 315 29.012 135.287 155.093 1.00125.64 C
ANISOU 3401 CB VAL A 315 18460 11828 17449 -1846 -3886 2263 C
ATOM 3402 CG1 VAL A 315 28.893 136.242 156.278 1.00125.96 C
ANISOU 3402 CG1 VAL A 315 18909 11847 17102 -2082 -4093 2305 C
ATOM 3403 CG2 VAL A 315 29.954 135.852 154.042 1.00124.29 C
ANISOU 3403 CG2 VAL A 315 17860 11659 17704 -1659 -3829 2260 C
ATOM 3404 N LEU A 316 27.642 132.902 156.799 1.00132.19 N
ANISOU 3404 N LEU A 316 19926 12501 17799 -2141 -4053 2375 N
ATOM 3405 CA LEU A 316 26.912 132.338 157.925 1.00134.54 C
ANISOU 3405 CA LEU A 316 20673 12739 17708 -2362 -4145 2418 C
ATOM 3406 C LEU A 316 27.806 131.240 158.544 1.00144.37 C
ANISOU 3406 C LEU A 316 21934 13717 19205 -2451 -4596 2674 C
ATOM 3407 O LEU A 316 28.066 131.283 159.746 1.00146.15 O
ANISOU 3407 O LEU A 316 22532 13784 19214 -2697 -4952 2831 O
ATOM 3408 CB LEU A 316 25.602 131.740 157.368 1.00132.62 C
ANISOU 3408 CB LEU A 316 20435 12666 17290 -2278 -3711 2226 C
ATOM 3409 CG LEU A 316 24.478 131.374 158.335 1.00138.00 C
ANISOU 3409 CG LEU A 316 21573 13351 17509 -2485 -3626 2192 C
ATOM 3410 CD1 LEU A 316 23.563 132.573 158.597 1.00137.02 C
ANISOU 3410 CD1 LEU A 316 21694 13380 16988 -2566 -3345 2025 C
ATOM 3411 CD2 LEU A 316 23.652 130.209 157.784 1.00138.13 C
ANISOU 3411 CD2 LEU A 316 21491 13432 17562 -2393 -3371 2109 C
ATOM 3412 N ARG A 317 28.357 130.337 157.688 1.00143.89 N
ANISOU 3412 N ARG A 317 21462 13585 19623 -2253 -4591 2723 N
ATOM 3413 CA ARG A 317 29.234 129.211 158.041 1.00147.94 C
ANISOU 3413 CA ARG A 317 21879 13833 20498 -2279 -4975 2962 C
ATOM 3414 C ARG A 317 30.584 129.627 158.658 1.00157.94 C
ANISOU 3414 C ARG A 317 23098 14869 22042 -2383 -5495 3217 C
ATOM 3415 O ARG A 317 30.925 129.134 159.735 1.00160.22 O
ANISOU 3415 O ARG A 317 23652 14946 22279 -2591 -5929 3433 O
ATOM 3416 CB ARG A 317 29.451 128.277 156.829 1.00147.44 C
ANISOU 3416 CB ARG A 317 21366 13757 20898 -2016 -4748 2912 C
ATOM 3417 CG ARG A 317 28.257 127.375 156.512 1.00156.27 C
ANISOU 3417 CG ARG A 317 22588 14992 21797 -1977 -4414 2760 C
ATOM 3418 CD ARG A 317 28.339 126.787 155.112 1.00165.42 C
ANISOU 3418 CD ARG A 317 23334 16188 23330 -1712 -4092 2643 C
ATOM 3419 NE ARG A 317 27.010 126.480 154.573 1.00173.76 N
ANISOU 3419 NE ARG A 317 24483 17455 24082 -1666 -3674 2420 N
ATOM 3420 CZ ARG A 317 26.744 126.268 153.285 1.00185.17 C
ANISOU 3420 CZ ARG A 317 25665 19000 25693 -1467 -3316 2257 C
ATOM 3421 NH1 ARG A 317 27.715 126.326 152.380 1.00171.81 N
ANISOU 3421 NH1 ARG A 317 23607 17215 24458 -1288 -3276 2275 N
ATOM 3422 NH2 ARG A 317 25.505 126.004 152.892 1.00168.14 N
ANISOU 3422 NH2 ARG A 317 23618 17019 23248 -1457 -2994 2077 N
ATOM 3423 N ARG A 318 31.348 130.510 157.975 1.00156.74 N
ANISOU 3423 N ARG A 318 22611 14746 22198 -2248 -5467 3202 N
ATOM 3424 CA ARG A 318 32.655 130.991 158.438 1.00160.75 C
ANISOU 3424 CA ARG A 318 23007 15039 23031 -2329 -5944 3440 C
ATOM 3425 C ARG A 318 32.543 131.884 159.685 1.00170.51 C
ANISOU 3425 C ARG A 318 24744 16246 23795 -2628 -6254 3515 C
ATOM 3426 O ARG A 318 33.450 131.882 160.523 1.00173.56 O
ANISOU 3426 O ARG A 318 25230 16386 24328 -2807 -6793 3777 O
ATOM 3427 CB ARG A 318 33.418 131.697 157.302 1.00159.31 C
ANISOU 3427 CB ARG A 318 22326 14906 23297 -2098 -5763 3382 C
ATOM 3428 CG ARG A 318 34.878 132.006 157.630 1.00173.37 C
ANISOU 3428 CG ARG A 318 23870 16427 25574 -2142 -6246 3652 C
ATOM 3429 CD ARG A 318 35.697 132.324 156.400 1.00183.30 C
ANISOU 3429 CD ARG A 318 24566 17684 27397 -1882 -6021 3611 C
ATOM 3430 NE ARG A 318 36.990 132.918 156.746 1.00196.32 N
ANISOU 3430 NE ARG A 318 26017 19125 29451 -1949 -6451 3843 N
ATOM 3431 CZ ARG A 318 38.113 132.231 156.941 1.00209.63 C
ANISOU 3431 CZ ARG A 318 27439 20980 31232 -1693 -6055 3769 C
ATOM 3432 NH1 ARG A 318 39.237 132.862 157.249 1.00204.23 N
ANISOU 3432 NH1 ARG A 318 26585 20114 30900 -1766 -6451 3976 N
ATOM 3433 NH2 ARG A 318 38.119 130.907 156.830 1.00200.05 N
ANISOU 3433 NH2 ARG A 318 26065 19142 30802 -1862 -6841 4190 N
ATOM 3434 N LEU A 319 31.428 132.627 159.816 1.00168.15 N
ANISOU 3434 N LEU A 319 24771 16177 22941 -2693 -5918 3291 N
ATOM 3435 CA LEU A 319 31.185 133.517 160.959 1.00170.62 C
ANISOU 3435 CA LEU A 319 25608 16471 22750 -2976 -6110 3314 C
ATOM 3436 C LEU A 319 29.985 133.024 161.810 1.00178.44 C
ANISOU 3436 C LEU A 319 27134 17497 23167 -3172 -5976 3236 C
ATOM 3437 O LEU A 319 29.031 133.761 162.078 1.00177.03 O
ANISOU 3437 O LEU A 319 27280 17472 22511 -3257 -5675 3051 O
ATOM 3438 CB LEU A 319 31.066 134.995 160.504 1.00168.33 C
ANISOU 3438 CB LEU A 319 25256 16366 22333 -2910 -5856 3140 C
ATOM 3439 CG LEU A 319 32.303 135.554 159.780 1.00172.37 C
ANISOU 3439 CG LEU A 319 25282 16821 23388 -2753 -6008 3232 C
ATOM 3440 CD1 LEU A 319 31.916 136.391 158.590 1.00168.78 C
ANISOU 3440 CD1 LEU A 319 24535 16623 22971 -2518 -5511 2984 C
ATOM 3441 CD2 LEU A 319 33.209 136.316 160.724 1.00176.96 C
ANISOU 3441 CD2 LEU A 319 26074 17212 23952 -2986 -6524 3438 C
ATOM 3442 N GLN A 320 30.068 131.746 162.223 1.00179.14 N
ANISOU 3442 N GLN A 320 27295 17423 23345 -3238 -6194 3387 N
ATOM 3443 CA GLN A 320 29.095 131.021 163.045 1.00180.62 C
ANISOU 3443 CA GLN A 320 27959 17592 23077 -3428 -6126 3363 C
ATOM 3444 C GLN A 320 29.561 130.923 164.521 1.00190.63 C
ANISOU 3444 C GLN A 320 29755 18587 24088 -3788 -6685 3613 C
ATOM 3445 O GLN A 320 28.777 131.311 165.393 1.00190.76 O
ANISOU 3445 O GLN A 320 30332 18621 23527 -4028 -6587 3537 O
ATOM 3446 CB GLN A 320 28.808 129.617 162.453 1.00180.96 C
ANISOU 3446 CB GLN A 320 27741 17638 23377 -3262 -5972 3354 C
ATOM 3447 CG GLN A 320 27.559 128.932 162.995 1.00187.97 C
ANISOU 3447 CG GLN A 320 29037 18581 23805 -3397 -5734 3256 C
ATOM 3448 CD GLN A 320 26.304 129.451 162.345 1.00200.88 C
ANISOU 3448 CD GLN A 320 30644 20507 25175 -3273 -5122 2950 C
ATOM 3449 OE1 GLN A 320 25.766 130.500 162.719 1.00195.88 O
ANISOU 3449 OE1 GLN A 320 30288 19972 24165 -3380 -4945 2827 O
ATOM 3450 NE2 GLN A 320 25.807 128.724 161.356 1.00189.61 N
ANISOU 3450 NE2 GLN A 320 28884 19205 23953 -3050 -4795 2826 N
ATOM 3451 N PRO A 321 30.810 130.467 164.848 1.00191.71 N
ANISOU 3451 N PRO A 321 29755 18454 24632 -3850 -7270 3914 N
ATOM 3452 CA PRO A 321 31.201 130.360 166.269 1.00191.50 C
ANISOU 3452 CA PRO A 321 29797 18595 24368 -3823 -7070 3878 C
ATOM 3453 C PRO A 321 31.443 131.688 167.008 1.00193.89 C
ANISOU 3453 C PRO A 321 30121 19160 24388 -3772 -6751 3704 C
ATOM 3454 O PRO A 321 32.054 131.682 168.084 1.00193.55 O
ANISOU 3454 O PRO A 321 30077 19193 24268 -3754 -6726 3728 O
ATOM 3455 CB PRO A 321 32.463 129.480 166.231 1.00193.18 C
ANISOU 3455 CB PRO A 321 29456 18795 25150 -3566 -7142 4008 C
ATOM 3456 CG PRO A 321 32.506 128.898 164.845 1.00195.89 C
ANISOU 3456 CG PRO A 321 29298 19157 25976 -3298 -6964 3962 C
ATOM 3457 CD PRO A 321 31.886 129.938 163.985 1.00192.57 C
ANISOU 3457 CD PRO A 321 29142 18557 25469 -3524 -7279 3990 C
ATOM 3458 N ARG A 322 30.934 132.816 166.465 1.00191.43 N
ANISOU 3458 N ARG A 322 30087 18770 23876 -3946 -6865 3659 N
ATOM 3459 CA ARG A 322 31.044 134.133 167.104 1.00191.33 C
ANISOU 3459 CA ARG A 322 30296 18847 23553 -4044 -6793 3570 C
ATOM 3460 C ARG A 322 30.020 134.218 168.246 1.00194.63 C
ANISOU 3460 C ARG A 322 31055 19484 23410 -4085 -6280 3352 C
ATOM 3461 O ARG A 322 30.305 134.813 169.293 1.00194.47 O
ANISOU 3461 O ARG A 322 31163 19542 23186 -4131 -6222 3321 O
ATOM 3462 CB ARG A 322 30.821 135.280 166.091 1.00190.64 C
ANISOU 3462 CB ARG A 322 30251 18711 23471 -4096 -6862 3516 C
ATOM 3463 CG ARG A 322 31.655 135.210 164.803 1.00196.37 C
ANISOU 3463 CG ARG A 322 30176 19561 24876 -3713 -6738 3503 C
ATOM 3464 CD ARG A 322 33.159 135.348 165.017 1.00199.46 C
ANISOU 3464 CD ARG A 322 29965 20126 25695 -3416 -6609 3516 C
ATOM 3465 NE ARG A 322 33.912 135.028 163.802 1.00202.65 N
ANISOU 3465 NE ARG A 322 29780 20509 26710 -3161 -6616 3569 N
ATOM 3466 CZ ARG A 322 34.268 133.801 163.430 1.00210.34 C
ANISOU 3466 CZ ARG A 322 30266 21654 28000 -2819 -6203 3489 C
ATOM 3467 NH1 ARG A 322 34.943 133.613 162.305 1.00200.96 N
ANISOU 3467 NH1 ARG A 322 28854 20013 27490 -2921 -6919 3815 N
ATOM 3468 NH2 ARG A 322 33.948 132.752 164.178 1.00196.99 N
ANISOU 3468 NH2 ARG A 322 29152 19459 26238 -3268 -7057 3858 N
ATOM 3469 N LEU A 323 28.836 133.592 168.035 1.00192.48 N
ANISOU 3469 N LEU A 323 31212 19086 22836 -4279 -6258 3334 N
ATOM 3470 CA LEU A 323 27.726 133.521 168.988 1.00211.30 C
ANISOU 3470 CA LEU A 323 33151 22103 25030 -3832 -5063 2893 C
ATOM 3471 C LEU A 323 27.896 132.347 169.960 1.00221.15 C
ANISOU 3471 C LEU A 323 33563 23868 26596 -3268 -4299 2704 C
ATOM 3472 O LEU A 323 27.751 132.516 171.169 1.00187.37 O
ANISOU 3472 O LEU A 323 31413 18482 21298 -4596 -5926 3287 O
ATOM 3473 CB LEU A 323 26.369 133.445 168.252 1.00211.07 C
ANISOU 3473 CB LEU A 323 33404 22034 24759 -3941 -4861 2781 C
ATOM 3474 CG LEU A 323 26.154 132.284 167.284 1.00214.20 C
ANISOU 3474 CG LEU A 323 33461 22451 25472 -3765 -4798 2798 C
ATOM 3475 CD1 LEU A 323 25.178 131.280 167.850 1.00214.63 C
ANISOU 3475 CD1 LEU A 323 33712 22531 25308 -3820 -4565 2756 C
ATOM 3476 CD2 LEU A 323 25.670 132.782 165.945 1.00215.33 C
ANISOU 3476 CD2 LEU A 323 33578 22573 25665 -3752 -4752 2719 C
TER 3477 LEU A 323
HETATM 3478 C4 A90 A9001 26.269 163.518 143.884 1.00103.14 C
ANISOU 3478 C4 A90 A9001 14574 10924 13692 -760 -762 321 C
HETATM 3479 C14 A90 A9001 26.390 165.672 146.860 1.00109.21 C
ANISOU 3479 C14 A90 A9001 16021 11434 14042 -1079 -967 288 C
HETATM 3480 C5 A90 A9001 26.453 162.245 144.433 1.00103.30 C
ANISOU 3480 C5 A90 A9001 14622 10917 13712 -801 -857 370 C
HETATM 3481 C6 A90 A9001 26.473 161.168 143.547 1.00 99.62 C
ANISOU 3481 C6 A90 A9001 13967 10509 13375 -714 -794 384 C
HETATM 3482 C11 A90 A9001 21.247 159.257 142.294 1.00 93.15 C
ANISOU 3482 C11 A90 A9001 13140 9954 12301 -530 -154 125 C
HETATM 3483 C7 A90 A9001 26.277 159.805 144.206 1.00 98.40 C
ANISOU 3483 C7 A90 A9001 13877 10330 13180 -753 -854 413 C
HETATM 3484 C8 A90 A9001 23.753 158.200 142.880 1.00 94.25 C
ANISOU 3484 C8 A90 A9001 13258 9991 12561 -601 -466 268 C
HETATM 3485 C9 A90 A9001 23.294 158.195 141.561 1.00 92.07 C
ANISOU 3485 C9 A90 A9001 12842 9792 12351 -511 -336 231 C
HETATM 3486 C10 A90 A9001 22.035 158.714 141.274 1.00 91.74 C
ANISOU 3486 C10 A90 A9001 12819 9802 12237 -483 -205 165 C
HETATM 3487 C12 A90 A9001 21.710 159.277 143.609 1.00 93.09 C
ANISOU 3487 C12 A90 A9001 13306 9869 12196 -624 -244 144 C
HETATM 3488 C13 A90 A9001 22.956 158.723 143.904 1.00 94.37 C
ANISOU 3488 C13 A90 A9001 13465 9983 12408 -667 -423 222 C
HETATM 3489 C3 A90 A9001 26.264 164.650 144.701 1.00104.58 C
ANISOU 3489 C3 A90 A9001 14949 11035 13751 -844 -806 299 C
HETATM 3490 O2 A90 A9001 27.866 165.328 148.698 1.00117.16 O
ANISOU 3490 O2 A90 A9001 17349 12229 14937 -1356 -1428 442 O
HETATM 3491 C15 A90 A9001 27.721 165.902 147.600 1.00113.04 C
ANISOU 3491 C15 A90 A9001 16603 11799 14550 -1221 -1275 399 C
HETATM 3492 O3 A90 A9001 28.566 166.642 147.062 1.00112.20 O
ANISOU 3492 O3 A90 A9001 16348 11684 14599 -1202 -1364 448 O
HETATM 3493 C2 A90 A9001 26.426 164.521 146.077 1.00107.22 C
ANISOU 3493 C2 A90 A9001 15537 11268 13935 -984 -944 322 C
HETATM 3494 C1 A90 A9001 26.590 163.244 146.640 1.00108.62 C
ANISOU 3494 C1 A90 A9001 15757 11417 14095 -1036 -1054 378 C
HETATM 3495 C A90 A9001 26.628 162.108 145.822 1.00106.66 C
ANISOU 3495 C A90 A9001 15284 11243 13999 -938 -1014 404 C
HETATM 3496 N A90 A9001 26.482 158.756 143.203 1.00 97.88 N
ANISOU 3496 N A90 A9001 13609 10304 13276 -663 -791 431 N
HETATM 3497 S A90 A9001 25.365 157.565 143.234 1.00 97.39 S
ANISOU 3497 S A90 A9001 13596 10295 13112 -643 -682 382 S
HETATM 3498 O A90 A9001 25.750 156.547 142.159 1.00 97.18 O
ANISOU 3498 O A90 A9001 13381 10286 13258 -561 -626 402 O
HETATM 3499 O1 A90 A9001 25.383 156.903 144.611 1.00 99.48 O
ANISOU 3499 O1 A90 A9001 14045 10484 13270 -752 -825 427 O
HETATM 3500 CL A90 A9001 19.687 159.927 141.911 1.00 96.51 CL
ANISOU 3500 CL A90 A9001 13532 10413 12723 -482 22 58 CL
HETATM 3501 ZN ZN A9002 -1.849 122.320 136.961 1.00117.55 ZN2+
HETATM 3502 C1 CLR A9003 25.657 164.474 127.314 1.00110.14 C
HETATM 3503 C2 CLR A9003 25.622 165.956 127.755 1.00108.01 C
HETATM 3504 C3 CLR A9003 25.138 166.940 126.684 1.00107.60 C
HETATM 3505 C4 CLR A9003 23.790 166.501 126.111 1.00109.63 C
HETATM 3506 C5 CLR A9003 23.771 165.018 125.739 1.00111.46 C
HETATM 3507 C6 CLR A9003 23.226 164.756 124.518 1.00108.64 C
HETATM 3508 C7 CLR A9003 23.158 163.387 123.881 1.00109.10 C
HETATM 3509 C8 CLR A9003 23.384 162.258 124.898 1.00112.69 C
HETATM 3510 C9 CLR A9003 24.563 162.600 125.876 1.00114.98 C
HETATM 3511 C10 CLR A9003 24.348 163.922 126.695 1.00112.72 C
HETATM 3512 C11 CLR A9003 24.932 161.372 126.770 1.00115.49 C
HETATM 3513 C12 CLR A9003 25.059 160.026 126.018 1.00115.04 C
HETATM 3514 C13 CLR A9003 23.861 159.697 125.097 1.00115.09 C
HETATM 3515 C14 CLR A9003 23.648 160.916 124.189 1.00113.67 C
HETATM 3516 C15 CLR A9003 22.657 160.431 123.126 1.00113.41 C
HETATM 3517 C16 CLR A9003 23.116 158.992 122.882 1.00113.97 C
HETATM 3518 C17 CLR A9003 24.111 158.628 124.003 1.00115.29 C
HETATM 3519 C18 CLR A9003 22.627 159.344 125.960 1.00115.64 C
HETATM 3520 C19 CLR A9003 23.430 163.652 127.897 1.00111.41 C
HETATM 3521 C20 CLR A9003 24.166 157.133 124.433 1.00116.60 C
HETATM 3522 C21 CLR A9003 25.586 156.758 124.867 1.00116.26 C
HETATM 3523 C22 CLR A9003 23.669 156.125 123.382 1.00116.61 C
HETATM 3524 C23 CLR A9003 23.164 154.804 123.964 1.00114.92 C
HETATM 3525 C24 CLR A9003 22.207 154.113 122.996 1.00114.20 C
HETATM 3526 C25 CLR A9003 22.639 152.729 122.492 1.00114.96 C
HETATM 3527 C26 CLR A9003 24.044 152.580 121.914 1.00114.29 C
HETATM 3528 C27 CLR A9003 22.272 151.585 123.421 1.00115.86 C
HETATM 3529 O1 CLR A9003 24.964 168.237 127.262 1.00106.78 O
HETATM 3530 C1 GOL A9004 29.604 179.639 137.933 1.00 82.64 C
HETATM 3531 O1 GOL A9004 30.711 178.745 137.931 1.00 78.47 O
HETATM 3532 C2 GOL A9004 29.117 180.003 139.321 1.00 85.23 C
HETATM 3533 O2 GOL A9004 30.094 180.813 139.996 1.00 85.90 O
HETATM 3534 C3 GOL A9004 27.833 180.790 139.148 1.00 83.46 C
HETATM 3535 O3 GOL A9004 27.234 181.162 140.387 1.00 80.65 O
CONECT 825 1458
CONECT 1458 825
CONECT 1483 2059
CONECT 2059 1483
CONECT 2420 3501
CONECT 2440 3501
CONECT 2667 3501
CONECT 2685 3501
CONECT 3478 3480 3489
CONECT 3479 3491 3493
CONECT 3480 3478 3481 3495
CONECT 3481 3480 3483
CONECT 3482 3486 3487 3500
CONECT 3483 3481 3496
CONECT 3484 3485 3488 3497
CONECT 3485 3484 3486
CONECT 3486 3482 3485
CONECT 3487 3482 3488
CONECT 3488 3484 3487
CONECT 3489 3478 3493
CONECT 3490 3491
CONECT 3491 3479 3490 3492
CONECT 3492 3491
CONECT 3493 3479 3489 3494
CONECT 3494 3493 3495
CONECT 3495 3480 3494
CONECT 3496 3483 3497
CONECT 3497 3484 3496 3498 3499
CONECT 3498 3497
CONECT 3499 3497
CONECT 3500 3482
CONECT 3501 2420 2440 2667 2685
CONECT 3502 3503 3511
CONECT 3503 3502 3504
CONECT 3504 3503 3505 3529
CONECT 3505 3504 3506
CONECT 3506 3505 3507 3511
CONECT 3507 3506 3508
CONECT 3508 3507 3509
CONECT 3509 3508 3510 3515
CONECT 3510 3509 3511 3512
CONECT 3511 3502 3506 3510 3520
CONECT 3512 3510 3513
CONECT 3513 3512 3514
CONECT 3514 3513 3515 3518 3519
CONECT 3515 3509 3514 3516
CONECT 3516 3515 3517
CONECT 3517 3516 3518
CONECT 3518 3514 3517 3521
CONECT 3519 3514
CONECT 3520 3511
CONECT 3521 3518 3522 3523
CONECT 3522 3521
CONECT 3523 3521 3524
CONECT 3524 3523 3525
CONECT 3525 3524 3526
CONECT 3526 3525 3527 3528
CONECT 3527 3526
CONECT 3528 3526
CONECT 3529 3504
CONECT 3530 3531 3532
CONECT 3531 3530
CONECT 3532 3530 3533 3534
CONECT 3533 3532
CONECT 3534 3532 3535
CONECT 3535 3534
MASTER 363 0 4 21 5 0 9 6 3534 1 66 38
END